data_9CVR
# 
_entry.id   9CVR 
# 
_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   9CVR         pdb_00009cvr 10.2210/pdb9cvr/pdb 
WWPDB D_1000286184 ?            ?                   
# 
_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                        9CVR 
_pdbx_database_status.recvd_initial_deposition_date   2024-07-29 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    RCSB 
_pdbx_database_status.process_site                    RCSB 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           N 
# 
_pdbx_contact_author.id                 2 
_pdbx_contact_author.email              poulos@uci.edu 
_pdbx_contact_author.name_first         Thomas 
_pdbx_contact_author.name_last          Poulos 
_pdbx_contact_author.name_mi            L 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0002-5648-3510 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Li, H.'       1 0000-0003-4867-367X 
'Poulos, T.L.' 2 0000-0002-5648-3510 
# 
_citation.abstract                  ? 
_citation.abstract_id_CAS           ? 
_citation.book_id_ISBN              ? 
_citation.book_publisher            ? 
_citation.book_publisher_city       ? 
_citation.book_title                ? 
_citation.coordinate_linkage        ? 
_citation.country                   UK 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            Bioorg.Med.Chem. 
_citation.journal_id_ASTM           BMECEP 
_citation.journal_id_CSD            1200 
_citation.journal_id_ISSN           1464-3391 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            124 
_citation.language                  ? 
_citation.page_first                118193 
_citation.page_last                 118193 
_citation.title                     
;Truncated pyridinylbenzylamines: Potent, selective, and highly membrane permeable inhibitors of human neuronal nitric oxide synthase.
;
_citation.year                      2025 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1016/j.bmc.2025.118193 
_citation.pdbx_database_id_PubMed   40252563 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Vasu, D.'        1 ? 
primary 'Do, H.T.'        2 ? 
primary 'Li, H.'          3 ? 
primary 'Hardy, C.D.'     4 ? 
primary 'Poulos, T.L.'    5 ? 
primary 'Silverman, R.B.' 6 ? 
# 
loop_
_entity.id 
_entity.type 
_entity.src_method 
_entity.pdbx_description 
_entity.formula_weight 
_entity.pdbx_number_of_molecules 
_entity.pdbx_ec 
_entity.pdbx_mutation 
_entity.pdbx_fragment 
_entity.details 
1 polymer     man 'Nitric oxide synthase, brain'                                                 48726.410 1  1.14.13.39 R349A ? ? 
2 non-polymer syn 'PROTOPORPHYRIN IX CONTAINING FE'                                              616.487   1  ?          ?     ? ? 
3 non-polymer syn 5,6,7,8-TETRAHYDROBIOPTERIN                                                    241.247   1  ?          ?     ? ? 
4 non-polymer syn '(6M)-6-{2,3-difluoro-5-[2-(methylamino)ethyl]phenyl}-4-methylpyridin-2-amine' 277.312   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    50 ?          ?     ? ? 
# 
_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-[2-(methylamino)ethyl]phenyl}-4-methylpyridin-2-amine' A1A0C 
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 
A1A0C non-polymer         . '(6M)-6-{2,3-difluoro-5-[2-(methylamino)ethyl]phenyl}-4-methylpyridin-2-amine' ?    'C15 H17 F2 N3'    
277.312 
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 ?   ?   ?   A . n 
A 1 422 GLY 422 718 ?   ?   ?   A . n 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        A1A0C 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   A1A0C 
_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 A1A0C 1  803 800 A1A0C 4V7 A . 
E 5 ACT   1  804 860 ACT   ACT A . 
F 6 ZN    1  805 900 ZN    ZN  A . 
G 7 HOH   1  901 4   HOH   HOH A . 
G 7 HOH   2  902 12  HOH   HOH A . 
G 7 HOH   3  903 26  HOH   HOH A . 
G 7 HOH   4  904 39  HOH   HOH A . 
G 7 HOH   5  905 16  HOH   HOH A . 
G 7 HOH   6  906 13  HOH   HOH A . 
G 7 HOH   7  907 17  HOH   HOH A . 
G 7 HOH   8  908 36  HOH   HOH A . 
G 7 HOH   9  909 27  HOH   HOH A . 
G 7 HOH   10 910 46  HOH   HOH A . 
G 7 HOH   11 911 45  HOH   HOH A . 
G 7 HOH   12 912 50  HOH   HOH A . 
G 7 HOH   13 913 10  HOH   HOH A . 
G 7 HOH   14 914 20  HOH   HOH A . 
G 7 HOH   15 915 15  HOH   HOH A . 
G 7 HOH   16 916 9   HOH   HOH A . 
G 7 HOH   17 917 35  HOH   HOH A . 
G 7 HOH   18 918 49  HOH   HOH A . 
G 7 HOH   19 919 28  HOH   HOH A . 
G 7 HOH   20 920 38  HOH   HOH A . 
G 7 HOH   21 921 40  HOH   HOH A . 
G 7 HOH   22 922 29  HOH   HOH A . 
G 7 HOH   23 923 25  HOH   HOH A . 
G 7 HOH   24 924 30  HOH   HOH A . 
G 7 HOH   25 925 1   HOH   HOH A . 
G 7 HOH   26 926 7   HOH   HOH A . 
G 7 HOH   27 927 31  HOH   HOH A . 
G 7 HOH   28 928 24  HOH   HOH A . 
G 7 HOH   29 929 2   HOH   HOH A . 
G 7 HOH   30 930 47  HOH   HOH A . 
G 7 HOH   31 931 14  HOH   HOH A . 
G 7 HOH   32 932 6   HOH   HOH A . 
G 7 HOH   33 933 33  HOH   HOH A . 
G 7 HOH   34 934 34  HOH   HOH A . 
G 7 HOH   35 935 32  HOH   HOH A . 
G 7 HOH   36 936 11  HOH   HOH A . 
G 7 HOH   37 937 5   HOH   HOH A . 
G 7 HOH   38 938 21  HOH   HOH A . 
G 7 HOH   39 939 23  HOH   HOH A . 
G 7 HOH   40 940 42  HOH   HOH A . 
G 7 HOH   41 941 43  HOH   HOH A . 
G 7 HOH   42 942 37  HOH   HOH A . 
G 7 HOH   43 943 41  HOH   HOH A . 
G 7 HOH   44 944 8   HOH   HOH A . 
G 7 HOH   45 945 19  HOH   HOH A . 
G 7 HOH   46 946 44  HOH   HOH A . 
G 7 HOH   47 947 18  HOH   HOH A . 
G 7 HOH   48 948 3   HOH   HOH A . 
G 7 HOH   49 949 22  HOH   HOH A . 
G 7 HOH   50 950 48  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  ? ? ? '(1.20.1_4487: ???)' 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                     9CVR 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     48.410 
_cell.length_a_esd                 ? 
_cell.length_b                     112.831 
_cell.length_b_esd                 ? 
_cell.length_c                     162.622 
_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                         9CVR 
_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                   9CVR 
_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         2023-03-21 
_diffrn_detector.pdbx_frequency               ? 
_diffrn_detector.id                           ? 
_diffrn_detector.number_of_axes               ? 
# 
_diffrn_radiation.collimation                      ? 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.filter_edge                      ? 
_diffrn_radiation.inhomogeneity                    ? 
_diffrn_radiation.monochromator                    'DOUBLE CRYSTAL SI(III)' 
_diffrn_radiation.polarisn_norm                    ? 
_diffrn_radiation.polarisn_ratio                   ? 
_diffrn_radiation.probe                            ? 
_diffrn_radiation.type                             ? 
_diffrn_radiation.xray_symbol                      ? 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.pdbx_wavelength_list             ? 
_diffrn_radiation.pdbx_wavelength                  ? 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_analyzer                    ? 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   1.000 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.current                     ? 
_diffrn_source.details                     ? 
_diffrn_source.diffrn_id                   1 
_diffrn_source.power                       ? 
_diffrn_source.size                        ? 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.target                      ? 
_diffrn_source.type                        'ALS BEAMLINE 5.0.2' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        1.000 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   5.0.2 
_diffrn_source.pdbx_synchrotron_site       ALS 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       9CVR 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              1.87 
_reflns.d_resolution_low                               44.49 
_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                                     37012 
_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                                11.4 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          9.7 
_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                                0.150 
_reflns.pdbx_Rpim_I_all                                0.045 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       423131 
_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                              0.143 
_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                                    1.87 
_reflns_shell.d_res_low                                     1.91 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           ? 
_reflns_shell.number_measured_all                           26149 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             2376 
_reflns_shell.percent_possible_obs                          99.8 
_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                               11.0 
_reflns_shell.pdbx_chi_squared                              ? 
_reflns_shell.pdbx_netI_over_sigmaI_all                     ? 
_reflns_shell.pdbx_netI_over_sigmaI_obs                     0.5 
_reflns_shell.pdbx_Rrim_I_all                               8.637 
_reflns_shell.pdbx_Rpim_I_all                               2.528 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.756 
_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                                  8.244 
_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                                 9CVR 
_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                            1.87 
_refine.ls_d_res_low                             44.49 
_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                     36486 
_refine.ls_number_reflns_R_free                  3553 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    98.02 
_refine.ls_percent_reflns_R_free                 5.10 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.2334 
_refine.ls_R_factor_R_free                       0.2600 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.2319 
_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                          0.09 
_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             1.10 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             0.90 
_refine.pdbx_real_space_R                        ? 
_refine.pdbx_density_correlation                 ? 
_refine.pdbx_pd_number_of_powder_patterns        ? 
_refine.pdbx_pd_number_of_points                 ? 
_refine.pdbx_pd_meas_number_of_points            ? 
_refine.pdbx_pd_proc_ls_prof_R_factor            ? 
_refine.pdbx_pd_proc_ls_prof_wR_factor           ? 
_refine.pdbx_pd_Marquardt_correlation_coeff      ? 
_refine.pdbx_pd_Fsqrd_R_factor                   ? 
_refine.pdbx_pd_ls_matrix_band_width             ? 
_refine.pdbx_overall_phase_error                 44.34 
_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                            0.30 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.overall_SU_R_free                        ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.pdbx_average_fsc_overall                 ? 
_refine.pdbx_average_fsc_work                    ? 
_refine.pdbx_average_fsc_free                    ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.details                          ? 
_refine_hist.d_res_high                       1.87 
_refine_hist.d_res_low                        44.49 
_refine_hist.number_atoms_solvent             50 
_refine_hist.number_atoms_total               3456 
_refine_hist.number_reflns_all                ? 
_refine_hist.number_reflns_obs                ? 
_refine_hist.number_reflns_R_free             ? 
_refine_hist.number_reflns_R_work             ? 
_refine_hist.R_factor_all                     ? 
_refine_hist.R_factor_obs                     ? 
_refine_hist.R_factor_R_free                  ? 
_refine_hist.R_factor_R_work                  ? 
_refine_hist.pdbx_number_residues_total       ? 
_refine_hist.pdbx_B_iso_mean_ligand           ? 
_refine_hist.pdbx_B_iso_mean_solvent          ? 
_refine_hist.pdbx_number_atoms_protein        3321 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         85 
_refine_hist.pdbx_number_atoms_lipid          ? 
_refine_hist.pdbx_number_atoms_carb           ? 
_refine_hist.pdbx_pseudo_atom_details         ? 
# 
loop_
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.criterion 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.number 
_refine_ls_restr.rejects 
_refine_ls_restr.type 
_refine_ls_restr.weight 
_refine_ls_restr.pdbx_restraint_function 
'X-RAY DIFFRACTION' ? 0.006  ? 3510 ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 0.927  ? 4781 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 16.707 ? 1268 ? f_dihedral_angle_d ? ? 
'X-RAY DIFFRACTION' ? 0.047  ? 496  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.008  ? 603  ? 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' 1.87 1.90  . . 140 2584 99.00 . . . . 0.5960 . . . . . . . . . . . 0.6077 
'X-RAY DIFFRACTION' 1.90 1.92  . . 149 2763 99.00 . . . . 0.5751 . . . . . . . . . . . 0.5995 
'X-RAY DIFFRACTION' 1.92 1.95  . . 157 2624 99.00 . . . . 0.5742 . . . . . . . . . . . 0.4939 
'X-RAY DIFFRACTION' 1.95 1.98  . . 149 2695 99.00 . . . . 0.5280 . . . . . . . . . . . 0.5633 
'X-RAY DIFFRACTION' 1.98 2.01  . . 125 2642 99.00 . . . . 0.4819 . . . . . . . . . . . 0.5051 
'X-RAY DIFFRACTION' 2.01 2.05  . . 110 2694 98.00 . . . . 0.4736 . . . . . . . . . . . 0.4970 
'X-RAY DIFFRACTION' 2.05 2.09  . . 149 2591 98.00 . . . . 0.4401 . . . . . . . . . . . 0.4594 
'X-RAY DIFFRACTION' 2.09 2.13  . . 163 2656 98.00 . . . . 0.4063 . . . . . . . . . . . 0.4851 
'X-RAY DIFFRACTION' 2.13 2.17  . . 142 2615 98.00 . . . . 0.4021 . . . . . . . . . . . 0.4394 
'X-RAY DIFFRACTION' 2.17 2.22  . . 144 2637 98.00 . . . . 0.3692 . . . . . . . . . . . 0.4385 
'X-RAY DIFFRACTION' 2.22 2.27  . . 147 2653 98.00 . . . . 0.3377 . . . . . . . . . . . 0.3877 
'X-RAY DIFFRACTION' 2.27 2.33  . . 126 2605 98.00 . . . . 0.3152 . . . . . . . . . . . 0.3281 
'X-RAY DIFFRACTION' 2.33 2.39  . . 156 2668 98.00 . . . . 0.3171 . . . . . . . . . . . 0.3639 
'X-RAY DIFFRACTION' 2.39 2.46  . . 127 2685 98.00 . . . . 0.3064 . . . . . . . . . . . 0.3250 
'X-RAY DIFFRACTION' 2.46 2.54  . . 125 2640 98.00 . . . . 0.2763 . . . . . . . . . . . 0.3460 
'X-RAY DIFFRACTION' 2.54 2.63  . . 144 2637 98.00 . . . . 0.2742 . . . . . . . . . . . 0.2807 
'X-RAY DIFFRACTION' 2.63 2.73  . . 120 2656 99.00 . . . . 0.2578 . . . . . . . . . . . 0.3248 
'X-RAY DIFFRACTION' 2.73 2.86  . . 136 2693 99.00 . . . . 0.2650 . . . . . . . . . . . 0.2333 
'X-RAY DIFFRACTION' 2.86 3.01  . . 123 2685 99.00 . . . . 0.2635 . . . . . . . . . . . 0.3318 
'X-RAY DIFFRACTION' 3.01 3.20  . . 157 2680 99.00 . . . . 0.2598 . . . . . . . . . . . 0.2889 
'X-RAY DIFFRACTION' 3.20 3.44  . . 170 2645 99.00 . . . . 0.2221 . . . . . . . . . . . 0.2535 
'X-RAY DIFFRACTION' 3.44 3.79  . . 144 2646 98.00 . . . . 0.1997 . . . . . . . . . . . 0.1812 
'X-RAY DIFFRACTION' 3.79 4.34  . . 155 2649 98.00 . . . . 0.1647 . . . . . . . . . . . 0.2216 
'X-RAY DIFFRACTION' 4.34 5.46  . . 161 2577 97.00 . . . . 0.1491 . . . . . . . . . . . 0.1840 
'X-RAY DIFFRACTION' 5.47 44.49 . . 134 2556 94.00 . . . . 0.1488 . . . . . . . . . . . 0.1789 
# 
_struct.entry_id                     9CVR 
_struct.title                        
;Structure of rat neuronal nitric oxide synthase R349A mutant heme domain bound with 6-(2,3-difluoro-5-(2-(methylamino)ethyl)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        9CVR 
_struct_keywords.text            'nitric oxide synthase inhibitor binding, OXIDOREDUCTASE' 
_struct_keywords.pdbx_keywords   OXIDOREDUCTASE 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 2 ? 
C N N 3 ? 
D N N 4 ? 
E N N 5 ? 
F N N 6 ? 
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              9CVR 
_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             9CVR 
_struct_ref_seq_dif.mon_id                       ALA 
_struct_ref_seq_dif.pdbx_pdb_strand_id           A 
_struct_ref_seq_dif.seq_num                      53 
_struct_ref_seq_dif.pdbx_pdb_ins_code            ? 
_struct_ref_seq_dif.pdbx_seq_db_name             UNP 
_struct_ref_seq_dif.pdbx_seq_db_accession_code   P29476 
_struct_ref_seq_dif.db_mon_id                    ARG 
_struct_ref_seq_dif.pdbx_seq_db_seq_num          349 
_struct_ref_seq_dif.details                      'engineered mutation' 
_struct_ref_seq_dif.pdbx_auth_seq_num            349 
_struct_ref_seq_dif.pdbx_ordinal                 1 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_defined_assembly 
_pdbx_struct_assembly.method_details       ? 
_pdbx_struct_assembly.oligomeric_details   monomeric 
_pdbx_struct_assembly.oligomeric_count     1 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,D,E,F,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                ? 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1  AA1 THR A 19  ? SER A 24  ? THR A 315 SER A 320 5 ? 6  
HELX_P HELX_P2  AA2 THR A 54  ? ILE A 73  ? THR A 350 ILE A 369 1 ? 20 
HELX_P HELX_P3  AA3 SER A 78  ? SER A 96  ? SER A 374 SER A 392 1 ? 19 
HELX_P HELX_P4  AA4 LYS A 101 ? ASN A 115 ? LYS A 397 ASN A 411 1 ? 15 
HELX_P HELX_P5  AA5 GLY A 121 ? TRP A 125 ? GLY A 417 TRP A 421 5 ? 5  
HELX_P HELX_P6  AA6 THR A 138 ? ASN A 155 ? THR A 434 ASN A 451 1 ? 18 
HELX_P HELX_P7  AA7 LYS A 156 ? ASN A 158 ? LYS A 452 ASN A 454 5 ? 3  
HELX_P HELX_P8  AA8 ASN A 202 ? GLN A 212 ? ASN A 498 GLN A 508 1 ? 11 
HELX_P HELX_P9  AA9 PRO A 241 ? VAL A 245 ? PRO A 537 VAL A 541 5 ? 5  
HELX_P HELX_P10 AB1 PHE A 255 ? GLY A 262 ? PHE A 551 GLY A 558 5 ? 8  
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 ? MET A 318 ? ILE A 606 MET A 614 1 ? 9  
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 ? ASP A 348 ? LEU A 624 ASP A 644 1 ? 21 
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 ? HIS A 418 ? ASP A 709 HIS A 714 1 ? 6  
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_conn.id 
_struct_conn.conn_type_id 
_struct_conn.pdbx_leaving_atom_flag 
_struct_conn.pdbx_PDB_id 
_struct_conn.ptnr1_label_asym_id 
_struct_conn.ptnr1_label_comp_id 
_struct_conn.ptnr1_label_seq_id 
_struct_conn.ptnr1_label_atom_id 
_struct_conn.pdbx_ptnr1_label_alt_id 
_struct_conn.pdbx_ptnr1_PDB_ins_code 
_struct_conn.pdbx_ptnr1_standard_comp_id 
_struct_conn.ptnr1_symmetry 
_struct_conn.ptnr2_label_asym_id 
_struct_conn.ptnr2_label_comp_id 
_struct_conn.ptnr2_label_seq_id 
_struct_conn.ptnr2_label_atom_id 
_struct_conn.pdbx_ptnr2_label_alt_id 
_struct_conn.pdbx_ptnr2_PDB_ins_code 
_struct_conn.ptnr1_auth_asym_id 
_struct_conn.ptnr1_auth_comp_id 
_struct_conn.ptnr1_auth_seq_id 
_struct_conn.ptnr2_auth_asym_id 
_struct_conn.ptnr2_auth_comp_id 
_struct_conn.ptnr2_auth_seq_id 
_struct_conn.ptnr2_symmetry 
_struct_conn.pdbx_ptnr3_label_atom_id 
_struct_conn.pdbx_ptnr3_label_seq_id 
_struct_conn.pdbx_ptnr3_label_comp_id 
_struct_conn.pdbx_ptnr3_label_asym_id 
_struct_conn.pdbx_ptnr3_label_alt_id 
_struct_conn.pdbx_ptnr3_PDB_ins_code 
_struct_conn.details 
_struct_conn.pdbx_dist_value 
_struct_conn.pdbx_value_order 
_struct_conn.pdbx_role 
metalc1 metalc ? ? A CYS 30  SG ? ? ? 1_555 F ZN  . ZN ? ? A CYS 326 A ZN  805 1_555 ? ? ? ? ? ? ? 2.297 ? ? 
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 ? ? ? ? ? ? ? 2.320 ? ? 
metalc5 metalc ? ? A CYS 119 SG ? ? ? 1_555 B HEM . FE ? ? A CYS 415 A HEM 801 1_555 ? ? ? ? ? ? ? 2.354 ? ? 
# 
_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_555 115.3 ? 
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_555 115.3 ? 
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_555 115.3 ? 
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_555 115.3 ? 
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_555 103.3 ? 
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 98.4  ? 
9  NA ? B HEM .   ? A HEM 801 ? 1_555 FE ? B HEM . ? A HEM 801 ? 1_555 NB ? B HEM .  ? A HEM 801 ? 1_555 85.2  ? 
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 97.8  ? 
11 NA ? B HEM .   ? A HEM 801 ? 1_555 FE ? B HEM . ? A HEM 801 ? 1_555 NC ? B HEM .  ? A HEM 801 ? 1_555 158.4 ? 
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 87.6  ? 
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_555 107.5 ? 
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_555 154.1 ? 
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 87.6  ? 
# 
_struct_mon_prot_cis.pdbx_id                1 
_struct_mon_prot_cis.label_comp_id          THR 
_struct_mon_prot_cis.label_seq_id           405 
_struct_mon_prot_cis.label_asym_id          A 
_struct_mon_prot_cis.label_alt_id           . 
_struct_mon_prot_cis.pdbx_PDB_ins_code      ? 
_struct_mon_prot_cis.auth_comp_id           THR 
_struct_mon_prot_cis.auth_seq_id            701 
_struct_mon_prot_cis.auth_asym_id           A 
_struct_mon_prot_cis.pdbx_label_comp_id_2   PRO 
_struct_mon_prot_cis.pdbx_label_seq_id_2    406 
_struct_mon_prot_cis.pdbx_label_asym_id_2   A 
_struct_mon_prot_cis.pdbx_PDB_ins_code_2    ? 
_struct_mon_prot_cis.pdbx_auth_comp_id_2    PRO 
_struct_mon_prot_cis.pdbx_auth_seq_id_2     702 
_struct_mon_prot_cis.pdbx_auth_asym_id_2    A 
_struct_mon_prot_cis.pdbx_PDB_model_num     1 
_struct_mon_prot_cis.pdbx_omega_angle       -3.17 
# 
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 LEU A 5   ? LYS A 8   ? LEU A 301 LYS A 304 
AA1 2 VAL A 15  ? ASP A 18  ? VAL A 311 ASP A 314 
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 LEU A 5   ? N LEU A 301 O ASP A 18  ? O ASP A 314 
AA2 1 2 N PHE A 131 ? N PHE A 427 O ILE A 163 ? O ILE A 459 
AA2 2 3 N ALA A 162 ? N ALA A 458 O SER A 289 ? O SER A 585 
AA2 3 4 O PHE A 288 ? O PHE A 584 N VAL A 271 ? N VAL A 567 
AA3 1 2 N ARG A 177 ? N ARG A 473 O GLN A 229 ? O GLN A 525 
AA3 2 3 N LEU A 226 ? N LEU A 522 O PHE A 238 ? O PHE A 534 
AA4 1 2 N TYR A 189 ? N TYR A 485 O LEU A 197 ? O LEU A 493 
AA5 1 2 N VAL A 248 ? N VAL A 544 O TRP A 265 ? O TRP A 561 
AA6 1 2 O LEU A 281 ? O LEU A 577 N ILE A 278 ? N ILE A 574 
AA6 2 3 N LEU A 275 ? N LEU A 571 O GLU A 409 ? O GLU A 705 
AA7 1 2 N TYR A 292 ? N TYR A 588 O VAL A 353 ? O VAL A 649 
# 
_pdbx_entry_details.entry_id                   9CVR 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.has_protein_modification   N 
# 
_pdbx_validate_symm_contact.id                1 
_pdbx_validate_symm_contact.PDB_model_num     1 
_pdbx_validate_symm_contact.auth_atom_id_1    O 
_pdbx_validate_symm_contact.auth_asym_id_1    A 
_pdbx_validate_symm_contact.auth_comp_id_1    HOH 
_pdbx_validate_symm_contact.auth_seq_id_1     950 
_pdbx_validate_symm_contact.PDB_ins_code_1    ? 
_pdbx_validate_symm_contact.label_alt_id_1    ? 
_pdbx_validate_symm_contact.site_symmetry_1   1_555 
_pdbx_validate_symm_contact.auth_atom_id_2    O 
_pdbx_validate_symm_contact.auth_asym_id_2    A 
_pdbx_validate_symm_contact.auth_comp_id_2    HOH 
_pdbx_validate_symm_contact.auth_seq_id_2     950 
_pdbx_validate_symm_contact.PDB_ins_code_2    ? 
_pdbx_validate_symm_contact.label_alt_id_2    ? 
_pdbx_validate_symm_contact.site_symmetry_2   3_455 
_pdbx_validate_symm_contact.dist              2.13 
# 
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 ARG A 371 ? ? -140.89 44.18   
2 1 THR A 393 ? ? -172.40 -176.90 
3 1 THR A 466 ? ? -117.25 -83.32  
4 1 PRO A 513 ? ? -78.77  39.24   
5 1 ARG A 514 ? ? -10.51  65.90   
6 1 ARG A 516 ? ? -85.59  -77.72  
7 1 CYS A 582 ? ? -150.29 54.62   
8 1 ARG A 603 ? ? -112.38 -140.19 
# 
_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         -23.4230 
_pdbx_refine_tls.origin_y         -4.8048 
_pdbx_refine_tls.origin_z         22.0665 
_pdbx_refine_tls.T[1][1]          0.3372 
_pdbx_refine_tls.T[1][1]_esd      ? 
_pdbx_refine_tls.T[1][2]          -0.0269 
_pdbx_refine_tls.T[1][2]_esd      ? 
_pdbx_refine_tls.T[1][3]          -0.0697 
_pdbx_refine_tls.T[1][3]_esd      ? 
_pdbx_refine_tls.T[2][2]          0.4011 
_pdbx_refine_tls.T[2][2]_esd      ? 
_pdbx_refine_tls.T[2][3]          0.0038 
_pdbx_refine_tls.T[2][3]_esd      ? 
_pdbx_refine_tls.T[3][3]          0.4551 
_pdbx_refine_tls.T[3][3]_esd      ? 
_pdbx_refine_tls.L[1][1]          1.2867 
_pdbx_refine_tls.L[1][1]_esd      ? 
_pdbx_refine_tls.L[1][2]          -0.1168 
_pdbx_refine_tls.L[1][2]_esd      ? 
_pdbx_refine_tls.L[1][3]          0.4829 
_pdbx_refine_tls.L[1][3]_esd      ? 
_pdbx_refine_tls.L[2][2]          1.7268 
_pdbx_refine_tls.L[2][2]_esd      ? 
_pdbx_refine_tls.L[2][3]          -0.0332 
_pdbx_refine_tls.L[2][3]_esd      ? 
_pdbx_refine_tls.L[3][3]          9.3926 
_pdbx_refine_tls.L[3][3]_esd      ? 
_pdbx_refine_tls.S[1][1]          -0.0057 
_pdbx_refine_tls.S[1][1]_esd      ? 
_pdbx_refine_tls.S[1][2]          0.1346 
_pdbx_refine_tls.S[1][2]_esd      ? 
_pdbx_refine_tls.S[1][3]          0.0097 
_pdbx_refine_tls.S[1][3]_esd      ? 
_pdbx_refine_tls.S[2][1]          -0.0227 
_pdbx_refine_tls.S[2][1]_esd      ? 
_pdbx_refine_tls.S[2][2]          -0.0930 
_pdbx_refine_tls.S[2][2]_esd      ? 
_pdbx_refine_tls.S[2][3]          -0.0742 
_pdbx_refine_tls.S[2][3]_esd      ? 
_pdbx_refine_tls.S[3][1]          -0.8143 
_pdbx_refine_tls.S[3][1]_esd      ? 
_pdbx_refine_tls.S[3][2]          0.3693 
_pdbx_refine_tls.S[3][2]_esd      ? 
_pdbx_refine_tls.S[3][3]          0.0788 
_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 300:716)' 
# 
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  
12 1 Y 1 A LYS 717 ? A LYS 421 
13 1 Y 1 A GLY 718 ? A GLY 422 
# 
loop_
_chem_comp_atom.comp_id 
_chem_comp_atom.atom_id 
_chem_comp_atom.type_symbol 
_chem_comp_atom.pdbx_aromatic_flag 
_chem_comp_atom.pdbx_stereo_config 
_chem_comp_atom.pdbx_ordinal 
A1A0C C11  C  Y N 1   
A1A0C C12  C  Y N 2   
A1A0C C17  C  N N 3   
A1A0C C16  C  Y N 4   
A1A0C C15  C  Y N 5   
A1A0C C14  C  Y N 6   
A1A0C C13  C  Y N 7   
A1A0C C18  C  N N 8   
A1A0C C20  C  N N 9   
A1A0C C02  C  Y N 10  
A1A0C C03  C  Y N 11  
A1A0C C04  C  Y N 12  
A1A0C C05  C  Y N 13  
A1A0C C06  C  Y N 14  
A1A0C C07  C  N N 15  
A1A0C F12  F  N N 16  
A1A0C F13  F  N N 17  
A1A0C N01  N  Y N 18  
A1A0C N02  N  N N 19  
A1A0C N19  N  N N 20  
A1A0C H1   H  N N 21  
A1A0C H2   H  N N 22  
A1A0C H3   H  N N 23  
A1A0C H4   H  N N 24  
A1A0C H5   H  N N 25  
A1A0C H6   H  N N 26  
A1A0C H7   H  N N 27  
A1A0C H8   H  N N 28  
A1A0C H9   H  N N 29  
A1A0C H10  H  N N 30  
A1A0C H11  H  N N 31  
A1A0C H12  H  N N 32  
A1A0C H13  H  N N 33  
A1A0C H14  H  N N 34  
A1A0C H15  H  N N 35  
A1A0C H16  H  N N 36  
A1A0C H17  H  N N 37  
ACT   C    C  N N 38  
ACT   O    O  N N 39  
ACT   OXT  O  N N 40  
ACT   CH3  C  N N 41  
ACT   H1   H  N N 42  
ACT   H2   H  N N 43  
ACT   H3   H  N N 44  
ALA   N    N  N N 45  
ALA   CA   C  N S 46  
ALA   C    C  N N 47  
ALA   O    O  N N 48  
ALA   CB   C  N N 49  
ALA   OXT  O  N N 50  
ALA   H    H  N N 51  
ALA   H2   H  N N 52  
ALA   HA   H  N N 53  
ALA   HB1  H  N N 54  
ALA   HB2  H  N N 55  
ALA   HB3  H  N N 56  
ALA   HXT  H  N N 57  
ARG   N    N  N N 58  
ARG   CA   C  N S 59  
ARG   C    C  N N 60  
ARG   O    O  N N 61  
ARG   CB   C  N N 62  
ARG   CG   C  N N 63  
ARG   CD   C  N N 64  
ARG   NE   N  N N 65  
ARG   CZ   C  N N 66  
ARG   NH1  N  N N 67  
ARG   NH2  N  N N 68  
ARG   OXT  O  N N 69  
ARG   H    H  N N 70  
ARG   H2   H  N N 71  
ARG   HA   H  N N 72  
ARG   HB2  H  N N 73  
ARG   HB3  H  N N 74  
ARG   HG2  H  N N 75  
ARG   HG3  H  N N 76  
ARG   HD2  H  N N 77  
ARG   HD3  H  N N 78  
ARG   HE   H  N N 79  
ARG   HH11 H  N N 80  
ARG   HH12 H  N N 81  
ARG   HH21 H  N N 82  
ARG   HH22 H  N N 83  
ARG   HXT  H  N N 84  
ASN   N    N  N N 85  
ASN   CA   C  N S 86  
ASN   C    C  N N 87  
ASN   O    O  N N 88  
ASN   CB   C  N N 89  
ASN   CG   C  N N 90  
ASN   OD1  O  N N 91  
ASN   ND2  N  N N 92  
ASN   OXT  O  N N 93  
ASN   H    H  N N 94  
ASN   H2   H  N N 95  
ASN   HA   H  N N 96  
ASN   HB2  H  N N 97  
ASN   HB3  H  N N 98  
ASN   HD21 H  N N 99  
ASN   HD22 H  N N 100 
ASN   HXT  H  N N 101 
ASP   N    N  N N 102 
ASP   CA   C  N S 103 
ASP   C    C  N N 104 
ASP   O    O  N N 105 
ASP   CB   C  N N 106 
ASP   CG   C  N N 107 
ASP   OD1  O  N N 108 
ASP   OD2  O  N N 109 
ASP   OXT  O  N N 110 
ASP   H    H  N N 111 
ASP   H2   H  N N 112 
ASP   HA   H  N N 113 
ASP   HB2  H  N N 114 
ASP   HB3  H  N N 115 
ASP   HD2  H  N N 116 
ASP   HXT  H  N N 117 
CYS   N    N  N N 118 
CYS   CA   C  N R 119 
CYS   C    C  N N 120 
CYS   O    O  N N 121 
CYS   CB   C  N N 122 
CYS   SG   S  N N 123 
CYS   OXT  O  N N 124 
CYS   H    H  N N 125 
CYS   H2   H  N N 126 
CYS   HA   H  N N 127 
CYS   HB2  H  N N 128 
CYS   HB3  H  N N 129 
CYS   HG   H  N N 130 
CYS   HXT  H  N N 131 
GLN   N    N  N N 132 
GLN   CA   C  N S 133 
GLN   C    C  N N 134 
GLN   O    O  N N 135 
GLN   CB   C  N N 136 
GLN   CG   C  N N 137 
GLN   CD   C  N N 138 
GLN   OE1  O  N N 139 
GLN   NE2  N  N N 140 
GLN   OXT  O  N N 141 
GLN   H    H  N N 142 
GLN   H2   H  N N 143 
GLN   HA   H  N N 144 
GLN   HB2  H  N N 145 
GLN   HB3  H  N N 146 
GLN   HG2  H  N N 147 
GLN   HG3  H  N N 148 
GLN   HE21 H  N N 149 
GLN   HE22 H  N N 150 
GLN   HXT  H  N N 151 
GLU   N    N  N N 152 
GLU   CA   C  N S 153 
GLU   C    C  N N 154 
GLU   O    O  N N 155 
GLU   CB   C  N N 156 
GLU   CG   C  N N 157 
GLU   CD   C  N N 158 
GLU   OE1  O  N N 159 
GLU   OE2  O  N N 160 
GLU   OXT  O  N N 161 
GLU   H    H  N N 162 
GLU   H2   H  N N 163 
GLU   HA   H  N N 164 
GLU   HB2  H  N N 165 
GLU   HB3  H  N N 166 
GLU   HG2  H  N N 167 
GLU   HG3  H  N N 168 
GLU   HE2  H  N N 169 
GLU   HXT  H  N N 170 
GLY   N    N  N N 171 
GLY   CA   C  N N 172 
GLY   C    C  N N 173 
GLY   O    O  N N 174 
GLY   OXT  O  N N 175 
GLY   H    H  N N 176 
GLY   H2   H  N N 177 
GLY   HA2  H  N N 178 
GLY   HA3  H  N N 179 
GLY   HXT  H  N N 180 
H4B   N1   N  Y N 181 
H4B   C2   C  Y N 182 
H4B   N2   N  N N 183 
H4B   N3   N  Y N 184 
H4B   C4   C  Y N 185 
H4B   O4   O  N N 186 
H4B   C4A  C  Y N 187 
H4B   C8A  C  Y N 188 
H4B   N5   N  N N 189 
H4B   N8   N  N N 190 
H4B   C6   C  N R 191 
H4B   C7   C  N N 192 
H4B   C9   C  N R 193 
H4B   O9   O  N N 194 
H4B   C10  C  N S 195 
H4B   C11  C  N N 196 
H4B   O10  O  N N 197 
H4B   HN21 H  N N 198 
H4B   HN22 H  N N 199 
H4B   HN3  H  N N 200 
H4B   HN5  H  N N 201 
H4B   HN8  H  N N 202 
H4B   H6   H  N N 203 
H4B   H71  H  N N 204 
H4B   H72  H  N N 205 
H4B   H9   H  N N 206 
H4B   HO9  H  N N 207 
H4B   H10  H  N N 208 
H4B   H111 H  N N 209 
H4B   H112 H  N N 210 
H4B   H113 H  N N 211 
H4B   HO0  H  N N 212 
HEM   CHA  C  N N 213 
HEM   CHB  C  N N 214 
HEM   CHC  C  N N 215 
HEM   CHD  C  N N 216 
HEM   C1A  C  Y N 217 
HEM   C2A  C  Y N 218 
HEM   C3A  C  Y N 219 
HEM   C4A  C  Y N 220 
HEM   CMA  C  N N 221 
HEM   CAA  C  N N 222 
HEM   CBA  C  N N 223 
HEM   CGA  C  N N 224 
HEM   O1A  O  N N 225 
HEM   O2A  O  N N 226 
HEM   C1B  C  N N 227 
HEM   C2B  C  N N 228 
HEM   C3B  C  N N 229 
HEM   C4B  C  N N 230 
HEM   CMB  C  N N 231 
HEM   CAB  C  N N 232 
HEM   CBB  C  N N 233 
HEM   C1C  C  Y N 234 
HEM   C2C  C  Y N 235 
HEM   C3C  C  Y N 236 
HEM   C4C  C  Y N 237 
HEM   CMC  C  N N 238 
HEM   CAC  C  N N 239 
HEM   CBC  C  N N 240 
HEM   C1D  C  N N 241 
HEM   C2D  C  N N 242 
HEM   C3D  C  N N 243 
HEM   C4D  C  N N 244 
HEM   CMD  C  N N 245 
HEM   CAD  C  N N 246 
HEM   CBD  C  N N 247 
HEM   CGD  C  N N 248 
HEM   O1D  O  N N 249 
HEM   O2D  O  N N 250 
HEM   NA   N  Y N 251 
HEM   NB   N  N N 252 
HEM   NC   N  Y N 253 
HEM   ND   N  N N 254 
HEM   FE   FE N N 255 
HEM   HHB  H  N N 256 
HEM   HHC  H  N N 257 
HEM   HHD  H  N N 258 
HEM   HMA  H  N N 259 
HEM   HMAA H  N N 260 
HEM   HMAB H  N N 261 
HEM   HAA  H  N N 262 
HEM   HAAA H  N N 263 
HEM   HBA  H  N N 264 
HEM   HBAA H  N N 265 
HEM   HMB  H  N N 266 
HEM   HMBA H  N N 267 
HEM   HMBB H  N N 268 
HEM   HAB  H  N N 269 
HEM   HBB  H  N N 270 
HEM   HBBA H  N N 271 
HEM   HMC  H  N N 272 
HEM   HMCA H  N N 273 
HEM   HMCB H  N N 274 
HEM   HAC  H  N N 275 
HEM   HBC  H  N N 276 
HEM   HBCA H  N N 277 
HEM   HMD  H  N N 278 
HEM   HMDA H  N N 279 
HEM   HMDB H  N N 280 
HEM   HAD  H  N N 281 
HEM   HADA H  N N 282 
HEM   HBD  H  N N 283 
HEM   HBDA H  N N 284 
HEM   H2A  H  N N 285 
HEM   H2D  H  N N 286 
HEM   HHA  H  N N 287 
HIS   N    N  N N 288 
HIS   CA   C  N S 289 
HIS   C    C  N N 290 
HIS   O    O  N N 291 
HIS   CB   C  N N 292 
HIS   CG   C  Y N 293 
HIS   ND1  N  Y N 294 
HIS   CD2  C  Y N 295 
HIS   CE1  C  Y N 296 
HIS   NE2  N  Y N 297 
HIS   OXT  O  N N 298 
HIS   H    H  N N 299 
HIS   H2   H  N N 300 
HIS   HA   H  N N 301 
HIS   HB2  H  N N 302 
HIS   HB3  H  N N 303 
HIS   HD1  H  N N 304 
HIS   HD2  H  N N 305 
HIS   HE1  H  N N 306 
HIS   HE2  H  N N 307 
HIS   HXT  H  N N 308 
HOH   O    O  N N 309 
HOH   H1   H  N N 310 
HOH   H2   H  N N 311 
ILE   N    N  N N 312 
ILE   CA   C  N S 313 
ILE   C    C  N N 314 
ILE   O    O  N N 315 
ILE   CB   C  N S 316 
ILE   CG1  C  N N 317 
ILE   CG2  C  N N 318 
ILE   CD1  C  N N 319 
ILE   OXT  O  N N 320 
ILE   H    H  N N 321 
ILE   H2   H  N N 322 
ILE   HA   H  N N 323 
ILE   HB   H  N N 324 
ILE   HG12 H  N N 325 
ILE   HG13 H  N N 326 
ILE   HG21 H  N N 327 
ILE   HG22 H  N N 328 
ILE   HG23 H  N N 329 
ILE   HD11 H  N N 330 
ILE   HD12 H  N N 331 
ILE   HD13 H  N N 332 
ILE   HXT  H  N N 333 
LEU   N    N  N N 334 
LEU   CA   C  N S 335 
LEU   C    C  N N 336 
LEU   O    O  N N 337 
LEU   CB   C  N N 338 
LEU   CG   C  N N 339 
LEU   CD1  C  N N 340 
LEU   CD2  C  N N 341 
LEU   OXT  O  N N 342 
LEU   H    H  N N 343 
LEU   H2   H  N N 344 
LEU   HA   H  N N 345 
LEU   HB2  H  N N 346 
LEU   HB3  H  N N 347 
LEU   HG   H  N N 348 
LEU   HD11 H  N N 349 
LEU   HD12 H  N N 350 
LEU   HD13 H  N N 351 
LEU   HD21 H  N N 352 
LEU   HD22 H  N N 353 
LEU   HD23 H  N N 354 
LEU   HXT  H  N N 355 
LYS   N    N  N N 356 
LYS   CA   C  N S 357 
LYS   C    C  N N 358 
LYS   O    O  N N 359 
LYS   CB   C  N N 360 
LYS   CG   C  N N 361 
LYS   CD   C  N N 362 
LYS   CE   C  N N 363 
LYS   NZ   N  N N 364 
LYS   OXT  O  N N 365 
LYS   H    H  N N 366 
LYS   H2   H  N N 367 
LYS   HA   H  N N 368 
LYS   HB2  H  N N 369 
LYS   HB3  H  N N 370 
LYS   HG2  H  N N 371 
LYS   HG3  H  N N 372 
LYS   HD2  H  N N 373 
LYS   HD3  H  N N 374 
LYS   HE2  H  N N 375 
LYS   HE3  H  N N 376 
LYS   HZ1  H  N N 377 
LYS   HZ2  H  N N 378 
LYS   HZ3  H  N N 379 
LYS   HXT  H  N N 380 
MET   N    N  N N 381 
MET   CA   C  N S 382 
MET   C    C  N N 383 
MET   O    O  N N 384 
MET   CB   C  N N 385 
MET   CG   C  N N 386 
MET   SD   S  N N 387 
MET   CE   C  N N 388 
MET   OXT  O  N N 389 
MET   H    H  N N 390 
MET   H2   H  N N 391 
MET   HA   H  N N 392 
MET   HB2  H  N N 393 
MET   HB3  H  N N 394 
MET   HG2  H  N N 395 
MET   HG3  H  N N 396 
MET   HE1  H  N N 397 
MET   HE2  H  N N 398 
MET   HE3  H  N N 399 
MET   HXT  H  N N 400 
PHE   N    N  N N 401 
PHE   CA   C  N S 402 
PHE   C    C  N N 403 
PHE   O    O  N N 404 
PHE   CB   C  N N 405 
PHE   CG   C  Y N 406 
PHE   CD1  C  Y N 407 
PHE   CD2  C  Y N 408 
PHE   CE1  C  Y N 409 
PHE   CE2  C  Y N 410 
PHE   CZ   C  Y N 411 
PHE   OXT  O  N N 412 
PHE   H    H  N N 413 
PHE   H2   H  N N 414 
PHE   HA   H  N N 415 
PHE   HB2  H  N N 416 
PHE   HB3  H  N N 417 
PHE   HD1  H  N N 418 
PHE   HD2  H  N N 419 
PHE   HE1  H  N N 420 
PHE   HE2  H  N N 421 
PHE   HZ   H  N N 422 
PHE   HXT  H  N N 423 
PRO   N    N  N N 424 
PRO   CA   C  N S 425 
PRO   C    C  N N 426 
PRO   O    O  N N 427 
PRO   CB   C  N N 428 
PRO   CG   C  N N 429 
PRO   CD   C  N N 430 
PRO   OXT  O  N N 431 
PRO   H    H  N N 432 
PRO   HA   H  N N 433 
PRO   HB2  H  N N 434 
PRO   HB3  H  N N 435 
PRO   HG2  H  N N 436 
PRO   HG3  H  N N 437 
PRO   HD2  H  N N 438 
PRO   HD3  H  N N 439 
PRO   HXT  H  N N 440 
SER   N    N  N N 441 
SER   CA   C  N S 442 
SER   C    C  N N 443 
SER   O    O  N N 444 
SER   CB   C  N N 445 
SER   OG   O  N N 446 
SER   OXT  O  N N 447 
SER   H    H  N N 448 
SER   H2   H  N N 449 
SER   HA   H  N N 450 
SER   HB2  H  N N 451 
SER   HB3  H  N N 452 
SER   HG   H  N N 453 
SER   HXT  H  N N 454 
THR   N    N  N N 455 
THR   CA   C  N S 456 
THR   C    C  N N 457 
THR   O    O  N N 458 
THR   CB   C  N R 459 
THR   OG1  O  N N 460 
THR   CG2  C  N N 461 
THR   OXT  O  N N 462 
THR   H    H  N N 463 
THR   H2   H  N N 464 
THR   HA   H  N N 465 
THR   HB   H  N N 466 
THR   HG1  H  N N 467 
THR   HG21 H  N N 468 
THR   HG22 H  N N 469 
THR   HG23 H  N N 470 
THR   HXT  H  N N 471 
TRP   N    N  N N 472 
TRP   CA   C  N S 473 
TRP   C    C  N N 474 
TRP   O    O  N N 475 
TRP   CB   C  N N 476 
TRP   CG   C  Y N 477 
TRP   CD1  C  Y N 478 
TRP   CD2  C  Y N 479 
TRP   NE1  N  Y N 480 
TRP   CE2  C  Y N 481 
TRP   CE3  C  Y N 482 
TRP   CZ2  C  Y N 483 
TRP   CZ3  C  Y N 484 
TRP   CH2  C  Y N 485 
TRP   OXT  O  N N 486 
TRP   H    H  N N 487 
TRP   H2   H  N N 488 
TRP   HA   H  N N 489 
TRP   HB2  H  N N 490 
TRP   HB3  H  N N 491 
TRP   HD1  H  N N 492 
TRP   HE1  H  N N 493 
TRP   HE3  H  N N 494 
TRP   HZ2  H  N N 495 
TRP   HZ3  H  N N 496 
TRP   HH2  H  N N 497 
TRP   HXT  H  N N 498 
TYR   N    N  N N 499 
TYR   CA   C  N S 500 
TYR   C    C  N N 501 
TYR   O    O  N N 502 
TYR   CB   C  N N 503 
TYR   CG   C  Y N 504 
TYR   CD1  C  Y N 505 
TYR   CD2  C  Y N 506 
TYR   CE1  C  Y N 507 
TYR   CE2  C  Y N 508 
TYR   CZ   C  Y N 509 
TYR   OH   O  N N 510 
TYR   OXT  O  N N 511 
TYR   H    H  N N 512 
TYR   H2   H  N N 513 
TYR   HA   H  N N 514 
TYR   HB2  H  N N 515 
TYR   HB3  H  N N 516 
TYR   HD1  H  N N 517 
TYR   HD2  H  N N 518 
TYR   HE1  H  N N 519 
TYR   HE2  H  N N 520 
TYR   HH   H  N N 521 
TYR   HXT  H  N N 522 
VAL   N    N  N N 523 
VAL   CA   C  N S 524 
VAL   C    C  N N 525 
VAL   O    O  N N 526 
VAL   CB   C  N N 527 
VAL   CG1  C  N N 528 
VAL   CG2  C  N N 529 
VAL   OXT  O  N N 530 
VAL   H    H  N N 531 
VAL   H2   H  N N 532 
VAL   HA   H  N N 533 
VAL   HB   H  N N 534 
VAL   HG11 H  N N 535 
VAL   HG12 H  N N 536 
VAL   HG13 H  N N 537 
VAL   HG21 H  N N 538 
VAL   HG22 H  N N 539 
VAL   HG23 H  N N 540 
VAL   HXT  H  N N 541 
ZN    ZN   ZN N N 542 
# 
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 
A1A0C C07 C04  sing N N 1   
A1A0C C04 C03  doub Y N 2   
A1A0C C04 C05  sing Y N 3   
A1A0C C03 C02  sing Y N 4   
A1A0C C05 C06  doub Y N 5   
A1A0C F12 C12  sing N N 6   
A1A0C C02 N01  doub Y N 7   
A1A0C C02 N02  sing N N 8   
A1A0C C06 N01  sing Y N 9   
A1A0C C06 C11  sing N N 10  
A1A0C C12 C11  doub Y N 11  
A1A0C C12 C13  sing Y N 12  
A1A0C C11 C16  sing Y N 13  
A1A0C F13 C13  sing N N 14  
A1A0C C13 C14  doub Y N 15  
A1A0C C20 N19  sing N N 16  
A1A0C C16 C15  doub Y N 17  
A1A0C C14 C15  sing Y N 18  
A1A0C C18 N19  sing N N 19  
A1A0C C18 C17  sing N N 20  
A1A0C C15 C17  sing N N 21  
A1A0C C17 H1   sing N N 22  
A1A0C C17 H2   sing N N 23  
A1A0C C16 H3   sing N N 24  
A1A0C C14 H4   sing N N 25  
A1A0C C18 H5   sing N N 26  
A1A0C C18 H6   sing N N 27  
A1A0C C20 H7   sing N N 28  
A1A0C C20 H8   sing N N 29  
A1A0C C20 H9   sing N N 30  
A1A0C C03 H10  sing N N 31  
A1A0C C05 H11  sing N N 32  
A1A0C C07 H12  sing N N 33  
A1A0C C07 H13  sing N N 34  
A1A0C C07 H14  sing N N 35  
A1A0C N02 H15  sing N N 36  
A1A0C N02 H16  sing N N 37  
A1A0C N19 H17  sing N N 38  
ACT   C   O    doub N N 39  
ACT   C   OXT  sing N N 40  
ACT   C   CH3  sing N N 41  
ACT   CH3 H1   sing N N 42  
ACT   CH3 H2   sing N N 43  
ACT   CH3 H3   sing N N 44  
ALA   N   CA   sing N N 45  
ALA   N   H    sing N N 46  
ALA   N   H2   sing N N 47  
ALA   CA  C    sing N N 48  
ALA   CA  CB   sing N N 49  
ALA   CA  HA   sing N N 50  
ALA   C   O    doub N N 51  
ALA   C   OXT  sing N N 52  
ALA   CB  HB1  sing N N 53  
ALA   CB  HB2  sing N N 54  
ALA   CB  HB3  sing N N 55  
ALA   OXT HXT  sing N N 56  
ARG   N   CA   sing N N 57  
ARG   N   H    sing N N 58  
ARG   N   H2   sing N N 59  
ARG   CA  C    sing N N 60  
ARG   CA  CB   sing N N 61  
ARG   CA  HA   sing N N 62  
ARG   C   O    doub N N 63  
ARG   C   OXT  sing N N 64  
ARG   CB  CG   sing N N 65  
ARG   CB  HB2  sing N N 66  
ARG   CB  HB3  sing N N 67  
ARG   CG  CD   sing N N 68  
ARG   CG  HG2  sing N N 69  
ARG   CG  HG3  sing N N 70  
ARG   CD  NE   sing N N 71  
ARG   CD  HD2  sing N N 72  
ARG   CD  HD3  sing N N 73  
ARG   NE  CZ   sing N N 74  
ARG   NE  HE   sing N N 75  
ARG   CZ  NH1  sing N N 76  
ARG   CZ  NH2  doub N N 77  
ARG   NH1 HH11 sing N N 78  
ARG   NH1 HH12 sing N N 79  
ARG   NH2 HH21 sing N N 80  
ARG   NH2 HH22 sing N N 81  
ARG   OXT HXT  sing N N 82  
ASN   N   CA   sing N N 83  
ASN   N   H    sing N N 84  
ASN   N   H2   sing N N 85  
ASN   CA  C    sing N N 86  
ASN   CA  CB   sing N N 87  
ASN   CA  HA   sing N N 88  
ASN   C   O    doub N N 89  
ASN   C   OXT  sing N N 90  
ASN   CB  CG   sing N N 91  
ASN   CB  HB2  sing N N 92  
ASN   CB  HB3  sing N N 93  
ASN   CG  OD1  doub N N 94  
ASN   CG  ND2  sing N N 95  
ASN   ND2 HD21 sing N N 96  
ASN   ND2 HD22 sing N N 97  
ASN   OXT HXT  sing N N 98  
ASP   N   CA   sing N N 99  
ASP   N   H    sing N N 100 
ASP   N   H2   sing N N 101 
ASP   CA  C    sing N N 102 
ASP   CA  CB   sing N N 103 
ASP   CA  HA   sing N N 104 
ASP   C   O    doub N N 105 
ASP   C   OXT  sing N N 106 
ASP   CB  CG   sing N N 107 
ASP   CB  HB2  sing N N 108 
ASP   CB  HB3  sing N N 109 
ASP   CG  OD1  doub N N 110 
ASP   CG  OD2  sing N N 111 
ASP   OD2 HD2  sing N N 112 
ASP   OXT HXT  sing N N 113 
CYS   N   CA   sing N N 114 
CYS   N   H    sing N N 115 
CYS   N   H2   sing N N 116 
CYS   CA  C    sing N N 117 
CYS   CA  CB   sing N N 118 
CYS   CA  HA   sing N N 119 
CYS   C   O    doub N N 120 
CYS   C   OXT  sing N N 121 
CYS   CB  SG   sing N N 122 
CYS   CB  HB2  sing N N 123 
CYS   CB  HB3  sing N N 124 
CYS   SG  HG   sing N N 125 
CYS   OXT HXT  sing N N 126 
GLN   N   CA   sing N N 127 
GLN   N   H    sing N N 128 
GLN   N   H2   sing N N 129 
GLN   CA  C    sing N N 130 
GLN   CA  CB   sing N N 131 
GLN   CA  HA   sing N N 132 
GLN   C   O    doub N N 133 
GLN   C   OXT  sing N N 134 
GLN   CB  CG   sing N N 135 
GLN   CB  HB2  sing N N 136 
GLN   CB  HB3  sing N N 137 
GLN   CG  CD   sing N N 138 
GLN   CG  HG2  sing N N 139 
GLN   CG  HG3  sing N N 140 
GLN   CD  OE1  doub N N 141 
GLN   CD  NE2  sing N N 142 
GLN   NE2 HE21 sing N N 143 
GLN   NE2 HE22 sing N N 144 
GLN   OXT HXT  sing N N 145 
GLU   N   CA   sing N N 146 
GLU   N   H    sing N N 147 
GLU   N   H2   sing N N 148 
GLU   CA  C    sing N N 149 
GLU   CA  CB   sing N N 150 
GLU   CA  HA   sing N N 151 
GLU   C   O    doub N N 152 
GLU   C   OXT  sing N N 153 
GLU   CB  CG   sing N N 154 
GLU   CB  HB2  sing N N 155 
GLU   CB  HB3  sing N N 156 
GLU   CG  CD   sing N N 157 
GLU   CG  HG2  sing N N 158 
GLU   CG  HG3  sing N N 159 
GLU   CD  OE1  doub N N 160 
GLU   CD  OE2  sing N N 161 
GLU   OE2 HE2  sing N N 162 
GLU   OXT HXT  sing N N 163 
GLY   N   CA   sing N N 164 
GLY   N   H    sing N N 165 
GLY   N   H2   sing N N 166 
GLY   CA  C    sing N N 167 
GLY   CA  HA2  sing N N 168 
GLY   CA  HA3  sing N N 169 
GLY   C   O    doub N N 170 
GLY   C   OXT  sing N N 171 
GLY   OXT HXT  sing N N 172 
H4B   N1  C2   doub Y N 173 
H4B   N1  C8A  sing Y N 174 
H4B   C2  N2   sing N N 175 
H4B   C2  N3   sing Y N 176 
H4B   N2  HN21 sing N N 177 
H4B   N2  HN22 sing N N 178 
H4B   N3  C4   sing Y N 179 
H4B   N3  HN3  sing N N 180 
H4B   C4  O4   doub N N 181 
H4B   C4  C4A  sing Y N 182 
H4B   C4A C8A  doub Y N 183 
H4B   C4A N5   sing N N 184 
H4B   C8A N8   sing N N 185 
H4B   N5  C6   sing N N 186 
H4B   N5  HN5  sing N N 187 
H4B   N8  C7   sing N N 188 
H4B   N8  HN8  sing N N 189 
H4B   C6  C7   sing N N 190 
H4B   C6  C9   sing N N 191 
H4B   C6  H6   sing N N 192 
H4B   C7  H71  sing N N 193 
H4B   C7  H72  sing N N 194 
H4B   C9  O9   sing N N 195 
H4B   C9  C10  sing N N 196 
H4B   C9  H9   sing N N 197 
H4B   O9  HO9  sing N N 198 
H4B   C10 C11  sing N N 199 
H4B   C10 O10  sing N N 200 
H4B   C10 H10  sing N N 201 
H4B   C11 H111 sing N N 202 
H4B   C11 H112 sing N N 203 
H4B   C11 H113 sing N N 204 
H4B   O10 HO0  sing N N 205 
HEM   CHA C1A  sing N N 206 
HEM   CHA C4D  doub N N 207 
HEM   CHA HHA  sing N N 208 
HEM   CHB C4A  sing N N 209 
HEM   CHB C1B  doub N N 210 
HEM   CHB HHB  sing N N 211 
HEM   CHC C4B  sing N N 212 
HEM   CHC C1C  doub N N 213 
HEM   CHC HHC  sing N N 214 
HEM   CHD C4C  doub N N 215 
HEM   CHD C1D  sing N N 216 
HEM   CHD HHD  sing N N 217 
HEM   C1A C2A  doub Y N 218 
HEM   C1A NA   sing Y N 219 
HEM   C2A C3A  sing Y N 220 
HEM   C2A CAA  sing N N 221 
HEM   C3A C4A  doub Y N 222 
HEM   C3A CMA  sing N N 223 
HEM   C4A NA   sing Y N 224 
HEM   CMA HMA  sing N N 225 
HEM   CMA HMAA sing N N 226 
HEM   CMA HMAB sing N N 227 
HEM   CAA CBA  sing N N 228 
HEM   CAA HAA  sing N N 229 
HEM   CAA HAAA sing N N 230 
HEM   CBA CGA  sing N N 231 
HEM   CBA HBA  sing N N 232 
HEM   CBA HBAA sing N N 233 
HEM   CGA O1A  doub N N 234 
HEM   CGA O2A  sing N N 235 
HEM   C1B C2B  sing N N 236 
HEM   C1B NB   sing N N 237 
HEM   C2B C3B  doub N N 238 
HEM   C2B CMB  sing N N 239 
HEM   C3B C4B  sing N N 240 
HEM   C3B CAB  sing N N 241 
HEM   C4B NB   doub N N 242 
HEM   CMB HMB  sing N N 243 
HEM   CMB HMBA sing N N 244 
HEM   CMB HMBB sing N N 245 
HEM   CAB CBB  doub N N 246 
HEM   CAB HAB  sing N N 247 
HEM   CBB HBB  sing N N 248 
HEM   CBB HBBA sing N N 249 
HEM   C1C C2C  sing Y N 250 
HEM   C1C NC   sing Y N 251 
HEM   C2C C3C  doub Y N 252 
HEM   C2C CMC  sing N N 253 
HEM   C3C C4C  sing Y N 254 
HEM   C3C CAC  sing N N 255 
HEM   C4C NC   sing Y N 256 
HEM   CMC HMC  sing N N 257 
HEM   CMC HMCA sing N N 258 
HEM   CMC HMCB sing N N 259 
HEM   CAC CBC  doub N N 260 
HEM   CAC HAC  sing N N 261 
HEM   CBC HBC  sing N N 262 
HEM   CBC HBCA sing N N 263 
HEM   C1D C2D  sing N N 264 
HEM   C1D ND   doub N N 265 
HEM   C2D C3D  doub N N 266 
HEM   C2D CMD  sing N N 267 
HEM   C3D C4D  sing N N 268 
HEM   C3D CAD  sing N N 269 
HEM   C4D ND   sing N N 270 
HEM   CMD HMD  sing N N 271 
HEM   CMD HMDA sing N N 272 
HEM   CMD HMDB sing N N 273 
HEM   CAD CBD  sing N N 274 
HEM   CAD HAD  sing N N 275 
HEM   CAD HADA sing N N 276 
HEM   CBD CGD  sing N N 277 
HEM   CBD HBD  sing N N 278 
HEM   CBD HBDA sing N N 279 
HEM   CGD O1D  doub N N 280 
HEM   CGD O2D  sing N N 281 
HEM   O2A H2A  sing N N 282 
HEM   O2D H2D  sing N N 283 
HEM   FE  NA   sing N N 284 
HEM   FE  NB   sing N N 285 
HEM   FE  NC   sing N N 286 
HEM   FE  ND   sing N N 287 
HIS   N   CA   sing N N 288 
HIS   N   H    sing N N 289 
HIS   N   H2   sing N N 290 
HIS   CA  C    sing N N 291 
HIS   CA  CB   sing N N 292 
HIS   CA  HA   sing N N 293 
HIS   C   O    doub N N 294 
HIS   C   OXT  sing N N 295 
HIS   CB  CG   sing N N 296 
HIS   CB  HB2  sing N N 297 
HIS   CB  HB3  sing N N 298 
HIS   CG  ND1  sing Y N 299 
HIS   CG  CD2  doub Y N 300 
HIS   ND1 CE1  doub Y N 301 
HIS   ND1 HD1  sing N N 302 
HIS   CD2 NE2  sing Y N 303 
HIS   CD2 HD2  sing N N 304 
HIS   CE1 NE2  sing Y N 305 
HIS   CE1 HE1  sing N N 306 
HIS   NE2 HE2  sing N N 307 
HIS   OXT HXT  sing N N 308 
HOH   O   H1   sing N N 309 
HOH   O   H2   sing N N 310 
ILE   N   CA   sing N N 311 
ILE   N   H    sing N N 312 
ILE   N   H2   sing N N 313 
ILE   CA  C    sing N N 314 
ILE   CA  CB   sing N N 315 
ILE   CA  HA   sing N N 316 
ILE   C   O    doub N N 317 
ILE   C   OXT  sing N N 318 
ILE   CB  CG1  sing N N 319 
ILE   CB  CG2  sing N N 320 
ILE   CB  HB   sing N N 321 
ILE   CG1 CD1  sing N N 322 
ILE   CG1 HG12 sing N N 323 
ILE   CG1 HG13 sing N N 324 
ILE   CG2 HG21 sing N N 325 
ILE   CG2 HG22 sing N N 326 
ILE   CG2 HG23 sing N N 327 
ILE   CD1 HD11 sing N N 328 
ILE   CD1 HD12 sing N N 329 
ILE   CD1 HD13 sing N N 330 
ILE   OXT HXT  sing N N 331 
LEU   N   CA   sing N N 332 
LEU   N   H    sing N N 333 
LEU   N   H2   sing N N 334 
LEU   CA  C    sing N N 335 
LEU   CA  CB   sing N N 336 
LEU   CA  HA   sing N N 337 
LEU   C   O    doub N N 338 
LEU   C   OXT  sing N N 339 
LEU   CB  CG   sing N N 340 
LEU   CB  HB2  sing N N 341 
LEU   CB  HB3  sing N N 342 
LEU   CG  CD1  sing N N 343 
LEU   CG  CD2  sing N N 344 
LEU   CG  HG   sing N N 345 
LEU   CD1 HD11 sing N N 346 
LEU   CD1 HD12 sing N N 347 
LEU   CD1 HD13 sing N N 348 
LEU   CD2 HD21 sing N N 349 
LEU   CD2 HD22 sing N N 350 
LEU   CD2 HD23 sing N N 351 
LEU   OXT HXT  sing N N 352 
LYS   N   CA   sing N N 353 
LYS   N   H    sing N N 354 
LYS   N   H2   sing N N 355 
LYS   CA  C    sing N N 356 
LYS   CA  CB   sing N N 357 
LYS   CA  HA   sing N N 358 
LYS   C   O    doub N N 359 
LYS   C   OXT  sing N N 360 
LYS   CB  CG   sing N N 361 
LYS   CB  HB2  sing N N 362 
LYS   CB  HB3  sing N N 363 
LYS   CG  CD   sing N N 364 
LYS   CG  HG2  sing N N 365 
LYS   CG  HG3  sing N N 366 
LYS   CD  CE   sing N N 367 
LYS   CD  HD2  sing N N 368 
LYS   CD  HD3  sing N N 369 
LYS   CE  NZ   sing N N 370 
LYS   CE  HE2  sing N N 371 
LYS   CE  HE3  sing N N 372 
LYS   NZ  HZ1  sing N N 373 
LYS   NZ  HZ2  sing N N 374 
LYS   NZ  HZ3  sing N N 375 
LYS   OXT HXT  sing N N 376 
MET   N   CA   sing N N 377 
MET   N   H    sing N N 378 
MET   N   H2   sing N N 379 
MET   CA  C    sing N N 380 
MET   CA  CB   sing N N 381 
MET   CA  HA   sing N N 382 
MET   C   O    doub N N 383 
MET   C   OXT  sing N N 384 
MET   CB  CG   sing N N 385 
MET   CB  HB2  sing N N 386 
MET   CB  HB3  sing N N 387 
MET   CG  SD   sing N N 388 
MET   CG  HG2  sing N N 389 
MET   CG  HG3  sing N N 390 
MET   SD  CE   sing N N 391 
MET   CE  HE1  sing N N 392 
MET   CE  HE2  sing N N 393 
MET   CE  HE3  sing N N 394 
MET   OXT HXT  sing N N 395 
PHE   N   CA   sing N N 396 
PHE   N   H    sing N N 397 
PHE   N   H2   sing N N 398 
PHE   CA  C    sing N N 399 
PHE   CA  CB   sing N N 400 
PHE   CA  HA   sing N N 401 
PHE   C   O    doub N N 402 
PHE   C   OXT  sing N N 403 
PHE   CB  CG   sing N N 404 
PHE   CB  HB2  sing N N 405 
PHE   CB  HB3  sing N N 406 
PHE   CG  CD1  doub Y N 407 
PHE   CG  CD2  sing Y N 408 
PHE   CD1 CE1  sing Y N 409 
PHE   CD1 HD1  sing N N 410 
PHE   CD2 CE2  doub Y N 411 
PHE   CD2 HD2  sing N N 412 
PHE   CE1 CZ   doub Y N 413 
PHE   CE1 HE1  sing N N 414 
PHE   CE2 CZ   sing Y N 415 
PHE   CE2 HE2  sing N N 416 
PHE   CZ  HZ   sing N N 417 
PHE   OXT HXT  sing N N 418 
PRO   N   CA   sing N N 419 
PRO   N   CD   sing N N 420 
PRO   N   H    sing N N 421 
PRO   CA  C    sing N N 422 
PRO   CA  CB   sing N N 423 
PRO   CA  HA   sing N N 424 
PRO   C   O    doub N N 425 
PRO   C   OXT  sing N N 426 
PRO   CB  CG   sing N N 427 
PRO   CB  HB2  sing N N 428 
PRO   CB  HB3  sing N N 429 
PRO   CG  CD   sing N N 430 
PRO   CG  HG2  sing N N 431 
PRO   CG  HG3  sing N N 432 
PRO   CD  HD2  sing N N 433 
PRO   CD  HD3  sing N N 434 
PRO   OXT HXT  sing N N 435 
SER   N   CA   sing N N 436 
SER   N   H    sing N N 437 
SER   N   H2   sing N N 438 
SER   CA  C    sing N N 439 
SER   CA  CB   sing N N 440 
SER   CA  HA   sing N N 441 
SER   C   O    doub N N 442 
SER   C   OXT  sing N N 443 
SER   CB  OG   sing N N 444 
SER   CB  HB2  sing N N 445 
SER   CB  HB3  sing N N 446 
SER   OG  HG   sing N N 447 
SER   OXT HXT  sing N N 448 
THR   N   CA   sing N N 449 
THR   N   H    sing N N 450 
THR   N   H2   sing N N 451 
THR   CA  C    sing N N 452 
THR   CA  CB   sing N N 453 
THR   CA  HA   sing N N 454 
THR   C   O    doub N N 455 
THR   C   OXT  sing N N 456 
THR   CB  OG1  sing N N 457 
THR   CB  CG2  sing N N 458 
THR   CB  HB   sing N N 459 
THR   OG1 HG1  sing N N 460 
THR   CG2 HG21 sing N N 461 
THR   CG2 HG22 sing N N 462 
THR   CG2 HG23 sing N N 463 
THR   OXT HXT  sing N N 464 
TRP   N   CA   sing N N 465 
TRP   N   H    sing N N 466 
TRP   N   H2   sing N N 467 
TRP   CA  C    sing N N 468 
TRP   CA  CB   sing N N 469 
TRP   CA  HA   sing N N 470 
TRP   C   O    doub N N 471 
TRP   C   OXT  sing N N 472 
TRP   CB  CG   sing N N 473 
TRP   CB  HB2  sing N N 474 
TRP   CB  HB3  sing N N 475 
TRP   CG  CD1  doub Y N 476 
TRP   CG  CD2  sing Y N 477 
TRP   CD1 NE1  sing Y N 478 
TRP   CD1 HD1  sing N N 479 
TRP   CD2 CE2  doub Y N 480 
TRP   CD2 CE3  sing Y N 481 
TRP   NE1 CE2  sing Y N 482 
TRP   NE1 HE1  sing N N 483 
TRP   CE2 CZ2  sing Y N 484 
TRP   CE3 CZ3  doub Y N 485 
TRP   CE3 HE3  sing N N 486 
TRP   CZ2 CH2  doub Y N 487 
TRP   CZ2 HZ2  sing N N 488 
TRP   CZ3 CH2  sing Y N 489 
TRP   CZ3 HZ3  sing N N 490 
TRP   CH2 HH2  sing N N 491 
TRP   OXT HXT  sing N N 492 
TYR   N   CA   sing N N 493 
TYR   N   H    sing N N 494 
TYR   N   H2   sing N N 495 
TYR   CA  C    sing N N 496 
TYR   CA  CB   sing N N 497 
TYR   CA  HA   sing N N 498 
TYR   C   O    doub N N 499 
TYR   C   OXT  sing N N 500 
TYR   CB  CG   sing N N 501 
TYR   CB  HB2  sing N N 502 
TYR   CB  HB3  sing N N 503 
TYR   CG  CD1  doub Y N 504 
TYR   CG  CD2  sing Y N 505 
TYR   CD1 CE1  sing Y N 506 
TYR   CD1 HD1  sing N N 507 
TYR   CD2 CE2  doub Y N 508 
TYR   CD2 HD2  sing N N 509 
TYR   CE1 CZ   doub Y N 510 
TYR   CE1 HE1  sing N N 511 
TYR   CE2 CZ   sing Y N 512 
TYR   CE2 HE2  sing N N 513 
TYR   CZ  OH   sing N N 514 
TYR   OH  HH   sing N N 515 
TYR   OXT HXT  sing N N 516 
VAL   N   CA   sing N N 517 
VAL   N   H    sing N N 518 
VAL   N   H2   sing N N 519 
VAL   CA  C    sing N N 520 
VAL   CA  CB   sing N N 521 
VAL   CA  HA   sing N N 522 
VAL   C   O    doub N N 523 
VAL   C   OXT  sing N N 524 
VAL   CB  CG1  sing N N 525 
VAL   CB  CG2  sing N N 526 
VAL   CB  HB   sing N N 527 
VAL   CG1 HG11 sing N N 528 
VAL   CG1 HG12 sing N N 529 
VAL   CG1 HG13 sing N N 530 
VAL   CG2 HG21 sing N N 531 
VAL   CG2 HG22 sing N N 532 
VAL   CG2 HG23 sing N N 533 
VAL   OXT HXT  sing N N 534 
# 
_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                    9CVR 
_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]   0.020657 
_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]   0.008863 
_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]   0.006149 
_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   ? -39.287 -23.062 39.347 1.00 108.65 ? 300 PHE   A N   1 
ATOM   2    C  CA  . PHE   A 1 4   ? -40.199 -21.941 39.144 1.00 109.22 ? 300 PHE   A CA  1 
ATOM   3    C  C   . PHE   A 1 4   ? -39.937 -20.842 40.169 1.00 104.47 ? 300 PHE   A C   1 
ATOM   4    O  O   . PHE   A 1 4   ? -40.711 -20.661 41.115 1.00 108.72 ? 300 PHE   A O   1 
ATOM   5    C  CB  . PHE   A 1 4   ? -41.646 -22.414 39.233 1.00 116.36 ? 300 PHE   A CB  1 
ATOM   6    C  CG  . PHE   A 1 4   ? -41.818 -23.879 38.959 1.00 124.18 ? 300 PHE   A CG  1 
ATOM   7    C  CD1 . PHE   A 1 4   ? -41.853 -24.357 37.659 1.00 124.50 ? 300 PHE   A CD1 1 
ATOM   8    C  CD2 . PHE   A 1 4   ? -41.941 -24.780 40.004 1.00 129.67 ? 300 PHE   A CD2 1 
ATOM   9    C  CE1 . PHE   A 1 4   ? -42.011 -25.707 37.407 1.00 128.96 ? 300 PHE   A CE1 1 
ATOM   10   C  CE2 . PHE   A 1 4   ? -42.100 -26.131 39.760 1.00 135.60 ? 300 PHE   A CE2 1 
ATOM   11   C  CZ  . PHE   A 1 4   ? -42.135 -26.596 38.460 1.00 134.00 ? 300 PHE   A CZ  1 
ATOM   12   N  N   . LEU   A 1 5   ? -38.848 -20.105 39.964 1.00 96.89  ? 301 LEU   A N   1 
ATOM   13   C  CA  . LEU   A 1 5   ? -38.315 -19.183 40.958 1.00 92.93  ? 301 LEU   A CA  1 
ATOM   14   C  C   . LEU   A 1 5   ? -38.984 -17.817 40.866 1.00 90.39  ? 301 LEU   A C   1 
ATOM   15   O  O   . LEU   A 1 5   ? -39.420 -17.384 39.797 1.00 89.06  ? 301 LEU   A O   1 
ATOM   16   C  CB  . LEU   A 1 5   ? -36.808 -19.020 40.769 1.00 89.35  ? 301 LEU   A CB  1 
ATOM   17   C  CG  . LEU   A 1 5   ? -36.065 -20.324 40.479 1.00 88.45  ? 301 LEU   A CG  1 
ATOM   18   C  CD1 . LEU   A 1 5   ? -35.017 -20.089 39.428 1.00 85.28  ? 301 LEU   A CD1 1 
ATOM   19   C  CD2 . LEU   A 1 5   ? -35.439 -20.877 41.732 1.00 87.17  ? 301 LEU   A CD2 1 
ATOM   20   N  N   . LYS   A 1 6   ? -39.036 -17.127 42.002 1.00 88.70  ? 302 LYS   A N   1 
ATOM   21   C  CA  . LYS   A 1 6   ? -39.634 -15.804 42.089 1.00 86.18  ? 302 LYS   A CA  1 
ATOM   22   C  C   . LYS   A 1 6   ? -38.546 -14.742 42.148 1.00 81.30  ? 302 LYS   A C   1 
ATOM   23   O  O   . LYS   A 1 6   ? -37.517 -14.931 42.805 1.00 77.75  ? 302 LYS   A O   1 
ATOM   24   C  CB  . LYS   A 1 6   ? -40.534 -15.686 43.318 1.00 88.50  ? 302 LYS   A CB  1 
ATOM   25   C  CG  . LYS   A 1 6   ? -41.388 -16.920 43.599 1.00 94.62  ? 302 LYS   A CG  1 
ATOM   26   C  CD  . LYS   A 1 6   ? -42.726 -16.845 42.874 1.00 97.01  ? 302 LYS   A CD  1 
ATOM   27   C  CE  . LYS   A 1 6   ? -43.484 -18.173 42.918 1.00 100.04 ? 302 LYS   A CE  1 
ATOM   28   N  NZ  . LYS   A 1 6   ? -43.820 -18.618 44.302 1.00 99.62  ? 302 LYS   A NZ  1 
ATOM   29   N  N   . VAL   A 1 7   ? -38.772 -13.636 41.446 1.00 80.09  ? 303 VAL   A N   1 
ATOM   30   C  CA  . VAL   A 1 7   ? -37.916 -12.460 41.520 1.00 75.48  ? 303 VAL   A CA  1 
ATOM   31   C  C   . VAL   A 1 7   ? -38.760 -11.300 42.023 1.00 76.45  ? 303 VAL   A C   1 
ATOM   32   O  O   . VAL   A 1 7   ? -39.881 -11.081 41.546 1.00 78.09  ? 303 VAL   A O   1 
ATOM   33   C  CB  . VAL   A 1 7   ? -37.253 -12.134 40.167 1.00 73.82  ? 303 VAL   A CB  1 
ATOM   34   C  CG1 . VAL   A 1 7   ? -36.517 -13.346 39.658 1.00 73.62  ? 303 VAL   A CG1 1 
ATOM   35   C  CG2 . VAL   A 1 7   ? -38.266 -11.668 39.126 1.00 75.03  ? 303 VAL   A CG2 1 
ATOM   36   N  N   . LYS   A 1 8   ? -38.239 -10.585 43.012 1.00 74.00  ? 304 LYS   A N   1 
ATOM   37   C  CA  . LYS   A 1 8   ? -38.955 -9.497  43.656 1.00 74.23  ? 304 LYS   A CA  1 
ATOM   38   C  C   . LYS   A 1 8   ? -38.354 -8.167  43.236 1.00 73.25  ? 304 LYS   A C   1 
ATOM   39   O  O   . LYS   A 1 8   ? -37.158 -8.062  42.964 1.00 70.85  ? 304 LYS   A O   1 
ATOM   40   C  CB  . LYS   A 1 8   ? -38.906 -9.628  45.189 1.00 73.81  ? 304 LYS   A CB  1 
ATOM   41   C  CG  . LYS   A 1 8   ? -39.789 -8.630  45.941 1.00 77.52  ? 304 LYS   A CG  1 
ATOM   42   C  CD  . LYS   A 1 8   ? -39.868 -8.965  47.441 1.00 76.91  ? 304 LYS   A CD  1 
ATOM   43   C  CE  . LYS   A 1 8   ? -40.652 -7.922  48.235 1.00 81.01  ? 304 LYS   A CE  1 
ATOM   44   N  NZ  . LYS   A 1 8   ? -40.829 -8.335  49.667 1.00 83.72  ? 304 LYS   A NZ  1 
ATOM   45   N  N   . ASN   A 1 9   ? -39.197 -7.154  43.155 1.00 76.15  ? 305 ASN   A N   1 
ATOM   46   C  CA  . ASN   A 1 9   ? -38.737 -5.777  43.090 1.00 77.03  ? 305 ASN   A CA  1 
ATOM   47   C  C   . ASN   A 1 9   ? -38.952 -5.192  44.479 1.00 80.14  ? 305 ASN   A C   1 
ATOM   48   O  O   . ASN   A 1 9   ? -40.064 -5.244  45.013 1.00 82.93  ? 305 ASN   A O   1 
ATOM   49   C  CB  . ASN   A 1 9   ? -39.473 -4.976  42.009 1.00 77.23  ? 305 ASN   A CB  1 
ATOM   50   C  CG  . ASN   A 1 9   ? -38.985 -3.528  41.914 1.00 78.39  ? 305 ASN   A CG  1 
ATOM   51   O  OD1 . ASN   A 1 9   ? -38.949 -2.804  42.910 1.00 80.30  ? 305 ASN   A OD1 1 
ATOM   52   N  ND2 . ASN   A 1 9   ? -38.599 -3.108  40.711 1.00 71.60  ? 305 ASN   A ND2 1 
ATOM   53   N  N   . TRP   A 1 10  ? -37.884 -4.681  45.078 1.00 77.66  ? 306 TRP   A N   1 
ATOM   54   C  CA  . TRP   A 1 10  ? -37.934 -4.186  46.446 1.00 80.11  ? 306 TRP   A CA  1 
ATOM   55   C  C   . TRP   A 1 10  ? -38.243 -2.698  46.527 1.00 83.00  ? 306 TRP   A C   1 
ATOM   56   O  O   . TRP   A 1 10  ? -38.230 -2.134  47.624 1.00 87.73  ? 306 TRP   A O   1 
ATOM   57   C  CB  . TRP   A 1 10  ? -36.620 -4.494  47.154 1.00 76.64  ? 306 TRP   A CB  1 
ATOM   58   C  CG  . TRP   A 1 10  ? -36.404 -5.955  47.330 1.00 73.99  ? 306 TRP   A CG  1 
ATOM   59   C  CD1 . TRP   A 1 10  ? -35.760 -6.788  46.480 1.00 71.63  ? 306 TRP   A CD1 1 
ATOM   60   C  CD2 . TRP   A 1 10  ? -36.837 -6.761  48.432 1.00 76.62  ? 306 TRP   A CD2 1 
ATOM   61   N  NE1 . TRP   A 1 10  ? -35.767 -8.065  46.967 1.00 68.35  ? 306 TRP   A NE1 1 
ATOM   62   C  CE2 . TRP   A 1 10  ? -36.417 -8.078  48.171 1.00 75.54  ? 306 TRP   A CE2 1 
ATOM   63   C  CE3 . TRP   A 1 10  ? -37.544 -6.501  49.602 1.00 74.42  ? 306 TRP   A CE3 1 
ATOM   64   C  CZ2 . TRP   A 1 10  ? -36.669 -9.128  49.045 1.00 76.29  ? 306 TRP   A CZ2 1 
ATOM   65   C  CZ3 . TRP   A 1 10  ? -37.798 -7.545  50.467 1.00 76.87  ? 306 TRP   A CZ3 1 
ATOM   66   C  CH2 . TRP   A 1 10  ? -37.365 -8.844  50.181 1.00 75.18  ? 306 TRP   A CH2 1 
ATOM   67   N  N   . GLU   A 1 11  ? -38.509 -2.051  45.396 1.00 83.63  ? 307 GLU   A N   1 
ATOM   68   C  CA  . GLU   A 1 11  ? -39.055 -0.700  45.383 1.00 86.25  ? 307 GLU   A CA  1 
ATOM   69   C  C   . GLU   A 1 11  ? -40.565 -0.690  45.205 1.00 89.60  ? 307 GLU   A C   1 
ATOM   70   O  O   . GLU   A 1 11  ? -41.234 0.202   45.735 1.00 95.82  ? 307 GLU   A O   1 
ATOM   71   C  CB  . GLU   A 1 11  ? -38.412 0.130   44.258 1.00 85.95  ? 307 GLU   A CB  1 
ATOM   72   C  CG  . GLU   A 1 11  ? -38.738 1.629   44.299 1.00 87.44  ? 307 GLU   A CG  1 
ATOM   73   C  CD  . GLU   A 1 11  ? -38.597 2.314   42.923 1.00 93.84  ? 307 GLU   A CD  1 
ATOM   74   O  OE1 . GLU   A 1 11  ? -37.975 1.738   42.001 1.00 86.35  ? 307 GLU   A OE1 1 
ATOM   75   O  OE2 . GLU   A 1 11  ? -39.118 3.446   42.770 1.00 102.80 ? 307 GLU   A OE2 1 
ATOM   76   N  N   . THR   A 1 12  ? -41.116 -1.676  44.489 1.00 89.62  ? 308 THR   A N   1 
ATOM   77   C  CA  . THR   A 1 12  ? -42.544 -1.755  44.206 1.00 93.05  ? 308 THR   A CA  1 
ATOM   78   C  C   . THR   A 1 12  ? -43.232 -2.963  44.823 1.00 94.79  ? 308 THR   A C   1 
ATOM   79   O  O   . THR   A 1 12  ? -44.449 -3.111  44.653 1.00 95.15  ? 308 THR   A O   1 
ATOM   80   C  CB  . THR   A 1 12  ? -42.792 -1.798  42.693 1.00 89.43  ? 308 THR   A CB  1 
ATOM   81   O  OG1 . THR   A 1 12  ? -42.332 -3.055  42.175 1.00 90.23  ? 308 THR   A OG1 1 
ATOM   82   C  CG2 . THR   A 1 12  ? -42.060 -0.668  41.995 1.00 91.09  ? 308 THR   A CG2 1 
ATOM   83   N  N   . ASP   A 1 13  ? -42.495 -3.845  45.496 1.00 100.94 ? 309 ASP   A N   1 
ATOM   84   C  CA  . ASP   A 1 13  ? -43.014 -5.086  46.066 1.00 99.41  ? 309 ASP   A CA  1 
ATOM   85   C  C   . ASP   A 1 13  ? -43.597 -6.024  45.004 1.00 99.94  ? 309 ASP   A C   1 
ATOM   86   O  O   . ASP   A 1 13  ? -44.260 -7.008  45.348 1.00 102.45 ? 309 ASP   A O   1 
ATOM   87   C  CB  . ASP   A 1 13  ? -44.059 -4.807  47.159 1.00 102.26 ? 309 ASP   A CB  1 
ATOM   88   C  CG  . ASP   A 1 13  ? -43.458 -4.137  48.405 1.00 111.80 ? 309 ASP   A CG  1 
ATOM   89   O  OD1 . ASP   A 1 13  ? -42.547 -4.727  49.032 1.00 114.61 ? 309 ASP   A OD1 1 
ATOM   90   O  OD2 . ASP   A 1 13  ? -43.910 -3.025  48.774 1.00 115.89 ? 309 ASP   A OD2 1 
ATOM   91   N  N   . VAL   A 1 14  ? -43.356 -5.754  43.719 1.00 94.13  ? 310 VAL   A N   1 
ATOM   92   C  CA  . VAL   A 1 14  ? -43.895 -6.593  42.654 1.00 92.92  ? 310 VAL   A CA  1 
ATOM   93   C  C   . VAL   A 1 14  ? -43.089 -7.879  42.541 1.00 90.51  ? 310 VAL   A C   1 
ATOM   94   O  O   . VAL   A 1 14  ? -41.850 -7.861  42.503 1.00 88.47  ? 310 VAL   A O   1 
ATOM   95   C  CB  . VAL   A 1 14  ? -43.898 -5.841  41.312 1.00 88.73  ? 310 VAL   A CB  1 
ATOM   96   C  CG1 . VAL   A 1 14  ? -44.052 -6.819  40.164 1.00 88.90  ? 310 VAL   A CG1 1 
ATOM   97   C  CG2 . VAL   A 1 14  ? -45.007 -4.815  41.276 1.00 85.42  ? 310 VAL   A CG2 1 
ATOM   98   N  N   . VAL   A 1 15  ? -43.792 -9.006  42.453 1.00 91.59  ? 311 VAL   A N   1 
ATOM   99   C  CA  . VAL   A 1 15  ? -43.169 -10.311 42.289 1.00 89.69  ? 311 VAL   A CA  1 
ATOM   100  C  C   . VAL   A 1 15  ? -43.535 -10.876 40.923 1.00 88.31  ? 311 VAL   A C   1 
ATOM   101  O  O   . VAL   A 1 15  ? -44.679 -10.756 40.469 1.00 89.51  ? 311 VAL   A O   1 
ATOM   102  C  CB  . VAL   A 1 15  ? -43.588 -11.273 43.418 1.00 90.66  ? 311 VAL   A CB  1 
ATOM   103  C  CG1 . VAL   A 1 15  ? -42.923 -12.631 43.240 1.00 89.37  ? 311 VAL   A CG1 1 
ATOM   104  C  CG2 . VAL   A 1 15  ? -43.227 -10.671 44.757 1.00 88.08  ? 311 VAL   A CG2 1 
ATOM   105  N  N   . LEU   A 1 16  ? -42.551 -11.474 40.264 1.00 85.76  ? 312 LEU   A N   1 
ATOM   106  C  CA  . LEU   A 1 16  ? -42.752 -12.182 39.012 1.00 87.19  ? 312 LEU   A CA  1 
ATOM   107  C  C   . LEU   A 1 16  ? -42.160 -13.573 39.157 1.00 86.30  ? 312 LEU   A C   1 
ATOM   108  O  O   . LEU   A 1 16  ? -41.136 -13.751 39.826 1.00 84.69  ? 312 LEU   A O   1 
ATOM   109  C  CB  . LEU   A 1 16  ? -42.104 -11.440 37.843 1.00 84.46  ? 312 LEU   A CB  1 
ATOM   110  C  CG  . LEU   A 1 16  ? -42.575 -9.994  37.679 1.00 85.73  ? 312 LEU   A CG  1 
ATOM   111  C  CD1 . LEU   A 1 16  ? -41.557 -9.185  36.905 1.00 80.54  ? 312 LEU   A CD1 1 
ATOM   112  C  CD2 . LEU   A 1 16  ? -43.933 -9.947  36.994 1.00 89.36  ? 312 LEU   A CD2 1 
ATOM   113  N  N   . THR   A 1 17  ? -42.816 -14.558 38.550 1.00 87.79  ? 313 THR   A N   1 
ATOM   114  C  CA  . THR   A 1 17  ? -42.365 -15.940 38.607 1.00 87.32  ? 313 THR   A CA  1 
ATOM   115  C  C   . THR   A 1 17  ? -41.676 -16.293 37.300 1.00 85.10  ? 313 THR   A C   1 
ATOM   116  O  O   . THR   A 1 17  ? -42.264 -16.145 36.224 1.00 87.14  ? 313 THR   A O   1 
ATOM   117  C  CB  . THR   A 1 17  ? -43.526 -16.902 38.859 1.00 89.88  ? 313 THR   A CB  1 
ATOM   118  O  OG1 . THR   A 1 17  ? -44.199 -16.543 40.072 1.00 93.09  ? 313 THR   A OG1 1 
ATOM   119  C  CG2 . THR   A 1 17  ? -43.009 -18.335 38.975 1.00 92.05  ? 313 THR   A CG2 1 
ATOM   120  N  N   . ASP   A 1 18  ? -40.437 -16.765 37.401 1.00 86.00  ? 314 ASP   A N   1 
ATOM   121  C  CA  . ASP   A 1 18  ? -39.630 -17.112 36.239 1.00 84.45  ? 314 ASP   A CA  1 
ATOM   122  C  C   . ASP   A 1 18  ? -39.692 -18.618 36.024 1.00 85.67  ? 314 ASP   A C   1 
ATOM   123  O  O   . ASP   A 1 18  ? -39.246 -19.389 36.876 1.00 88.07  ? 314 ASP   A O   1 
ATOM   124  C  CB  . ASP   A 1 18  ? -38.182 -16.649 36.424 1.00 81.98  ? 314 ASP   A CB  1 
ATOM   125  C  CG  . ASP   A 1 18  ? -37.354 -16.778 35.152 1.00 78.98  ? 314 ASP   A CG  1 
ATOM   126  O  OD1 . ASP   A 1 18  ? -37.162 -17.920 34.689 1.00 78.72  ? 314 ASP   A OD1 1 
ATOM   127  O  OD2 . ASP   A 1 18  ? -36.904 -15.739 34.616 1.00 75.02  ? 314 ASP   A OD2 1 
ATOM   128  N  N   . THR   A 1 19  ? -40.266 -19.030 34.893 1.00 83.14  ? 315 THR   A N   1 
ATOM   129  C  CA  . THR   A 1 19  ? -40.158 -20.402 34.420 1.00 82.29  ? 315 THR   A CA  1 
ATOM   130  C  C   . THR   A 1 19  ? -39.299 -20.532 33.176 1.00 80.61  ? 315 THR   A C   1 
ATOM   131  O  O   . THR   A 1 19  ? -38.897 -21.648 32.838 1.00 82.67  ? 315 THR   A O   1 
ATOM   132  C  CB  . THR   A 1 19  ? -41.544 -20.978 34.111 1.00 88.15  ? 315 THR   A CB  1 
ATOM   133  O  OG1 . THR   A 1 19  ? -42.364 -19.957 33.528 1.00 91.15  ? 315 THR   A OG1 1 
ATOM   134  C  CG2 . THR   A 1 19  ? -42.199 -21.501 35.366 1.00 95.07  ? 315 THR   A CG2 1 
ATOM   135  N  N   . LEU   A 1 20  ? -39.004 -19.421 32.499 1.00 79.38  ? 316 LEU   A N   1 
ATOM   136  C  CA  . LEU   A 1 20  ? -38.207 -19.472 31.280 1.00 78.95  ? 316 LEU   A CA  1 
ATOM   137  C  C   . LEU   A 1 20  ? -36.841 -20.096 31.529 1.00 76.22  ? 316 LEU   A C   1 
ATOM   138  O  O   . LEU   A 1 20  ? -36.269 -20.716 30.626 1.00 78.01  ? 316 LEU   A O   1 
ATOM   139  C  CB  . LEU   A 1 20  ? -38.054 -18.061 30.710 1.00 77.63  ? 316 LEU   A CB  1 
ATOM   140  C  CG  . LEU   A 1 20  ? -37.333 -17.916 29.369 1.00 73.38  ? 316 LEU   A CG  1 
ATOM   141  C  CD1 . LEU   A 1 20  ? -38.048 -18.732 28.329 1.00 69.75  ? 316 LEU   A CD1 1 
ATOM   142  C  CD2 . LEU   A 1 20  ? -37.261 -16.457 28.963 1.00 71.89  ? 316 LEU   A CD2 1 
ATOM   143  N  N   . HIS   A 1 21  ? -36.310 -19.957 32.748 1.00 76.79  ? 317 HIS   A N   1 
ATOM   144  C  CA  . HIS   A 1 21  ? -34.987 -20.490 33.050 1.00 74.75  ? 317 HIS   A CA  1 
ATOM   145  C  C   . HIS   A 1 21  ? -34.925 -21.995 32.865 1.00 75.53  ? 317 HIS   A C   1 
ATOM   146  O  O   . HIS   A 1 21  ? -33.827 -22.549 32.768 1.00 75.83  ? 317 HIS   A O   1 
ATOM   147  C  CB  . HIS   A 1 21  ? -34.583 -20.128 34.485 1.00 75.70  ? 317 HIS   A CB  1 
ATOM   148  C  CG  . HIS   A 1 21  ? -35.369 -20.854 35.529 1.00 76.87  ? 317 HIS   A CG  1 
ATOM   149  N  ND1 . HIS   A 1 21  ? -36.613 -20.435 35.947 1.00 79.79  ? 317 HIS   A ND1 1 
ATOM   150  C  CD2 . HIS   A 1 21  ? -35.095 -21.979 36.229 1.00 79.04  ? 317 HIS   A CD2 1 
ATOM   151  C  CE1 . HIS   A 1 21  ? -37.068 -21.267 36.868 1.00 84.01  ? 317 HIS   A CE1 1 
ATOM   152  N  NE2 . HIS   A 1 21  ? -36.167 -22.213 37.056 1.00 83.06  ? 317 HIS   A NE2 1 
ATOM   153  N  N   . LEU   A 1 22  ? -36.080 -22.665 32.830 1.00 76.91  ? 318 LEU   A N   1 
ATOM   154  C  CA  . LEU   A 1 22  ? -36.114 -24.094 32.544 1.00 77.90  ? 318 LEU   A CA  1 
ATOM   155  C  C   . LEU   A 1 22  ? -35.638 -24.398 31.129 1.00 82.44  ? 318 LEU   A C   1 
ATOM   156  O  O   . LEU   A 1 22  ? -35.061 -25.465 30.884 1.00 82.94  ? 318 LEU   A O   1 
ATOM   157  C  CB  . LEU   A 1 22  ? -37.531 -24.632 32.743 1.00 80.36  ? 318 LEU   A CB  1 
ATOM   158  C  CG  . LEU   A 1 22  ? -38.177 -24.398 34.118 1.00 80.22  ? 318 LEU   A CG  1 
ATOM   159  C  CD1 . LEU   A 1 22  ? -39.585 -24.993 34.138 1.00 85.74  ? 318 LEU   A CD1 1 
ATOM   160  C  CD2 . LEU   A 1 22  ? -37.325 -24.952 35.255 1.00 80.99  ? 318 LEU   A CD2 1 
ATOM   161  N  N   . LYS   A 1 23  ? -35.889 -23.492 30.185 1.00 79.46  ? 319 LYS   A N   1 
ATOM   162  C  CA  . LYS   A 1 23  ? -35.442 -23.697 28.812 1.00 83.61  ? 319 LYS   A CA  1 
ATOM   163  C  C   . LYS   A 1 23  ? -33.961 -23.398 28.646 1.00 84.42  ? 319 LYS   A C   1 
ATOM   164  O  O   . LYS   A 1 23  ? -33.393 -23.724 27.599 1.00 90.52  ? 319 LYS   A O   1 
ATOM   165  C  CB  . LYS   A 1 23  ? -36.261 -22.829 27.841 1.00 83.43  ? 319 LYS   A CB  1 
ATOM   166  C  CG  . LYS   A 1 23  ? -37.780 -23.022 27.919 1.00 86.31  ? 319 LYS   A CG  1 
ATOM   167  C  CD  . LYS   A 1 23  ? -38.201 -24.454 27.633 1.00 95.87  ? 319 LYS   A CD  1 
ATOM   168  C  CE  . LYS   A 1 23  ? -38.458 -24.698 26.154 1.00 106.69 ? 319 LYS   A CE  1 
ATOM   169  N  NZ  . LYS   A 1 23  ? -39.774 -24.154 25.695 1.00 108.03 ? 319 LYS   A NZ  1 
ATOM   170  N  N   . SER   A 1 24  ? -33.337 -22.786 29.651 1.00 84.64  ? 320 SER   A N   1 
ATOM   171  C  CA  . SER   A 1 24  ? -31.905 -22.518 29.625 1.00 86.08  ? 320 SER   A CA  1 
ATOM   172  C  C   . SER   A 1 24  ? -31.117 -23.803 29.423 1.00 93.62  ? 320 SER   A C   1 
ATOM   173  O  O   . SER   A 1 24  ? -31.436 -24.850 29.993 1.00 92.70  ? 320 SER   A O   1 
ATOM   174  C  CB  . SER   A 1 24  ? -31.472 -21.839 30.931 1.00 82.47  ? 320 SER   A CB  1 
ATOM   175  O  OG  . SER   A 1 24  ? -30.086 -22.015 31.169 1.00 84.99  ? 320 SER   A OG  1 
ATOM   176  N  N   . THR   A 1 25  ? -30.080 -23.717 28.599 1.00 106.93 ? 321 THR   A N   1 
ATOM   177  C  CA  . THR   A 1 25  ? -29.237 -24.867 28.307 1.00 111.84 ? 321 THR   A CA  1 
ATOM   178  C  C   . THR   A 1 25  ? -27.802 -24.665 28.767 1.00 111.21 ? 321 THR   A C   1 
ATOM   179  O  O   . THR   A 1 25  ? -27.258 -25.521 29.477 1.00 109.81 ? 321 THR   A O   1 
ATOM   180  C  CB  . THR   A 1 25  ? -29.286 -25.189 26.796 1.00 115.67 ? 321 THR   A CB  1 
ATOM   181  O  OG1 . THR   A 1 25  ? -28.237 -26.107 26.459 1.00 119.44 ? 321 THR   A OG1 1 
ATOM   182  C  CG2 . THR   A 1 25  ? -29.176 -23.919 25.942 1.00 112.56 ? 321 THR   A CG2 1 
ATOM   183  N  N   . LEU   A 1 26  ? -27.184 -23.541 28.409 1.00 100.57 ? 322 LEU   A N   1 
ATOM   184  C  CA  . LEU   A 1 26  ? -25.780 -23.312 28.714 1.00 98.87  ? 322 LEU   A CA  1 
ATOM   185  C  C   . LEU   A 1 26  ? -25.578 -23.121 30.217 1.00 97.89  ? 322 LEU   A C   1 
ATOM   186  O  O   . LEU   A 1 26  ? -26.521 -23.130 31.014 1.00 97.75  ? 322 LEU   A O   1 
ATOM   187  C  CB  . LEU   A 1 26  ? -25.261 -22.101 27.945 1.00 92.45  ? 322 LEU   A CB  1 
ATOM   188  C  CG  . LEU   A 1 26  ? -25.092 -22.220 26.427 1.00 91.06  ? 322 LEU   A CG  1 
ATOM   189  C  CD1 . LEU   A 1 26  ? -25.023 -20.828 25.829 1.00 85.90  ? 322 LEU   A CD1 1 
ATOM   190  C  CD2 . LEU   A 1 26  ? -23.839 -23.025 26.078 1.00 89.01  ? 322 LEU   A CD2 1 
ATOM   191  N  N   . GLU   A 1 27  ? -24.320 -22.936 30.602 1.00 96.84  ? 323 GLU   A N   1 
ATOM   192  C  CA  . GLU   A 1 27  ? -23.932 -22.811 31.996 1.00 97.27  ? 323 GLU   A CA  1 
ATOM   193  C  C   . GLU   A 1 27  ? -23.477 -21.384 32.290 1.00 93.65  ? 323 GLU   A C   1 
ATOM   194  O  O   . GLU   A 1 27  ? -23.104 -20.628 31.387 1.00 92.26  ? 323 GLU   A O   1 
ATOM   195  C  CB  . GLU   A 1 27  ? -22.844 -23.837 32.340 1.00 99.03  ? 323 GLU   A CB  1 
ATOM   196  C  CG  . GLU   A 1 27  ? -23.241 -25.254 31.909 1.00 105.20 ? 323 GLU   A CG  1 
ATOM   197  C  CD  . GLU   A 1 27  ? -22.327 -26.354 32.440 1.00 114.16 ? 323 GLU   A CD  1 
ATOM   198  O  OE1 . GLU   A 1 27  ? -21.789 -26.216 33.562 1.00 112.54 ? 323 GLU   A OE1 1 
ATOM   199  O  OE2 . GLU   A 1 27  ? -22.160 -27.371 31.727 1.00 117.25 ? 323 GLU   A OE2 1 
ATOM   200  N  N   . THR   A 1 28  ? -23.542 -21.012 33.572 1.00 88.25  ? 324 THR   A N   1 
ATOM   201  C  CA  . THR   A 1 28  ? -23.345 -19.630 33.998 1.00 85.10  ? 324 THR   A CA  1 
ATOM   202  C  C   . THR   A 1 28  ? -21.935 -19.323 34.485 1.00 82.53  ? 324 THR   A C   1 
ATOM   203  O  O   . THR   A 1 28  ? -21.527 -18.156 34.458 1.00 82.36  ? 324 THR   A O   1 
ATOM   204  C  CB  . THR   A 1 28  ? -24.323 -19.278 35.126 1.00 81.50  ? 324 THR   A CB  1 
ATOM   205  O  OG1 . THR   A 1 28  ? -24.078 -20.121 36.262 1.00 81.52  ? 324 THR   A OG1 1 
ATOM   206  C  CG2 . THR   A 1 28  ? -25.758 -19.453 34.666 1.00 81.63  ? 324 THR   A CG2 1 
ATOM   207  N  N   . GLY   A 1 29  ? -21.181 -20.330 34.918 1.00 78.10  ? 325 GLY   A N   1 
ATOM   208  C  CA  . GLY   A 1 29  ? -19.971 -20.128 35.671 1.00 75.73  ? 325 GLY   A CA  1 
ATOM   209  C  C   . GLY   A 1 29  ? -20.180 -20.267 37.163 1.00 76.37  ? 325 GLY   A C   1 
ATOM   210  O  O   . GLY   A 1 29  ? -19.251 -20.657 37.881 1.00 79.23  ? 325 GLY   A O   1 
ATOM   211  N  N   . CYS   A 1 30  ? -21.385 -19.982 37.642 1.00 75.85  ? 326 CYS   A N   1 
ATOM   212  C  CA  . CYS   A 1 30  ? -21.685 -20.147 39.055 1.00 76.02  ? 326 CYS   A CA  1 
ATOM   213  C  C   . CYS   A 1 30  ? -21.904 -21.616 39.385 1.00 79.60  ? 326 CYS   A C   1 
ATOM   214  O  O   . CYS   A 1 30  ? -22.347 -22.404 38.550 1.00 82.54  ? 326 CYS   A O   1 
ATOM   215  C  CB  . CYS   A 1 30  ? -22.930 -19.356 39.446 1.00 72.17  ? 326 CYS   A CB  1 
ATOM   216  S  SG  . CYS   A 1 30  ? -22.846 -17.595 39.124 1.00 68.81  ? 326 CYS   A SG  1 
ATOM   217  N  N   . THR   A 1 31  ? -21.603 -21.979 40.618 1.00 78.70  ? 327 THR   A N   1 
ATOM   218  C  CA  . THR   A 1 31  ? -21.945 -23.292 41.134 1.00 83.51  ? 327 THR   A CA  1 
ATOM   219  C  C   . THR   A 1 31  ? -22.820 -23.114 42.367 1.00 86.06  ? 327 THR   A C   1 
ATOM   220  O  O   . THR   A 1 31  ? -23.202 -21.998 42.731 1.00 84.80  ? 327 THR   A O   1 
ATOM   221  C  CB  . THR   A 1 31  ? -20.690 -24.111 41.451 1.00 83.93  ? 327 THR   A CB  1 
ATOM   222  O  OG1 . THR   A 1 31  ? -20.016 -23.549 42.582 1.00 84.39  ? 327 THR   A OG1 1 
ATOM   223  C  CG2 . THR   A 1 31  ? -19.743 -24.118 40.265 1.00 81.26  ? 327 THR   A CG2 1 
ATOM   224  N  N   . GLU   A 1 32  ? -23.143 -24.231 43.014 1.00 89.07  ? 328 GLU   A N   1 
ATOM   225  C  CA  . GLU   A 1 32  ? -23.888 -24.152 44.261 1.00 92.64  ? 328 GLU   A CA  1 
ATOM   226  C  C   . GLU   A 1 32  ? -23.078 -23.485 45.368 1.00 92.05  ? 328 GLU   A C   1 
ATOM   227  O  O   . GLU   A 1 32  ? -23.658 -23.042 46.367 1.00 93.09  ? 328 GLU   A O   1 
ATOM   228  C  CB  . GLU   A 1 32  ? -24.334 -25.554 44.693 1.00 101.30 ? 328 GLU   A CB  1 
ATOM   229  C  CG  . GLU   A 1 32  ? -25.567 -26.092 43.960 1.00 101.96 ? 328 GLU   A CG  1 
ATOM   230  C  CD  . GLU   A 1 32  ? -25.225 -27.064 42.841 1.00 106.01 ? 328 GLU   A CD  1 
ATOM   231  O  OE1 . GLU   A 1 32  ? -24.839 -26.603 41.754 1.00 102.12 ? 328 GLU   A OE1 1 
ATOM   232  O  OE2 . GLU   A 1 32  ? -25.336 -28.295 43.050 1.00 118.61 ? 328 GLU   A OE2 1 
ATOM   233  N  N   . HIS   A 1 33  ? -21.756 -23.390 45.215 1.00 93.06  ? 329 HIS   A N   1 
ATOM   234  C  CA  . HIS   A 1 33  ? -20.893 -22.902 46.282 1.00 91.51  ? 329 HIS   A CA  1 
ATOM   235  C  C   . HIS   A 1 33  ? -20.072 -21.681 45.885 1.00 87.29  ? 329 HIS   A C   1 
ATOM   236  O  O   . HIS   A 1 33  ? -19.216 -21.246 46.665 1.00 84.35  ? 329 HIS   A O   1 
ATOM   237  C  CB  . HIS   A 1 33  ? -19.952 -24.018 46.747 1.00 99.91  ? 329 HIS   A CB  1 
ATOM   238  C  CG  . HIS   A 1 33  ? -20.624 -25.348 46.905 1.00 106.89 ? 329 HIS   A CG  1 
ATOM   239  N  ND1 . HIS   A 1 33  ? -21.091 -25.810 48.118 1.00 109.70 ? 329 HIS   A ND1 1 
ATOM   240  C  CD2 . HIS   A 1 33  ? -20.907 -26.317 46.000 1.00 109.99 ? 329 HIS   A CD2 1 
ATOM   241  C  CE1 . HIS   A 1 33  ? -21.632 -27.005 47.953 1.00 112.42 ? 329 HIS   A CE1 1 
ATOM   242  N  NE2 . HIS   A 1 33  ? -21.533 -27.336 46.678 1.00 113.36 ? 329 HIS   A NE2 1 
ATOM   243  N  N   . ILE   A 1 34  ? -20.305 -21.112 44.708 1.00 81.31  ? 330 ILE   A N   1 
ATOM   244  C  CA  . ILE   A 1 34  ? -19.597 -19.912 44.284 1.00 74.44  ? 330 ILE   A CA  1 
ATOM   245  C  C   . ILE   A 1 34  ? -20.462 -19.177 43.272 1.00 74.83  ? 330 ILE   A C   1 
ATOM   246  O  O   . ILE   A 1 34  ? -21.112 -19.790 42.420 1.00 73.36  ? 330 ILE   A O   1 
ATOM   247  C  CB  . ILE   A 1 34  ? -18.204 -20.243 43.708 1.00 76.38  ? 330 ILE   A CB  1 
ATOM   248  C  CG1 . ILE   A 1 34  ? -17.374 -18.966 43.573 1.00 73.81  ? 330 ILE   A CG1 1 
ATOM   249  C  CG2 . ILE   A 1 34  ? -18.323 -20.904 42.325 1.00 80.07  ? 330 ILE   A CG2 1 
ATOM   250  C  CD1 . ILE   A 1 34  ? -15.959 -19.128 44.073 1.00 73.57  ? 330 ILE   A CD1 1 
ATOM   251  N  N   . CYS   A 1 35  ? -20.481 -17.858 43.381 1.00 68.17  ? 331 CYS   A N   1 
ATOM   252  C  CA  . CYS   A 1 35  ? -21.209 -17.015 42.455 1.00 66.51  ? 331 CYS   A CA  1 
ATOM   253  C  C   . CYS   A 1 35  ? -20.204 -16.184 41.680 1.00 66.65  ? 331 CYS   A C   1 
ATOM   254  O  O   . CYS   A 1 35  ? -19.367 -15.495 42.278 1.00 65.09  ? 331 CYS   A O   1 
ATOM   255  C  CB  . CYS   A 1 35  ? -22.208 -16.112 43.169 1.00 64.12  ? 331 CYS   A CB  1 
ATOM   256  S  SG  . CYS   A 1 35  ? -23.031 -15.015 42.021 1.00 62.01  ? 331 CYS   A SG  1 
ATOM   257  N  N   . MET   A 1 36  ? -20.272 -16.295 40.352 1.00 65.09  ? 332 MET   A N   1 
ATOM   258  C  CA  . MET   A 1 36  ? -19.389 -15.609 39.418 1.00 65.60  ? 332 MET   A CA  1 
ATOM   259  C  C   . MET   A 1 36  ? -20.073 -14.423 38.760 1.00 63.29  ? 332 MET   A C   1 
ATOM   260  O  O   . MET   A 1 36  ? -19.603 -13.933 37.726 1.00 62.96  ? 332 MET   A O   1 
ATOM   261  C  CB  . MET   A 1 36  ? -18.901 -16.588 38.351 1.00 68.53  ? 332 MET   A CB  1 
ATOM   262  C  CG  . MET   A 1 36  ? -18.366 -17.878 38.923 1.00 74.80  ? 332 MET   A CG  1 
ATOM   263  S  SD  . MET   A 1 36  ? -16.584 -18.029 38.747 1.00 88.75  ? 332 MET   A SD  1 
ATOM   264  C  CE  . MET   A 1 36  ? -16.265 -19.404 39.844 1.00 83.64  ? 332 MET   A CE  1 
ATOM   265  N  N   . GLY   A 1 37  ? -21.184 -13.962 39.334 1.00 62.04  ? 333 GLY   A N   1 
ATOM   266  C  CA  . GLY   A 1 37  ? -21.997 -12.926 38.726 1.00 62.06  ? 333 GLY   A CA  1 
ATOM   267  C  C   . GLY   A 1 37  ? -21.284 -11.615 38.478 1.00 60.78  ? 333 GLY   A C   1 
ATOM   268  O  O   . GLY   A 1 37  ? -21.832 -10.769 37.764 1.00 61.00  ? 333 GLY   A O   1 
ATOM   269  N  N   . SER   A 1 38  ? -20.095 -11.403 39.043 1.00 60.40  ? 334 SER   A N   1 
ATOM   270  C  CA  . SER   A 1 38  ? -19.339 -10.202 38.711 1.00 58.24  ? 334 SER   A CA  1 
ATOM   271  C  C   . SER   A 1 38  ? -18.104 -10.488 37.867 1.00 60.02  ? 334 SER   A C   1 
ATOM   272  O  O   . SER   A 1 38  ? -17.311 -9.573  37.634 1.00 62.11  ? 334 SER   A O   1 
ATOM   273  C  CB  . SER   A 1 38  ? -18.939 -9.447  39.972 1.00 58.24  ? 334 SER   A CB  1 
ATOM   274  O  OG  . SER   A 1 38  ? -17.942 -10.149 40.694 1.00 58.68  ? 334 SER   A OG  1 
ATOM   275  N  N   . ILE   A 1 39  ? -17.911 -11.727 37.420 1.00 62.86  ? 335 ILE   A N   1 
ATOM   276  C  CA  . ILE   A 1 39  ? -16.799 -12.052 36.533 1.00 65.34  ? 335 ILE   A CA  1 
ATOM   277  C  C   . ILE   A 1 39  ? -17.154 -11.579 35.129 1.00 70.46  ? 335 ILE   A C   1 
ATOM   278  O  O   . ILE   A 1 39  ? -18.242 -11.875 34.619 1.00 70.30  ? 335 ILE   A O   1 
ATOM   279  C  CB  . ILE   A 1 39  ? -16.496 -13.558 36.561 1.00 66.38  ? 335 ILE   A CB  1 
ATOM   280  C  CG1 . ILE   A 1 39  ? -16.214 -14.031 38.002 1.00 66.84  ? 335 ILE   A CG1 1 
ATOM   281  C  CG2 . ILE   A 1 39  ? -15.330 -13.883 35.646 1.00 70.51  ? 335 ILE   A CG2 1 
ATOM   282  C  CD1 . ILE   A 1 39  ? -15.025 -13.366 38.641 1.00 65.89  ? 335 ILE   A CD1 1 
ATOM   283  N  N   . MET   A 1 40  ? -16.242 -10.823 34.513 1.00 66.29  ? 336 MET   A N   1 
ATOM   284  C  CA  . MET   A 1 40  ? -16.556 -10.122 33.266 1.00 70.98  ? 336 MET   A CA  1 
ATOM   285  C  C   . MET   A 1 40  ? -16.770 -11.095 32.107 1.00 77.12  ? 336 MET   A C   1 
ATOM   286  O  O   . MET   A 1 40  ? -17.762 -10.999 31.371 1.00 75.90  ? 336 MET   A O   1 
ATOM   287  C  CB  . MET   A 1 40  ? -15.437 -9.135  32.932 1.00 70.83  ? 336 MET   A CB  1 
ATOM   288  C  CG  . MET   A 1 40  ? -15.552 -8.538  31.543 1.00 76.37  ? 336 MET   A CG  1 
ATOM   289  S  SD  . MET   A 1 40  ? -16.357 -6.927  31.579 1.00 78.48  ? 336 MET   A SD  1 
ATOM   290  C  CE  . MET   A 1 40  ? -15.162 -6.003  32.544 1.00 64.33  ? 336 MET   A CE  1 
ATOM   291  N  N   . LEU   A 1 41  ? -15.840 -12.028 31.919 1.00 81.65  ? 337 LEU   A N   1 
ATOM   292  C  CA  . LEU   A 1 41  ? -15.945 -13.040 30.873 1.00 92.34  ? 337 LEU   A CA  1 
ATOM   293  C  C   . LEU   A 1 41  ? -16.159 -14.400 31.525 1.00 103.53 ? 337 LEU   A C   1 
ATOM   294  O  O   . LEU   A 1 41  ? -15.205 -14.992 32.058 1.00 103.33 ? 337 LEU   A O   1 
ATOM   295  C  CB  . LEU   A 1 41  ? -14.684 -13.052 30.004 1.00 90.42  ? 337 LEU   A CB  1 
ATOM   296  C  CG  . LEU   A 1 41  ? -13.974 -11.708 29.811 1.00 86.55  ? 337 LEU   A CG  1 
ATOM   297  C  CD1 . LEU   A 1 41  ? -12.470 -11.891 29.946 1.00 84.82  ? 337 LEU   A CD1 1 
ATOM   298  C  CD2 . LEU   A 1 41  ? -14.320 -11.068 28.474 1.00 77.57  ? 337 LEU   A CD2 1 
ATOM   299  N  N   . PRO   A 1 42  ? -17.381 -14.933 31.528 1.00 125.89 ? 338 PRO   A N   1 
ATOM   300  C  CA  . PRO   A 1 42  ? -17.610 -16.240 32.158 1.00 127.82 ? 338 PRO   A CA  1 
ATOM   301  C  C   . PRO   A 1 42  ? -17.352 -17.398 31.204 1.00 130.09 ? 338 PRO   A C   1 
ATOM   302  O  O   . PRO   A 1 42  ? -18.057 -17.559 30.202 1.00 126.52 ? 338 PRO   A O   1 
ATOM   303  C  CB  . PRO   A 1 42  ? -19.087 -16.175 32.586 1.00 129.71 ? 338 PRO   A CB  1 
ATOM   304  C  CG  . PRO   A 1 42  ? -19.618 -14.822 32.084 1.00 126.86 ? 338 PRO   A CG  1 
ATOM   305  C  CD  . PRO   A 1 42  ? -18.638 -14.323 31.068 1.00 125.47 ? 338 PRO   A CD  1 
ATOM   306  N  N   . SER   A 1 43  ? -16.337 -18.204 31.506 1.00 121.29 ? 339 SER   A N   1 
ATOM   307  C  CA  . SER   A 1 43  ? -15.996 -19.359 30.682 1.00 119.75 ? 339 SER   A CA  1 
ATOM   308  C  C   . SER   A 1 43  ? -15.307 -20.435 31.512 1.00 117.63 ? 339 SER   A C   1 
ATOM   309  O  O   . SER   A 1 43  ? -15.596 -21.621 31.363 1.00 117.28 ? 339 SER   A O   1 
ATOM   310  C  CB  . SER   A 1 43  ? -15.099 -18.945 29.511 1.00 119.26 ? 339 SER   A CB  1 
ATOM   311  O  OG  . SER   A 1 43  ? -14.725 -20.066 28.724 1.00 118.29 ? 339 SER   A OG  1 
ATOM   312  N  N   . VAL   A 1 52  ? -13.662 -26.579 16.602 1.00 136.13 ? 348 VAL   A N   1 
ATOM   313  C  CA  . VAL   A 1 52  ? -14.600 -26.810 15.508 1.00 134.24 ? 348 VAL   A CA  1 
ATOM   314  C  C   . VAL   A 1 52  ? -15.712 -27.750 15.979 1.00 134.62 ? 348 VAL   A C   1 
ATOM   315  O  O   . VAL   A 1 52  ? -15.450 -28.728 16.681 1.00 136.09 ? 348 VAL   A O   1 
ATOM   316  C  CB  . VAL   A 1 52  ? -13.871 -27.360 14.247 1.00 130.92 ? 348 VAL   A CB  1 
ATOM   317  C  CG1 . VAL   A 1 52  ? -13.115 -28.655 14.553 1.00 130.89 ? 348 VAL   A CG1 1 
ATOM   318  C  CG2 . VAL   A 1 52  ? -14.851 -27.564 13.105 1.00 124.59 ? 348 VAL   A CG2 1 
ATOM   319  N  N   . ALA   A 1 53  ? -16.954 -27.444 15.603 1.00 132.15 ? 349 ALA   A N   1 
ATOM   320  C  CA  . ALA   A 1 53  ? -18.115 -28.201 16.059 1.00 129.31 ? 349 ALA   A CA  1 
ATOM   321  C  C   . ALA   A 1 53  ? -18.439 -29.339 15.095 1.00 128.92 ? 349 ALA   A C   1 
ATOM   322  O  O   . ALA   A 1 53  ? -18.319 -29.188 13.876 1.00 129.32 ? 349 ALA   A O   1 
ATOM   323  C  CB  . ALA   A 1 53  ? -19.328 -27.283 16.211 1.00 125.96 ? 349 ALA   A CB  1 
ATOM   324  N  N   . THR   A 1 54  ? -18.866 -30.473 15.653 1.00 127.78 ? 350 THR   A N   1 
ATOM   325  C  CA  . THR   A 1 54  ? -19.121 -31.692 14.896 1.00 126.56 ? 350 THR   A CA  1 
ATOM   326  C  C   . THR   A 1 54  ? -20.607 -31.839 14.572 1.00 125.19 ? 350 THR   A C   1 
ATOM   327  O  O   . THR   A 1 54  ? -21.454 -31.062 15.019 1.00 121.22 ? 350 THR   A O   1 
ATOM   328  C  CB  . THR   A 1 54  ? -18.630 -32.918 15.675 1.00 126.76 ? 350 THR   A CB  1 
ATOM   329  O  OG1 . THR   A 1 54  ? -19.630 -33.316 16.621 1.00 128.03 ? 350 THR   A OG1 1 
ATOM   330  C  CG2 . THR   A 1 54  ? -17.349 -32.585 16.430 1.00 125.38 ? 350 THR   A CG2 1 
ATOM   331  N  N   . LYS   A 1 55  ? -20.919 -32.867 13.780 1.00 126.56 ? 351 LYS   A N   1 
ATOM   332  C  CA  . LYS   A 1 55  ? -22.297 -33.073 13.347 1.00 125.05 ? 351 LYS   A CA  1 
ATOM   333  C  C   . LYS   A 1 55  ? -23.138 -33.777 14.402 1.00 125.58 ? 351 LYS   A C   1 
ATOM   334  O  O   . LYS   A 1 55  ? -24.362 -33.600 14.424 1.00 122.41 ? 351 LYS   A O   1 
ATOM   335  C  CB  . LYS   A 1 55  ? -22.334 -33.858 12.034 1.00 126.99 ? 351 LYS   A CB  1 
ATOM   336  C  CG  . LYS   A 1 55  ? -21.174 -34.811 11.830 1.00 131.73 ? 351 LYS   A CG  1 
ATOM   337  C  CD  . LYS   A 1 55  ? -21.289 -35.517 10.482 1.00 138.22 ? 351 LYS   A CD  1 
ATOM   338  C  CE  . LYS   A 1 55  ? -20.081 -36.405 10.219 1.00 143.95 ? 351 LYS   A CE  1 
ATOM   339  N  NZ  . LYS   A 1 55  ? -20.353 -37.433 9.184  1.00 145.14 ? 351 LYS   A NZ  1 
ATOM   340  N  N   . ASP   A 1 56  ? -22.510 -34.581 15.266 1.00 129.58 ? 352 ASP   A N   1 
ATOM   341  C  CA  . ASP   A 1 56  ? -23.225 -35.151 16.404 1.00 129.23 ? 352 ASP   A CA  1 
ATOM   342  C  C   . ASP   A 1 56  ? -23.869 -34.052 17.234 1.00 123.52 ? 352 ASP   A C   1 
ATOM   343  O  O   . ASP   A 1 56  ? -25.073 -34.087 17.511 1.00 121.95 ? 352 ASP   A O   1 
ATOM   344  C  CB  . ASP   A 1 56  ? -22.272 -35.978 17.268 1.00 134.81 ? 352 ASP   A CB  1 
ATOM   345  C  CG  . ASP   A 1 56  ? -21.339 -36.844 16.444 1.00 139.07 ? 352 ASP   A CG  1 
ATOM   346  O  OD1 . ASP   A 1 56  ? -21.790 -37.401 15.421 1.00 138.72 ? 352 ASP   A OD1 1 
ATOM   347  O  OD2 . ASP   A 1 56  ? -20.152 -36.960 16.818 1.00 142.06 ? 352 ASP   A OD2 1 
ATOM   348  N  N   . GLN   A 1 57  ? -23.078 -33.052 17.624 1.00 122.05 ? 353 GLN   A N   1 
ATOM   349  C  CA  . GLN   A 1 57  ? -23.584 -31.959 18.441 1.00 117.39 ? 353 GLN   A CA  1 
ATOM   350  C  C   . GLN   A 1 57  ? -24.544 -31.057 17.682 1.00 108.45 ? 353 GLN   A C   1 
ATOM   351  O  O   . GLN   A 1 57  ? -25.322 -30.333 18.312 1.00 102.98 ? 353 GLN   A O   1 
ATOM   352  C  CB  . GLN   A 1 57  ? -22.421 -31.118 18.961 1.00 120.16 ? 353 GLN   A CB  1 
ATOM   353  C  CG  . GLN   A 1 57  ? -21.109 -31.872 19.053 1.00 124.14 ? 353 GLN   A CG  1 
ATOM   354  C  CD  . GLN   A 1 57  ? -19.910 -30.980 18.803 1.00 126.13 ? 353 GLN   A CD  1 
ATOM   355  O  OE1 . GLN   A 1 57  ? -19.982 -30.028 18.023 1.00 126.86 ? 353 GLN   A OE1 1 
ATOM   356  N  NE2 . GLN   A 1 57  ? -18.799 -31.281 19.466 1.00 128.06 ? 353 GLN   A NE2 1 
ATOM   357  N  N   . LEU   A 1 58  ? -24.516 -31.090 16.351 1.00 111.28 ? 354 LEU   A N   1 
ATOM   358  C  CA  . LEU   A 1 58  ? -25.165 -30.040 15.577 1.00 103.99 ? 354 LEU   A CA  1 
ATOM   359  C  C   . LEU   A 1 58  ? -26.670 -30.245 15.455 1.00 100.85 ? 354 LEU   A C   1 
ATOM   360  O  O   . LEU   A 1 58  ? -27.427 -29.272 15.529 1.00 95.38  ? 354 LEU   A O   1 
ATOM   361  C  CB  . LEU   A 1 58  ? -24.532 -29.947 14.196 1.00 103.35 ? 354 LEU   A CB  1 
ATOM   362  C  CG  . LEU   A 1 58  ? -24.471 -28.555 13.584 1.00 93.20  ? 354 LEU   A CG  1 
ATOM   363  C  CD1 . LEU   A 1 58  ? -23.597 -27.627 14.415 1.00 88.91  ? 354 LEU   A CD1 1 
ATOM   364  C  CD2 . LEU   A 1 58  ? -23.963 -28.639 12.151 1.00 92.65  ? 354 LEU   A CD2 1 
ATOM   365  N  N   . PHE   A 1 59  ? -27.137 -31.486 15.291 1.00 99.10  ? 355 PHE   A N   1 
ATOM   366  C  CA  . PHE   A 1 59  ? -28.574 -31.655 15.088 1.00 100.25 ? 355 PHE   A CA  1 
ATOM   367  C  C   . PHE   A 1 59  ? -29.408 -31.380 16.337 1.00 99.38  ? 355 PHE   A C   1 
ATOM   368  O  O   . PHE   A 1 59  ? -30.508 -30.827 16.203 1.00 97.40  ? 355 PHE   A O   1 
ATOM   369  C  CB  . PHE   A 1 59  ? -28.919 -33.045 14.569 1.00 107.75 ? 355 PHE   A CB  1 
ATOM   370  C  CG  . PHE   A 1 59  ? -30.337 -33.153 14.082 1.00 112.53 ? 355 PHE   A CG  1 
ATOM   371  C  CD1 . PHE   A 1 59  ? -30.844 -32.208 13.193 1.00 111.76 ? 355 PHE   A CD1 1 
ATOM   372  C  CD2 . PHE   A 1 59  ? -31.168 -34.175 14.513 1.00 116.83 ? 355 PHE   A CD2 1 
ATOM   373  C  CE1 . PHE   A 1 59  ? -32.151 -32.287 12.738 1.00 111.05 ? 355 PHE   A CE1 1 
ATOM   374  C  CE2 . PHE   A 1 59  ? -32.476 -34.261 14.061 1.00 120.06 ? 355 PHE   A CE2 1 
ATOM   375  C  CZ  . PHE   A 1 59  ? -32.967 -33.315 13.173 1.00 116.83 ? 355 PHE   A CZ  1 
ATOM   376  N  N   . PRO   A 1 60  ? -28.969 -31.761 17.550 1.00 101.60 ? 356 PRO   A N   1 
ATOM   377  C  CA  . PRO   A 1 60  ? -29.696 -31.297 18.748 1.00 95.28  ? 356 PRO   A CA  1 
ATOM   378  C  C   . PRO   A 1 60  ? -29.914 -29.793 18.770 1.00 91.72  ? 356 PRO   A C   1 
ATOM   379  O  O   . PRO   A 1 60  ? -31.036 -29.329 19.005 1.00 90.03  ? 356 PRO   A O   1 
ATOM   380  C  CB  . PRO   A 1 60  ? -28.795 -31.770 19.895 1.00 96.23  ? 356 PRO   A CB  1 
ATOM   381  C  CG  . PRO   A 1 60  ? -28.168 -33.002 19.380 1.00 100.92 ? 356 PRO   A CG  1 
ATOM   382  C  CD  . PRO   A 1 60  ? -27.966 -32.788 17.897 1.00 103.08 ? 356 PRO   A CD  1 
ATOM   383  N  N   . LEU   A 1 61  ? -28.858 -29.019 18.512 1.00 90.23  ? 357 LEU   A N   1 
ATOM   384  C  CA  . LEU   A 1 61  ? -28.966 -27.564 18.493 1.00 85.82  ? 357 LEU   A CA  1 
ATOM   385  C  C   . LEU   A 1 61  ? -29.870 -27.077 17.362 1.00 87.00  ? 357 LEU   A C   1 
ATOM   386  O  O   . LEU   A 1 61  ? -30.673 -26.155 17.558 1.00 85.82  ? 357 LEU   A O   1 
ATOM   387  C  CB  . LEU   A 1 61  ? -27.574 -26.955 18.364 1.00 84.96  ? 357 LEU   A CB  1 
ATOM   388  C  CG  . LEU   A 1 61  ? -26.562 -27.304 19.455 1.00 88.34  ? 357 LEU   A CG  1 
ATOM   389  C  CD1 . LEU   A 1 61  ? -25.146 -27.142 18.937 1.00 90.26  ? 357 LEU   A CD1 1 
ATOM   390  C  CD2 . LEU   A 1 61  ? -26.785 -26.427 20.679 1.00 87.51  ? 357 LEU   A CD2 1 
ATOM   391  N  N   . ALA   A 1 62  ? -29.740 -27.663 16.167 1.00 88.28  ? 358 ALA   A N   1 
ATOM   392  C  CA  . ALA   A 1 62  ? -30.634 -27.302 15.072 1.00 87.34  ? 358 ALA   A CA  1 
ATOM   393  C  C   . ALA   A 1 62  ? -32.079 -27.613 15.431 1.00 88.79  ? 358 ALA   A C   1 
ATOM   394  O  O   . ALA   A 1 62  ? -32.962 -26.755 15.306 1.00 86.81  ? 358 ALA   A O   1 
ATOM   395  C  CB  . ALA   A 1 62  ? -30.234 -28.037 13.787 1.00 87.51  ? 358 ALA   A CB  1 
ATOM   396  N  N   . LYS   A 1 63  ? -32.333 -28.845 15.884 1.00 88.98  ? 359 LYS   A N   1 
ATOM   397  C  CA  . LYS   A 1 63  ? -33.684 -29.266 16.247 1.00 90.23  ? 359 LYS   A CA  1 
ATOM   398  C  C   . LYS   A 1 63  ? -34.273 -28.371 17.328 1.00 89.95  ? 359 LYS   A C   1 
ATOM   399  O  O   . LYS   A 1 63  ? -35.402 -27.884 17.198 1.00 91.64  ? 359 LYS   A O   1 
ATOM   400  C  CB  . LYS   A 1 63  ? -33.671 -30.721 16.717 1.00 96.50  ? 359 LYS   A CB  1 
ATOM   401  C  CG  . LYS   A 1 63  ? -35.016 -31.211 17.204 1.00 95.87  ? 359 LYS   A CG  1 
ATOM   402  C  CD  . LYS   A 1 63  ? -34.984 -32.690 17.531 1.00 99.20  ? 359 LYS   A CD  1 
ATOM   403  C  CE  . LYS   A 1 63  ? -36.396 -33.237 17.596 1.00 98.39  ? 359 LYS   A CE  1 
ATOM   404  N  NZ  . LYS   A 1 63  ? -37.222 -32.406 18.525 1.00 103.92 ? 359 LYS   A NZ  1 
ATOM   405  N  N   . GLU   A 1 64  ? -33.521 -28.149 18.408 1.00 86.29  ? 360 GLU   A N   1 
ATOM   406  C  CA  . GLU   A 1 64  ? -33.997 -27.269 19.470 1.00 88.55  ? 360 GLU   A CA  1 
ATOM   407  C  C   . GLU   A 1 64  ? -34.394 -25.905 18.911 1.00 87.06  ? 360 GLU   A C   1 
ATOM   408  O  O   . GLU   A 1 64  ? -35.473 -25.386 19.220 1.00 85.83  ? 360 GLU   A O   1 
ATOM   409  C  CB  . GLU   A 1 64  ? -32.922 -27.128 20.551 1.00 89.05  ? 360 GLU   A CB  1 
ATOM   410  C  CG  . GLU   A 1 64  ? -33.235 -26.095 21.630 1.00 92.18  ? 360 GLU   A CG  1 
ATOM   411  C  CD  . GLU   A 1 64  ? -32.000 -25.693 22.439 1.00 96.10  ? 360 GLU   A CD  1 
ATOM   412  O  OE1 . GLU   A 1 64  ? -31.043 -26.498 22.498 1.00 96.20  ? 360 GLU   A OE1 1 
ATOM   413  O  OE2 . GLU   A 1 64  ? -31.984 -24.572 23.011 1.00 95.28  ? 360 GLU   A OE2 1 
ATOM   414  N  N   . PHE   A 1 65  ? -33.548 -25.324 18.054 1.00 86.91  ? 361 PHE   A N   1 
ATOM   415  C  CA  . PHE   A 1 65  ? -33.841 -23.998 17.517 1.00 83.78  ? 361 PHE   A CA  1 
ATOM   416  C  C   . PHE   A 1 65  ? -35.035 -24.031 16.573 1.00 83.85  ? 361 PHE   A C   1 
ATOM   417  O  O   . PHE   A 1 65  ? -35.900 -23.149 16.621 1.00 83.94  ? 361 PHE   A O   1 
ATOM   418  C  CB  . PHE   A 1 65  ? -32.619 -23.428 16.802 1.00 79.16  ? 361 PHE   A CB  1 
ATOM   419  C  CG  . PHE   A 1 65  ? -32.918 -22.207 15.980 1.00 74.92  ? 361 PHE   A CG  1 
ATOM   420  C  CD1 . PHE   A 1 65  ? -33.004 -20.961 16.575 1.00 73.25  ? 361 PHE   A CD1 1 
ATOM   421  C  CD2 . PHE   A 1 65  ? -33.115 -22.307 14.611 1.00 74.36  ? 361 PHE   A CD2 1 
ATOM   422  C  CE1 . PHE   A 1 65  ? -33.281 -19.833 15.821 1.00 71.06  ? 361 PHE   A CE1 1 
ATOM   423  C  CE2 . PHE   A 1 65  ? -33.395 -21.180 13.856 1.00 73.82  ? 361 PHE   A CE2 1 
ATOM   424  C  CZ  . PHE   A 1 65  ? -33.478 -19.940 14.470 1.00 70.61  ? 361 PHE   A CZ  1 
ATOM   425  N  N   . LEU   A 1 66  ? -35.088 -25.029 15.686 1.00 86.20  ? 362 LEU   A N   1 
ATOM   426  C  CA  . LEU   A 1 66  ? -36.193 -25.096 14.736 1.00 85.09  ? 362 LEU   A CA  1 
ATOM   427  C  C   . LEU   A 1 66  ? -37.518 -25.339 15.445 1.00 91.17  ? 362 LEU   A C   1 
ATOM   428  O  O   . LEU   A 1 66  ? -38.564 -24.866 14.985 1.00 92.25  ? 362 LEU   A O   1 
ATOM   429  C  CB  . LEU   A 1 66  ? -35.934 -26.188 13.698 1.00 86.65  ? 362 LEU   A CB  1 
ATOM   430  C  CG  . LEU   A 1 66  ? -34.946 -25.847 12.574 1.00 83.78  ? 362 LEU   A CG  1 
ATOM   431  C  CD1 . LEU   A 1 66  ? -34.822 -27.008 11.610 1.00 86.19  ? 362 LEU   A CD1 1 
ATOM   432  C  CD2 . LEU   A 1 66  ? -35.362 -24.585 11.842 1.00 82.46  ? 362 LEU   A CD2 1 
ATOM   433  N  N   . ASP   A 1 67  ? -37.490 -26.071 16.563 1.00 88.90  ? 363 ASP   A N   1 
ATOM   434  C  CA  . ASP   A 1 67  ? -38.701 -26.281 17.352 1.00 92.23  ? 363 ASP   A CA  1 
ATOM   435  C  C   . ASP   A 1 67  ? -39.262 -24.960 17.867 1.00 91.91  ? 363 ASP   A C   1 
ATOM   436  O  O   . ASP   A 1 67  ? -40.471 -24.714 17.785 1.00 96.81  ? 363 ASP   A O   1 
ATOM   437  C  CB  . ASP   A 1 67  ? -38.410 -27.228 18.523 1.00 94.89  ? 363 ASP   A CB  1 
ATOM   438  C  CG  . ASP   A 1 67  ? -38.521 -28.695 18.137 1.00 100.39 ? 363 ASP   A CG  1 
ATOM   439  O  OD1 . ASP   A 1 67  ? -39.627 -29.132 17.742 1.00 107.36 ? 363 ASP   A OD1 1 
ATOM   440  O  OD2 . ASP   A 1 67  ? -37.502 -29.417 18.228 1.00 98.57  ? 363 ASP   A OD2 1 
ATOM   441  N  N   . GLN   A 1 68  ? -38.401 -24.095 18.405 1.00 91.70  ? 364 GLN   A N   1 
ATOM   442  C  CA  . GLN   A 1 68  ? -38.903 -22.853 18.978 1.00 90.43  ? 364 GLN   A CA  1 
ATOM   443  C  C   . GLN   A 1 68  ? -39.253 -21.849 17.892 1.00 90.32  ? 364 GLN   A C   1 
ATOM   444  O  O   . GLN   A 1 68  ? -40.202 -21.072 18.051 1.00 91.80  ? 364 GLN   A O   1 
ATOM   445  C  CB  . GLN   A 1 68  ? -37.890 -22.271 19.979 1.00 85.62  ? 364 GLN   A CB  1 
ATOM   446  C  CG  . GLN   A 1 68  ? -36.461 -22.184 19.462 1.00 84.61  ? 364 GLN   A CG  1 
ATOM   447  C  CD  . GLN   A 1 68  ? -35.435 -21.846 20.537 1.00 81.20  ? 364 GLN   A CD  1 
ATOM   448  O  OE1 . GLN   A 1 68  ? -34.924 -20.723 20.595 1.00 78.29  ? 364 GLN   A OE1 1 
ATOM   449  N  NE2 . GLN   A 1 68  ? -35.103 -22.827 21.371 1.00 85.37  ? 364 GLN   A NE2 1 
ATOM   450  N  N   . TYR   A 1 69  ? -38.531 -21.878 16.770 1.00 89.27  ? 365 TYR   A N   1 
ATOM   451  C  CA  . TYR   A 1 69  ? -38.905 -21.032 15.644 1.00 87.40  ? 365 TYR   A CA  1 
ATOM   452  C  C   . TYR   A 1 69  ? -40.303 -21.368 15.150 1.00 92.12  ? 365 TYR   A C   1 
ATOM   453  O  O   . TYR   A 1 69  ? -41.140 -20.479 14.963 1.00 94.01  ? 365 TYR   A O   1 
ATOM   454  C  CB  . TYR   A 1 69  ? -37.904 -21.170 14.499 1.00 83.58  ? 365 TYR   A CB  1 
ATOM   455  C  CG  . TYR   A 1 69  ? -38.406 -20.466 13.267 1.00 84.28  ? 365 TYR   A CG  1 
ATOM   456  C  CD1 . TYR   A 1 69  ? -38.572 -19.090 13.262 1.00 82.34  ? 365 TYR   A CD1 1 
ATOM   457  C  CD2 . TYR   A 1 69  ? -38.752 -21.174 12.124 1.00 86.45  ? 365 TYR   A CD2 1 
ATOM   458  C  CE1 . TYR   A 1 69  ? -39.047 -18.430 12.140 1.00 82.19  ? 365 TYR   A CE1 1 
ATOM   459  C  CE2 . TYR   A 1 69  ? -39.232 -20.524 11.004 1.00 85.64  ? 365 TYR   A CE2 1 
ATOM   460  C  CZ  . TYR   A 1 69  ? -39.373 -19.153 11.022 1.00 81.97  ? 365 TYR   A CZ  1 
ATOM   461  O  OH  . TYR   A 1 69  ? -39.850 -18.499 9.909  1.00 82.96  ? 365 TYR   A OH  1 
ATOM   462  N  N   . TYR   A 1 70  ? -40.570 -22.653 14.914 1.00 96.71  ? 366 TYR   A N   1 
ATOM   463  C  CA  . TYR   A 1 70  ? -41.877 -23.033 14.395 1.00 99.81  ? 366 TYR   A CA  1 
ATOM   464  C  C   . TYR   A 1 70  ? -42.961 -22.865 15.448 1.00 106.09 ? 366 TYR   A C   1 
ATOM   465  O  O   . TYR   A 1 70  ? -44.117 -22.587 15.108 1.00 109.91 ? 366 TYR   A O   1 
ATOM   466  C  CB  . TYR   A 1 70  ? -41.837 -24.463 13.857 1.00 101.37 ? 366 TYR   A CB  1 
ATOM   467  C  CG  . TYR   A 1 70  ? -41.295 -24.516 12.444 1.00 99.30  ? 366 TYR   A CG  1 
ATOM   468  C  CD1 . TYR   A 1 70  ? -42.138 -24.359 11.353 1.00 101.15 ? 366 TYR   A CD1 1 
ATOM   469  C  CD2 . TYR   A 1 70  ? -39.938 -24.685 12.205 1.00 96.28  ? 366 TYR   A CD2 1 
ATOM   470  C  CE1 . TYR   A 1 70  ? -41.647 -24.390 10.055 1.00 100.94 ? 366 TYR   A CE1 1 
ATOM   471  C  CE2 . TYR   A 1 70  ? -39.435 -24.718 10.917 1.00 94.44  ? 366 TYR   A CE2 1 
ATOM   472  C  CZ  . TYR   A 1 70  ? -40.294 -24.568 9.846  1.00 98.18  ? 366 TYR   A CZ  1 
ATOM   473  O  OH  . TYR   A 1 70  ? -39.796 -24.596 8.564  1.00 92.56  ? 366 TYR   A OH  1 
ATOM   474  N  N   . SER   A 1 71  ? -42.608 -23.008 16.726 1.00 110.36 ? 367 SER   A N   1 
ATOM   475  C  CA  . SER   A 1 71  ? -43.549 -22.666 17.782 1.00 111.81 ? 367 SER   A CA  1 
ATOM   476  C  C   . SER   A 1 71  ? -43.842 -21.173 17.801 1.00 110.16 ? 367 SER   A C   1 
ATOM   477  O  O   . SER   A 1 71  ? -44.883 -20.762 18.322 1.00 119.49 ? 367 SER   A O   1 
ATOM   478  C  CB  . SER   A 1 71  ? -43.006 -23.129 19.138 1.00 113.36 ? 367 SER   A CB  1 
ATOM   479  O  OG  . SER   A 1 71  ? -43.919 -22.849 20.185 1.00 121.28 ? 367 SER   A OG  1 
ATOM   480  N  N   . SER   A 1 72  ? -42.959 -20.356 17.230 1.00 102.92 ? 368 SER   A N   1 
ATOM   481  C  CA  . SER   A 1 72  ? -43.145 -18.911 17.225 1.00 100.15 ? 368 SER   A CA  1 
ATOM   482  C  C   . SER   A 1 72  ? -44.070 -18.430 16.116 1.00 104.28 ? 368 SER   A C   1 
ATOM   483  O  O   . SER   A 1 72  ? -44.701 -17.377 16.264 1.00 104.79 ? 368 SER   A O   1 
ATOM   484  C  CB  . SER   A 1 72  ? -41.795 -18.203 17.089 1.00 93.34  ? 368 SER   A CB  1 
ATOM   485  O  OG  . SER   A 1 72  ? -41.654 -17.619 15.806 1.00 91.59  ? 368 SER   A OG  1 
ATOM   486  N  N   . ILE   A 1 73  ? -44.154 -19.148 14.996 1.00 103.51 ? 369 ILE   A N   1 
ATOM   487  C  CA  . ILE   A 1 73  ? -45.047 -18.731 13.923 1.00 105.71 ? 369 ILE   A CA  1 
ATOM   488  C  C   . ILE   A 1 73  ? -46.355 -19.496 14.062 1.00 112.65 ? 369 ILE   A C   1 
ATOM   489  O  O   . ILE   A 1 73  ? -47.113 -19.632 13.098 1.00 113.43 ? 369 ILE   A O   1 
ATOM   490  C  CB  . ILE   A 1 73  ? -44.396 -18.942 12.543 1.00 103.32 ? 369 ILE   A CB  1 
ATOM   491  C  CG1 . ILE   A 1 73  ? -43.945 -20.396 12.388 1.00 103.66 ? 369 ILE   A CG1 1 
ATOM   492  C  CG2 . ILE   A 1 73  ? -43.215 -17.985 12.367 1.00 97.94  ? 369 ILE   A CG2 1 
ATOM   493  C  CD1 . ILE   A 1 73  ? -43.096 -20.640 11.167 1.00 99.16  ? 369 ILE   A CD1 1 
ATOM   494  N  N   . LYS   A 1 74  ? -46.625 -19.982 15.276 1.00 114.51 ? 370 LYS   A N   1 
ATOM   495  C  CA  . LYS   A 1 74  ? -47.839 -20.738 15.597 1.00 121.11 ? 370 LYS   A CA  1 
ATOM   496  C  C   . LYS   A 1 74  ? -48.024 -21.919 14.644 1.00 124.41 ? 370 LYS   A C   1 
ATOM   497  O  O   . LYS   A 1 74  ? -49.128 -22.195 14.166 1.00 131.21 ? 370 LYS   A O   1 
ATOM   498  C  CB  . LYS   A 1 74  ? -49.077 -19.834 15.599 1.00 124.00 ? 370 LYS   A CB  1 
ATOM   499  C  CG  . LYS   A 1 74  ? -48.790 -18.370 15.935 1.00 120.46 ? 370 LYS   A CG  1 
ATOM   500  C  CD  . LYS   A 1 74  ? -49.426 -17.913 17.234 1.00 122.91 ? 370 LYS   A CD  1 
ATOM   501  C  CE  . LYS   A 1 74  ? -49.184 -16.419 17.425 1.00 122.71 ? 370 LYS   A CE  1 
ATOM   502  N  NZ  . LYS   A 1 74  ? -49.479 -15.957 18.804 1.00 122.63 ? 370 LYS   A NZ  1 
ATOM   503  N  N   . ARG   A 1 75  ? -46.925 -22.628 14.366 1.00 120.29 ? 371 ARG   A N   1 
ATOM   504  C  CA  . ARG   A 1 75  ? -46.949 -23.833 13.536 1.00 121.12 ? 371 ARG   A CA  1 
ATOM   505  C  C   . ARG   A 1 75  ? -46.002 -24.893 14.094 1.00 121.65 ? 371 ARG   A C   1 
ATOM   506  O  O   . ARG   A 1 75  ? -45.249 -25.534 13.350 1.00 118.85 ? 371 ARG   A O   1 
ATOM   507  C  CB  . ARG   A 1 75  ? -46.607 -23.509 12.086 1.00 117.63 ? 371 ARG   A CB  1 
ATOM   508  C  CG  . ARG   A 1 75  ? -47.653 -22.664 11.397 1.00 119.43 ? 371 ARG   A CG  1 
ATOM   509  C  CD  . ARG   A 1 75  ? -47.004 -21.599 10.545 1.00 117.97 ? 371 ARG   A CD  1 
ATOM   510  N  NE  . ARG   A 1 75  ? -47.397 -21.719 9.148  1.00 121.60 ? 371 ARG   A NE  1 
ATOM   511  C  CZ  . ARG   A 1 75  ? -46.759 -22.462 8.255  1.00 123.80 ? 371 ARG   A CZ  1 
ATOM   512  N  NH1 . ARG   A 1 75  ? -45.689 -23.170 8.584  1.00 122.17 ? 371 ARG   A NH1 1 
ATOM   513  N  NH2 . ARG   A 1 75  ? -47.204 -22.497 7.002  1.00 125.15 ? 371 ARG   A NH2 1 
ATOM   514  N  N   . PHE   A 1 76  ? -46.035 -25.085 15.416 1.00 121.61 ? 372 PHE   A N   1 
ATOM   515  C  CA  . PHE   A 1 76  ? -45.293 -26.151 16.079 1.00 121.99 ? 372 PHE   A CA  1 
ATOM   516  C  C   . PHE   A 1 76  ? -45.842 -27.499 15.627 1.00 124.11 ? 372 PHE   A C   1 
ATOM   517  O  O   . PHE   A 1 76  ? -47.040 -27.768 15.769 1.00 127.24 ? 372 PHE   A O   1 
ATOM   518  C  CB  . PHE   A 1 76  ? -45.418 -25.982 17.598 1.00 125.82 ? 372 PHE   A CB  1 
ATOM   519  C  CG  . PHE   A 1 76  ? -44.505 -26.876 18.430 1.00 124.87 ? 372 PHE   A CG  1 
ATOM   520  C  CD1 . PHE   A 1 76  ? -44.162 -28.161 18.032 1.00 126.02 ? 372 PHE   A CD1 1 
ATOM   521  C  CD2 . PHE   A 1 76  ? -44.021 -26.421 19.645 1.00 128.38 ? 372 PHE   A CD2 1 
ATOM   522  C  CE1 . PHE   A 1 76  ? -43.347 -28.958 18.810 1.00 126.81 ? 372 PHE   A CE1 1 
ATOM   523  C  CE2 . PHE   A 1 76  ? -43.203 -27.217 20.432 1.00 131.03 ? 372 PHE   A CE2 1 
ATOM   524  C  CZ  . PHE   A 1 76  ? -42.866 -28.490 20.009 1.00 128.39 ? 372 PHE   A CZ  1 
ATOM   525  N  N   . GLY   A 1 77  ? -44.967 -28.348 15.093 1.00 123.94 ? 373 GLY   A N   1 
ATOM   526  C  CA  . GLY   A 1 77  ? -45.338 -29.700 14.729 1.00 126.18 ? 373 GLY   A CA  1 
ATOM   527  C  C   . GLY   A 1 77  ? -46.087 -29.835 13.423 1.00 129.17 ? 373 GLY   A C   1 
ATOM   528  O  O   . GLY   A 1 77  ? -46.420 -30.962 13.031 1.00 134.98 ? 373 GLY   A O   1 
ATOM   529  N  N   . SER   A 1 78  ? -46.358 -28.730 12.733 1.00 125.69 ? 374 SER   A N   1 
ATOM   530  C  CA  . SER   A 1 78  ? -47.018 -28.789 11.437 1.00 123.48 ? 374 SER   A CA  1 
ATOM   531  C  C   . SER   A 1 78  ? -46.155 -29.548 10.435 1.00 120.98 ? 374 SER   A C   1 
ATOM   532  O  O   . SER   A 1 78  ? -45.033 -29.955 10.758 1.00 119.98 ? 374 SER   A O   1 
ATOM   533  C  CB  . SER   A 1 78  ? -47.322 -27.380 10.928 1.00 122.52 ? 374 SER   A CB  1 
ATOM   534  O  OG  . SER   A 1 78  ? -46.139 -26.608 10.846 1.00 121.29 ? 374 SER   A OG  1 
ATOM   535  N  N   . LYS   A 1 79  ? -46.675 -29.745 9.220  1.00 120.60 ? 375 LYS   A N   1 
ATOM   536  C  CA  . LYS   A 1 79  ? -45.927 -30.478 8.204  1.00 118.15 ? 375 LYS   A CA  1 
ATOM   537  C  C   . LYS   A 1 79  ? -44.652 -29.739 7.819  1.00 113.97 ? 375 LYS   A C   1 
ATOM   538  O  O   . LYS   A 1 79  ? -43.583 -30.348 7.694  1.00 112.73 ? 375 LYS   A O   1 
ATOM   539  C  CB  . LYS   A 1 79  ? -46.805 -30.720 6.974  1.00 119.69 ? 375 LYS   A CB  1 
ATOM   540  C  CG  . LYS   A 1 79  ? -46.099 -31.468 5.843  1.00 120.40 ? 375 LYS   A CG  1 
ATOM   541  C  CD  . LYS   A 1 79  ? -46.617 -32.898 5.690  1.00 125.90 ? 375 LYS   A CD  1 
ATOM   542  C  CE  . LYS   A 1 79  ? -45.643 -33.766 4.895  1.00 124.38 ? 375 LYS   A CE  1 
ATOM   543  N  NZ  . LYS   A 1 79  ? -44.347 -33.943 5.626  1.00 126.30 ? 375 LYS   A NZ  1 
ATOM   544  N  N   . ALA   A 1 80  ? -44.743 -28.419 7.631  1.00 113.35 ? 376 ALA   A N   1 
ATOM   545  C  CA  . ALA   A 1 80  ? -43.562 -27.655 7.240  1.00 112.08 ? 376 ALA   A CA  1 
ATOM   546  C  C   . ALA   A 1 80  ? -42.460 -27.775 8.288  1.00 109.58 ? 376 ALA   A C   1 
ATOM   547  O  O   . ALA   A 1 80  ? -41.276 -27.873 7.943  1.00 107.19 ? 376 ALA   A O   1 
ATOM   548  C  CB  . ALA   A 1 80  ? -43.930 -26.189 6.997  1.00 109.04 ? 376 ALA   A CB  1 
ATOM   549  N  N   . HIS   A 1 81  ? -42.834 -27.792 9.571  1.00 109.91 ? 377 HIS   A N   1 
ATOM   550  C  CA  . HIS   A 1 81  ? -41.862 -28.015 10.640 1.00 109.11 ? 377 HIS   A CA  1 
ATOM   551  C  C   . HIS   A 1 81  ? -41.180 -29.369 10.490 1.00 111.34 ? 377 HIS   A C   1 
ATOM   552  O  O   . HIS   A 1 81  ? -39.947 -29.464 10.506 1.00 107.81 ? 377 HIS   A O   1 
ATOM   553  C  CB  . HIS   A 1 81  ? -42.554 -27.914 12.002 1.00 110.02 ? 377 HIS   A CB  1 
ATOM   554  C  CG  . HIS   A 1 81  ? -41.647 -28.162 13.170 1.00 107.89 ? 377 HIS   A CG  1 
ATOM   555  N  ND1 . HIS   A 1 81  ? -42.126 -28.355 14.449 1.00 110.25 ? 377 HIS   A ND1 1 
ATOM   556  C  CD2 . HIS   A 1 81  ? -40.297 -28.231 13.261 1.00 103.42 ? 377 HIS   A CD2 1 
ATOM   557  C  CE1 . HIS   A 1 81  ? -41.112 -28.538 15.276 1.00 106.35 ? 377 HIS   A CE1 1 
ATOM   558  N  NE2 . HIS   A 1 81  ? -39.991 -28.465 14.582 1.00 102.55 ? 377 HIS   A NE2 1 
ATOM   559  N  N   . MET   A 1 82  ? -41.972 -30.433 10.364 1.00 115.44 ? 378 MET   A N   1 
ATOM   560  C  CA  . MET   A 1 82  ? -41.408 -31.772 10.227 1.00 116.54 ? 378 MET   A CA  1 
ATOM   561  C  C   . MET   A 1 82  ? -40.478 -31.869 9.019  1.00 115.46 ? 378 MET   A C   1 
ATOM   562  O  O   . MET   A 1 82  ? -39.402 -32.475 9.102  1.00 118.00 ? 378 MET   A O   1 
ATOM   563  C  CB  . MET   A 1 82  ? -42.537 -32.797 10.126 1.00 120.90 ? 378 MET   A CB  1 
ATOM   564  C  CG  . MET   A 1 82  ? -43.425 -32.846 11.364 1.00 128.69 ? 378 MET   A CG  1 
ATOM   565  S  SD  . MET   A 1 82  ? -42.530 -33.396 12.833 1.00 138.77 ? 378 MET   A SD  1 
ATOM   566  C  CE  . MET   A 1 82  ? -42.252 -31.855 13.706 1.00 125.67 ? 378 MET   A CE  1 
ATOM   567  N  N   . ASP   A 1 83  ? -40.868 -31.271 7.890  1.00 112.09 ? 379 ASP   A N   1 
ATOM   568  C  CA  . ASP   A 1 83  ? -40.045 -31.377 6.689  1.00 110.26 ? 379 ASP   A CA  1 
ATOM   569  C  C   . ASP   A 1 83  ? -38.761 -30.575 6.821  1.00 108.49 ? 379 ASP   A C   1 
ATOM   570  O  O   . ASP   A 1 83  ? -37.692 -31.037 6.404  1.00 105.99 ? 379 ASP   A O   1 
ATOM   571  C  CB  . ASP   A 1 83  ? -40.835 -30.920 5.466  1.00 110.92 ? 379 ASP   A CB  1 
ATOM   572  C  CG  . ASP   A 1 83  ? -41.878 -31.917 5.059  1.00 115.35 ? 379 ASP   A CG  1 
ATOM   573  O  OD1 . ASP   A 1 83  ? -41.589 -33.132 5.128  1.00 116.58 ? 379 ASP   A OD1 1 
ATOM   574  O  OD2 . ASP   A 1 83  ? -42.987 -31.490 4.682  1.00 118.73 ? 379 ASP   A OD2 1 
ATOM   575  N  N   . ARG   A 1 84  ? -38.851 -29.366 7.383  1.00 105.03 ? 380 ARG   A N   1 
ATOM   576  C  CA  . ARG   A 1 84  ? -37.660 -28.559 7.619  1.00 100.21 ? 380 ARG   A CA  1 
ATOM   577  C  C   . ARG   A 1 84  ? -36.724 -29.241 8.603  1.00 101.27 ? 380 ARG   A C   1 
ATOM   578  O  O   . ARG   A 1 84  ? -35.500 -29.077 8.529  1.00 100.84 ? 380 ARG   A O   1 
ATOM   579  C  CB  . ARG   A 1 84  ? -38.059 -27.185 8.146  1.00 96.99  ? 380 ARG   A CB  1 
ATOM   580  C  CG  . ARG   A 1 84  ? -36.896 -26.290 8.455  1.00 90.51  ? 380 ARG   A CG  1 
ATOM   581  C  CD  . ARG   A 1 84  ? -36.499 -25.484 7.242  1.00 87.85  ? 380 ARG   A CD  1 
ATOM   582  N  NE  . ARG   A 1 84  ? -35.269 -24.746 7.488  1.00 83.47  ? 380 ARG   A NE  1 
ATOM   583  C  CZ  . ARG   A 1 84  ? -34.105 -25.045 6.933  1.00 82.90  ? 380 ARG   A CZ  1 
ATOM   584  N  NH1 . ARG   A 1 84  ? -33.997 -26.012 6.042  1.00 88.27  ? 380 ARG   A NH1 1 
ATOM   585  N  NH2 . ARG   A 1 84  ? -33.021 -24.358 7.283  1.00 79.20  ? 380 ARG   A NH2 1 
ATOM   586  N  N   . LEU   A 1 85  ? -37.287 -29.991 9.548  1.00 105.12 ? 381 LEU   A N   1 
ATOM   587  C  CA  . LEU   A 1 85  ? -36.467 -30.783 10.455 1.00 103.47 ? 381 LEU   A CA  1 
ATOM   588  C  C   . LEU   A 1 85  ? -35.688 -31.846 9.696  1.00 106.69 ? 381 LEU   A C   1 
ATOM   589  O  O   . LEU   A 1 85  ? -34.463 -31.951 9.824  1.00 105.13 ? 381 LEU   A O   1 
ATOM   590  C  CB  . LEU   A 1 85  ? -37.353 -31.433 11.510 1.00 104.80 ? 381 LEU   A CB  1 
ATOM   591  C  CG  . LEU   A 1 85  ? -36.694 -31.533 12.875 1.00 100.93 ? 381 LEU   A CG  1 
ATOM   592  C  CD1 . LEU   A 1 85  ? -36.503 -30.139 13.411 1.00 97.69  ? 381 LEU   A CD1 1 
ATOM   593  C  CD2 . LEU   A 1 85  ? -37.558 -32.364 13.793 1.00 103.99 ? 381 LEU   A CD2 1 
ATOM   594  N  N   . GLU   A 1 86  ? -36.392 -32.649 8.898  1.00 109.62 ? 382 GLU   A N   1 
ATOM   595  C  CA  . GLU   A 1 86  ? -35.730 -33.669 8.091  1.00 114.24 ? 382 GLU   A CA  1 
ATOM   596  C  C   . GLU   A 1 86  ? -34.808 -33.036 7.055  1.00 110.02 ? 382 GLU   A C   1 
ATOM   597  O  O   . GLU   A 1 86  ? -33.734 -33.572 6.759  1.00 112.59 ? 382 GLU   A O   1 
ATOM   598  C  CB  . GLU   A 1 86  ? -36.775 -34.555 7.411  1.00 124.92 ? 382 GLU   A CB  1 
ATOM   599  C  CG  . GLU   A 1 86  ? -36.201 -35.733 6.638  1.00 132.95 ? 382 GLU   A CG  1 
ATOM   600  C  CD  . GLU   A 1 86  ? -36.067 -36.992 7.480  1.00 142.08 ? 382 GLU   A CD  1 
ATOM   601  O  OE1 . GLU   A 1 86  ? -36.196 -36.908 8.723  1.00 144.61 ? 382 GLU   A OE1 1 
ATOM   602  O  OE2 . GLU   A 1 86  ? -35.838 -38.072 6.894  1.00 149.53 ? 382 GLU   A OE2 1 
ATOM   603  N  N   . GLU   A 1 87  ? -35.212 -31.896 6.494  1.00 104.69 ? 383 GLU   A N   1 
ATOM   604  C  CA  . GLU   A 1 87  ? -34.371 -31.203 5.526  1.00 99.83  ? 383 GLU   A CA  1 
ATOM   605  C  C   . GLU   A 1 87  ? -33.035 -30.806 6.143  1.00 100.64 ? 383 GLU   A C   1 
ATOM   606  O  O   . GLU   A 1 87  ? -31.975 -30.991 5.534  1.00 96.20  ? 383 GLU   A O   1 
ATOM   607  C  CB  . GLU   A 1 87  ? -35.115 -29.981 4.991  1.00 97.63  ? 383 GLU   A CB  1 
ATOM   608  C  CG  . GLU   A 1 87  ? -34.277 -29.042 4.153  1.00 96.62  ? 383 GLU   A CG  1 
ATOM   609  C  CD  . GLU   A 1 87  ? -35.110 -27.957 3.490  1.00 94.07  ? 383 GLU   A CD  1 
ATOM   610  O  OE1 . GLU   A 1 87  ? -35.700 -27.131 4.230  1.00 91.12  ? 383 GLU   A OE1 1 
ATOM   611  O  OE2 . GLU   A 1 87  ? -35.174 -27.935 2.233  1.00 89.34  ? 383 GLU   A OE2 1 
ATOM   612  N  N   . VAL   A 1 88  ? -33.065 -30.264 7.364  1.00 100.92 ? 384 VAL   A N   1 
ATOM   613  C  CA  . VAL   A 1 88  ? -31.832 -29.844 8.027  1.00 98.97  ? 384 VAL   A CA  1 
ATOM   614  C  C   . VAL   A 1 88  ? -31.039 -31.044 8.528  1.00 103.60 ? 384 VAL   A C   1 
ATOM   615  O  O   . VAL   A 1 88  ? -29.806 -31.062 8.446  1.00 101.52 ? 384 VAL   A O   1 
ATOM   616  C  CB  . VAL   A 1 88  ? -32.157 -28.863 9.167  1.00 94.04  ? 384 VAL   A CB  1 
ATOM   617  C  CG1 . VAL   A 1 88  ? -30.963 -28.702 10.106 1.00 92.56  ? 384 VAL   A CG1 1 
ATOM   618  C  CG2 . VAL   A 1 88  ? -32.573 -27.524 8.595  1.00 90.23  ? 384 VAL   A CG2 1 
ATOM   619  N  N   . ASN   A 1 89  ? -31.723 -32.051 9.078  1.00 105.79 ? 385 ASN   A N   1 
ATOM   620  C  CA  . ASN   A 1 89  ? -31.049 -33.295 9.441  1.00 107.67 ? 385 ASN   A CA  1 
ATOM   621  C  C   . ASN   A 1 89  ? -30.283 -33.865 8.246  1.00 108.73 ? 385 ASN   A C   1 
ATOM   622  O  O   . ASN   A 1 89  ? -29.099 -34.203 8.350  1.00 112.85 ? 385 ASN   A O   1 
ATOM   623  C  CB  . ASN   A 1 89  ? -32.074 -34.308 9.966  1.00 113.16 ? 385 ASN   A CB  1 
ATOM   624  C  CG  . ASN   A 1 89  ? -31.430 -35.495 10.663 1.00 118.28 ? 385 ASN   A CG  1 
ATOM   625  O  OD1 . ASN   A 1 89  ? -30.550 -35.330 11.509 1.00 119.58 ? 385 ASN   A OD1 1 
ATOM   626  N  ND2 . ASN   A 1 89  ? -31.866 -36.702 10.306 1.00 123.07 ? 385 ASN   A ND2 1 
ATOM   627  N  N   . LYS   A 1 90  ? -30.937 -33.948 7.088  1.00 107.89 ? 386 LYS   A N   1 
ATOM   628  C  CA  . LYS   A 1 90  ? -30.260 -34.487 5.914  1.00 107.39 ? 386 LYS   A CA  1 
ATOM   629  C  C   . LYS   A 1 90  ? -29.124 -33.581 5.443  1.00 106.21 ? 386 LYS   A C   1 
ATOM   630  O  O   . LYS   A 1 90  ? -28.097 -34.078 4.967  1.00 107.64 ? 386 LYS   A O   1 
ATOM   631  C  CB  . LYS   A 1 90  ? -31.267 -34.725 4.788  1.00 109.51 ? 386 LYS   A CB  1 
ATOM   632  C  CG  . LYS   A 1 90  ? -32.113 -35.984 4.971  1.00 115.02 ? 386 LYS   A CG  1 
ATOM   633  C  CD  . LYS   A 1 90  ? -33.144 -36.154 3.862  1.00 115.64 ? 386 LYS   A CD  1 
ATOM   634  C  CE  . LYS   A 1 90  ? -34.045 -37.345 4.141  1.00 118.87 ? 386 LYS   A CE  1 
ATOM   635  N  NZ  . LYS   A 1 90  ? -35.221 -37.395 3.234  1.00 125.99 ? 386 LYS   A NZ  1 
ATOM   636  N  N   . GLU   A 1 91  ? -29.270 -32.259 5.571  1.00 103.51 ? 387 GLU   A N   1 
ATOM   637  C  CA  . GLU   A 1 91  ? -28.179 -31.382 5.156  1.00 101.34 ? 387 GLU   A CA  1 
ATOM   638  C  C   . GLU   A 1 91  ? -26.991 -31.460 6.112  1.00 104.15 ? 387 GLU   A C   1 
ATOM   639  O  O   . GLU   A 1 91  ? -25.842 -31.294 5.682  1.00 104.77 ? 387 GLU   A O   1 
ATOM   640  C  CB  . GLU   A 1 91  ? -28.663 -29.939 5.032  1.00 95.13  ? 387 GLU   A CB  1 
ATOM   641  C  CG  . GLU   A 1 91  ? -27.553 -28.998 4.601  1.00 91.75  ? 387 GLU   A CG  1 
ATOM   642  C  CD  . GLU   A 1 91  ? -27.990 -27.558 4.494  1.00 89.95  ? 387 GLU   A CD  1 
ATOM   643  O  OE1 . GLU   A 1 91  ? -29.143 -27.240 4.866  1.00 89.70  ? 387 GLU   A OE1 1 
ATOM   644  O  OE2 . GLU   A 1 91  ? -27.161 -26.734 4.055  1.00 88.57  ? 387 GLU   A OE2 1 
ATOM   645  N  N   . ILE   A 1 92  ? -27.236 -31.703 7.404  1.00 105.01 ? 388 ILE   A N   1 
ATOM   646  C  CA  . ILE   A 1 92  ? -26.134 -31.957 8.325  1.00 103.87 ? 388 ILE   A CA  1 
ATOM   647  C  C   . ILE   A 1 92  ? -25.473 -33.299 8.026  1.00 108.55 ? 388 ILE   A C   1 
ATOM   648  O  O   . ILE   A 1 92  ? -24.291 -33.493 8.327  1.00 110.25 ? 388 ILE   A O   1 
ATOM   649  C  CB  . ILE   A 1 92  ? -26.628 -31.874 9.784  1.00 101.37 ? 388 ILE   A CB  1 
ATOM   650  C  CG1 . ILE   A 1 92  ? -27.233 -30.498 10.057 1.00 96.45  ? 388 ILE   A CG1 1 
ATOM   651  C  CG2 . ILE   A 1 92  ? -25.488 -32.115 10.768 1.00 102.57 ? 388 ILE   A CG2 1 
ATOM   652  C  CD1 . ILE   A 1 92  ? -27.814 -30.358 11.447 1.00 96.25  ? 388 ILE   A CD1 1 
ATOM   653  N  N   . GLU   A 1 93  ? -26.195 -34.235 7.418  1.00 109.18 ? 389 GLU   A N   1 
ATOM   654  C  CA  . GLU   A 1 93  ? -25.549 -35.456 6.951  1.00 114.14 ? 389 GLU   A CA  1 
ATOM   655  C  C   . GLU   A 1 93  ? -24.590 -35.159 5.802  1.00 114.01 ? 389 GLU   A C   1 
ATOM   656  O  O   . GLU   A 1 93  ? -23.384 -35.419 5.898  1.00 115.54 ? 389 GLU   A O   1 
ATOM   657  C  CB  . GLU   A 1 93  ? -26.607 -36.475 6.529  1.00 117.88 ? 389 GLU   A CB  1 
ATOM   658  C  CG  . GLU   A 1 93  ? -27.593 -36.826 7.627  1.00 119.29 ? 389 GLU   A CG  1 
ATOM   659  C  CD  . GLU   A 1 93  ? -26.995 -37.748 8.668  1.00 127.04 ? 389 GLU   A CD  1 
ATOM   660  O  OE1 . GLU   A 1 93  ? -26.003 -38.439 8.340  1.00 127.81 ? 389 GLU   A OE1 1 
ATOM   661  O  OE2 . GLU   A 1 93  ? -27.515 -37.782 9.811  1.00 129.40 ? 389 GLU   A OE2 1 
ATOM   662  N  N   . SER   A 1 94  ? -25.109 -34.585 4.713  1.00 113.85 ? 390 SER   A N   1 
ATOM   663  C  CA  . SER   A 1 94  ? -24.327 -34.460 3.485  1.00 116.68 ? 390 SER   A CA  1 
ATOM   664  C  C   . SER   A 1 94  ? -23.170 -33.479 3.648  1.00 117.28 ? 390 SER   A C   1 
ATOM   665  O  O   . SER   A 1 94  ? -22.111 -33.655 3.033  1.00 117.68 ? 390 SER   A O   1 
ATOM   666  C  CB  . SER   A 1 94  ? -25.227 -34.017 2.333  1.00 116.49 ? 390 SER   A CB  1 
ATOM   667  O  OG  . SER   A 1 94  ? -25.331 -32.604 2.291  1.00 120.40 ? 390 SER   A OG  1 
ATOM   668  N  N   . THR   A 1 95  ? -23.354 -32.438 4.463  1.00 114.57 ? 391 THR   A N   1 
ATOM   669  C  CA  . THR   A 1 95  ? -22.393 -31.346 4.555  1.00 114.36 ? 391 THR   A CA  1 
ATOM   670  C  C   . THR   A 1 95  ? -21.831 -31.131 5.958  1.00 110.69 ? 391 THR   A C   1 
ATOM   671  O  O   . THR   A 1 95  ? -20.928 -30.302 6.121  1.00 109.57 ? 391 THR   A O   1 
ATOM   672  C  CB  . THR   A 1 95  ? -23.037 -30.036 4.058  1.00 112.59 ? 391 THR   A CB  1 
ATOM   673  O  OG1 . THR   A 1 95  ? -23.937 -30.330 2.977  1.00 111.80 ? 391 THR   A OG1 1 
ATOM   674  C  CG2 . THR   A 1 95  ? -21.976 -29.047 3.563  1.00 111.49 ? 391 THR   A CG2 1 
ATOM   675  N  N   . SER   A 1 96  ? -22.315 -31.861 6.966  1.00 111.55 ? 392 SER   A N   1 
ATOM   676  C  CA  . SER   A 1 96  ? -21.897 -31.678 8.362  1.00 111.92 ? 392 SER   A CA  1 
ATOM   677  C  C   . SER   A 1 96  ? -22.093 -30.236 8.816  1.00 108.15 ? 392 SER   A C   1 
ATOM   678  O  O   . SER   A 1 96  ? -21.309 -29.707 9.607  1.00 107.57 ? 392 SER   A O   1 
ATOM   679  C  CB  . SER   A 1 96  ? -20.449 -32.132 8.590  1.00 120.21 ? 392 SER   A CB  1 
ATOM   680  O  OG  . SER   A 1 96  ? -19.536 -31.364 7.829  1.00 124.24 ? 392 SER   A OG  1 
ATOM   681  N  N   . THR   A 1 97  ? -23.136 -29.603 8.291  1.00 103.14 ? 393 THR   A N   1 
ATOM   682  C  CA  . THR   A 1 97  ? -23.568 -28.260 8.659  1.00 95.15  ? 393 THR   A CA  1 
ATOM   683  C  C   . THR   A 1 97  ? -24.896 -28.028 7.952  1.00 93.36  ? 393 THR   A C   1 
ATOM   684  O  O   . THR   A 1 97  ? -25.430 -28.923 7.289  1.00 94.39  ? 393 THR   A O   1 
ATOM   685  C  CB  . THR   A 1 97  ? -22.539 -27.191 8.286  1.00 89.31  ? 393 THR   A CB  1 
ATOM   686  O  OG1 . THR   A 1 97  ? -22.946 -25.929 8.834  1.00 85.80  ? 393 THR   A OG1 1 
ATOM   687  C  CG2 . THR   A 1 97  ? -22.430 -27.060 6.770  1.00 91.68  ? 393 THR   A CG2 1 
ATOM   688  N  N   . TYR   A 1 98  ? -25.438 -26.827 8.104  1.00 83.99  ? 394 TYR   A N   1 
ATOM   689  C  CA  . TYR   A 1 98  ? -26.658 -26.483 7.389  1.00 82.59  ? 394 TYR   A CA  1 
ATOM   690  C  C   . TYR   A 1 98  ? -26.734 -24.967 7.242  1.00 79.26  ? 394 TYR   A C   1 
ATOM   691  O  O   . TYR   A 1 98  ? -25.896 -24.226 7.759  1.00 78.46  ? 394 TYR   A O   1 
ATOM   692  C  CB  . TYR   A 1 98  ? -27.895 -27.067 8.088  1.00 82.51  ? 394 TYR   A CB  1 
ATOM   693  C  CG  . TYR   A 1 98  ? -28.210 -26.436 9.412  1.00 80.07  ? 394 TYR   A CG  1 
ATOM   694  C  CD1 . TYR   A 1 98  ? -27.509 -26.789 10.564 1.00 80.47  ? 394 TYR   A CD1 1 
ATOM   695  C  CD2 . TYR   A 1 98  ? -29.219 -25.492 9.522  1.00 78.91  ? 394 TYR   A CD2 1 
ATOM   696  C  CE1 . TYR   A 1 98  ? -27.802 -26.207 11.780 1.00 77.26  ? 394 TYR   A CE1 1 
ATOM   697  C  CE2 . TYR   A 1 98  ? -29.517 -24.908 10.736 1.00 75.33  ? 394 TYR   A CE2 1 
ATOM   698  C  CZ  . TYR   A 1 98  ? -28.811 -25.271 11.854 1.00 74.29  ? 394 TYR   A CZ  1 
ATOM   699  O  OH  . TYR   A 1 98  ? -29.125 -24.673 13.046 1.00 74.97  ? 394 TYR   A OH  1 
ATOM   700  N  N   . GLN   A 1 99  ? -27.750 -24.517 6.511  1.00 77.82  ? 395 GLN   A N   1 
ATOM   701  C  CA  . GLN   A 1 99  ? -27.940 -23.111 6.183  1.00 75.99  ? 395 GLN   A CA  1 
ATOM   702  C  C   . GLN   A 1 99  ? -29.312 -22.670 6.664  1.00 72.48  ? 395 GLN   A C   1 
ATOM   703  O  O   . GLN   A 1 99  ? -30.317 -23.332 6.376  1.00 73.69  ? 395 GLN   A O   1 
ATOM   704  C  CB  . GLN   A 1 99  ? -27.815 -22.872 4.667  1.00 73.14  ? 395 GLN   A CB  1 
ATOM   705  C  CG  . GLN   A 1 99  ? -26.462 -23.229 4.078  1.00 71.54  ? 395 GLN   A CG  1 
ATOM   706  C  CD  . GLN   A 1 99  ? -25.356 -22.326 4.579  1.00 72.98  ? 395 GLN   A CD  1 
ATOM   707  O  OE1 . GLN   A 1 99  ? -25.577 -21.149 4.867  1.00 75.07  ? 395 GLN   A OE1 1 
ATOM   708  N  NE2 . GLN   A 1 99  ? -24.159 -22.879 4.710  1.00 74.30  ? 395 GLN   A NE2 1 
ATOM   709  N  N   . LEU   A 1 100 ? -29.354 -21.540 7.357  1.00 69.82  ? 396 LEU   A N   1 
ATOM   710  C  CA  . LEU   A 1 100 ? -30.617 -20.995 7.826  1.00 70.29  ? 396 LEU   A CA  1 
ATOM   711  C  C   . LEU   A 1 100 ? -31.405 -20.376 6.678  1.00 70.93  ? 396 LEU   A C   1 
ATOM   712  O  O   . LEU   A 1 100 ? -30.839 -19.728 5.793  1.00 69.24  ? 396 LEU   A O   1 
ATOM   713  C  CB  . LEU   A 1 100 ? -30.369 -19.941 8.906  1.00 69.48  ? 396 LEU   A CB  1 
ATOM   714  C  CG  . LEU   A 1 100 ? -29.704 -20.467 10.177 1.00 66.57  ? 396 LEU   A CG  1 
ATOM   715  C  CD1 . LEU   A 1 100 ? -29.263 -19.309 11.047 1.00 66.15  ? 396 LEU   A CD1 1 
ATOM   716  C  CD2 . LEU   A 1 100 ? -30.681 -21.363 10.912 1.00 69.80  ? 396 LEU   A CD2 1 
ATOM   717  N  N   . LYS   A 1 101 ? -32.722 -20.569 6.710  1.00 69.61  ? 397 LYS   A N   1 
ATOM   718  C  CA  . LYS   A 1 101 ? -33.611 -19.738 5.915  1.00 71.06  ? 397 LYS   A CA  1 
ATOM   719  C  C   . LYS   A 1 101 ? -33.499 -18.288 6.360  1.00 69.41  ? 397 LYS   A C   1 
ATOM   720  O  O   . LYS   A 1 101 ? -33.210 -17.998 7.524  1.00 70.22  ? 397 LYS   A O   1 
ATOM   721  C  CB  . LYS   A 1 101 ? -35.058 -20.208 6.063  1.00 72.80  ? 397 LYS   A CB  1 
ATOM   722  C  CG  . LYS   A 1 101 ? -35.325 -21.594 5.543  1.00 76.63  ? 397 LYS   A CG  1 
ATOM   723  C  CD  . LYS   A 1 101 ? -35.145 -21.630 4.045  1.00 80.61  ? 397 LYS   A CD  1 
ATOM   724  C  CE  . LYS   A 1 101 ? -35.209 -23.033 3.508  1.00 82.48  ? 397 LYS   A CE  1 
ATOM   725  N  NZ  . LYS   A 1 101 ? -34.652 -23.042 2.146  1.00 81.87  ? 397 LYS   A NZ  1 
ATOM   726  N  N   . ASP   A 1 102 ? -33.743 -17.373 5.421  1.00 66.06  ? 398 ASP   A N   1 
ATOM   727  C  CA  . ASP   A 1 102 ? -33.815 -15.951 5.744  1.00 69.14  ? 398 ASP   A CA  1 
ATOM   728  C  C   . ASP   A 1 102 ? -34.666 -15.701 6.982  1.00 67.75  ? 398 ASP   A C   1 
ATOM   729  O  O   . ASP   A 1 102 ? -34.257 -14.981 7.898  1.00 66.83  ? 398 ASP   A O   1 
ATOM   730  C  CB  . ASP   A 1 102 ? -34.398 -15.169 4.566  1.00 73.01  ? 398 ASP   A CB  1 
ATOM   731  C  CG  . ASP   A 1 102 ? -33.373 -14.850 3.494  1.00 77.45  ? 398 ASP   A CG  1 
ATOM   732  O  OD1 . ASP   A 1 102 ? -32.270 -15.443 3.501  1.00 75.57  ? 398 ASP   A OD1 1 
ATOM   733  O  OD2 . ASP   A 1 102 ? -33.680 -13.989 2.642  1.00 79.59  ? 398 ASP   A OD2 1 
ATOM   734  N  N   . THR   A 1 103 ? -35.862 -16.296 7.021  1.00 68.38  ? 399 THR   A N   1 
ATOM   735  C  CA  . THR   A 1 103 ? -36.755 -16.096 8.159  1.00 70.86  ? 399 THR   A CA  1 
ATOM   736  C  C   . THR   A 1 103 ? -36.135 -16.599 9.457  1.00 71.92  ? 399 THR   A C   1 
ATOM   737  O  O   . THR   A 1 103 ? -36.207 -15.922 10.491 1.00 70.48  ? 399 THR   A O   1 
ATOM   738  C  CB  . THR   A 1 103 ? -38.082 -16.796 7.896  1.00 73.21  ? 399 THR   A CB  1 
ATOM   739  O  OG1 . THR   A 1 103 ? -37.830 -18.170 7.579  1.00 74.56  ? 399 THR   A OG1 1 
ATOM   740  C  CG2 . THR   A 1 103 ? -38.791 -16.138 6.733  1.00 71.98  ? 399 THR   A CG2 1 
ATOM   741  N  N   . GLU   A 1 104 ? -35.531 -17.791 9.429  1.00 70.54  ? 400 GLU   A N   1 
ATOM   742  C  CA  . GLU   A 1 104 ? -34.876 -18.322 10.623 1.00 69.66  ? 400 GLU   A CA  1 
ATOM   743  C  C   . GLU   A 1 104 ? -33.714 -17.441 11.061 1.00 66.62  ? 400 GLU   A C   1 
ATOM   744  O  O   . GLU   A 1 104 ? -33.457 -17.293 12.267 1.00 65.59  ? 400 GLU   A O   1 
ATOM   745  C  CB  . GLU   A 1 104 ? -34.390 -19.747 10.353 1.00 72.46  ? 400 GLU   A CB  1 
ATOM   746  C  CG  . GLU   A 1 104 ? -35.504 -20.747 10.085 1.00 75.35  ? 400 GLU   A CG  1 
ATOM   747  C  CD  . GLU   A 1 104 ? -35.037 -21.973 9.308  1.00 76.74  ? 400 GLU   A CD  1 
ATOM   748  O  OE1 . GLU   A 1 104 ? -33.841 -22.039 8.937  1.00 73.80  ? 400 GLU   A OE1 1 
ATOM   749  O  OE2 . GLU   A 1 104 ? -35.872 -22.869 9.058  1.00 79.39  ? 400 GLU   A OE2 1 
ATOM   750  N  N   . LEU   A 1 105 ? -32.999 -16.859 10.099 1.00 67.21  ? 401 LEU   A N   1 
ATOM   751  C  CA  . LEU   A 1 105 ? -31.914 -15.939 10.424 1.00 66.16  ? 401 LEU   A CA  1 
ATOM   752  C  C   . LEU   A 1 105 ? -32.439 -14.711 11.153 1.00 63.32  ? 401 LEU   A C   1 
ATOM   753  O  O   . LEU   A 1 105 ? -31.895 -14.326 12.193 1.00 61.09  ? 401 LEU   A O   1 
ATOM   754  C  CB  . LEU   A 1 105 ? -31.169 -15.539 9.146  1.00 64.84  ? 401 LEU   A CB  1 
ATOM   755  C  CG  . LEU   A 1 105 ? -29.826 -14.810 9.268  1.00 62.16  ? 401 LEU   A CG  1 
ATOM   756  C  CD1 . LEU   A 1 105 ? -28.716 -15.743 9.736  1.00 59.93  ? 401 LEU   A CD1 1 
ATOM   757  C  CD2 . LEU   A 1 105 ? -29.475 -14.194 7.916  1.00 61.47  ? 401 LEU   A CD2 1 
ATOM   758  N  N   . ILE   A 1 106 ? -33.522 -14.111 10.648 1.00 64.25  ? 402 ILE   A N   1 
ATOM   759  C  CA  . ILE   A 1 106 ? -34.104 -12.935 11.297 1.00 64.24  ? 402 ILE   A CA  1 
ATOM   760  C  C   . ILE   A 1 106 ? -34.649 -13.295 12.683 1.00 62.61  ? 402 ILE   A C   1 
ATOM   761  O  O   . ILE   A 1 106 ? -34.491 -12.535 13.646 1.00 62.27  ? 402 ILE   A O   1 
ATOM   762  C  CB  . ILE   A 1 106 ? -35.190 -12.321 10.390 1.00 62.08  ? 402 ILE   A CB  1 
ATOM   763  C  CG1 . ILE   A 1 106 ? -34.587 -11.926 9.030  1.00 61.57  ? 402 ILE   A CG1 1 
ATOM   764  C  CG2 . ILE   A 1 106 ? -35.839 -11.121 11.059 1.00 62.49  ? 402 ILE   A CG2 1 
ATOM   765  C  CD1 . ILE   A 1 106 ? -35.600 -11.498 7.978  1.00 62.52  ? 402 ILE   A CD1 1 
ATOM   766  N  N   . TYR   A 1 107 ? -35.317 -14.444 12.800 1.00 64.43  ? 403 TYR   A N   1 
ATOM   767  C  CA  . TYR   A 1 107 ? -35.765 -14.915 14.106 1.00 63.48  ? 403 TYR   A CA  1 
ATOM   768  C  C   . TYR   A 1 107 ? -34.580 -15.129 15.038 1.00 64.74  ? 403 TYR   A C   1 
ATOM   769  O  O   . TYR   A 1 107 ? -34.568 -14.646 16.182 1.00 60.33  ? 403 TYR   A O   1 
ATOM   770  C  CB  . TYR   A 1 107 ? -36.562 -16.214 13.953 1.00 66.22  ? 403 TYR   A CB  1 
ATOM   771  C  CG  . TYR   A 1 107 ? -36.934 -16.857 15.275 1.00 70.93  ? 403 TYR   A CG  1 
ATOM   772  C  CD1 . TYR   A 1 107 ? -36.007 -17.616 15.988 1.00 71.00  ? 403 TYR   A CD1 1 
ATOM   773  C  CD2 . TYR   A 1 107 ? -38.204 -16.705 15.815 1.00 73.27  ? 403 TYR   A CD2 1 
ATOM   774  C  CE1 . TYR   A 1 107 ? -36.325 -18.196 17.188 1.00 71.53  ? 403 TYR   A CE1 1 
ATOM   775  C  CE2 . TYR   A 1 107 ? -38.538 -17.294 17.030 1.00 74.00  ? 403 TYR   A CE2 1 
ATOM   776  C  CZ  . TYR   A 1 107 ? -37.590 -18.035 17.710 1.00 74.60  ? 403 TYR   A CZ  1 
ATOM   777  O  OH  . TYR   A 1 107 ? -37.900 -18.620 18.920 1.00 75.60  ? 403 TYR   A OH  1 
ATOM   778  N  N   . GLY   A 1 108 ? -33.585 -15.885 14.568 1.00 65.33  ? 404 GLY   A N   1 
ATOM   779  C  CA  . GLY   A 1 108 ? -32.415 -16.155 15.387 1.00 63.89  ? 404 GLY   A CA  1 
ATOM   780  C  C   . GLY   A 1 108 ? -31.776 -14.887 15.909 1.00 61.76  ? 404 GLY   A C   1 
ATOM   781  O  O   . GLY   A 1 108 ? -31.503 -14.757 17.101 1.00 57.33  ? 404 GLY   A O   1 
ATOM   782  N  N   . ALA   A 1 109 ? -31.552 -13.920 15.021 1.00 58.90  ? 405 ALA   A N   1 
ATOM   783  C  CA  . ALA   A 1 109 ? -30.862 -12.703 15.432 1.00 58.01  ? 405 ALA   A CA  1 
ATOM   784  C  C   . ALA   A 1 109 ? -31.674 -11.914 16.452 1.00 56.09  ? 405 ALA   A C   1 
ATOM   785  O  O   . ALA   A 1 109 ? -31.121 -11.399 17.431 1.00 56.08  ? 405 ALA   A O   1 
ATOM   786  C  CB  . ALA   A 1 109 ? -30.555 -11.846 14.203 1.00 54.01  ? 405 ALA   A CB  1 
ATOM   787  N  N   . LYS   A 1 110 ? -32.983 -11.786 16.234 1.00 57.29  ? 406 LYS   A N   1 
ATOM   788  C  CA  . LYS   A 1 110 ? -33.792 -10.999 17.156 1.00 56.72  ? 406 LYS   A CA  1 
ATOM   789  C  C   . LYS   A 1 110 ? -33.808 -11.626 18.537 1.00 58.63  ? 406 LYS   A C   1 
ATOM   790  O  O   . LYS   A 1 110 ? -33.819 -10.911 19.552 1.00 57.20  ? 406 LYS   A O   1 
ATOM   791  C  CB  . LYS   A 1 110 ? -35.218 -10.862 16.628 1.00 59.31  ? 406 LYS   A CB  1 
ATOM   792  C  CG  . LYS   A 1 110 ? -35.368 -9.776  15.591 1.00 61.00  ? 406 LYS   A CG  1 
ATOM   793  C  CD  . LYS   A 1 110 ? -36.783 -9.739  15.066 1.00 60.72  ? 406 LYS   A CD  1 
ATOM   794  C  CE  . LYS   A 1 110 ? -36.875 -8.934  13.799 1.00 63.06  ? 406 LYS   A CE  1 
ATOM   795  N  NZ  . LYS   A 1 110 ? -38.278 -8.469  13.649 1.00 67.58  ? 406 LYS   A NZ  1 
ATOM   796  N  N   . HIS   A 1 111 ? -33.788 -12.958 18.593 1.00 58.00  ? 407 HIS   A N   1 
ATOM   797  C  CA  . HIS   A 1 111 ? -33.841 -13.653 19.866 1.00 58.52  ? 407 HIS   A CA  1 
ATOM   798  C  C   . HIS   A 1 111 ? -32.481 -13.729 20.534 1.00 59.50  ? 407 HIS   A C   1 
ATOM   799  O  O   . HIS   A 1 111 ? -32.409 -13.776 21.771 1.00 57.12  ? 407 HIS   A O   1 
ATOM   800  C  CB  . HIS   A 1 111 ? -34.453 -15.027 19.657 1.00 58.41  ? 407 HIS   A CB  1 
ATOM   801  C  CG  . HIS   A 1 111 ? -35.942 -14.987 19.610 1.00 62.99  ? 407 HIS   A CG  1 
ATOM   802  N  ND1 . HIS   A 1 111 ? -36.632 -14.528 18.510 1.00 62.44  ? 407 HIS   A ND1 1 
ATOM   803  C  CD2 . HIS   A 1 111 ? -36.875 -15.270 20.552 1.00 63.30  ? 407 HIS   A CD2 1 
ATOM   804  C  CE1 . HIS   A 1 111 ? -37.929 -14.580 18.754 1.00 64.65  ? 407 HIS   A CE1 1 
ATOM   805  N  NE2 . HIS   A 1 111 ? -38.104 -15.030 19.985 1.00 66.88  ? 407 HIS   A NE2 1 
ATOM   806  N  N   . ALA   A 1 112 ? -31.401 -13.718 19.753 1.00 54.35  ? 408 ALA   A N   1 
ATOM   807  C  CA  . ALA   A 1 112 ? -30.086 -13.499 20.343 1.00 55.21  ? 408 ALA   A CA  1 
ATOM   808  C  C   . ALA   A 1 112 ? -30.052 -12.184 21.118 1.00 57.46  ? 408 ALA   A C   1 
ATOM   809  O  O   . ALA   A 1 112 ? -29.540 -12.124 22.244 1.00 56.33  ? 408 ALA   A O   1 
ATOM   810  C  CB  . ALA   A 1 112 ? -29.014 -13.508 19.261 1.00 54.93  ? 408 ALA   A CB  1 
ATOM   811  N  N   . TRP   A 1 113 ? -30.603 -11.114 20.530 1.00 55.31  ? 409 TRP   A N   1 
ATOM   812  C  CA  . TRP   A 1 113 ? -30.733 -9.854  21.262 1.00 53.89  ? 409 TRP   A CA  1 
ATOM   813  C  C   . TRP   A 1 113 ? -31.697 -10.001 22.434 1.00 56.67  ? 409 TRP   A C   1 
ATOM   814  O  O   . TRP   A 1 113 ? -31.381 -9.603  23.565 1.00 52.65  ? 409 TRP   A O   1 
ATOM   815  C  CB  . TRP   A 1 113 ? -31.204 -8.755  20.316 1.00 56.83  ? 409 TRP   A CB  1 
ATOM   816  C  CG  . TRP   A 1 113 ? -31.324 -7.377  20.930 1.00 56.34  ? 409 TRP   A CG  1 
ATOM   817  C  CD1 . TRP   A 1 113 ? -30.866 -6.962  22.143 1.00 59.39  ? 409 TRP   A CD1 1 
ATOM   818  C  CD2 . TRP   A 1 113 ? -31.925 -6.235  20.313 1.00 59.12  ? 409 TRP   A CD2 1 
ATOM   819  N  NE1 . TRP   A 1 113 ? -31.161 -5.622  22.331 1.00 58.42  ? 409 TRP   A NE1 1 
ATOM   820  C  CE2 . TRP   A 1 113 ? -31.815 -5.160  21.215 1.00 58.60  ? 409 TRP   A CE2 1 
ATOM   821  C  CE3 . TRP   A 1 113 ? -32.555 -6.023  19.081 1.00 56.95  ? 409 TRP   A CE3 1 
ATOM   822  C  CZ2 . TRP   A 1 113 ? -32.308 -3.888  20.922 1.00 59.30  ? 409 TRP   A CZ2 1 
ATOM   823  C  CZ3 . TRP   A 1 113 ? -33.046 -4.765  18.793 1.00 59.59  ? 409 TRP   A CZ3 1 
ATOM   824  C  CH2 . TRP   A 1 113 ? -32.926 -3.712  19.716 1.00 62.59  ? 409 TRP   A CH2 1 
ATOM   825  N  N   . ARG   A 1 114 ? -32.880 -10.567 22.179 1.00 55.90  ? 410 ARG   A N   1 
ATOM   826  C  CA  . ARG   A 1 114 ? -33.858 -10.788 23.239 1.00 56.72  ? 410 ARG   A CA  1 
ATOM   827  C  C   . ARG   A 1 114 ? -33.242 -11.487 24.447 1.00 57.48  ? 410 ARG   A C   1 
ATOM   828  O  O   . ARG   A 1 114 ? -33.563 -11.159 25.600 1.00 53.23  ? 410 ARG   A O   1 
ATOM   829  C  CB  . ARG   A 1 114 ? -35.022 -11.607 22.700 1.00 57.92  ? 410 ARG   A CB  1 
ATOM   830  C  CG  . ARG   A 1 114 ? -36.256 -11.574 23.541 1.00 61.39  ? 410 ARG   A CG  1 
ATOM   831  C  CD  . ARG   A 1 114 ? -37.320 -12.482 22.953 1.00 61.59  ? 410 ARG   A CD  1 
ATOM   832  N  NE  . ARG   A 1 114 ? -38.554 -12.414 23.729 1.00 63.30  ? 410 ARG   A NE  1 
ATOM   833  C  CZ  . ARG   A 1 114 ? -39.710 -12.921 23.332 1.00 65.68  ? 410 ARG   A CZ  1 
ATOM   834  N  NH1 . ARG   A 1 114 ? -39.821 -13.570 22.180 1.00 67.05  ? 410 ARG   A NH1 1 
ATOM   835  N  NH2 . ARG   A 1 114 ? -40.785 -12.761 24.098 1.00 65.50  ? 410 ARG   A NH2 1 
ATOM   836  N  N   . ASN   A 1 115 ? -32.329 -12.424 24.202 1.00 55.79  ? 411 ASN   A N   1 
ATOM   837  C  CA  . ASN   A 1 115 ? -31.756 -13.254 25.247 1.00 55.88  ? 411 ASN   A CA  1 
ATOM   838  C  C   . ASN   A 1 115 ? -30.510 -12.660 25.893 1.00 56.17  ? 411 ASN   A C   1 
ATOM   839  O  O   . ASN   A 1 115 ? -29.959 -13.262 26.824 1.00 54.42  ? 411 ASN   A O   1 
ATOM   840  C  CB  . ASN   A 1 115 ? -31.444 -14.630 24.664 1.00 56.15  ? 411 ASN   A CB  1 
ATOM   841  C  CG  . ASN   A 1 115 ? -32.698 -15.378 24.289 1.00 58.16  ? 411 ASN   A CG  1 
ATOM   842  O  OD1 . ASN   A 1 115 ? -33.779 -15.048 24.772 1.00 58.59  ? 411 ASN   A OD1 1 
ATOM   843  N  ND2 . ASN   A 1 115 ? -32.571 -16.383 23.423 1.00 59.02  ? 411 ASN   A ND2 1 
ATOM   844  N  N   . ALA   A 1 116 ? -30.057 -11.506 25.431 1.00 53.16  ? 412 ALA   A N   1 
ATOM   845  C  CA  . ALA   A 1 116 ? -28.824 -10.875 25.901 1.00 52.73  ? 412 ALA   A CA  1 
ATOM   846  C  C   . ALA   A 1 116 ? -29.075 -10.302 27.283 1.00 52.51  ? 412 ALA   A C   1 
ATOM   847  O  O   . ALA   A 1 116 ? -29.577 -9.192  27.437 1.00 51.79  ? 412 ALA   A O   1 
ATOM   848  C  CB  . ALA   A 1 116 ? -28.382 -9.787  24.927 1.00 53.71  ? 412 ALA   A CB  1 
ATOM   849  N  N   . SER   A 1 117 ? -28.721 -11.064 28.315 1.00 52.89  ? 413 SER   A N   1 
ATOM   850  C  CA  . SER   A 1 117 ? -29.101 -10.666 29.662 1.00 52.00  ? 413 SER   A CA  1 
ATOM   851  C  C   . SER   A 1 117 ? -28.403 -9.389  30.119 1.00 52.82  ? 413 SER   A C   1 
ATOM   852  O  O   . SER   A 1 117 ? -28.882 -8.742  31.061 1.00 51.68  ? 413 SER   A O   1 
ATOM   853  C  CB  . SER   A 1 117 ? -28.823 -11.811 30.637 1.00 52.49  ? 413 SER   A CB  1 
ATOM   854  O  OG  . SER   A 1 117 ? -27.464 -12.198 30.567 1.00 52.84  ? 413 SER   A OG  1 
ATOM   855  N  N   . ARG   A 1 118 ? -27.313 -8.989  29.458 1.00 51.91  ? 414 ARG   A N   1 
ATOM   856  C  CA  . ARG   A 1 118 ? -26.568 -7.811  29.883 1.00 51.66  ? 414 ARG   A CA  1 
ATOM   857  C  C   . ARG   A 1 118 ? -27.030 -6.532  29.207 1.00 54.20  ? 414 ARG   A C   1 
ATOM   858  O  O   . ARG   A 1 118 ? -26.496 -5.456  29.521 1.00 51.66  ? 414 ARG   A O   1 
ATOM   859  C  CB  . ARG   A 1 118 ? -25.078 -8.006  29.623 1.00 54.52  ? 414 ARG   A CB  1 
ATOM   860  C  CG  . ARG   A 1 118 ? -24.450 -9.102  30.456 1.00 56.19  ? 414 ARG   A CG  1 
ATOM   861  C  CD  . ARG   A 1 118 ? -22.961 -9.178  30.174 1.00 58.46  ? 414 ARG   A CD  1 
ATOM   862  N  NE  . ARG   A 1 118 ? -22.218 -9.760  31.288 1.00 57.87  ? 414 ARG   A NE  1 
ATOM   863  C  CZ  . ARG   A 1 118 ? -20.951 -10.141 31.203 1.00 65.09  ? 414 ARG   A CZ  1 
ATOM   864  N  NH1 . ARG   A 1 118 ? -20.273 -10.025 30.068 1.00 66.45  ? 414 ARG   A NH1 1 
ATOM   865  N  NH2 . ARG   A 1 118 ? -20.354 -10.661 32.272 1.00 65.43  ? 414 ARG   A NH2 1 
ATOM   866  N  N   . CYS   A 1 119 ? -28.030 -6.617  28.324 1.00 50.88  ? 415 CYS   A N   1 
ATOM   867  C  CA  . CYS   A 1 119 ? -28.479 -5.485  27.522 1.00 53.17  ? 415 CYS   A CA  1 
ATOM   868  C  C   . CYS   A 1 119 ? -29.725 -4.905  28.164 1.00 53.88  ? 415 CYS   A C   1 
ATOM   869  O  O   . CYS   A 1 119 ? -30.730 -5.604  28.311 1.00 52.62  ? 415 CYS   A O   1 
ATOM   870  C  CB  . CYS   A 1 119 ? -28.773 -5.887  26.065 1.00 52.60  ? 415 CYS   A CB  1 
ATOM   871  S  SG  . CYS   A 1 119 ? -29.582 -4.588  25.075 1.00 50.18  ? 415 CYS   A SG  1 
ATOM   872  N  N   . VAL   A 1 120 ? -29.674 -3.611  28.490 1.00 55.59  ? 416 VAL   A N   1 
ATOM   873  C  CA  . VAL   A 1 120 ? -30.811 -2.927  29.100 1.00 55.80  ? 416 VAL   A CA  1 
ATOM   874  C  C   . VAL   A 1 120 ? -31.785 -2.385  28.060 1.00 55.81  ? 416 VAL   A C   1 
ATOM   875  O  O   . VAL   A 1 120 ? -32.887 -1.938  28.418 1.00 55.28  ? 416 VAL   A O   1 
ATOM   876  C  CB  . VAL   A 1 120 ? -30.294 -1.791  30.015 1.00 54.95  ? 416 VAL   A CB  1 
ATOM   877  C  CG1 . VAL   A 1 120 ? -29.703 -0.629  29.159 1.00 55.80  ? 416 VAL   A CG1 1 
ATOM   878  C  CG2 . VAL   A 1 120 ? -31.391 -1.296  30.950 1.00 56.58  ? 416 VAL   A CG2 1 
ATOM   879  N  N   . GLY   A 1 121 ? -31.439 -2.450  26.781 1.00 57.01  ? 417 GLY   A N   1 
ATOM   880  C  CA  . GLY   A 1 121 ? -32.259 -1.845  25.750 1.00 58.08  ? 417 GLY   A CA  1 
ATOM   881  C  C   . GLY   A 1 121 ? -33.197 -2.804  25.054 1.00 60.97  ? 417 GLY   A C   1 
ATOM   882  O  O   . GLY   A 1 121 ? -33.755 -2.471  24.004 1.00 61.61  ? 417 GLY   A O   1 
ATOM   883  N  N   . ARG   A 1 122 ? -33.416 -3.981  25.636 1.00 57.01  ? 418 ARG   A N   1 
ATOM   884  C  CA  . ARG   A 1 122 ? -34.069 -5.065  24.908 1.00 62.51  ? 418 ARG   A CA  1 
ATOM   885  C  C   . ARG   A 1 122 ? -35.566 -4.876  24.718 1.00 65.45  ? 418 ARG   A C   1 
ATOM   886  O  O   . ARG   A 1 122 ? -36.195 -5.730  24.080 1.00 64.29  ? 418 ARG   A O   1 
ATOM   887  C  CB  . ARG   A 1 122 ? -33.839 -6.405  25.595 1.00 59.00  ? 418 ARG   A CB  1 
ATOM   888  C  CG  . ARG   A 1 122 ? -32.430 -6.902  25.501 1.00 56.53  ? 418 ARG   A CG  1 
ATOM   889  C  CD  . ARG   A 1 122 ? -32.327 -8.220  26.209 1.00 55.09  ? 418 ARG   A CD  1 
ATOM   890  N  NE  . ARG   A 1 122 ? -32.208 -8.043  27.655 1.00 56.12  ? 418 ARG   A NE  1 
ATOM   891  C  CZ  . ARG   A 1 122 ? -32.370 -9.016  28.540 1.00 54.22  ? 418 ARG   A CZ  1 
ATOM   892  N  NH1 . ARG   A 1 122 ? -32.779 -10.222 28.170 1.00 53.37  ? 418 ARG   A NH1 1 
ATOM   893  N  NH2 . ARG   A 1 122 ? -32.109 -8.773  29.833 1.00 54.66  ? 418 ARG   A NH2 1 
ATOM   894  N  N   . ILE   A 1 123 ? -36.163 -3.795  25.224 1.00 64.42  ? 419 ILE   A N   1 
ATOM   895  C  CA  . ILE   A 1 123 ? -37.574 -3.580  24.941 1.00 65.08  ? 419 ILE   A CA  1 
ATOM   896  C  C   . ILE   A 1 123 ? -37.809 -3.464  23.430 1.00 70.15  ? 419 ILE   A C   1 
ATOM   897  O  O   . ILE   A 1 123 ? -38.929 -3.680  22.957 1.00 65.93  ? 419 ILE   A O   1 
ATOM   898  C  CB  . ILE   A 1 123 ? -38.090 -2.337  25.686 1.00 70.04  ? 419 ILE   A CB  1 
ATOM   899  C  CG1 . ILE   A 1 123 ? -39.622 -2.302  25.654 1.00 70.39  ? 419 ILE   A CG1 1 
ATOM   900  C  CG2 . ILE   A 1 123 ? -37.473 -1.074  25.099 1.00 71.20  ? 419 ILE   A CG2 1 
ATOM   901  C  CD1 . ILE   A 1 123 ? -40.254 -1.331  26.623 1.00 75.88  ? 419 ILE   A CD1 1 
ATOM   902  N  N   . GLN   A 1 124 ? -36.759 -3.156  22.670 1.00 71.07  ? 420 GLN   A N   1 
ATOM   903  C  CA  . GLN   A 1 124 ? -36.794 -2.934  21.232 1.00 71.46  ? 420 GLN   A CA  1 
ATOM   904  C  C   . GLN   A 1 124 ? -36.473 -4.185  20.426 1.00 69.56  ? 420 GLN   A C   1 
ATOM   905  O  O   . GLN   A 1 124 ? -36.346 -4.093  19.201 1.00 67.02  ? 420 GLN   A O   1 
ATOM   906  C  CB  . GLN   A 1 124 ? -35.794 -1.832  20.863 1.00 74.38  ? 420 GLN   A CB  1 
ATOM   907  C  CG  . GLN   A 1 124 ? -36.221 -0.423  21.243 1.00 82.32  ? 420 GLN   A CG  1 
ATOM   908  C  CD  . GLN   A 1 124 ? -37.005 0.255   20.135 1.00 85.85  ? 420 GLN   A CD  1 
ATOM   909  O  OE1 . GLN   A 1 124 ? -37.333 -0.359  19.116 1.00 88.37  ? 420 GLN   A OE1 1 
ATOM   910  N  NE2 . GLN   A 1 124 ? -37.312 1.532   20.333 1.00 91.59  ? 420 GLN   A NE2 1 
ATOM   911  N  N   . TRP   A 1 125 ? -36.345 -5.344  21.079 1.00 64.31  ? 421 TRP   A N   1 
ATOM   912  C  CA  . TRP   A 1 125 ? -35.654 -6.473  20.461 1.00 62.96  ? 421 TRP   A CA  1 
ATOM   913  C  C   . TRP   A 1 125 ? -36.334 -6.941  19.179 1.00 62.52  ? 421 TRP   A C   1 
ATOM   914  O  O   . TRP   A 1 125 ? -35.661 -7.441  18.275 1.00 62.70  ? 421 TRP   A O   1 
ATOM   915  C  CB  . TRP   A 1 125 ? -35.542 -7.629  21.461 1.00 60.24  ? 421 TRP   A CB  1 
ATOM   916  C  CG  . TRP   A 1 125 ? -36.856 -8.260  21.708 1.00 62.92  ? 421 TRP   A CG  1 
ATOM   917  C  CD1 . TRP   A 1 125 ? -37.750 -7.933  22.679 1.00 62.93  ? 421 TRP   A CD1 1 
ATOM   918  C  CD2 . TRP   A 1 125 ? -37.461 -9.306  20.941 1.00 64.40  ? 421 TRP   A CD2 1 
ATOM   919  N  NE1 . TRP   A 1 125 ? -38.867 -8.720  22.581 1.00 62.16  ? 421 TRP   A NE1 1 
ATOM   920  C  CE2 . TRP   A 1 125 ? -38.716 -9.572  21.519 1.00 65.48  ? 421 TRP   A CE2 1 
ATOM   921  C  CE3 . TRP   A 1 125 ? -37.057 -10.053 19.833 1.00 59.56  ? 421 TRP   A CE3 1 
ATOM   922  C  CZ2 . TRP   A 1 125 ? -39.575 -10.550 21.019 1.00 61.61  ? 421 TRP   A CZ2 1 
ATOM   923  C  CZ3 . TRP   A 1 125 ? -37.907 -11.027 19.348 1.00 62.57  ? 421 TRP   A CZ3 1 
ATOM   924  C  CH2 . TRP   A 1 125 ? -39.148 -11.268 19.938 1.00 62.70  ? 421 TRP   A CH2 1 
ATOM   925  N  N   . SER   A 1 126 ? -37.658 -6.803  19.080 1.00 63.62  ? 422 SER   A N   1 
ATOM   926  C  CA  . SER   A 1 126 ? -38.363 -7.240  17.883 1.00 65.06  ? 422 SER   A CA  1 
ATOM   927  C  C   . SER   A 1 126 ? -38.231 -6.253  16.730 1.00 66.84  ? 422 SER   A C   1 
ATOM   928  O  O   . SER   A 1 126 ? -38.462 -6.630  15.574 1.00 68.58  ? 422 SER   A O   1 
ATOM   929  C  CB  . SER   A 1 126 ? -39.843 -7.470  18.195 1.00 65.39  ? 422 SER   A CB  1 
ATOM   930  O  OG  . SER   A 1 126 ? -40.534 -6.239  18.330 1.00 69.66  ? 422 SER   A OG  1 
ATOM   931  N  N   . LYS   A 1 127 ? -37.882 -4.996  17.009 1.00 68.16  ? 423 LYS   A N   1 
ATOM   932  C  CA  . LYS   A 1 127 ? -37.583 -4.034  15.948 1.00 68.55  ? 423 LYS   A CA  1 
ATOM   933  C  C   . LYS   A 1 127 ? -36.071 -4.060  15.723 1.00 66.04  ? 423 LYS   A C   1 
ATOM   934  O  O   . LYS   A 1 127 ? -35.301 -3.248  16.251 1.00 65.15  ? 423 LYS   A O   1 
ATOM   935  C  CB  . LYS   A 1 127 ? -38.094 -2.647  16.314 1.00 72.09  ? 423 LYS   A CB  1 
ATOM   936  C  CG  . LYS   A 1 127 ? -39.617 -2.538  16.368 1.00 76.23  ? 423 LYS   A CG  1 
ATOM   937  C  CD  . LYS   A 1 127 ? -40.113 -1.343  15.538 1.00 86.31  ? 423 LYS   A CD  1 
ATOM   938  C  CE  . LYS   A 1 127 ? -41.079 -1.765  14.430 1.00 88.09  ? 423 LYS   A CE  1 
ATOM   939  N  NZ  . LYS   A 1 127 ? -40.540 -1.522  13.043 1.00 92.48  ? 423 LYS   A NZ  1 
ATOM   940  N  N   . LEU   A 1 128 ? -35.635 -5.047  14.947 1.00 64.23  ? 424 LEU   A N   1 
ATOM   941  C  CA  . LEU   A 1 128 ? -34.233 -5.198  14.583 1.00 62.96  ? 424 LEU   A CA  1 
ATOM   942  C  C   . LEU   A 1 128 ? -34.168 -5.415  13.078 1.00 61.28  ? 424 LEU   A C   1 
ATOM   943  O  O   . LEU   A 1 128 ? -34.911 -6.238  12.536 1.00 61.81  ? 424 LEU   A O   1 
ATOM   944  C  CB  . LEU   A 1 128 ? -33.576 -6.366  15.330 1.00 59.04  ? 424 LEU   A CB  1 
ATOM   945  C  CG  . LEU   A 1 128 ? -32.110 -6.694  15.022 1.00 57.33  ? 424 LEU   A CG  1 
ATOM   946  C  CD1 . LEU   A 1 128 ? -31.182 -5.579  15.446 1.00 58.72  ? 424 LEU   A CD1 1 
ATOM   947  C  CD2 . LEU   A 1 128 ? -31.663 -8.010  15.650 1.00 54.53  ? 424 LEU   A CD2 1 
ATOM   948  N  N   . GLN   A 1 129 ? -33.310 -4.672  12.400 1.00 58.50  ? 425 GLN   A N   1 
ATOM   949  C  CA  . GLN   A 1 129 ? -33.165 -4.817  10.956 1.00 59.99  ? 425 GLN   A CA  1 
ATOM   950  C  C   . GLN   A 1 129 ? -32.010 -5.771  10.691 1.00 59.28  ? 425 GLN   A C   1 
ATOM   951  O  O   . GLN   A 1 129 ? -30.869 -5.495  11.077 1.00 56.56  ? 425 GLN   A O   1 
ATOM   952  C  CB  . GLN   A 1 129 ? -32.928 -3.472  10.274 1.00 63.39  ? 425 GLN   A CB  1 
ATOM   953  C  CG  . GLN   A 1 129 ? -32.796 -3.594  8.772  1.00 61.02  ? 425 GLN   A CG  1 
ATOM   954  C  CD  . GLN   A 1 129 ? -34.035 -4.202  8.130  1.00 66.13  ? 425 GLN   A CD  1 
ATOM   955  O  OE1 . GLN   A 1 129 ? -35.168 -3.925  8.544  1.00 69.69  ? 425 GLN   A OE1 1 
ATOM   956  N  NE2 . GLN   A 1 129 ? -33.823 -5.038  7.114  1.00 67.43  ? 425 GLN   A NE2 1 
ATOM   957  N  N   . VAL   A 1 130 ? -32.305 -6.907  10.075 1.00 58.86  ? 426 VAL   A N   1 
ATOM   958  C  CA  . VAL   A 1 130 ? -31.309 -7.943  9.859  1.00 58.21  ? 426 VAL   A CA  1 
ATOM   959  C  C   . VAL   A 1 130 ? -30.841 -7.823  8.421  1.00 58.65  ? 426 VAL   A C   1 
ATOM   960  O  O   . VAL   A 1 130 ? -31.649 -7.895  7.490  1.00 56.94  ? 426 VAL   A O   1 
ATOM   961  C  CB  . VAL   A 1 130 ? -31.875 -9.341  10.150 1.00 59.16  ? 426 VAL   A CB  1 
ATOM   962  C  CG1 . VAL   A 1 130 ? -30.772 -10.398 10.018 1.00 57.71  ? 426 VAL   A CG1 1 
ATOM   963  C  CG2 . VAL   A 1 130 ? -32.483 -9.378  11.551 1.00 56.99  ? 426 VAL   A CG2 1 
ATOM   964  N  N   . PHE   A 1 131 ? -29.548 -7.597  8.240  1.00 58.41  ? 427 PHE   A N   1 
ATOM   965  C  CA  . PHE   A 1 131 ? -28.950 -7.538  6.917  1.00 58.75  ? 427 PHE   A CA  1 
ATOM   966  C  C   . PHE   A 1 131 ? -28.224 -8.847  6.689  1.00 56.73  ? 427 PHE   A C   1 
ATOM   967  O  O   . PHE   A 1 131 ? -27.296 -9.188  7.430  1.00 55.60  ? 427 PHE   A O   1 
ATOM   968  C  CB  . PHE   A 1 131 ? -27.996 -6.355  6.789  1.00 57.35  ? 427 PHE   A CB  1 
ATOM   969  C  CG  . PHE   A 1 131 ? -28.687 -5.038  6.776  1.00 58.30  ? 427 PHE   A CG  1 
ATOM   970  C  CD1 . PHE   A 1 131 ? -29.506 -4.684  5.713  1.00 59.70  ? 427 PHE   A CD1 1 
ATOM   971  C  CD2 . PHE   A 1 131 ? -28.528 -4.155  7.822  1.00 56.03  ? 427 PHE   A CD2 1 
ATOM   972  C  CE1 . PHE   A 1 131 ? -30.153 -3.463  5.706  1.00 61.04  ? 427 PHE   A CE1 1 
ATOM   973  C  CE2 . PHE   A 1 131 ? -29.168 -2.944  7.816  1.00 58.43  ? 427 PHE   A CE2 1 
ATOM   974  C  CZ  . PHE   A 1 131 ? -29.979 -2.592  6.761  1.00 60.25  ? 427 PHE   A CZ  1 
ATOM   975  N  N   . ASP   A 1 132 ? -28.678 -9.592  5.695  1.00 57.94  ? 428 ASP   A N   1 
ATOM   976  C  CA  . ASP   A 1 132 ? -28.128 -10.903 5.392  1.00 56.84  ? 428 ASP   A CA  1 
ATOM   977  C  C   . ASP   A 1 132 ? -26.929 -10.667 4.492  1.00 57.64  ? 428 ASP   A C   1 
ATOM   978  O  O   . ASP   A 1 132 ? -27.082 -10.340 3.320  1.00 60.33  ? 428 ASP   A O   1 
ATOM   979  C  CB  . ASP   A 1 132 ? -29.189 -11.780 4.738  1.00 55.23  ? 428 ASP   A CB  1 
ATOM   980  C  CG  . ASP   A 1 132 ? -28.687 -13.174 4.443  1.00 59.96  ? 428 ASP   A CG  1 
ATOM   981  O  OD1 . ASP   A 1 132 ? -27.479 -13.427 4.623  1.00 59.79  ? 428 ASP   A OD1 1 
ATOM   982  O  OD2 . ASP   A 1 132 ? -29.492 -14.024 4.002  1.00 66.15  ? 428 ASP   A OD2 1 
ATOM   983  N  N   . ALA   A 1 133 ? -25.729 -10.809 5.039  1.00 57.96  ? 429 ALA   A N   1 
ATOM   984  C  CA  . ALA   A 1 133 ? -24.487 -10.700 4.281  1.00 55.49  ? 429 ALA   A CA  1 
ATOM   985  C  C   . ALA   A 1 133 ? -23.831 -12.065 4.128  1.00 57.53  ? 429 ALA   A C   1 
ATOM   986  O  O   . ALA   A 1 133 ? -22.609 -12.176 4.000  1.00 57.56  ? 429 ALA   A O   1 
ATOM   987  C  CB  . ALA   A 1 133 ? -23.523 -9.711  4.945  1.00 58.49  ? 429 ALA   A CB  1 
ATOM   988  N  N   . ARG   A 1 134 ? -24.637 -13.121 4.133  1.00 55.96  ? 430 ARG   A N   1 
ATOM   989  C  CA  . ARG   A 1 134 ? -24.057 -14.444 3.984  1.00 59.01  ? 430 ARG   A CA  1 
ATOM   990  C  C   . ARG   A 1 134 ? -23.563 -14.726 2.564  1.00 60.02  ? 430 ARG   A C   1 
ATOM   991  O  O   . ARG   A 1 134 ? -22.882 -15.736 2.376  1.00 61.77  ? 430 ARG   A O   1 
ATOM   992  C  CB  . ARG   A 1 134 ? -25.061 -15.506 4.425  1.00 59.50  ? 430 ARG   A CB  1 
ATOM   993  C  CG  . ARG   A 1 134 ? -25.275 -15.536 5.949  1.00 59.95  ? 430 ARG   A CG  1 
ATOM   994  C  CD  . ARG   A 1 134 ? -26.345 -16.533 6.351  1.00 60.80  ? 430 ARG   A CD  1 
ATOM   995  N  NE  . ARG   A 1 134 ? -27.625 -16.190 5.749  1.00 63.58  ? 430 ARG   A NE  1 
ATOM   996  C  CZ  . ARG   A 1 134 ? -28.689 -16.978 5.740  1.00 64.91  ? 430 ARG   A CZ  1 
ATOM   997  N  NH1 . ARG   A 1 134 ? -28.670 -18.170 6.320  1.00 65.56  ? 430 ARG   A NH1 1 
ATOM   998  N  NH2 . ARG   A 1 134 ? -29.800 -16.559 5.131  1.00 64.20  ? 430 ARG   A NH2 1 
ATOM   999  N  N   . ASP   A 1 135 ? -23.840 -13.862 1.573  1.00 59.15  ? 431 ASP   A N   1 
ATOM   1000 C  CA  . ASP   A 1 135 ? -23.243 -14.040 0.249  1.00 61.80  ? 431 ASP   A CA  1 
ATOM   1001 C  C   . ASP   A 1 135 ? -21.891 -13.356 0.138  1.00 64.78  ? 431 ASP   A C   1 
ATOM   1002 O  O   . ASP   A 1 135 ? -21.285 -13.380 -0.938 1.00 64.77  ? 431 ASP   A O   1 
ATOM   1003 C  CB  . ASP   A 1 135 ? -24.169 -13.522 -0.887 1.00 62.20  ? 431 ASP   A CB  1 
ATOM   1004 C  CG  . ASP   A 1 135 ? -24.552 -12.044 -0.722 1.00 64.11  ? 431 ASP   A CG  1 
ATOM   1005 O  OD1 . ASP   A 1 135 ? -23.922 -11.322 0.084  1.00 63.16  ? 431 ASP   A OD1 1 
ATOM   1006 O  OD2 . ASP   A 1 135 ? -25.519 -11.609 -1.379 1.00 66.46  ? 431 ASP   A OD2 1 
ATOM   1007 N  N   . CYS   A 1 136 ? -21.422 -12.733 1.212  1.00 60.34  ? 432 CYS   A N   1 
ATOM   1008 C  CA  . CYS   A 1 136 ? -20.171 -12.000 1.170  1.00 63.73  ? 432 CYS   A CA  1 
ATOM   1009 C  C   . CYS   A 1 136 ? -18.995 -12.960 1.024  1.00 66.82  ? 432 CYS   A C   1 
ATOM   1010 O  O   . CYS   A 1 136 ? -19.018 -14.090 1.519  1.00 65.52  ? 432 CYS   A O   1 
ATOM   1011 C  CB  . CYS   A 1 136 ? -20.025 -11.141 2.423  1.00 61.73  ? 432 CYS   A CB  1 
ATOM   1012 S  SG  . CYS   A 1 136 ? -18.715 -9.910  2.289  1.00 61.25  ? 432 CYS   A SG  1 
ATOM   1013 N  N   . THR   A 1 137 ? -17.972 -12.518 0.287  1.00 70.57  ? 433 THR   A N   1 
ATOM   1014 C  CA  . THR   A 1 137 ? -16.810 -13.356 0.013  1.00 67.38  ? 433 THR   A CA  1 
ATOM   1015 C  C   . THR   A 1 137 ? -15.470 -12.673 0.239  1.00 69.77  ? 433 THR   A C   1 
ATOM   1016 O  O   . THR   A 1 137 ? -14.462 -13.374 0.374  1.00 71.77  ? 433 THR   A O   1 
ATOM   1017 C  CB  . THR   A 1 137 ? -16.841 -13.865 -1.438 1.00 73.25  ? 433 THR   A CB  1 
ATOM   1018 O  OG1 . THR   A 1 137 ? -16.796 -12.736 -2.314 1.00 70.93  ? 433 THR   A OG1 1 
ATOM   1019 C  CG2 . THR   A 1 137 ? -18.106 -14.674 -1.709 1.00 71.19  ? 433 THR   A CG2 1 
ATOM   1020 N  N   . THR   A 1 138 ? -15.411 -11.346 0.258  1.00 69.92  ? 434 THR   A N   1 
ATOM   1021 C  CA  . THR   A 1 138 ? -14.158 -10.609 0.357  1.00 71.71  ? 434 THR   A CA  1 
ATOM   1022 C  C   . THR   A 1 138 ? -14.286 -9.538  1.424  1.00 71.60  ? 434 THR   A C   1 
ATOM   1023 O  O   . THR   A 1 138 ? -15.389 -9.205  1.874  1.00 68.32  ? 434 THR   A O   1 
ATOM   1024 C  CB  . THR   A 1 138 ? -13.772 -9.947  -0.976 1.00 73.59  ? 434 THR   A CB  1 
ATOM   1025 O  OG1 . THR   A 1 138 ? -14.820 -9.061  -1.378 1.00 75.43  ? 434 THR   A OG1 1 
ATOM   1026 C  CG2 . THR   A 1 138 ? -13.536 -10.989 -2.048 1.00 76.14  ? 434 THR   A CG2 1 
ATOM   1027 N  N   . ALA   A 1 139 ? -13.135 -9.001  1.839  1.00 71.03  ? 435 ALA   A N   1 
ATOM   1028 C  CA  . ALA   A 1 139 ? -13.155 -7.926  2.824  1.00 69.39  ? 435 ALA   A CA  1 
ATOM   1029 C  C   . ALA   A 1 139 ? -13.773 -6.668  2.235  1.00 69.32  ? 435 ALA   A C   1 
ATOM   1030 O  O   . ALA   A 1 139 ? -14.500 -5.944  2.925  1.00 67.81  ? 435 ALA   A O   1 
ATOM   1031 C  CB  . ALA   A 1 139 ? -11.744 -7.642  3.333  1.00 76.11  ? 435 ALA   A CB  1 
ATOM   1032 N  N   . HIS   A 1 140 ? -13.496 -6.398  0.957  1.00 71.84  ? 436 HIS   A N   1 
ATOM   1033 C  CA  . HIS   A 1 140 ? -14.174 -5.316  0.251  1.00 73.00  ? 436 HIS   A CA  1 
ATOM   1034 C  C   . HIS   A 1 140 ? -15.684 -5.477  0.311  1.00 68.84  ? 436 HIS   A C   1 
ATOM   1035 O  O   . HIS   A 1 140 ? -16.412 -4.498  0.491  1.00 70.09  ? 436 HIS   A O   1 
ATOM   1036 C  CB  . HIS   A 1 140 ? -13.704 -5.262  -1.207 1.00 79.25  ? 436 HIS   A CB  1 
ATOM   1037 C  CG  . HIS   A 1 140 ? -12.441 -4.486  -1.403 1.00 82.34  ? 436 HIS   A CG  1 
ATOM   1038 N  ND1 . HIS   A 1 140 ? -11.210 -4.947  -0.988 1.00 83.82  ? 436 HIS   A ND1 1 
ATOM   1039 C  CD2 . HIS   A 1 140 ? -12.223 -3.266  -1.950 1.00 81.79  ? 436 HIS   A CD2 1 
ATOM   1040 C  CE1 . HIS   A 1 140 ? -10.284 -4.053  -1.290 1.00 85.92  ? 436 HIS   A CE1 1 
ATOM   1041 N  NE2 . HIS   A 1 140 ? -10.872 -3.025  -1.876 1.00 84.51  ? 436 HIS   A NE2 1 
ATOM   1042 N  N   . GLY   A 1 141 ? -16.180 -6.699  0.136  1.00 65.51  ? 437 GLY   A N   1 
ATOM   1043 C  CA  . GLY   A 1 141 ? -17.605 -6.923  0.297  1.00 66.77  ? 437 GLY   A CA  1 
ATOM   1044 C  C   . GLY   A 1 141 ? -18.082 -6.621  1.704  1.00 64.92  ? 437 GLY   A C   1 
ATOM   1045 O  O   . GLY   A 1 141 ? -19.133 -6.002  1.892  1.00 64.97  ? 437 GLY   A O   1 
ATOM   1046 N  N   . MET   A 1 142 ? -17.318 -7.062  2.715  1.00 67.37  ? 438 MET   A N   1 
ATOM   1047 C  CA  . MET   A 1 142 ? -17.658 -6.742  4.099  1.00 63.40  ? 438 MET   A CA  1 
ATOM   1048 C  C   . MET   A 1 142 ? -17.716 -5.234  4.307  1.00 64.01  ? 438 MET   A C   1 
ATOM   1049 O  O   . MET   A 1 142 ? -18.692 -4.707  4.851  1.00 61.85  ? 438 MET   A O   1 
ATOM   1050 C  CB  . MET   A 1 142 ? -16.640 -7.372  5.056  1.00 63.65  ? 438 MET   A CB  1 
ATOM   1051 C  CG  . MET   A 1 142 ? -16.493 -8.872  4.944  1.00 64.87  ? 438 MET   A CG  1 
ATOM   1052 S  SD  . MET   A 1 142 ? -15.227 -9.496  6.079  1.00 66.26  ? 438 MET   A SD  1 
ATOM   1053 C  CE  . MET   A 1 142 ? -15.950 -9.108  7.668  1.00 66.44  ? 438 MET   A CE  1 
ATOM   1054 N  N   . PHE   A 1 143 ? -16.676 -4.524  3.867  1.00 62.28  ? 439 PHE   A N   1 
ATOM   1055 C  CA  . PHE   A 1 143 ? -16.659 -3.070  3.969  1.00 63.31  ? 439 PHE   A CA  1 
ATOM   1056 C  C   . PHE   A 1 143 ? -17.926 -2.461  3.389  1.00 64.62  ? 439 PHE   A C   1 
ATOM   1057 O  O   . PHE   A 1 143 ? -18.559 -1.606  4.012  1.00 63.20  ? 439 PHE   A O   1 
ATOM   1058 C  CB  . PHE   A 1 143 ? -15.413 -2.522  3.272  1.00 68.91  ? 439 PHE   A CB  1 
ATOM   1059 C  CG  . PHE   A 1 143 ? -15.406 -1.028  3.131  1.00 71.46  ? 439 PHE   A CG  1 
ATOM   1060 C  CD1 . PHE   A 1 143 ? -15.372 -0.217  4.259  1.00 71.88  ? 439 PHE   A CD1 1 
ATOM   1061 C  CD2 . PHE   A 1 143 ? -15.434 -0.433  1.870  1.00 71.94  ? 439 PHE   A CD2 1 
ATOM   1062 C  CE1 . PHE   A 1 143 ? -15.361 1.145   4.145  1.00 76.07  ? 439 PHE   A CE1 1 
ATOM   1063 C  CE2 . PHE   A 1 143 ? -15.428 0.946   1.745  1.00 74.05  ? 439 PHE   A CE2 1 
ATOM   1064 C  CZ  . PHE   A 1 143 ? -15.395 1.740   2.897  1.00 76.11  ? 439 PHE   A CZ  1 
ATOM   1065 N  N   . ASN   A 1 144 ? -18.313 -2.897  2.188  1.00 63.63  ? 440 ASN   A N   1 
ATOM   1066 C  CA  . ASN   A 1 144 ? -19.526 -2.386  1.569  1.00 60.69  ? 440 ASN   A CA  1 
ATOM   1067 C  C   . ASN   A 1 144 ? -20.756 -2.695  2.410  1.00 60.56  ? 440 ASN   A C   1 
ATOM   1068 O  O   . ASN   A 1 144 ? -21.639 -1.849  2.579  1.00 61.60  ? 440 ASN   A O   1 
ATOM   1069 C  CB  . ASN   A 1 144 ? -19.693 -2.987  0.178  1.00 66.23  ? 440 ASN   A CB  1 
ATOM   1070 C  CG  . ASN   A 1 144 ? -20.714 -2.242  -0.626 1.00 65.01  ? 440 ASN   A CG  1 
ATOM   1071 O  OD1 . ASN   A 1 144 ? -20.544 -1.058  -0.884 1.00 65.02  ? 440 ASN   A OD1 1 
ATOM   1072 N  ND2 . ASN   A 1 144 ? -21.800 -2.908  -0.986 1.00 64.95  ? 440 ASN   A ND2 1 
ATOM   1073 N  N   . TYR   A 1 145 ? -20.856 -3.927  2.899  1.00 61.78  ? 441 TYR   A N   1 
ATOM   1074 C  CA  . TYR   A 1 145 ? -21.985 -4.294  3.749  1.00 62.88  ? 441 TYR   A CA  1 
ATOM   1075 C  C   . TYR   A 1 145 ? -22.007 -3.479  5.036  1.00 58.93  ? 441 TYR   A C   1 
ATOM   1076 O  O   . TYR   A 1 145 ? -23.079 -3.088  5.517  1.00 58.28  ? 441 TYR   A O   1 
ATOM   1077 C  CB  . TYR   A 1 145 ? -21.923 -5.779  4.077  1.00 62.11  ? 441 TYR   A CB  1 
ATOM   1078 C  CG  . TYR   A 1 145 ? -22.746 -6.654  3.161  1.00 57.72  ? 441 TYR   A CG  1 
ATOM   1079 C  CD1 . TYR   A 1 145 ? -24.122 -6.545  3.139  1.00 58.03  ? 441 TYR   A CD1 1 
ATOM   1080 C  CD2 . TYR   A 1 145 ? -22.153 -7.613  2.377  1.00 57.24  ? 441 TYR   A CD2 1 
ATOM   1081 C  CE1 . TYR   A 1 145 ? -24.883 -7.340  2.352  1.00 58.44  ? 441 TYR   A CE1 1 
ATOM   1082 C  CE2 . TYR   A 1 145 ? -22.906 -8.433  1.563  1.00 60.28  ? 441 TYR   A CE2 1 
ATOM   1083 C  CZ  . TYR   A 1 145 ? -24.277 -8.283  1.559  1.00 61.56  ? 441 TYR   A CZ  1 
ATOM   1084 O  OH  . TYR   A 1 145 ? -25.066 -9.071  0.780  1.00 63.25  ? 441 TYR   A OH  1 
ATOM   1085 N  N   . ILE   A 1 146 ? -20.834 -3.229  5.616  1.00 60.31  ? 442 ILE   A N   1 
ATOM   1086 C  CA  . ILE   A 1 146 ? -20.771 -2.465  6.864  1.00 59.71  ? 442 ILE   A CA  1 
ATOM   1087 C  C   . ILE   A 1 146 ? -21.127 -1.005  6.596  1.00 60.56  ? 442 ILE   A C   1 
ATOM   1088 O  O   . ILE   A 1 146 ? -21.861 -0.383  7.370  1.00 60.61  ? 442 ILE   A O   1 
ATOM   1089 C  CB  . ILE   A 1 146 ? -19.382 -2.619  7.509  1.00 58.97  ? 442 ILE   A CB  1 
ATOM   1090 C  CG1 . ILE   A 1 146 ? -19.194 -4.049  8.012  1.00 56.48  ? 442 ILE   A CG1 1 
ATOM   1091 C  CG2 . ILE   A 1 146 ? -19.183 -1.618  8.645  1.00 59.98  ? 442 ILE   A CG2 1 
ATOM   1092 C  CD1 . ILE   A 1 146 ? -17.796 -4.353  8.464  1.00 58.72  ? 442 ILE   A CD1 1 
ATOM   1093 N  N   . CYS   A 1 147 ? -20.680 -0.452  5.458  1.00 62.04  ? 443 CYS   A N   1 
ATOM   1094 C  CA  . CYS   A 1 147 ? -21.035 0.933   5.167  1.00 57.94  ? 443 CYS   A CA  1 
ATOM   1095 C  C   . CYS   A 1 147 ? -22.540 1.089   5.056  1.00 58.43  ? 443 CYS   A C   1 
ATOM   1096 O  O   . CYS   A 1 147 ? -23.109 2.065   5.560  1.00 61.62  ? 443 CYS   A O   1 
ATOM   1097 C  CB  . CYS   A 1 147 ? -20.365 1.426   3.891  1.00 64.05  ? 443 CYS   A CB  1 
ATOM   1098 S  SG  . CYS   A 1 147 ? -18.644 1.821   4.051  1.00 72.64  ? 443 CYS   A SG  1 
ATOM   1099 N  N   . ASN   A 1 148 ? -23.206 0.132   4.407  1.00 59.67  ? 444 ASN   A N   1 
ATOM   1100 C  CA  . ASN   A 1 148 ? -24.653 0.227   4.271  1.00 57.32  ? 444 ASN   A CA  1 
ATOM   1101 C  C   . ASN   A 1 148 ? -25.333 0.037   5.620  1.00 58.20  ? 444 ASN   A C   1 
ATOM   1102 O  O   . ASN   A 1 148 ? -26.362 0.662   5.891  1.00 57.34  ? 444 ASN   A O   1 
ATOM   1103 C  CB  . ASN   A 1 148 ? -25.154 -0.797  3.258  1.00 61.32  ? 444 ASN   A CB  1 
ATOM   1104 C  CG  . ASN   A 1 148 ? -24.714 -0.475  1.826  1.00 63.31  ? 444 ASN   A CG  1 
ATOM   1105 O  OD1 . ASN   A 1 148 ? -24.319 0.654   1.516  1.00 64.70  ? 444 ASN   A OD1 1 
ATOM   1106 N  ND2 . ASN   A 1 148 ? -24.804 -1.464  0.945  1.00 66.27  ? 444 ASN   A ND2 1 
ATOM   1107 N  N   . HIS   A 1 149 ? -24.763 -0.816  6.466  1.00 54.23  ? 445 HIS   A N   1 
ATOM   1108 C  CA  . HIS   A 1 149 ? -25.239 -0.951  7.842  1.00 57.23  ? 445 HIS   A CA  1 
ATOM   1109 C  C   . HIS   A 1 149 ? -25.147 0.375   8.588  1.00 55.82  ? 445 HIS   A C   1 
ATOM   1110 O  O   . HIS   A 1 149 ? -26.146 0.870   9.120  1.00 59.26  ? 445 HIS   A O   1 
ATOM   1111 C  CB  . HIS   A 1 149 ? -24.426 -2.032  8.540  1.00 53.90  ? 445 HIS   A CB  1 
ATOM   1112 C  CG  . HIS   A 1 149 ? -24.804 -2.256  9.974  1.00 55.37  ? 445 HIS   A CG  1 
ATOM   1113 N  ND1 . HIS   A 1 149 ? -25.024 -3.512  10.493 1.00 53.38  ? 445 HIS   A ND1 1 
ATOM   1114 C  CD2 . HIS   A 1 149 ? -24.982 -1.387  11.001 1.00 54.69  ? 445 HIS   A CD2 1 
ATOM   1115 C  CE1 . HIS   A 1 149 ? -25.325 -3.410  11.780 1.00 53.76  ? 445 HIS   A CE1 1 
ATOM   1116 N  NE2 . HIS   A 1 149 ? -25.301 -2.133  12.114 1.00 54.10  ? 445 HIS   A NE2 1 
ATOM   1117 N  N   . VAL   A 1 150 ? -23.949 0.967   8.632  1.00 56.46  ? 446 VAL   A N   1 
ATOM   1118 C  CA  . VAL   A 1 150 ? -23.762 2.263   9.284  1.00 59.00  ? 446 VAL   A CA  1 
ATOM   1119 C  C   . VAL   A 1 150 ? -24.767 3.277   8.759  1.00 61.55  ? 446 VAL   A C   1 
ATOM   1120 O  O   . VAL   A 1 150 ? -25.482 3.917   9.532  1.00 63.52  ? 446 VAL   A O   1 
ATOM   1121 C  CB  . VAL   A 1 150 ? -22.315 2.761   9.098  1.00 61.08  ? 446 VAL   A CB  1 
ATOM   1122 C  CG1 . VAL   A 1 150 ? -22.150 4.183   9.652  1.00 60.36  ? 446 VAL   A CG1 1 
ATOM   1123 C  CG2 . VAL   A 1 150 ? -21.322 1.800   9.734  1.00 58.01  ? 446 VAL   A CG2 1 
ATOM   1124 N  N   . LYS   A 1 151 ? -24.844 3.438   7.435  1.00 60.37  ? 447 LYS   A N   1 
ATOM   1125 C  CA  . LYS   A 1 151 ? -25.735 4.456   6.885  1.00 63.62  ? 447 LYS   A CA  1 
ATOM   1126 C  C   . LYS   A 1 151 ? -27.182 4.184   7.278  1.00 63.61  ? 447 LYS   A C   1 
ATOM   1127 O  O   . LYS   A 1 151 ? -27.898 5.095   7.717  1.00 65.50  ? 447 LYS   A O   1 
ATOM   1128 C  CB  . LYS   A 1 151 ? -25.591 4.534   5.361  1.00 61.13  ? 447 LYS   A CB  1 
ATOM   1129 C  CG  . LYS   A 1 151 ? -26.164 5.818   4.777  1.00 64.51  ? 447 LYS   A CG  1 
ATOM   1130 C  CD  . LYS   A 1 151 ? -25.883 5.865   3.307  1.00 64.26  ? 447 LYS   A CD  1 
ATOM   1131 C  CE  . LYS   A 1 151 ? -26.031 7.260   2.708  1.00 64.76  ? 447 LYS   A CE  1 
ATOM   1132 N  NZ  . LYS   A 1 151 ? -25.695 7.243   1.255  1.00 68.96  ? 447 LYS   A NZ  1 
ATOM   1133 N  N   . TYR   A 1 152 ? -27.630 2.930   7.135  1.00 59.70  ? 448 TYR   A N   1 
ATOM   1134 C  CA  . TYR   A 1 152 ? -29.004 2.606   7.499  1.00 61.95  ? 448 TYR   A CA  1 
ATOM   1135 C  C   . TYR   A 1 152 ? -29.242 2.869   8.981  1.00 64.26  ? 448 TYR   A C   1 
ATOM   1136 O  O   . TYR   A 1 152 ? -30.182 3.583   9.350  1.00 65.69  ? 448 TYR   A O   1 
ATOM   1137 C  CB  . TYR   A 1 152 ? -29.329 1.149   7.156  1.00 61.90  ? 448 TYR   A CB  1 
ATOM   1138 C  CG  . TYR   A 1 152 ? -30.689 0.728   7.685  1.00 63.72  ? 448 TYR   A CG  1 
ATOM   1139 C  CD1 . TYR   A 1 152 ? -31.844 0.907   6.930  1.00 65.83  ? 448 TYR   A CD1 1 
ATOM   1140 C  CD2 . TYR   A 1 152 ? -30.818 0.179   8.951  1.00 62.93  ? 448 TYR   A CD2 1 
ATOM   1141 C  CE1 . TYR   A 1 152 ? -33.090 0.544   7.426  1.00 64.45  ? 448 TYR   A CE1 1 
ATOM   1142 C  CE2 . TYR   A 1 152 ? -32.049 -0.186  9.451  1.00 62.83  ? 448 TYR   A CE2 1 
ATOM   1143 C  CZ  . TYR   A 1 152 ? -33.176 -0.002  8.691  1.00 68.31  ? 448 TYR   A CZ  1 
ATOM   1144 O  OH  . TYR   A 1 152 ? -34.393 -0.373  9.208  1.00 72.11  ? 448 TYR   A OH  1 
ATOM   1145 N  N   . ALA   A 1 153 ? -28.379 2.316   9.844  1.00 59.98  ? 449 ALA   A N   1 
ATOM   1146 C  CA  . ALA   A 1 153 ? -28.583 2.420   11.285 1.00 61.89  ? 449 ALA   A CA  1 
ATOM   1147 C  C   . ALA   A 1 153 ? -28.516 3.864   11.773 1.00 66.92  ? 449 ALA   A C   1 
ATOM   1148 O  O   . ALA   A 1 153 ? -29.185 4.223   12.753 1.00 69.42  ? 449 ALA   A O   1 
ATOM   1149 C  CB  . ALA   A 1 153 ? -27.548 1.567   12.023 1.00 57.49  ? 449 ALA   A CB  1 
ATOM   1150 N  N   . THR   A 1 154 ? -27.701 4.699   11.132 1.00 61.69  ? 450 THR   A N   1 
ATOM   1151 C  CA  . THR   A 1 154 ? -27.595 6.088   11.563 1.00 67.14  ? 450 THR   A CA  1 
ATOM   1152 C  C   . THR   A 1 154 ? -28.840 6.878   11.177 1.00 72.54  ? 450 THR   A C   1 
ATOM   1153 O  O   . THR   A 1 154 ? -29.413 7.599   11.999 1.00 72.13  ? 450 THR   A O   1 
ATOM   1154 C  CB  . THR   A 1 154 ? -26.340 6.717   10.965 1.00 66.37  ? 450 THR   A CB  1 
ATOM   1155 O  OG1 . THR   A 1 154 ? -25.184 6.024   11.447 1.00 66.57  ? 450 THR   A OG1 1 
ATOM   1156 C  CG2 . THR   A 1 154 ? -26.253 8.179   11.323 1.00 69.37  ? 450 THR   A CG2 1 
ATOM   1157 N  N   . ASN   A 1 155 ? -29.263 6.776   9.923  1.00 70.29  ? 451 ASN   A N   1 
ATOM   1158 C  CA  . ASN   A 1 155 ? -30.550 7.316   9.495  1.00 72.14  ? 451 ASN   A CA  1 
ATOM   1159 C  C   . ASN   A 1 155 ? -30.713 8.778   9.917  1.00 75.96  ? 451 ASN   A C   1 
ATOM   1160 O  O   . ASN   A 1 155 ? -31.713 9.172   10.514 1.00 81.17  ? 451 ASN   A O   1 
ATOM   1161 C  CB  . ASN   A 1 155 ? -31.693 6.461   10.039 1.00 71.30  ? 451 ASN   A CB  1 
ATOM   1162 C  CG  . ASN   A 1 155 ? -33.037 6.837   9.451  1.00 76.38  ? 451 ASN   A CG  1 
ATOM   1163 O  OD1 . ASN   A 1 155 ? -33.140 7.260   8.294  1.00 75.31  ? 451 ASN   A OD1 1 
ATOM   1164 N  ND2 . ASN   A 1 155 ? -34.082 6.707   10.263 1.00 77.18  ? 451 ASN   A ND2 1 
ATOM   1165 N  N   . LYS   A 1 156 ? -29.709 9.589   9.596  1.00 77.38  ? 452 LYS   A N   1 
ATOM   1166 C  CA  . LYS   A 1 156 ? -29.757 11.032  9.807  1.00 79.07  ? 452 LYS   A CA  1 
ATOM   1167 C  C   . LYS   A 1 156 ? -29.914 11.390  11.278 1.00 81.24  ? 452 LYS   A C   1 
ATOM   1168 O  O   . LYS   A 1 156 ? -30.431 12.456  11.605 1.00 83.07  ? 452 LYS   A O   1 
ATOM   1169 C  CB  . LYS   A 1 156 ? -30.878 11.680  8.993  1.00 84.04  ? 452 LYS   A CB  1 
ATOM   1170 C  CG  . LYS   A 1 156 ? -30.633 11.762  7.491  1.00 88.70  ? 452 LYS   A CG  1 
ATOM   1171 C  CD  . LYS   A 1 156 ? -31.603 12.731  6.838  1.00 92.77  ? 452 LYS   A CD  1 
ATOM   1172 C  CE  . LYS   A 1 156 ? -32.791 12.012  6.196  1.00 100.19 ? 452 LYS   A CE  1 
ATOM   1173 N  NZ  . LYS   A 1 156 ? -32.547 11.631  4.773  1.00 102.32 ? 452 LYS   A NZ  1 
ATOM   1174 N  N   . GLY   A 1 157 ? -29.479 10.508  12.176 1.00 80.63  ? 453 GLY   A N   1 
ATOM   1175 C  CA  . GLY   A 1 157 ? -29.609 10.708  13.596 1.00 82.80  ? 453 GLY   A CA  1 
ATOM   1176 C  C   . GLY   A 1 157 ? -30.834 10.061  14.202 1.00 83.07  ? 453 GLY   A C   1 
ATOM   1177 O  O   . GLY   A 1 157 ? -30.918 9.950   15.430 1.00 78.61  ? 453 GLY   A O   1 
ATOM   1178 N  N   . ASN   A 1 158 ? -31.796 9.651   13.373 1.00 77.84  ? 454 ASN   A N   1 
ATOM   1179 C  CA  . ASN   A 1 158 ? -32.944 8.889   13.857 1.00 77.76  ? 454 ASN   A CA  1 
ATOM   1180 C  C   . ASN   A 1 158 ? -32.573 7.410   13.823 1.00 74.69  ? 454 ASN   A C   1 
ATOM   1181 O  O   . ASN   A 1 158 ? -33.056 6.622   13.008 1.00 74.82  ? 454 ASN   A O   1 
ATOM   1182 C  CB  . ASN   A 1 158 ? -34.181 9.197   13.027 1.00 81.62  ? 454 ASN   A CB  1 
ATOM   1183 C  CG  . ASN   A 1 158 ? -35.415 8.473   13.533 1.00 86.00  ? 454 ASN   A CG  1 
ATOM   1184 O  OD1 . ASN   A 1 158 ? -35.424 7.937   14.643 1.00 84.97  ? 454 ASN   A OD1 1 
ATOM   1185 N  ND2 . ASN   A 1 158 ? -36.464 8.447   12.715 1.00 88.92  ? 454 ASN   A ND2 1 
ATOM   1186 N  N   . LEU   A 1 159 ? -31.676 7.060   14.740 1.00 72.25  ? 455 LEU   A N   1 
ATOM   1187 C  CA  . LEU   A 1 159 ? -31.006 5.766   14.751 1.00 69.94  ? 455 LEU   A CA  1 
ATOM   1188 C  C   . LEU   A 1 159 ? -31.999 4.609   14.770 1.00 67.86  ? 455 LEU   A C   1 
ATOM   1189 O  O   . LEU   A 1 159 ? -33.094 4.699   15.334 1.00 68.14  ? 455 LEU   A O   1 
ATOM   1190 C  CB  . LEU   A 1 159 ? -30.086 5.655   15.968 1.00 70.89  ? 455 LEU   A CB  1 
ATOM   1191 C  CG  . LEU   A 1 159 ? -28.631 6.145   15.900 1.00 70.96  ? 455 LEU   A CG  1 
ATOM   1192 C  CD1 . LEU   A 1 159 ? -28.495 7.346   14.999 1.00 74.31  ? 455 LEU   A CD1 1 
ATOM   1193 C  CD2 . LEU   A 1 159 ? -28.094 6.451   17.307 1.00 70.45  ? 455 LEU   A CD2 1 
ATOM   1194 N  N   . ARG   A 1 160 ? -31.576 3.500   14.170 1.00 63.58  ? 456 ARG   A N   1 
ATOM   1195 C  CA  . ARG   A 1 160 ? -32.394 2.322   13.960 1.00 61.13  ? 456 ARG   A CA  1 
ATOM   1196 C  C   . ARG   A 1 160 ? -31.511 1.137   14.254 1.00 58.87  ? 456 ARG   A C   1 
ATOM   1197 O  O   . ARG   A 1 160 ? -30.339 1.122   13.871 1.00 60.02  ? 456 ARG   A O   1 
ATOM   1198 C  CB  . ARG   A 1 160 ? -32.926 2.220   12.493 1.00 62.81  ? 456 ARG   A CB  1 
ATOM   1199 C  CG  . ARG   A 1 160 ? -33.915 3.288   12.126 1.00 66.32  ? 456 ARG   A CG  1 
ATOM   1200 C  CD  . ARG   A 1 160 ? -34.458 3.111   10.699 1.00 70.84  ? 456 ARG   A CD  1 
ATOM   1201 N  NE  . ARG   A 1 160 ? -33.509 3.463   9.649  1.00 66.19  ? 456 ARG   A NE  1 
ATOM   1202 C  CZ  . ARG   A 1 160 ? -33.872 3.685   8.393  1.00 72.32  ? 456 ARG   A CZ  1 
ATOM   1203 N  NH1 . ARG   A 1 160 ? -35.144 3.645   8.029  1.00 76.51  ? 456 ARG   A NH1 1 
ATOM   1204 N  NH2 . ARG   A 1 160 ? -32.941 3.956   7.479  1.00 68.51  ? 456 ARG   A NH2 1 
ATOM   1205 N  N   . SER   A 1 161 ? -32.079 0.144   14.912 1.00 58.51  ? 457 SER   A N   1 
ATOM   1206 C  CA  . SER   A 1 161 ? -31.321 -1.033  15.300 1.00 59.42  ? 457 SER   A CA  1 
ATOM   1207 C  C   . SER   A 1 161 ? -31.095 -1.927  14.102 1.00 56.87  ? 457 SER   A C   1 
ATOM   1208 O  O   . SER   A 1 161 ? -31.987 -2.095  13.263 1.00 58.40  ? 457 SER   A O   1 
ATOM   1209 C  CB  . SER   A 1 161 ? -32.051 -1.805  16.404 1.00 59.16  ? 457 SER   A CB  1 
ATOM   1210 O  OG  . SER   A 1 161 ? -32.584 -0.898  17.368 1.00 61.01  ? 457 SER   A OG  1 
ATOM   1211 N  N   . ALA   A 1 162 ? -29.904 -2.520  14.034 1.00 55.15  ? 458 ALA   A N   1 
ATOM   1212 C  CA  . ALA   A 1 162 ? -29.534 -3.274  12.844 1.00 55.47  ? 458 ALA   A CA  1 
ATOM   1213 C  C   . ALA   A 1 162 ? -28.425 -4.254  13.177 1.00 55.14  ? 458 ALA   A C   1 
ATOM   1214 O  O   . ALA   A 1 162 ? -27.608 -4.008  14.066 1.00 54.76  ? 458 ALA   A O   1 
ATOM   1215 C  CB  . ALA   A 1 162 ? -29.082 -2.336  11.716 1.00 55.18  ? 458 ALA   A CB  1 
ATOM   1216 N  N   . ILE   A 1 163 ? -28.397 -5.359  12.441 1.00 50.71  ? 459 ILE   A N   1 
ATOM   1217 C  CA  . ILE   A 1 163 ? -27.323 -6.337  12.524 1.00 51.71  ? 459 ILE   A CA  1 
ATOM   1218 C  C   . ILE   A 1 163 ? -27.021 -6.814  11.112 1.00 54.63  ? 459 ILE   A C   1 
ATOM   1219 O  O   . ILE   A 1 163 ? -27.936 -7.004  10.304 1.00 56.20  ? 459 ILE   A O   1 
ATOM   1220 C  CB  . ILE   A 1 163 ? -27.696 -7.518  13.450 1.00 53.22  ? 459 ILE   A CB  1 
ATOM   1221 C  CG1 . ILE   A 1 163 ? -26.557 -8.529  13.529 1.00 51.84  ? 459 ILE   A CG1 1 
ATOM   1222 C  CG2 . ILE   A 1 163 ? -29.005 -8.172  13.006 1.00 49.77  ? 459 ILE   A CG2 1 
ATOM   1223 C  CD1 . ILE   A 1 163 ? -26.663 -9.495  14.715 1.00 53.10  ? 459 ILE   A CD1 1 
ATOM   1224 N  N   . THR   A 1 164 ? -25.736 -6.965  10.801 1.00 53.27  ? 460 THR   A N   1 
ATOM   1225 C  CA  . THR   A 1 164 ? -25.285 -7.514  9.527  1.00 54.11  ? 460 THR   A CA  1 
ATOM   1226 C  C   . THR   A 1 164 ? -24.592 -8.832  9.811  1.00 53.10  ? 460 THR   A C   1 
ATOM   1227 O  O   . THR   A 1 164 ? -23.664 -8.876  10.626 1.00 57.01  ? 460 THR   A O   1 
ATOM   1228 C  CB  . THR   A 1 164 ? -24.337 -6.556  8.814  1.00 53.29  ? 460 THR   A CB  1 
ATOM   1229 O  OG1 . THR   A 1 164 ? -25.044 -5.355  8.503  1.00 54.43  ? 460 THR   A OG1 1 
ATOM   1230 C  CG2 . THR   A 1 164 ? -23.841 -7.182  7.495  1.00 54.70  ? 460 THR   A CG2 1 
ATOM   1231 N  N   . ILE   A 1 165 ? -25.048 -9.900  9.166  1.00 54.37  ? 461 ILE   A N   1 
ATOM   1232 C  CA  . ILE   A 1 165 ? -24.604 -11.253 9.470  1.00 53.47  ? 461 ILE   A CA  1 
ATOM   1233 C  C   . ILE   A 1 165 ? -23.778 -11.777 8.303  1.00 56.97  ? 461 ILE   A C   1 
ATOM   1234 O  O   . ILE   A 1 165 ? -24.292 -11.977 7.193  1.00 56.50  ? 461 ILE   A O   1 
ATOM   1235 C  CB  . ILE   A 1 165 ? -25.787 -12.173 9.784  1.00 52.74  ? 461 ILE   A CB  1 
ATOM   1236 C  CG1 . ILE   A 1 165 ? -26.552 -11.647 11.010 1.00 55.77  ? 461 ILE   A CG1 1 
ATOM   1237 C  CG2 . ILE   A 1 165 ? -25.289 -13.544 10.114 1.00 57.70  ? 461 ILE   A CG2 1 
ATOM   1238 C  CD1 . ILE   A 1 165 ? -27.841 -12.368 11.292 1.00 56.45  ? 461 ILE   A CD1 1 
ATOM   1239 N  N   . PHE   A 1 166 ? -22.496 -12.000 8.558  1.00 56.26  ? 462 PHE   A N   1 
ATOM   1240 C  CA  . PHE   A 1 166 ? -21.564 -12.507 7.563  1.00 56.58  ? 462 PHE   A CA  1 
ATOM   1241 C  C   . PHE   A 1 166 ? -21.550 -14.023 7.590  1.00 58.90  ? 462 PHE   A C   1 
ATOM   1242 O  O   . PHE   A 1 166 ? -22.141 -14.639 8.484  1.00 61.00  ? 462 PHE   A O   1 
ATOM   1243 C  CB  . PHE   A 1 166 ? -20.182 -11.914 7.812  1.00 57.28  ? 462 PHE   A CB  1 
ATOM   1244 C  CG  . PHE   A 1 166 ? -20.113 -10.457 7.477  1.00 59.48  ? 462 PHE   A CG  1 
ATOM   1245 C  CD1 . PHE   A 1 166 ? -20.156 -10.043 6.143  1.00 58.72  ? 462 PHE   A CD1 1 
ATOM   1246 C  CD2 . PHE   A 1 166 ? -20.068 -9.499  8.482  1.00 55.29  ? 462 PHE   A CD2 1 
ATOM   1247 C  CE1 . PHE   A 1 166 ? -20.116 -8.695  5.820  1.00 61.14  ? 462 PHE   A CE1 1 
ATOM   1248 C  CE2 . PHE   A 1 166 ? -20.024 -8.146  8.170  1.00 55.63  ? 462 PHE   A CE2 1 
ATOM   1249 C  CZ  . PHE   A 1 166 ? -20.052 -7.736  6.830  1.00 58.58  ? 462 PHE   A CZ  1 
ATOM   1250 N  N   . PRO   A 1 167 ? -20.937 -14.658 6.586  1.00 61.84  ? 463 PRO   A N   1 
ATOM   1251 C  CA  . PRO   A 1 167 ? -20.960 -16.125 6.518  1.00 61.57  ? 463 PRO   A CA  1 
ATOM   1252 C  C   . PRO   A 1 167 ? -20.586 -16.787 7.837  1.00 62.30  ? 463 PRO   A C   1 
ATOM   1253 O  O   . PRO   A 1 167 ? -19.727 -16.304 8.580  1.00 62.06  ? 463 PRO   A O   1 
ATOM   1254 C  CB  . PRO   A 1 167 ? -19.934 -16.432 5.428  1.00 60.59  ? 463 PRO   A CB  1 
ATOM   1255 C  CG  . PRO   A 1 167 ? -20.114 -15.292 4.468  1.00 61.19  ? 463 PRO   A CG  1 
ATOM   1256 C  CD  . PRO   A 1 167 ? -20.381 -14.076 5.339  1.00 60.85  ? 463 PRO   A CD  1 
ATOM   1257 N  N   . GLN   A 1 168 ? -21.246 -17.907 8.115  1.00 63.45  ? 464 GLN   A N   1 
ATOM   1258 C  CA  . GLN   A 1 168 ? -21.000 -18.645 9.342  1.00 63.49  ? 464 GLN   A CA  1 
ATOM   1259 C  C   . GLN   A 1 168 ? -19.641 -19.326 9.280  1.00 66.25  ? 464 GLN   A C   1 
ATOM   1260 O  O   . GLN   A 1 168 ? -19.118 -19.643 8.204  1.00 68.25  ? 464 GLN   A O   1 
ATOM   1261 C  CB  . GLN   A 1 168 ? -22.092 -19.690 9.561  1.00 62.51  ? 464 GLN   A CB  1 
ATOM   1262 C  CG  . GLN   A 1 168 ? -22.190 -20.708 8.410  1.00 65.95  ? 464 GLN   A CG  1 
ATOM   1263 C  CD  . GLN   A 1 168 ? -23.549 -21.378 8.333  1.00 68.81  ? 464 GLN   A CD  1 
ATOM   1264 O  OE1 . GLN   A 1 168 ? -24.576 -20.712 8.381  1.00 69.82  ? 464 GLN   A OE1 1 
ATOM   1265 N  NE2 . GLN   A 1 168 ? -23.559 -22.710 8.230  1.00 71.09  ? 464 GLN   A NE2 1 
ATOM   1266 N  N   . ARG   A 1 169 ? -19.057 -19.521 10.454 1.00 64.17  ? 465 ARG   A N   1 
ATOM   1267 C  CA  . ARG   A 1 169 ? -17.878 -20.355 10.581 1.00 70.14  ? 465 ARG   A CA  1 
ATOM   1268 C  C   . ARG   A 1 169 ? -18.137 -21.711 9.943  1.00 73.03  ? 465 ARG   A C   1 
ATOM   1269 O  O   . ARG   A 1 169 ? -19.245 -22.248 10.019 1.00 72.54  ? 465 ARG   A O   1 
ATOM   1270 C  CB  . ARG   A 1 169 ? -17.524 -20.519 12.064 1.00 72.42  ? 465 ARG   A CB  1 
ATOM   1271 C  CG  . ARG   A 1 169 ? -16.466 -21.555 12.327 1.00 78.06  ? 465 ARG   A CG  1 
ATOM   1272 C  CD  . ARG   A 1 169 ? -16.016 -21.536 13.770 1.00 78.84  ? 465 ARG   A CD  1 
ATOM   1273 N  NE  . ARG   A 1 169 ? -15.229 -20.351 14.090 1.00 81.25  ? 465 ARG   A NE  1 
ATOM   1274 C  CZ  . ARG   A 1 169 ? -15.519 -19.503 15.065 1.00 79.04  ? 465 ARG   A CZ  1 
ATOM   1275 N  NH1 . ARG   A 1 169 ? -16.586 -19.674 15.830 1.00 80.19  ? 465 ARG   A NH1 1 
ATOM   1276 N  NH2 . ARG   A 1 169 ? -14.712 -18.467 15.287 1.00 75.63  ? 465 ARG   A NH2 1 
ATOM   1277 N  N   . THR   A 1 170 ? -17.116 -22.252 9.282  1.00 77.61  ? 466 THR   A N   1 
ATOM   1278 C  CA  . THR   A 1 170 ? -17.230 -23.576 8.686  1.00 79.47  ? 466 THR   A CA  1 
ATOM   1279 C  C   . THR   A 1 170 ? -16.229 -24.517 9.341  1.00 85.26  ? 466 THR   A C   1 
ATOM   1280 O  O   . THR   A 1 170 ? -16.574 -25.242 10.278 1.00 88.77  ? 466 THR   A O   1 
ATOM   1281 C  CB  . THR   A 1 170 ? -17.019 -23.516 7.169  1.00 81.41  ? 466 THR   A CB  1 
ATOM   1282 O  OG1 . THR   A 1 170 ? -15.869 -22.715 6.869  1.00 82.68  ? 466 THR   A OG1 1 
ATOM   1283 C  CG2 . THR   A 1 170 ? -18.245 -22.919 6.488  1.00 76.98  ? 466 THR   A CG2 1 
ATOM   1284 N  N   . ASP   A 1 171 ? -14.980 -24.496 8.876  1.00 85.51  ? 467 ASP   A N   1 
ATOM   1285 C  CA  . ASP   A 1 171 ? -13.941 -25.304 9.506  1.00 89.89  ? 467 ASP   A CA  1 
ATOM   1286 C  C   . ASP   A 1 171 ? -13.377 -24.649 10.762 1.00 93.46  ? 467 ASP   A C   1 
ATOM   1287 O  O   . ASP   A 1 171 ? -12.918 -25.353 11.668 1.00 98.52  ? 467 ASP   A O   1 
ATOM   1288 C  CB  . ASP   A 1 171 ? -12.806 -25.553 8.522  1.00 93.79  ? 467 ASP   A CB  1 
ATOM   1289 C  CG  . ASP   A 1 171 ? -12.062 -24.278 8.165  1.00 96.04  ? 467 ASP   A CG  1 
ATOM   1290 O  OD1 . ASP   A 1 171 ? -12.617 -23.180 8.388  1.00 94.81  ? 467 ASP   A OD1 1 
ATOM   1291 O  OD2 . ASP   A 1 171 ? -10.924 -24.374 7.658  1.00 99.46  ? 467 ASP   A OD2 1 
ATOM   1292 N  N   . GLY   A 1 172 ? -13.378 -23.320 10.826 1.00 92.45  ? 468 GLY   A N   1 
ATOM   1293 C  CA  . GLY   A 1 172 ? -12.709 -22.608 11.896 1.00 91.38  ? 468 GLY   A CA  1 
ATOM   1294 C  C   . GLY   A 1 172 ? -11.562 -21.744 11.408 1.00 95.79  ? 468 GLY   A C   1 
ATOM   1295 O  O   . GLY   A 1 172 ? -11.290 -20.691 11.988 1.00 93.57  ? 468 GLY   A O   1 
ATOM   1296 N  N   . LYS   A 1 173 ? -10.884 -22.170 10.340 1.00 96.87  ? 469 LYS   A N   1 
ATOM   1297 C  CA  . LYS   A 1 173 ? -9.810  -21.388 9.737  1.00 99.23  ? 469 LYS   A CA  1 
ATOM   1298 C  C   . LYS   A 1 173 ? -10.289 -20.563 8.545  1.00 98.85  ? 469 LYS   A C   1 
ATOM   1299 O  O   . LYS   A 1 173 ? -9.464  -19.998 7.816  1.00 98.60  ? 469 LYS   A O   1 
ATOM   1300 C  CB  . LYS   A 1 173 ? -8.653  -22.305 9.325  1.00 104.05 ? 469 LYS   A CB  1 
ATOM   1301 C  CG  . LYS   A 1 173 ? -7.262  -21.695 9.548  1.00 109.31 ? 469 LYS   A CG  1 
ATOM   1302 C  CD  . LYS   A 1 173 ? -7.161  -20.990 10.912 1.00 110.29 ? 469 LYS   A CD  1 
ATOM   1303 C  CE  . LYS   A 1 173 ? -6.842  -19.502 10.750 1.00 110.59 ? 469 LYS   A CE  1 
ATOM   1304 N  NZ  . LYS   A 1 173 ? -7.219  -18.689 11.938 1.00 109.67 ? 469 LYS   A NZ  1 
ATOM   1305 N  N   . HIS   A 1 174 ? -11.602 -20.487 8.336  1.00 94.17  ? 470 HIS   A N   1 
ATOM   1306 C  CA  . HIS   A 1 174 ? -12.185 -19.596 7.344  1.00 93.47  ? 470 HIS   A CA  1 
ATOM   1307 C  C   . HIS   A 1 174 ? -13.248 -18.732 8.005  1.00 91.83  ? 470 HIS   A C   1 
ATOM   1308 O  O   . HIS   A 1 174 ? -14.395 -18.675 7.547  1.00 95.96  ? 470 HIS   A O   1 
ATOM   1309 C  CB  . HIS   A 1 174 ? -12.764 -20.391 6.175  1.00 94.59  ? 470 HIS   A CB  1 
ATOM   1310 C  CG  . HIS   A 1 174 ? -11.733 -21.169 5.426  1.00 96.99  ? 470 HIS   A CG  1 
ATOM   1311 N  ND1 . HIS   A 1 174 ? -11.728 -22.546 5.374  1.00 98.47  ? 470 HIS   A ND1 1 
ATOM   1312 C  CD2 . HIS   A 1 174 ? -10.645 -20.761 4.732  1.00 98.79  ? 470 HIS   A CD2 1 
ATOM   1313 C  CE1 . HIS   A 1 174 ? -10.690 -22.952 4.665  1.00 102.92 ? 470 HIS   A CE1 1 
ATOM   1314 N  NE2 . HIS   A 1 174 ? -10.017 -21.888 4.264  1.00 103.88 ? 470 HIS   A NE2 1 
ATOM   1315 N  N   . ASP   A 1 175 ? -12.868 -18.069 9.091  1.00 86.52  ? 471 ASP   A N   1 
ATOM   1316 C  CA  . ASP   A 1 175 ? -13.765 -17.184 9.810  1.00 80.39  ? 471 ASP   A CA  1 
ATOM   1317 C  C   . ASP   A 1 175 ? -13.840 -15.825 9.141  1.00 77.87  ? 471 ASP   A C   1 
ATOM   1318 O  O   . ASP   A 1 175 ? -12.826 -15.276 8.700  1.00 80.66  ? 471 ASP   A O   1 
ATOM   1319 C  CB  . ASP   A 1 175 ? -13.296 -16.993 11.250 1.00 79.24  ? 471 ASP   A CB  1 
ATOM   1320 C  CG  . ASP   A 1 175 ? -13.462 -18.230 12.076 1.00 81.78  ? 471 ASP   A CG  1 
ATOM   1321 O  OD1 . ASP   A 1 175 ? -14.004 -19.224 11.551 1.00 83.37  ? 471 ASP   A OD1 1 
ATOM   1322 O  OD2 . ASP   A 1 175 ? -13.054 -18.206 13.250 1.00 81.31  ? 471 ASP   A OD2 1 
ATOM   1323 N  N   . PHE   A 1 176 ? -15.046 -15.278 9.085  1.00 71.00  ? 472 PHE   A N   1 
ATOM   1324 C  CA  . PHE   A 1 176 ? -15.229 -13.863 8.798  1.00 70.32  ? 472 PHE   A CA  1 
ATOM   1325 C  C   . PHE   A 1 176 ? -15.178 -13.129 10.126 1.00 66.16  ? 472 PHE   A C   1 
ATOM   1326 O  O   . PHE   A 1 176 ? -15.899 -13.493 11.056 1.00 65.09  ? 472 PHE   A O   1 
ATOM   1327 C  CB  . PHE   A 1 176 ? -16.549 -13.601 8.076  1.00 66.12  ? 472 PHE   A CB  1 
ATOM   1328 C  CG  . PHE   A 1 176 ? -16.531 -14.003 6.644  1.00 69.26  ? 472 PHE   A CG  1 
ATOM   1329 C  CD1 . PHE   A 1 176 ? -16.453 -15.337 6.285  1.00 69.94  ? 472 PHE   A CD1 1 
ATOM   1330 C  CD2 . PHE   A 1 176 ? -16.585 -13.040 5.640  1.00 69.07  ? 472 PHE   A CD2 1 
ATOM   1331 C  CE1 . PHE   A 1 176 ? -16.434 -15.706 4.946  1.00 72.24  ? 472 PHE   A CE1 1 
ATOM   1332 C  CE2 . PHE   A 1 176 ? -16.565 -13.395 4.321  1.00 67.65  ? 472 PHE   A CE2 1 
ATOM   1333 C  CZ  . PHE   A 1 176 ? -16.489 -14.734 3.960  1.00 69.03  ? 472 PHE   A CZ  1 
ATOM   1334 N  N   . ARG   A 1 177 ? -14.326 -12.114 10.218 1.00 68.30  ? 473 ARG   A N   1 
ATOM   1335 C  CA  . ARG   A 1 177 ? -14.158 -11.368 11.456 1.00 67.53  ? 473 ARG   A CA  1 
ATOM   1336 C  C   . ARG   A 1 177 ? -14.045 -9.879  11.170 1.00 68.28  ? 473 ARG   A C   1 
ATOM   1337 O  O   . ARG   A 1 177 ? -13.331 -9.466  10.246 1.00 70.00  ? 473 ARG   A O   1 
ATOM   1338 C  CB  . ARG   A 1 177 ? -12.912 -11.837 12.211 1.00 70.91  ? 473 ARG   A CB  1 
ATOM   1339 C  CG  . ARG   A 1 177 ? -13.040 -13.203 12.857 1.00 71.50  ? 473 ARG   A CG  1 
ATOM   1340 C  CD  . ARG   A 1 177 ? -14.186 -13.234 13.861 1.00 67.55  ? 473 ARG   A CD  1 
ATOM   1341 N  NE  . ARG   A 1 177 ? -14.098 -12.183 14.870 1.00 68.58  ? 473 ARG   A NE  1 
ATOM   1342 C  CZ  . ARG   A 1 177 ? -13.391 -12.277 15.990 1.00 73.05  ? 473 ARG   A CZ  1 
ATOM   1343 N  NH1 . ARG   A 1 177 ? -12.658 -13.350 16.255 1.00 72.32  ? 473 ARG   A NH1 1 
ATOM   1344 N  NH2 . ARG   A 1 177 ? -13.421 -11.271 16.867 1.00 71.54  ? 473 ARG   A NH2 1 
ATOM   1345 N  N   . VAL   A 1 178 ? -14.758 -9.075  11.953 1.00 64.65  ? 474 VAL   A N   1 
ATOM   1346 C  CA  . VAL   A 1 178 ? -14.440 -7.658  12.083 1.00 65.79  ? 474 VAL   A CA  1 
ATOM   1347 C  C   . VAL   A 1 178 ? -13.464 -7.522  13.240 1.00 68.42  ? 474 VAL   A C   1 
ATOM   1348 O  O   . VAL   A 1 178 ? -13.814 -7.803  14.393 1.00 69.78  ? 474 VAL   A O   1 
ATOM   1349 C  CB  . VAL   A 1 178 ? -15.695 -6.804  12.314 1.00 62.45  ? 474 VAL   A CB  1 
ATOM   1350 C  CG1 . VAL   A 1 178 ? -15.333 -5.318  12.337 1.00 63.71  ? 474 VAL   A CG1 1 
ATOM   1351 C  CG2 . VAL   A 1 178 ? -16.746 -7.069  11.251 1.00 63.17  ? 474 VAL   A CG2 1 
ATOM   1352 N  N   . TRP   A 1 179 ? -12.229 -7.119  12.937 1.00 70.17  ? 475 TRP   A N   1 
ATOM   1353 C  CA  . TRP   A 1 179 ? -11.215 -7.057  13.987 1.00 74.28  ? 475 TRP   A CA  1 
ATOM   1354 C  C   . TRP   A 1 179 ? -11.480 -5.930  14.975 1.00 73.80  ? 475 TRP   A C   1 
ATOM   1355 O  O   . TRP   A 1 179 ? -11.040 -6.002  16.129 1.00 75.31  ? 475 TRP   A O   1 
ATOM   1356 C  CB  . TRP   A 1 179 ? -9.827  -6.922  13.366 1.00 76.26  ? 475 TRP   A CB  1 
ATOM   1357 C  CG  . TRP   A 1 179 ? -9.346  -8.215  12.808 1.00 77.56  ? 475 TRP   A CG  1 
ATOM   1358 C  CD1 . TRP   A 1 179 ? -10.106 -9.170  12.209 1.00 76.75  ? 475 TRP   A CD1 1 
ATOM   1359 C  CD2 . TRP   A 1 179 ? -8.008  -8.728  12.842 1.00 81.78  ? 475 TRP   A CD2 1 
ATOM   1360 N  NE1 . TRP   A 1 179 ? -9.324  -10.237 11.838 1.00 80.13  ? 475 TRP   A NE1 1 
ATOM   1361 C  CE2 . TRP   A 1 179 ? -8.032  -9.992  12.221 1.00 82.88  ? 475 TRP   A CE2 1 
ATOM   1362 C  CE3 . TRP   A 1 179 ? -6.792  -8.238  13.330 1.00 82.55  ? 475 TRP   A CE3 1 
ATOM   1363 C  CZ2 . TRP   A 1 179 ? -6.890  -10.773 12.076 1.00 88.34  ? 475 TRP   A CZ2 1 
ATOM   1364 C  CZ3 . TRP   A 1 179 ? -5.662  -9.013  13.184 1.00 87.01  ? 475 TRP   A CZ3 1 
ATOM   1365 C  CH2 . TRP   A 1 179 ? -5.717  -10.267 12.562 1.00 90.58  ? 475 TRP   A CH2 1 
ATOM   1366 N  N   . ASN   A 1 180 ? -12.192 -4.893  14.551 1.00 71.20  ? 476 ASN   A N   1 
ATOM   1367 C  CA  . ASN   A 1 180 ? -12.570 -3.826  15.463 1.00 69.81  ? 476 ASN   A CA  1 
ATOM   1368 C  C   . ASN   A 1 180 ? -13.537 -4.352  16.513 1.00 68.49  ? 476 ASN   A C   1 
ATOM   1369 O  O   . ASN   A 1 180 ? -14.396 -5.188  16.218 1.00 63.95  ? 476 ASN   A O   1 
ATOM   1370 C  CB  . ASN   A 1 180 ? -13.221 -2.674  14.699 1.00 70.37  ? 476 ASN   A CB  1 
ATOM   1371 C  CG  . ASN   A 1 180 ? -12.394 -2.219  13.527 1.00 76.05  ? 476 ASN   A CG  1 
ATOM   1372 O  OD1 . ASN   A 1 180 ? -11.960 -3.036  12.713 1.00 75.17  ? 476 ASN   A OD1 1 
ATOM   1373 N  ND2 . ASN   A 1 180 ? -12.156 -0.914  13.433 1.00 76.70  ? 476 ASN   A ND2 1 
ATOM   1374 N  N   . SER   A 1 181 ? -13.390 -3.859  17.751 1.00 68.56  ? 477 SER   A N   1 
ATOM   1375 C  CA  . SER   A 1 181 ? -14.342 -4.213  18.797 1.00 63.99  ? 477 SER   A CA  1 
ATOM   1376 C  C   . SER   A 1 181 ? -15.686 -3.539  18.570 1.00 62.98  ? 477 SER   A C   1 
ATOM   1377 O  O   . SER   A 1 181 ? -16.730 -4.108  18.900 1.00 60.94  ? 477 SER   A O   1 
ATOM   1378 C  CB  . SER   A 1 181 ? -13.781 -3.831  20.167 1.00 67.06  ? 477 SER   A CB  1 
ATOM   1379 O  OG  . SER   A 1 181 ? -13.255 -2.517  20.119 1.00 69.77  ? 477 SER   A OG  1 
ATOM   1380 N  N   . GLN   A 1 182 ? -15.675 -2.328  18.019 1.00 65.06  ? 478 GLN   A N   1 
ATOM   1381 C  CA  . GLN   A 1 182 ? -16.868 -1.651  17.532 1.00 63.12  ? 478 GLN   A CA  1 
ATOM   1382 C  C   . GLN   A 1 182 ? -16.535 -1.045  16.188 1.00 65.53  ? 478 GLN   A C   1 
ATOM   1383 O  O   . GLN   A 1 182 ? -15.390 -0.657  15.953 1.00 69.84  ? 478 GLN   A O   1 
ATOM   1384 C  CB  . GLN   A 1 182 ? -17.346 -0.512  18.444 1.00 65.76  ? 478 GLN   A CB  1 
ATOM   1385 C  CG  . GLN   A 1 182 ? -17.840 -0.887  19.801 1.00 66.11  ? 478 GLN   A CG  1 
ATOM   1386 C  CD  . GLN   A 1 182 ? -17.733 0.294   20.765 1.00 70.02  ? 478 GLN   A CD  1 
ATOM   1387 O  OE1 . GLN   A 1 182 ? -18.074 1.440   20.417 1.00 69.66  ? 478 GLN   A OE1 1 
ATOM   1388 N  NE2 . GLN   A 1 182 ? -17.231 0.032   21.950 1.00 68.62  ? 478 GLN   A NE2 1 
ATOM   1389 N  N   . LEU   A 1 183 ? -17.547 -0.946  15.316 1.00 63.27  ? 479 LEU   A N   1 
ATOM   1390 C  CA  . LEU   A 1 183 ? -17.343 -0.369  13.992 1.00 64.84  ? 479 LEU   A CA  1 
ATOM   1391 C  C   . LEU   A 1 183 ? -16.744 1.026   14.073 1.00 67.30  ? 479 LEU   A C   1 
ATOM   1392 O  O   . LEU   A 1 183 ? -15.860 1.378   13.282 1.00 70.97  ? 479 LEU   A O   1 
ATOM   1393 C  CB  . LEU   A 1 183 ? -18.668 -0.325  13.224 1.00 61.74  ? 479 LEU   A CB  1 
ATOM   1394 C  CG  . LEU   A 1 183 ? -19.366 -1.659  12.985 1.00 60.20  ? 479 LEU   A CG  1 
ATOM   1395 C  CD1 . LEU   A 1 183 ? -20.614 -1.477  12.112 1.00 60.15  ? 479 LEU   A CD1 1 
ATOM   1396 C  CD2 . LEU   A 1 183 ? -18.383 -2.650  12.365 1.00 62.84  ? 479 LEU   A CD2 1 
ATOM   1397 N  N   . ILE   A 1 184 ? -17.233 1.847   14.991 1.00 67.98  ? 480 ILE   A N   1 
ATOM   1398 C  CA  . ILE   A 1 184 ? -16.796 3.227   15.114 1.00 69.60  ? 480 ILE   A CA  1 
ATOM   1399 C  C   . ILE   A 1 184 ? -16.221 3.413   16.517 1.00 73.78  ? 480 ILE   A C   1 
ATOM   1400 O  O   . ILE   A 1 184 ? -16.958 3.403   17.511 1.00 71.22  ? 480 ILE   A O   1 
ATOM   1401 C  CB  . ILE   A 1 184 ? -17.938 4.206   14.826 1.00 69.14  ? 480 ILE   A CB  1 
ATOM   1402 C  CG1 . ILE   A 1 184 ? -18.417 4.019   13.380 1.00 71.87  ? 480 ILE   A CG1 1 
ATOM   1403 C  CG2 . ILE   A 1 184 ? -17.466 5.627   15.017 1.00 73.09  ? 480 ILE   A CG2 1 
ATOM   1404 C  CD1 . ILE   A 1 184 ? -19.476 4.980   12.942 1.00 73.07  ? 480 ILE   A CD1 1 
ATOM   1405 N  N   . ARG   A 1 185 ? -14.897 3.528   16.596 1.00 72.16  ? 481 ARG   A N   1 
ATOM   1406 C  CA  . ARG   A 1 185 ? -14.184 3.842   17.821 1.00 75.62  ? 481 ARG   A CA  1 
ATOM   1407 C  C   . ARG   A 1 185 ? -13.089 4.846   17.501 1.00 80.28  ? 481 ARG   A C   1 
ATOM   1408 O  O   . ARG   A 1 185 ? -12.574 4.892   16.382 1.00 83.55  ? 481 ARG   A O   1 
ATOM   1409 C  CB  . ARG   A 1 185 ? -13.557 2.600   18.473 1.00 76.63  ? 481 ARG   A CB  1 
ATOM   1410 C  CG  . ARG   A 1 185 ? -14.502 1.446   18.715 1.00 74.81  ? 481 ARG   A CG  1 
ATOM   1411 C  CD  . ARG   A 1 185 ? -14.001 0.588   19.877 1.00 71.43  ? 481 ARG   A CD  1 
ATOM   1412 N  NE  . ARG   A 1 185 ? -14.102 1.295   21.146 1.00 76.58  ? 481 ARG   A NE  1 
ATOM   1413 C  CZ  . ARG   A 1 185 ? -13.771 0.768   22.315 1.00 76.62  ? 481 ARG   A CZ  1 
ATOM   1414 N  NH1 . ARG   A 1 185 ? -13.312 -0.469  22.408 1.00 75.02  ? 481 ARG   A NH1 1 
ATOM   1415 N  NH2 . ARG   A 1 185 ? -13.906 1.499   23.417 1.00 80.38  ? 481 ARG   A NH2 1 
ATOM   1416 N  N   . TYR   A 1 186 ? -12.733 5.649   18.498 1.00 83.55  ? 482 TYR   A N   1 
ATOM   1417 C  CA  . TYR   A 1 186 ? -11.652 6.613   18.374 1.00 87.08  ? 482 TYR   A CA  1 
ATOM   1418 C  C   . TYR   A 1 186 ? -10.301 5.961   18.649 1.00 87.05  ? 482 TYR   A C   1 
ATOM   1419 O  O   . TYR   A 1 186 ? -10.194 4.996   19.410 1.00 85.90  ? 482 TYR   A O   1 
ATOM   1420 C  CB  . TYR   A 1 186 ? -11.877 7.793   19.322 1.00 89.65  ? 482 TYR   A CB  1 
ATOM   1421 C  CG  . TYR   A 1 186 ? -13.133 8.551   18.977 1.00 90.70  ? 482 TYR   A CG  1 
ATOM   1422 C  CD1 . TYR   A 1 186 ? -13.281 9.140   17.727 1.00 92.46  ? 482 TYR   A CD1 1 
ATOM   1423 C  CD2 . TYR   A 1 186 ? -14.187 8.642   19.871 1.00 86.95  ? 482 TYR   A CD2 1 
ATOM   1424 C  CE1 . TYR   A 1 186 ? -14.428 9.827   17.388 1.00 91.82  ? 482 TYR   A CE1 1 
ATOM   1425 C  CE2 . TYR   A 1 186 ? -15.341 9.334   19.542 1.00 86.45  ? 482 TYR   A CE2 1 
ATOM   1426 C  CZ  . TYR   A 1 186 ? -15.457 9.921   18.294 1.00 88.78  ? 482 TYR   A CZ  1 
ATOM   1427 O  OH  . TYR   A 1 186 ? -16.601 10.605  17.938 1.00 86.47  ? 482 TYR   A OH  1 
ATOM   1428 N  N   . ALA   A 1 187 ? -9.266  6.497   18.008 1.00 91.54  ? 483 ALA   A N   1 
ATOM   1429 C  CA  . ALA   A 1 187 ? -7.927  5.939   18.123 1.00 92.06  ? 483 ALA   A CA  1 
ATOM   1430 C  C   . ALA   A 1 187 ? -7.334  6.200   19.501 1.00 95.36  ? 483 ALA   A C   1 
ATOM   1431 O  O   . ALA   A 1 187 ? -7.693  7.156   20.192 1.00 96.20  ? 483 ALA   A O   1 
ATOM   1432 C  CB  . ALA   A 1 187 ? -7.008  6.536   17.061 1.00 97.45  ? 483 ALA   A CB  1 
ATOM   1433 N  N   . GLY   A 1 188 ? -6.405  5.333   19.887 1.00 93.17  ? 484 GLY   A N   1 
ATOM   1434 C  CA  . GLY   A 1 188 ? -5.579  5.561   21.049 1.00 98.02  ? 484 GLY   A CA  1 
ATOM   1435 C  C   . GLY   A 1 188 ? -4.111  5.533   20.694 1.00 101.51 ? 484 GLY   A C   1 
ATOM   1436 O  O   . GLY   A 1 188 ? -3.647  4.617   20.009 1.00 101.14 ? 484 GLY   A O   1 
ATOM   1437 N  N   . TYR   A 1 189 ? -3.370  6.538   21.146 1.00 109.42 ? 485 TYR   A N   1 
ATOM   1438 C  CA  . TYR   A 1 189 ? -1.936  6.619   20.910 1.00 115.03 ? 485 TYR   A CA  1 
ATOM   1439 C  C   . TYR   A 1 189 ? -1.235  6.873   22.231 1.00 122.25 ? 485 TYR   A C   1 
ATOM   1440 O  O   . TYR   A 1 189 ? -1.500  7.883   22.892 1.00 123.60 ? 485 TYR   A O   1 
ATOM   1441 C  CB  . TYR   A 1 189 ? -1.581  7.736   19.929 1.00 116.70 ? 485 TYR   A CB  1 
ATOM   1442 C  CG  . TYR   A 1 189 ? -2.442  7.830   18.694 1.00 111.73 ? 485 TYR   A CG  1 
ATOM   1443 C  CD1 . TYR   A 1 189 ? -2.090  7.170   17.525 1.00 114.38 ? 485 TYR   A CD1 1 
ATOM   1444 C  CD2 . TYR   A 1 189 ? -3.586  8.615   18.686 1.00 111.12 ? 485 TYR   A CD2 1 
ATOM   1445 C  CE1 . TYR   A 1 189 ? -2.868  7.273   16.383 1.00 113.56 ? 485 TYR   A CE1 1 
ATOM   1446 C  CE2 . TYR   A 1 189 ? -4.368  8.726   17.555 1.00 113.22 ? 485 TYR   A CE2 1 
ATOM   1447 C  CZ  . TYR   A 1 189 ? -4.005  8.055   16.403 1.00 111.41 ? 485 TYR   A CZ  1 
ATOM   1448 O  OH  . TYR   A 1 189 ? -4.791  8.177   15.285 1.00 110.82 ? 485 TYR   A OH  1 
ATOM   1449 N  N   . LYS   A 1 190 ? -0.342  5.967   22.608 1.00 127.24 ? 486 LYS   A N   1 
ATOM   1450 C  CA  . LYS   A 1 190 ? 0.612   6.291   23.650 1.00 137.63 ? 486 LYS   A CA  1 
ATOM   1451 C  C   . LYS   A 1 190 ? 1.513   7.424   23.167 1.00 144.56 ? 486 LYS   A C   1 
ATOM   1452 O  O   . LYS   A 1 190 ? 1.702   7.632   21.966 1.00 147.77 ? 486 LYS   A O   1 
ATOM   1453 C  CB  . LYS   A 1 190 ? 1.426   5.055   24.026 1.00 139.21 ? 486 LYS   A CB  1 
ATOM   1454 C  CG  . LYS   A 1 190 ? 1.617   4.087   22.869 1.00 140.09 ? 486 LYS   A CG  1 
ATOM   1455 C  CD  . LYS   A 1 190 ? 2.446   2.874   23.265 1.00 141.48 ? 486 LYS   A CD  1 
ATOM   1456 C  CE  . LYS   A 1 190 ? 1.689   1.938   24.196 1.00 139.41 ? 486 LYS   A CE  1 
ATOM   1457 N  NZ  . LYS   A 1 190 ? 1.983   2.177   25.641 1.00 137.16 ? 486 LYS   A NZ  1 
ATOM   1458 N  N   . GLN   A 1 191 ? 2.053   8.176   24.113 1.00 143.52 ? 487 GLN   A N   1 
ATOM   1459 C  CA  . GLN   A 1 191 ? 2.785   9.388   23.789 1.00 146.65 ? 487 GLN   A CA  1 
ATOM   1460 C  C   . GLN   A 1 191 ? 4.280   9.216   24.022 1.00 150.78 ? 487 GLN   A C   1 
ATOM   1461 O  O   . GLN   A 1 191 ? 4.706   8.312   24.748 1.00 150.29 ? 487 GLN   A O   1 
ATOM   1462 C  CB  . GLN   A 1 191 ? 2.259   10.567  24.621 1.00 148.53 ? 487 GLN   A CB  1 
ATOM   1463 C  CG  . GLN   A 1 191 ? 0.920   11.114  24.136 1.00 142.82 ? 487 GLN   A CG  1 
ATOM   1464 C  CD  . GLN   A 1 191 ? 1.019   11.872  22.813 1.00 145.90 ? 487 GLN   A CD  1 
ATOM   1465 O  OE1 . GLN   A 1 191 ? 1.295   11.294  21.754 1.00 142.58 ? 487 GLN   A OE1 1 
ATOM   1466 N  NE2 . GLN   A 1 191 ? 0.783   13.178  22.872 1.00 148.26 ? 487 GLN   A NE2 1 
ATOM   1467 N  N   . PRO   A 1 192 ? 5.112   10.057  23.399 1.00 154.46 ? 488 PRO   A N   1 
ATOM   1468 C  CA  . PRO   A 1 192 ? 6.555   10.003  23.688 1.00 156.68 ? 488 PRO   A CA  1 
ATOM   1469 C  C   . PRO   A 1 192 ? 6.888   10.308  25.136 1.00 159.31 ? 488 PRO   A C   1 
ATOM   1470 O  O   . PRO   A 1 192 ? 8.016   10.037  25.567 1.00 162.27 ? 488 PRO   A O   1 
ATOM   1471 C  CB  . PRO   A 1 192 ? 7.148   11.056  22.738 1.00 161.39 ? 488 PRO   A CB  1 
ATOM   1472 C  CG  . PRO   A 1 192 ? 5.992   11.920  22.335 1.00 157.96 ? 488 PRO   A CG  1 
ATOM   1473 C  CD  . PRO   A 1 192 ? 4.808   11.007  22.315 1.00 156.04 ? 488 PRO   A CD  1 
ATOM   1474 N  N   . ASP   A 1 193 ? 5.945   10.860  25.900 1.00 160.96 ? 489 ASP   A N   1 
ATOM   1475 C  CA  . ASP   A 1 193 ? 6.106   11.080  27.330 1.00 160.94 ? 489 ASP   A CA  1 
ATOM   1476 C  C   . ASP   A 1 193 ? 5.327   10.071  28.166 1.00 152.53 ? 489 ASP   A C   1 
ATOM   1477 O  O   . ASP   A 1 193 ? 5.059   10.328  29.344 1.00 154.48 ? 489 ASP   A O   1 
ATOM   1478 C  CB  . ASP   A 1 193 ? 5.687   12.503  27.699 1.00 165.47 ? 489 ASP   A CB  1 
ATOM   1479 C  CG  . ASP   A 1 193 ? 4.302   12.851  27.193 1.00 162.91 ? 489 ASP   A CG  1 
ATOM   1480 O  OD1 . ASP   A 1 193 ? 4.108   12.887  25.959 1.00 161.71 ? 489 ASP   A OD1 1 
ATOM   1481 O  OD2 . ASP   A 1 193 ? 3.406   13.075  28.034 1.00 163.15 ? 489 ASP   A OD2 1 
ATOM   1482 N  N   . GLY   A 1 194 ? 4.943   8.940   27.576 1.00 148.79 ? 490 GLY   A N   1 
ATOM   1483 C  CA  . GLY   A 1 194 ? 4.340   7.849   28.313 1.00 142.16 ? 490 GLY   A CA  1 
ATOM   1484 C  C   . GLY   A 1 194 ? 2.861   7.977   28.618 1.00 139.79 ? 490 GLY   A C   1 
ATOM   1485 O  O   . GLY   A 1 194 ? 2.279   7.031   29.167 1.00 130.62 ? 490 GLY   A O   1 
ATOM   1486 N  N   . SER   A 1 195 ? 2.228   9.102   28.297 1.00 141.49 ? 491 SER   A N   1 
ATOM   1487 C  CA  . SER   A 1 195 ? 0.798   9.252   28.530 1.00 139.48 ? 491 SER   A CA  1 
ATOM   1488 C  C   . SER   A 1 195 ? 0.037   8.675   27.331 1.00 136.10 ? 491 SER   A C   1 
ATOM   1489 O  O   . SER   A 1 195 ? 0.579   7.874   26.565 1.00 136.11 ? 491 SER   A O   1 
ATOM   1490 C  CB  . SER   A 1 195 ? 0.462   10.721  28.807 1.00 140.53 ? 491 SER   A CB  1 
ATOM   1491 O  OG  . SER   A 1 195 ? 0.655   11.517  27.654 1.00 146.15 ? 491 SER   A OG  1 
ATOM   1492 N  N   . THR   A 1 196 ? -1.226  9.063   27.154 1.00 133.19 ? 492 THR   A N   1 
ATOM   1493 C  CA  . THR   A 1 196 ? -2.053  8.512   26.089 1.00 128.31 ? 492 THR   A CA  1 
ATOM   1494 C  C   . THR   A 1 196 ? -2.888  9.613   25.449 1.00 125.68 ? 492 THR   A C   1 
ATOM   1495 O  O   . THR   A 1 196 ? -3.402  10.496  26.140 1.00 127.35 ? 492 THR   A O   1 
ATOM   1496 C  CB  . THR   A 1 196 ? -2.966  7.391   26.618 1.00 122.91 ? 492 THR   A CB  1 
ATOM   1497 O  OG1 . THR   A 1 196 ? -2.167  6.350   27.200 1.00 122.19 ? 492 THR   A OG1 1 
ATOM   1498 C  CG2 . THR   A 1 196 ? -3.805  6.800   25.487 1.00 114.54 ? 492 THR   A CG2 1 
ATOM   1499 N  N   . LEU   A 1 197 ? -3.005  9.560   24.123 1.00 122.46 ? 493 LEU   A N   1 
ATOM   1500 C  CA  . LEU   A 1 197 ? -3.894  10.427  23.365 1.00 119.27 ? 493 LEU   A CA  1 
ATOM   1501 C  C   . LEU   A 1 197 ? -5.077  9.620   22.841 1.00 112.84 ? 493 LEU   A C   1 
ATOM   1502 O  O   . LEU   A 1 197 ? -4.934  8.452   22.467 1.00 111.06 ? 493 LEU   A O   1 
ATOM   1503 C  CB  . LEU   A 1 197 ? -3.152  11.096  22.200 1.00 117.79 ? 493 LEU   A CB  1 
ATOM   1504 C  CG  . LEU   A 1 197 ? -3.897  12.168  21.403 1.00 120.95 ? 493 LEU   A CG  1 
ATOM   1505 C  CD1 . LEU   A 1 197 ? -4.608  13.145  22.329 1.00 119.20 ? 493 LEU   A CD1 1 
ATOM   1506 C  CD2 . LEU   A 1 197 ? -2.935  12.910  20.485 1.00 122.32 ? 493 LEU   A CD2 1 
ATOM   1507 N  N   . GLY   A 1 198 ? -6.251  10.247  22.844 1.00 113.49 ? 494 GLY   A N   1 
ATOM   1508 C  CA  . GLY   A 1 198 ? -7.435  9.582   22.329 1.00 106.88 ? 494 GLY   A CA  1 
ATOM   1509 C  C   . GLY   A 1 198 ? -7.997  8.593   23.335 1.00 97.60  ? 494 GLY   A C   1 
ATOM   1510 O  O   . GLY   A 1 198 ? -8.153  8.891   24.530 1.00 100.86 ? 494 GLY   A O   1 
ATOM   1511 N  N   . ASP   A 1 199 ? -8.293  7.385   22.859 1.00 94.59  ? 495 ASP   A N   1 
ATOM   1512 C  CA  . ASP   A 1 199 ? -8.922  6.371   23.700 1.00 91.33  ? 495 ASP   A CA  1 
ATOM   1513 C  C   . ASP   A 1 199 ? -7.903  5.313   24.103 1.00 90.35  ? 495 ASP   A C   1 
ATOM   1514 O  O   . ASP   A 1 199 ? -7.488  4.507   23.256 1.00 86.79  ? 495 ASP   A O   1 
ATOM   1515 C  CB  . ASP   A 1 199 ? -10.095 5.728   22.963 1.00 88.90  ? 495 ASP   A CB  1 
ATOM   1516 C  CG  . ASP   A 1 199 ? -11.054 5.021   23.893 1.00 85.60  ? 495 ASP   A CG  1 
ATOM   1517 O  OD1 . ASP   A 1 199 ? -10.656 4.697   25.045 1.00 85.90  ? 495 ASP   A OD1 1 
ATOM   1518 O  OD2 . ASP   A 1 199 ? -12.214 4.781   23.486 1.00 83.13  ? 495 ASP   A OD2 1 
ATOM   1519 N  N   . PRO   A 1 200 ? -7.489  5.251   25.373 1.00 90.70  ? 496 PRO   A N   1 
ATOM   1520 C  CA  . PRO   A 1 200 ? -6.468  4.260   25.758 1.00 90.36  ? 496 PRO   A CA  1 
ATOM   1521 C  C   . PRO   A 1 200 ? -6.906  2.818   25.552 1.00 86.25  ? 496 PRO   A C   1 
ATOM   1522 O  O   . PRO   A 1 200 ? -6.047  1.946   25.375 1.00 86.57  ? 496 PRO   A O   1 
ATOM   1523 C  CB  . PRO   A 1 200 ? -6.219  4.568   27.242 1.00 88.82  ? 496 PRO   A CB  1 
ATOM   1524 C  CG  . PRO   A 1 200 ? -6.713  5.990   27.429 1.00 89.76  ? 496 PRO   A CG  1 
ATOM   1525 C  CD  . PRO   A 1 200 ? -7.900  6.087   26.514 1.00 86.79  ? 496 PRO   A CD  1 
ATOM   1526 N  N   . ALA   A 1 201 ? -8.211  2.543   25.541 1.00 85.00  ? 497 ALA   A N   1 
ATOM   1527 C  CA  . ALA   A 1 201 ? -8.689  1.177   25.346 1.00 84.44  ? 497 ALA   A CA  1 
ATOM   1528 C  C   . ALA   A 1 201 ? -8.279  0.601   23.994 1.00 83.80  ? 497 ALA   A C   1 
ATOM   1529 O  O   . ALA   A 1 201 ? -8.238  -0.622  23.831 1.00 85.20  ? 497 ALA   A O   1 
ATOM   1530 C  CB  . ALA   A 1 201 ? -10.211 1.132   25.484 1.00 83.08  ? 497 ALA   A CB  1 
ATOM   1531 N  N   . ASN   A 1 202 ? -7.973  1.448   23.014 1.00 84.89  ? 498 ASN   A N   1 
ATOM   1532 C  CA  . ASN   A 1 202 ? -7.753  0.985   21.649 1.00 87.58  ? 498 ASN   A CA  1 
ATOM   1533 C  C   . ASN   A 1 202 ? -6.286  1.037   21.241 1.00 91.21  ? 498 ASN   A C   1 
ATOM   1534 O  O   . ASN   A 1 202 ? -5.976  0.928   20.053 1.00 93.36  ? 498 ASN   A O   1 
ATOM   1535 C  CB  . ASN   A 1 202 ? -8.602  1.804   20.678 1.00 84.86  ? 498 ASN   A CB  1 
ATOM   1536 C  CG  . ASN   A 1 202 ? -10.083 1.748   21.011 1.00 80.31  ? 498 ASN   A CG  1 
ATOM   1537 O  OD1 . ASN   A 1 202 ? -10.637 0.678   21.261 1.00 78.67  ? 498 ASN   A OD1 1 
ATOM   1538 N  ND2 . ASN   A 1 202 ? -10.733 2.904   21.015 1.00 80.74  ? 498 ASN   A ND2 1 
ATOM   1539 N  N   . VAL   A 1 203 ? -5.374  1.177   22.203 1.00 94.22  ? 499 VAL   A N   1 
ATOM   1540 C  CA  . VAL   A 1 203 ? -3.981  1.443   21.855 1.00 95.68  ? 499 VAL   A CA  1 
ATOM   1541 C  C   . VAL   A 1 203 ? -3.346  0.230   21.190 1.00 101.81 ? 499 VAL   A C   1 
ATOM   1542 O  O   . VAL   A 1 203 ? -2.520  0.369   20.283 1.00 103.61 ? 499 VAL   A O   1 
ATOM   1543 C  CB  . VAL   A 1 203 ? -3.197  1.889   23.102 1.00 96.03  ? 499 VAL   A CB  1 
ATOM   1544 C  CG1 . VAL   A 1 203 ? -1.711  1.975   22.801 1.00 108.65 ? 499 VAL   A CG1 1 
ATOM   1545 C  CG2 . VAL   A 1 203 ? -3.710  3.230   23.580 1.00 97.54  ? 499 VAL   A CG2 1 
ATOM   1546 N  N   . GLN   A 1 204 ? -3.707  -0.977  21.625 1.00 97.76  ? 500 GLN   A N   1 
ATOM   1547 C  CA  . GLN   A 1 204 ? -3.204  -2.157  20.930 1.00 102.53 ? 500 GLN   A CA  1 
ATOM   1548 C  C   . GLN   A 1 204 ? -3.821  -2.272  19.545 1.00 100.88 ? 500 GLN   A C   1 
ATOM   1549 O  O   . GLN   A 1 204 ? -3.123  -2.574  18.568 1.00 102.71 ? 500 GLN   A O   1 
ATOM   1550 C  CB  . GLN   A 1 204 ? -3.477  -3.427  21.736 1.00 106.87 ? 500 GLN   A CB  1 
ATOM   1551 C  CG  . GLN   A 1 204 ? -2.818  -4.673  21.133 1.00 106.95 ? 500 GLN   A CG  1 
ATOM   1552 C  CD  . GLN   A 1 204 ? -3.286  -5.973  21.769 1.00 111.84 ? 500 GLN   A CD  1 
ATOM   1553 O  OE1 . GLN   A 1 204 ? -4.487  -6.214  21.915 1.00 109.58 ? 500 GLN   A OE1 1 
ATOM   1554 N  NE2 . GLN   A 1 204 ? -2.334  -6.822  22.149 1.00 118.25 ? 500 GLN   A NE2 1 
ATOM   1555 N  N   . PHE   A 1 205 ? -5.129  -2.023  19.434 1.00 98.57  ? 501 PHE   A N   1 
ATOM   1556 C  CA  . PHE   A 1 205 ? -5.767  -2.084  18.122 1.00 95.09  ? 501 PHE   A CA  1 
ATOM   1557 C  C   . PHE   A 1 205 ? -5.241  -0.991  17.199 1.00 96.28  ? 501 PHE   A C   1 
ATOM   1558 O  O   . PHE   A 1 205 ? -5.064  -1.219  15.992 1.00 94.41  ? 501 PHE   A O   1 
ATOM   1559 C  CB  . PHE   A 1 205 ? -7.286  -1.976  18.250 1.00 90.85  ? 501 PHE   A CB  1 
ATOM   1560 C  CG  . PHE   A 1 205 ? -7.998  -2.063  16.938 1.00 94.39  ? 501 PHE   A CG  1 
ATOM   1561 C  CD1 . PHE   A 1 205 ? -8.159  -3.284  16.305 1.00 90.65  ? 501 PHE   A CD1 1 
ATOM   1562 C  CD2 . PHE   A 1 205 ? -8.480  -0.921  16.314 1.00 90.80  ? 501 PHE   A CD2 1 
ATOM   1563 C  CE1 . PHE   A 1 205 ? -8.801  -3.367  15.091 1.00 85.38  ? 501 PHE   A CE1 1 
ATOM   1564 C  CE2 . PHE   A 1 205 ? -9.128  -1.001  15.101 1.00 86.45  ? 501 PHE   A CE2 1 
ATOM   1565 C  CZ  . PHE   A 1 205 ? -9.283  -2.226  14.485 1.00 84.70  ? 501 PHE   A CZ  1 
ATOM   1566 N  N   . THR   A 1 206 ? -5.000  0.208   17.737 1.00 97.36  ? 502 THR   A N   1 
ATOM   1567 C  CA  . THR   A 1 206 ? -4.492  1.283   16.889 1.00 100.05 ? 502 THR   A CA  1 
ATOM   1568 C  C   . THR   A 1 206 ? -3.105  0.943   16.356 1.00 105.46 ? 502 THR   A C   1 
ATOM   1569 O  O   . THR   A 1 206 ? -2.777  1.265   15.210 1.00 103.49 ? 502 THR   A O   1 
ATOM   1570 C  CB  . THR   A 1 206 ? -4.475  2.609   17.654 1.00 98.30  ? 502 THR   A CB  1 
ATOM   1571 O  OG1 . THR   A 1 206 ? -5.810  2.943   18.056 1.00 94.36  ? 502 THR   A OG1 1 
ATOM   1572 C  CG2 . THR   A 1 206 ? -3.919  3.731   16.770 1.00 99.74  ? 502 THR   A CG2 1 
ATOM   1573 N  N   . GLU   A 1 207 ? -2.285  0.269   17.165 1.00 108.75 ? 503 GLU   A N   1 
ATOM   1574 C  CA  . GLU   A 1 207 ? -0.967  -0.143  16.689 1.00 112.75 ? 503 GLU   A CA  1 
ATOM   1575 C  C   . GLU   A 1 207 ? -1.078  -1.244  15.642 1.00 110.40 ? 503 GLU   A C   1 
ATOM   1576 O  O   . GLU   A 1 207 ? -0.269  -1.302  14.708 1.00 114.43 ? 503 GLU   A O   1 
ATOM   1577 C  CB  . GLU   A 1 207 ? -0.103  -0.600  17.865 1.00 117.07 ? 503 GLU   A CB  1 
ATOM   1578 C  CG  . GLU   A 1 207 ? 0.397   0.539   18.729 1.00 126.77 ? 503 GLU   A CG  1 
ATOM   1579 C  CD  . GLU   A 1 207 ? 0.833   0.074   20.108 1.00 132.59 ? 503 GLU   A CD  1 
ATOM   1580 O  OE1 . GLU   A 1 207 ? 0.845   -1.155  20.342 1.00 132.08 ? 503 GLU   A OE1 1 
ATOM   1581 O  OE2 . GLU   A 1 207 ? 1.157   0.934   20.958 1.00 136.53 ? 503 GLU   A OE2 1 
ATOM   1582 N  N   . ILE   A 1 208 ? -2.071  -2.125  15.783 1.00 105.25 ? 504 ILE   A N   1 
ATOM   1583 C  CA  . ILE   A 1 208 ? -2.283  -3.183  14.796 1.00 103.37 ? 504 ILE   A CA  1 
ATOM   1584 C  C   . ILE   A 1 208 ? -2.622  -2.577  13.439 1.00 103.77 ? 504 ILE   A C   1 
ATOM   1585 O  O   . ILE   A 1 208 ? -2.072  -2.973  12.406 1.00 104.02 ? 504 ILE   A O   1 
ATOM   1586 C  CB  . ILE   A 1 208 ? -3.380  -4.150  15.274 1.00 96.80  ? 504 ILE   A CB  1 
ATOM   1587 C  CG1 . ILE   A 1 208 ? -2.818  -5.137  16.290 1.00 93.31  ? 504 ILE   A CG1 1 
ATOM   1588 C  CG2 . ILE   A 1 208 ? -3.980  -4.900  14.104 1.00 93.34  ? 504 ILE   A CG2 1 
ATOM   1589 C  CD1 . ILE   A 1 208 ? -3.888  -5.966  16.964 1.00 96.39  ? 504 ILE   A CD1 1 
ATOM   1590 N  N   . CYS   A 1 209 ? -3.545  -1.612  13.426 1.00 103.10 ? 505 CYS   A N   1 
ATOM   1591 C  CA  . CYS   A 1 209 ? -3.836  -0.872  12.205 1.00 101.28 ? 505 CYS   A CA  1 
ATOM   1592 C  C   . CYS   A 1 209 ? -2.575  -0.237  11.635 1.00 107.83 ? 505 CYS   A C   1 
ATOM   1593 O  O   . CYS   A 1 209 ? -2.359  -0.245  10.416 1.00 108.49 ? 505 CYS   A O   1 
ATOM   1594 C  CB  . CYS   A 1 209 ? -4.892  0.197   12.481 1.00 97.56  ? 505 CYS   A CB  1 
ATOM   1595 S  SG  . CYS   A 1 209 ? -6.501  -0.457  12.950 1.00 90.84  ? 505 CYS   A SG  1 
ATOM   1596 N  N   . ILE   A 1 210 ? -1.722  0.309   12.504 1.00 106.08 ? 506 ILE   A N   1 
ATOM   1597 C  CA  . ILE   A 1 210 ? -0.486  0.924   12.029 1.00 109.56 ? 506 ILE   A CA  1 
ATOM   1598 C  C   . ILE   A 1 210 ? 0.453   -0.136  11.458 1.00 110.07 ? 506 ILE   A C   1 
ATOM   1599 O  O   . ILE   A 1 210 ? 1.130   0.093   10.447 1.00 108.26 ? 506 ILE   A O   1 
ATOM   1600 C  CB  . ILE   A 1 210 ? 0.160   1.736   13.166 1.00 109.70 ? 506 ILE   A CB  1 
ATOM   1601 C  CG1 . ILE   A 1 210 ? -0.707  2.953   13.489 1.00 108.76 ? 506 ILE   A CG1 1 
ATOM   1602 C  CG2 . ILE   A 1 210 ? 1.565   2.186   12.801 1.00 114.70 ? 506 ILE   A CG2 1 
ATOM   1603 C  CD1 . ILE   A 1 210 ? -0.154  3.802   14.630 1.00 116.18 ? 506 ILE   A CD1 1 
ATOM   1604 N  N   . GLN   A 1 211 ? 0.493   -1.317  12.084 1.00 109.65 ? 507 GLN   A N   1 
ATOM   1605 C  CA  . GLN   A 1 211 ? 1.288   -2.422  11.553 1.00 110.90 ? 507 GLN   A CA  1 
ATOM   1606 C  C   . GLN   A 1 211 ? 0.776   -2.879  10.193 1.00 110.43 ? 507 GLN   A C   1 
ATOM   1607 O  O   . GLN   A 1 211 ? 1.565   -3.314  9.345  1.00 109.31 ? 507 GLN   A O   1 
ATOM   1608 C  CB  . GLN   A 1 211 ? 1.289   -3.589  12.545 1.00 111.90 ? 507 GLN   A CB  1 
ATOM   1609 C  CG  . GLN   A 1 211 ? 2.161   -3.371  13.776 1.00 113.47 ? 507 GLN   A CG  1 
ATOM   1610 C  CD  . GLN   A 1 211 ? 3.483   -4.129  13.709 1.00 117.00 ? 507 GLN   A CD  1 
ATOM   1611 O  OE1 . GLN   A 1 211 ? 3.541   -5.252  13.207 1.00 118.87 ? 507 GLN   A OE1 1 
ATOM   1612 N  NE2 . GLN   A 1 211 ? 4.551   -3.515  14.219 1.00 118.07 ? 507 GLN   A NE2 1 
ATOM   1613 N  N   . GLN   A 1 212 ? -0.536  -2.795  9.967  1.00 109.12 ? 508 GLN   A N   1 
ATOM   1614 C  CA  . GLN   A 1 212 ? -1.114  -3.135  8.672  1.00 109.61 ? 508 GLN   A CA  1 
ATOM   1615 C  C   . GLN   A 1 212 ? -1.098  -1.969  7.696  1.00 109.28 ? 508 GLN   A C   1 
ATOM   1616 O  O   . GLN   A 1 212 ? -1.540  -2.130  6.550  1.00 108.04 ? 508 GLN   A O   1 
ATOM   1617 C  CB  . GLN   A 1 212 ? -2.546  -3.647  8.851  1.00 108.33 ? 508 GLN   A CB  1 
ATOM   1618 C  CG  . GLN   A 1 212 ? -2.623  -4.945  9.628  1.00 108.44 ? 508 GLN   A CG  1 
ATOM   1619 C  CD  . GLN   A 1 212 ? -1.651  -5.979  9.095  1.00 114.40 ? 508 GLN   A CD  1 
ATOM   1620 O  OE1 . GLN   A 1 212 ? -1.602  -6.238  7.889  1.00 115.12 ? 508 GLN   A OE1 1 
ATOM   1621 N  NE2 . GLN   A 1 212 ? -0.859  -6.564  9.987  1.00 115.20 ? 508 GLN   A NE2 1 
ATOM   1622 N  N   . GLY   A 1 213 ? -0.603  -0.807  8.113  1.00 111.21 ? 509 GLY   A N   1 
ATOM   1623 C  CA  . GLY   A 1 213 ? -0.398  0.306   7.213  1.00 108.40 ? 509 GLY   A CA  1 
ATOM   1624 C  C   . GLY   A 1 213 ? -1.239  1.539   7.462  1.00 110.21 ? 509 GLY   A C   1 
ATOM   1625 O  O   . GLY   A 1 213 ? -1.186  2.468   6.648  1.00 112.91 ? 509 GLY   A O   1 
ATOM   1626 N  N   . TRP   A 1 214 ? -2.004  1.597   8.553  1.00 111.86 ? 510 TRP   A N   1 
ATOM   1627 C  CA  . TRP   A 1 214 ? -2.819  2.780   8.798  1.00 112.02 ? 510 TRP   A CA  1 
ATOM   1628 C  C   . TRP   A 1 214 ? -1.924  3.986   9.027  1.00 114.67 ? 510 TRP   A C   1 
ATOM   1629 O  O   . TRP   A 1 214 ? -0.973  3.935   9.815  1.00 113.22 ? 510 TRP   A O   1 
ATOM   1630 C  CB  . TRP   A 1 214 ? -3.756  2.590   9.990  1.00 106.73 ? 510 TRP   A CB  1 
ATOM   1631 C  CG  . TRP   A 1 214 ? -4.791  3.693   10.078 1.00 106.04 ? 510 TRP   A CG  1 
ATOM   1632 C  CD1 . TRP   A 1 214 ? -5.570  4.152   9.060  1.00 105.21 ? 510 TRP   A CD1 1 
ATOM   1633 C  CD2 . TRP   A 1 214 ? -5.146  4.470   11.237 1.00 105.77 ? 510 TRP   A CD2 1 
ATOM   1634 N  NE1 . TRP   A 1 214 ? -6.388  5.161   9.504  1.00 104.11 ? 510 TRP   A NE1 1 
ATOM   1635 C  CE2 . TRP   A 1 214 ? -6.151  5.376   10.836 1.00 103.45 ? 510 TRP   A CE2 1 
ATOM   1636 C  CE3 . TRP   A 1 214 ? -4.718  4.482   12.570 1.00 106.45 ? 510 TRP   A CE3 1 
ATOM   1637 C  CZ2 . TRP   A 1 214 ? -6.730  6.290   11.713 1.00 100.48 ? 510 TRP   A CZ2 1 
ATOM   1638 C  CZ3 . TRP   A 1 214 ? -5.301  5.393   13.452 1.00 102.52 ? 510 TRP   A CZ3 1 
ATOM   1639 C  CH2 . TRP   A 1 214 ? -6.297  6.280   13.018 1.00 104.92 ? 510 TRP   A CH2 1 
ATOM   1640 N  N   . LYS   A 1 215 ? -2.208  5.057   8.300  1.00 118.21 ? 511 LYS   A N   1 
ATOM   1641 C  CA  . LYS   A 1 215 ? -1.525  6.325   8.490  1.00 122.38 ? 511 LYS   A CA  1 
ATOM   1642 C  C   . LYS   A 1 215 ? -2.339  7.128   9.496  1.00 115.48 ? 511 LYS   A C   1 
ATOM   1643 O  O   . LYS   A 1 215 ? -3.426  7.623   9.180  1.00 114.06 ? 511 LYS   A O   1 
ATOM   1644 C  CB  . LYS   A 1 215 ? -1.360  7.046   7.156  1.00 126.36 ? 511 LYS   A CB  1 
ATOM   1645 C  CG  . LYS   A 1 215 ? -0.518  6.266   6.146  1.00 133.06 ? 511 LYS   A CG  1 
ATOM   1646 C  CD  . LYS   A 1 215 ? 0.953   6.693   6.166  1.00 141.43 ? 511 LYS   A CD  1 
ATOM   1647 C  CE  . LYS   A 1 215 ? 1.724   6.086   7.332  1.00 144.20 ? 511 LYS   A CE  1 
ATOM   1648 N  NZ  . LYS   A 1 215 ? 2.807   6.988   7.827  1.00 154.36 ? 511 LYS   A NZ  1 
ATOM   1649 N  N   . ALA   A 1 216 ? -1.826  7.234   10.705 1.00 119.27 ? 512 ALA   A N   1 
ATOM   1650 C  CA  . ALA   A 1 216 ? -2.611  7.749   11.817 1.00 112.61 ? 512 ALA   A CA  1 
ATOM   1651 C  C   . ALA   A 1 216 ? -2.541  9.269   11.862 1.00 116.30 ? 512 ALA   A C   1 
ATOM   1652 O  O   . ALA   A 1 216 ? -1.443  9.836   11.810 1.00 119.16 ? 512 ALA   A O   1 
ATOM   1653 C  CB  . ALA   A 1 216 ? -2.112  7.173   13.131 1.00 115.35 ? 512 ALA   A CB  1 
ATOM   1654 N  N   . PRO   A 1 217 ? -3.676  9.952   11.951 1.00 115.07 ? 513 PRO   A N   1 
ATOM   1655 C  CA  . PRO   A 1 217 ? -3.651  11.402  12.184 1.00 117.74 ? 513 PRO   A CA  1 
ATOM   1656 C  C   . PRO   A 1 217 ? -3.393  11.773  13.637 1.00 123.39 ? 513 PRO   A C   1 
ATOM   1657 O  O   . PRO   A 1 217 ? -3.989  12.739  14.125 1.00 126.25 ? 513 PRO   A O   1 
ATOM   1658 C  CB  . PRO   A 1 217 ? -5.052  11.846  11.746 1.00 119.25 ? 513 PRO   A CB  1 
ATOM   1659 C  CG  . PRO   A 1 217 ? -5.905  10.629  11.916 1.00 116.48 ? 513 PRO   A CG  1 
ATOM   1660 C  CD  . PRO   A 1 217 ? -5.023  9.456   11.619 1.00 114.24 ? 513 PRO   A CD  1 
ATOM   1661 N  N   . ARG   A 1 218 ? -2.494  11.034  14.311 1.00 125.52 ? 514 ARG   A N   1 
ATOM   1662 C  CA  . ARG   A 1 218 ? -2.237  11.069  15.756 1.00 124.83 ? 514 ARG   A CA  1 
ATOM   1663 C  C   . ARG   A 1 218 ? -2.904  12.216  16.502 1.00 123.92 ? 514 ARG   A C   1 
ATOM   1664 O  O   . ARG   A 1 218 ? -2.222  13.104  17.026 1.00 131.23 ? 514 ARG   A O   1 
ATOM   1665 C  CB  . ARG   A 1 218 ? -0.730  11.115  16.032 1.00 130.27 ? 514 ARG   A CB  1 
ATOM   1666 C  CG  . ARG   A 1 218 ? -0.015  9.816   15.735 1.00 129.50 ? 514 ARG   A CG  1 
ATOM   1667 C  CD  . ARG   A 1 218 ? 1.003   9.473   16.809 1.00 134.11 ? 514 ARG   A CD  1 
ATOM   1668 N  NE  . ARG   A 1 218 ? 1.093   8.027   16.970 1.00 137.73 ? 514 ARG   A NE  1 
ATOM   1669 C  CZ  . ARG   A 1 218 ? 1.982   7.255   16.361 1.00 140.00 ? 514 ARG   A CZ  1 
ATOM   1670 N  NH1 . ARG   A 1 218 ? 2.934   7.767   15.601 1.00 147.59 ? 514 ARG   A NH1 1 
ATOM   1671 N  NH2 . ARG   A 1 218 ? 1.912   5.935   16.518 1.00 140.30 ? 514 ARG   A NH2 1 
ATOM   1672 N  N   . GLY   A 1 219 ? -4.235  12.203  16.548 1.00 122.13 ? 515 GLY   A N   1 
ATOM   1673 C  CA  . GLY   A 1 219 ? -4.984  13.157  17.342 1.00 123.96 ? 515 GLY   A CA  1 
ATOM   1674 C  C   . GLY   A 1 219 ? -5.859  12.476  18.373 1.00 121.85 ? 515 GLY   A C   1 
ATOM   1675 O  O   . GLY   A 1 219 ? -5.612  11.328  18.750 1.00 119.13 ? 515 GLY   A O   1 
ATOM   1676 N  N   . ARG   A 1 220 ? -6.900  13.164  18.825 1.00 126.34 ? 516 ARG   A N   1 
ATOM   1677 C  CA  . ARG   A 1 220 ? -7.798  12.617  19.851 1.00 124.69 ? 516 ARG   A CA  1 
ATOM   1678 C  C   . ARG   A 1 220 ? -8.884  11.758  19.220 1.00 120.19 ? 516 ARG   A C   1 
ATOM   1679 O  O   . ARG   A 1 220 ? -8.800  10.519  19.223 1.00 119.34 ? 516 ARG   A O   1 
ATOM   1680 C  CB  . ARG   A 1 220 ? -8.412  13.758  20.666 1.00 128.09 ? 516 ARG   A CB  1 
ATOM   1681 C  CG  . ARG   A 1 220 ? -9.238  13.297  21.845 1.00 123.49 ? 516 ARG   A CG  1 
ATOM   1682 C  CD  . ARG   A 1 220 ? -8.411  13.245  23.108 1.00 124.32 ? 516 ARG   A CD  1 
ATOM   1683 N  NE  . ARG   A 1 220 ? -8.861  14.228  24.087 1.00 128.98 ? 516 ARG   A NE  1 
ATOM   1684 C  CZ  . ARG   A 1 220 ? -8.618  14.158  25.389 1.00 131.00 ? 516 ARG   A CZ  1 
ATOM   1685 N  NH1 . ARG   A 1 220 ? -7.910  13.168  25.908 1.00 128.82 ? 516 ARG   A NH1 1 
ATOM   1686 N  NH2 . ARG   A 1 220 ? -9.107  15.101  26.190 1.00 132.87 ? 516 ARG   A NH2 1 
ATOM   1687 N  N   . PHE   A 1 221 ? -9.897  12.396  18.644 1.00 111.83 ? 517 PHE   A N   1 
ATOM   1688 C  CA  . PHE   A 1 221 ? -11.095 11.707  18.170 1.00 104.01 ? 517 PHE   A CA  1 
ATOM   1689 C  C   . PHE   A 1 221 ? -10.957 11.341  16.689 1.00 104.96 ? 517 PHE   A C   1 
ATOM   1690 O  O   . PHE   A 1 221 ? -11.700 11.802  15.814 1.00 104.82 ? 517 PHE   A O   1 
ATOM   1691 C  CB  . PHE   A 1 221 ? -12.329 12.565  18.430 1.00 101.11 ? 517 PHE   A CB  1 
ATOM   1692 C  CG  . PHE   A 1 221 ? -12.530 12.930  19.886 1.00 102.84 ? 517 PHE   A CG  1 
ATOM   1693 C  CD1 . PHE   A 1 221 ? -12.894 11.971  20.808 1.00 97.70  ? 517 PHE   A CD1 1 
ATOM   1694 C  CD2 . PHE   A 1 221 ? -12.373 14.236  20.318 1.00 106.10 ? 517 PHE   A CD2 1 
ATOM   1695 C  CE1 . PHE   A 1 221 ? -13.101 12.303  22.127 1.00 101.14 ? 517 PHE   A CE1 1 
ATOM   1696 C  CE2 . PHE   A 1 221 ? -12.572 14.573  21.642 1.00 108.27 ? 517 PHE   A CE2 1 
ATOM   1697 C  CZ  . PHE   A 1 221 ? -12.930 13.603  22.549 1.00 102.78 ? 517 PHE   A CZ  1 
ATOM   1698 N  N   . ASP   A 1 222 ? -9.966  10.493  16.416 1.00 104.33 ? 518 ASP   A N   1 
ATOM   1699 C  CA  . ASP   A 1 222 ? -9.718  9.971   15.079 1.00 100.80 ? 518 ASP   A CA  1 
ATOM   1700 C  C   . ASP   A 1 222 ? -10.478 8.663   14.920 1.00 96.74  ? 518 ASP   A C   1 
ATOM   1701 O  O   . ASP   A 1 222 ? -10.191 7.687   15.622 1.00 92.85  ? 518 ASP   A O   1 
ATOM   1702 C  CB  . ASP   A 1 222 ? -8.226  9.738   14.856 1.00 103.53 ? 518 ASP   A CB  1 
ATOM   1703 C  CG  . ASP   A 1 222 ? -7.398  10.962  15.143 1.00 111.49 ? 518 ASP   A CG  1 
ATOM   1704 O  OD1 . ASP   A 1 222 ? -7.984  12.053  15.305 1.00 113.84 ? 518 ASP   A OD1 1 
ATOM   1705 O  OD2 . ASP   A 1 222 ? -6.157  10.833  15.211 1.00 114.98 ? 518 ASP   A OD2 1 
ATOM   1706 N  N   . VAL   A 1 223 ? -11.444 8.642   14.000 1.00 93.93  ? 519 VAL   A N   1 
ATOM   1707 C  CA  . VAL   A 1 223 ? -12.182 7.415   13.740 1.00 88.88  ? 519 VAL   A CA  1 
ATOM   1708 C  C   . VAL   A 1 223 ? -11.206 6.362   13.239 1.00 88.24  ? 519 VAL   A C   1 
ATOM   1709 O  O   . VAL   A 1 223 ? -10.453 6.598   12.285 1.00 90.07  ? 519 VAL   A O   1 
ATOM   1710 C  CB  . VAL   A 1 223 ? -13.305 7.679   12.724 1.00 89.24  ? 519 VAL   A CB  1 
ATOM   1711 C  CG1 . VAL   A 1 223 ? -14.194 6.448   12.550 1.00 82.00  ? 519 VAL   A CG1 1 
ATOM   1712 C  CG2 . VAL   A 1 223 ? -14.118 8.906   13.140 1.00 92.16  ? 519 VAL   A CG2 1 
ATOM   1713 N  N   . LEU   A 1 224 ? -11.194 5.203   13.889 1.00 84.18  ? 520 LEU   A N   1 
ATOM   1714 C  CA  . LEU   A 1 224 ? -10.329 4.126   13.438 1.00 84.87  ? 520 LEU   A CA  1 
ATOM   1715 C  C   . LEU   A 1 224 ? -10.847 3.520   12.133 1.00 83.96  ? 520 LEU   A C   1 
ATOM   1716 O  O   . LEU   A 1 224 ? -12.048 3.547   11.861 1.00 84.43  ? 520 LEU   A O   1 
ATOM   1717 C  CB  . LEU   A 1 224 ? -10.230 3.035   14.493 1.00 82.80  ? 520 LEU   A CB  1 
ATOM   1718 C  CG  . LEU   A 1 224 ? -9.337  3.323   15.692 1.00 86.14  ? 520 LEU   A CG  1 
ATOM   1719 C  CD1 . LEU   A 1 224 ? -10.022 2.744   16.917 1.00 80.57  ? 520 LEU   A CD1 1 
ATOM   1720 C  CD2 . LEU   A 1 224 ? -7.934  2.735   15.506 1.00 87.08  ? 520 LEU   A CD2 1 
ATOM   1721 N  N   . PRO   A 1 225 ? -9.962  2.957   11.320 1.00 83.54  ? 521 PRO   A N   1 
ATOM   1722 C  CA  . PRO   A 1 225 ? -10.407 2.236   10.127 1.00 83.25  ? 521 PRO   A CA  1 
ATOM   1723 C  C   . PRO   A 1 225 ? -10.926 0.855   10.491 1.00 81.41  ? 521 PRO   A C   1 
ATOM   1724 O  O   . PRO   A 1 225 ? -10.642 0.314   11.561 1.00 80.26  ? 521 PRO   A O   1 
ATOM   1725 C  CB  . PRO   A 1 225 ? -9.129  2.130   9.290  1.00 88.11  ? 521 PRO   A CB  1 
ATOM   1726 C  CG  . PRO   A 1 225 ? -8.050  2.040   10.359 1.00 89.51  ? 521 PRO   A CG  1 
ATOM   1727 C  CD  . PRO   A 1 225 ? -8.493  2.993   11.422 1.00 88.36  ? 521 PRO   A CD  1 
ATOM   1728 N  N   . LEU   A 1 226 ? -11.707 0.295   9.575  1.00 79.18  ? 522 LEU   A N   1 
ATOM   1729 C  CA  . LEU   A 1 226 ? -12.148 -1.086  9.698  1.00 77.86  ? 522 LEU   A CA  1 
ATOM   1730 C  C   . LEU   A 1 226 ? -11.018 -2.037  9.335  1.00 77.42  ? 522 LEU   A C   1 
ATOM   1731 O  O   . LEU   A 1 226 ? -10.322 -1.843  8.338  1.00 80.42  ? 522 LEU   A O   1 
ATOM   1732 C  CB  . LEU   A 1 226 ? -13.348 -1.350  8.792  1.00 74.95  ? 522 LEU   A CB  1 
ATOM   1733 C  CG  . LEU   A 1 226 ? -14.648 -0.620  9.116  1.00 71.57  ? 522 LEU   A CG  1 
ATOM   1734 C  CD1 . LEU   A 1 226 ? -15.638 -0.777  7.957  1.00 71.56  ? 522 LEU   A CD1 1 
ATOM   1735 C  CD2 . LEU   A 1 226 ? -15.243 -1.130  10.421 1.00 71.92  ? 522 LEU   A CD2 1 
ATOM   1736 N  N   . LEU   A 1 227 ? -10.828 -3.057  10.164 1.00 76.66  ? 523 LEU   A N   1 
ATOM   1737 C  CA  . LEU   A 1 227 ? -9.935  -4.166  9.851  1.00 76.89  ? 523 LEU   A CA  1 
ATOM   1738 C  C   . LEU   A 1 227 ? -10.814 -5.382  9.626  1.00 76.25  ? 523 LEU   A C   1 
ATOM   1739 O  O   . LEU   A 1 227 ? -11.362 -5.936  10.583 1.00 71.76  ? 523 LEU   A O   1 
ATOM   1740 C  CB  . LEU   A 1 227 ? -8.935  -4.418  10.974 1.00 76.53  ? 523 LEU   A CB  1 
ATOM   1741 C  CG  . LEU   A 1 227 ? -7.448  -4.246  10.672 1.00 80.18  ? 523 LEU   A CG  1 
ATOM   1742 C  CD1 . LEU   A 1 227 ? -6.634  -4.923  11.757 1.00 85.69  ? 523 LEU   A CD1 1 
ATOM   1743 C  CD2 . LEU   A 1 227 ? -7.074  -4.780  9.294  1.00 83.83  ? 523 LEU   A CD2 1 
ATOM   1744 N  N   . LEU   A 1 228 ? -10.952 -5.787  8.367  1.00 75.97  ? 524 LEU   A N   1 
ATOM   1745 C  CA  . LEU   A 1 228 ? -11.932 -6.783  7.957  1.00 73.81  ? 524 LEU   A CA  1 
ATOM   1746 C  C   . LEU   A 1 228 ? -11.222 -8.020  7.425  1.00 75.92  ? 524 LEU   A C   1 
ATOM   1747 O  O   . LEU   A 1 228 ? -10.394 -7.924  6.513  1.00 78.21  ? 524 LEU   A O   1 
ATOM   1748 C  CB  . LEU   A 1 228 ? -12.870 -6.208  6.897  1.00 73.03  ? 524 LEU   A CB  1 
ATOM   1749 C  CG  . LEU   A 1 228 ? -13.450 -4.858  7.318  1.00 72.87  ? 524 LEU   A CG  1 
ATOM   1750 C  CD1 . LEU   A 1 228 ? -14.317 -4.309  6.219  1.00 68.96  ? 524 LEU   A CD1 1 
ATOM   1751 C  CD2 . LEU   A 1 228 ? -14.230 -4.970  8.634  1.00 68.47  ? 524 LEU   A CD2 1 
ATOM   1752 N  N   . GLN   A 1 229 ? -11.558 -9.170  8.002  1.00 73.68  ? 525 GLN   A N   1 
ATOM   1753 C  CA  . GLN   A 1 229 ? -11.038 -10.474 7.615  1.00 76.30  ? 525 GLN   A CA  1 
ATOM   1754 C  C   . GLN   A 1 229 ? -12.176 -11.269 6.982  1.00 73.68  ? 525 GLN   A C   1 
ATOM   1755 O  O   . GLN   A 1 229 ? -13.222 -11.477 7.613  1.00 71.07  ? 525 GLN   A O   1 
ATOM   1756 C  CB  . GLN   A 1 229 ? -10.468 -11.207 8.833  1.00 75.36  ? 525 GLN   A CB  1 
ATOM   1757 C  CG  . GLN   A 1 229 ? -10.428 -12.730 8.744  1.00 76.44  ? 525 GLN   A CG  1 
ATOM   1758 C  CD  . GLN   A 1 229 ? -9.982  -13.390 10.049 1.00 83.63  ? 525 GLN   A CD  1 
ATOM   1759 O  OE1 . GLN   A 1 229 ? -9.790  -12.720 11.066 1.00 79.78  ? 525 GLN   A OE1 1 
ATOM   1760 N  NE2 . GLN   A 1 229 ? -9.822  -14.709 10.023 1.00 87.07  ? 525 GLN   A NE2 1 
ATOM   1761 N  N   . ALA   A 1 230 ? -11.975 -11.701 5.744  1.00 77.00  ? 526 ALA   A N   1 
ATOM   1762 C  CA  . ALA   A 1 230 ? -12.970 -12.466 5.007  1.00 76.33  ? 526 ALA   A CA  1 
ATOM   1763 C  C   . ALA   A 1 230 ? -12.433 -13.863 4.736  1.00 79.71  ? 526 ALA   A C   1 
ATOM   1764 O  O   . ALA   A 1 230 ? -11.275 -14.020 4.336  1.00 81.69  ? 526 ALA   A O   1 
ATOM   1765 C  CB  . ALA   A 1 230 ? -13.330 -11.783 3.684  1.00 75.23  ? 526 ALA   A CB  1 
ATOM   1766 N  N   . ASN   A 1 231 ? -13.280 -14.865 4.968  1.00 79.88  ? 527 ASN   A N   1 
ATOM   1767 C  CA  . ASN   A 1 231 ? -12.974 -16.269 4.692  1.00 82.55  ? 527 ASN   A CA  1 
ATOM   1768 C  C   . ASN   A 1 231 ? -11.635 -16.679 5.298  1.00 88.50  ? 527 ASN   A C   1 
ATOM   1769 O  O   . ASN   A 1 231 ? -10.841 -17.395 4.685  1.00 89.68  ? 527 ASN   A O   1 
ATOM   1770 C  CB  . ASN   A 1 231 ? -13.005 -16.554 3.191  1.00 82.66  ? 527 ASN   A CB  1 
ATOM   1771 C  CG  . ASN   A 1 231 ? -13.219 -18.018 2.891  1.00 85.17  ? 527 ASN   A CG  1 
ATOM   1772 O  OD1 . ASN   A 1 231 ? -14.051 -18.671 3.521  1.00 86.44  ? 527 ASN   A OD1 1 
ATOM   1773 N  ND2 . ASN   A 1 231 ? -12.463 -18.548 1.936  1.00 89.68  ? 527 ASN   A ND2 1 
ATOM   1774 N  N   . GLY   A 1 232 ? -11.382 -16.217 6.518  1.00 92.40  ? 528 GLY   A N   1 
ATOM   1775 C  CA  . GLY   A 1 232 ? -10.155 -16.537 7.215  1.00 95.57  ? 528 GLY   A CA  1 
ATOM   1776 C  C   . GLY   A 1 232 ? -8.893  -15.942 6.629  1.00 97.77  ? 528 GLY   A C   1 
ATOM   1777 O  O   . GLY   A 1 232 ? -7.805  -16.225 7.146  1.00 101.42 ? 528 GLY   A O   1 
ATOM   1778 N  N   . ASN   A 1 233 ? -8.992  -15.129 5.578  1.00 90.94  ? 529 ASN   A N   1 
ATOM   1779 C  CA  . ASN   A 1 233 ? -7.815  -14.491 5.006  1.00 94.13  ? 529 ASN   A CA  1 
ATOM   1780 C  C   . ASN   A 1 233 ? -7.321  -13.356 5.903  1.00 94.46  ? 529 ASN   A C   1 
ATOM   1781 O  O   . ASN   A 1 233 ? -8.038  -12.863 6.773  1.00 91.45  ? 529 ASN   A O   1 
ATOM   1782 C  CB  . ASN   A 1 233 ? -8.120  -13.948 3.607  1.00 92.39  ? 529 ASN   A CB  1 
ATOM   1783 C  CG  . ASN   A 1 233 ? -8.374  -15.046 2.594  1.00 88.50  ? 529 ASN   A CG  1 
ATOM   1784 O  OD1 . ASN   A 1 233 ? -7.442  -15.635 2.069  1.00 92.88  ? 529 ASN   A OD1 1 
ATOM   1785 N  ND2 . ASN   A 1 233 ? -9.641  -15.320 2.316  1.00 85.82  ? 529 ASN   A ND2 1 
ATOM   1786 N  N   . ASP   A 1 234 ? -6.078  -12.939 5.674  1.00 95.51  ? 530 ASP   A N   1 
ATOM   1787 C  CA  . ASP   A 1 234 ? -5.520  -11.814 6.412  1.00 95.82  ? 530 ASP   A CA  1 
ATOM   1788 C  C   . ASP   A 1 234 ? -6.459  -10.610 6.307  1.00 91.50  ? 530 ASP   A C   1 
ATOM   1789 O  O   . ASP   A 1 234 ? -7.107  -10.417 5.266  1.00 91.39  ? 530 ASP   A O   1 
ATOM   1790 C  CB  . ASP   A 1 234 ? -4.131  -11.453 5.866  1.00 102.38 ? 530 ASP   A CB  1 
ATOM   1791 C  CG  . ASP   A 1 234 ? -3.084  -12.536 6.122  1.00 110.04 ? 530 ASP   A CG  1 
ATOM   1792 O  OD1 . ASP   A 1 234 ? -3.306  -13.417 6.980  1.00 109.33 ? 530 ASP   A OD1 1 
ATOM   1793 O  OD2 . ASP   A 1 234 ? -2.024  -12.492 5.459  1.00 116.06 ? 530 ASP   A OD2 1 
ATOM   1794 N  N   . PRO   A 1 235 ? -6.569  -9.793  7.349  1.00 88.95  ? 531 PRO   A N   1 
ATOM   1795 C  CA  . PRO   A 1 235 ? -7.535  -8.691  7.329  1.00 85.78  ? 531 PRO   A CA  1 
ATOM   1796 C  C   . PRO   A 1 235 ? -6.969  -7.460  6.640  1.00 86.68  ? 531 PRO   A C   1 
ATOM   1797 O  O   . PRO   A 1 235 ? -5.756  -7.277  6.532  1.00 89.89  ? 531 PRO   A O   1 
ATOM   1798 C  CB  . PRO   A 1 235 ? -7.772  -8.424  8.820  1.00 83.28  ? 531 PRO   A CB  1 
ATOM   1799 C  CG  . PRO   A 1 235 ? -6.450  -8.715  9.410  1.00 85.72  ? 531 PRO   A CG  1 
ATOM   1800 C  CD  . PRO   A 1 235 ? -5.921  -9.914  8.670  1.00 92.71  ? 531 PRO   A CD  1 
ATOM   1801 N  N   . GLU   A 1 236 ? -7.882  -6.596  6.191  1.00 84.37  ? 532 GLU   A N   1 
ATOM   1802 C  CA  . GLU   A 1 236 ? -7.545  -5.490  5.301  1.00 84.96  ? 532 GLU   A CA  1 
ATOM   1803 C  C   . GLU   A 1 236 ? -8.175  -4.197  5.800  1.00 83.64  ? 532 GLU   A C   1 
ATOM   1804 O  O   . GLU   A 1 236 ? -9.269  -4.197  6.366  1.00 81.00  ? 532 GLU   A O   1 
ATOM   1805 C  CB  . GLU   A 1 236 ? -8.007  -5.790  3.871  1.00 85.54  ? 532 GLU   A CB  1 
ATOM   1806 C  CG  . GLU   A 1 236 ? -7.305  -6.994  3.260  1.00 86.50  ? 532 GLU   A CG  1 
ATOM   1807 C  CD  . GLU   A 1 236 ? -8.166  -7.726  2.240  1.00 92.16  ? 532 GLU   A CD  1 
ATOM   1808 O  OE1 . GLU   A 1 236 ? -8.739  -7.065  1.343  1.00 81.61  ? 532 GLU   A OE1 1 
ATOM   1809 O  OE2 . GLU   A 1 236 ? -8.273  -8.970  2.352  1.00 95.62  ? 532 GLU   A OE2 1 
ATOM   1810 N  N   . LEU   A 1 237 ? -7.486  -3.087  5.573  1.00 85.91  ? 533 LEU   A N   1 
ATOM   1811 C  CA  . LEU   A 1 237 ? -7.898  -1.810  6.142  1.00 85.90  ? 533 LEU   A CA  1 
ATOM   1812 C  C   . LEU   A 1 237 ? -8.822  -1.058  5.196  1.00 86.53  ? 533 LEU   A C   1 
ATOM   1813 O  O   . LEU   A 1 237 ? -8.579  -1.001  3.993  1.00 87.98  ? 533 LEU   A O   1 
ATOM   1814 C  CB  . LEU   A 1 237 ? -6.677  -0.944  6.450  1.00 89.83  ? 533 LEU   A CB  1 
ATOM   1815 C  CG  . LEU   A 1 237 ? -5.841  -1.325  7.669  1.00 91.96  ? 533 LEU   A CG  1 
ATOM   1816 C  CD1 . LEU   A 1 237 ? -4.587  -0.470  7.695  1.00 98.17  ? 533 LEU   A CD1 1 
ATOM   1817 C  CD2 . LEU   A 1 237 ? -6.661  -1.151  8.942  1.00 87.75  ? 533 LEU   A CD2 1 
ATOM   1818 N  N   . PHE   A 1 238 ? -9.883  -0.474  5.752  1.00 86.36  ? 534 PHE   A N   1 
ATOM   1819 C  CA  . PHE   A 1 238 ? -10.759 0.411   4.996  1.00 86.80  ? 534 PHE   A CA  1 
ATOM   1820 C  C   . PHE   A 1 238 ? -11.221 1.542   5.901  1.00 88.84  ? 534 PHE   A C   1 
ATOM   1821 O  O   . PHE   A 1 238 ? -11.557 1.316   7.069  1.00 82.42  ? 534 PHE   A O   1 
ATOM   1822 C  CB  . PHE   A 1 238 ? -11.988 -0.316  4.439  1.00 83.04  ? 534 PHE   A CB  1 
ATOM   1823 C  CG  . PHE   A 1 238 ? -11.681 -1.609  3.755  1.00 80.58  ? 534 PHE   A CG  1 
ATOM   1824 C  CD1 . PHE   A 1 238 ? -11.532 -2.778  4.488  1.00 80.42  ? 534 PHE   A CD1 1 
ATOM   1825 C  CD2 . PHE   A 1 238 ? -11.564 -1.659  2.372  1.00 81.15  ? 534 PHE   A CD2 1 
ATOM   1826 C  CE1 . PHE   A 1 238 ? -11.256 -3.974  3.854  1.00 80.32  ? 534 PHE   A CE1 1 
ATOM   1827 C  CE2 . PHE   A 1 238 ? -11.292 -2.849  1.728  1.00 80.22  ? 534 PHE   A CE2 1 
ATOM   1828 C  CZ  . PHE   A 1 238 ? -11.141 -4.009  2.467  1.00 78.87  ? 534 PHE   A CZ  1 
ATOM   1829 N  N   . GLN   A 1 239 ? -11.247 2.755   5.350  1.00 97.17  ? 535 GLN   A N   1 
ATOM   1830 C  CA  . GLN   A 1 239 ? -11.745 3.930   6.055  1.00 95.99  ? 535 GLN   A CA  1 
ATOM   1831 C  C   . GLN   A 1 239 ? -13.226 4.106   5.741  1.00 95.89  ? 535 GLN   A C   1 
ATOM   1832 O  O   . GLN   A 1 239 ? -13.608 4.228   4.567  1.00 94.38  ? 535 GLN   A O   1 
ATOM   1833 C  CB  . GLN   A 1 239 ? -10.975 5.183   5.638  1.00 100.15 ? 535 GLN   A CB  1 
ATOM   1834 C  CG  . GLN   A 1 239 ? -11.682 6.482   6.011  1.00 104.05 ? 535 GLN   A CG  1 
ATOM   1835 C  CD  . GLN   A 1 239 ? -11.115 7.692   5.301  1.00 111.78 ? 535 GLN   A CD  1 
ATOM   1836 O  OE1 . GLN   A 1 239 ? -11.802 8.344   4.508  1.00 111.25 ? 535 GLN   A OE1 1 
ATOM   1837 N  NE2 . GLN   A 1 239 ? -9.853  8.002   5.579  1.00 120.65 ? 535 GLN   A NE2 1 
ATOM   1838 N  N   . ILE   A 1 240 ? -14.048 4.140   6.783  1.00 85.50  ? 536 ILE   A N   1 
ATOM   1839 C  CA  . ILE   A 1 240 ? -15.467 4.462   6.662  1.00 84.83  ? 536 ILE   A CA  1 
ATOM   1840 C  C   . ILE   A 1 240 ? -15.550 5.880   6.125  1.00 87.47  ? 536 ILE   A C   1 
ATOM   1841 O  O   . ILE   A 1 240 ? -14.938 6.782   6.715  1.00 87.69  ? 536 ILE   A O   1 
ATOM   1842 C  CB  . ILE   A 1 240 ? -16.190 4.331   8.014  1.00 82.25  ? 536 ILE   A CB  1 
ATOM   1843 C  CG1 . ILE   A 1 240 ? -16.007 2.925   8.591  1.00 81.14  ? 536 ILE   A CG1 1 
ATOM   1844 C  CG2 . ILE   A 1 240 ? -17.665 4.668   7.891  1.00 78.08  ? 536 ILE   A CG2 1 
ATOM   1845 C  CD1 . ILE   A 1 240 ? -15.226 2.909   9.886  1.00 77.61  ? 536 ILE   A CD1 1 
ATOM   1846 N  N   . PRO   A 1 241 ? -16.246 6.125   5.013  1.00 83.68  ? 537 PRO   A N   1 
ATOM   1847 C  CA  . PRO   A 1 241 ? -16.367 7.497   4.508  1.00 84.90  ? 537 PRO   A CA  1 
ATOM   1848 C  C   . PRO   A 1 241 ? -16.838 8.416   5.619  1.00 84.03  ? 537 PRO   A C   1 
ATOM   1849 O  O   . PRO   A 1 241 ? -17.860 8.142   6.267  1.00 82.42  ? 537 PRO   A O   1 
ATOM   1850 C  CB  . PRO   A 1 241 ? -17.412 7.388   3.384  1.00 80.76  ? 537 PRO   A CB  1 
ATOM   1851 C  CG  . PRO   A 1 241 ? -17.486 5.912   3.064  1.00 79.58  ? 537 PRO   A CG  1 
ATOM   1852 C  CD  . PRO   A 1 241 ? -17.177 5.204   4.344  1.00 79.85  ? 537 PRO   A CD  1 
ATOM   1853 N  N   . PRO   A 1 242 ? -16.083 9.468   5.927  1.00 84.57  ? 538 PRO   A N   1 
ATOM   1854 C  CA  . PRO   A 1 242 ? -16.373 10.224  7.159  1.00 85.78  ? 538 PRO   A CA  1 
ATOM   1855 C  C   . PRO   A 1 242 ? -17.771 10.812  7.171  1.00 85.21  ? 538 PRO   A C   1 
ATOM   1856 O  O   . PRO   A 1 242 ? -18.328 11.031  8.244  1.00 82.30  ? 538 PRO   A O   1 
ATOM   1857 C  CB  . PRO   A 1 242 ? -15.297 11.315  7.166  1.00 86.62  ? 538 PRO   A CB  1 
ATOM   1858 C  CG  . PRO   A 1 242 ? -14.228 10.802  6.255  1.00 90.01  ? 538 PRO   A CG  1 
ATOM   1859 C  CD  . PRO   A 1 242 ? -14.915 9.994   5.210  1.00 84.64  ? 538 PRO   A CD  1 
ATOM   1860 N  N   . GLU   A 1 243 ? -18.377 11.036  6.004  1.00 82.89  ? 539 GLU   A N   1 
ATOM   1861 C  CA  . GLU   A 1 243 ? -19.756 11.514  5.939  1.00 82.32  ? 539 GLU   A CA  1 
ATOM   1862 C  C   . GLU   A 1 243 ? -20.741 10.509  6.523  1.00 82.22  ? 539 GLU   A C   1 
ATOM   1863 O  O   . GLU   A 1 243 ? -21.869 10.890  6.850  1.00 82.77  ? 539 GLU   A O   1 
ATOM   1864 C  CB  . GLU   A 1 243 ? -20.130 11.853  4.479  1.00 92.29  ? 539 GLU   A CB  1 
ATOM   1865 C  CG  . GLU   A 1 243 ? -20.192 10.673  3.493  1.00 85.81  ? 539 GLU   A CG  1 
ATOM   1866 C  CD  . GLU   A 1 243 ? -18.958 10.573  2.586  1.00 81.63  ? 539 GLU   A CD  1 
ATOM   1867 O  OE1 . GLU   A 1 243 ? -17.842 10.629  3.144  1.00 82.29  ? 539 GLU   A OE1 1 
ATOM   1868 O  OE2 . GLU   A 1 243 ? -19.089 10.414  1.331  1.00 81.34  ? 539 GLU   A OE2 1 
ATOM   1869 N  N   . LEU   A 1 244 ? -20.349 9.236   6.642  1.00 81.13  ? 540 LEU   A N   1 
ATOM   1870 C  CA  . LEU   A 1 244 ? -21.175 8.207   7.256  1.00 78.05  ? 540 LEU   A CA  1 
ATOM   1871 C  C   . LEU   A 1 244 ? -20.980 8.110   8.762  1.00 78.29  ? 540 LEU   A C   1 
ATOM   1872 O  O   . LEU   A 1 244 ? -21.781 7.449   9.425  1.00 76.55  ? 540 LEU   A O   1 
ATOM   1873 C  CB  . LEU   A 1 244 ? -20.883 6.835   6.632  1.00 77.15  ? 540 LEU   A CB  1 
ATOM   1874 C  CG  . LEU   A 1 244 ? -21.310 6.570   5.178  1.00 77.60  ? 540 LEU   A CG  1 
ATOM   1875 C  CD1 . LEU   A 1 244 ? -21.316 5.063   4.875  1.00 71.45  ? 540 LEU   A CD1 1 
ATOM   1876 C  CD2 . LEU   A 1 244 ? -22.663 7.207   4.871  1.00 75.32  ? 540 LEU   A CD2 1 
ATOM   1877 N  N   . VAL   A 1 245 ? -19.950 8.742   9.314  1.00 79.33  ? 541 VAL   A N   1 
ATOM   1878 C  CA  . VAL   A 1 245 ? -19.672 8.701   10.747 1.00 80.90  ? 541 VAL   A CA  1 
ATOM   1879 C  C   . VAL   A 1 245 ? -20.297 9.949   11.355 1.00 78.87  ? 541 VAL   A C   1 
ATOM   1880 O  O   . VAL   A 1 245 ? -19.717 11.030  11.299 1.00 80.12  ? 541 VAL   A O   1 
ATOM   1881 C  CB  . VAL   A 1 245 ? -18.170 8.620   11.037 1.00 82.43  ? 541 VAL   A CB  1 
ATOM   1882 C  CG1 . VAL   A 1 245 ? -17.914 8.525   12.553 1.00 80.37  ? 541 VAL   A CG1 1 
ATOM   1883 C  CG2 . VAL   A 1 245 ? -17.559 7.429   10.332 1.00 79.79  ? 541 VAL   A CG2 1 
ATOM   1884 N  N   . LEU   A 1 246 ? -21.478 9.794   11.951 1.00 80.10  ? 542 LEU   A N   1 
ATOM   1885 C  CA  . LEU   A 1 246 ? -22.165 10.913  12.584 1.00 79.37  ? 542 LEU   A CA  1 
ATOM   1886 C  C   . LEU   A 1 246 ? -21.598 11.138  13.975 1.00 80.71  ? 542 LEU   A C   1 
ATOM   1887 O  O   . LEU   A 1 246 ? -21.554 10.218  14.791 1.00 78.30  ? 542 LEU   A O   1 
ATOM   1888 C  CB  . LEU   A 1 246 ? -23.668 10.648  12.667 1.00 79.84  ? 542 LEU   A CB  1 
ATOM   1889 C  CG  . LEU   A 1 246 ? -24.530 11.632  13.458 1.00 81.07  ? 542 LEU   A CG  1 
ATOM   1890 C  CD1 . LEU   A 1 246 ? -24.513 12.987  12.823 1.00 81.41  ? 542 LEU   A CD1 1 
ATOM   1891 C  CD2 . LEU   A 1 246 ? -25.961 11.106  13.609 1.00 82.98  ? 542 LEU   A CD2 1 
ATOM   1892 N  N   . GLU   A 1 247 ? -21.169 12.359  14.237 1.00 80.58  ? 543 GLU   A N   1 
ATOM   1893 C  CA  . GLU   A 1 247 ? -20.580 12.733  15.508 1.00 84.29  ? 543 GLU   A CA  1 
ATOM   1894 C  C   . GLU   A 1 247 ? -21.380 13.876  16.120 1.00 86.22  ? 543 GLU   A C   1 
ATOM   1895 O  O   . GLU   A 1 247 ? -21.972 14.696  15.401 1.00 82.31  ? 543 GLU   A O   1 
ATOM   1896 C  CB  . GLU   A 1 247 ? -19.109 13.130  15.323 1.00 86.75  ? 543 GLU   A CB  1 
ATOM   1897 C  CG  . GLU   A 1 247 ? -18.185 11.923  15.119 1.00 87.05  ? 543 GLU   A CG  1 
ATOM   1898 C  CD  . GLU   A 1 247 ? -16.811 12.323  14.602 1.00 95.81  ? 543 GLU   A CD  1 
ATOM   1899 O  OE1 . GLU   A 1 247 ? -16.735 12.944  13.526 1.00 97.70  ? 543 GLU   A OE1 1 
ATOM   1900 O  OE2 . GLU   A 1 247 ? -15.804 12.011  15.279 1.00 98.57  ? 543 GLU   A OE2 1 
ATOM   1901 N  N   . VAL   A 1 248 ? -21.400 13.906  17.448 1.00 84.35  ? 544 VAL   A N   1 
ATOM   1902 C  CA  . VAL   A 1 248 ? -22.129 14.884  18.251 1.00 90.03  ? 544 VAL   A CA  1 
ATOM   1903 C  C   . VAL   A 1 248 ? -21.108 15.683  19.051 1.00 90.79  ? 544 VAL   A C   1 
ATOM   1904 O  O   . VAL   A 1 248 ? -20.425 15.112  19.913 1.00 90.21  ? 544 VAL   A O   1 
ATOM   1905 C  CB  . VAL   A 1 248 ? -23.148 14.207  19.188 1.00 89.47  ? 544 VAL   A CB  1 
ATOM   1906 C  CG1 . VAL   A 1 248 ? -23.848 15.264  20.037 1.00 89.99  ? 544 VAL   A CG1 1 
ATOM   1907 C  CG2 . VAL   A 1 248 ? -24.143 13.389  18.382 1.00 85.87  ? 544 VAL   A CG2 1 
ATOM   1908 N  N   . PRO   A 1 249 ? -20.928 16.975  18.776 1.00 93.20  ? 545 PRO   A N   1 
ATOM   1909 C  CA  . PRO   A 1 249 ? -20.096 17.807  19.649 1.00 96.66  ? 545 PRO   A CA  1 
ATOM   1910 C  C   . PRO   A 1 249 ? -20.799 17.973  20.983 1.00 96.85  ? 545 PRO   A C   1 
ATOM   1911 O  O   . PRO   A 1 249 ? -22.001 18.244  21.033 1.00 96.98  ? 545 PRO   A O   1 
ATOM   1912 C  CB  . PRO   A 1 249 ? -19.991 19.135  18.884 1.00 101.95 ? 545 PRO   A CB  1 
ATOM   1913 C  CG  . PRO   A 1 249 ? -21.155 19.132  17.964 1.00 101.09 ? 545 PRO   A CG  1 
ATOM   1914 C  CD  . PRO   A 1 249 ? -21.394 17.711  17.582 1.00 96.27  ? 545 PRO   A CD  1 
ATOM   1915 N  N   . ILE   A 1 250 ? -20.055 17.777  22.065 1.00 99.43  ? 546 ILE   A N   1 
ATOM   1916 C  CA  . ILE   A 1 250 ? -20.628 17.760  23.403 1.00 96.83  ? 546 ILE   A CA  1 
ATOM   1917 C  C   . ILE   A 1 250 ? -20.553 19.164  23.981 1.00 101.86 ? 546 ILE   A C   1 
ATOM   1918 O  O   . ILE   A 1 250 ? -19.461 19.725  24.137 1.00 104.46 ? 546 ILE   A O   1 
ATOM   1919 C  CB  . ILE   A 1 250 ? -19.908 16.751  24.310 1.00 98.32  ? 546 ILE   A CB  1 
ATOM   1920 C  CG1 . ILE   A 1 250 ? -19.835 15.371  23.629 1.00 96.89  ? 546 ILE   A CG1 1 
ATOM   1921 C  CG2 . ILE   A 1 250 ? -20.623 16.654  25.642 1.00 96.07  ? 546 ILE   A CG2 1 
ATOM   1922 C  CD1 . ILE   A 1 250 ? -21.188 14.733  23.375 1.00 91.81  ? 546 ILE   A CD1 1 
ATOM   1923 N  N   . ARG   A 1 251 ? -21.719 19.727  24.297 1.00 105.24 ? 547 ARG   A N   1 
ATOM   1924 C  CA  . ARG   A 1 251 ? -21.828 21.013  24.958 1.00 108.76 ? 547 ARG   A CA  1 
ATOM   1925 C  C   . ARG   A 1 251 ? -22.726 20.870  26.180 1.00 110.42 ? 547 ARG   A C   1 
ATOM   1926 O  O   . ARG   A 1 251 ? -23.537 19.943  26.282 1.00 106.59 ? 547 ARG   A O   1 
ATOM   1927 C  CB  . ARG   A 1 251 ? -22.374 22.100  24.007 1.00 114.15 ? 547 ARG   A CB  1 
ATOM   1928 C  CG  . ARG   A 1 251 ? -23.803 21.876  23.526 1.00 112.26 ? 547 ARG   A CG  1 
ATOM   1929 C  CD  . ARG   A 1 251 ? -23.834 21.071  22.215 1.00 108.45 ? 547 ARG   A CD  1 
ATOM   1930 N  NE  . ARG   A 1 251 ? -25.069 21.219  21.452 1.00 108.66 ? 547 ARG   A NE  1 
ATOM   1931 C  CZ  . ARG   A 1 251 ? -25.348 20.526  20.354 1.00 105.89 ? 547 ARG   A CZ  1 
ATOM   1932 N  NH1 . ARG   A 1 251 ? -24.553 19.551  19.934 1.00 100.98 ? 547 ARG   A NH1 1 
ATOM   1933 N  NH2 . ARG   A 1 251 ? -26.424 20.851  19.634 1.00 107.02 ? 547 ARG   A NH2 1 
ATOM   1934 N  N   . HIS   A 1 252 ? -22.564 21.794  27.108 1.00 112.50 ? 548 HIS   A N   1 
ATOM   1935 C  CA  . HIS   A 1 252 ? -23.472 21.784  28.231 1.00 118.67 ? 548 HIS   A CA  1 
ATOM   1936 C  C   . HIS   A 1 252 ? -24.527 22.870  28.074 1.00 122.63 ? 548 HIS   A C   1 
ATOM   1937 O  O   . HIS   A 1 252 ? -24.306 23.883  27.395 1.00 123.28 ? 548 HIS   A O   1 
ATOM   1938 C  CB  . HIS   A 1 252 ? -22.717 21.980  29.544 1.00 113.81 ? 548 HIS   A CB  1 
ATOM   1939 C  CG  . HIS   A 1 252 ? -23.490 21.514  30.736 1.00 119.01 ? 548 HIS   A CG  1 
ATOM   1940 N  ND1 . HIS   A 1 252 ? -24.196 22.374  31.550 1.00 119.40 ? 548 HIS   A ND1 1 
ATOM   1941 C  CD2 . HIS   A 1 252 ? -23.707 20.269  31.225 1.00 111.58 ? 548 HIS   A CD2 1 
ATOM   1942 C  CE1 . HIS   A 1 252 ? -24.799 21.681  32.500 1.00 114.84 ? 548 HIS   A CE1 1 
ATOM   1943 N  NE2 . HIS   A 1 252 ? -24.523 20.402  32.321 1.00 110.47 ? 548 HIS   A NE2 1 
ATOM   1944 N  N   . PRO   A 1 253 ? -25.708 22.675  28.674 1.00 117.97 ? 549 PRO   A N   1 
ATOM   1945 C  CA  . PRO   A 1 253 ? -26.762 23.692  28.581 1.00 123.31 ? 549 PRO   A CA  1 
ATOM   1946 C  C   . PRO   A 1 253 ? -26.558 24.885  29.497 1.00 130.15 ? 549 PRO   A C   1 
ATOM   1947 O  O   . PRO   A 1 253 ? -27.204 25.919  29.274 1.00 135.54 ? 549 PRO   A O   1 
ATOM   1948 C  CB  . PRO   A 1 253 ? -28.033 22.911  28.961 1.00 119.85 ? 549 PRO   A CB  1 
ATOM   1949 C  CG  . PRO   A 1 253 ? -27.550 21.753  29.743 1.00 116.04 ? 549 PRO   A CG  1 
ATOM   1950 C  CD  . PRO   A 1 253 ? -26.239 21.383  29.142 1.00 113.72 ? 549 PRO   A CD  1 
ATOM   1951 N  N   . LYS   A 1 254 ? -25.693 24.783  30.507 1.00 128.95 ? 550 LYS   A N   1 
ATOM   1952 C  CA  . LYS   A 1 254 ? -25.364 25.910  31.369 1.00 135.90 ? 550 LYS   A CA  1 
ATOM   1953 C  C   . LYS   A 1 254 ? -23.946 26.421  31.180 1.00 139.19 ? 550 LYS   A C   1 
ATOM   1954 O  O   . LYS   A 1 254 ? -23.729 27.637  31.178 1.00 146.81 ? 550 LYS   A O   1 
ATOM   1955 C  CB  . LYS   A 1 254 ? -25.555 25.534  32.851 1.00 137.76 ? 550 LYS   A CB  1 
ATOM   1956 C  CG  . LYS   A 1 254 ? -26.873 24.856  33.187 1.00 140.08 ? 550 LYS   A CG  1 
ATOM   1957 C  CD  . LYS   A 1 254 ? -28.063 25.754  32.893 1.00 146.83 ? 550 LYS   A CD  1 
ATOM   1958 C  CE  . LYS   A 1 254 ? -29.362 25.084  33.315 1.00 149.46 ? 550 LYS   A CE  1 
ATOM   1959 N  NZ  . LYS   A 1 254 ? -30.529 26.010  33.242 1.00 153.15 ? 550 LYS   A NZ  1 
ATOM   1960 N  N   . PHE   A 1 255 ? -22.968 25.531  31.034 1.00 134.15 ? 551 PHE   A N   1 
ATOM   1961 C  CA  . PHE   A 1 255 ? -21.554 25.889  31.142 1.00 137.18 ? 551 PHE   A CA  1 
ATOM   1962 C  C   . PHE   A 1 255 ? -20.985 26.118  29.747 1.00 139.96 ? 551 PHE   A C   1 
ATOM   1963 O  O   . PHE   A 1 255 ? -20.643 25.163  29.045 1.00 135.98 ? 551 PHE   A O   1 
ATOM   1964 C  CB  . PHE   A 1 255 ? -20.786 24.795  31.878 1.00 133.92 ? 551 PHE   A CB  1 
ATOM   1965 C  CG  . PHE   A 1 255 ? -21.269 24.540  33.297 1.00 132.48 ? 551 PHE   A CG  1 
ATOM   1966 C  CD1 . PHE   A 1 255 ? -20.821 25.315  34.352 1.00 135.51 ? 551 PHE   A CD1 1 
ATOM   1967 C  CD2 . PHE   A 1 255 ? -22.151 23.506  33.570 1.00 129.03 ? 551 PHE   A CD2 1 
ATOM   1968 C  CE1 . PHE   A 1 255 ? -21.257 25.066  35.663 1.00 134.32 ? 551 PHE   A CE1 1 
ATOM   1969 C  CE2 . PHE   A 1 255 ? -22.589 23.251  34.866 1.00 126.11 ? 551 PHE   A CE2 1 
ATOM   1970 C  CZ  . PHE   A 1 255 ? -22.145 24.032  35.912 1.00 127.88 ? 551 PHE   A CZ  1 
ATOM   1971 N  N   . ASP   A 1 256 ? -20.866 27.388  29.342 1.00 146.50 ? 552 ASP   A N   1 
ATOM   1972 C  CA  . ASP   A 1 256 ? -20.381 27.664  27.991 1.00 148.52 ? 552 ASP   A CA  1 
ATOM   1973 C  C   . ASP   A 1 256 ? -18.923 27.269  27.813 1.00 147.54 ? 552 ASP   A C   1 
ATOM   1974 O  O   . ASP   A 1 256 ? -18.499 27.008  26.685 1.00 146.35 ? 552 ASP   A O   1 
ATOM   1975 C  CB  . ASP   A 1 256 ? -20.565 29.139  27.631 1.00 157.74 ? 552 ASP   A CB  1 
ATOM   1976 C  CG  . ASP   A 1 256 ? -21.893 29.408  26.950 1.00 161.82 ? 552 ASP   A CG  1 
ATOM   1977 O  OD1 . ASP   A 1 256 ? -22.897 29.594  27.674 1.00 163.24 ? 552 ASP   A OD1 1 
ATOM   1978 O  OD2 . ASP   A 1 256 ? -21.933 29.421  25.696 1.00 163.40 ? 552 ASP   A OD2 1 
ATOM   1979 N  N   . TRP   A 1 257 ? -18.143 27.211  28.895 1.00 148.33 ? 553 TRP   A N   1 
ATOM   1980 C  CA  . TRP   A 1 257 ? -16.784 26.701  28.770 1.00 147.15 ? 553 TRP   A CA  1 
ATOM   1981 C  C   . TRP   A 1 257 ? -16.755 25.219  28.425 1.00 138.20 ? 553 TRP   A C   1 
ATOM   1982 O  O   . TRP   A 1 257 ? -15.690 24.700  28.073 1.00 136.93 ? 553 TRP   A O   1 
ATOM   1983 C  CB  . TRP   A 1 257 ? -16.012 26.948  30.062 1.00 150.19 ? 553 TRP   A CB  1 
ATOM   1984 C  CG  . TRP   A 1 257 ? -16.721 26.423  31.260 1.00 146.06 ? 553 TRP   A CG  1 
ATOM   1985 C  CD1 . TRP   A 1 257 ? -17.486 27.133  32.140 1.00 149.54 ? 553 TRP   A CD1 1 
ATOM   1986 C  CD2 . TRP   A 1 257 ? -16.752 25.064  31.708 1.00 138.37 ? 553 TRP   A CD2 1 
ATOM   1987 N  NE1 . TRP   A 1 257 ? -17.984 26.298  33.115 1.00 144.02 ? 553 TRP   A NE1 1 
ATOM   1988 C  CE2 . TRP   A 1 257 ? -17.544 25.024  32.870 1.00 137.58 ? 553 TRP   A CE2 1 
ATOM   1989 C  CE3 . TRP   A 1 257 ? -16.180 23.876  31.242 1.00 135.27 ? 553 TRP   A CE3 1 
ATOM   1990 C  CZ2 . TRP   A 1 257 ? -17.784 23.846  33.563 1.00 134.72 ? 553 TRP   A CZ2 1 
ATOM   1991 C  CZ3 . TRP   A 1 257 ? -16.420 22.707  31.938 1.00 131.42 ? 553 TRP   A CZ3 1 
ATOM   1992 C  CH2 . TRP   A 1 257 ? -17.215 22.701  33.078 1.00 129.61 ? 553 TRP   A CH2 1 
ATOM   1993 N  N   . PHE   A 1 258 ? -17.892 24.530  28.533 1.00 132.48 ? 554 PHE   A N   1 
ATOM   1994 C  CA  . PHE   A 1 258 ? -17.911 23.098  28.274 1.00 128.38 ? 554 PHE   A CA  1 
ATOM   1995 C  C   . PHE   A 1 258 ? -17.549 22.795  26.825 1.00 129.60 ? 554 PHE   A C   1 
ATOM   1996 O  O   . PHE   A 1 258 ? -16.904 21.779  26.545 1.00 128.45 ? 554 PHE   A O   1 
ATOM   1997 C  CB  . PHE   A 1 258 ? -19.279 22.520  28.620 1.00 121.86 ? 554 PHE   A CB  1 
ATOM   1998 C  CG  . PHE   A 1 258 ? -19.242 21.078  28.977 1.00 115.50 ? 554 PHE   A CG  1 
ATOM   1999 C  CD1 . PHE   A 1 258 ? -19.294 20.102  27.999 1.00 111.51 ? 554 PHE   A CD1 1 
ATOM   2000 C  CD2 . PHE   A 1 258 ? -19.145 20.690  30.307 1.00 116.64 ? 554 PHE   A CD2 1 
ATOM   2001 C  CE1 . PHE   A 1 258 ? -19.258 18.755  28.338 1.00 107.86 ? 554 PHE   A CE1 1 
ATOM   2002 C  CE2 . PHE   A 1 258 ? -19.106 19.353  30.654 1.00 106.75 ? 554 PHE   A CE2 1 
ATOM   2003 C  CZ  . PHE   A 1 258 ? -19.162 18.384  29.672 1.00 106.78 ? 554 PHE   A CZ  1 
ATOM   2004 N  N   . LYS   A 1 259 ? -17.938 23.672  25.889 1.00 127.30 ? 555 LYS   A N   1 
ATOM   2005 C  CA  . LYS   A 1 259 ? -17.512 23.484  24.504 1.00 135.01 ? 555 LYS   A CA  1 
ATOM   2006 C  C   . LYS   A 1 259 ? -15.995 23.546  24.380 1.00 138.41 ? 555 LYS   A C   1 
ATOM   2007 O  O   . LYS   A 1 259 ? -15.417 22.898  23.498 1.00 137.67 ? 555 LYS   A O   1 
ATOM   2008 C  CB  . LYS   A 1 259 ? -18.141 24.536  23.578 1.00 134.48 ? 555 LYS   A CB  1 
ATOM   2009 C  CG  . LYS   A 1 259 ? -19.546 24.982  23.955 1.00 137.41 ? 555 LYS   A CG  1 
ATOM   2010 C  CD  . LYS   A 1 259 ? -19.992 26.179  23.126 1.00 139.57 ? 555 LYS   A CD  1 
ATOM   2011 C  CE  . LYS   A 1 259 ? -21.108 26.940  23.826 1.00 146.40 ? 555 LYS   A CE  1 
ATOM   2012 N  NZ  . LYS   A 1 259 ? -22.096 26.001  24.434 1.00 142.02 ? 555 LYS   A NZ  1 
ATOM   2013 N  N   . ASP   A 1 260 ? -15.335 24.323  25.245 1.00 138.96 ? 556 ASP   A N   1 
ATOM   2014 C  CA  . ASP   A 1 260 ? -13.882 24.448  25.174 1.00 143.29 ? 556 ASP   A CA  1 
ATOM   2015 C  C   . ASP   A 1 260 ? -13.190 23.135  25.501 1.00 137.02 ? 556 ASP   A C   1 
ATOM   2016 O  O   . ASP   A 1 260 ? -12.058 22.913  25.055 1.00 136.80 ? 556 ASP   A O   1 
ATOM   2017 C  CB  . ASP   A 1 260 ? -13.390 25.556  26.112 1.00 146.50 ? 556 ASP   A CB  1 
ATOM   2018 C  CG  . ASP   A 1 260 ? -13.618 26.942  25.543 1.00 155.03 ? 556 ASP   A CG  1 
ATOM   2019 O  OD1 . ASP   A 1 260 ? -13.555 27.095  24.306 1.00 156.87 ? 556 ASP   A OD1 1 
ATOM   2020 O  OD2 . ASP   A 1 260 ? -13.862 27.877  26.331 1.00 161.16 ? 556 ASP   A OD2 1 
ATOM   2021 N  N   . LEU   A 1 261 ? -13.852 22.263  26.263 1.00 136.35 ? 557 LEU   A N   1 
ATOM   2022 C  CA  . LEU   A 1 261 ? -13.349 20.908  26.443 1.00 131.47 ? 557 LEU   A CA  1 
ATOM   2023 C  C   . LEU   A 1 261 ? -13.102 20.230  25.102 1.00 134.02 ? 557 LEU   A C   1 
ATOM   2024 O  O   . LEU   A 1 261 ? -12.205 19.388  24.987 1.00 132.13 ? 557 LEU   A O   1 
ATOM   2025 C  CB  . LEU   A 1 261 ? -14.330 20.105  27.298 1.00 124.95 ? 557 LEU   A CB  1 
ATOM   2026 C  CG  . LEU   A 1 261 ? -14.417 20.606  28.746 1.00 124.42 ? 557 LEU   A CG  1 
ATOM   2027 C  CD1 . LEU   A 1 261 ? -15.484 19.871  29.555 1.00 115.93 ? 557 LEU   A CD1 1 
ATOM   2028 C  CD2 . LEU   A 1 261 ? -13.058 20.459  29.398 1.00 127.30 ? 557 LEU   A CD2 1 
ATOM   2029 N  N   . GLY   A 1 262 ? -13.863 20.602  24.077 1.00 146.95 ? 558 GLY   A N   1 
ATOM   2030 C  CA  . GLY   A 1 262 ? -13.660 20.039  22.756 1.00 145.63 ? 558 GLY   A CA  1 
ATOM   2031 C  C   . GLY   A 1 262 ? -13.987 18.566  22.700 1.00 136.94 ? 558 GLY   A C   1 
ATOM   2032 O  O   . GLY   A 1 262 ? -13.372 17.826  21.921 1.00 139.42 ? 558 GLY   A O   1 
ATOM   2033 N  N   . LEU   A 1 263 ? -14.934 18.119  23.521 1.00 120.05 ? 559 LEU   A N   1 
ATOM   2034 C  CA  . LEU   A 1 263 ? -15.362 16.731  23.498 1.00 109.19 ? 559 LEU   A CA  1 
ATOM   2035 C  C   . LEU   A 1 263 ? -16.372 16.490  22.378 1.00 106.07 ? 559 LEU   A C   1 
ATOM   2036 O  O   . LEU   A 1 263 ? -17.110 17.392  21.966 1.00 104.29 ? 559 LEU   A O   1 
ATOM   2037 C  CB  . LEU   A 1 263 ? -15.957 16.330  24.848 1.00 107.77 ? 559 LEU   A CB  1 
ATOM   2038 C  CG  . LEU   A 1 263 ? -14.919 16.478  25.963 1.00 106.74 ? 559 LEU   A CG  1 
ATOM   2039 C  CD1 . LEU   A 1 263 ? -15.547 16.321  27.346 1.00 102.35 ? 559 LEU   A CD1 1 
ATOM   2040 C  CD2 . LEU   A 1 263 ? -13.778 15.484  25.744 1.00 102.84 ? 559 LEU   A CD2 1 
ATOM   2041 N  N   . LYS   A 1 264 ? -16.366 15.261  21.866 1.00 97.81  ? 560 LYS   A N   1 
ATOM   2042 C  CA  . LYS   A 1 264 ? -17.345 14.804  20.890 1.00 97.25  ? 560 LYS   A CA  1 
ATOM   2043 C  C   . LYS   A 1 264 ? -17.435 13.290  20.986 1.00 91.72  ? 560 LYS   A C   1 
ATOM   2044 O  O   . LYS   A 1 264 ? -16.553 12.627  21.542 1.00 90.25  ? 560 LYS   A O   1 
ATOM   2045 C  CB  . LYS   A 1 264 ? -17.003 15.227  19.453 1.00 95.84  ? 560 LYS   A CB  1 
ATOM   2046 C  CG  . LYS   A 1 264 ? -15.674 14.706  18.910 1.00 97.88  ? 560 LYS   A CG  1 
ATOM   2047 C  CD  . LYS   A 1 264 ? -15.634 14.802  17.373 1.00 100.24 ? 560 LYS   A CD  1 
ATOM   2048 C  CE  . LYS   A 1 264 ? -14.221 15.037  16.839 1.00 103.80 ? 560 LYS   A CE  1 
ATOM   2049 N  NZ  . LYS   A 1 264 ? -14.095 14.790  15.373 1.00 101.15 ? 560 LYS   A NZ  1 
ATOM   2050 N  N   . TRP   A 1 265 ? -18.536 12.748  20.481 1.00 87.56  ? 561 TRP   A N   1 
ATOM   2051 C  CA  . TRP   A 1 265 ? -18.679 11.302  20.442 1.00 83.65  ? 561 TRP   A CA  1 
ATOM   2052 C  C   . TRP   A 1 265 ? -19.437 10.941  19.175 1.00 83.47  ? 561 TRP   A C   1 
ATOM   2053 O  O   . TRP   A 1 265 ? -20.059 11.797  18.541 1.00 82.79  ? 561 TRP   A O   1 
ATOM   2054 C  CB  . TRP   A 1 265 ? -19.381 10.754  21.693 1.00 79.49  ? 561 TRP   A CB  1 
ATOM   2055 C  CG  . TRP   A 1 265 ? -19.009 9.308   21.966 1.00 75.64  ? 561 TRP   A CG  1 
ATOM   2056 C  CD1 . TRP   A 1 265 ? -19.810 8.217   21.833 1.00 72.42  ? 561 TRP   A CD1 1 
ATOM   2057 C  CD2 . TRP   A 1 265 ? -17.728 8.813   22.375 1.00 76.40  ? 561 TRP   A CD2 1 
ATOM   2058 N  NE1 . TRP   A 1 265 ? -19.116 7.074   22.139 1.00 73.12  ? 561 TRP   A NE1 1 
ATOM   2059 C  CE2 . TRP   A 1 265 ? -17.833 7.416   22.474 1.00 74.85  ? 561 TRP   A CE2 1 
ATOM   2060 C  CE3 . TRP   A 1 265 ? -16.505 9.421   22.686 1.00 80.19  ? 561 TRP   A CE3 1 
ATOM   2061 C  CZ2 . TRP   A 1 265 ? -16.767 6.614   22.864 1.00 75.34  ? 561 TRP   A CZ2 1 
ATOM   2062 C  CZ3 . TRP   A 1 265 ? -15.445 8.621   23.062 1.00 79.93  ? 561 TRP   A CZ3 1 
ATOM   2063 C  CH2 . TRP   A 1 265 ? -15.585 7.232   23.154 1.00 76.93  ? 561 TRP   A CH2 1 
ATOM   2064 N  N   . TYR   A 1 266 ? -19.350 9.672   18.793 1.00 79.49  ? 562 TYR   A N   1 
ATOM   2065 C  CA  . TYR   A 1 266 ? -20.073 9.191   17.629 1.00 77.40  ? 562 TYR   A CA  1 
ATOM   2066 C  C   . TYR   A 1 266 ? -21.454 8.714   18.046 1.00 74.76  ? 562 TYR   A C   1 
ATOM   2067 O  O   . TYR   A 1 266 ? -21.650 8.217   19.157 1.00 70.68  ? 562 TYR   A O   1 
ATOM   2068 C  CB  . TYR   A 1 266 ? -19.317 8.053   16.941 1.00 76.08  ? 562 TYR   A CB  1 
ATOM   2069 C  CG  . TYR   A 1 266 ? -18.785 6.992   17.893 1.00 73.07  ? 562 TYR   A CG  1 
ATOM   2070 C  CD1 . TYR   A 1 266 ? -19.539 5.876   18.208 1.00 70.74  ? 562 TYR   A CD1 1 
ATOM   2071 C  CD2 . TYR   A 1 266 ? -17.522 7.109   18.460 1.00 75.72  ? 562 TYR   A CD2 1 
ATOM   2072 C  CE1 . TYR   A 1 266 ? -19.055 4.913   19.057 1.00 70.82  ? 562 TYR   A CE1 1 
ATOM   2073 C  CE2 . TYR   A 1 266 ? -17.032 6.157   19.315 1.00 74.96  ? 562 TYR   A CE2 1 
ATOM   2074 C  CZ  . TYR   A 1 266 ? -17.802 5.065   19.622 1.00 72.56  ? 562 TYR   A CZ  1 
ATOM   2075 O  OH  . TYR   A 1 266 ? -17.318 4.097   20.467 1.00 72.39  ? 562 TYR   A OH  1 
ATOM   2076 N  N   . GLY   A 1 267 ? -22.418 8.853   17.135 1.00 70.30  ? 563 GLY   A N   1 
ATOM   2077 C  CA  . GLY   A 1 267 ? -23.781 8.523   17.496 1.00 68.34  ? 563 GLY   A CA  1 
ATOM   2078 C  C   . GLY   A 1 267 ? -24.091 7.049   17.516 1.00 67.15  ? 563 GLY   A C   1 
ATOM   2079 O  O   . GLY   A 1 267 ? -25.034 6.644   18.205 1.00 69.35  ? 563 GLY   A O   1 
ATOM   2080 N  N   . LEU   A 1 268 ? -23.305 6.235   16.808 1.00 62.53  ? 564 LEU   A N   1 
ATOM   2081 C  CA  . LEU   A 1 268 ? -23.693 4.863   16.505 1.00 61.68  ? 564 LEU   A CA  1 
ATOM   2082 C  C   . LEU   A 1 268 ? -22.889 3.866   17.320 1.00 61.00  ? 564 LEU   A C   1 
ATOM   2083 O  O   . LEU   A 1 268 ? -21.711 3.624   17.000 1.00 60.59  ? 564 LEU   A O   1 
ATOM   2084 C  CB  . LEU   A 1 268 ? -23.517 4.570   15.008 1.00 59.02  ? 564 LEU   A CB  1 
ATOM   2085 C  CG  . LEU   A 1 268 ? -24.082 3.204   14.609 1.00 59.10  ? 564 LEU   A CG  1 
ATOM   2086 C  CD1 . LEU   A 1 268 ? -25.596 3.257   14.693 1.00 63.96  ? 564 LEU   A CD1 1 
ATOM   2087 C  CD2 . LEU   A 1 268 ? -23.640 2.775   13.214 1.00 60.39  ? 564 LEU   A CD2 1 
ATOM   2088 N  N   . PRO   A 1 269 ? -23.484 3.244   18.375 1.00 62.01  ? 565 PRO   A N   1 
ATOM   2089 C  CA  . PRO   A 1 269 ? -22.789 2.167   19.085 1.00 59.63  ? 565 PRO   A CA  1 
ATOM   2090 C  C   . PRO   A 1 269 ? -22.997 0.845   18.370 1.00 55.35  ? 565 PRO   A C   1 
ATOM   2091 O  O   . PRO   A 1 269 ? -24.138 0.380   18.259 1.00 54.38  ? 565 PRO   A O   1 
ATOM   2092 C  CB  . PRO   A 1 269 ? -23.457 2.174   20.467 1.00 59.79  ? 565 PRO   A CB  1 
ATOM   2093 C  CG  . PRO   A 1 269 ? -24.883 2.574   20.180 1.00 60.50  ? 565 PRO   A CG  1 
ATOM   2094 C  CD  . PRO   A 1 269 ? -24.801 3.538   18.978 1.00 60.22  ? 565 PRO   A CD  1 
ATOM   2095 N  N   . ALA   A 1 270 ? -21.921 0.225   17.888 1.00 55.74  ? 566 ALA   A N   1 
ATOM   2096 C  CA  . ALA   A 1 270 ? -22.048 -0.921  16.983 1.00 55.12  ? 566 ALA   A CA  1 
ATOM   2097 C  C   . ALA   A 1 270 ? -20.978 -1.931  17.372 1.00 56.93  ? 566 ALA   A C   1 
ATOM   2098 O  O   . ALA   A 1 270 ? -19.807 -1.759  17.029 1.00 58.01  ? 566 ALA   A O   1 
ATOM   2099 C  CB  . ALA   A 1 270 ? -21.929 -0.500  15.513 1.00 55.81  ? 566 ALA   A CB  1 
ATOM   2100 N  N   . VAL   A 1 271 ? -21.379 -2.962  18.104 1.00 56.27  ? 567 VAL   A N   1 
ATOM   2101 C  CA  . VAL   A 1 271 ? -20.449 -3.978  18.570 1.00 56.71  ? 567 VAL   A CA  1 
ATOM   2102 C  C   . VAL   A 1 271 ? -20.143 -4.936  17.437 1.00 56.51  ? 567 VAL   A C   1 
ATOM   2103 O  O   . VAL   A 1 271 ? -21.053 -5.547  16.866 1.00 56.24  ? 567 VAL   A O   1 
ATOM   2104 C  CB  . VAL   A 1 271 ? -21.029 -4.732  19.768 1.00 56.31  ? 567 VAL   A CB  1 
ATOM   2105 C  CG1 . VAL   A 1 271 ? -20.292 -6.040  19.960 1.00 56.47  ? 567 VAL   A CG1 1 
ATOM   2106 C  CG2 . VAL   A 1 271 ? -20.918 -3.848  21.044 1.00 54.47  ? 567 VAL   A CG2 1 
ATOM   2107 N  N   . SER   A 1 272 ? -18.860 -5.132  17.155 1.00 58.66  ? 568 SER   A N   1 
ATOM   2108 C  CA  . SER   A 1 272 ? -18.477 -5.940  16.008 1.00 58.87  ? 568 SER   A CA  1 
ATOM   2109 C  C   . SER   A 1 272 ? -17.593 -7.132  16.338 1.00 58.82  ? 568 SER   A C   1 
ATOM   2110 O  O   . SER   A 1 272 ? -17.171 -7.834  15.410 1.00 60.52  ? 568 SER   A O   1 
ATOM   2111 C  CB  . SER   A 1 272 ? -17.789 -5.058  14.957 1.00 59.58  ? 568 SER   A CB  1 
ATOM   2112 O  OG  . SER   A 1 272 ? -16.761 -4.264  15.523 1.00 63.91  ? 568 SER   A OG  1 
ATOM   2113 N  N   . ASN   A 1 273 ? -17.317 -7.405  17.619 1.00 58.47  ? 569 ASN   A N   1 
ATOM   2114 C  CA  . ASN   A 1 273 ? -16.411 -8.482  17.991 1.00 58.22  ? 569 ASN   A CA  1 
ATOM   2115 C  C   . ASN   A 1 273 ? -17.114 -9.676  18.620 1.00 57.74  ? 569 ASN   A C   1 
ATOM   2116 O  O   . ASN   A 1 273 ? -16.434 -10.597 19.082 1.00 59.77  ? 569 ASN   A O   1 
ATOM   2117 C  CB  . ASN   A 1 273 ? -15.327 -7.973  18.960 1.00 60.04  ? 569 ASN   A CB  1 
ATOM   2118 C  CG  . ASN   A 1 273 ? -15.907 -7.396  20.246 1.00 59.22  ? 569 ASN   A CG  1 
ATOM   2119 O  OD1 . ASN   A 1 273 ? -17.122 -7.372  20.445 1.00 56.63  ? 569 ASN   A OD1 1 
ATOM   2120 N  ND2 . ASN   A 1 273 ? -15.027 -6.939  21.135 1.00 63.79  ? 569 ASN   A ND2 1 
ATOM   2121 N  N   . MET   A 1 274 ? -18.440 -9.688  18.673 1.00 57.22  ? 570 MET   A N   1 
ATOM   2122 C  CA  . MET   A 1 274 ? -19.124 -10.795 19.317 1.00 56.08  ? 570 MET   A CA  1 
ATOM   2123 C  C   . MET   A 1 274 ? -19.492 -11.868 18.304 1.00 59.44  ? 570 MET   A C   1 
ATOM   2124 O  O   . MET   A 1 274 ? -19.334 -11.699 17.103 1.00 58.00  ? 570 MET   A O   1 
ATOM   2125 C  CB  . MET   A 1 274 ? -20.350 -10.287 20.069 1.00 56.73  ? 570 MET   A CB  1 
ATOM   2126 C  CG  . MET   A 1 274 ? -19.945 -9.422  21.275 1.00 57.18  ? 570 MET   A CG  1 
ATOM   2127 S  SD  . MET   A 1 274 ? -21.349 -9.001  22.312 1.00 53.25  ? 570 MET   A SD  1 
ATOM   2128 C  CE  . MET   A 1 274 ? -21.548 -10.540 23.190 1.00 54.34  ? 570 MET   A CE  1 
ATOM   2129 N  N   . LEU   A 1 275 ? -19.950 -13.005 18.811 1.00 57.52  ? 571 LEU   A N   1 
ATOM   2130 C  CA  . LEU   A 1 275 ? -20.291 -14.155 17.992 1.00 59.79  ? 571 LEU   A CA  1 
ATOM   2131 C  C   . LEU   A 1 275 ? -21.777 -14.420 18.147 1.00 59.53  ? 571 LEU   A C   1 
ATOM   2132 O  O   . LEU   A 1 275 ? -22.278 -14.522 19.272 1.00 57.10  ? 571 LEU   A O   1 
ATOM   2133 C  CB  . LEU   A 1 275 ? -19.498 -15.398 18.402 1.00 60.74  ? 571 LEU   A CB  1 
ATOM   2134 C  CG  . LEU   A 1 275 ? -19.587 -16.532 17.376 1.00 61.90  ? 571 LEU   A CG  1 
ATOM   2135 C  CD1 . LEU   A 1 275 ? -18.221 -17.142 17.110 1.00 64.62  ? 571 LEU   A CD1 1 
ATOM   2136 C  CD2 . LEU   A 1 275 ? -20.584 -17.589 17.825 1.00 64.45  ? 571 LEU   A CD2 1 
ATOM   2137 N  N   . LEU   A 1 276 ? -22.473 -14.529 17.022 1.00 57.57  ? 572 LEU   A N   1 
ATOM   2138 C  CA  . LEU   A 1 276 ? -23.897 -14.827 17.017 1.00 58.69  ? 572 LEU   A CA  1 
ATOM   2139 C  C   . LEU   A 1 276 ? -24.086 -16.330 16.826 1.00 62.34  ? 572 LEU   A C   1 
ATOM   2140 O  O   . LEU   A 1 276 ? -23.628 -16.904 15.826 1.00 61.10  ? 572 LEU   A O   1 
ATOM   2141 C  CB  . LEU   A 1 276 ? -24.595 -14.027 15.917 1.00 59.44  ? 572 LEU   A CB  1 
ATOM   2142 C  CG  . LEU   A 1 276 ? -26.030 -14.378 15.536 1.00 59.08  ? 572 LEU   A CG  1 
ATOM   2143 C  CD1 . LEU   A 1 276 ? -26.923 -14.335 16.747 1.00 57.14  ? 572 LEU   A CD1 1 
ATOM   2144 C  CD2 . LEU   A 1 276 ? -26.549 -13.431 14.461 1.00 55.36  ? 572 LEU   A CD2 1 
ATOM   2145 N  N   . GLU   A 1 277 ? -24.747 -16.963 17.793 1.00 58.68  ? 573 GLU   A N   1 
ATOM   2146 C  CA  . GLU   A 1 277 ? -25.029 -18.391 17.784 1.00 61.79  ? 573 GLU   A CA  1 
ATOM   2147 C  C   . GLU   A 1 277 ? -26.509 -18.597 17.478 1.00 62.33  ? 573 GLU   A C   1 
ATOM   2148 O  O   . GLU   A 1 277 ? -27.372 -18.098 18.211 1.00 62.15  ? 573 GLU   A O   1 
ATOM   2149 C  CB  . GLU   A 1 277 ? -24.677 -19.010 19.134 1.00 64.65  ? 573 GLU   A CB  1 
ATOM   2150 C  CG  . GLU   A 1 277 ? -23.910 -20.297 19.056 1.00 69.26  ? 573 GLU   A CG  1 
ATOM   2151 C  CD  . GLU   A 1 277 ? -24.688 -21.465 19.617 1.00 75.68  ? 573 GLU   A CD  1 
ATOM   2152 O  OE1 . GLU   A 1 277 ? -25.783 -21.781 19.081 1.00 73.82  ? 573 GLU   A OE1 1 
ATOM   2153 O  OE2 . GLU   A 1 277 ? -24.199 -22.066 20.599 1.00 81.61  ? 573 GLU   A OE2 1 
ATOM   2154 N  N   . ILE   A 1 278 ? -26.801 -19.331 16.409 1.00 65.27  ? 574 ILE   A N   1 
ATOM   2155 C  CA  . ILE   A 1 278 ? -28.170 -19.635 16.002 1.00 64.93  ? 574 ILE   A CA  1 
ATOM   2156 C  C   . ILE   A 1 278 ? -28.215 -21.090 15.572 1.00 69.50  ? 574 ILE   A C   1 
ATOM   2157 O  O   . ILE   A 1 278 ? -27.478 -21.491 14.664 1.00 69.67  ? 574 ILE   A O   1 
ATOM   2158 C  CB  . ILE   A 1 278 ? -28.665 -18.732 14.858 1.00 63.30  ? 574 ILE   A CB  1 
ATOM   2159 C  CG1 . ILE   A 1 278 ? -28.719 -17.273 15.300 1.00 61.28  ? 574 ILE   A CG1 1 
ATOM   2160 C  CG2 . ILE   A 1 278 ? -30.045 -19.180 14.421 1.00 65.37  ? 574 ILE   A CG2 1 
ATOM   2161 C  CD1 . ILE   A 1 278 ? -28.926 -16.287 14.161 1.00 59.46  ? 574 ILE   A CD1 1 
ATOM   2162 N  N   . GLY   A 1 279 ? -29.073 -21.872 16.221 1.00 68.52  ? 575 GLY   A N   1 
ATOM   2163 C  CA  . GLY   A 1 279 ? -29.202 -23.285 15.893 1.00 71.04  ? 575 GLY   A CA  1 
ATOM   2164 C  C   . GLY   A 1 279 ? -27.883 -24.015 15.815 1.00 72.87  ? 575 GLY   A C   1 
ATOM   2165 O  O   . GLY   A 1 279 ? -27.721 -24.919 14.987 1.00 76.38  ? 575 GLY   A O   1 
ATOM   2166 N  N   . GLY   A 1 280 ? -26.924 -23.640 16.660 1.00 72.49  ? 576 GLY   A N   1 
ATOM   2167 C  CA  . GLY   A 1 280 ? -25.613 -24.256 16.628 1.00 74.02  ? 576 GLY   A CA  1 
ATOM   2168 C  C   . GLY   A 1 280 ? -24.692 -23.761 15.531 1.00 71.79  ? 576 GLY   A C   1 
ATOM   2169 O  O   . GLY   A 1 280 ? -23.522 -24.159 15.499 1.00 73.72  ? 576 GLY   A O   1 
ATOM   2170 N  N   . LEU   A 1 281 ? -25.171 -22.909 14.635 1.00 70.70  ? 577 LEU   A N   1 
ATOM   2171 C  CA  . LEU   A 1 281 ? -24.313 -22.255 13.660 1.00 71.61  ? 577 LEU   A CA  1 
ATOM   2172 C  C   . LEU   A 1 281 ? -23.670 -21.033 14.296 1.00 69.45  ? 577 LEU   A C   1 
ATOM   2173 O  O   . LEU   A 1 281 ? -24.309 -20.317 15.069 1.00 69.25  ? 577 LEU   A O   1 
ATOM   2174 C  CB  . LEU   A 1 281 ? -25.115 -21.852 12.423 1.00 70.62  ? 577 LEU   A CB  1 
ATOM   2175 C  CG  . LEU   A 1 281 ? -25.799 -23.012 11.702 1.00 73.48  ? 577 LEU   A CG  1 
ATOM   2176 C  CD1 . LEU   A 1 281 ? -26.550 -22.557 10.438 1.00 69.71  ? 577 LEU   A CD1 1 
ATOM   2177 C  CD2 . LEU   A 1 281 ? -24.770 -24.085 11.387 1.00 74.27  ? 577 LEU   A CD2 1 
ATOM   2178 N  N   . GLU   A 1 282 ? -22.403 -20.795 13.968 1.00 66.93  ? 578 GLU   A N   1 
ATOM   2179 C  CA  . GLU   A 1 282 ? -21.625 -19.739 14.606 1.00 66.42  ? 578 GLU   A CA  1 
ATOM   2180 C  C   . GLU   A 1 282 ? -21.295 -18.664 13.585 1.00 63.89  ? 578 GLU   A C   1 
ATOM   2181 O  O   . GLU   A 1 282 ? -20.639 -18.944 12.574 1.00 62.61  ? 578 GLU   A O   1 
ATOM   2182 C  CB  . GLU   A 1 282 ? -20.347 -20.300 15.229 1.00 69.54  ? 578 GLU   A CB  1 
ATOM   2183 C  CG  . GLU   A 1 282 ? -20.618 -21.352 16.272 1.00 74.23  ? 578 GLU   A CG  1 
ATOM   2184 C  CD  . GLU   A 1 282 ? -19.364 -21.784 16.984 1.00 79.31  ? 578 GLU   A CD  1 
ATOM   2185 O  OE1 . GLU   A 1 282 ? -18.348 -22.005 16.294 1.00 77.86  ? 578 GLU   A OE1 1 
ATOM   2186 O  OE2 . GLU   A 1 282 ? -19.388 -21.889 18.231 1.00 85.02  ? 578 GLU   A OE2 1 
ATOM   2187 N  N   . PHE   A 1 283 ? -21.741 -17.442 13.856 1.00 62.48  ? 579 PHE   A N   1 
ATOM   2188 C  CA  . PHE   A 1 283 ? -21.519 -16.290 12.990 1.00 60.14  ? 579 PHE   A CA  1 
ATOM   2189 C  C   . PHE   A 1 283 ? -20.479 -15.391 13.654 1.00 59.34  ? 579 PHE   A C   1 
ATOM   2190 O  O   . PHE   A 1 283 ? -20.801 -14.555 14.498 1.00 60.21  ? 579 PHE   A O   1 
ATOM   2191 C  CB  . PHE   A 1 283 ? -22.837 -15.575 12.721 1.00 58.86  ? 579 PHE   A CB  1 
ATOM   2192 C  CG  . PHE   A 1 283 ? -23.818 -16.408 11.928 1.00 62.33  ? 579 PHE   A CG  1 
ATOM   2193 C  CD1 . PHE   A 1 283 ? -23.691 -16.518 10.558 1.00 60.05  ? 579 PHE   A CD1 1 
ATOM   2194 C  CD2 . PHE   A 1 283 ? -24.837 -17.109 12.562 1.00 62.59  ? 579 PHE   A CD2 1 
ATOM   2195 C  CE1 . PHE   A 1 283 ? -24.586 -17.284 9.811  1.00 64.44  ? 579 PHE   A CE1 1 
ATOM   2196 C  CE2 . PHE   A 1 283 ? -25.725 -17.886 11.840 1.00 62.22  ? 579 PHE   A CE2 1 
ATOM   2197 C  CZ  . PHE   A 1 283 ? -25.602 -17.974 10.459 1.00 64.52  ? 579 PHE   A CZ  1 
ATOM   2198 N  N   . SER   A 1 284 ? -19.217 -15.577 13.266 1.00 62.60  ? 580 SER   A N   1 
ATOM   2199 C  CA  . SER   A 1 284 ? -18.096 -14.901 13.912 1.00 63.18  ? 580 SER   A CA  1 
ATOM   2200 C  C   . SER   A 1 284 ? -18.046 -13.408 13.618 1.00 62.88  ? 580 SER   A C   1 
ATOM   2201 O  O   . SER   A 1 284 ? -17.353 -12.671 14.323 1.00 62.71  ? 580 SER   A O   1 
ATOM   2202 C  CB  . SER   A 1 284 ? -16.797 -15.558 13.463 1.00 66.76  ? 580 SER   A CB  1 
ATOM   2203 O  OG  . SER   A 1 284 ? -16.756 -15.660 12.043 1.00 67.36  ? 580 SER   A OG  1 
ATOM   2204 N  N   . ALA   A 1 285 ? -18.747 -12.953 12.584 1.00 59.08  ? 581 ALA   A N   1 
ATOM   2205 C  CA  . ALA   A 1 285 ? -18.804 -11.546 12.213 1.00 57.25  ? 581 ALA   A CA  1 
ATOM   2206 C  C   . ALA   A 1 285 ? -20.274 -11.181 12.123 1.00 56.91  ? 581 ALA   A C   1 
ATOM   2207 O  O   . ALA   A 1 285 ? -20.974 -11.621 11.207 1.00 57.01  ? 581 ALA   A O   1 
ATOM   2208 C  CB  . ALA   A 1 285 ? -18.079 -11.287 10.891 1.00 58.41  ? 581 ALA   A CB  1 
ATOM   2209 N  N   . CYS   A 1 286 ? -20.739 -10.391 13.062 1.00 55.32  ? 582 CYS   A N   1 
ATOM   2210 C  CA  . CYS   A 1 286 ? -22.153 -10.064 13.102 1.00 54.07  ? 582 CYS   A CA  1 
ATOM   2211 C  C   . CYS   A 1 286 ? -22.353 -8.683  13.708 1.00 54.35  ? 582 CYS   A C   1 
ATOM   2212 O  O   . CYS   A 1 286 ? -23.127 -8.544  14.659 1.00 55.04  ? 582 CYS   A O   1 
ATOM   2213 C  CB  . CYS   A 1 286 ? -22.914 -11.117 13.900 1.00 54.55  ? 582 CYS   A CB  1 
ATOM   2214 S  SG  . CYS   A 1 286 ? -22.242 -11.333 15.578 1.00 50.90  ? 582 CYS   A SG  1 
ATOM   2215 N  N   . PRO   A 1 287 ? -21.704 -7.641  13.179 1.00 55.34  ? 583 PRO   A N   1 
ATOM   2216 C  CA  . PRO   A 1 287 ? -21.806 -6.317  13.805 1.00 53.41  ? 583 PRO   A CA  1 
ATOM   2217 C  C   . PRO   A 1 287 ? -23.258 -5.917  14.009 1.00 54.65  ? 583 PRO   A C   1 
ATOM   2218 O  O   . PRO   A 1 287 ? -24.082 -6.045  13.104 1.00 51.48  ? 583 PRO   A O   1 
ATOM   2219 C  CB  . PRO   A 1 287 ? -21.102 -5.396  12.803 1.00 53.38  ? 583 PRO   A CB  1 
ATOM   2220 C  CG  . PRO   A 1 287 ? -21.211 -6.125  11.461 1.00 54.17  ? 583 PRO   A CG  1 
ATOM   2221 C  CD  . PRO   A 1 287 ? -21.060 -7.573  11.850 1.00 54.50  ? 583 PRO   A CD  1 
ATOM   2222 N  N   . PHE   A 1 288 ? -23.572 -5.436  15.218 1.00 50.53  ? 584 PHE   A N   1 
ATOM   2223 C  CA  . PHE   A 1 288 ? -24.918 -5.004  15.571 1.00 51.98  ? 584 PHE   A CA  1 
ATOM   2224 C  C   . PHE   A 1 288 ? -24.873 -3.640  16.242 1.00 55.71  ? 584 PHE   A C   1 
ATOM   2225 O  O   . PHE   A 1 288 ? -23.936 -3.322  16.986 1.00 53.09  ? 584 PHE   A O   1 
ATOM   2226 C  CB  . PHE   A 1 288 ? -25.653 -6.020  16.501 1.00 53.67  ? 584 PHE   A CB  1 
ATOM   2227 C  CG  . PHE   A 1 288 ? -24.908 -6.394  17.775 1.00 55.82  ? 584 PHE   A CG  1 
ATOM   2228 C  CD1 . PHE   A 1 288 ? -25.080 -5.665  18.961 1.00 54.35  ? 584 PHE   A CD1 1 
ATOM   2229 C  CD2 . PHE   A 1 288 ? -24.116 -7.535  17.812 1.00 55.52  ? 584 PHE   A CD2 1 
ATOM   2230 C  CE1 . PHE   A 1 288 ? -24.434 -6.035  20.130 1.00 53.43  ? 584 PHE   A CE1 1 
ATOM   2231 C  CE2 . PHE   A 1 288 ? -23.462 -7.914  18.984 1.00 53.66  ? 584 PHE   A CE2 1 
ATOM   2232 C  CZ  . PHE   A 1 288 ? -23.632 -7.159  20.149 1.00 53.15  ? 584 PHE   A CZ  1 
ATOM   2233 N  N   . SER   A 1 289 ? -25.890 -2.829  15.974 1.00 53.00  ? 585 SER   A N   1 
ATOM   2234 C  CA  . SER   A 1 289 ? -25.902 -1.480  16.506 1.00 55.47  ? 585 SER   A CA  1 
ATOM   2235 C  C   . SER   A 1 289 ? -27.286 -1.118  17.020 1.00 55.15  ? 585 SER   A C   1 
ATOM   2236 O  O   . SER   A 1 289 ? -28.308 -1.622  16.546 1.00 54.63  ? 585 SER   A O   1 
ATOM   2237 C  CB  . SER   A 1 289 ? -25.446 -0.449  15.449 1.00 55.41  ? 585 SER   A CB  1 
ATOM   2238 O  OG  . SER   A 1 289 ? -26.234 -0.505  14.270 1.00 57.53  ? 585 SER   A OG  1 
ATOM   2239 N  N   . GLY   A 1 290 ? -27.301 -0.200  17.974 1.00 53.57  ? 586 GLY   A N   1 
ATOM   2240 C  CA  . GLY   A 1 290 ? -28.539 0.401   18.407 1.00 59.68  ? 586 GLY   A CA  1 
ATOM   2241 C  C   . GLY   A 1 290 ? -28.367 1.893   18.576 1.00 63.72  ? 586 GLY   A C   1 
ATOM   2242 O  O   . GLY   A 1 290 ? -27.925 2.586   17.653 1.00 59.72  ? 586 GLY   A O   1 
ATOM   2243 N  N   . TRP   A 1 291 ? -28.727 2.410   19.744 1.00 58.40  ? 587 TRP   A N   1 
ATOM   2244 C  CA  . TRP   A 1 291 ? -28.417 3.787   20.096 1.00 64.01  ? 587 TRP   A CA  1 
ATOM   2245 C  C   . TRP   A 1 291 ? -27.849 3.797   21.503 1.00 60.08  ? 587 TRP   A C   1 
ATOM   2246 O  O   . TRP   A 1 291 ? -27.948 2.809   22.228 1.00 56.19  ? 587 TRP   A O   1 
ATOM   2247 C  CB  . TRP   A 1 291 ? -29.633 4.711   20.006 1.00 66.54  ? 587 TRP   A CB  1 
ATOM   2248 C  CG  . TRP   A 1 291 ? -30.874 4.177   20.614 1.00 68.35  ? 587 TRP   A CG  1 
ATOM   2249 C  CD1 . TRP   A 1 291 ? -31.236 4.222   21.935 1.00 69.32  ? 587 TRP   A CD1 1 
ATOM   2250 C  CD2 . TRP   A 1 291 ? -31.944 3.529   19.922 1.00 69.33  ? 587 TRP   A CD2 1 
ATOM   2251 N  NE1 . TRP   A 1 291 ? -32.471 3.633   22.104 1.00 72.38  ? 587 TRP   A NE1 1 
ATOM   2252 C  CE2 . TRP   A 1 291 ? -32.923 3.199   20.880 1.00 74.43  ? 587 TRP   A CE2 1 
ATOM   2253 C  CE3 . TRP   A 1 291 ? -32.174 3.204   18.579 1.00 69.11  ? 587 TRP   A CE3 1 
ATOM   2254 C  CZ2 . TRP   A 1 291 ? -34.110 2.546   20.540 1.00 77.59  ? 587 TRP   A CZ2 1 
ATOM   2255 C  CZ3 . TRP   A 1 291 ? -33.355 2.558   18.243 1.00 71.54  ? 587 TRP   A CZ3 1 
ATOM   2256 C  CH2 . TRP   A 1 291 ? -34.306 2.233   19.224 1.00 75.76  ? 587 TRP   A CH2 1 
ATOM   2257 N  N   . TYR   A 1 292 ? -27.223 4.909   21.875 1.00 62.09  ? 588 TYR   A N   1 
ATOM   2258 C  CA  . TYR   A 1 292 ? -26.527 4.964   23.156 1.00 62.89  ? 588 TYR   A CA  1 
ATOM   2259 C  C   . TYR   A 1 292 ? -27.488 5.251   24.294 1.00 65.63  ? 588 TYR   A C   1 
ATOM   2260 O  O   . TYR   A 1 292 ? -28.429 6.042   24.157 1.00 63.86  ? 588 TYR   A O   1 
ATOM   2261 C  CB  . TYR   A 1 292 ? -25.443 6.044   23.152 1.00 63.24  ? 588 TYR   A CB  1 
ATOM   2262 C  CG  . TYR   A 1 292 ? -24.054 5.561   22.778 1.00 65.79  ? 588 TYR   A CG  1 
ATOM   2263 C  CD1 . TYR   A 1 292 ? -23.362 4.678   23.591 1.00 64.84  ? 588 TYR   A CD1 1 
ATOM   2264 C  CD2 . TYR   A 1 292 ? -23.430 6.006   21.613 1.00 65.05  ? 588 TYR   A CD2 1 
ATOM   2265 C  CE1 . TYR   A 1 292 ? -22.079 4.255   23.268 1.00 66.66  ? 588 TYR   A CE1 1 
ATOM   2266 C  CE2 . TYR   A 1 292 ? -22.150 5.591   21.284 1.00 65.09  ? 588 TYR   A CE2 1 
ATOM   2267 C  CZ  . TYR   A 1 292 ? -21.481 4.711   22.106 1.00 65.79  ? 588 TYR   A CZ  1 
ATOM   2268 O  OH  . TYR   A 1 292 ? -20.213 4.290   21.770 1.00 66.81  ? 588 TYR   A OH  1 
ATOM   2269 N  N   . MET   A 1 293 ? -27.238 4.595   25.420 1.00 60.81  ? 589 MET   A N   1 
ATOM   2270 C  CA  . MET   A 1 293 ? -27.635 5.127   26.710 1.00 65.79  ? 589 MET   A CA  1 
ATOM   2271 C  C   . MET   A 1 293 ? -26.583 6.138   27.137 1.00 65.98  ? 589 MET   A C   1 
ATOM   2272 O  O   . MET   A 1 293 ? -25.380 5.905   26.974 1.00 65.92  ? 589 MET   A O   1 
ATOM   2273 C  CB  . MET   A 1 293 ? -27.769 4.009   27.749 1.00 62.88  ? 589 MET   A CB  1 
ATOM   2274 C  CG  . MET   A 1 293 ? -28.383 4.473   29.076 1.00 64.75  ? 589 MET   A CG  1 
ATOM   2275 S  SD  . MET   A 1 293 ? -28.879 3.106   30.140 1.00 61.33  ? 589 MET   A SD  1 
ATOM   2276 C  CE  . MET   A 1 293 ? -27.311 2.442   30.707 1.00 61.26  ? 589 MET   A CE  1 
ATOM   2277 N  N   . GLY   A 1 294 ? -27.044 7.277   27.656 1.00 68.41  ? 590 GLY   A N   1 
ATOM   2278 C  CA  . GLY   A 1 294 ? -26.137 8.382   27.927 1.00 67.57  ? 590 GLY   A CA  1 
ATOM   2279 C  C   . GLY   A 1 294 ? -24.924 7.989   28.748 1.00 67.61  ? 590 GLY   A C   1 
ATOM   2280 O  O   . GLY   A 1 294 ? -23.810 8.464   28.498 1.00 67.55  ? 590 GLY   A O   1 
ATOM   2281 N  N   . THR   A 1 295 ? -25.124 7.125   29.752 1.00 63.49  ? 591 THR   A N   1 
ATOM   2282 C  CA  . THR   A 1 295 ? -24.042 6.819   30.682 1.00 66.42  ? 591 THR   A CA  1 
ATOM   2283 C  C   . THR   A 1 295 ? -22.882 6.077   30.022 1.00 64.89  ? 591 THR   A C   1 
ATOM   2284 O  O   . THR   A 1 295 ? -21.743 6.165   30.502 1.00 64.42  ? 591 THR   A O   1 
ATOM   2285 C  CB  . THR   A 1 295 ? -24.573 6.006   31.862 1.00 62.41  ? 591 THR   A CB  1 
ATOM   2286 O  OG1 . THR   A 1 295 ? -25.355 4.920   31.366 1.00 61.28  ? 591 THR   A OG1 1 
ATOM   2287 C  CG2 . THR   A 1 295 ? -25.431 6.887   32.726 1.00 64.94  ? 591 THR   A CG2 1 
ATOM   2288 N  N   . GLU   A 1 296 ? -23.126 5.345   28.934 1.00 62.28  ? 592 GLU   A N   1 
ATOM   2289 C  CA  . GLU   A 1 296 ? -22.014 4.660   28.283 1.00 62.98  ? 592 GLU   A CA  1 
ATOM   2290 C  C   . GLU   A 1 296 ? -20.927 5.647   27.899 1.00 66.39  ? 592 GLU   A C   1 
ATOM   2291 O  O   . GLU   A 1 296 ? -19.739 5.374   28.088 1.00 67.51  ? 592 GLU   A O   1 
ATOM   2292 C  CB  . GLU   A 1 296 ? -22.494 3.907   27.052 1.00 64.28  ? 592 GLU   A CB  1 
ATOM   2293 C  CG  . GLU   A 1 296 ? -23.515 2.855   27.327 1.00 62.88  ? 592 GLU   A CG  1 
ATOM   2294 C  CD  . GLU   A 1 296 ? -23.923 2.157   26.055 1.00 62.54  ? 592 GLU   A CD  1 
ATOM   2295 O  OE1 . GLU   A 1 296 ? -23.121 1.322   25.571 1.00 59.38  ? 592 GLU   A OE1 1 
ATOM   2296 O  OE2 . GLU   A 1 296 ? -25.019 2.476   25.526 1.00 61.75  ? 592 GLU   A OE2 1 
ATOM   2297 N  N   . ILE   A 1 297 ? -21.319 6.802   27.366 1.00 68.42  ? 593 ILE   A N   1 
ATOM   2298 C  CA  . ILE   A 1 297 ? -20.362 7.831   26.984 1.00 70.27  ? 593 ILE   A CA  1 
ATOM   2299 C  C   . ILE   A 1 297 ? -19.966 8.651   28.198 1.00 73.17  ? 593 ILE   A C   1 
ATOM   2300 O  O   . ILE   A 1 297 ? -18.782 8.788   28.534 1.00 74.67  ? 593 ILE   A O   1 
ATOM   2301 C  CB  . ILE   A 1 297 ? -20.965 8.744   25.901 1.00 71.98  ? 593 ILE   A CB  1 
ATOM   2302 C  CG1 . ILE   A 1 297 ? -21.634 7.925   24.808 1.00 69.10  ? 593 ILE   A CG1 1 
ATOM   2303 C  CG2 . ILE   A 1 297 ? -19.896 9.597   25.276 1.00 76.59  ? 593 ILE   A CG2 1 
ATOM   2304 C  CD1 . ILE   A 1 297 ? -22.500 8.772   23.908 1.00 65.95  ? 593 ILE   A CD1 1 
ATOM   2305 N  N   . GLY   A 1 298 ? -20.968 9.225   28.868 1.00 72.60  ? 594 GLY   A N   1 
ATOM   2306 C  CA  . GLY   A 1 298 ? -20.687 10.214  29.898 1.00 78.87  ? 594 GLY   A CA  1 
ATOM   2307 C  C   . GLY   A 1 298 ? -19.941 9.637   31.083 1.00 74.38  ? 594 GLY   A C   1 
ATOM   2308 O  O   . GLY   A 1 298 ? -19.076 10.291  31.669 1.00 77.38  ? 594 GLY   A O   1 
ATOM   2309 N  N   . VAL   A 1 299 ? -20.250 8.402   31.445 1.00 72.02  ? 595 VAL   A N   1 
ATOM   2310 C  CA  . VAL   A 1 299 ? -19.667 7.818   32.651 1.00 73.43  ? 595 VAL   A CA  1 
ATOM   2311 C  C   . VAL   A 1 299 ? -18.472 6.940   32.301 1.00 71.86  ? 595 VAL   A C   1 
ATOM   2312 O  O   . VAL   A 1 299 ? -17.365 7.133   32.814 1.00 74.39  ? 595 VAL   A O   1 
ATOM   2313 C  CB  . VAL   A 1 299 ? -20.708 7.010   33.450 1.00 70.06  ? 595 VAL   A CB  1 
ATOM   2314 C  CG1 . VAL   A 1 299 ? -20.083 6.528   34.738 1.00 70.22  ? 595 VAL   A CG1 1 
ATOM   2315 C  CG2 . VAL   A 1 299 ? -21.935 7.848   33.748 1.00 70.15  ? 595 VAL   A CG2 1 
ATOM   2316 N  N   . ARG   A 1 300 ? -18.693 5.960   31.439 1.00 70.37  ? 596 ARG   A N   1 
ATOM   2317 C  CA  . ARG   A 1 300 ? -17.657 4.977   31.154 1.00 70.93  ? 596 ARG   A CA  1 
ATOM   2318 C  C   . ARG   A 1 300 ? -16.622 5.521   30.170 1.00 74.99  ? 596 ARG   A C   1 
ATOM   2319 O  O   . ARG   A 1 300 ? -15.426 5.595   30.482 1.00 73.18  ? 596 ARG   A O   1 
ATOM   2320 C  CB  . ARG   A 1 300 ? -18.306 3.692   30.616 1.00 68.44  ? 596 ARG   A CB  1 
ATOM   2321 C  CG  . ARG   A 1 300 ? -19.368 3.106   31.551 1.00 66.38  ? 596 ARG   A CG  1 
ATOM   2322 C  CD  . ARG   A 1 300 ? -18.786 2.813   32.952 1.00 68.26  ? 596 ARG   A CD  1 
ATOM   2323 N  NE  . ARG   A 1 300 ? -17.547 2.044   32.890 1.00 66.46  ? 596 ARG   A NE  1 
ATOM   2324 C  CZ  . ARG   A 1 300 ? -17.488 0.752   32.597 1.00 62.64  ? 596 ARG   A CZ  1 
ATOM   2325 N  NH1 . ARG   A 1 300 ? -18.582 0.039   32.391 1.00 57.70  ? 596 ARG   A NH1 1 
ATOM   2326 N  NH2 . ARG   A 1 300 ? -16.302 0.162   32.504 1.00 63.69  ? 596 ARG   A NH2 1 
ATOM   2327 N  N   . ASP   A 1 301 ? -17.066 5.896   28.963 1.00 72.48  ? 597 ASP   A N   1 
ATOM   2328 C  CA  . ASP   A 1 301 ? -16.124 6.378   27.957 1.00 74.11  ? 597 ASP   A CA  1 
ATOM   2329 C  C   . ASP   A 1 301 ? -15.347 7.581   28.472 1.00 77.23  ? 597 ASP   A C   1 
ATOM   2330 O  O   . ASP   A 1 301 ? -14.116 7.631   28.370 1.00 78.91  ? 597 ASP   A O   1 
ATOM   2331 C  CB  . ASP   A 1 301 ? -16.864 6.723   26.654 1.00 71.14  ? 597 ASP   A CB  1 
ATOM   2332 C  CG  . ASP   A 1 301 ? -17.438 5.494   25.964 1.00 71.14  ? 597 ASP   A CG  1 
ATOM   2333 O  OD1 . ASP   A 1 301 ? -16.806 4.418   26.013 1.00 69.80  ? 597 ASP   A OD1 1 
ATOM   2334 O  OD2 . ASP   A 1 301 ? -18.528 5.596   25.368 1.00 72.84  ? 597 ASP   A OD2 1 
ATOM   2335 N  N   . TYR   A 1 302 ? -16.037 8.541   29.069 1.00 76.49  ? 598 TYR   A N   1 
ATOM   2336 C  CA  . TYR   A 1 302 ? -15.386 9.776   29.484 1.00 79.67  ? 598 TYR   A CA  1 
ATOM   2337 C  C   . TYR   A 1 302 ? -14.690 9.696   30.839 1.00 81.55  ? 598 TYR   A C   1 
ATOM   2338 O  O   . TYR   A 1 302 ? -13.651 10.346  31.026 1.00 82.30  ? 598 TYR   A O   1 
ATOM   2339 C  CB  . TYR   A 1 302 ? -16.412 10.907  29.508 1.00 81.46  ? 598 TYR   A CB  1 
ATOM   2340 C  CG  . TYR   A 1 302 ? -16.707 11.443  28.130 1.00 86.46  ? 598 TYR   A CG  1 
ATOM   2341 C  CD1 . TYR   A 1 302 ? -15.792 11.291  27.101 1.00 84.14  ? 598 TYR   A CD1 1 
ATOM   2342 C  CD2 . TYR   A 1 302 ? -17.893 12.103  27.865 1.00 88.88  ? 598 TYR   A CD2 1 
ATOM   2343 C  CE1 . TYR   A 1 302 ? -16.049 11.792  25.833 1.00 90.98  ? 598 TYR   A CE1 1 
ATOM   2344 C  CE2 . TYR   A 1 302 ? -18.168 12.608  26.619 1.00 88.14  ? 598 TYR   A CE2 1 
ATOM   2345 C  CZ  . TYR   A 1 302 ? -17.244 12.449  25.598 1.00 91.18  ? 598 TYR   A CZ  1 
ATOM   2346 O  OH  . TYR   A 1 302 ? -17.515 12.951  24.363 1.00 86.67  ? 598 TYR   A OH  1 
ATOM   2347 N  N   . CYS   A 1 303 ? -15.216 8.921   31.793 1.00 77.99  ? 599 CYS   A N   1 
ATOM   2348 C  CA  . CYS   A 1 303 ? -14.760 9.053   33.171 1.00 82.25  ? 599 CYS   A CA  1 
ATOM   2349 C  C   . CYS   A 1 303 ? -14.140 7.800   33.774 1.00 81.60  ? 599 CYS   A C   1 
ATOM   2350 O  O   . CYS   A 1 303 ? -13.624 7.876   34.898 1.00 82.15  ? 599 CYS   A O   1 
ATOM   2351 C  CB  . CYS   A 1 303 ? -15.913 9.528   34.066 1.00 80.23  ? 599 CYS   A CB  1 
ATOM   2352 S  SG  . CYS   A 1 303 ? -16.575 11.125  33.543 1.00 81.88  ? 599 CYS   A SG  1 
ATOM   2353 N  N   . ASP   A 1 304 ? -14.162 6.662   33.079 1.00 78.27  ? 600 ASP   A N   1 
ATOM   2354 C  CA  . ASP   A 1 304 ? -13.286 5.559   33.460 1.00 81.27  ? 600 ASP   A CA  1 
ATOM   2355 C  C   . ASP   A 1 304 ? -11.855 6.067   33.583 1.00 84.85  ? 600 ASP   A C   1 
ATOM   2356 O  O   . ASP   A 1 304 ? -11.422 6.926   32.810 1.00 86.81  ? 600 ASP   A O   1 
ATOM   2357 C  CB  . ASP   A 1 304 ? -13.335 4.436   32.417 1.00 79.97  ? 600 ASP   A CB  1 
ATOM   2358 C  CG  . ASP   A 1 304 ? -14.351 3.349   32.746 1.00 75.44  ? 600 ASP   A CG  1 
ATOM   2359 O  OD1 . ASP   A 1 304 ? -15.214 3.563   33.627 1.00 73.90  ? 600 ASP   A OD1 1 
ATOM   2360 O  OD2 . ASP   A 1 304 ? -14.279 2.266   32.116 1.00 73.64  ? 600 ASP   A OD2 1 
ATOM   2361 N  N   . ASN   A 1 305 ? -11.117 5.530   34.553 1.00 87.31  ? 601 ASN   A N   1 
ATOM   2362 C  CA  . ASN   A 1 305 ? -9.723  5.928   34.728 1.00 89.59  ? 601 ASN   A CA  1 
ATOM   2363 C  C   . ASN   A 1 305 ? -8.850  5.456   33.581 1.00 88.26  ? 601 ASN   A C   1 
ATOM   2364 O  O   . ASN   A 1 305 ? -7.814  6.070   33.297 1.00 87.30  ? 601 ASN   A O   1 
ATOM   2365 C  CB  . ASN   A 1 305 ? -9.165  5.371   36.034 1.00 91.37  ? 601 ASN   A CB  1 
ATOM   2366 C  CG  . ASN   A 1 305 ? -9.268  6.346   37.165 1.00 95.41  ? 601 ASN   A CG  1 
ATOM   2367 O  OD1 . ASN   A 1 305 ? -9.038  7.544   36.986 1.00 98.89  ? 601 ASN   A OD1 1 
ATOM   2368 N  ND2 . ASN   A 1 305 ? -9.608  5.845   38.348 1.00 95.38  ? 601 ASN   A ND2 1 
ATOM   2369 N  N   . SER   A 1 306 ? -9.228  4.356   32.942 1.00 86.23  ? 602 SER   A N   1 
ATOM   2370 C  CA  . SER   A 1 306 ? -8.472  3.789   31.842 1.00 88.42  ? 602 SER   A CA  1 
ATOM   2371 C  C   . SER   A 1 306 ? -9.009  4.227   30.485 1.00 86.55  ? 602 SER   A C   1 
ATOM   2372 O  O   . SER   A 1 306 ? -8.528  3.743   29.457 1.00 86.14  ? 602 SER   A O   1 
ATOM   2373 C  CB  . SER   A 1 306 ? -8.473  2.265   31.951 1.00 91.58  ? 602 SER   A CB  1 
ATOM   2374 O  OG  . SER   A 1 306 ? -9.796  1.779   32.101 1.00 91.43  ? 602 SER   A OG  1 
ATOM   2375 N  N   . ARG   A 1 307 ? -9.996  5.125   30.467 1.00 85.77  ? 603 ARG   A N   1 
ATOM   2376 C  CA  . ARG   A 1 307 ? -10.518 5.694   29.231 1.00 86.20  ? 603 ARG   A CA  1 
ATOM   2377 C  C   . ARG   A 1 307 ? -10.153 7.175   29.182 1.00 86.34  ? 603 ARG   A C   1 
ATOM   2378 O  O   . ARG   A 1 307 ? -9.042  7.538   29.575 1.00 89.99  ? 603 ARG   A O   1 
ATOM   2379 C  CB  . ARG   A 1 307 ? -12.026 5.458   29.130 1.00 82.14  ? 603 ARG   A CB  1 
ATOM   2380 C  CG  . ARG   A 1 307 ? -12.405 3.981   29.148 1.00 80.32  ? 603 ARG   A CG  1 
ATOM   2381 C  CD  . ARG   A 1 307 ? -11.986 3.260   27.877 1.00 80.07  ? 603 ARG   A CD  1 
ATOM   2382 N  NE  . ARG   A 1 307 ? -12.602 3.891   26.718 1.00 76.55  ? 603 ARG   A NE  1 
ATOM   2383 C  CZ  . ARG   A 1 307 ? -13.894 3.807   26.440 1.00 75.70  ? 603 ARG   A CZ  1 
ATOM   2384 N  NH1 . ARG   A 1 307 ? -14.706 3.054   27.161 1.00 74.49  ? 603 ARG   A NH1 1 
ATOM   2385 N  NH2 . ARG   A 1 307 ? -14.386 4.502   25.420 1.00 77.03  ? 603 ARG   A NH2 1 
ATOM   2386 N  N   . TYR   A 1 308 ? -11.055 8.045   28.714 1.00 85.75  ? 604 TYR   A N   1 
ATOM   2387 C  CA  . TYR   A 1 308 ? -10.666 9.439   28.484 1.00 86.74  ? 604 TYR   A CA  1 
ATOM   2388 C  C   . TYR   A 1 308 ? -10.353 10.168  29.786 1.00 90.85  ? 604 TYR   A C   1 
ATOM   2389 O  O   . TYR   A 1 308 ? -9.522  11.088  29.796 1.00 92.36  ? 604 TYR   A O   1 
ATOM   2390 C  CB  . TYR   A 1 308 ? -11.753 10.168  27.694 1.00 87.67  ? 604 TYR   A CB  1 
ATOM   2391 C  CG  . TYR   A 1 308 ? -11.613 9.970   26.193 1.00 93.63  ? 604 TYR   A CG  1 
ATOM   2392 C  CD1 . TYR   A 1 308 ? -11.992 8.780   25.589 1.00 89.71  ? 604 TYR   A CD1 1 
ATOM   2393 C  CD2 . TYR   A 1 308 ? -11.091 10.971  25.386 1.00 103.07 ? 604 TYR   A CD2 1 
ATOM   2394 C  CE1 . TYR   A 1 308 ? -11.857 8.592   24.221 1.00 90.28  ? 604 TYR   A CE1 1 
ATOM   2395 C  CE2 . TYR   A 1 308 ? -10.949 10.794  24.008 1.00 96.82  ? 604 TYR   A CE2 1 
ATOM   2396 C  CZ  . TYR   A 1 308 ? -11.335 9.600   23.436 1.00 94.62  ? 604 TYR   A CZ  1 
ATOM   2397 O  OH  . TYR   A 1 308 ? -11.209 9.403   22.073 1.00 96.92  ? 604 TYR   A OH  1 
ATOM   2398 N  N   . ASN   A 1 309 ? -10.999 9.776   30.884 1.00 88.83  ? 605 ASN   A N   1 
ATOM   2399 C  CA  . ASN   A 1 309 ? -10.600 10.196  32.220 1.00 89.25  ? 605 ASN   A CA  1 
ATOM   2400 C  C   . ASN   A 1 309 ? -10.628 11.720  32.352 1.00 93.75  ? 605 ASN   A C   1 
ATOM   2401 O  O   . ASN   A 1 309 ? -9.629  12.366  32.685 1.00 101.25 ? 605 ASN   A O   1 
ATOM   2402 C  CB  . ASN   A 1 309 ? -9.215  9.633   32.557 1.00 91.20  ? 605 ASN   A CB  1 
ATOM   2403 C  CG  . ASN   A 1 309 ? -8.848  9.830   33.997 1.00 93.56  ? 605 ASN   A CG  1 
ATOM   2404 O  OD1 . ASN   A 1 309 ? -9.717  9.832   34.867 1.00 90.95  ? 605 ASN   A OD1 1 
ATOM   2405 N  ND2 . ASN   A 1 309 ? -7.556  10.020  34.262 1.00 96.74  ? 605 ASN   A ND2 1 
ATOM   2406 N  N   . ILE   A 1 310 ? -11.809 12.291  32.101 1.00 93.15  ? 606 ILE   A N   1 
ATOM   2407 C  CA  . ILE   A 1 310 ? -11.953 13.743  32.058 1.00 96.41  ? 606 ILE   A CA  1 
ATOM   2408 C  C   . ILE   A 1 310 ? -12.455 14.338  33.367 1.00 102.85 ? 606 ILE   A C   1 
ATOM   2409 O  O   . ILE   A 1 310 ? -12.602 15.565  33.448 1.00 105.79 ? 606 ILE   A O   1 
ATOM   2410 C  CB  . ILE   A 1 310 ? -12.882 14.178  30.911 1.00 97.99  ? 606 ILE   A CB  1 
ATOM   2411 C  CG1 . ILE   A 1 310 ? -14.335 13.835  31.248 1.00 97.88  ? 606 ILE   A CG1 1 
ATOM   2412 C  CG2 . ILE   A 1 310 ? -12.468 13.517  29.615 1.00 89.28  ? 606 ILE   A CG2 1 
ATOM   2413 C  CD1 . ILE   A 1 310 ? -15.307 14.217  30.141 1.00 87.52  ? 606 ILE   A CD1 1 
ATOM   2414 N  N   . LEU   A 1 311 ? -12.743 13.515  34.386 1.00 102.53 ? 607 LEU   A N   1 
ATOM   2415 C  CA  . LEU   A 1 311 ? -13.173 14.072  35.672 1.00 102.99 ? 607 LEU   A CA  1 
ATOM   2416 C  C   . LEU   A 1 311 ? -12.178 15.097  36.185 1.00 111.43 ? 607 LEU   A C   1 
ATOM   2417 O  O   . LEU   A 1 311 ? -12.570 16.112  36.772 1.00 114.22 ? 607 LEU   A O   1 
ATOM   2418 C  CB  . LEU   A 1 311 ? -13.371 12.971  36.719 1.00 92.13  ? 607 LEU   A CB  1 
ATOM   2419 C  CG  . LEU   A 1 311 ? -14.651 12.128  36.648 1.00 89.06  ? 607 LEU   A CG  1 
ATOM   2420 C  CD1 . LEU   A 1 311 ? -14.656 11.048  37.722 1.00 91.04  ? 607 LEU   A CD1 1 
ATOM   2421 C  CD2 . LEU   A 1 311 ? -15.907 12.984  36.748 1.00 83.74  ? 607 LEU   A CD2 1 
ATOM   2422 N  N   . GLU   A 1 312 ? -10.884 14.858  35.951 1.00 121.70 ? 608 GLU   A N   1 
ATOM   2423 C  CA  . GLU   A 1 312 ? -9.846  15.821  36.311 1.00 131.03 ? 608 GLU   A CA  1 
ATOM   2424 C  C   . GLU   A 1 312 ? -10.158 17.217  35.776 1.00 132.13 ? 608 GLU   A C   1 
ATOM   2425 O  O   . GLU   A 1 312 ? -10.313 18.174  36.544 1.00 133.02 ? 608 GLU   A O   1 
ATOM   2426 C  CB  . GLU   A 1 312 ? -8.496  15.344  35.772 1.00 140.52 ? 608 GLU   A CB  1 
ATOM   2427 C  CG  . GLU   A 1 312 ? -8.105  13.945  36.202 1.00 139.84 ? 608 GLU   A CG  1 
ATOM   2428 C  CD  . GLU   A 1 312 ? -7.132  13.960  37.359 1.00 155.91 ? 608 GLU   A CD  1 
ATOM   2429 O  OE1 . GLU   A 1 312 ? -7.088  14.972  38.095 1.00 153.75 ? 608 GLU   A OE1 1 
ATOM   2430 O  OE2 . GLU   A 1 312 ? -6.404  12.961  37.526 1.00 160.82 ? 608 GLU   A OE2 1 
ATOM   2431 N  N   . GLU   A 1 313 ? -10.262 17.342  34.448 1.00 126.30 ? 609 GLU   A N   1 
ATOM   2432 C  CA  . GLU   A 1 313 ? -10.413 18.654  33.821 1.00 128.89 ? 609 GLU   A CA  1 
ATOM   2433 C  C   . GLU   A 1 313 ? -11.774 19.271  34.121 1.00 127.70 ? 609 GLU   A C   1 
ATOM   2434 O  O   . GLU   A 1 313 ? -11.864 20.456  34.459 1.00 130.37 ? 609 GLU   A O   1 
ATOM   2435 C  CB  . GLU   A 1 313 ? -10.206 18.542  32.308 1.00 135.48 ? 609 GLU   A CB  1 
ATOM   2436 C  CG  . GLU   A 1 313 ? -8.809  18.920  31.816 1.00 143.08 ? 609 GLU   A CG  1 
ATOM   2437 C  CD  . GLU   A 1 313 ? -8.495  20.405  31.977 1.00 148.90 ? 609 GLU   A CD  1 
ATOM   2438 O  OE1 . GLU   A 1 313 ? -8.259  20.859  33.126 1.00 147.21 ? 609 GLU   A OE1 1 
ATOM   2439 O  OE2 . GLU   A 1 313 ? -8.486  21.117  30.946 1.00 149.20 ? 609 GLU   A OE2 1 
ATOM   2440 N  N   . VAL   A 1 314 ? -12.847 18.488  33.986 1.00 122.04 ? 610 VAL   A N   1 
ATOM   2441 C  CA  . VAL   A 1 314 ? -14.195 19.025  34.171 1.00 121.77 ? 610 VAL   A CA  1 
ATOM   2442 C  C   . VAL   A 1 314 ? -14.366 19.593  35.574 1.00 124.37 ? 610 VAL   A C   1 
ATOM   2443 O  O   . VAL   A 1 314 ? -15.014 20.629  35.765 1.00 127.27 ? 610 VAL   A O   1 
ATOM   2444 C  CB  . VAL   A 1 314 ? -15.247 17.943  33.873 1.00 115.16 ? 610 VAL   A CB  1 
ATOM   2445 C  CG1 . VAL   A 1 314 ? -16.640 18.421  34.275 1.00 112.82 ? 610 VAL   A CG1 1 
ATOM   2446 C  CG2 . VAL   A 1 314 ? -15.209 17.586  32.413 1.00 106.66 ? 610 VAL   A CG2 1 
ATOM   2447 N  N   . ALA   A 1 315 ? -13.794 18.924  36.575 1.00 121.31 ? 611 ALA   A N   1 
ATOM   2448 C  CA  . ALA   A 1 315 ? -13.920 19.411  37.941 1.00 125.15 ? 611 ALA   A CA  1 
ATOM   2449 C  C   . ALA   A 1 315 ? -13.222 20.748  38.109 1.00 130.48 ? 611 ALA   A C   1 
ATOM   2450 O  O   . ALA   A 1 315 ? -13.710 21.627  38.828 1.00 136.31 ? 611 ALA   A O   1 
ATOM   2451 C  CB  . ALA   A 1 315 ? -13.354 18.385  38.918 1.00 120.05 ? 611 ALA   A CB  1 
ATOM   2452 N  N   . LYS   A 1 316 ? -12.070 20.914  37.461 1.00 129.98 ? 612 LYS   A N   1 
ATOM   2453 C  CA  . LYS   A 1 316 ? -11.351 22.176  37.527 1.00 135.73 ? 612 LYS   A CA  1 
ATOM   2454 C  C   . LYS   A 1 316 ? -12.239 23.330  37.079 1.00 139.37 ? 612 LYS   A C   1 
ATOM   2455 O  O   . LYS   A 1 316 ? -12.471 24.285  37.830 1.00 144.26 ? 612 LYS   A O   1 
ATOM   2456 C  CB  . LYS   A 1 316 ? -10.089 22.100  36.666 1.00 137.45 ? 612 LYS   A CB  1 
ATOM   2457 C  CG  . LYS   A 1 316 ? -8.969  21.244  37.239 1.00 138.69 ? 612 LYS   A CG  1 
ATOM   2458 C  CD  . LYS   A 1 316 ? -7.653  21.552  36.530 1.00 142.42 ? 612 LYS   A CD  1 
ATOM   2459 C  CE  . LYS   A 1 316 ? -7.370  23.054  36.550 1.00 150.69 ? 612 LYS   A CE  1 
ATOM   2460 N  NZ  . LYS   A 1 316 ? -6.076  23.445  35.919 1.00 156.92 ? 612 LYS   A NZ  1 
ATOM   2461 N  N   . LYS   A 1 317 ? -12.766 23.240  35.852 1.00 136.67 ? 613 LYS   A N   1 
ATOM   2462 C  CA  . LYS   A 1 317 ? -13.588 24.305  35.288 1.00 140.67 ? 613 LYS   A CA  1 
ATOM   2463 C  C   . LYS   A 1 317 ? -14.878 24.538  36.061 1.00 139.80 ? 613 LYS   A C   1 
ATOM   2464 O  O   . LYS   A 1 317 ? -15.537 25.558  35.832 1.00 144.50 ? 613 LYS   A O   1 
ATOM   2465 C  CB  . LYS   A 1 317 ? -13.937 24.006  33.822 1.00 137.64 ? 613 LYS   A CB  1 
ATOM   2466 C  CG  . LYS   A 1 317 ? -12.829 24.271  32.822 1.00 141.22 ? 613 LYS   A CG  1 
ATOM   2467 C  CD  . LYS   A 1 317 ? -12.024 23.017  32.564 1.00 138.48 ? 613 LYS   A CD  1 
ATOM   2468 C  CE  . LYS   A 1 317 ? -11.291 23.091  31.236 1.00 138.78 ? 613 LYS   A CE  1 
ATOM   2469 N  NZ  . LYS   A 1 317 ? -10.214 24.113  31.261 1.00 146.46 ? 613 LYS   A NZ  1 
ATOM   2470 N  N   . MET   A 1 318 ? -15.258 23.635  36.963 1.00 138.18 ? 614 MET   A N   1 
ATOM   2471 C  CA  . MET   A 1 318 ? -16.470 23.842  37.742 1.00 137.73 ? 614 MET   A CA  1 
ATOM   2472 C  C   . MET   A 1 318 ? -16.236 24.602  39.036 1.00 141.12 ? 614 MET   A C   1 
ATOM   2473 O  O   . MET   A 1 318 ? -17.214 24.929  39.716 1.00 146.25 ? 614 MET   A O   1 
ATOM   2474 C  CB  . MET   A 1 318 ? -17.137 22.503  38.048 1.00 131.34 ? 614 MET   A CB  1 
ATOM   2475 C  CG  . MET   A 1 318 ? -17.963 21.994  36.900 1.00 129.53 ? 614 MET   A CG  1 
ATOM   2476 S  SD  . MET   A 1 318 ? -18.754 20.424  37.239 1.00 118.30 ? 614 MET   A SD  1 
ATOM   2477 C  CE  . MET   A 1 318 ? -19.744 20.846  38.671 1.00 117.84 ? 614 MET   A CE  1 
ATOM   2478 N  N   . ASP   A 1 319 ? -14.980 24.899  39.380 1.00 143.58 ? 615 ASP   A N   1 
ATOM   2479 C  CA  . ASP   A 1 319 ? -14.614 25.524  40.655 1.00 151.43 ? 615 ASP   A CA  1 
ATOM   2480 C  C   . ASP   A 1 319 ? -14.961 24.598  41.828 1.00 147.68 ? 615 ASP   A C   1 
ATOM   2481 O  O   . ASP   A 1 319 ? -15.739 24.937  42.722 1.00 153.01 ? 615 ASP   A O   1 
ATOM   2482 C  CB  . ASP   A 1 319 ? -15.274 26.905  40.809 1.00 157.88 ? 615 ASP   A CB  1 
ATOM   2483 C  CG  . ASP   A 1 319 ? -14.852 27.625  42.087 1.00 166.89 ? 615 ASP   A CG  1 
ATOM   2484 O  OD1 . ASP   A 1 319 ? -13.716 28.142  42.133 1.00 173.76 ? 615 ASP   A OD1 1 
ATOM   2485 O  OD2 . ASP   A 1 319 ? -15.660 27.682  43.043 1.00 165.37 ? 615 ASP   A OD2 1 
ATOM   2486 N  N   . LEU   A 1 320 ? -14.356 23.411  41.814 1.00 144.30 ? 616 LEU   A N   1 
ATOM   2487 C  CA  . LEU   A 1 320 ? -14.658 22.374  42.791 1.00 136.69 ? 616 LEU   A CA  1 
ATOM   2488 C  C   . LEU   A 1 320 ? -13.493 22.138  43.744 1.00 136.44 ? 616 LEU   A C   1 
ATOM   2489 O  O   . LEU   A 1 320 ? -12.338 22.471  43.458 1.00 138.22 ? 616 LEU   A O   1 
ATOM   2490 C  CB  . LEU   A 1 320 ? -15.015 21.053  42.108 1.00 132.20 ? 616 LEU   A CB  1 
ATOM   2491 C  CG  . LEU   A 1 320 ? -16.332 21.052  41.339 1.00 130.35 ? 616 LEU   A CG  1 
ATOM   2492 C  CD1 . LEU   A 1 320 ? -16.673 19.633  40.886 1.00 120.83 ? 616 LEU   A CD1 1 
ATOM   2493 C  CD2 . LEU   A 1 320 ? -17.437 21.641  42.202 1.00 129.42 ? 616 LEU   A CD2 1 
ATOM   2494 N  N   . ASP   A 1 321 ? -13.821 21.524  44.882 1.00 131.20 ? 617 ASP   A N   1 
ATOM   2495 C  CA  . ASP   A 1 321 ? -12.842 21.186  45.912 1.00 133.88 ? 617 ASP   A CA  1 
ATOM   2496 C  C   . ASP   A 1 321 ? -12.255 19.819  45.588 1.00 127.90 ? 617 ASP   A C   1 
ATOM   2497 O  O   . ASP   A 1 321 ? -12.814 18.788  45.967 1.00 127.52 ? 617 ASP   A O   1 
ATOM   2498 C  CB  . ASP   A 1 321 ? -13.497 21.207  47.291 1.00 133.77 ? 617 ASP   A CB  1 
ATOM   2499 C  CG  . ASP   A 1 321 ? -12.502 21.018  48.418 1.00 138.91 ? 617 ASP   A CG  1 
ATOM   2500 O  OD1 . ASP   A 1 321 ? -11.318 20.742  48.133 1.00 141.58 ? 617 ASP   A OD1 1 
ATOM   2501 O  OD2 . ASP   A 1 321 ? -12.907 21.153  49.595 1.00 138.76 ? 617 ASP   A OD2 1 
ATOM   2502 N  N   . MET   A 1 322 ? -11.109 19.808  44.907 1.00 128.43 ? 618 MET   A N   1 
ATOM   2503 C  CA  . MET   A 1 322 ? -10.439 18.570  44.532 1.00 128.09 ? 618 MET   A CA  1 
ATOM   2504 C  C   . MET   A 1 322 ? -9.397  18.123  45.551 1.00 135.09 ? 618 MET   A C   1 
ATOM   2505 O  O   . MET   A 1 322 ? -8.698  17.133  45.310 1.00 134.79 ? 618 MET   A O   1 
ATOM   2506 C  CB  . MET   A 1 322 ? -9.794  18.717  43.150 1.00 130.52 ? 618 MET   A CB  1 
ATOM   2507 C  CG  . MET   A 1 322 ? -10.792 18.816  42.006 1.00 122.23 ? 618 MET   A CG  1 
ATOM   2508 S  SD  . MET   A 1 322 ? -10.051 18.779  40.352 1.00 133.37 ? 618 MET   A SD  1 
ATOM   2509 C  CE  . MET   A 1 322 ? -8.471  18.008  40.714 1.00 137.06 ? 618 MET   A CE  1 
ATOM   2510 N  N   . ARG   A 1 323 ? -9.275  18.824  46.678 1.00 138.90 ? 619 ARG   A N   1 
ATOM   2511 C  CA  . ARG   A 1 323 ? -8.326  18.404  47.701 1.00 142.71 ? 619 ARG   A CA  1 
ATOM   2512 C  C   . ARG   A 1 323 ? -8.855  17.209  48.488 1.00 141.90 ? 619 ARG   A C   1 
ATOM   2513 O  O   . ARG   A 1 323 ? -8.126  16.237  48.711 1.00 142.08 ? 619 ARG   A O   1 
ATOM   2514 C  CB  . ARG   A 1 323 ? -8.012  19.575  48.637 1.00 150.35 ? 619 ARG   A CB  1 
ATOM   2515 C  CG  . ARG   A 1 323 ? -7.404  20.788  47.940 1.00 155.04 ? 619 ARG   A CG  1 
ATOM   2516 C  CD  . ARG   A 1 323 ? -7.624  22.067  48.739 1.00 163.42 ? 619 ARG   A CD  1 
ATOM   2517 N  NE  . ARG   A 1 323 ? -9.043  22.376  48.881 1.00 161.75 ? 619 ARG   A NE  1 
ATOM   2518 C  CZ  . ARG   A 1 323 ? -9.528  23.407  49.561 1.00 167.82 ? 619 ARG   A CZ  1 
ATOM   2519 N  NH1 . ARG   A 1 323 ? -8.732  24.264  50.181 1.00 173.21 ? 619 ARG   A NH1 1 
ATOM   2520 N  NH2 . ARG   A 1 323 ? -10.846 23.581  49.621 1.00 164.86 ? 619 ARG   A NH2 1 
ATOM   2521 N  N   . LYS   A 1 324 ? -10.119 17.253  48.896 1.00 138.35 ? 620 LYS   A N   1 
ATOM   2522 C  CA  . LYS   A 1 324 ? -10.700 16.234  49.759 1.00 131.18 ? 620 LYS   A CA  1 
ATOM   2523 C  C   . LYS   A 1 324 ? -11.543 15.274  48.929 1.00 124.68 ? 620 LYS   A C   1 
ATOM   2524 O  O   . LYS   A 1 324 ? -12.380 15.702  48.128 1.00 126.10 ? 620 LYS   A O   1 
ATOM   2525 C  CB  . LYS   A 1 324 ? -11.545 16.874  50.865 1.00 132.53 ? 620 LYS   A CB  1 
ATOM   2526 C  CG  . LYS   A 1 324 ? -10.747 17.354  52.082 1.00 146.93 ? 620 LYS   A CG  1 
ATOM   2527 C  CD  . LYS   A 1 324 ? -9.892  18.580  51.781 1.00 153.06 ? 620 LYS   A CD  1 
ATOM   2528 C  CE  . LYS   A 1 324 ? -9.007  18.950  52.964 1.00 156.38 ? 620 LYS   A CE  1 
ATOM   2529 N  NZ  . LYS   A 1 324 ? -8.115  20.097  52.641 1.00 165.74 ? 620 LYS   A NZ  1 
ATOM   2530 N  N   . THR   A 1 325 ? -11.310 13.974  49.124 1.00 116.46 ? 621 THR   A N   1 
ATOM   2531 C  CA  . THR   A 1 325 ? -12.080 12.952  48.422 1.00 106.88 ? 621 THR   A CA  1 
ATOM   2532 C  C   . THR   A 1 325 ? -13.576 13.071  48.709 1.00 105.49 ? 621 THR   A C   1 
ATOM   2533 O  O   . THR   A 1 325 ? -14.409 12.816  47.828 1.00 96.97  ? 621 THR   A O   1 
ATOM   2534 C  CB  . THR   A 1 325 ? -11.562 11.564  48.813 1.00 102.70 ? 621 THR   A CB  1 
ATOM   2535 O  OG1 . THR   A 1 325 ? -12.484 10.561  48.377 1.00 99.42  ? 621 THR   A OG1 1 
ATOM   2536 C  CG2 . THR   A 1 325 ? -11.362 11.447  50.341 1.00 106.73 ? 621 THR   A CG2 1 
ATOM   2537 N  N   . SER   A 1 326 ? -13.930 13.463  49.934 1.00 105.13 ? 622 SER   A N   1 
ATOM   2538 C  CA  . SER   A 1 326 ? -15.300 13.501  50.437 1.00 102.25 ? 622 SER   A CA  1 
ATOM   2539 C  C   . SER   A 1 326 ? -16.068 14.750  50.023 1.00 101.99 ? 622 SER   A C   1 
ATOM   2540 O  O   . SER   A 1 326 ? -17.247 14.872  50.370 1.00 101.90 ? 622 SER   A O   1 
ATOM   2541 C  CB  . SER   A 1 326 ? -15.281 13.395  51.967 1.00 98.73  ? 622 SER   A CB  1 
ATOM   2542 O  OG  . SER   A 1 326 ? -14.030 13.833  52.426 1.00 103.25 ? 622 SER   A OG  1 
ATOM   2543 N  N   . SER   A 1 327 ? -15.446 15.682  49.303 1.00 105.35 ? 623 SER   A N   1 
ATOM   2544 C  CA  . SER   A 1 327 ? -16.232 16.761  48.719 1.00 107.52 ? 623 SER   A CA  1 
ATOM   2545 C  C   . SER   A 1 327 ? -17.095 16.281  47.556 1.00 103.45 ? 623 SER   A C   1 
ATOM   2546 O  O   . SER   A 1 327 ? -17.873 17.072  47.012 1.00 104.83 ? 623 SER   A O   1 
ATOM   2547 C  CB  . SER   A 1 327 ? -15.309 17.885  48.250 1.00 113.63 ? 623 SER   A CB  1 
ATOM   2548 O  OG  . SER   A 1 327 ? -14.578 17.485  47.098 1.00 115.26 ? 623 SER   A OG  1 
ATOM   2549 N  N   . LEU   A 1 328 ? -16.966 15.010  47.170 1.00 99.81  ? 624 LEU   A N   1 
ATOM   2550 C  CA  . LEU   A 1 328 ? -17.701 14.423  46.045 1.00 99.09  ? 624 LEU   A CA  1 
ATOM   2551 C  C   . LEU   A 1 328 ? -17.555 15.250  44.772 1.00 100.26 ? 624 LEU   A C   1 
ATOM   2552 O  O   . LEU   A 1 328 ? -18.469 15.302  43.941 1.00 97.96  ? 624 LEU   A O   1 
ATOM   2553 C  CB  . LEU   A 1 328 ? -19.180 14.221  46.383 1.00 95.35  ? 624 LEU   A CB  1 
ATOM   2554 C  CG  . LEU   A 1 328 ? -19.471 13.392  47.638 1.00 95.26  ? 624 LEU   A CG  1 
ATOM   2555 C  CD1 . LEU   A 1 328 ? -20.857 12.775  47.539 1.00 90.31  ? 624 LEU   A CD1 1 
ATOM   2556 C  CD2 . LEU   A 1 328 ? -18.427 12.313  47.803 1.00 94.58  ? 624 LEU   A CD2 1 
ATOM   2557 N  N   . TRP   A 1 329 ? -16.400 15.898  44.601 1.00 103.87 ? 625 TRP   A N   1 
ATOM   2558 C  CA  . TRP   A 1 329 ? -16.166 16.619  43.357 1.00 103.37 ? 625 TRP   A CA  1 
ATOM   2559 C  C   . TRP   A 1 329 ? -16.310 15.693  42.158 1.00 102.51 ? 625 TRP   A C   1 
ATOM   2560 O  O   . TRP   A 1 329 ? -16.852 16.096  41.125 1.00 100.68 ? 625 TRP   A O   1 
ATOM   2561 C  CB  . TRP   A 1 329 ? -14.790 17.286  43.361 1.00 108.58 ? 625 TRP   A CB  1 
ATOM   2562 C  CG  . TRP   A 1 329 ? -13.630 16.341  43.469 1.00 108.23 ? 625 TRP   A CG  1 
ATOM   2563 C  CD1 . TRP   A 1 329 ? -13.063 15.878  44.617 1.00 111.18 ? 625 TRP   A CD1 1 
ATOM   2564 C  CD2 . TRP   A 1 329 ? -12.885 15.755  42.388 1.00 109.97 ? 625 TRP   A CD2 1 
ATOM   2565 N  NE1 . TRP   A 1 329 ? -12.014 15.040  44.324 1.00 111.24 ? 625 TRP   A NE1 1 
ATOM   2566 C  CE2 . TRP   A 1 329 ? -11.885 14.946  42.963 1.00 109.43 ? 625 TRP   A CE2 1 
ATOM   2567 C  CE3 . TRP   A 1 329 ? -12.970 15.832  40.992 1.00 105.09 ? 625 TRP   A CE3 1 
ATOM   2568 C  CZ2 . TRP   A 1 329 ? -10.976 14.221  42.193 1.00 106.50 ? 625 TRP   A CZ2 1 
ATOM   2569 C  CZ3 . TRP   A 1 329 ? -12.065 15.115  40.229 1.00 104.94 ? 625 TRP   A CZ3 1 
ATOM   2570 C  CH2 . TRP   A 1 329 ? -11.080 14.323  40.829 1.00 108.43 ? 625 TRP   A CH2 1 
ATOM   2571 N  N   . LYS   A 1 330 ? -15.867 14.437  42.290 1.00 99.68  ? 626 LYS   A N   1 
ATOM   2572 C  CA  . LYS   A 1 330 ? -15.986 13.487  41.185 1.00 95.62  ? 626 LYS   A CA  1 
ATOM   2573 C  C   . LYS   A 1 330 ? -17.441 13.225  40.827 1.00 93.66  ? 626 LYS   A C   1 
ATOM   2574 O  O   . LYS   A 1 330 ? -17.815 13.257  39.643 1.00 93.52  ? 626 LYS   A O   1 
ATOM   2575 C  CB  . LYS   A 1 330 ? -15.289 12.172  41.535 1.00 96.65  ? 626 LYS   A CB  1 
ATOM   2576 C  CG  . LYS   A 1 330 ? -13.781 12.202  41.434 1.00 98.51  ? 626 LYS   A CG  1 
ATOM   2577 C  CD  . LYS   A 1 330 ? -13.220 10.791  41.359 1.00 95.96  ? 626 LYS   A CD  1 
ATOM   2578 C  CE  . LYS   A 1 330 ? -11.703 10.800  41.269 1.00 97.97  ? 626 LYS   A CE  1 
ATOM   2579 N  NZ  . LYS   A 1 330 ? -11.162 9.415   41.337 1.00 97.08  ? 626 LYS   A NZ  1 
ATOM   2580 N  N   . ASP   A 1 331 ? -18.265 12.912  41.835 1.00 92.52  ? 627 ASP   A N   1 
ATOM   2581 C  CA  . ASP   A 1 331 ? -19.687 12.677  41.606 1.00 92.72  ? 627 ASP   A CA  1 
ATOM   2582 C  C   . ASP   A 1 331 ? -20.325 13.884  40.942 1.00 93.41  ? 627 ASP   A C   1 
ATOM   2583 O  O   . ASP   A 1 331 ? -21.075 13.750  39.963 1.00 94.40  ? 627 ASP   A O   1 
ATOM   2584 C  CB  . ASP   A 1 331 ? -20.409 12.370  42.922 1.00 90.63  ? 627 ASP   A CB  1 
ATOM   2585 C  CG  . ASP   A 1 331 ? -19.768 11.236  43.709 1.00 86.50  ? 627 ASP   A CG  1 
ATOM   2586 O  OD1 . ASP   A 1 331 ? -18.642 11.411  44.206 1.00 81.49  ? 627 ASP   A OD1 1 
ATOM   2587 O  OD2 . ASP   A 1 331 ? -20.401 10.172  43.845 1.00 82.46  ? 627 ASP   A OD2 1 
ATOM   2588 N  N   . GLN   A 1 332 ? -19.999 15.077  41.442 1.00 89.43  ? 628 GLN   A N   1 
ATOM   2589 C  CA  . GLN   A 1 332 ? -20.599 16.304  40.929 1.00 97.78  ? 628 GLN   A CA  1 
ATOM   2590 C  C   . GLN   A 1 332 ? -20.243 16.524  39.459 1.00 97.58  ? 628 GLN   A C   1 
ATOM   2591 O  O   . GLN   A 1 332 ? -21.126 16.735  38.615 1.00 95.52  ? 628 GLN   A O   1 
ATOM   2592 C  CB  . GLN   A 1 332 ? -20.154 17.486  41.797 1.00 104.64 ? 628 GLN   A CB  1 
ATOM   2593 C  CG  . GLN   A 1 332 ? -21.239 18.514  42.009 1.00 107.85 ? 628 GLN   A CG  1 
ATOM   2594 C  CD  . GLN   A 1 332 ? -21.065 19.311  43.285 1.00 112.84 ? 628 GLN   A CD  1 
ATOM   2595 O  OE1 . GLN   A 1 332 ? -20.005 19.297  43.927 1.00 113.40 ? 628 GLN   A OE1 1 
ATOM   2596 N  NE2 . GLN   A 1 332 ? -22.121 20.011  43.669 1.00 116.86 ? 628 GLN   A NE2 1 
ATOM   2597 N  N   . ALA   A 1 333 ? -18.953 16.450  39.124 1.00 96.64  ? 629 ALA   A N   1 
ATOM   2598 C  CA  . ALA   A 1 333 ? -18.563 16.628  37.727 1.00 97.41  ? 629 ALA   A CA  1 
ATOM   2599 C  C   . ALA   A 1 333 ? -19.092 15.503  36.842 1.00 97.15  ? 629 ALA   A C   1 
ATOM   2600 O  O   . ALA   A 1 333 ? -19.254 15.694  35.626 1.00 93.05  ? 629 ALA   A O   1 
ATOM   2601 C  CB  . ALA   A 1 333 ? -17.042 16.733  37.604 1.00 99.28  ? 629 ALA   A CB  1 
ATOM   2602 N  N   . LEU   A 1 334 ? -19.376 14.331  37.423 1.00 92.07  ? 630 LEU   A N   1 
ATOM   2603 C  CA  . LEU   A 1 334 ? -19.892 13.219  36.629 1.00 89.20  ? 630 LEU   A CA  1 
ATOM   2604 C  C   . LEU   A 1 334 ? -21.316 13.484  36.162 1.00 90.36  ? 630 LEU   A C   1 
ATOM   2605 O  O   . LEU   A 1 334 ? -21.685 13.120  35.037 1.00 89.70  ? 630 LEU   A O   1 
ATOM   2606 C  CB  . LEU   A 1 334 ? -19.843 11.918  37.427 1.00 84.98  ? 630 LEU   A CB  1 
ATOM   2607 C  CG  . LEU   A 1 334 ? -20.332 10.709  36.639 1.00 84.80  ? 630 LEU   A CG  1 
ATOM   2608 C  CD1 . LEU   A 1 334 ? -19.255 10.274  35.666 1.00 79.94  ? 630 LEU   A CD1 1 
ATOM   2609 C  CD2 . LEU   A 1 334 ? -20.734 9.562   37.541 1.00 78.92  ? 630 LEU   A CD2 1 
ATOM   2610 N  N   . VAL   A 1 335 ? -22.129 14.107  37.017 1.00 87.53  ? 631 VAL   A N   1 
ATOM   2611 C  CA  . VAL   A 1 335 ? -23.500 14.449  36.645 1.00 91.87  ? 631 VAL   A CA  1 
ATOM   2612 C  C   . VAL   A 1 335 ? -23.515 15.483  35.522 1.00 95.99  ? 631 VAL   A C   1 
ATOM   2613 O  O   . VAL   A 1 335 ? -24.211 15.313  34.512 1.00 93.55  ? 631 VAL   A O   1 
ATOM   2614 C  CB  . VAL   A 1 335 ? -24.281 14.955  37.867 1.00 93.42  ? 631 VAL   A CB  1 
ATOM   2615 C  CG1 . VAL   A 1 335 ? -25.629 15.500  37.440 1.00 95.42  ? 631 VAL   A CG1 1 
ATOM   2616 C  CG2 . VAL   A 1 335 ? -24.440 13.838  38.905 1.00 94.25  ? 631 VAL   A CG2 1 
ATOM   2617 N  N   . GLU   A 1 336 ? -22.750 16.570  35.682 1.00 93.95  ? 632 GLU   A N   1 
ATOM   2618 C  CA  . GLU   A 1 336 ? -22.699 17.602  34.643 1.00 97.80  ? 632 GLU   A CA  1 
ATOM   2619 C  C   . GLU   A 1 336 ? -22.305 17.015  33.296 1.00 96.61  ? 632 GLU   A C   1 
ATOM   2620 O  O   . GLU   A 1 336 ? -22.855 17.399  32.254 1.00 95.96  ? 632 GLU   A O   1 
ATOM   2621 C  CB  . GLU   A 1 336 ? -21.710 18.702  35.019 1.00 104.32 ? 632 GLU   A CB  1 
ATOM   2622 C  CG  . GLU   A 1 336 ? -21.961 19.330  36.358 1.00 110.85 ? 632 GLU   A CG  1 
ATOM   2623 C  CD  . GLU   A 1 336 ? -23.289 20.050  36.427 1.00 116.71 ? 632 GLU   A CD  1 
ATOM   2624 O  OE1 . GLU   A 1 336 ? -23.788 20.507  35.364 1.00 114.22 ? 632 GLU   A OE1 1 
ATOM   2625 O  OE2 . GLU   A 1 336 ? -23.833 20.148  37.549 1.00 118.45 ? 632 GLU   A OE2 1 
ATOM   2626 N  N   . ILE   A 1 337 ? -21.339 16.093  33.295 1.00 93.43  ? 633 ILE   A N   1 
ATOM   2627 C  CA  . ILE   A 1 337 ? -20.875 15.502  32.045 1.00 94.71  ? 633 ILE   A CA  1 
ATOM   2628 C  C   . ILE   A 1 337 ? -22.014 14.763  31.356 1.00 92.82  ? 633 ILE   A C   1 
ATOM   2629 O  O   . ILE   A 1 337 ? -22.188 14.853  30.135 1.00 90.42  ? 633 ILE   A O   1 
ATOM   2630 C  CB  . ILE   A 1 337 ? -19.664 14.586  32.303 1.00 88.50  ? 633 ILE   A CB  1 
ATOM   2631 C  CG1 . ILE   A 1 337 ? -18.458 15.439  32.683 1.00 93.29  ? 633 ILE   A CG1 1 
ATOM   2632 C  CG2 . ILE   A 1 337 ? -19.313 13.806  31.048 1.00 92.86  ? 633 ILE   A CG2 1 
ATOM   2633 C  CD1 . ILE   A 1 337 ? -17.268 14.641  33.139 1.00 95.23  ? 633 ILE   A CD1 1 
ATOM   2634 N  N   . ASN   A 1 338 ? -22.831 14.053  32.134 1.00 90.96  ? 634 ASN   A N   1 
ATOM   2635 C  CA  . ASN   A 1 338 ? -23.915 13.254  31.573 1.00 90.31  ? 634 ASN   A CA  1 
ATOM   2636 C  C   . ASN   A 1 338 ? -25.138 14.095  31.221 1.00 91.82  ? 634 ASN   A C   1 
ATOM   2637 O  O   . ASN   A 1 338 ? -25.900 13.719  30.324 1.00 89.49  ? 634 ASN   A O   1 
ATOM   2638 C  CB  . ASN   A 1 338 ? -24.269 12.128  32.552 1.00 86.37  ? 634 ASN   A CB  1 
ATOM   2639 C  CG  . ASN   A 1 338 ? -23.288 10.986  32.469 1.00 80.58  ? 634 ASN   A CG  1 
ATOM   2640 O  OD1 . ASN   A 1 338 ? -23.500 10.031  31.721 1.00 79.97  ? 634 ASN   A OD1 1 
ATOM   2641 N  ND2 . ASN   A 1 338 ? -22.173 11.119  33.152 1.00 78.60  ? 634 ASN   A ND2 1 
ATOM   2642 N  N   . ILE   A 1 339 ? -25.353 15.222  31.905 1.00 94.82  ? 635 ILE   A N   1 
ATOM   2643 C  CA  . ILE   A 1 339 ? -26.349 16.181  31.431 1.00 94.95  ? 635 ILE   A CA  1 
ATOM   2644 C  C   . ILE   A 1 339 ? -25.931 16.720  30.074 1.00 94.75  ? 635 ILE   A C   1 
ATOM   2645 O  O   . ILE   A 1 339 ? -26.762 16.896  29.170 1.00 92.38  ? 635 ILE   A O   1 
ATOM   2646 C  CB  . ILE   A 1 339 ? -26.546 17.311  32.464 1.00 95.73  ? 635 ILE   A CB  1 
ATOM   2647 C  CG1 . ILE   A 1 339 ? -27.278 16.778  33.688 1.00 97.26  ? 635 ILE   A CG1 1 
ATOM   2648 C  CG2 . ILE   A 1 339 ? -27.350 18.466  31.881 1.00 96.32  ? 635 ILE   A CG2 1 
ATOM   2649 C  CD1 . ILE   A 1 339 ? -27.505 17.815  34.760 1.00 98.91  ? 635 ILE   A CD1 1 
ATOM   2650 N  N   . ALA   A 1 340 ? -24.624 16.922  29.891 1.00 94.65  ? 636 ALA   A N   1 
ATOM   2651 C  CA  . ALA   A 1 340 ? -24.108 17.496  28.653 1.00 97.55  ? 636 ALA   A CA  1 
ATOM   2652 C  C   . ALA   A 1 340 ? -24.179 16.501  27.494 1.00 95.14  ? 636 ALA   A C   1 
ATOM   2653 O  O   . ALA   A 1 340 ? -24.547 16.867  26.366 1.00 94.37  ? 636 ALA   A O   1 
ATOM   2654 C  CB  . ALA   A 1 340 ? -22.671 17.971  28.866 1.00 99.95  ? 636 ALA   A CB  1 
ATOM   2655 N  N   . VAL   A 1 341 ? -23.801 15.242  27.733 1.00 89.77  ? 637 VAL   A N   1 
ATOM   2656 C  CA  . VAL   A 1 341 ? -23.885 14.251  26.662 1.00 90.81  ? 637 VAL   A CA  1 
ATOM   2657 C  C   . VAL   A 1 341 ? -25.321 14.154  26.166 1.00 91.36  ? 637 VAL   A C   1 
ATOM   2658 O  O   . VAL   A 1 341 ? -25.590 14.243  24.964 1.00 90.82  ? 637 VAL   A O   1 
ATOM   2659 C  CB  . VAL   A 1 341 ? -23.352 12.883  27.130 1.00 89.73  ? 637 VAL   A CB  1 
ATOM   2660 C  CG1 . VAL   A 1 341 ? -23.568 11.839  26.046 1.00 84.30  ? 637 VAL   A CG1 1 
ATOM   2661 C  CG2 . VAL   A 1 341 ? -21.878 12.973  27.477 1.00 90.90  ? 637 VAL   A CG2 1 
ATOM   2662 N  N   . LEU   A 1 342 ? -26.267 14.018  27.094 1.00 91.62  ? 638 LEU   A N   1 
ATOM   2663 C  CA  . LEU   A 1 342 ? -27.678 13.933  26.729 1.00 91.77  ? 638 LEU   A CA  1 
ATOM   2664 C  C   . LEU   A 1 342 ? -28.126 15.173  25.969 1.00 93.92  ? 638 LEU   A C   1 
ATOM   2665 O  O   . LEU   A 1 342 ? -28.678 15.073  24.866 1.00 93.46  ? 638 LEU   A O   1 
ATOM   2666 C  CB  . LEU   A 1 342 ? -28.523 13.733  27.988 1.00 93.05  ? 638 LEU   A CB  1 
ATOM   2667 C  CG  . LEU   A 1 342 ? -28.316 12.391  28.684 1.00 88.79  ? 638 LEU   A CG  1 
ATOM   2668 C  CD1 . LEU   A 1 342 ? -29.109 12.331  29.974 1.00 88.87  ? 638 LEU   A CD1 1 
ATOM   2669 C  CD2 . LEU   A 1 342 ? -28.709 11.264  27.756 1.00 78.21  ? 638 LEU   A CD2 1 
ATOM   2670 N  N   . TYR   A 1 343 ? -27.890 16.357  26.547 1.00 94.98  ? 639 TYR   A N   1 
ATOM   2671 C  CA  . TYR   A 1 343 ? -28.324 17.601  25.913 1.00 100.22 ? 639 TYR   A CA  1 
ATOM   2672 C  C   . TYR   A 1 343 ? -27.758 17.748  24.508 1.00 98.64  ? 639 TYR   A C   1 
ATOM   2673 O  O   . TYR   A 1 343 ? -28.449 18.217  23.597 1.00 97.09  ? 639 TYR   A O   1 
ATOM   2674 C  CB  . TYR   A 1 343 ? -27.913 18.799  26.768 1.00 104.78 ? 639 TYR   A CB  1 
ATOM   2675 C  CG  . TYR   A 1 343 ? -28.138 20.163  26.109 1.00 108.49 ? 639 TYR   A CG  1 
ATOM   2676 C  CD1 . TYR   A 1 343 ? -29.389 20.770  26.136 1.00 109.73 ? 639 TYR   A CD1 1 
ATOM   2677 C  CD2 . TYR   A 1 343 ? -27.094 20.852  25.506 1.00 110.33 ? 639 TYR   A CD2 1 
ATOM   2678 C  CE1 . TYR   A 1 343 ? -29.601 22.011  25.578 1.00 113.86 ? 639 TYR   A CE1 1 
ATOM   2679 C  CE2 . TYR   A 1 343 ? -27.298 22.102  24.921 1.00 113.24 ? 639 TYR   A CE2 1 
ATOM   2680 C  CZ  . TYR   A 1 343 ? -28.554 22.677  24.971 1.00 116.81 ? 639 TYR   A CZ  1 
ATOM   2681 O  OH  . TYR   A 1 343 ? -28.776 23.921  24.403 1.00 124.03 ? 639 TYR   A OH  1 
ATOM   2682 N  N   . SER   A 1 344 ? -26.498 17.360  24.316 1.00 99.51  ? 640 SER   A N   1 
ATOM   2683 C  CA  . SER   A 1 344 ? -25.867 17.539  23.015 1.00 95.01  ? 640 SER   A CA  1 
ATOM   2684 C  C   . SER   A 1 344 ? -26.485 16.617  21.974 1.00 96.52  ? 640 SER   A C   1 
ATOM   2685 O  O   . SER   A 1 344 ? -26.778 17.050  20.852 1.00 93.50  ? 640 SER   A O   1 
ATOM   2686 C  CB  . SER   A 1 344 ? -24.363 17.297  23.129 1.00 96.25  ? 640 SER   A CB  1 
ATOM   2687 O  OG  . SER   A 1 344 ? -23.814 18.016  24.230 1.00 101.63 ? 640 SER   A OG  1 
ATOM   2688 N  N   . PHE   A 1 345 ? -26.684 15.341  22.322 1.00 91.62  ? 641 PHE   A N   1 
ATOM   2689 C  CA  . PHE   A 1 345 ? -27.328 14.415  21.393 1.00 89.62  ? 641 PHE   A CA  1 
ATOM   2690 C  C   . PHE   A 1 345 ? -28.741 14.884  21.054 1.00 93.46  ? 641 PHE   A C   1 
ATOM   2691 O  O   . PHE   A 1 345 ? -29.114 14.957  19.877 1.00 96.84  ? 641 PHE   A O   1 
ATOM   2692 C  CB  . PHE   A 1 345 ? -27.351 13.003  21.981 1.00 84.94  ? 641 PHE   A CB  1 
ATOM   2693 C  CG  . PHE   A 1 345 ? -26.121 12.175  21.686 1.00 80.37  ? 641 PHE   A CG  1 
ATOM   2694 C  CD1 . PHE   A 1 345 ? -24.871 12.557  22.160 1.00 80.20  ? 641 PHE   A CD1 1 
ATOM   2695 C  CD2 . PHE   A 1 345 ? -26.236 10.977  20.974 1.00 76.45  ? 641 PHE   A CD2 1 
ATOM   2696 C  CE1 . PHE   A 1 345 ? -23.745 11.776  21.905 1.00 78.63  ? 641 PHE   A CE1 1 
ATOM   2697 C  CE2 . PHE   A 1 345 ? -25.127 10.176  20.730 1.00 72.83  ? 641 PHE   A CE2 1 
ATOM   2698 C  CZ  . PHE   A 1 345 ? -23.875 10.577  21.173 1.00 74.03  ? 641 PHE   A CZ  1 
ATOM   2699 N  N   . GLN   A 1 346 ? -29.523 15.263  22.075 1.00 94.72  ? 642 GLN   A N   1 
ATOM   2700 C  CA  . GLN   A 1 346 ? -30.917 15.652  21.858 1.00 96.85  ? 642 GLN   A CA  1 
ATOM   2701 C  C   . GLN   A 1 346 ? -31.026 16.905  21.000 1.00 98.61  ? 642 GLN   A C   1 
ATOM   2702 O  O   . GLN   A 1 346 ? -31.866 16.970  20.094 1.00 92.27  ? 642 GLN   A O   1 
ATOM   2703 C  CB  . GLN   A 1 346 ? -31.618 15.884  23.193 1.00 96.83  ? 642 GLN   A CB  1 
ATOM   2704 C  CG  . GLN   A 1 346 ? -31.936 14.624  23.989 1.00 98.07  ? 642 GLN   A CG  1 
ATOM   2705 C  CD  . GLN   A 1 346 ? -32.280 14.946  25.421 1.00 103.09 ? 642 GLN   A CD  1 
ATOM   2706 O  OE1 . GLN   A 1 346 ? -31.609 15.762  26.053 1.00 99.89  ? 642 GLN   A OE1 1 
ATOM   2707 N  NE2 . GLN   A 1 346 ? -33.340 14.328  25.937 1.00 108.15 ? 642 GLN   A NE2 1 
ATOM   2708 N  N   . SER   A 1 347 ? -30.207 17.920  21.289 1.00 96.61  ? 643 SER   A N   1 
ATOM   2709 C  CA  . SER   A 1 347 ? -30.239 19.155  20.513 1.00 100.86 ? 643 SER   A CA  1 
ATOM   2710 C  C   . SER   A 1 347 ? -29.883 18.923  19.046 1.00 102.47 ? 643 SER   A C   1 
ATOM   2711 O  O   . SER   A 1 347 ? -30.275 19.721  18.184 1.00 103.53 ? 643 SER   A O   1 
ATOM   2712 C  CB  . SER   A 1 347 ? -29.294 20.183  21.146 1.00 104.29 ? 643 SER   A CB  1 
ATOM   2713 O  OG  . SER   A 1 347 ? -29.662 20.487  22.493 1.00 105.93 ? 643 SER   A OG  1 
ATOM   2714 N  N   . ASP   A 1 348 ? -29.169 17.842  18.738 1.00 100.93 ? 644 ASP   A N   1 
ATOM   2715 C  CA  . ASP   A 1 348 ? -28.831 17.480  17.367 1.00 102.19 ? 644 ASP   A CA  1 
ATOM   2716 C  C   . ASP   A 1 348 ? -29.785 16.447  16.780 1.00 101.21 ? 644 ASP   A C   1 
ATOM   2717 O  O   . ASP   A 1 348 ? -29.524 15.931  15.689 1.00 101.25 ? 644 ASP   A O   1 
ATOM   2718 C  CB  . ASP   A 1 348 ? -27.402 16.940  17.302 1.00 100.25 ? 644 ASP   A CB  1 
ATOM   2719 C  CG  . ASP   A 1 348 ? -26.353 18.009  17.536 1.00 100.24 ? 644 ASP   A CG  1 
ATOM   2720 O  OD1 . ASP   A 1 348 ? -26.698 19.214  17.540 1.00 100.26 ? 644 ASP   A OD1 1 
ATOM   2721 O  OD2 . ASP   A 1 348 ? -25.177 17.633  17.721 1.00 95.21  ? 644 ASP   A OD2 1 
ATOM   2722 N  N   . LYS   A 1 349 ? -30.865 16.111  17.493 1.00 102.42 ? 645 LYS   A N   1 
ATOM   2723 C  CA  . LYS   A 1 349 ? -31.823 15.103  17.043 1.00 104.87 ? 645 LYS   A CA  1 
ATOM   2724 C  C   . LYS   A 1 349 ? -31.131 13.773  16.762 1.00 99.76  ? 645 LYS   A C   1 
ATOM   2725 O  O   . LYS   A 1 349 ? -31.476 13.068  15.816 1.00 92.10  ? 645 LYS   A O   1 
ATOM   2726 C  CB  . LYS   A 1 349 ? -32.588 15.580  15.803 1.00 112.58 ? 645 LYS   A CB  1 
ATOM   2727 C  CG  . LYS   A 1 349 ? -34.024 15.082  15.699 1.00 121.85 ? 645 LYS   A CG  1 
ATOM   2728 C  CD  . LYS   A 1 349 ? -35.004 16.162  16.152 1.00 127.89 ? 645 LYS   A CD  1 
ATOM   2729 C  CE  . LYS   A 1 349 ? -36.443 15.813  15.788 1.00 133.11 ? 645 LYS   A CE  1 
ATOM   2730 N  NZ  . LYS   A 1 349 ? -36.960 14.648  16.561 1.00 135.77 ? 645 LYS   A NZ  1 
ATOM   2731 N  N   . VAL   A 1 350 ? -30.141 13.413  17.575 1.00 94.14  ? 646 VAL   A N   1 
ATOM   2732 C  CA  . VAL   A 1 350 ? -29.489 12.111  17.468 1.00 88.45  ? 646 VAL   A CA  1 
ATOM   2733 C  C   . VAL   A 1 350 ? -29.988 11.248  18.615 1.00 84.90  ? 646 VAL   A C   1 
ATOM   2734 O  O   . VAL   A 1 350 ? -29.850 11.619  19.789 1.00 85.23  ? 646 VAL   A O   1 
ATOM   2735 C  CB  . VAL   A 1 350 ? -27.958 12.228  17.487 1.00 85.31  ? 646 VAL   A CB  1 
ATOM   2736 C  CG1 . VAL   A 1 350 ? -27.326 10.833  17.415 1.00 77.74  ? 646 VAL   A CG1 1 
ATOM   2737 C  CG2 . VAL   A 1 350 ? -27.484 13.096  16.355 1.00 89.11  ? 646 VAL   A CG2 1 
ATOM   2738 N  N   . THR   A 1 351 ? -30.560 10.096  18.269 1.00 81.03  ? 647 THR   A N   1 
ATOM   2739 C  CA  . THR   A 1 351 ? -31.189 9.215   19.247 1.00 78.91  ? 647 THR   A CA  1 
ATOM   2740 C  C   . THR   A 1 351 ? -30.243 8.912   20.399 1.00 76.31  ? 647 THR   A C   1 
ATOM   2741 O  O   . THR   A 1 351 ? -29.080 8.557   20.193 1.00 73.92  ? 647 THR   A O   1 
ATOM   2742 C  CB  . THR   A 1 351 ? -31.624 7.912   18.563 1.00 75.88  ? 647 THR   A CB  1 
ATOM   2743 O  OG1 . THR   A 1 351 ? -32.346 8.217   17.361 1.00 77.23  ? 647 THR   A OG1 1 
ATOM   2744 C  CG2 . THR   A 1 351 ? -32.498 7.063   19.493 1.00 70.98  ? 647 THR   A CG2 1 
ATOM   2745 N  N   . ILE   A 1 352 ? -30.750 9.076   21.622 1.00 76.52  ? 648 ILE   A N   1 
ATOM   2746 C  CA  . ILE   A 1 352 ? -30.024 8.709   22.829 1.00 73.69  ? 648 ILE   A CA  1 
ATOM   2747 C  C   . ILE   A 1 352 ? -31.064 8.546   23.928 1.00 73.15  ? 648 ILE   A C   1 
ATOM   2748 O  O   . ILE   A 1 352 ? -32.119 9.184   23.899 1.00 72.65  ? 648 ILE   A O   1 
ATOM   2749 C  CB  . ILE   A 1 352 ? -28.947 9.763   23.198 1.00 73.75  ? 648 ILE   A CB  1 
ATOM   2750 C  CG1 . ILE   A 1 352 ? -27.957 9.191   24.220 1.00 73.10  ? 648 ILE   A CG1 1 
ATOM   2751 C  CG2 . ILE   A 1 352 ? -29.599 11.031  23.705 1.00 75.13  ? 648 ILE   A CG2 1 
ATOM   2752 C  CD1 . ILE   A 1 352 ? -26.676 9.979   24.311 1.00 74.19  ? 648 ILE   A CD1 1 
ATOM   2753 N  N   . VAL   A 1 353 ? -30.777 7.677   24.888 1.00 70.75  ? 649 VAL   A N   1 
ATOM   2754 C  CA  . VAL   A 1 353 ? -31.699 7.422   25.985 1.00 72.54  ? 649 VAL   A CA  1 
ATOM   2755 C  C   . VAL   A 1 353 ? -30.975 7.657   27.305 1.00 73.84  ? 649 VAL   A C   1 
ATOM   2756 O  O   . VAL   A 1 353 ? -29.816 7.265   27.476 1.00 71.57  ? 649 VAL   A O   1 
ATOM   2757 C  CB  . VAL   A 1 353 ? -32.284 5.994   25.895 1.00 75.17  ? 649 VAL   A CB  1 
ATOM   2758 C  CG1 . VAL   A 1 353 ? -31.181 4.951   25.937 1.00 74.00  ? 649 VAL   A CG1 1 
ATOM   2759 C  CG2 . VAL   A 1 353 ? -33.333 5.761   26.973 1.00 77.04  ? 649 VAL   A CG2 1 
ATOM   2760 N  N   . ASP   A 1 354 ? -31.651 8.318   28.231 1.00 74.44  ? 650 ASP   A N   1 
ATOM   2761 C  CA  . ASP   A 1 354 ? -31.051 8.577   29.521 1.00 74.76  ? 650 ASP   A CA  1 
ATOM   2762 C  C   . ASP   A 1 354 ? -31.203 7.334   30.397 1.00 74.24  ? 650 ASP   A C   1 
ATOM   2763 O  O   . ASP   A 1 354 ? -32.102 6.510   30.188 1.00 73.68  ? 650 ASP   A O   1 
ATOM   2764 C  CB  . ASP   A 1 354 ? -31.682 9.820   30.147 1.00 76.31  ? 650 ASP   A CB  1 
ATOM   2765 C  CG  . ASP   A 1 354 ? -33.130 9.606   30.577 1.00 81.72  ? 650 ASP   A CG  1 
ATOM   2766 O  OD1 . ASP   A 1 354 ? -33.398 8.675   31.365 1.00 82.67  ? 650 ASP   A OD1 1 
ATOM   2767 O  OD2 . ASP   A 1 354 ? -34.000 10.409  30.201 1.00 84.62  ? 650 ASP   A OD2 1 
ATOM   2768 N  N   . HIS   A 1 355 ? -30.303 7.178   31.370 1.00 74.08  ? 651 HIS   A N   1 
ATOM   2769 C  CA  . HIS   A 1 355 ? -30.317 5.934   32.137 1.00 71.42  ? 651 HIS   A CA  1 
ATOM   2770 C  C   . HIS   A 1 355 ? -31.598 5.768   32.944 1.00 70.97  ? 651 HIS   A C   1 
ATOM   2771 O  O   . HIS   A 1 355 ? -31.921 4.648   33.339 1.00 70.42  ? 651 HIS   A O   1 
ATOM   2772 C  CB  . HIS   A 1 355 ? -29.094 5.854   33.051 1.00 71.17  ? 651 HIS   A CB  1 
ATOM   2773 C  CG  . HIS   A 1 355 ? -28.878 7.080   33.880 1.00 71.52  ? 651 HIS   A CG  1 
ATOM   2774 N  ND1 . HIS   A 1 355 ? -28.371 8.249   33.358 1.00 70.49  ? 651 HIS   A ND1 1 
ATOM   2775 C  CD2 . HIS   A 1 355 ? -29.072 7.312   35.203 1.00 73.52  ? 651 HIS   A CD2 1 
ATOM   2776 C  CE1 . HIS   A 1 355 ? -28.271 9.152   34.319 1.00 77.36  ? 651 HIS   A CE1 1 
ATOM   2777 N  NE2 . HIS   A 1 355 ? -28.699 8.613   35.445 1.00 73.55  ? 651 HIS   A NE2 1 
ATOM   2778 N  N   . HIS   A 1 356 ? -32.345 6.846   33.175 1.00 72.14  ? 652 HIS   A N   1 
ATOM   2779 C  CA  . HIS   A 1 356 ? -33.630 6.727   33.852 1.00 74.45  ? 652 HIS   A CA  1 
ATOM   2780 C  C   . HIS   A 1 356 ? -34.694 6.159   32.926 1.00 72.95  ? 652 HIS   A C   1 
ATOM   2781 O  O   . HIS   A 1 356 ? -35.366 5.180   33.265 1.00 72.03  ? 652 HIS   A O   1 
ATOM   2782 C  CB  . HIS   A 1 356 ? -34.061 8.083   34.393 1.00 77.60  ? 652 HIS   A CB  1 
ATOM   2783 C  CG  . HIS   A 1 356 ? -33.056 8.708   35.303 1.00 77.71  ? 652 HIS   A CG  1 
ATOM   2784 N  ND1 . HIS   A 1 356 ? -32.760 8.192   36.544 1.00 78.46  ? 652 HIS   A ND1 1 
ATOM   2785 C  CD2 . HIS   A 1 356 ? -32.283 9.809   35.160 1.00 80.06  ? 652 HIS   A CD2 1 
ATOM   2786 C  CE1 . HIS   A 1 356 ? -31.848 8.947   37.128 1.00 79.95  ? 652 HIS   A CE1 1 
ATOM   2787 N  NE2 . HIS   A 1 356 ? -31.542 9.935   36.309 1.00 81.50  ? 652 HIS   A NE2 1 
ATOM   2788 N  N   . SER   A 1 357 ? -34.839 6.732   31.732 1.00 75.72  ? 653 SER   A N   1 
ATOM   2789 C  CA  . SER   A 1 357 ? -35.833 6.206   30.809 1.00 74.97  ? 653 SER   A CA  1 
ATOM   2790 C  C   . SER   A 1 357 ? -35.466 4.808   30.328 1.00 69.44  ? 653 SER   A C   1 
ATOM   2791 O  O   . SER   A 1 357 ? -36.349 3.976   30.101 1.00 70.73  ? 653 SER   A O   1 
ATOM   2792 C  CB  . SER   A 1 357 ? -36.012 7.146   29.626 1.00 78.59  ? 653 SER   A CB  1 
ATOM   2793 O  OG  . SER   A 1 357 ? -37.160 6.741   28.920 1.00 81.07  ? 653 SER   A OG  1 
ATOM   2794 N  N   . ALA   A 1 358 ? -34.170 4.522   30.183 1.00 70.00  ? 654 ALA   A N   1 
ATOM   2795 C  CA  . ALA   A 1 358 ? -33.769 3.207   29.692 1.00 73.88  ? 654 ALA   A CA  1 
ATOM   2796 C  C   . ALA   A 1 358 ? -34.074 2.122   30.716 1.00 70.99  ? 654 ALA   A C   1 
ATOM   2797 O  O   . ALA   A 1 358 ? -34.571 1.042   30.368 1.00 67.61  ? 654 ALA   A O   1 
ATOM   2798 C  CB  . ALA   A 1 358 ? -32.279 3.203   29.341 1.00 70.96  ? 654 ALA   A CB  1 
ATOM   2799 N  N   . THR   A 1 359 ? -33.791 2.396   31.991 1.00 69.79  ? 655 THR   A N   1 
ATOM   2800 C  CA  . THR   A 1 359 ? -34.034 1.387   33.010 1.00 69.06  ? 655 THR   A CA  1 
ATOM   2801 C  C   . THR   A 1 359 ? -35.523 1.221   33.267 1.00 70.16  ? 655 THR   A C   1 
ATOM   2802 O  O   . THR   A 1 359 ? -35.996 0.104   33.504 1.00 69.46  ? 655 THR   A O   1 
ATOM   2803 C  CB  . THR   A 1 359 ? -33.277 1.754   34.275 1.00 64.52  ? 655 THR   A CB  1 
ATOM   2804 O  OG1 . THR   A 1 359 ? -33.678 3.063   34.700 1.00 66.02  ? 655 THR   A OG1 1 
ATOM   2805 C  CG2 . THR   A 1 359 ? -31.792 1.746   33.968 1.00 59.59  ? 655 THR   A CG2 1 
ATOM   2806 N  N   . GLU   A 1 360 ? -36.286 2.313   33.186 1.00 69.55  ? 656 GLU   A N   1 
ATOM   2807 C  CA  . GLU   A 1 360 ? -37.732 2.189   33.333 1.00 72.85  ? 656 GLU   A CA  1 
ATOM   2808 C  C   . GLU   A 1 360 ? -38.298 1.287   32.248 1.00 72.78  ? 656 GLU   A C   1 
ATOM   2809 O  O   . GLU   A 1 360 ? -39.090 0.378   32.523 1.00 72.59  ? 656 GLU   A O   1 
ATOM   2810 C  CB  . GLU   A 1 360 ? -38.404 3.558   33.280 1.00 75.90  ? 656 GLU   A CB  1 
ATOM   2811 C  CG  . GLU   A 1 360 ? -39.909 3.492   33.523 1.00 83.33  ? 656 GLU   A CG  1 
ATOM   2812 C  CD  . GLU   A 1 360 ? -40.653 4.704   32.991 1.00 89.43  ? 656 GLU   A CD  1 
ATOM   2813 O  OE1 . GLU   A 1 360 ? -40.018 5.565   32.336 1.00 86.19  ? 656 GLU   A OE1 1 
ATOM   2814 O  OE2 . GLU   A 1 360 ? -41.879 4.793   33.230 1.00 96.47  ? 656 GLU   A OE2 1 
ATOM   2815 N  N   . SER   A 1 361 ? -37.880 1.513   31.003 1.00 75.83  ? 657 SER   A N   1 
ATOM   2816 C  CA  A SER   A 1 361 ? -38.350 0.670   29.912 0.58 78.48  ? 657 SER   A CA  1 
ATOM   2817 C  CA  B SER   A 1 361 ? -38.339 0.669   29.904 0.42 74.47  ? 657 SER   A CA  1 
ATOM   2818 C  C   . SER   A 1 361 ? -37.950 -0.786  30.120 1.00 74.80  ? 657 SER   A C   1 
ATOM   2819 O  O   . SER   A 1 361 ? -38.702 -1.696  29.744 1.00 72.45  ? 657 SER   A O   1 
ATOM   2820 C  CB  A SER   A 1 361 ? -37.814 1.199   28.585 0.58 76.06  ? 657 SER   A CB  1 
ATOM   2821 C  CB  B SER   A 1 361 ? -37.768 1.168   28.577 0.42 76.28  ? 657 SER   A CB  1 
ATOM   2822 O  OG  A SER   A 1 361 ? -38.257 2.526   28.357 0.58 74.71  ? 657 SER   A OG  1 
ATOM   2823 O  OG  B SER   A 1 361 ? -36.409 0.785   28.431 0.42 76.05  ? 657 SER   A OG  1 
ATOM   2824 N  N   . PHE   A 1 362 ? -36.784 -1.029  30.724 1.00 69.76  ? 658 PHE   A N   1 
ATOM   2825 C  CA  . PHE   A 1 362 ? -36.362 -2.409  30.923 1.00 68.53  ? 658 PHE   A CA  1 
ATOM   2826 C  C   . PHE   A 1 362 ? -37.226 -3.115  31.958 1.00 68.32  ? 658 PHE   A C   1 
ATOM   2827 O  O   . PHE   A 1 362 ? -37.532 -4.302  31.801 1.00 68.23  ? 658 PHE   A O   1 
ATOM   2828 C  CB  . PHE   A 1 362 ? -34.896 -2.486  31.328 1.00 63.42  ? 658 PHE   A CB  1 
ATOM   2829 C  CG  . PHE   A 1 362 ? -34.425 -3.886  31.514 1.00 61.94  ? 658 PHE   A CG  1 
ATOM   2830 C  CD1 . PHE   A 1 362 ? -34.233 -4.704  30.417 1.00 59.43  ? 658 PHE   A CD1 1 
ATOM   2831 C  CD2 . PHE   A 1 362 ? -34.233 -4.409  32.783 1.00 61.69  ? 658 PHE   A CD2 1 
ATOM   2832 C  CE1 . PHE   A 1 362 ? -33.824 -6.009  30.567 1.00 59.63  ? 658 PHE   A CE1 1 
ATOM   2833 C  CE2 . PHE   A 1 362 ? -33.821 -5.720  32.943 1.00 60.38  ? 658 PHE   A CE2 1 
ATOM   2834 C  CZ  . PHE   A 1 362 ? -33.620 -6.525  31.824 1.00 58.10  ? 658 PHE   A CZ  1 
ATOM   2835 N  N   . ILE   A 1 363 ? -37.612 -2.417  33.031 1.00 69.66  ? 659 ILE   A N   1 
ATOM   2836 C  CA  . ILE   A 1 363 ? -38.570 -2.997  33.967 1.00 71.96  ? 659 ILE   A CA  1 
ATOM   2837 C  C   . ILE   A 1 363 ? -39.865 -3.341  33.238 1.00 72.46  ? 659 ILE   A C   1 
ATOM   2838 O  O   . ILE   A 1 363 ? -40.377 -4.462  33.333 1.00 72.63  ? 659 ILE   A O   1 
ATOM   2839 C  CB  . ILE   A 1 363 ? -38.819 -2.042  35.148 1.00 70.49  ? 659 ILE   A CB  1 
ATOM   2840 C  CG1 . ILE   A 1 363 ? -37.542 -1.868  35.987 1.00 69.91  ? 659 ILE   A CG1 1 
ATOM   2841 C  CG2 . ILE   A 1 363 ? -39.959 -2.558  36.020 1.00 74.98  ? 659 ILE   A CG2 1 
ATOM   2842 C  CD1 . ILE   A 1 363 ? -37.228 -3.044  36.903 1.00 67.56  ? 659 ILE   A CD1 1 
ATOM   2843 N  N   . LYS   A 1 364 ? -40.405 -2.381  32.488 1.00 74.76  ? 660 LYS   A N   1 
ATOM   2844 C  CA  . LYS   A 1 364 ? -41.593 -2.657  31.682 1.00 77.21  ? 660 LYS   A CA  1 
ATOM   2845 C  C   . LYS   A 1 364 ? -41.348 -3.810  30.714 1.00 73.84  ? 660 LYS   A C   1 
ATOM   2846 O  O   . LYS   A 1 364 ? -42.200 -4.695  30.568 1.00 73.00  ? 660 LYS   A O   1 
ATOM   2847 C  CB  . LYS   A 1 364 ? -42.020 -1.401  30.921 1.00 78.42  ? 660 LYS   A CB  1 
ATOM   2848 C  CG  . LYS   A 1 364 ? -43.405 -1.486  30.291 1.00 81.20  ? 660 LYS   A CG  1 
ATOM   2849 C  CD  . LYS   A 1 364 ? -43.561 -0.449  29.185 1.00 87.67  ? 660 LYS   A CD  1 
ATOM   2850 C  CE  . LYS   A 1 364 ? -44.566 -0.891  28.125 1.00 88.40  ? 660 LYS   A CE  1 
ATOM   2851 N  NZ  . LYS   A 1 364 ? -44.449 -0.063  26.894 1.00 98.98  ? 660 LYS   A NZ  1 
ATOM   2852 N  N   . HIS   A 1 365 ? -40.179 -3.828  30.059 1.00 69.62  ? 661 HIS   A N   1 
ATOM   2853 C  CA  . HIS   A 1 365 ? -39.817 -4.968  29.218 1.00 69.91  ? 661 HIS   A CA  1 
ATOM   2854 C  C   . HIS   A 1 365 ? -39.804 -6.261  30.016 1.00 70.17  ? 661 HIS   A C   1 
ATOM   2855 O  O   . HIS   A 1 365 ? -40.296 -7.296  29.552 1.00 71.02  ? 661 HIS   A O   1 
ATOM   2856 C  CB  . HIS   A 1 365 ? -38.447 -4.764  28.574 1.00 68.50  ? 661 HIS   A CB  1 
ATOM   2857 C  CG  . HIS   A 1 365 ? -37.961 -5.966  27.818 1.00 66.76  ? 661 HIS   A CG  1 
ATOM   2858 N  ND1 . HIS   A 1 365 ? -36.732 -6.551  28.047 1.00 65.50  ? 661 HIS   A ND1 1 
ATOM   2859 C  CD2 . HIS   A 1 365 ? -38.559 -6.716  26.863 1.00 65.46  ? 661 HIS   A CD2 1 
ATOM   2860 C  CE1 . HIS   A 1 365 ? -36.587 -7.597  27.251 1.00 62.94  ? 661 HIS   A CE1 1 
ATOM   2861 N  NE2 . HIS   A 1 365 ? -37.681 -7.718  26.524 1.00 65.36  ? 661 HIS   A NE2 1 
ATOM   2862 N  N   . MET   A 1 366 ? -39.219 -6.232  31.210 1.00 72.85  ? 662 MET   A N   1 
ATOM   2863 C  CA  . MET   A 1 366 ? -39.184 -7.436  32.025 1.00 71.41  ? 662 MET   A CA  1 
ATOM   2864 C  C   . MET   A 1 366 ? -40.590 -7.934  32.319 1.00 74.18  ? 662 MET   A C   1 
ATOM   2865 O  O   . MET   A 1 366 ? -40.861 -9.136  32.235 1.00 76.82  ? 662 MET   A O   1 
ATOM   2866 C  CB  . MET   A 1 366 ? -38.428 -7.153  33.318 1.00 68.80  ? 662 MET   A CB  1 
ATOM   2867 C  CG  . MET   A 1 366 ? -37.163 -7.941  33.472 1.00 64.89  ? 662 MET   A CG  1 
ATOM   2868 S  SD  . MET   A 1 366 ? -36.432 -7.458  35.044 1.00 68.40  ? 662 MET   A SD  1 
ATOM   2869 C  CE  . MET   A 1 366 ? -35.932 -9.050  35.690 1.00 68.00  ? 662 MET   A CE  1 
ATOM   2870 N  N   . GLU   A 1 367 ? -41.503 -7.017  32.647 1.00 69.22  ? 663 GLU   A N   1 
ATOM   2871 C  CA  . GLU   A 1 367 ? -42.874 -7.409  32.947 1.00 76.19  ? 663 GLU   A CA  1 
ATOM   2872 C  C   . GLU   A 1 367 ? -43.515 -8.116  31.765 1.00 78.54  ? 663 GLU   A C   1 
ATOM   2873 O  O   . GLU   A 1 367 ? -44.209 -9.125  31.938 1.00 82.84  ? 663 GLU   A O   1 
ATOM   2874 C  CB  . GLU   A 1 367 ? -43.691 -6.182  33.342 1.00 78.57  ? 663 GLU   A CB  1 
ATOM   2875 C  CG  . GLU   A 1 367 ? -43.226 -5.513  34.636 1.00 83.30  ? 663 GLU   A CG  1 
ATOM   2876 C  CD  . GLU   A 1 367 ? -43.961 -4.214  34.892 1.00 87.54  ? 663 GLU   A CD  1 
ATOM   2877 O  OE1 . GLU   A 1 367 ? -44.847 -3.867  34.072 1.00 91.75  ? 663 GLU   A OE1 1 
ATOM   2878 O  OE2 . GLU   A 1 367 ? -43.653 -3.543  35.900 1.00 92.14  ? 663 GLU   A OE2 1 
ATOM   2879 N  N   . ASN   A 1 368 ? -43.297 -7.594  30.555 1.00 80.26  ? 664 ASN   A N   1 
ATOM   2880 C  CA  . ASN   A 1 368 ? -43.825 -8.231  29.355 1.00 80.77  ? 664 ASN   A CA  1 
ATOM   2881 C  C   . ASN   A 1 368 ? -43.245 -9.629  29.165 1.00 83.03  ? 664 ASN   A C   1 
ATOM   2882 O  O   . ASN   A 1 368 ? -43.972 -10.568 28.820 1.00 89.73  ? 664 ASN   A O   1 
ATOM   2883 C  CB  . ASN   A 1 368 ? -43.525 -7.362  28.133 1.00 78.75  ? 664 ASN   A CB  1 
ATOM   2884 C  CG  . ASN   A 1 368 ? -44.162 -5.981  28.217 1.00 80.91  ? 664 ASN   A CG  1 
ATOM   2885 O  OD1 . ASN   A 1 368 ? -45.122 -5.767  28.966 1.00 82.65  ? 664 ASN   A OD1 1 
ATOM   2886 N  ND2 . ASN   A 1 368 ? -43.636 -5.037  27.436 1.00 78.21  ? 664 ASN   A ND2 1 
ATOM   2887 N  N   . GLU   A 1 369 ? -41.936 -9.788  29.388 1.00 80.36  ? 665 GLU   A N   1 
ATOM   2888 C  CA  . GLU   A 1 369 ? -41.306 -11.085 29.163 1.00 79.38  ? 665 GLU   A CA  1 
ATOM   2889 C  C   . GLU   A 1 369 ? -41.783 -12.118 30.175 1.00 84.38  ? 665 GLU   A C   1 
ATOM   2890 O  O   . GLU   A 1 369 ? -42.045 -13.267 29.812 1.00 85.10  ? 665 GLU   A O   1 
ATOM   2891 C  CB  . GLU   A 1 369 ? -39.786 -10.954 29.211 1.00 72.30  ? 665 GLU   A CB  1 
ATOM   2892 C  CG  . GLU   A 1 369 ? -39.196 -10.052 28.147 1.00 72.33  ? 665 GLU   A CG  1 
ATOM   2893 C  CD  . GLU   A 1 369 ? -38.981 -10.765 26.812 1.00 69.72  ? 665 GLU   A CD  1 
ATOM   2894 O  OE1 . GLU   A 1 369 ? -39.975 -11.223 26.209 1.00 67.22  ? 665 GLU   A OE1 1 
ATOM   2895 O  OE2 . GLU   A 1 369 ? -37.811 -10.879 26.385 1.00 69.12  ? 665 GLU   A OE2 1 
ATOM   2896 N  N   . TYR   A 1 370 ? -41.898 -11.740 31.452 1.00 83.69  ? 666 TYR   A N   1 
ATOM   2897 C  CA  . TYR   A 1 370 ? -42.425 -12.686 32.430 1.00 85.74  ? 666 TYR   A CA  1 
ATOM   2898 C  C   . TYR   A 1 370 ? -43.865 -13.072 32.107 1.00 91.48  ? 666 TYR   A C   1 
ATOM   2899 O  O   . TYR   A 1 370 ? -44.252 -14.233 32.287 1.00 92.64  ? 666 TYR   A O   1 
ATOM   2900 C  CB  . TYR   A 1 370 ? -42.296 -12.107 33.843 1.00 81.70  ? 666 TYR   A CB  1 
ATOM   2901 C  CG  . TYR   A 1 370 ? -40.904 -12.298 34.397 1.00 79.22  ? 666 TYR   A CG  1 
ATOM   2902 C  CD1 . TYR   A 1 370 ? -39.860 -11.489 33.984 1.00 74.41  ? 666 TYR   A CD1 1 
ATOM   2903 C  CD2 . TYR   A 1 370 ? -40.629 -13.307 35.313 1.00 80.97  ? 666 TYR   A CD2 1 
ATOM   2904 C  CE1 . TYR   A 1 370 ? -38.583 -11.667 34.462 1.00 72.04  ? 666 TYR   A CE1 1 
ATOM   2905 C  CE2 . TYR   A 1 370 ? -39.350 -13.489 35.810 1.00 79.24  ? 666 TYR   A CE2 1 
ATOM   2906 C  CZ  . TYR   A 1 370 ? -38.330 -12.669 35.371 1.00 74.62  ? 666 TYR   A CZ  1 
ATOM   2907 O  OH  . TYR   A 1 370 ? -37.055 -12.846 35.863 1.00 74.98  ? 666 TYR   A OH  1 
ATOM   2908 N  N   . ARG   A 1 371 ? -44.659 -12.134 31.591 1.00 102.03 ? 667 ARG   A N   1 
ATOM   2909 C  CA  . ARG   A 1 371 ? -46.044 -12.427 31.245 1.00 105.65 ? 667 ARG   A CA  1 
ATOM   2910 C  C   . ARG   A 1 371 ? -46.133 -13.434 30.101 1.00 105.43 ? 667 ARG   A C   1 
ATOM   2911 O  O   . ARG   A 1 371 ? -46.602 -14.560 30.296 1.00 107.81 ? 667 ARG   A O   1 
ATOM   2912 C  CB  . ARG   A 1 371 ? -46.785 -11.139 30.878 1.00 111.74 ? 667 ARG   A CB  1 
ATOM   2913 C  CG  . ARG   A 1 371 ? -48.275 -11.321 30.640 1.00 122.15 ? 667 ARG   A CG  1 
ATOM   2914 C  CD  . ARG   A 1 371 ? -48.871 -10.103 29.949 1.00 129.26 ? 667 ARG   A CD  1 
ATOM   2915 N  NE  . ARG   A 1 371 ? -48.153 -9.772  28.724 1.00 127.52 ? 667 ARG   A NE  1 
ATOM   2916 C  CZ  . ARG   A 1 371 ? -48.437 -10.266 27.524 1.00 130.46 ? 667 ARG   A CZ  1 
ATOM   2917 N  NH1 . ARG   A 1 371 ? -49.434 -11.120 27.343 1.00 137.06 ? 667 ARG   A NH1 1 
ATOM   2918 N  NH2 . ARG   A 1 371 ? -47.704 -9.893  26.478 1.00 127.54 ? 667 ARG   A NH2 1 
ATOM   2919 N  N   . CYS   A 1 372 ? -45.671 -13.054 28.909 1.00 108.08 ? 668 CYS   A N   1 
ATOM   2920 C  CA  . CYS   A 1 372 ? -45.901 -13.846 27.707 1.00 109.38 ? 668 CYS   A CA  1 
ATOM   2921 C  C   . CYS   A 1 372 ? -44.709 -14.709 27.307 1.00 104.52 ? 668 CYS   A C   1 
ATOM   2922 O  O   . CYS   A 1 372 ? -44.701 -15.255 26.198 1.00 107.40 ? 668 CYS   A O   1 
ATOM   2923 C  CB  . CYS   A 1 372 ? -46.296 -12.932 26.545 1.00 115.78 ? 668 CYS   A CB  1 
ATOM   2924 S  SG  . CYS   A 1 372 ? -45.007 -11.774 26.007 1.00 125.11 ? 668 CYS   A SG  1 
ATOM   2925 N  N   . ARG   A 1 373 ? -43.702 -14.841 28.170 1.00 94.30  ? 669 ARG   A N   1 
ATOM   2926 C  CA  . ARG   A 1 373 ? -42.576 -15.731 27.898 1.00 88.61  ? 669 ARG   A CA  1 
ATOM   2927 C  C   . ARG   A 1 373 ? -42.114 -16.520 29.114 1.00 86.85  ? 669 ARG   A C   1 
ATOM   2928 O  O   . ARG   A 1 373 ? -41.308 -17.444 28.955 1.00 81.20  ? 669 ARG   A O   1 
ATOM   2929 C  CB  . ARG   A 1 373 ? -41.380 -14.938 27.346 1.00 80.36  ? 669 ARG   A CB  1 
ATOM   2930 C  CG  . ARG   A 1 373 ? -40.392 -15.765 26.525 1.00 75.33  ? 669 ARG   A CG  1 
ATOM   2931 C  CD  . ARG   A 1 373 ? -39.075 -15.019 26.303 1.00 71.71  ? 669 ARG   A CD  1 
ATOM   2932 N  NE  . ARG   A 1 373 ? -38.214 -15.727 25.361 1.00 66.73  ? 669 ARG   A NE  1 
ATOM   2933 C  CZ  . ARG   A 1 373 ? -36.934 -15.449 25.159 1.00 66.16  ? 669 ARG   A CZ  1 
ATOM   2934 N  NH1 . ARG   A 1 373 ? -36.327 -14.470 25.814 1.00 62.23  ? 669 ARG   A NH1 1 
ATOM   2935 N  NH2 . ARG   A 1 373 ? -36.243 -16.173 24.282 1.00 62.09  ? 669 ARG   A NH2 1 
ATOM   2936 N  N   . GLY   A 1 374 ? -42.578 -16.185 30.317 1.00 87.48  ? 670 GLY   A N   1 
ATOM   2937 C  CA  . GLY   A 1 374 ? -42.198 -16.884 31.522 1.00 88.19  ? 670 GLY   A CA  1 
ATOM   2938 C  C   . GLY   A 1 374 ? -40.904 -16.429 32.157 1.00 85.67  ? 670 GLY   A C   1 
ATOM   2939 O  O   . GLY   A 1 374 ? -40.453 -17.062 33.121 1.00 84.11  ? 670 GLY   A O   1 
ATOM   2940 N  N   . GLY   A 1 375 ? -40.291 -15.367 31.659 1.00 78.66  ? 671 GLY   A N   1 
ATOM   2941 C  CA  . GLY   A 1 375 ? -39.060 -14.890 32.250 1.00 75.40  ? 671 GLY   A CA  1 
ATOM   2942 C  C   . GLY   A 1 375 ? -38.297 -13.992 31.303 1.00 73.76  ? 671 GLY   A C   1 
ATOM   2943 O  O   . GLY   A 1 375 ? -38.672 -13.792 30.145 1.00 74.53  ? 671 GLY   A O   1 
ATOM   2944 N  N   . CYS   A 1 376 ? -37.203 -13.454 31.838 1.00 70.80  ? 672 CYS   A N   1 
ATOM   2945 C  CA  . CYS   A 1 376 ? -36.328 -12.545 31.104 1.00 65.58  ? 672 CYS   A CA  1 
ATOM   2946 C  C   . CYS   A 1 376 ? -34.963 -12.637 31.747 1.00 63.15  ? 672 CYS   A C   1 
ATOM   2947 O  O   . CYS   A 1 376 ? -34.734 -12.061 32.824 1.00 63.00  ? 672 CYS   A O   1 
ATOM   2948 C  CB  . CYS   A 1 376 ? -36.849 -11.112 31.133 1.00 64.95  ? 672 CYS   A CB  1 
ATOM   2949 S  SG  . CYS   A 1 376 ? -35.773 -9.912  30.295 1.00 62.14  ? 672 CYS   A SG  1 
ATOM   2950 N  N   . PRO   A 1 377 ? -34.022 -13.359 31.148 1.00 62.03  ? 673 PRO   A N   1 
ATOM   2951 C  CA  . PRO   A 1 377 ? -32.674 -13.433 31.718 1.00 59.67  ? 673 PRO   A CA  1 
ATOM   2952 C  C   . PRO   A 1 377 ? -32.068 -12.043 31.806 1.00 58.13  ? 673 PRO   A C   1 
ATOM   2953 O  O   . PRO   A 1 377 ? -32.103 -11.274 30.843 1.00 53.77  ? 673 PRO   A O   1 
ATOM   2954 C  CB  . PRO   A 1 377 ? -31.914 -14.319 30.729 1.00 60.17  ? 673 PRO   A CB  1 
ATOM   2955 C  CG  . PRO   A 1 377 ? -32.644 -14.130 29.407 1.00 59.37  ? 673 PRO   A CG  1 
ATOM   2956 C  CD  . PRO   A 1 377 ? -34.092 -13.903 29.769 1.00 59.53  ? 673 PRO   A CD  1 
ATOM   2957 N  N   . ALA   A 1 378 ? -31.519 -11.711 32.976 1.00 55.11  ? 674 ALA   A N   1 
ATOM   2958 C  CA  . ALA   A 1 378 ? -31.007 -10.365 33.183 1.00 52.30  ? 674 ALA   A CA  1 
ATOM   2959 C  C   . ALA   A 1 378 ? -29.819 -10.395 34.135 1.00 53.87  ? 674 ALA   A C   1 
ATOM   2960 O  O   . ALA   A 1 378 ? -29.824 -11.126 35.128 1.00 54.46  ? 674 ALA   A O   1 
ATOM   2961 C  CB  . ALA   A 1 378 ? -32.114 -9.440  33.700 1.00 55.31  ? 674 ALA   A CB  1 
ATOM   2962 N  N   . ASP   A 1 379 ? -28.799 -9.609  33.803 1.00 51.55  ? 675 ASP   A N   1 
ATOM   2963 C  CA  . ASP   A 1 379 ? -27.538 -9.562  34.528 1.00 50.20  ? 675 ASP   A CA  1 
ATOM   2964 C  C   . ASP   A 1 379 ? -27.539 -8.226  35.254 1.00 53.05  ? 675 ASP   A C   1 
ATOM   2965 O  O   . ASP   A 1 379 ? -27.244 -7.174  34.668 1.00 48.40  ? 675 ASP   A O   1 
ATOM   2966 C  CB  . ASP   A 1 379 ? -26.343 -9.701  33.594 1.00 51.34  ? 675 ASP   A CB  1 
ATOM   2967 C  CG  . ASP   A 1 379 ? -25.025 -9.759  34.324 1.00 53.64  ? 675 ASP   A CG  1 
ATOM   2968 O  OD1 . ASP   A 1 379 ? -24.951 -9.337  35.505 1.00 53.67  ? 675 ASP   A OD1 1 
ATOM   2969 O  OD2 . ASP   A 1 379 ? -24.044 -10.223 33.714 1.00 51.57  ? 675 ASP   A OD2 1 
ATOM   2970 N  N   . TRP   A 1 380 ? -27.893 -8.283  36.537 1.00 49.50  ? 676 TRP   A N   1 
ATOM   2971 C  CA  . TRP   A 1 380 ? -27.970 -7.085  37.343 1.00 48.07  ? 676 TRP   A CA  1 
ATOM   2972 C  C   . TRP   A 1 380 ? -26.682 -6.288  37.261 1.00 47.24  ? 676 TRP   A C   1 
ATOM   2973 O  O   . TRP   A 1 380 ? -26.705 -5.065  37.124 1.00 48.61  ? 676 TRP   A O   1 
ATOM   2974 C  CB  . TRP   A 1 380 ? -28.259 -7.507  38.793 1.00 51.28  ? 676 TRP   A CB  1 
ATOM   2975 C  CG  . TRP   A 1 380 ? -28.717 -6.440  39.658 1.00 51.55  ? 676 TRP   A CG  1 
ATOM   2976 C  CD1 . TRP   A 1 380 ? -30.009 -6.164  39.996 1.00 54.25  ? 676 TRP   A CD1 1 
ATOM   2977 C  CD2 . TRP   A 1 380 ? -27.904 -5.502  40.361 1.00 50.87  ? 676 TRP   A CD2 1 
ATOM   2978 N  NE1 . TRP   A 1 380 ? -30.048 -5.110  40.857 1.00 56.70  ? 676 TRP   A NE1 1 
ATOM   2979 C  CE2 . TRP   A 1 380 ? -28.769 -4.689  41.113 1.00 56.46  ? 676 TRP   A CE2 1 
ATOM   2980 C  CE3 . TRP   A 1 380 ? -26.528 -5.277  40.438 1.00 50.13  ? 676 TRP   A CE3 1 
ATOM   2981 C  CZ2 . TRP   A 1 380 ? -28.305 -3.642  41.927 1.00 55.18  ? 676 TRP   A CZ2 1 
ATOM   2982 C  CZ3 . TRP   A 1 380 ? -26.065 -4.242  41.252 1.00 53.41  ? 676 TRP   A CZ3 1 
ATOM   2983 C  CH2 . TRP   A 1 380 ? -26.955 -3.437  41.981 1.00 51.56  ? 676 TRP   A CH2 1 
ATOM   2984 N  N   . VAL   A 1 381 ? -25.541 -6.969  37.375 1.00 46.74  ? 677 VAL   A N   1 
ATOM   2985 C  CA  . VAL   A 1 381 ? -24.242 -6.300  37.395 1.00 49.42  ? 677 VAL   A CA  1 
ATOM   2986 C  C   . VAL   A 1 381 ? -24.086 -5.393  36.194 1.00 51.01  ? 677 VAL   A C   1 
ATOM   2987 O  O   . VAL   A 1 381 ? -23.466 -4.328  36.291 1.00 48.10  ? 677 VAL   A O   1 
ATOM   2988 C  CB  . VAL   A 1 381 ? -23.114 -7.353  37.473 1.00 49.15  ? 677 VAL   A CB  1 
ATOM   2989 C  CG1 . VAL   A 1 381 ? -21.755 -6.732  37.192 1.00 50.16  ? 677 VAL   A CG1 1 
ATOM   2990 C  CG2 . VAL   A 1 381 ? -23.107 -7.997  38.863 1.00 52.67  ? 677 VAL   A CG2 1 
ATOM   2991 N  N   . TRP   A 1 382 ? -24.664 -5.784  35.047 1.00 50.49  ? 678 TRP   A N   1 
ATOM   2992 C  CA  . TRP   A 1 382 ? -24.597 -5.004  33.821 1.00 52.90  ? 678 TRP   A CA  1 
ATOM   2993 C  C   . TRP   A 1 382 ? -25.816 -4.129  33.577 1.00 51.70  ? 678 TRP   A C   1 
ATOM   2994 O  O   . TRP   A 1 382 ? -25.676 -3.062  32.958 1.00 51.17  ? 678 TRP   A O   1 
ATOM   2995 C  CB  . TRP   A 1 382 ? -24.415 -5.938  32.622 1.00 52.80  ? 678 TRP   A CB  1 
ATOM   2996 C  CG  . TRP   A 1 382 ? -22.984 -6.285  32.375 1.00 55.18  ? 678 TRP   A CG  1 
ATOM   2997 C  CD1 . TRP   A 1 382 ? -22.145 -6.987  33.202 1.00 56.76  ? 678 TRP   A CD1 1 
ATOM   2998 C  CD2 . TRP   A 1 382 ? -22.211 -5.937  31.215 1.00 55.81  ? 678 TRP   A CD2 1 
ATOM   2999 N  NE1 . TRP   A 1 382 ? -20.895 -7.097  32.615 1.00 59.70  ? 678 TRP   A NE1 1 
ATOM   3000 C  CE2 . TRP   A 1 382 ? -20.914 -6.459  31.399 1.00 57.90  ? 678 TRP   A CE2 1 
ATOM   3001 C  CE3 . TRP   A 1 382 ? -22.494 -5.239  30.048 1.00 57.11  ? 678 TRP   A CE3 1 
ATOM   3002 C  CZ2 . TRP   A 1 382 ? -19.899 -6.295  30.455 1.00 57.78  ? 678 TRP   A CZ2 1 
ATOM   3003 C  CZ3 . TRP   A 1 382 ? -21.485 -5.085  29.093 1.00 57.64  ? 678 TRP   A CZ3 1 
ATOM   3004 C  CH2 . TRP   A 1 382 ? -20.208 -5.617  29.304 1.00 59.36  ? 678 TRP   A CH2 1 
ATOM   3005 N  N   . ILE   A 1 383 ? -27.007 -4.550  34.023 1.00 51.36  ? 679 ILE   A N   1 
ATOM   3006 C  CA  . ILE   A 1 383 ? -28.211 -3.764  33.753 1.00 50.56  ? 679 ILE   A CA  1 
ATOM   3007 C  C   . ILE   A 1 383 ? -28.186 -2.461  34.551 1.00 56.06  ? 679 ILE   A C   1 
ATOM   3008 O  O   . ILE   A 1 383 ? -28.576 -1.401  34.049 1.00 54.64  ? 679 ILE   A O   1 
ATOM   3009 C  CB  . ILE   A 1 383 ? -29.472 -4.594  34.067 1.00 50.64  ? 679 ILE   A CB  1 
ATOM   3010 C  CG1 . ILE   A 1 383 ? -29.589 -5.794  33.129 1.00 51.22  ? 679 ILE   A CG1 1 
ATOM   3011 C  CG2 . ILE   A 1 383 ? -30.740 -3.719  34.040 1.00 51.27  ? 679 ILE   A CG2 1 
ATOM   3012 C  CD1 . ILE   A 1 383 ? -29.894 -5.411  31.635 1.00 53.66  ? 679 ILE   A CD1 1 
ATOM   3013 N  N   . VAL   A 1 384 ? -27.735 -2.510  35.801 1.00 52.40  ? 680 VAL   A N   1 
ATOM   3014 C  CA  . VAL   A 1 384 ? -27.749 -1.287  36.623 1.00 53.10  ? 680 VAL   A CA  1 
ATOM   3015 C  C   . VAL   A 1 384 ? -26.754 -0.283  36.053 1.00 54.40  ? 680 VAL   A C   1 
ATOM   3016 O  O   . VAL   A 1 384 ? -25.578 -0.625  35.863 1.00 52.55  ? 680 VAL   A O   1 
ATOM   3017 C  CB  . VAL   A 1 384 ? -27.417 -1.615  38.076 1.00 54.83  ? 680 VAL   A CB  1 
ATOM   3018 C  CG1 . VAL   A 1 384 ? -27.271 -0.332  38.903 1.00 56.74  ? 680 VAL   A CG1 1 
ATOM   3019 C  CG2 . VAL   A 1 384 ? -28.497 -2.490  38.653 1.00 56.48  ? 680 VAL   A CG2 1 
ATOM   3020 N  N   . PRO   A 1 385 ? -27.167 0.952   35.774 1.00 56.28  ? 681 PRO   A N   1 
ATOM   3021 C  CA  . PRO   A 1 385 ? -26.245 1.960   35.200 1.00 57.19  ? 681 PRO   A CA  1 
ATOM   3022 C  C   . PRO   A 1 385 ? -25.061 2.249   36.106 1.00 62.34  ? 681 PRO   A C   1 
ATOM   3023 O  O   . PRO   A 1 385 ? -25.136 2.041   37.325 1.00 56.42  ? 681 PRO   A O   1 
ATOM   3024 C  CB  . PRO   A 1 385 ? -27.132 3.200   35.078 1.00 59.98  ? 681 PRO   A CB  1 
ATOM   3025 C  CG  . PRO   A 1 385 ? -28.497 2.674   34.970 1.00 63.30  ? 681 PRO   A CG  1 
ATOM   3026 C  CD  . PRO   A 1 385 ? -28.556 1.451   35.837 1.00 60.48  ? 681 PRO   A CD  1 
ATOM   3027 N  N   . PRO   A 1 386 ? -23.960 2.760   35.553 1.00 62.23  ? 682 PRO   A N   1 
ATOM   3028 C  CA  . PRO   A 1 386 ? -22.740 3.013   36.333 1.00 62.23  ? 682 PRO   A CA  1 
ATOM   3029 C  C   . PRO   A 1 386 ? -22.724 4.337   37.089 1.00 64.68  ? 682 PRO   A C   1 
ATOM   3030 O  O   . PRO   A 1 386 ? -21.657 4.739   37.574 1.00 67.54  ? 682 PRO   A O   1 
ATOM   3031 C  CB  . PRO   A 1 386 ? -21.674 3.020   35.232 1.00 64.47  ? 682 PRO   A CB  1 
ATOM   3032 C  CG  . PRO   A 1 386 ? -22.389 3.757   34.149 1.00 61.09  ? 682 PRO   A CG  1 
ATOM   3033 C  CD  . PRO   A 1 386 ? -23.773 3.145   34.145 1.00 61.07  ? 682 PRO   A CD  1 
ATOM   3034 N  N   . MET   A 1 387 ? -23.863 5.024   37.190 1.00 66.46  ? 683 MET   A N   1 
ATOM   3035 C  CA  . MET   A 1 387 ? -24.046 6.113   38.145 1.00 67.40  ? 683 MET   A CA  1 
ATOM   3036 C  C   . MET   A 1 387 ? -25.491 6.074   38.611 1.00 68.73  ? 683 MET   A C   1 
ATOM   3037 O  O   . MET   A 1 387 ? -26.359 5.522   37.921 1.00 66.42  ? 683 MET   A O   1 
ATOM   3038 C  CB  . MET   A 1 387 ? -23.759 7.485   37.513 1.00 76.40  ? 683 MET   A CB  1 
ATOM   3039 C  CG  . MET   A 1 387 ? -24.828 7.872   36.496 1.00 69.97  ? 683 MET   A CG  1 
ATOM   3040 S  SD  . MET   A 1 387 ? -24.538 9.442   35.638 1.00 86.07  ? 683 MET   A SD  1 
ATOM   3041 C  CE  . MET   A 1 387 ? -24.355 10.559  37.009 1.00 79.63  ? 683 MET   A CE  1 
ATOM   3042 N  N   . SER   A 1 388 ? -25.734 6.616   39.801 1.00 71.48  ? 684 SER   A N   1 
ATOM   3043 C  CA  . SER   A 1 388 ? -27.093 6.809   40.295 1.00 70.95  ? 684 SER   A CA  1 
ATOM   3044 C  C   . SER   A 1 388 ? -27.853 5.491   40.382 1.00 67.61  ? 684 SER   A C   1 
ATOM   3045 O  O   . SER   A 1 388 ? -29.067 5.460   40.180 1.00 72.68  ? 684 SER   A O   1 
ATOM   3046 C  CB  . SER   A 1 388 ? -27.860 7.792   39.403 1.00 72.70  ? 684 SER   A CB  1 
ATOM   3047 O  OG  . SER   A 1 388 ? -27.282 9.088   39.424 1.00 78.47  ? 684 SER   A OG  1 
ATOM   3048 N  N   . GLY   A 1 389 ? -27.134 4.395   40.636 1.00 65.31  ? 685 GLY   A N   1 
ATOM   3049 C  CA  . GLY   A 1 389 ? -27.743 3.074   40.527 1.00 65.74  ? 685 GLY   A CA  1 
ATOM   3050 C  C   . GLY   A 1 389 ? -29.107 2.959   41.188 1.00 66.68  ? 685 GLY   A C   1 
ATOM   3051 O  O   . GLY   A 1 389 ? -30.076 2.509   40.575 1.00 64.54  ? 685 GLY   A O   1 
ATOM   3052 N  N   . SER   A 1 390 ? -29.206 3.368   42.455 1.00 66.92  ? 686 SER   A N   1 
ATOM   3053 C  CA  . SER   A 1 390 ? -30.406 3.044   43.218 1.00 66.32  ? 686 SER   A CA  1 
ATOM   3054 C  C   . SER   A 1 390 ? -31.532 4.048   43.039 1.00 68.98  ? 686 SER   A C   1 
ATOM   3055 O  O   . SER   A 1 390 ? -32.603 3.852   43.621 1.00 68.86  ? 686 SER   A O   1 
ATOM   3056 C  CB  . SER   A 1 390 ? -30.091 2.938   44.703 1.00 64.82  ? 686 SER   A CB  1 
ATOM   3057 O  OG  . SER   A 1 390 ? -29.651 4.204   45.106 1.00 65.80  ? 686 SER   A OG  1 
ATOM   3058 N  N   . ILE   A 1 391 ? -31.335 5.131   42.277 1.00 70.98  ? 687 ILE   A N   1 
ATOM   3059 C  CA  . ILE   A 1 391 ? -32.480 5.958   41.924 1.00 68.24  ? 687 ILE   A CA  1 
ATOM   3060 C  C   . ILE   A 1 391 ? -33.064 5.562   40.575 1.00 70.12  ? 687 ILE   A C   1 
ATOM   3061 O  O   . ILE   A 1 391 ? -33.961 6.251   40.075 1.00 73.75  ? 687 ILE   A O   1 
ATOM   3062 C  CB  . ILE   A 1 391 ? -32.143 7.463   41.958 1.00 73.93  ? 687 ILE   A CB  1 
ATOM   3063 C  CG1 . ILE   A 1 391 ? -31.088 7.828   40.917 1.00 79.94  ? 687 ILE   A CG1 1 
ATOM   3064 C  CG2 . ILE   A 1 391 ? -31.724 7.910   43.369 1.00 79.37  ? 687 ILE   A CG2 1 
ATOM   3065 C  CD1 . ILE   A 1 391 ? -30.769 9.323   40.922 1.00 83.75  ? 687 ILE   A CD1 1 
ATOM   3066 N  N   . THR   A 1 392 ? -32.598 4.468   39.986 1.00 70.28  ? 688 THR   A N   1 
ATOM   3067 C  CA  . THR   A 1 392 ? -33.210 3.810   38.839 1.00 71.53  ? 688 THR   A CA  1 
ATOM   3068 C  C   . THR   A 1 392 ? -33.904 2.530   39.292 1.00 68.69  ? 688 THR   A C   1 
ATOM   3069 O  O   . THR   A 1 392 ? -33.443 1.870   40.227 1.00 69.02  ? 688 THR   A O   1 
ATOM   3070 C  CB  . THR   A 1 392 ? -32.193 3.457   37.741 1.00 70.71  ? 688 THR   A CB  1 
ATOM   3071 O  OG1 . THR   A 1 392 ? -31.401 2.329   38.155 1.00 67.46  ? 688 THR   A OG1 1 
ATOM   3072 C  CG2 . THR   A 1 392 ? -31.295 4.655   37.418 1.00 67.05  ? 688 THR   A CG2 1 
ATOM   3073 N  N   . PRO   A 1 393 ? -35.001 2.138   38.635 1.00 67.96  ? 689 PRO   A N   1 
ATOM   3074 C  CA  . PRO   A 1 393 ? -35.798 1.014   39.155 1.00 68.50  ? 689 PRO   A CA  1 
ATOM   3075 C  C   . PRO   A 1 393 ? -35.130 -0.352  39.025 1.00 66.51  ? 689 PRO   A C   1 
ATOM   3076 O  O   . PRO   A 1 393 ? -35.503 -1.269  39.774 1.00 66.04  ? 689 PRO   A O   1 
ATOM   3077 C  CB  . PRO   A 1 393 ? -37.084 1.087   38.319 1.00 71.48  ? 689 PRO   A CB  1 
ATOM   3078 C  CG  . PRO   A 1 393 ? -36.596 1.635   36.983 1.00 69.11  ? 689 PRO   A CG  1 
ATOM   3079 C  CD  . PRO   A 1 393 ? -35.585 2.697   37.402 1.00 69.56  ? 689 PRO   A CD  1 
ATOM   3080 N  N   . VAL   A 1 394 ? -34.147 -0.523  38.136 1.00 63.95  ? 690 VAL   A N   1 
ATOM   3081 C  CA  . VAL   A 1 394 ? -33.511 -1.834  37.997 1.00 63.97  ? 690 VAL   A CA  1 
ATOM   3082 C  C   . VAL   A 1 394 ? -32.648 -2.186  39.220 1.00 62.47  ? 690 VAL   A C   1 
ATOM   3083 O  O   . VAL   A 1 394 ? -32.423 -3.372  39.503 1.00 61.74  ? 690 VAL   A O   1 
ATOM   3084 C  CB  . VAL   A 1 394 ? -32.693 -1.894  36.691 1.00 61.30  ? 690 VAL   A CB  1 
ATOM   3085 C  CG1 . VAL   A 1 394 ? -33.613 -1.748  35.475 1.00 62.59  ? 690 VAL   A CG1 1 
ATOM   3086 C  CG2 . VAL   A 1 394 ? -31.632 -0.824  36.687 1.00 61.58  ? 690 VAL   A CG2 1 
ATOM   3087 N  N   . PHE   A 1 395 ? -32.152 -1.184  39.962 1.00 62.71  ? 691 PHE   A N   1 
ATOM   3088 C  CA  . PHE   A 1 395 ? -31.373 -1.464  41.176 1.00 63.52  ? 691 PHE   A CA  1 
ATOM   3089 C  C   . PHE   A 1 395 ? -32.166 -2.306  42.161 1.00 61.22  ? 691 PHE   A C   1 
ATOM   3090 O  O   . PHE   A 1 395 ? -31.621 -3.205  42.814 1.00 61.35  ? 691 PHE   A O   1 
ATOM   3091 C  CB  . PHE   A 1 395 ? -30.944 -0.155  41.843 1.00 62.82  ? 691 PHE   A CB  1 
ATOM   3092 C  CG  . PHE   A 1 395 ? -30.082 -0.333  43.077 1.00 61.62  ? 691 PHE   A CG  1 
ATOM   3093 C  CD1 . PHE   A 1 395 ? -30.659 -0.495  44.334 1.00 63.85  ? 691 PHE   A CD1 1 
ATOM   3094 C  CD2 . PHE   A 1 395 ? -28.698 -0.310  42.983 1.00 58.58  ? 691 PHE   A CD2 1 
ATOM   3095 C  CE1 . PHE   A 1 395 ? -29.860 -0.640  45.482 1.00 62.23  ? 691 PHE   A CE1 1 
ATOM   3096 C  CE2 . PHE   A 1 395 ? -27.901 -0.469  44.113 1.00 62.54  ? 691 PHE   A CE2 1 
ATOM   3097 C  CZ  . PHE   A 1 395 ? -28.476 -0.621  45.366 1.00 60.37  ? 691 PHE   A CZ  1 
ATOM   3098 N  N   . HIS   A 1 396 ? -33.453 -2.026  42.284 1.00 62.89  ? 692 HIS   A N   1 
ATOM   3099 C  CA  . HIS   A 1 396 ? -34.302 -2.670  43.264 1.00 65.27  ? 692 HIS   A CA  1 
ATOM   3100 C  C   . HIS   A 1 396 ? -34.985 -3.904  42.722 1.00 66.86  ? 692 HIS   A C   1 
ATOM   3101 O  O   . HIS   A 1 396 ? -35.827 -4.484  43.408 1.00 67.44  ? 692 HIS   A O   1 
ATOM   3102 C  CB  . HIS   A 1 396 ? -35.329 -1.663  43.766 1.00 70.69  ? 692 HIS   A CB  1 
ATOM   3103 C  CG  . HIS   A 1 396 ? -34.716 -0.363  44.172 1.00 70.38  ? 692 HIS   A CG  1 
ATOM   3104 N  ND1 . HIS   A 1 396 ? -33.873 -0.247  45.255 1.00 69.64  ? 692 HIS   A ND1 1 
ATOM   3105 C  CD2 . HIS   A 1 396 ? -34.795 0.871   43.622 1.00 72.32  ? 692 HIS   A CD2 1 
ATOM   3106 C  CE1 . HIS   A 1 396 ? -33.474 1.009   45.366 1.00 70.83  ? 692 HIS   A CE1 1 
ATOM   3107 N  NE2 . HIS   A 1 396 ? -34.015 1.707   44.383 1.00 69.96  ? 692 HIS   A NE2 1 
ATOM   3108 N  N   . GLN   A 1 397 ? -34.623 -4.323  41.519 1.00 64.41  ? 693 GLN   A N   1 
ATOM   3109 C  CA  . GLN   A 1 397 ? -35.254 -5.441  40.835 1.00 64.95  ? 693 GLN   A CA  1 
ATOM   3110 C  C   . GLN   A 1 397 ? -34.319 -6.636  40.882 1.00 61.35  ? 693 GLN   A C   1 
ATOM   3111 O  O   . GLN   A 1 397 ? -33.251 -6.620  40.260 1.00 58.08  ? 693 GLN   A O   1 
ATOM   3112 C  CB  . GLN   A 1 397 ? -35.578 -5.071  39.390 1.00 65.85  ? 693 GLN   A CB  1 
ATOM   3113 C  CG  . GLN   A 1 397 ? -36.234 -6.188  38.623 1.00 64.89  ? 693 GLN   A CG  1 
ATOM   3114 C  CD  . GLN   A 1 397 ? -37.655 -6.439  39.066 1.00 68.43  ? 693 GLN   A CD  1 
ATOM   3115 O  OE1 . GLN   A 1 397 ? -38.503 -5.547  39.015 1.00 69.90  ? 693 GLN   A OE1 1 
ATOM   3116 N  NE2 . GLN   A 1 397 ? -37.928 -7.664  39.502 1.00 69.77  ? 693 GLN   A NE2 1 
ATOM   3117 N  N   . GLU   A 1 398 ? -34.709 -7.660  41.635 1.00 61.36  ? 694 GLU   A N   1 
ATOM   3118 C  CA  . GLU   A 1 398 ? -34.032 -8.940  41.533 1.00 63.04  ? 694 GLU   A CA  1 
ATOM   3119 C  C   . GLU   A 1 398 ? -34.143 -9.460  40.105 1.00 62.63  ? 694 GLU   A C   1 
ATOM   3120 O  O   . GLU   A 1 398 ? -35.187 -9.332  39.462 1.00 63.04  ? 694 GLU   A O   1 
ATOM   3121 C  CB  . GLU   A 1 398 ? -34.634 -9.939  42.510 1.00 62.86  ? 694 GLU   A CB  1 
ATOM   3122 C  CG  . GLU   A 1 398 ? -34.427 -9.553  43.980 1.00 66.20  ? 694 GLU   A CG  1 
ATOM   3123 C  CD  . GLU   A 1 398 ? -35.212 -10.429 44.901 1.00 68.17  ? 694 GLU   A CD  1 
ATOM   3124 O  OE1 . GLU   A 1 398 ? -35.986 -11.263 44.394 1.00 70.45  ? 694 GLU   A OE1 1 
ATOM   3125 O  OE2 . GLU   A 1 398 ? -35.051 -10.294 46.141 1.00 71.07  ? 694 GLU   A OE2 1 
ATOM   3126 N  N   . MET   A 1 399 ? -33.054 -10.036 39.612 1.00 60.41  ? 695 MET   A N   1 
ATOM   3127 C  CA  . MET   A 1 399 ? -32.960 -10.532 38.248 1.00 61.52  ? 695 MET   A CA  1 
ATOM   3128 C  C   . MET   A 1 399 ? -32.302 -11.899 38.259 1.00 62.88  ? 695 MET   A C   1 
ATOM   3129 O  O   . MET   A 1 399 ? -31.275 -12.093 38.914 1.00 64.75  ? 695 MET   A O   1 
ATOM   3130 C  CB  . MET   A 1 399 ? -32.134 -9.590  37.345 1.00 55.98  ? 695 MET   A CB  1 
ATOM   3131 C  CG  . MET   A 1 399 ? -32.771 -8.253  37.053 1.00 55.31  ? 695 MET   A CG  1 
ATOM   3132 S  SD  . MET   A 1 399 ? -31.560 -7.090  36.430 1.00 54.38  ? 695 MET   A SD  1 
ATOM   3133 C  CE  . MET   A 1 399 ? -32.368 -5.534  36.784 1.00 53.07  ? 695 MET   A CE  1 
ATOM   3134 N  N   . LEU   A 1 400 ? -32.889 -12.842 37.530 1.00 60.79  ? 696 LEU   A N   1 
ATOM   3135 C  CA  . LEU   A 1 400 ? -32.275 -14.145 37.331 1.00 61.75  ? 696 LEU   A CA  1 
ATOM   3136 C  C   . LEU   A 1 400 ? -31.478 -14.109 36.036 1.00 61.19  ? 696 LEU   A C   1 
ATOM   3137 O  O   . LEU   A 1 400 ? -32.014 -13.742 34.983 1.00 59.76  ? 696 LEU   A O   1 
ATOM   3138 C  CB  . LEU   A 1 400 ? -33.328 -15.249 37.267 1.00 64.15  ? 696 LEU   A CB  1 
ATOM   3139 C  CG  . LEU   A 1 400 ? -34.083 -15.547 38.561 1.00 68.94  ? 696 LEU   A CG  1 
ATOM   3140 C  CD1 . LEU   A 1 400 ? -35.147 -16.608 38.324 1.00 73.99  ? 696 LEU   A CD1 1 
ATOM   3141 C  CD2 . LEU   A 1 400 ? -33.123 -15.966 39.655 1.00 68.69  ? 696 LEU   A CD2 1 
ATOM   3142 N  N   . ASN   A 1 401 ? -30.198 -14.456 36.121 1.00 59.26  ? 697 ASN   A N   1 
ATOM   3143 C  CA  . ASN   A 1 401 ? -29.343 -14.563 34.949 1.00 59.25  ? 697 ASN   A CA  1 
ATOM   3144 C  C   . ASN   A 1 401 ? -29.246 -16.021 34.533 1.00 62.11  ? 697 ASN   A C   1 
ATOM   3145 O  O   . ASN   A 1 401 ? -28.984 -16.893 35.367 1.00 63.12  ? 697 ASN   A O   1 
ATOM   3146 C  CB  . ASN   A 1 401 ? -27.945 -13.999 35.205 1.00 57.39  ? 697 ASN   A CB  1 
ATOM   3147 C  CG  . ASN   A 1 401 ? -27.206 -13.713 33.917 1.00 57.19  ? 697 ASN   A CG  1 
ATOM   3148 O  OD1 . ASN   A 1 401 ? -27.826 -13.623 32.862 1.00 58.28  ? 697 ASN   A OD1 1 
ATOM   3149 N  ND2 . ASN   A 1 401 ? -25.886 -13.585 33.986 1.00 55.48  ? 697 ASN   A ND2 1 
ATOM   3150 N  N   . TYR   A 1 402 ? -29.480 -16.278 33.246 1.00 63.43  ? 698 TYR   A N   1 
ATOM   3151 C  CA  . TYR   A 1 402 ? -29.308 -17.602 32.675 1.00 63.61  ? 698 TYR   A CA  1 
ATOM   3152 C  C   . TYR   A 1 402 ? -29.162 -17.446 31.160 1.00 65.27  ? 698 TYR   A C   1 
ATOM   3153 O  O   . TYR   A 1 402 ? -29.509 -16.411 30.580 1.00 61.71  ? 698 TYR   A O   1 
ATOM   3154 C  CB  . TYR   A 1 402 ? -30.467 -18.534 33.059 1.00 65.11  ? 698 TYR   A CB  1 
ATOM   3155 C  CG  . TYR   A 1 402 ? -31.845 -17.924 32.889 1.00 66.41  ? 698 TYR   A CG  1 
ATOM   3156 C  CD1 . TYR   A 1 402 ? -32.515 -18.017 31.673 1.00 65.38  ? 698 TYR   A CD1 1 
ATOM   3157 C  CD2 . TYR   A 1 402 ? -32.483 -17.258 33.944 1.00 63.46  ? 698 TYR   A CD2 1 
ATOM   3158 C  CE1 . TYR   A 1 402 ? -33.769 -17.471 31.499 1.00 65.41  ? 698 TYR   A CE1 1 
ATOM   3159 C  CE2 . TYR   A 1 402 ? -33.749 -16.701 33.778 1.00 66.09  ? 698 TYR   A CE2 1 
ATOM   3160 C  CZ  . TYR   A 1 402 ? -34.385 -16.818 32.540 1.00 67.95  ? 698 TYR   A CZ  1 
ATOM   3161 O  OH  . TYR   A 1 402 ? -35.639 -16.285 32.328 1.00 68.66  ? 698 TYR   A OH  1 
ATOM   3162 N  N   . ARG   A 1 403 ? -28.611 -18.477 30.531 1.00 64.99  ? 699 ARG   A N   1 
ATOM   3163 C  CA  . ARG   A 1 403 ? -28.137 -18.393 29.156 1.00 66.71  ? 699 ARG   A CA  1 
ATOM   3164 C  C   . ARG   A 1 403 ? -29.132 -19.105 28.256 1.00 68.90  ? 699 ARG   A C   1 
ATOM   3165 O  O   . ARG   A 1 403 ? -29.194 -20.338 28.239 1.00 73.76  ? 699 ARG   A O   1 
ATOM   3166 C  CB  . ARG   A 1 403 ? -26.746 -19.007 29.034 1.00 74.53  ? 699 ARG   A CB  1 
ATOM   3167 C  CG  . ARG   A 1 403 ? -25.715 -18.366 29.939 1.00 77.45  ? 699 ARG   A CG  1 
ATOM   3168 C  CD  . ARG   A 1 403 ? -24.892 -17.341 29.182 1.00 82.59  ? 699 ARG   A CD  1 
ATOM   3169 N  NE  . ARG   A 1 403 ? -23.587 -17.879 28.817 1.00 86.60  ? 699 ARG   A NE  1 
ATOM   3170 C  CZ  . ARG   A 1 403 ? -22.747 -17.305 27.966 1.00 85.30  ? 699 ARG   A CZ  1 
ATOM   3171 N  NH1 . ARG   A 1 403 ? -23.065 -16.191 27.325 1.00 82.16  ? 699 ARG   A NH1 1 
ATOM   3172 N  NH2 . ARG   A 1 403 ? -21.557 -17.863 27.755 1.00 87.64  ? 699 ARG   A NH2 1 
ATOM   3173 N  N   . LEU   A 1 404 ? -29.921 -18.332 27.531 1.00 64.66  ? 700 LEU   A N   1 
ATOM   3174 C  CA  . LEU   A 1 404 ? -30.764 -18.881 26.487 1.00 64.11  ? 700 LEU   A CA  1 
ATOM   3175 C  C   . LEU   A 1 404 ? -30.067 -18.743 25.141 1.00 62.45  ? 700 LEU   A C   1 
ATOM   3176 O  O   . LEU   A 1 404 ? -29.173 -17.914 24.955 1.00 62.05  ? 700 LEU   A O   1 
ATOM   3177 C  CB  . LEU   A 1 404 ? -32.120 -18.178 26.443 1.00 61.80  ? 700 LEU   A CB  1 
ATOM   3178 C  CG  . LEU   A 1 404 ? -32.923 -18.219 27.740 1.00 64.43  ? 700 LEU   A CG  1 
ATOM   3179 C  CD1 . LEU   A 1 404 ? -34.151 -17.352 27.602 1.00 61.74  ? 700 LEU   A CD1 1 
ATOM   3180 C  CD2 . LEU   A 1 404 ? -33.301 -19.646 28.066 1.00 69.70  ? 700 LEU   A CD2 1 
ATOM   3181 N  N   . THR   A 1 405 ? -30.477 -19.590 24.209 1.00 62.76  ? 701 THR   A N   1 
ATOM   3182 C  CA  . THR   A 1 405 ? -30.007 -19.497 22.842 1.00 59.72  ? 701 THR   A CA  1 
ATOM   3183 C  C   . THR   A 1 405 ? -31.217 -19.344 21.923 1.00 60.20  ? 701 THR   A C   1 
ATOM   3184 O  O   . THR   A 1 405 ? -32.315 -19.779 22.289 1.00 62.37  ? 701 THR   A O   1 
ATOM   3185 C  CB  . THR   A 1 405 ? -29.187 -20.745 22.485 1.00 62.74  ? 701 THR   A CB  1 
ATOM   3186 O  OG1 . THR   A 1 405 ? -28.592 -20.585 21.199 1.00 66.73  ? 701 THR   A OG1 1 
ATOM   3187 C  CG2 . THR   A 1 405 ? -30.059 -21.995 22.510 1.00 67.03  ? 701 THR   A CG2 1 
ATOM   3188 N  N   . PRO   A 1 406 ? -31.082 -18.682 20.742 1.00 62.95  ? 702 PRO   A N   1 
ATOM   3189 C  CA  . PRO   A 1 406 ? -29.922 -17.980 20.155 1.00 60.13  ? 702 PRO   A CA  1 
ATOM   3190 C  C   . PRO   A 1 406 ? -29.291 -16.941 21.073 1.00 58.41  ? 702 PRO   A C   1 
ATOM   3191 O  O   . PRO   A 1 406 ? -29.961 -16.396 21.942 1.00 57.07  ? 702 PRO   A O   1 
ATOM   3192 C  CB  . PRO   A 1 406 ? -30.522 -17.297 18.914 1.00 58.67  ? 702 PRO   A CB  1 
ATOM   3193 C  CG  . PRO   A 1 406 ? -31.678 -18.143 18.532 1.00 60.04  ? 702 PRO   A CG  1 
ATOM   3194 C  CD  . PRO   A 1 406 ? -32.238 -18.671 19.822 1.00 62.68  ? 702 PRO   A CD  1 
ATOM   3195 N  N   . SER   A 1 407 ? -28.005 -16.646 20.896 1.00 58.74  ? 703 SER   A N   1 
ATOM   3196 C  CA  . SER   A 1 407 ? -27.296 -15.797 21.834 1.00 57.64  ? 703 SER   A CA  1 
ATOM   3197 C  C   . SER   A 1 407 ? -26.123 -15.119 21.147 1.00 56.75  ? 703 SER   A C   1 
ATOM   3198 O  O   . SER   A 1 407 ? -25.573 -15.615 20.155 1.00 58.29  ? 703 SER   A O   1 
ATOM   3199 C  CB  . SER   A 1 407 ? -26.784 -16.605 23.026 1.00 59.53  ? 703 SER   A CB  1 
ATOM   3200 O  OG  . SER   A 1 407 ? -25.730 -17.444 22.599 1.00 61.84  ? 703 SER   A OG  1 
ATOM   3201 N  N   . PHE   A 1 408 ? -25.749 -13.966 21.685 1.00 56.61  ? 704 PHE   A N   1 
ATOM   3202 C  CA  . PHE   A 1 408 ? -24.479 -13.351 21.343 1.00 55.03  ? 704 PHE   A CA  1 
ATOM   3203 C  C   . PHE   A 1 408 ? -23.452 -13.812 22.360 1.00 59.61  ? 704 PHE   A C   1 
ATOM   3204 O  O   . PHE   A 1 408 ? -23.683 -13.717 23.565 1.00 59.74  ? 704 PHE   A O   1 
ATOM   3205 C  CB  . PHE   A 1 408 ? -24.576 -11.829 21.325 1.00 53.38  ? 704 PHE   A CB  1 
ATOM   3206 C  CG  . PHE   A 1 408 ? -25.420 -11.295 20.207 1.00 54.88  ? 704 PHE   A CG  1 
ATOM   3207 C  CD1 . PHE   A 1 408 ? -24.919 -11.225 18.911 1.00 55.53  ? 704 PHE   A CD1 1 
ATOM   3208 C  CD2 . PHE   A 1 408 ? -26.720 -10.881 20.443 1.00 53.97  ? 704 PHE   A CD2 1 
ATOM   3209 C  CE1 . PHE   A 1 408 ? -25.706 -10.745 17.871 1.00 53.71  ? 704 PHE   A CE1 1 
ATOM   3210 C  CE2 . PHE   A 1 408 ? -27.505 -10.392 19.412 1.00 53.98  ? 704 PHE   A CE2 1 
ATOM   3211 C  CZ  . PHE   A 1 408 ? -26.993 -10.328 18.123 1.00 55.81  ? 704 PHE   A CZ  1 
ATOM   3212 N  N   . GLU   A 1 409 ? -22.336 -14.326 21.876 1.00 58.24  ? 705 GLU   A N   1 
ATOM   3213 C  CA  . GLU   A 1 409 ? -21.301 -14.882 22.723 1.00 59.38  ? 705 GLU   A CA  1 
ATOM   3214 C  C   . GLU   A 1 409 ? -20.020 -14.091 22.525 1.00 60.58  ? 705 GLU   A C   1 
ATOM   3215 O  O   . GLU   A 1 409 ? -19.802 -13.482 21.468 1.00 57.13  ? 705 GLU   A O   1 
ATOM   3216 C  CB  . GLU   A 1 409 ? -21.051 -16.364 22.398 1.00 61.67  ? 705 GLU   A CB  1 
ATOM   3217 C  CG  . GLU   A 1 409 ? -22.258 -17.267 22.618 1.00 64.14  ? 705 GLU   A CG  1 
ATOM   3218 C  CD  . GLU   A 1 409 ? -22.666 -17.335 24.091 1.00 69.26  ? 705 GLU   A CD  1 
ATOM   3219 O  OE1 . GLU   A 1 409 ? -21.786 -17.166 24.963 1.00 72.03  ? 705 GLU   A OE1 1 
ATOM   3220 O  OE2 . GLU   A 1 409 ? -23.866 -17.555 24.373 1.00 68.77  ? 705 GLU   A OE2 1 
ATOM   3221 N  N   . TYR   A 1 410 ? -19.184 -14.094 23.558 1.00 58.49  ? 706 TYR   A N   1 
ATOM   3222 C  CA  . TYR   A 1 410 ? -17.847 -13.553 23.424 1.00 59.08  ? 706 TYR   A CA  1 
ATOM   3223 C  C   . TYR   A 1 410 ? -16.987 -14.490 22.594 1.00 59.90  ? 706 TYR   A C   1 
ATOM   3224 O  O   . TYR   A 1 410 ? -17.239 -15.694 22.494 1.00 61.19  ? 706 TYR   A O   1 
ATOM   3225 C  CB  . TYR   A 1 410 ? -17.193 -13.367 24.788 1.00 62.60  ? 706 TYR   A CB  1 
ATOM   3226 C  CG  . TYR   A 1 410 ? -17.592 -12.141 25.565 1.00 66.27  ? 706 TYR   A CG  1 
ATOM   3227 C  CD1 . TYR   A 1 410 ? -17.058 -10.896 25.260 1.00 69.29  ? 706 TYR   A CD1 1 
ATOM   3228 C  CD2 . TYR   A 1 410 ? -18.442 -12.242 26.664 1.00 71.01  ? 706 TYR   A CD2 1 
ATOM   3229 C  CE1 . TYR   A 1 410 ? -17.388 -9.775  26.012 1.00 71.84  ? 706 TYR   A CE1 1 
ATOM   3230 C  CE2 . TYR   A 1 410 ? -18.779 -11.131 27.416 1.00 70.90  ? 706 TYR   A CE2 1 
ATOM   3231 C  CZ  . TYR   A 1 410 ? -18.249 -9.901  27.085 1.00 69.61  ? 706 TYR   A CZ  1 
ATOM   3232 O  OH  . TYR   A 1 410 ? -18.585 -8.794  27.829 1.00 67.94  ? 706 TYR   A OH  1 
ATOM   3233 N  N   . GLN   A 1 411 ? -15.939 -13.930 22.014 1.00 64.59  ? 707 GLN   A N   1 
ATOM   3234 C  CA  . GLN   A 1 411 ? -15.035 -14.744 21.220 1.00 68.27  ? 707 GLN   A CA  1 
ATOM   3235 C  C   . GLN   A 1 411 ? -13.657 -14.116 21.301 1.00 70.21  ? 707 GLN   A C   1 
ATOM   3236 O  O   . GLN   A 1 411 ? -13.534 -12.912 21.529 1.00 70.81  ? 707 GLN   A O   1 
ATOM   3237 C  CB  . GLN   A 1 411 ? -15.508 -14.851 19.760 1.00 66.87  ? 707 GLN   A CB  1 
ATOM   3238 C  CG  . GLN   A 1 411 ? -15.309 -13.602 18.956 1.00 67.52  ? 707 GLN   A CG  1 
ATOM   3239 C  CD  . GLN   A 1 411 ? -15.928 -13.703 17.563 1.00 65.44  ? 707 GLN   A CD  1 
ATOM   3240 O  OE1 . GLN   A 1 411 ? -15.865 -14.749 16.916 1.00 65.44  ? 707 GLN   A OE1 1 
ATOM   3241 N  NE2 . GLN   A 1 411 ? -16.545 -12.619 17.113 1.00 60.99  ? 707 GLN   A NE2 1 
ATOM   3242 N  N   . PRO   A 1 412 ? -12.608 -14.912 21.126 1.00 71.55  ? 708 PRO   A N   1 
ATOM   3243 C  CA  . PRO   A 1 412 ? -11.247 -14.364 21.203 1.00 77.46  ? 708 PRO   A CA  1 
ATOM   3244 C  C   . PRO   A 1 412 ? -11.019 -13.255 20.189 1.00 79.61  ? 708 PRO   A C   1 
ATOM   3245 O  O   . PRO   A 1 412 ? -11.537 -13.283 19.069 1.00 78.96  ? 708 PRO   A O   1 
ATOM   3246 C  CB  . PRO   A 1 412 ? -10.359 -15.577 20.893 1.00 83.30  ? 708 PRO   A CB  1 
ATOM   3247 C  CG  . PRO   A 1 412 ? -11.199 -16.774 21.208 1.00 80.51  ? 708 PRO   A CG  1 
ATOM   3248 C  CD  . PRO   A 1 412 ? -12.623 -16.372 20.943 1.00 74.96  ? 708 PRO   A CD  1 
ATOM   3249 N  N   . ASP   A 1 413 ? -10.223 -12.274 20.598 1.00 83.56  ? 709 ASP   A N   1 
ATOM   3250 C  CA  . ASP   A 1 413 ? -9.753  -11.270 19.660 1.00 87.05  ? 709 ASP   A CA  1 
ATOM   3251 C  C   . ASP   A 1 413 ? -8.983  -11.955 18.539 1.00 89.43  ? 709 ASP   A C   1 
ATOM   3252 O  O   . ASP   A 1 413 ? -8.143  -12.825 18.811 1.00 92.81  ? 709 ASP   A O   1 
ATOM   3253 C  CB  . ASP   A 1 413 ? -8.869  -10.243 20.359 1.00 89.71  ? 709 ASP   A CB  1 
ATOM   3254 C  CG  . ASP   A 1 413 ? -9.665  -9.289  21.224 1.00 90.11  ? 709 ASP   A CG  1 
ATOM   3255 O  OD1 . ASP   A 1 413 ? -10.872 -9.100  20.942 1.00 87.02  ? 709 ASP   A OD1 1 
ATOM   3256 O  OD2 . ASP   A 1 413 ? -9.085  -8.729  22.182 1.00 91.67  ? 709 ASP   A OD2 1 
ATOM   3257 N  N   . PRO   A 1 414 ? -9.241  -11.605 17.278 1.00 87.66  ? 710 PRO   A N   1 
ATOM   3258 C  CA  . PRO   A 1 414 ? -8.676  -12.384 16.164 1.00 88.28  ? 710 PRO   A CA  1 
ATOM   3259 C  C   . PRO   A 1 414 ? -7.166  -12.315 16.050 1.00 93.55  ? 710 PRO   A C   1 
ATOM   3260 O  O   . PRO   A 1 414 ? -6.576  -13.203 15.421 1.00 97.09  ? 710 PRO   A O   1 
ATOM   3261 C  CB  . PRO   A 1 414 ? -9.349  -11.771 14.923 1.00 83.21  ? 710 PRO   A CB  1 
ATOM   3262 C  CG  . PRO   A 1 414 ? -9.849  -10.430 15.366 1.00 81.12  ? 710 PRO   A CG  1 
ATOM   3263 C  CD  . PRO   A 1 414 ? -10.196 -10.584 16.821 1.00 84.65  ? 710 PRO   A CD  1 
ATOM   3264 N  N   . TRP   A 1 415 ? -6.512  -11.300 16.613 1.00 94.15  ? 711 TRP   A N   1 
ATOM   3265 C  CA  . TRP   A 1 415 ? -5.064  -11.231 16.450 1.00 97.39  ? 711 TRP   A CA  1 
ATOM   3266 C  C   . TRP   A 1 415 ? -4.330  -12.232 17.331 1.00 100.00 ? 711 TRP   A C   1 
ATOM   3267 O  O   . TRP   A 1 415 ? -3.105  -12.346 17.222 1.00 102.51 ? 711 TRP   A O   1 
ATOM   3268 C  CB  . TRP   A 1 415 ? -4.559  -9.810  16.721 1.00 95.44  ? 711 TRP   A CB  1 
ATOM   3269 C  CG  . TRP   A 1 415 ? -5.096  -9.180  17.966 1.00 94.65  ? 711 TRP   A CG  1 
ATOM   3270 C  CD1 . TRP   A 1 415 ? -4.564  -9.266  19.219 1.00 96.91  ? 711 TRP   A CD1 1 
ATOM   3271 C  CD2 . TRP   A 1 415 ? -6.263  -8.349  18.081 1.00 92.71  ? 711 TRP   A CD2 1 
ATOM   3272 N  NE1 . TRP   A 1 415 ? -5.328  -8.549  20.106 1.00 96.16  ? 711 TRP   A NE1 1 
ATOM   3273 C  CE2 . TRP   A 1 415 ? -6.376  -7.977  19.434 1.00 92.76  ? 711 TRP   A CE2 1 
ATOM   3274 C  CE3 . TRP   A 1 415 ? -7.222  -7.886  17.173 1.00 89.31  ? 711 TRP   A CE3 1 
ATOM   3275 C  CZ2 . TRP   A 1 415 ? -7.408  -7.164  19.902 1.00 92.16  ? 711 TRP   A CZ2 1 
ATOM   3276 C  CZ3 . TRP   A 1 415 ? -8.248  -7.082  17.639 1.00 86.69  ? 711 TRP   A CZ3 1 
ATOM   3277 C  CH2 . TRP   A 1 415 ? -8.333  -6.732  18.992 1.00 92.35  ? 711 TRP   A CH2 1 
ATOM   3278 N  N   . ASN   A 1 416 ? -5.048  -12.967 18.180 1.00 98.94  ? 712 ASN   A N   1 
ATOM   3279 C  CA  . ASN   A 1 416 ? -4.467  -14.030 18.989 1.00 104.59 ? 712 ASN   A CA  1 
ATOM   3280 C  C   . ASN   A 1 416 ? -4.663  -15.412 18.386 1.00 107.22 ? 712 ASN   A C   1 
ATOM   3281 O  O   . ASN   A 1 416 ? -3.843  -16.304 18.629 1.00 110.71 ? 712 ASN   A O   1 
ATOM   3282 C  CB  . ASN   A 1 416 ? -5.074  -14.016 20.395 1.00 104.23 ? 712 ASN   A CB  1 
ATOM   3283 C  CG  . ASN   A 1 416 ? -4.999  -12.651 21.043 1.00 103.69 ? 712 ASN   A CG  1 
ATOM   3284 O  OD1 . ASN   A 1 416 ? -4.101  -11.863 20.742 1.00 104.87 ? 712 ASN   A OD1 1 
ATOM   3285 N  ND2 . ASN   A 1 416 ? -5.941  -12.361 21.938 1.00 100.58 ? 712 ASN   A ND2 1 
ATOM   3286 N  N   . THR   A 1 417 ? -5.731  -15.609 17.613 1.00 105.30 ? 713 THR   A N   1 
ATOM   3287 C  CA  . THR   A 1 417 ? -6.059  -16.907 17.037 1.00 108.12 ? 713 THR   A CA  1 
ATOM   3288 C  C   . THR   A 1 417 ? -5.662  -17.042 15.576 1.00 109.52 ? 713 THR   A C   1 
ATOM   3289 O  O   . THR   A 1 417 ? -5.422  -18.163 15.112 1.00 112.57 ? 713 THR   A O   1 
ATOM   3290 C  CB  . THR   A 1 417 ? -7.564  -17.169 17.163 1.00 108.24 ? 713 THR   A CB  1 
ATOM   3291 O  OG1 . THR   A 1 417 ? -8.263  -15.917 17.200 1.00 102.41 ? 713 THR   A OG1 1 
ATOM   3292 C  CG2 . THR   A 1 417 ? -7.868  -17.953 18.433 1.00 109.02 ? 713 THR   A CG2 1 
ATOM   3293 N  N   . HIS   A 1 418 ? -5.585  -15.933 14.847 1.00 108.80 ? 714 HIS   A N   1 
ATOM   3294 C  CA  . HIS   A 1 418 ? -5.358  -15.994 13.412 1.00 109.77 ? 714 HIS   A CA  1 
ATOM   3295 C  C   . HIS   A 1 418 ? -4.021  -16.655 13.100 1.00 112.43 ? 714 HIS   A C   1 
ATOM   3296 O  O   . HIS   A 1 418 ? -3.067  -16.587 13.879 1.00 114.46 ? 714 HIS   A O   1 
ATOM   3297 C  CB  . HIS   A 1 418 ? -5.401  -14.590 12.809 1.00 108.17 ? 714 HIS   A CB  1 
ATOM   3298 C  CG  . HIS   A 1 418 ? -5.435  -14.575 11.312 1.00 108.03 ? 714 HIS   A CG  1 
ATOM   3299 N  ND1 . HIS   A 1 418 ? -6.209  -15.447 10.577 1.00 107.11 ? 714 HIS   A ND1 1 
ATOM   3300 C  CD2 . HIS   A 1 418 ? -4.796  -13.789 10.412 1.00 110.30 ? 714 HIS   A CD2 1 
ATOM   3301 C  CE1 . HIS   A 1 418 ? -6.043  -15.201 9.288  1.00 103.69 ? 714 HIS   A CE1 1 
ATOM   3302 N  NE2 . HIS   A 1 418 ? -5.192  -14.199 9.160  1.00 105.09 ? 714 HIS   A NE2 1 
ATOM   3303 N  N   . VAL   A 1 419 ? -3.970  -17.322 11.954 1.00 113.13 ? 715 VAL   A N   1 
ATOM   3304 C  CA  . VAL   A 1 419 ? -2.740  -17.881 11.410 1.00 114.84 ? 715 VAL   A CA  1 
ATOM   3305 C  C   . VAL   A 1 419 ? -2.425  -17.075 10.156 1.00 117.13 ? 715 VAL   A C   1 
ATOM   3306 O  O   . VAL   A 1 419 ? -3.086  -17.234 9.123  1.00 116.38 ? 715 VAL   A O   1 
ATOM   3307 C  CB  . VAL   A 1 419 ? -2.876  -19.381 11.116 1.00 115.81 ? 715 VAL   A CB  1 
ATOM   3308 C  CG1 . VAL   A 1 419 ? -1.644  -19.895 10.414 1.00 118.52 ? 715 VAL   A CG1 1 
ATOM   3309 C  CG2 . VAL   A 1 419 ? -3.111  -20.157 12.413 1.00 116.00 ? 715 VAL   A CG2 1 
ATOM   3310 N  N   . TRP   A 1 420 ? -1.425  -16.201 10.252 1.00 117.22 ? 716 TRP   A N   1 
ATOM   3311 C  CA  . TRP   A 1 420 ? -1.228  -15.111 9.293  1.00 120.49 ? 716 TRP   A CA  1 
ATOM   3312 C  C   . TRP   A 1 420 ? -0.724  -15.536 7.905  1.00 125.30 ? 716 TRP   A C   1 
ATOM   3313 O  O   . TRP   A 1 420 ? -0.664  -16.718 7.565  1.00 128.64 ? 716 TRP   A O   1 
ATOM   3314 C  CB  . TRP   A 1 420 ? -0.274  -14.075 9.899  1.00 120.41 ? 716 TRP   A CB  1 
ATOM   3315 C  CG  . TRP   A 1 420 ? -0.981  -13.070 10.765 1.00 120.04 ? 716 TRP   A CG  1 
ATOM   3316 C  CD1 . TRP   A 1 420 ? -1.346  -13.221 12.080 1.00 118.69 ? 716 TRP   A CD1 1 
ATOM   3317 C  CD2 . TRP   A 1 420 ? -1.423  -11.765 10.375 1.00 118.90 ? 716 TRP   A CD2 1 
ATOM   3318 N  NE1 . TRP   A 1 420 ? -1.983  -12.086 12.526 1.00 115.88 ? 716 TRP   A NE1 1 
ATOM   3319 C  CE2 . TRP   A 1 420 ? -2.042  -11.178 11.499 1.00 116.56 ? 716 TRP   A CE2 1 
ATOM   3320 C  CE3 . TRP   A 1 420 ? -1.353  -11.032 9.186  1.00 118.64 ? 716 TRP   A CE3 1 
ATOM   3321 C  CZ2 . TRP   A 1 420 ? -2.585  -9.893  11.464 1.00 112.67 ? 716 TRP   A CZ2 1 
ATOM   3322 C  CZ3 . TRP   A 1 420 ? -1.894  -9.760  9.156  1.00 116.65 ? 716 TRP   A CZ3 1 
ATOM   3323 C  CH2 . TRP   A 1 420 ? -2.504  -9.205  10.285 1.00 113.92 ? 716 TRP   A CH2 1 
HETATM 3324 C  CHA . HEM   B 2 .   ? -25.007 -4.383  26.073 1.00 57.03  ? 801 HEM   A CHA 1 
HETATM 3325 C  CHB . HEM   B 2 .   ? -28.051 -0.620  25.656 1.00 59.20  ? 801 HEM   A CHB 1 
HETATM 3326 C  CHC . HEM   B 2 .   ? -29.299 -2.358  21.278 1.00 57.32  ? 801 HEM   A CHC 1 
HETATM 3327 C  CHD . HEM   B 2 .   ? -27.057 -6.480  22.205 1.00 55.02  ? 801 HEM   A CHD 1 
HETATM 3328 C  C1A . HEM   B 2 .   ? -25.608 -3.158  26.275 1.00 55.91  ? 801 HEM   A C1A 1 
HETATM 3329 C  C2A . HEM   B 2 .   ? -25.228 -2.146  27.245 1.00 59.61  ? 801 HEM   A C2A 1 
HETATM 3330 C  C3A . HEM   B 2 .   ? -26.052 -1.096  27.130 1.00 60.71  ? 801 HEM   A C3A 1 
HETATM 3331 C  C4A . HEM   B 2 .   ? -27.015 -1.407  26.095 1.00 57.37  ? 801 HEM   A C4A 1 
HETATM 3332 C  CMA . HEM   B 2 .   ? -25.995 0.199   27.968 1.00 57.23  ? 801 HEM   A CMA 1 
HETATM 3333 C  CAA . HEM   B 2 .   ? -24.029 -2.251  28.188 1.00 57.53  ? 801 HEM   A CAA 1 
HETATM 3334 C  CBA . HEM   B 2 .   ? -22.869 -1.850  27.279 1.00 59.34  ? 801 HEM   A CBA 1 
HETATM 3335 C  CGA . HEM   B 2 .   ? -21.621 -1.656  28.087 1.00 63.58  ? 801 HEM   A CGA 1 
HETATM 3336 O  O1A . HEM   B 2 .   ? -21.731 -1.361  29.306 1.00 59.19  ? 801 HEM   A O1A 1 
HETATM 3337 O  O2A . HEM   B 2 .   ? -20.516 -1.801  27.511 1.00 63.74  ? 801 HEM   A O2A 1 
HETATM 3338 C  C1B . HEM   B 2 .   ? -28.638 -0.744  24.407 1.00 57.59  ? 801 HEM   A C1B 1 
HETATM 3339 C  C2B . HEM   B 2 .   ? -29.551 0.201   23.797 1.00 59.21  ? 801 HEM   A C2B 1 
HETATM 3340 C  C3B . HEM   B 2 .   ? -29.906 -0.293  22.605 1.00 60.81  ? 801 HEM   A C3B 1 
HETATM 3341 C  C4B . HEM   B 2 .   ? -29.217 -1.560  22.401 1.00 59.48  ? 801 HEM   A C4B 1 
HETATM 3342 C  CMB . HEM   B 2 .   ? -30.049 1.526   24.419 1.00 61.61  ? 801 HEM   A CMB 1 
HETATM 3343 C  CAB . HEM   B 2 .   ? -30.869 0.420   21.631 1.00 65.00  ? 801 HEM   A CAB 1 
HETATM 3344 C  CBB . HEM   B 2 .   ? -31.541 -0.247  20.687 1.00 65.66  ? 801 HEM   A CBB 1 
HETATM 3345 C  C1C . HEM   B 2 .   ? -28.785 -3.609  21.087 1.00 57.98  ? 801 HEM   A C1C 1 
HETATM 3346 C  C2C . HEM   B 2 .   ? -28.874 -4.440  19.887 1.00 55.71  ? 801 HEM   A C2C 1 
HETATM 3347 C  C3C . HEM   B 2 .   ? -28.226 -5.594  20.143 1.00 53.78  ? 801 HEM   A C3C 1 
HETATM 3348 C  C4C . HEM   B 2 .   ? -27.743 -5.522  21.516 1.00 57.81  ? 801 HEM   A C4C 1 
HETATM 3349 C  CMC . HEM   B 2 .   ? -29.577 -3.971  18.596 1.00 56.38  ? 801 HEM   A CMC 1 
HETATM 3350 C  CAC . HEM   B 2 .   ? -28.011 -6.864  19.318 1.00 52.17  ? 801 HEM   A CAC 1 
HETATM 3351 C  CBC . HEM   B 2 .   ? -28.792 -7.178  18.277 1.00 57.23  ? 801 HEM   A CBC 1 
HETATM 3352 C  C1D . HEM   B 2 .   ? -26.304 -6.263  23.329 1.00 54.05  ? 801 HEM   A C1D 1 
HETATM 3353 C  C2D . HEM   B 2 .   ? -25.417 -7.231  23.906 1.00 54.33  ? 801 HEM   A C2D 1 
HETATM 3354 C  C3D . HEM   B 2 .   ? -24.839 -6.677  24.990 1.00 53.76  ? 801 HEM   A C3D 1 
HETATM 3355 C  C4D . HEM   B 2 .   ? -25.341 -5.319  25.106 1.00 53.94  ? 801 HEM   A C4D 1 
HETATM 3356 C  CMD . HEM   B 2 .   ? -25.224 -8.662  23.365 1.00 52.25  ? 801 HEM   A CMD 1 
HETATM 3357 C  CAD . HEM   B 2 .   ? -23.816 -7.382  25.930 1.00 54.64  ? 801 HEM   A CAD 1 
HETATM 3358 C  CBD . HEM   B 2 .   ? -22.385 -7.081  25.481 1.00 57.49  ? 801 HEM   A CBD 1 
HETATM 3359 C  CGD . HEM   B 2 .   ? -21.359 -7.724  26.388 1.00 58.84  ? 801 HEM   A CGD 1 
HETATM 3360 O  O1D . HEM   B 2 .   ? -21.714 -8.722  27.074 1.00 58.12  ? 801 HEM   A O1D 1 
HETATM 3361 O  O2D . HEM   B 2 .   ? -20.186 -7.255  26.397 1.00 53.80  ? 801 HEM   A O2D 1 
HETATM 3362 N  NA  . HEM   B 2 .   ? -26.708 -2.662  25.613 1.00 56.04  ? 801 HEM   A NA  1 
HETATM 3363 N  NB  . HEM   B 2 .   ? -28.454 -1.806  23.536 1.00 55.92  ? 801 HEM   A NB  1 
HETATM 3364 N  NC  . HEM   B 2 .   ? -28.102 -4.312  22.019 1.00 56.56  ? 801 HEM   A NC  1 
HETATM 3365 N  ND  . HEM   B 2 .   ? -26.240 -5.093  24.084 1.00 54.85  ? 801 HEM   A ND  1 
HETATM 3366 FE FE  . HEM   B 2 .   ? -27.669 -3.684  24.043 1.00 58.65  ? 801 HEM   A FE  1 
HETATM 3367 N  N1  . H4B   C 3 .   ? -21.762 -3.187  33.472 1.00 57.98  ? 802 H4B   A N1  1 
HETATM 3368 C  C2  . H4B   C 3 .   ? -21.812 -2.684  32.220 1.00 56.00  ? 802 H4B   A C2  1 
HETATM 3369 N  N2  . H4B   C 3 .   ? -23.004 -2.286  31.711 1.00 55.23  ? 802 H4B   A N2  1 
HETATM 3370 N  N3  . H4B   C 3 .   ? -20.685 -2.576  31.491 1.00 58.37  ? 802 H4B   A N3  1 
HETATM 3371 C  C4  . H4B   C 3 .   ? -19.489 -2.961  31.967 1.00 58.89  ? 802 H4B   A C4  1 
HETATM 3372 O  O4  . H4B   C 3 .   ? -18.457 -2.860  31.268 1.00 56.37  ? 802 H4B   A O4  1 
HETATM 3373 C  C4A . H4B   C 3 .   ? -19.417 -3.494  33.240 1.00 58.01  ? 802 H4B   A C4A 1 
HETATM 3374 C  C8A . H4B   C 3 .   ? -20.583 -3.585  33.995 1.00 58.06  ? 802 H4B   A C8A 1 
HETATM 3375 N  N5  . H4B   C 3 .   ? -18.242 -3.901  33.770 1.00 59.79  ? 802 H4B   A N5  1 
HETATM 3376 N  N8  . H4B   C 3 .   ? -20.560 -4.086  35.255 1.00 55.35  ? 802 H4B   A N8  1 
HETATM 3377 C  C6  . H4B   C 3 .   ? -18.332 -4.864  34.885 1.00 58.81  ? 802 H4B   A C6  1 
HETATM 3378 C  C7  . H4B   C 3 .   ? -19.324 -4.404  35.938 1.00 57.72  ? 802 H4B   A C7  1 
HETATM 3379 C  C9  . H4B   C 3 .   ? -16.996 -5.189  35.551 1.00 56.20  ? 802 H4B   A C9  1 
HETATM 3380 O  O9  . H4B   C 3 .   ? -16.392 -3.949  35.886 1.00 58.24  ? 802 H4B   A O9  1 
HETATM 3381 C  C10 . H4B   C 3 .   ? -17.230 -6.074  36.783 1.00 59.47  ? 802 H4B   A C10 1 
HETATM 3382 C  C11 . H4B   C 3 .   ? -15.976 -6.326  37.623 1.00 60.77  ? 802 H4B   A C11 1 
HETATM 3383 O  O10 . H4B   C 3 .   ? -17.762 -7.341  36.371 1.00 59.16  ? 802 H4B   A O10 1 
HETATM 3384 C  C11 . A1A0C D 4 .   ? -22.117 -1.483  23.528 1.00 61.25  ? 803 A1A0C A C11 1 
HETATM 3385 C  C12 . A1A0C D 4 .   ? -21.153 -0.505  23.394 1.00 63.59  ? 803 A1A0C A C12 1 
HETATM 3386 C  C17 . A1A0C D 4 .   ? -20.091 -4.283  25.109 1.00 60.81  ? 803 A1A0C A C17 1 
HETATM 3387 C  C16 . A1A0C D 4 .   ? -21.790 -2.715  24.084 1.00 62.92  ? 803 A1A0C A C16 1 
HETATM 3388 C  C15 . A1A0C D 4 .   ? -20.481 -2.948  24.507 1.00 63.27  ? 803 A1A0C A C15 1 
HETATM 3389 C  C14 . A1A0C D 4 .   ? -19.514 -1.958  24.361 1.00 64.41  ? 803 A1A0C A C14 1 
HETATM 3390 C  C13 . A1A0C D 4 .   ? -19.856 -0.730  23.811 1.00 66.08  ? 803 A1A0C A C13 1 
HETATM 3391 C  C18 . A1A0C D 4 .   ? -19.090 -4.921  24.145 1.00 62.74  ? 803 A1A0C A C18 1 
HETATM 3392 C  C20 . A1A0C D 4 .   ? -17.735 -6.830  23.615 1.00 65.92  ? 803 A1A0C A C20 1 
HETATM 3393 C  C02 . A1A0C D 4 .   ? -25.442 0.145   23.187 1.00 58.66  ? 803 A1A0C A C02 1 
HETATM 3394 C  C03 . A1A0C D 4 .   ? -26.011 -0.565  22.118 1.00 57.85  ? 803 A1A0C A C03 1 
HETATM 3395 C  C04 . A1A0C D 4 .   ? -25.286 -1.591  21.537 1.00 56.86  ? 803 A1A0C A C04 1 
HETATM 3396 C  C05 . A1A0C D 4 .   ? -24.020 -1.885  22.019 1.00 56.85  ? 803 A1A0C A C05 1 
HETATM 3397 C  C06 . A1A0C D 4 .   ? -23.484 -1.158  23.065 1.00 60.71  ? 803 A1A0C A C06 1 
HETATM 3398 C  C07 . A1A0C D 4 .   ? -25.839 -2.395  20.374 1.00 54.17  ? 803 A1A0C A C07 1 
HETATM 3399 F  F12 . A1A0C D 4 .   ? -21.472 0.683   22.860 1.00 63.60  ? 803 A1A0C A F12 1 
HETATM 3400 F  F13 . A1A0C D 4 .   ? -18.950 0.256   23.662 1.00 71.96  ? 803 A1A0C A F13 1 
HETATM 3401 N  N01 . A1A0C D 4 .   ? -24.197 -0.152  23.622 1.00 57.96  ? 803 A1A0C A N01 1 
HETATM 3402 N  N02 . A1A0C D 4 .   ? -26.136 1.140   23.772 1.00 59.06  ? 803 A1A0C A N02 1 
HETATM 3403 N  N19 . A1A0C D 4 .   ? -18.839 -6.344  24.457 1.00 63.85  ? 803 A1A0C A N19 1 
HETATM 3404 C  C   . ACT   E 5 .   ? -34.451 2.084   25.134 1.00 98.90  ? 804 ACT   A C   1 
HETATM 3405 O  O   . ACT   E 5 .   ? -33.986 3.108   24.578 1.00 98.50  ? 804 ACT   A O   1 
HETATM 3406 O  OXT . ACT   E 5 .   ? -34.947 2.112   26.286 1.00 99.46  ? 804 ACT   A OXT 1 
HETATM 3407 C  CH3 . ACT   E 5 .   ? -34.444 0.786   24.381 1.00 99.32  ? 804 ACT   A CH3 1 
HETATM 3408 ZN ZN  . ZN    F 6 .   ? -24.158 -16.462 40.631 0.39 54.96  ? 805 ZN    A ZN  1 
HETATM 3409 O  O   . HOH   G 7 .   ? -18.653 -1.992  28.728 1.00 58.90  ? 901 HOH   A O   1 
HETATM 3410 O  O   . HOH   G 7 .   ? -29.442 -12.907 40.105 1.00 60.85  ? 902 HOH   A O   1 
HETATM 3411 O  O   . HOH   G 7 .   ? -28.407 0.873   15.300 1.00 58.68  ? 903 HOH   A O   1 
HETATM 3412 O  O   . HOH   G 7 .   ? -49.383 -12.793 25.594 1.00 112.57 ? 904 HOH   A O   1 
HETATM 3413 O  O   . HOH   G 7 .   ? -26.373 -34.929 13.923 1.00 111.23 ? 905 HOH   A O   1 
HETATM 3414 O  O   . HOH   G 7 .   ? -24.638 -10.762 37.513 1.00 55.98  ? 906 HOH   A O   1 
HETATM 3415 O  O   . HOH   G 7 .   ? -38.555 -22.484 8.058  1.00 82.09  ? 907 HOH   A O   1 
HETATM 3416 O  O   . HOH   G 7 .   ? -16.711 5.617   34.705 1.00 74.10  ? 908 HOH   A O   1 
HETATM 3417 O  O   . HOH   G 7 .   ? -17.136 -16.671 9.256  1.00 69.00  ? 909 HOH   A O   1 
HETATM 3418 O  O   . HOH   G 7 .   ? -36.951 -12.792 27.790 1.00 65.78  ? 910 HOH   A O   1 
HETATM 3419 O  O   . HOH   G 7 .   ? -34.689 -11.959 35.744 1.00 61.03  ? 911 HOH   A O   1 
HETATM 3420 O  O   . HOH   G 7 .   ? -27.798 -13.245 23.759 1.00 53.64  ? 912 HOH   A O   1 
HETATM 3421 O  O   . HOH   G 7 .   ? -26.909 -2.924  29.647 1.00 55.23  ? 913 HOH   A O   1 
HETATM 3422 O  O   . HOH   G 7 .   ? -25.313 -4.301  5.918  1.00 54.05  ? 914 HOH   A O   1 
HETATM 3423 O  O   . HOH   G 7 .   ? -19.483 -8.453  34.293 1.00 57.19  ? 915 HOH   A O   1 
HETATM 3424 O  O   . HOH   G 7 .   ? -24.107 2.630   30.970 1.00 55.12  ? 916 HOH   A O   1 
HETATM 3425 O  O   . HOH   G 7 .   ? -26.637 7.026   20.283 1.00 67.04  ? 917 HOH   A O   1 
HETATM 3426 O  O   . HOH   G 7 .   ? -29.736 -15.653 28.045 1.00 56.99  ? 918 HOH   A O   1 
HETATM 3427 O  O   . HOH   G 7 .   ? -20.138 -14.624 10.617 1.00 58.55  ? 919 HOH   A O   1 
HETATM 3428 O  O   . HOH   G 7 .   ? -34.775 6.488   37.492 1.00 74.02  ? 920 HOH   A O   1 
HETATM 3429 O  O   . HOH   G 7 .   ? -28.620 -10.611 37.771 1.00 57.23  ? 921 HOH   A O   1 
HETATM 3430 O  O   . HOH   G 7 .   ? -18.822 -9.980  14.973 1.00 56.04  ? 922 HOH   A O   1 
HETATM 3431 O  O   . HOH   G 7 .   ? -22.660 7.026   11.985 1.00 59.88  ? 923 HOH   A O   1 
HETATM 3432 O  O   . HOH   G 7 .   ? -14.675 -20.987 9.424  1.00 82.23  ? 924 HOH   A O   1 
HETATM 3433 O  O   . HOH   G 7 .   ? -18.629 3.259   23.898 1.00 65.95  ? 925 HOH   A O   1 
HETATM 3434 O  O   . HOH   G 7 .   ? -21.275 0.604   32.684 1.00 53.95  ? 926 HOH   A O   1 
HETATM 3435 O  O   . HOH   G 7 .   ? -9.531  -17.743 10.745 1.00 92.17  ? 927 HOH   A O   1 
HETATM 3436 O  O   . HOH   G 7 .   ? -26.466 -12.271 1.433  1.00 62.78  ? 928 HOH   A O   1 
HETATM 3437 O  O   . HOH   G 7 .   ? -14.989 3.946   22.003 1.00 77.00  ? 929 HOH   A O   1 
HETATM 3438 O  O   . HOH   G 7 .   ? -23.995 -2.043  37.811 1.00 54.40  ? 930 HOH   A O   1 
HETATM 3439 O  O   . HOH   G 7 .   ? -21.469 -10.228 35.030 1.00 63.67  ? 931 HOH   A O   1 
HETATM 3440 O  O   . HOH   G 7 .   ? -21.890 1.331   30.104 1.00 57.68  ? 932 HOH   A O   1 
HETATM 3441 O  O   . HOH   G 7 .   ? -16.330 -2.646  21.859 1.00 70.18  ? 933 HOH   A O   1 
HETATM 3442 O  O   . HOH   G 7 .   ? -17.424 -18.083 20.920 1.00 68.84  ? 934 HOH   A O   1 
HETATM 3443 O  O   . HOH   G 7 .   ? -13.462 1.325   15.133 1.00 76.10  ? 935 HOH   A O   1 
HETATM 3444 O  O   . HOH   G 7 .   ? -15.311 1.348   29.449 1.00 67.45  ? 936 HOH   A O   1 
HETATM 3445 O  O   . HOH   G 7 .   ? -20.220 1.414   25.900 1.00 67.11  ? 937 HOH   A O   1 
HETATM 3446 O  O   . HOH   G 7 .   ? -23.880 -18.388 6.752  1.00 56.02  ? 938 HOH   A O   1 
HETATM 3447 O  O   . HOH   G 7 .   ? -28.454 -14.679 1.311  1.00 70.54  ? 939 HOH   A O   1 
HETATM 3448 O  O   . HOH   G 7 .   ? -14.427 -22.692 4.114  1.00 89.97  ? 940 HOH   A O   1 
HETATM 3449 O  O   . HOH   G 7 .   ? -34.528 9.604   27.288 1.00 76.35  ? 941 HOH   A O   1 
HETATM 3450 O  O   . HOH   G 7 .   ? -27.937 23.647  21.345 1.00 106.56 ? 942 HOH   A O   1 
HETATM 3451 O  O   . HOH   G 7 .   ? -28.437 1.789   3.717  1.00 62.75  ? 943 HOH   A O   1 
HETATM 3452 O  O   . HOH   G 7 .   ? -24.966 0.431   32.145 1.00 56.60  ? 944 HOH   A O   1 
HETATM 3453 O  O   . HOH   G 7 .   ? -35.537 -7.612  9.315  1.00 62.08  ? 945 HOH   A O   1 
HETATM 3454 O  O   . HOH   G 7 .   ? -44.150 -11.371 23.640 1.00 93.69  ? 946 HOH   A O   1 
HETATM 3455 O  O   . HOH   G 7 .   ? -38.537 -12.755 13.370 1.00 68.77  ? 947 HOH   A O   1 
HETATM 3456 O  O   . HOH   G 7 .   ? -18.256 1.291   28.518 1.00 67.91  ? 948 HOH   A O   1 
HETATM 3457 O  O   . HOH   G 7 .   ? -27.389 -16.818 1.752  1.00 69.85  ? 949 HOH   A O   1 
HETATM 3458 O  O   . HOH   G 7 .   ? -23.295 -1.219  40.099 1.00 76.68  ? 950 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   ? 1.4080 1.5299 1.1904 -0.5615 0.0367  0.0813  300 PHE A N   
2    C CA  . PHE A 4   ? 1.3360 1.6144 1.1995 -0.5450 0.0457  0.0724  300 PHE A CA  
3    C C   . PHE A 4   ? 1.2462 1.5765 1.1468 -0.5022 0.0566  0.0739  300 PHE A C   
4    O O   . PHE A 4   ? 1.2731 1.6800 1.1777 -0.5199 0.0717  0.0788  300 PHE A O   
5    C CB  . PHE A 4   ? 1.4036 1.7608 1.2568 -0.5853 0.0506  0.0704  300 PHE A CB  
6    C CG  . PHE A 4   ? 1.5615 1.8227 1.3342 -0.6358 0.0415  0.0739  300 PHE A CG  
7    C CD1 . PHE A 4   ? 1.5801 1.8091 1.3414 -0.6458 0.0295  0.0668  300 PHE A CD1 
8    C CD2 . PHE A 4   ? 1.6750 1.8743 1.3776 -0.6724 0.0449  0.0839  300 PHE A CD2 
9    C CE1 . PHE A 4   ? 1.6955 1.8308 1.3736 -0.6911 0.0214  0.0694  300 PHE A CE1 
10   C CE2 . PHE A 4   ? 1.8097 1.9140 1.4285 -0.7178 0.0358  0.0863  300 PHE A CE2 
11   C CZ  . PHE A 4   ? 1.8050 1.8763 1.4099 -0.7270 0.0243  0.0789  300 PHE A CZ  
12   N N   . LEU A 5   ? 1.1580 1.4427 1.0808 -0.4377 0.0470  0.0675  301 LEU A N   
13   C CA  . LEU A 5   ? 1.1011 1.3912 1.0384 -0.3884 0.0512  0.0672  301 LEU A CA  
14   C C   . LEU A 5   ? 1.0074 1.4190 1.0080 -0.3503 0.0591  0.0565  301 LEU A C   
15   O O   . LEU A 5   ? 0.9572 1.4283 0.9984 -0.3399 0.0557  0.0474  301 LEU A O   
16   C CB  . LEU A 5   ? 1.0929 1.2817 1.0204 -0.3420 0.0362  0.0653  301 LEU A CB  
17   C CG  . LEU A 5   ? 1.1425 1.2094 1.0088 -0.3642 0.0249  0.0727  301 LEU A CG  
18   C CD1 . LEU A 5   ? 1.1115 1.1329 0.9957 -0.3233 0.0102  0.0647  301 LEU A CD1 
19   C CD2 . LEU A 5   ? 1.1721 1.1591 0.9807 -0.3654 0.0249  0.0847  301 LEU A CD2 
20   N N   . LYS A 6   ? 0.9756 1.4168 0.9779 -0.3252 0.0689  0.0573  302 LYS A N   
21   C CA  . LYS A 6   ? 0.8956 1.4368 0.9421 -0.2811 0.0769  0.0471  302 LYS A CA  
22   C C   . LYS A 6   ? 0.8508 1.3348 0.9036 -0.2204 0.0672  0.0399  302 LYS A C   
23   O O   . LYS A 6   ? 0.8454 1.2418 0.8671 -0.2139 0.0610  0.0450  302 LYS A O   
24   C CB  . LYS A 6   ? 0.9017 1.5212 0.9397 -0.2930 0.0960  0.0513  302 LYS A CB  
25   C CG  . LYS A 6   ? 0.9765 1.6293 0.9894 -0.3670 0.1063  0.0629  302 LYS A CG  
26   C CD  . LYS A 6   ? 0.9463 1.7387 1.0007 -0.3890 0.1141  0.0578  302 LYS A CD  
27   C CE  . LYS A 6   ? 1.0014 1.7833 1.0165 -0.4570 0.1115  0.0648  302 LYS A CE  
28   N NZ  . LYS A 6   ? 1.0096 1.7910 0.9845 -0.4842 0.1234  0.0743  302 LYS A NZ  
29   N N   . VAL A 7   ? 0.8072 1.3400 0.8957 -0.1780 0.0649  0.0284  303 VAL A N   
30   C CA  . VAL A 7   ? 0.7642 1.2512 0.8526 -0.1242 0.0572  0.0209  303 VAL A CA  
31   C C   . VAL A 7   ? 0.7481 1.3124 0.8442 -0.0843 0.0686  0.0126  303 VAL A C   
32   O O   . VAL A 7   ? 0.7275 1.3896 0.8499 -0.0790 0.0761  0.0079  303 VAL A O   
33   C CB  . VAL A 7   ? 0.7493 1.1984 0.8571 -0.1060 0.0422  0.0150  303 VAL A CB  
34   C CG1 . VAL A 7   ? 0.7737 1.1538 0.8697 -0.1413 0.0325  0.0222  303 VAL A CG1 
35   C CG2 . VAL A 7   ? 0.7249 1.2592 0.8667 -0.0935 0.0442  0.0072  303 VAL A CG2 
36   N N   . LYS A 8   ? 0.7399 1.2626 0.8091 -0.0551 0.0696  0.0104  304 LYS A N   
37   C CA  . LYS A 8   ? 0.7271 1.3051 0.7882 -0.0123 0.0807  0.0019  304 LYS A CA  
38   C C   . LYS A 8   ? 0.7367 1.2607 0.7857 0.0398  0.0697  -0.0089 304 LYS A C   
39   O O   . LYS A 8   ? 0.7398 1.1742 0.7780 0.0379  0.0551  -0.0080 304 LYS A O   
40   C CB  . LYS A 8   ? 0.7373 1.3034 0.7638 -0.0184 0.0911  0.0066  304 LYS A CB  
41   C CG  . LYS A 8   ? 0.7664 1.3995 0.7795 0.0257  0.1058  -0.0024 304 LYS A CG  
42   C CD  . LYS A 8   ? 0.7695 1.4032 0.7496 0.0109  0.1185  0.0037  304 LYS A CD  
43   C CE  . LYS A 8   ? 0.8090 1.5010 0.7680 0.0615  0.1333  -0.0067 304 LYS A CE  
44   N NZ  . LYS A 8   ? 0.8496 1.5539 0.7776 0.0430  0.1478  0.0000  304 LYS A NZ  
45   N N   . ASN A 9   ? 0.7555 1.3357 0.8021 0.0862  0.0766  -0.0189 305 ASN A N   
46   C CA  . ASN A 9   ? 0.7994 1.3155 0.8117 0.1384  0.0686  -0.0293 305 ASN A CA  
47   C C   . ASN A 9   ? 0.8546 1.3665 0.8238 0.1651  0.0791  -0.0338 305 ASN A C   
48   O O   . ASN A 9   ? 0.8570 1.4629 0.8313 0.1777  0.0959  -0.0354 305 ASN A O   
49   C CB  . ASN A 9   ? 0.7830 1.3447 0.8065 0.1810  0.0669  -0.0380 305 ASN A CB  
50   C CG  . ASN A 9   ? 0.8438 1.3190 0.8155 0.2335  0.0576  -0.0480 305 ASN A CG  
51   O OD1 . ASN A 9   ? 0.8960 1.3358 0.8194 0.2628  0.0620  -0.0539 305 ASN A OD1 
52   N ND2 . ASN A 9   ? 0.7708 1.2046 0.7452 0.2430  0.0446  -0.0499 305 ASN A ND2 
53   N N   . TRP A 10  ? 0.8718 1.2808 0.7982 0.1705  0.0695  -0.0356 306 TRP A N   
54   C CA  . TRP A 10  ? 0.9254 1.3147 0.8038 0.1909  0.0774  -0.0400 306 TRP A CA  
55   C C   . TRP A 10  ? 0.9896 1.3481 0.8159 0.2548  0.0774  -0.0547 306 TRP A C   
56   O O   . TRP A 10  ? 1.0774 1.4038 0.8521 0.2777  0.0824  -0.0607 306 TRP A O   
57   C CB  . TRP A 10  ? 0.9198 1.2176 0.7746 0.1591  0.0659  -0.0340 306 TRP A CB  
58   C CG  . TRP A 10  ? 0.8678 1.1880 0.7556 0.1056  0.0677  -0.0197 306 TRP A CG  
59   C CD1 . TRP A 10  ? 0.8338 1.1334 0.7543 0.0711  0.0567  -0.0114 306 TRP A CD1 
60   C CD2 . TRP A 10  ? 0.8901 1.2494 0.7716 0.0818  0.0814  -0.0117 306 TRP A CD2 
61   N NE1 . TRP A 10  ? 0.7843 1.0989 0.7138 0.0297  0.0617  0.0008  306 TRP A NE1 
62   C CE2 . TRP A 10  ? 0.8716 1.2215 0.7771 0.0325  0.0768  0.0017  306 TRP A CE2 
63   C CE3 . TRP A 10  ? 0.8590 1.2574 0.7114 0.0983  0.0976  -0.0144 306 TRP A CE3 
64   C CZ2 . TRP A 10  ? 0.8779 1.2469 0.7740 -0.0034 0.0868  0.0134  306 TRP A CZ2 
65   C CZ3 . TRP A 10  ? 0.8805 1.3092 0.7309 0.0605  0.1088  -0.0026 306 TRP A CZ3 
66   C CH2 . TRP A 10  ? 0.8588 1.2690 0.7288 0.0087  0.1030  0.0116  306 TRP A CH2 
67   N N   . GLU A 11  ? 0.9961 1.3548 0.8265 0.2855  0.0712  -0.0606 307 GLU A N   
68   C CA  . GLU A 11  ? 1.0547 1.3926 0.8298 0.3540  0.0729  -0.0743 307 GLU A CA  
69   C C   . GLU A 11  ? 1.0444 1.5152 0.8449 0.3939  0.0895  -0.0784 307 GLU A C   
70   O O   . GLU A 11  ? 1.1358 1.6177 0.8873 0.4547  0.0982  -0.0894 307 GLU A O   
71   C CB  . GLU A 11  ? 1.0899 1.3363 0.8395 0.3691  0.0549  -0.0782 307 GLU A CB  
72   C CG  . GLU A 11  ? 1.1585 1.3388 0.8249 0.4394  0.0526  -0.0922 307 GLU A CG  
73   C CD  . GLU A 11  ? 1.2613 1.3913 0.9130 0.4607  0.0391  -0.0943 307 GLU A CD  
74   O OE1 . GLU A 11  ? 1.1521 1.2773 0.8515 0.4161  0.0294  -0.0856 307 GLU A OE1 
75   O OE2 . GLU A 11  ? 1.4100 1.5008 0.9952 0.5256  0.0384  -0.1048 307 GLU A OE2 
76   N N   . THR A 12  ? 0.9859 1.5607 0.8586 0.3609  0.0939  -0.0702 308 THR A N   
77   C CA  . THR A 12  ? 0.9694 1.6904 0.8756 0.3900  0.1080  -0.0731 308 THR A CA  
78   C C   . THR A 12  ? 0.9347 1.7771 0.8897 0.3416  0.1251  -0.0638 308 THR A C   
79   O O   . THR A 12  ? 0.8876 1.8544 0.8731 0.3509  0.1325  -0.0632 308 THR A O   
80   C CB  . THR A 12  ? 0.8992 1.6541 0.8447 0.3925  0.0976  -0.0723 308 THR A CB  
81   O OG1 . THR A 12  ? 0.8883 1.6512 0.8887 0.3180  0.0922  -0.0603 308 THR A OG1 
82   C CG2 . THR A 12  ? 0.9801 1.6073 0.8737 0.4315  0.0803  -0.0791 308 THR A CG2 
83   N N   . ASP A 13  ? 1.0273 1.8219 0.9860 0.2820  0.1249  -0.0537 309 ASP A N   
84   C CA  . ASP A 13  ? 0.9663 1.8510 0.9597 0.2253  0.1395  -0.0424 309 ASP A CA  
85   C C   . ASP A 13  ? 0.9227 1.8978 0.9768 0.1816  0.1387  -0.0353 309 ASP A C   
86   O O   . ASP A 13  ? 0.9155 1.9819 0.9953 0.1333  0.1517  -0.0265 309 ASP A O   
87   C CB  . ASP A 13  ? 0.9740 1.9601 0.9512 0.2557  0.1620  -0.0467 309 ASP A CB  
88   C CG  . ASP A 13  ? 1.1477 2.0404 1.0597 0.2843  0.1640  -0.0522 309 ASP A CG  
89   O OD1 . ASP A 13  ? 1.2157 2.0260 1.1130 0.2390  0.1589  -0.0436 309 ASP A OD1 
90   O OD2 . ASP A 13  ? 1.2109 2.1112 1.0811 0.3541  0.1701  -0.0653 309 ASP A OD2 
91   N N   . VAL A 14  ? 0.8522 1.8001 0.9242 0.1934  0.1235  -0.0386 310 VAL A N   
92   C CA  . VAL A 14  ? 0.7927 1.8208 0.9170 0.1534  0.1209  -0.0333 310 VAL A CA  
93   C C   . VAL A 14  ? 0.7811 1.7419 0.9158 0.0780  0.1136  -0.0209 310 VAL A C   
94   O O   . VAL A 14  ? 0.8047 1.6388 0.9180 0.0719  0.1005  -0.0189 310 VAL A O   
95   C CB  . VAL A 14  ? 0.7400 1.7572 0.8742 0.1950  0.1067  -0.0412 310 VAL A CB  
96   C CG1 . VAL A 14  ? 0.7135 1.7704 0.8941 0.1429  0.0990  -0.0350 310 VAL A CG1 
97   C CG2 . VAL A 14  ? 0.6837 1.7618 0.8000 0.2580  0.1060  -0.0494 310 VAL A CG2 
98   N N   . VAL A 15  ? 0.7570 1.8028 0.9202 0.0202  0.1215  -0.0126 311 VAL A N   
99   C CA  . VAL A 15  ? 0.7549 1.7354 0.9174 -0.0505 0.1148  -0.0008 311 VAL A CA  
100  C C   . VAL A 15  ? 0.7123 1.7338 0.9093 -0.0804 0.1059  -0.0005 311 VAL A C   
101  O O   . VAL A 15  ? 0.6850 1.8121 0.9039 -0.0750 0.1077  -0.0045 311 VAL A O   
102  C CB  . VAL A 15  ? 0.7605 1.7768 0.9076 -0.1041 0.1304  0.0103  311 VAL A CB  
103  C CG1 . VAL A 15  ? 0.7783 1.7079 0.9094 -0.1725 0.1219  0.0225  311 VAL A CG1 
104  C CG2 . VAL A 15  ? 0.7532 1.7293 0.8640 -0.0713 0.1386  0.0091  311 VAL A CG2 
105  N N   . LEU A 16  ? 0.7176 1.6333 0.9076 -0.1073 0.0909  0.0035  312 LEU A N   
106  C CA  . LEU A 16  ? 0.7229 1.6547 0.9352 -0.1433 0.0814  0.0043  312 LEU A CA  
107  C C   . LEU A 16  ? 0.7489 1.5962 0.9340 -0.2086 0.0775  0.0154  312 LEU A C   
108  O O   . LEU A 16  ? 0.7740 1.5165 0.9273 -0.2069 0.0743  0.0204  312 LEU A O   
109  C CB  . LEU A 16  ? 0.7026 1.5805 0.9258 -0.1009 0.0656  -0.0037 312 LEU A CB  
110  C CG  . LEU A 16  ? 0.6971 1.6299 0.9304 -0.0296 0.0671  -0.0144 312 LEU A CG  
111  C CD1 . LEU A 16  ? 0.6681 1.5016 0.8905 0.0102  0.0521  -0.0196 312 LEU A CD1 
112  C CD2 . LEU A 16  ? 0.6905 1.7524 0.9525 -0.0267 0.0692  -0.0185 312 LEU A CD2 
113  N N   . THR A 17  ? 0.7509 1.6424 0.9423 -0.2654 0.0770  0.0192  313 THR A N   
114  C CA  . THR A 17  ? 0.7877 1.5903 0.9398 -0.3288 0.0726  0.0294  313 THR A CA  
115  C C   . THR A 17  ? 0.7857 1.5110 0.9368 -0.3313 0.0552  0.0259  313 THR A C   
116  O O   . THR A 17  ? 0.7818 1.5683 0.9609 -0.3311 0.0497  0.0190  313 THR A O   
117  C CB  . THR A 17  ? 0.8132 1.6615 0.9404 -0.3839 0.0770  0.0341  313 THR A CB  
118  O OG1 . THR A 17  ? 0.8309 1.7499 0.9563 -0.3757 0.0917  0.0363  313 THR A OG1 
119  C CG2 . THR A 17  ? 0.8983 1.6314 0.9676 -0.4447 0.0717  0.0446  313 THR A CG2 
120  N N   . ASP A 18  ? 0.8532 1.4456 0.9687 -0.3295 0.0461  0.0302  314 ASP A N   
121  C CA  . ASP A 18  ? 0.8627 1.3743 0.9717 -0.3257 0.0307  0.0268  314 ASP A CA  
122  C C   . ASP A 18  ? 0.9155 1.3636 0.9758 -0.3900 0.0269  0.0339  314 ASP A C   
123  O O   . ASP A 18  ? 0.9893 1.3574 0.9995 -0.4124 0.0287  0.0435  314 ASP A O   
124  C CB  . ASP A 18  ? 0.8672 1.2813 0.9665 -0.2784 0.0225  0.0263  314 ASP A CB  
125  C CG  . ASP A 18  ? 0.8490 1.2013 0.9505 -0.2640 0.0083  0.0212  314 ASP A CG  
126  O OD1 . ASP A 18  ? 0.8775 1.1686 0.9451 -0.2988 0.0024  0.0243  314 ASP A OD1 
127  O OD2 . ASP A 18  ? 0.7861 1.1472 0.9169 -0.2186 0.0034  0.0142  314 ASP A OD2 
128  N N   . THR A 19  ? 0.8709 1.3496 0.9385 -0.4197 0.0209  0.0292  315 THR A N   
129  C CA  . THR A 19  ? 0.9092 1.2985 0.9188 -0.4709 0.0130  0.0328  315 THR A CA  
130  C C   . THR A 19  ? 0.9141 1.2292 0.9196 -0.4507 -0.0017 0.0259  315 THR A C   
131  O O   . THR A 19  ? 0.9945 1.2060 0.9405 -0.4814 -0.0093 0.0284  315 THR A O   
132  C CB  . THR A 19  ? 0.9677 1.4190 0.9626 -0.5079 0.0149  0.0310  315 THR A CB  
133  O OG1 . THR A 19  ? 0.9434 1.5201 0.9998 -0.4774 0.0165  0.0222  315 THR A OG1 
134  C CG2 . THR A 19  ? 1.0622 1.5285 1.0215 -0.5429 0.0257  0.0400  315 THR A CG2 
135  N N   . LEU A 20  ? 0.8668 1.2240 0.9253 -0.3956 -0.0056 0.0170  316 LEU A N   
136  C CA  . LEU A 20  ? 0.8827 1.1781 0.9388 -0.3722 -0.0182 0.0102  316 LEU A CA  
137  C C   . LEU A 20  ? 0.9084 1.0713 0.9163 -0.3559 -0.0240 0.0146  316 LEU A C   
138  O O   . LEU A 20  ? 0.9650 1.0551 0.9437 -0.3559 -0.0335 0.0110  316 LEU A O   
139  C CB  . LEU A 20  ? 0.8259 1.1833 0.9405 -0.3145 -0.0198 0.0023  316 LEU A CB  
140  C CG  . LEU A 20  ? 0.7844 1.0994 0.9044 -0.2888 -0.0311 -0.0049 316 LEU A CG  
141  C CD1 . LEU A 20  ? 0.7392 1.0664 0.8445 -0.3321 -0.0375 -0.0094 316 LEU A CD1 
142  C CD2 . LEU A 20  ? 0.7303 1.1027 0.8986 -0.2361 -0.0314 -0.0105 316 LEU A CD2 
143  N N   . HIS A 21  ? 0.9293 1.0627 0.9255 -0.3394 -0.0186 0.0220  317 HIS A N   
144  C CA  . HIS A 21  ? 0.9554 0.9764 0.9084 -0.3169 -0.0250 0.0264  317 HIS A CA  
145  C C   . HIS A 21  ? 1.0248 0.9444 0.9006 -0.3567 -0.0305 0.0307  317 HIS A C   
146  O O   . HIS A 21  ? 1.0749 0.8972 0.9089 -0.3319 -0.0382 0.0321  317 HIS A O   
147  C CB  . HIS A 21  ? 0.9703 0.9858 0.9201 -0.2988 -0.0189 0.0343  317 HIS A CB  
148  C CG  . HIS A 21  ? 0.9996 1.0117 0.9097 -0.3464 -0.0102 0.0439  317 HIS A CG  
149  N ND1 . HIS A 21  ? 0.9924 1.1074 0.9321 -0.3729 0.0016  0.0442  317 HIS A ND1 
150  C CD2 . HIS A 21  ? 1.0821 1.0008 0.9204 -0.3724 -0.0112 0.0541  317 HIS A CD2 
151  C CE1 . HIS A 21  ? 1.0703 1.1605 0.9613 -0.4181 0.0085  0.0546  317 HIS A CE1 
152  N NE2 . HIS A 21  ? 1.1218 1.0865 0.9475 -0.4196 0.0005  0.0611  317 HIS A NE2 
153  N N   . LEU A 22  ? 1.0436 0.9840 0.8945 -0.4178 -0.0268 0.0327  318 LEU A N   
154  C CA  . LEU A 22  ? 1.1209 0.9532 0.8857 -0.4630 -0.0332 0.0358  318 LEU A CA  
155  C C   . LEU A 22  ? 1.1998 0.9812 0.9515 -0.4476 -0.0449 0.0256  318 LEU A C   
156  O O   . LEU A 22  ? 1.2744 0.9306 0.9465 -0.4527 -0.0529 0.0266  318 LEU A O   
157  C CB  . LEU A 22  ? 1.1408 1.0254 0.8871 -0.5279 -0.0266 0.0388  318 LEU A CB  
158  C CG  . LEU A 22  ? 1.1149 1.0622 0.8709 -0.5454 -0.0132 0.0481  318 LEU A CG  
159  C CD1 . LEU A 22  ? 1.1722 1.1780 0.9076 -0.5945 -0.0084 0.0483  318 LEU A CD1 
160  C CD2 . LEU A 22  ? 1.1824 1.0191 0.8756 -0.5408 -0.0125 0.0601  318 LEU A CD2 
161  N N   . LYS A 23  ? 1.1086 0.9806 0.9299 -0.4271 -0.0462 0.0157  319 LYS A N   
162  C CA  . LYS A 23  ? 1.1775 1.0095 0.9897 -0.4105 -0.0564 0.0057  319 LYS A CA  
163  C C   . LYS A 23  ? 1.2049 0.9813 1.0213 -0.3436 -0.0605 0.0041  319 LYS A C   
164  O O   . LYS A 23  ? 1.3059 1.0318 1.1016 -0.3251 -0.0682 -0.0032 319 LYS A O   
165  C CB  . LYS A 23  ? 1.1132 1.0627 0.9942 -0.4125 -0.0569 -0.0034 319 LYS A CB  
166  C CG  . LYS A 23  ? 1.1182 1.1542 1.0069 -0.4745 -0.0531 -0.0027 319 LYS A CG  
167  C CD  . LYS A 23  ? 1.2942 1.2488 1.0996 -0.5170 -0.0563 -0.0010 319 LYS A CD  
168  C CE  . LYS A 23  ? 1.4334 1.3877 1.2326 -0.5226 -0.0656 -0.0112 319 LYS A CE  
169  N NZ  . LYS A 23  ? 1.3873 1.4778 1.2396 -0.5370 -0.0625 -0.0143 319 LYS A NZ  
170  N N   . SER A 24  ? 1.1944 0.9851 1.0362 -0.3089 -0.0557 0.0104  320 SER A N   
171  C CA  . SER A 24  ? 1.2248 0.9753 1.0707 -0.2506 -0.0598 0.0101  320 SER A CA  
172  C C   . SER A 24  ? 1.3901 1.0149 1.1522 -0.2426 -0.0675 0.0110  320 SER A C   
173  O O   . SER A 24  ? 1.4286 0.9755 1.1182 -0.2759 -0.0683 0.0173  320 SER A O   
174  C CB  . SER A 24  ? 1.1612 0.9395 1.0328 -0.2272 -0.0545 0.0179  320 SER A CB  
175  O OG  . SER A 24  ? 1.2191 0.9401 1.0701 -0.1827 -0.0600 0.0204  320 SER A OG  
176  N N   . THR A 25  ? 1.5646 1.1676 1.3307 -0.1967 -0.0730 0.0049  321 THR A N   
177  C CA  . THR A 25  ? 1.6921 1.1799 1.3776 -0.1748 -0.0804 0.0040  321 THR A CA  
178  C C   . THR A 25  ? 1.6856 1.1630 1.3767 -0.1133 -0.0827 0.0075  321 THR A C   
179  O O   . THR A 25  ? 1.7188 1.1113 1.3423 -0.0978 -0.0866 0.0140  321 THR A O   
180  C CB  . THR A 25  ? 1.7532 1.2189 1.4229 -0.1744 -0.0853 -0.0078 321 THR A CB  
181  O OG1 . THR A 25  ? 1.8589 1.2224 1.4568 -0.1341 -0.0918 -0.0104 321 THR A OG1 
182  C CG2 . THR A 25  ? 1.6480 1.2211 1.4075 -0.1526 -0.0827 -0.0147 321 THR A CG2 
183  N N   . LEU A 26  ? 1.4973 1.0605 1.2636 -0.0797 -0.0809 0.0040  322 LEU A N   
184  C CA  . LEU A 26  ? 1.4699 1.0405 1.2463 -0.0254 -0.0837 0.0065  322 LEU A CA  
185  C C   . LEU A 26  ? 1.4546 1.0321 1.2327 -0.0229 -0.0829 0.0171  322 LEU A C   
186  O O   . LEU A 26  ? 1.4547 1.0319 1.2275 -0.0618 -0.0787 0.0225  322 LEU A O   
187  C CB  . LEU A 26  ? 1.3322 0.9953 1.1850 -0.0028 -0.0816 0.0009  322 LEU A CB  
188  C CG  . LEU A 26  ? 1.3153 0.9769 1.1676 0.0089  -0.0827 -0.0091 322 LEU A CG  
189  C CD1 . LEU A 26  ? 1.1920 0.9498 1.1218 0.0118  -0.0787 -0.0122 322 LEU A CD1 
190  C CD2 . LEU A 26  ? 1.3218 0.9329 1.1274 0.0585  -0.0873 -0.0113 322 LEU A CD2 
191  N N   . GLU A 27  ? 1.4339 1.0255 1.2201 0.0231  -0.0871 0.0201  323 GLU A N   
192  C CA  . GLU A 27  ? 1.4395 1.0347 1.2216 0.0323  -0.0887 0.0297  323 GLU A CA  
193  C C   . GLU A 27  ? 1.3331 1.0307 1.1944 0.0414  -0.0869 0.0295  323 GLU A C   
194  O O   . GLU A 27  ? 1.2802 1.0359 1.1895 0.0522  -0.0859 0.0230  323 GLU A O   
195  C CB  . GLU A 27  ? 1.5075 1.0322 1.2230 0.0784  -0.0975 0.0341  323 GLU A CB  
196  C CG  . GLU A 27  ? 1.6577 1.0608 1.2785 0.0718  -0.1004 0.0329  323 GLU A CG  
197  C CD  . GLU A 27  ? 1.8306 1.1421 1.3650 0.1190  -0.1095 0.0388  323 GLU A CD  
198  O OE1 . GLU A 27  ? 1.8049 1.1311 1.3398 0.1388  -0.1131 0.0477  323 GLU A OE1 
199  O OE2 . GLU A 27  ? 1.9254 1.1450 1.3847 0.1386  -0.1139 0.0342  323 GLU A OE2 
200  N N   . THR A 28  ? 1.2575 0.9704 1.1251 0.0335  -0.0864 0.0368  324 THR A N   
201  C CA  . THR A 28  ? 1.1695 0.9645 1.0993 0.0318  -0.0846 0.0363  324 THR A CA  
202  C C   . THR A 28  ? 1.1222 0.9501 1.0632 0.0672  -0.0928 0.0394  324 THR A C   
203  O O   . THR A 28  ? 1.0812 0.9766 1.0713 0.0667  -0.0931 0.0370  324 THR A O   
204  C CB  . THR A 28  ? 1.1220 0.9220 1.0526 0.0004  -0.0787 0.0410  324 THR A CB  
205  O OG1 . THR A 28  ? 1.1582 0.9035 1.0358 0.0061  -0.0824 0.0502  324 THR A OG1 
206  C CG2 . THR A 28  ? 1.1264 0.9200 1.0553 -0.0375 -0.0701 0.0379  324 THR A CG2 
207  N N   . GLY A 29  ? 1.0978 0.8798 0.9899 0.0976  -0.1003 0.0447  325 GLY A N   
208  C CA  . GLY A 29  ? 1.0537 0.8723 0.9513 0.1289  -0.1093 0.0494  325 GLY A CA  
209  C C   . GLY A 29  ? 1.0803 0.8722 0.9492 0.1205  -0.1119 0.0582  325 GLY A C   
210  O O   . GLY A 29  ? 1.1257 0.9150 0.9696 0.1525  -0.1217 0.0642  325 GLY A O   
211  N N   . CYS A 30  ? 1.0785 0.8549 0.9487 0.0803  -0.1033 0.0593  326 CYS A N   
212  C CA  . CYS A 30  ? 1.1002 0.8492 0.9389 0.0694  -0.1037 0.0679  326 CYS A CA  
213  C C   . CYS A 30  ? 1.2059 0.8554 0.9633 0.0742  -0.1057 0.0759  326 CYS A C   
214  O O   . CYS A 30  ? 1.2719 0.8668 0.9973 0.0672  -0.1029 0.0735  326 CYS A O   
215  C CB  . CYS A 30  ? 1.0349 0.8077 0.8995 0.0274  -0.0921 0.0661  326 CYS A CB  
216  S SG  . CYS A 30  ? 0.9372 0.8008 0.8764 0.0207  -0.0897 0.0568  326 CYS A SG  
217  N N   . THR A 31  ? 1.2184 0.8373 0.9347 0.0842  -0.1112 0.0855  327 THR A N   
218  C CA  . THR A 31  ? 1.3445 0.8568 0.9717 0.0812  -0.1124 0.0952  327 THR A CA  
219  C C   . THR A 31  ? 1.3848 0.8881 0.9970 0.0431  -0.1048 0.1030  327 THR A C   
220  O O   . THR A 31  ? 1.3247 0.9023 0.9949 0.0231  -0.0983 0.0992  327 THR A O   
221  C CB  . THR A 31  ? 1.3827 0.8513 0.9550 0.1380  -0.1274 0.1014  327 THR A CB  
222  O OG1 . THR A 31  ? 1.3659 0.8850 0.9557 0.1547  -0.1349 0.1066  327 THR A OG1 
223  C CG2 . THR A 31  ? 1.3285 0.8321 0.9267 0.1804  -0.1335 0.0927  327 THR A CG2 
224  N N   . GLU A 32  ? 1.4842 0.8900 1.0102 0.0337  -0.1054 0.1140  328 GLU A N   
225  C CA  . GLU A 32  ? 1.5399 0.9362 1.0436 -0.0007 -0.0978 0.1230  328 GLU A CA  
226  C C   . GLU A 32  ? 1.5102 0.9539 1.0333 0.0268  -0.1057 0.1265  328 GLU A C   
227  O O   . GLU A 32  ? 1.5156 0.9798 1.0417 0.0006  -0.0982 0.1306  328 GLU A O   
228  C CB  . GLU A 32  ? 1.7276 0.9986 1.1228 -0.0194 -0.0976 0.1357  328 GLU A CB  
229  C CG  . GLU A 32  ? 1.7571 0.9884 1.1287 -0.0741 -0.0860 0.1340  328 GLU A CG  
230  C CD  . GLU A 32  ? 1.8545 1.0007 1.1727 -0.0565 -0.0939 0.1304  328 GLU A CD  
231  O OE1 . GLU A 32  ? 1.7680 0.9673 1.1448 -0.0336 -0.0963 0.1182  328 GLU A OE1 
232  O OE2 . GLU A 32  ? 2.0924 1.1117 1.3027 -0.0652 -0.0978 0.1399  328 GLU A OE2 
233  N N   . HIS A 33  ? 1.5106 0.9789 1.0463 0.0780  -0.1207 0.1245  329 HIS A N   
234  C CA  . HIS A 33  ? 1.4745 0.9842 1.0182 0.1037  -0.1314 0.1285  329 HIS A CA  
235  C C   . HIS A 33  ? 1.3565 0.9760 0.9843 0.1200  -0.1375 0.1178  329 HIS A C   
236  O O   . HIS A 33  ? 1.3016 0.9647 0.9385 0.1407  -0.1491 0.1199  329 HIS A O   
237  C CB  . HIS A 33  ? 1.6305 1.0697 1.0958 0.1519  -0.1471 0.1392  329 HIS A CB  
238  C CG  . HIS A 33  ? 1.7956 1.1045 1.1612 0.1386  -0.1433 0.1498  329 HIS A CG  
239  N ND1 . HIS A 33  ? 1.8751 1.1196 1.1736 0.1189  -0.1412 0.1630  329 HIS A ND1 
240  C CD2 . HIS A 33  ? 1.8805 1.1046 1.1939 0.1385  -0.1414 0.1494  329 HIS A CD2 
241  C CE1 . HIS A 33  ? 1.9800 1.1039 1.1875 0.1039  -0.1381 0.1710  329 HIS A CE1 
242  N NE2 . HIS A 33  ? 1.9959 1.1024 1.2089 0.1154  -0.1388 0.1625  329 HIS A NE2 
243  N N   . ILE A 34  ? 1.2469 0.9109 0.9315 0.1081  -0.1307 0.1069  330 ILE A N   
244  C CA  . ILE A 34  ? 1.1038 0.8640 0.8607 0.1150  -0.1352 0.0975  330 ILE A CA  
245  C C   . ILE A 34  ? 1.0823 0.8715 0.8895 0.0837  -0.1220 0.0874  330 ILE A C   
246  O O   . ILE A 34  ? 1.0809 0.8305 0.8759 0.0744  -0.1144 0.0857  330 ILE A O   
247  C CB  . ILE A 34  ? 1.1157 0.9078 0.8784 0.1624  -0.1493 0.0967  330 ILE A CB  
248  C CG1 . ILE A 34  ? 1.0261 0.9232 0.8553 0.1611  -0.1556 0.0896  330 ILE A CG1 
249  C CG2 . ILE A 34  ? 1.1742 0.9362 0.9321 0.1741  -0.1446 0.0919  330 ILE A CG2 
250  C CD1 . ILE A 34  ? 1.0083 0.9550 0.8319 0.2009  -0.1734 0.0939  330 ILE A CD1 
251  N N   . CYS A 35  ? 0.9601 0.8131 0.8168 0.0675  -0.1201 0.0806  331 CYS A N   
252  C CA  . CYS A 35  ? 0.9141 0.7973 0.8156 0.0444  -0.1095 0.0711  331 CYS A CA  
253  C C   . CYS A 35  ? 0.8801 0.8257 0.8267 0.0559  -0.1170 0.0644  331 CYS A C   
254  O O   . CYS A 35  ? 0.8430 0.8296 0.8006 0.0596  -0.1266 0.0644  331 CYS A O   
255  C CB  . CYS A 35  ? 0.8773 0.7716 0.7873 0.0164  -0.0996 0.0683  331 CYS A CB  
256  S SG  . CYS A 35  ? 0.8219 0.7536 0.7805 -0.0015 -0.0890 0.0567  331 CYS A SG  
257  N N   . MET A 36  ? 0.8507 0.8034 0.8190 0.0585  -0.1131 0.0593  332 MET A N   
258  C CA  . MET A 36  ? 0.8246 0.8351 0.8327 0.0661  -0.1178 0.0537  332 MET A CA  
259  C C   . MET A 36  ? 0.7770 0.8090 0.8188 0.0400  -0.1095 0.0459  332 MET A C   
260  O O   . MET A 36  ? 0.7517 0.8188 0.8216 0.0407  -0.1101 0.0414  332 MET A O   
261  C CB  . MET A 36  ? 0.8669 0.8682 0.8688 0.0929  -0.1193 0.0534  332 MET A CB  
262  C CG  . MET A 36  ? 0.9763 0.9364 0.9295 0.1259  -0.1272 0.0610  332 MET A CG  
263  S SD  . MET A 36  ? 1.1259 1.1556 1.0906 0.1708  -0.1415 0.0623  332 MET A SD  
264  C CE  . MET A 36  ? 1.1072 1.0710 0.9999 0.2092  -0.1513 0.0728  332 MET A CE  
265  N N   . GLY A 37  ? 0.7702 0.7819 0.8052 0.0197  -0.1013 0.0445  333 GLY A N   
266  C CA  . GLY A 37  ? 0.7592 0.7827 0.8161 0.0027  -0.0932 0.0371  333 GLY A CA  
267  C C   . GLY A 37  ? 0.7257 0.7827 0.8008 -0.0039 -0.0989 0.0326  333 GLY A C   
268  O O   . GLY A 37  ? 0.7238 0.7833 0.8108 -0.0131 -0.0935 0.0269  333 GLY A O   
269  N N   . SER A 38  ? 0.7134 0.7955 0.7861 -0.0015 -0.1103 0.0353  334 SER A N   
270  C CA  . SER A 38  ? 0.6715 0.7854 0.7561 -0.0165 -0.1164 0.0317  334 SER A CA  
271  C C   . SER A 38  ? 0.6697 0.8340 0.7769 -0.0086 -0.1232 0.0336  334 SER A C   
272  O O   . SER A 38  ? 0.6814 0.8816 0.7968 -0.0266 -0.1292 0.0322  334 SER A O   
273  C CB  . SER A 38  ? 0.6784 0.7930 0.7414 -0.0300 -0.1249 0.0317  334 SER A CB  
274  O OG  . SER A 38  ? 0.6756 0.8189 0.7352 -0.0182 -0.1360 0.0378  334 SER A OG  
275  N N   . ILE A 39  ? 0.7032 0.8703 0.8150 0.0171  -0.1222 0.0367  335 ILE A N   
276  C CA  . ILE A 39  ? 0.7102 0.9300 0.8422 0.0321  -0.1265 0.0375  335 ILE A CA  
277  C C   . ILE A 39  ? 0.7679 0.9900 0.9190 0.0215  -0.1180 0.0325  335 ILE A C   
278  O O   . ILE A 39  ? 0.7822 0.9600 0.9290 0.0227  -0.1091 0.0297  335 ILE A O   
279  C CB  . ILE A 39  ? 0.7323 0.9405 0.8492 0.0703  -0.1287 0.0417  335 ILE A CB  
280  C CG1 . ILE A 39  ? 0.7509 0.9479 0.8410 0.0824  -0.1377 0.0478  335 ILE A CG1 
281  C CG2 . ILE A 39  ? 0.7577 1.0278 0.8935 0.0935  -0.1324 0.0415  335 ILE A CG2 
282  C CD1 . ILE A 39  ? 0.7110 0.9789 0.8136 0.0769  -0.1505 0.0498  335 ILE A CD1 
283  N N   . MET A 40  ? 0.6905 0.9676 0.8605 0.0081  -0.1213 0.0319  336 MET A N   
284  C CA  . MET A 40  ? 0.7466 1.0221 0.9281 -0.0079 -0.1139 0.0281  336 MET A CA  
285  C C   . MET A 40  ? 0.8230 1.0937 1.0136 0.0172  -0.1069 0.0262  336 MET A C   
286  O O   . MET A 40  ? 0.8207 1.0532 1.0099 0.0128  -0.0992 0.0225  336 MET A O   
287  C CB  . MET A 40  ? 0.7210 1.0568 0.9134 -0.0337 -0.1191 0.0294  336 MET A CB  
288  C CG  . MET A 40  ? 0.7876 1.1261 0.9878 -0.0478 -0.1118 0.0272  336 MET A CG  
289  S SD  . MET A 40  ? 0.8450 1.1215 1.0152 -0.0856 -0.1105 0.0246  336 MET A SD  
290  C CE  . MET A 40  ? 0.6581 0.9727 0.8135 -0.1230 -0.1230 0.0279  336 MET A CE  
291  N N   . LEU A 41  ? 0.8654 1.1755 1.0615 0.0459  -0.1102 0.0283  337 LEU A N   
292  C CA  . LEU A 41  ? 1.0057 1.3033 1.1995 0.0741  -0.1046 0.0255  337 LEU A CA  
293  C C   . LEU A 41  ? 1.1731 1.4235 1.3370 0.1059  -0.1073 0.0273  337 LEU A C   
294  O O   . LEU A 41  ? 1.1630 1.4441 1.3191 0.1341  -0.1148 0.0310  337 LEU A O   
295  C CB  . LEU A 41  ? 0.9486 1.3248 1.1623 0.0881  -0.1049 0.0256  337 LEU A CB  
296  C CG  . LEU A 41  ? 0.8700 1.3121 1.1065 0.0517  -0.1064 0.0275  337 LEU A CG  
297  C CD1 . LEU A 41  ? 0.8088 1.3514 1.0624 0.0663  -0.1127 0.0310  337 LEU A CD1 
298  C CD2 . LEU A 41  ? 0.7552 1.1924 0.9995 0.0325  -0.0974 0.0245  337 LEU A CD2 
299  N N   . PRO A 42  ? 1.4883 1.6649 1.6301 0.1017  -0.1022 0.0255  338 PRO A N   
300  C CA  . PRO A 42  ? 1.5458 1.6641 1.6468 0.1251  -0.1050 0.0284  338 PRO A CA  
301  C C   . PRO A 42  ? 1.5922 1.6831 1.6675 0.1583  -0.1038 0.0252  338 PRO A C   
302  O O   . PRO A 42  ? 1.5580 1.6190 1.6303 0.1492  -0.0974 0.0197  338 PRO A O   
303  C CB  . PRO A 42  ? 1.5935 1.6534 1.6817 0.0957  -0.0992 0.0280  338 PRO A CB  
304  C CG  . PRO A 42  ? 1.5355 1.6256 1.6589 0.0659  -0.0938 0.0238  338 PRO A CG  
305  C CD  . PRO A 42  ? 1.4910 1.6364 1.6400 0.0729  -0.0946 0.0215  338 PRO A CD  
306  N N   . SER A 43  ? 1.4855 1.5855 1.5375 0.1999  -0.1108 0.0281  339 SER A N   
307  C CA  . SER A 43  ? 1.4901 1.5552 1.5046 0.2411  -0.1107 0.0245  339 SER A CA  
308  C C   . SER A 43  ? 1.4906 1.5243 1.4544 0.2878  -0.1200 0.0297  339 SER A C   
309  O O   . SER A 43  ? 1.5377 1.4805 1.4378 0.3121  -0.1210 0.0288  339 SER A O   
310  C CB  . SER A 43  ? 1.4450 1.5916 1.4948 0.2573  -0.1074 0.0196  339 SER A CB  
311  O OG  . SER A 43  ? 1.4578 1.5706 1.4661 0.3036  -0.1068 0.0149  339 SER A OG  
312  N N   . VAL A 52  ? 1.9320 1.7039 1.5365 0.5697  -0.0615 -0.0831 348 VAL A N   
313  C CA  . VAL A 52  ? 1.9476 1.6378 1.5152 0.5510  -0.0611 -0.0944 348 VAL A CA  
314  C C   . VAL A 52  ? 2.0333 1.5636 1.5179 0.5259  -0.0721 -0.0969 348 VAL A C   
315  O O   . VAL A 52  ? 2.0978 1.5588 1.5143 0.5459  -0.0785 -0.0929 348 VAL A O   
316  C CB  . VAL A 52  ? 1.9164 1.6167 1.4412 0.5908  -0.0549 -0.1029 348 VAL A CB  
317  C CG1 . VAL A 52  ? 1.9656 1.6066 1.4011 0.6401  -0.0604 -0.1022 348 VAL A CG1 
318  C CG2 . VAL A 52  ? 1.8769 1.4941 1.3629 0.5679  -0.0552 -0.1153 348 VAL A CG2 
319  N N   . ALA A 53  ? 2.0198 1.4942 1.5070 0.4781  -0.0746 -0.1033 349 ALA A N   
320  C CA  . ALA A 53  ? 2.0533 1.3902 1.4698 0.4353  -0.0847 -0.1044 349 ALA A CA  
321  C C   . ALA A 53  ? 2.1182 1.3449 1.4351 0.4346  -0.0884 -0.1145 349 ALA A C   
322  O O   . ALA A 53  ? 2.1144 1.3650 1.4343 0.4453  -0.0835 -0.1245 349 ALA A O   
323  C CB  . ALA A 53  ? 1.9721 1.3526 1.4612 0.3529  -0.0850 -0.0985 349 ALA A CB  
324  N N   . THR A 54  ? 2.1741 1.2808 1.4001 0.4191  -0.0972 -0.1107 350 THR A N   
325  C CA  . THR A 54  ? 2.2326 1.2253 1.3506 0.4184  -0.1028 -0.1167 350 THR A CA  
326  C C   . THR A 54  ? 2.2505 1.1655 1.3405 0.3414  -0.1092 -0.1216 350 THR A C   
327  O O   . THR A 54  ? 2.1705 1.1159 1.3195 0.2891  -0.1098 -0.1204 350 THR A O   
328  C CB  . THR A 54  ? 2.2953 1.2025 1.3183 0.4489  -0.1093 -0.1086 350 THR A CB  
329  O OG1 . THR A 54  ? 2.3523 1.1750 1.3374 0.3921  -0.1165 -0.1012 350 THR A OG1 
330  C CG2 . THR A 54  ? 2.2308 1.2331 1.2998 0.5082  -0.1047 -0.1016 350 THR A CG2 
331  N N   . LYS A 55  ? 2.3315 1.1493 1.3278 0.3331  -0.1147 -0.1268 351 LYS A N   
332  C CA  . LYS A 55  ? 2.3420 1.0992 1.3103 0.2566  -0.1213 -0.1312 351 LYS A CA  
333  C C   . LYS A 55  ? 2.3942 1.0693 1.3080 0.2025  -0.1287 -0.1200 351 LYS A C   
334  O O   . LYS A 55  ? 2.3507 1.0216 1.2789 0.1278  -0.1323 -0.1201 351 LYS A O   
335  C CB  . LYS A 55  ? 2.4146 1.1052 1.3053 0.2646  -0.1246 -0.1402 351 LYS A CB  
336  C CG  . LYS A 55  ? 2.5187 1.1581 1.3282 0.3391  -0.1247 -0.1384 351 LYS A CG  
337  C CD  . LYS A 55  ? 2.6491 1.2206 1.3822 0.3440  -0.1283 -0.1475 351 LYS A CD  
338  C CE  . LYS A 55  ? 2.7629 1.2912 1.4151 0.4244  -0.1284 -0.1462 351 LYS A CE  
339  N NZ  . LYS A 55  ? 2.8522 1.2685 1.3938 0.4216  -0.1357 -0.1514 351 LYS A NZ  
340  N N   . ASP A 56  ? 2.4854 1.1026 1.3356 0.2379  -0.1309 -0.1103 352 ASP A N   
341  C CA  . ASP A 56  ? 2.5189 1.0687 1.3224 0.1893  -0.1362 -0.0985 352 ASP A CA  
342  C C   . ASP A 56  ? 2.3843 1.0189 1.2899 0.1426  -0.1325 -0.0938 352 ASP A C   
343  O O   . ASP A 56  ? 2.3696 0.9895 1.2744 0.0673  -0.1353 -0.0900 352 ASP A O   
344  C CB  . ASP A 56  ? 2.6327 1.1256 1.3639 0.2459  -0.1386 -0.0902 352 ASP A CB  
345  C CG  . ASP A 56  ? 2.7339 1.1705 1.3795 0.3125  -0.1410 -0.0958 352 ASP A CG  
346  O OD1 . ASP A 56  ? 2.7718 1.1430 1.3560 0.2930  -0.1450 -0.1020 352 ASP A OD1 
347  O OD2 . ASP A 56  ? 2.7651 1.2281 1.4046 0.3842  -0.1393 -0.0940 352 ASP A OD2 
348  N N   . GLN A 57  ? 2.3038 1.0353 1.2983 0.1863  -0.1262 -0.0933 353 GLN A N   
349  C CA  . GLN A 57  ? 2.1882 0.9967 1.2754 0.1497  -0.1234 -0.0882 353 GLN A CA  
350  C C   . GLN A 57  ? 2.0336 0.9004 1.1866 0.0961  -0.1230 -0.0976 353 GLN A C   
351  O O   . GLN A 57  ? 1.9265 0.8459 1.1403 0.0462  -0.1226 -0.0926 353 GLN A O   
352  C CB  . GLN A 57  ? 2.1687 1.0673 1.3297 0.2133  -0.1177 -0.0848 353 GLN A CB  
353  C CG  . GLN A 57  ? 2.2426 1.1225 1.3516 0.2892  -0.1174 -0.0825 353 GLN A CG  
354  C CD  . GLN A 57  ? 2.1996 1.2018 1.3909 0.3520  -0.1100 -0.0846 353 GLN A CD  
355  O OE1 . GLN A 57  ? 2.1594 1.2383 1.4224 0.3480  -0.1049 -0.0921 353 GLN A OE1 
356  N NE2 . GLN A 57  ? 2.2192 1.2471 1.3996 0.4077  -0.1097 -0.0780 353 GLN A NE2 
357  N N   . LEU A 58  ? 2.0726 0.9403 1.2153 0.1052  -0.1232 -0.1103 354 LEU A N   
358  C CA  . LEU A 58  ? 1.9230 0.8814 1.1468 0.0701  -0.1219 -0.1184 354 LEU A CA  
359  C C   . LEU A 58  ? 1.8975 0.8312 1.1032 -0.0170 -0.1294 -0.1202 354 LEU A C   
360  O O   . LEU A 58  ? 1.7578 0.8073 1.0588 -0.0578 -0.1268 -0.1151 354 LEU A O   
361  C CB  . LEU A 58  ? 1.9106 0.8856 1.1308 0.1144  -0.1191 -0.1314 354 LEU A CB  
362  C CG  . LEU A 58  ? 1.6889 0.8203 1.0320 0.1149  -0.1109 -0.1297 354 LEU A CG  
363  C CD1 . LEU A 58  ? 1.5692 0.8075 1.0015 0.1508  -0.1019 -0.1171 354 LEU A CD1 
364  C CD2 . LEU A 58  ? 1.6905 0.8194 1.0104 0.1509  -0.1086 -0.1433 354 LEU A CD2 
365  N N   . PHE A 59  ? 1.9375 0.7776 1.0504 -0.0446 -0.1342 -0.1173 355 PHE A N   
366  C CA  . PHE A 59  ? 1.9493 0.8001 1.0596 -0.1280 -0.1393 -0.1161 355 PHE A CA  
367  C C   . PHE A 59  ? 1.9110 0.8049 1.0601 -0.1822 -0.1378 -0.1033 355 PHE A C   
368  O O   . PHE A 59  ? 1.8404 0.8152 1.0452 -0.2405 -0.1392 -0.1037 355 PHE A O   
369  C CB  . PHE A 59  ? 2.1171 0.8608 1.1162 -0.1486 -0.1448 -0.1148 355 PHE A CB  
370  C CG  . PHE A 59  ? 2.1667 0.9394 1.1694 -0.2289 -0.1498 -0.1154 355 PHE A CG  
371  C CD1 . PHE A 59  ? 2.0989 0.9692 1.1782 -0.2484 -0.1516 -0.1263 355 PHE A CD1 
372  C CD2 . PHE A 59  ? 2.2668 0.9766 1.1955 -0.2843 -0.1531 -0.1048 355 PHE A CD2 
373  C CE1 . PHE A 59  ? 2.0722 0.9864 1.1608 -0.3180 -0.1566 -0.1262 355 PHE A CE1 
374  C CE2 . PHE A 59  ? 2.2912 1.0431 1.2274 -0.3571 -0.1570 -0.1046 355 PHE A CE2 
375  C CZ  . PHE A 59  ? 2.1868 1.0457 1.2064 -0.3721 -0.1588 -0.1152 355 PHE A CZ  
376  N N   . PRO A 60  ? 1.9627 0.8136 1.0840 -0.1647 -0.1349 -0.0912 356 PRO A N   
377  C CA  . PRO A 60  ? 1.8465 0.7555 1.0181 -0.2110 -0.1316 -0.0797 356 PRO A CA  
378  C C   . PRO A 60  ? 1.7207 0.7550 1.0092 -0.2188 -0.1294 -0.0839 356 PRO A C   
379  O O   . PRO A 60  ? 1.6549 0.7709 0.9951 -0.2771 -0.1285 -0.0801 356 PRO A O   
380  C CB  . PRO A 60  ? 1.8944 0.7391 1.0228 -0.1672 -0.1293 -0.0690 356 PRO A CB  
381  C CG  . PRO A 60  ? 2.0278 0.7587 1.0481 -0.1303 -0.1335 -0.0713 356 PRO A CG  
382  C CD  . PRO A 60  ? 2.0466 0.7923 1.0775 -0.1099 -0.1354 -0.0863 356 PRO A CD  
383  N N   . LEU A 61  ? 1.6616 0.7553 1.0114 -0.1517 -0.1240 -0.0855 357 LEU A N   
384  C CA  . LEU A 61  ? 1.5111 0.7610 0.9887 -0.1447 -0.1166 -0.0814 357 LEU A CA  
385  C C   . LEU A 61  ? 1.4904 0.8082 1.0069 -0.1795 -0.1197 -0.0899 357 LEU A C   
386  O O   . LEU A 61  ? 1.4128 0.8396 1.0085 -0.2076 -0.1171 -0.0855 357 LEU A O   
387  C CB  . LEU A 61  ? 1.4716 0.7634 0.9931 -0.0701 -0.1103 -0.0805 357 LEU A CB  
388  C CG  . LEU A 61  ? 1.5377 0.7861 1.0328 -0.0265 -0.1082 -0.0720 357 LEU A CG  
389  C CD1 . LEU A 61  ? 1.5533 0.8186 1.0573 0.0468  -0.1048 -0.0759 357 LEU A CD1 
390  C CD2 . LEU A 61  ? 1.4739 0.8068 1.0443 -0.0412 -0.1029 -0.0592 357 LEU A CD2 
391  N N   . ALA A 62  ? 1.5465 0.8025 1.0054 -0.1732 -0.1257 -0.1026 358 ALA A N   
392  C CA  . ALA A 62  ? 1.5063 0.8201 0.9921 -0.2085 -0.1307 -0.1111 358 ALA A CA  
393  C C   . ALA A 62  ? 1.5245 0.8510 0.9980 -0.2884 -0.1371 -0.1092 358 ALA A C   
394  O O   . ALA A 62  ? 1.4344 0.8793 0.9848 -0.3158 -0.1369 -0.1073 358 ALA A O   
395  C CB  . ALA A 62  ? 1.5627 0.7902 0.9719 -0.1903 -0.1369 -0.1259 358 ALA A CB  
396  N N   . LYS A 63  ? 1.5957 0.8111 0.9741 -0.3219 -0.1410 -0.1073 359 LYS A N   
397  C CA  . LYS A 63  ? 1.5995 0.8538 0.9753 -0.3893 -0.1403 -0.0978 359 LYS A CA  
398  C C   . LYS A 63  ? 1.5309 0.8961 0.9906 -0.4114 -0.1342 -0.0880 359 LYS A C   
399  O O   . LYS A 63  ? 1.4964 0.9728 1.0128 -0.4500 -0.1337 -0.0861 359 LYS A O   
400  C CB  . LYS A 63  ? 1.7562 0.8868 1.0234 -0.4041 -0.1398 -0.0891 359 LYS A CB  
401  C CG  . LYS A 63  ? 1.7415 0.9058 0.9952 -0.4749 -0.1382 -0.0784 359 LYS A CG  
402  C CD  . LYS A 63  ? 1.8701 0.8989 1.0000 -0.4923 -0.1399 -0.0705 359 LYS A CD  
403  C CE  . LYS A 63  ? 1.8577 0.9186 0.9622 -0.5689 -0.1402 -0.0631 359 LYS A CE  
404  N NZ  . LYS A 63  ? 1.8537 1.0475 1.0471 -0.5989 -0.1324 -0.0552 359 LYS A NZ  
405  N N   . GLU A 64  ? 1.4904 0.8306 0.9576 -0.3829 -0.1292 -0.0812 360 GLU A N   
406  C CA  . GLU A 64  ? 1.4594 0.9014 1.0037 -0.3989 -0.1228 -0.0717 360 GLU A CA  
407  C C   . GLU A 64  ? 1.3541 0.9462 1.0075 -0.3826 -0.1199 -0.0740 360 GLU A C   
408  O O   . GLU A 64  ? 1.2867 0.9824 0.9918 -0.4196 -0.1182 -0.0707 360 GLU A O   
409  C CB  . GLU A 64  ? 1.4751 0.8840 1.0243 -0.3474 -0.1151 -0.0619 360 GLU A CB  
410  C CG  . GLU A 64  ? 1.4484 0.9697 1.0845 -0.3459 -0.1056 -0.0511 360 GLU A CG  
411  C CD  . GLU A 64  ? 1.4953 1.0039 1.1521 -0.2846 -0.0996 -0.0438 360 GLU A CD  
412  O OE1 . GLU A 64  ? 1.5553 0.9566 1.1434 -0.2537 -0.1026 -0.0441 360 GLU A OE1 
413  O OE2 . GLU A 64  ? 1.4257 1.0317 1.1630 -0.2661 -0.0926 -0.0382 360 GLU A OE2 
414  N N   . PHE A 65  ? 1.3378 0.9429 1.0216 -0.3267 -0.1195 -0.0798 361 PHE A N   
415  C CA  . PHE A 65  ? 1.2257 0.9566 1.0011 -0.3072 -0.1172 -0.0808 361 PHE A CA  
416  C C   . PHE A 65  ? 1.2070 0.9923 0.9865 -0.3524 -0.1261 -0.0888 361 PHE A C   
417  O O   . PHE A 65  ? 1.1470 1.0492 0.9931 -0.3628 -0.1253 -0.0865 361 PHE A O   
418  C CB  . PHE A 65  ? 1.1620 0.8869 0.9587 -0.2432 -0.1143 -0.0840 361 PHE A CB  
419  C CG  . PHE A 65  ? 1.0508 0.8780 0.9178 -0.2270 -0.1143 -0.0862 361 PHE A CG  
420  C CD1 . PHE A 65  ? 0.9760 0.8915 0.9156 -0.2075 -0.1078 -0.0783 361 PHE A CD1 
421  C CD2 . PHE A 65  ? 1.0491 0.8756 0.9008 -0.2299 -0.1214 -0.0963 361 PHE A CD2 
422  C CE1 . PHE A 65  ? 0.9046 0.8995 0.8957 -0.1897 -0.1086 -0.0797 361 PHE A CE1 
423  C CE2 . PHE A 65  ? 0.9938 0.9080 0.9029 -0.2129 -0.1221 -0.0973 361 PHE A CE2 
424  C CZ  . PHE A 65  ? 0.9036 0.8990 0.8802 -0.1921 -0.1158 -0.0885 361 PHE A CZ  
425  N N   . LEU A 66  ? 1.2893 0.9916 0.9943 -0.3763 -0.1355 -0.0988 362 LEU A N   
426  C CA  . LEU A 66  ? 1.2575 1.0128 0.9627 -0.4220 -0.1460 -0.1073 362 LEU A CA  
427  C C   . LEU A 66  ? 1.3058 1.1312 1.0268 -0.4698 -0.1408 -0.0967 362 LEU A C   
428  O O   . LEU A 66  ? 1.2679 1.2019 1.0352 -0.4855 -0.1424 -0.0966 362 LEU A O   
429  C CB  . LEU A 66  ? 1.3436 0.9882 0.9604 -0.4291 -0.1535 -0.1174 362 LEU A CB  
430  C CG  . LEU A 66  ? 1.3181 0.9333 0.9319 -0.3752 -0.1559 -0.1278 362 LEU A CG  
431  C CD1 . LEU A 66  ? 1.4204 0.9201 0.9346 -0.3899 -0.1648 -0.1401 362 LEU A CD1 
432  C CD2 . LEU A 66  ? 1.2285 0.9750 0.9295 -0.3576 -0.1565 -0.1284 362 LEU A CD2 
433  N N   . ASP A 67  ? 1.3106 1.0768 0.9904 -0.4882 -0.1338 -0.0868 363 ASP A N   
434  C CA  . ASP A 67  ? 1.3262 1.1608 1.0174 -0.5313 -0.1266 -0.0757 363 ASP A CA  
435  C C   . ASP A 67  ? 1.2400 1.2220 1.0303 -0.5162 -0.1205 -0.0715 363 ASP A C   
436  O O   . ASP A 67  ? 1.2562 1.3428 1.0795 -0.5385 -0.1181 -0.0686 363 ASP A O   
437  C CB  . ASP A 67  ? 1.4145 1.1518 1.0392 -0.5481 -0.1205 -0.0655 363 ASP A CB  
438  C CG  . ASP A 67  ? 1.5598 1.1780 1.0766 -0.5813 -0.1250 -0.0650 363 ASP A CG  
439  O OD1 . ASP A 67  ? 1.6406 1.2984 1.1403 -0.6282 -0.1265 -0.0634 363 ASP A OD1 
440  O OD2 . ASP A 67  ? 1.6054 1.0899 1.0498 -0.5582 -0.1272 -0.0659 363 ASP A OD2 
441  N N   . GLN A 68  ? 1.2196 1.2111 1.0536 -0.4758 -0.1177 -0.0709 364 GLN A N   
442  C CA  . GLN A 68  ? 1.1322 1.2531 1.0507 -0.4563 -0.1110 -0.0661 364 GLN A CA  
443  C C   . GLN A 68  ? 1.0809 1.2954 1.0555 -0.4301 -0.1170 -0.0731 364 GLN A C   
444  O O   . GLN A 68  ? 1.0438 1.3731 1.0710 -0.4216 -0.1125 -0.0696 364 GLN A O   
445  C CB  . GLN A 68  ? 1.0714 1.1691 1.0125 -0.4233 -0.1055 -0.0614 364 GLN A CB  
446  C CG  . GLN A 68  ? 1.0930 1.1032 1.0184 -0.3673 -0.1060 -0.0641 364 GLN A CG  
447  C CD  . GLN A 68  ? 1.0582 1.0331 0.9940 -0.3259 -0.0968 -0.0555 364 GLN A CD  
448  O OE1 . GLN A 68  ? 0.9880 1.0094 0.9773 -0.2790 -0.0922 -0.0534 364 GLN A OE1 
449  N NE2 . GLN A 68  ? 1.1600 1.0464 1.0374 -0.3442 -0.0952 -0.0504 364 GLN A NE2 
450  N N   . TYR A 69  ? 1.0907 1.2542 1.0471 -0.4146 -0.1272 -0.0832 365 TYR A N   
451  C CA  . TYR A 69  ? 1.0261 1.2702 1.0245 -0.3923 -0.1341 -0.0893 365 TYR A CA  
452  C C   . TYR A 69  ? 1.0646 1.3746 1.0611 -0.4233 -0.1355 -0.0886 365 TYR A C   
453  O O   . TYR A 69  ? 1.0343 1.4551 1.0824 -0.4052 -0.1345 -0.0866 365 TYR A O   
454  C CB  . TYR A 69  ? 1.0151 1.1783 0.9824 -0.3630 -0.1397 -0.0973 365 TYR A CB  
455  C CG  . TYR A 69  ? 0.9887 1.2274 0.9863 -0.3493 -0.1484 -0.1036 365 TYR A CG  
456  C CD1 . TYR A 69  ? 0.9124 1.2419 0.9742 -0.3053 -0.1451 -0.0989 365 TYR A CD1 
457  C CD2 . TYR A 69  ? 1.0385 1.2531 0.9931 -0.3804 -0.1610 -0.1142 365 TYR A CD2 
458  C CE1 . TYR A 69  ? 0.8819 1.2761 0.9647 -0.2891 -0.1541 -0.1036 365 TYR A CE1 
459  C CE2 . TYR A 69  ? 0.9957 1.2817 0.9766 -0.3659 -0.1696 -0.1192 365 TYR A CE2 
460  C CZ  . TYR A 69  ? 0.8975 1.2742 0.9427 -0.3198 -0.1665 -0.1136 365 TYR A CZ  
461  O OH  . TYR A 69  ? 0.8819 1.3243 0.9460 -0.3025 -0.1764 -0.1179 365 TYR A OH  
462  N N   . TYR A 70  ? 1.1683 1.4074 1.0988 -0.4683 -0.1380 -0.0900 366 TYR A N   
463  C CA  . TYR A 70  ? 1.1891 1.4909 1.1125 -0.5042 -0.1401 -0.0893 366 TYR A CA  
464  C C   . TYR A 70  ? 1.2283 1.6226 1.1800 -0.5227 -0.1290 -0.0788 366 TYR A C   
465  O O   . TYR A 70  ? 1.2341 1.7312 1.2108 -0.5330 -0.1290 -0.0778 366 TYR A O   
466  C CB  . TYR A 70  ? 1.2740 1.4672 1.1105 -0.5487 -0.1458 -0.0931 366 TYR A CB  
467  C CG  . TYR A 70  ? 1.2712 1.4165 1.0854 -0.5329 -0.1581 -0.1056 366 TYR A CG  
468  C CD1 . TYR A 70  ? 1.2674 1.4815 1.0943 -0.5435 -0.1661 -0.1104 366 TYR A CD1 
469  C CD2 . TYR A 70  ? 1.2815 1.3165 1.0603 -0.5045 -0.1615 -0.1130 366 TYR A CD2 
470  C CE1 . TYR A 70  ? 1.2868 1.4576 1.0907 -0.5284 -0.1775 -0.1222 366 TYR A CE1 
471  C CE2 . TYR A 70  ? 1.2806 1.2732 1.0344 -0.4878 -0.1717 -0.1254 366 TYR A CE2 
472  C CZ  . TYR A 70  ? 1.3012 1.3612 1.0679 -0.5007 -0.1798 -0.1299 366 TYR A CZ  
473  O OH  . TYR A 70  ? 1.2535 1.2711 0.9923 -0.4839 -0.1899 -0.1423 366 TYR A OH  
474  N N   . SER A 71  ? 1.2949 1.6574 1.2409 -0.5252 -0.1194 -0.0713 367 SER A N   
475  C CA  . SER A 71  ? 1.2712 1.7285 1.2486 -0.5340 -0.1080 -0.0623 367 SER A CA  
476  C C   . SER A 71  ? 1.1861 1.7587 1.2410 -0.4811 -0.1052 -0.0628 367 SER A C   
477  O O   . SER A 71  ? 1.2611 1.9355 1.3432 -0.4820 -0.0975 -0.0582 367 SER A O   
478  C CB  . SER A 71  ? 1.3225 1.7120 1.2728 -0.5454 -0.0991 -0.0544 367 SER A CB  
479  O OG  . SER A 71  ? 1.3848 1.8640 1.3594 -0.5559 -0.0879 -0.0464 367 SER A OG  
480  N N   . SER A 72  ? 1.0905 1.6463 1.1738 -0.4338 -0.1112 -0.0683 368 SER A N   
481  C CA  . SER A 72  ? 1.0053 1.6509 1.1491 -0.3786 -0.1092 -0.0679 368 SER A CA  
482  C C   . SER A 72  ? 1.0238 1.7526 1.1860 -0.3662 -0.1158 -0.0720 368 SER A C   
483  O O   . SER A 72  ? 0.9877 1.8059 1.1879 -0.3279 -0.1117 -0.0699 368 SER A O   
484  C CB  . SER A 72  ? 0.9314 1.5234 1.0916 -0.3347 -0.1129 -0.0707 368 SER A CB  
485  O OG  . SER A 72  ? 0.9001 1.5078 1.0721 -0.3064 -0.1232 -0.0772 368 SER A OG  
486  N N   . ILE A 73  ? 1.0348 1.7320 1.1660 -0.3942 -0.1261 -0.0780 369 ILE A N   
487  C CA  . ILE A 73  ? 1.0308 1.8083 1.1774 -0.3845 -0.1332 -0.0817 369 ILE A CA  
488  C C   . ILE A 73  ? 1.1043 1.9431 1.2328 -0.4356 -0.1296 -0.0789 369 ILE A C   
489  O O   . ILE A 73  ? 1.0994 1.9874 1.2230 -0.4496 -0.1369 -0.0825 369 ILE A O   
490  C CB  . ILE A 73  ? 1.0281 1.7450 1.1527 -0.3816 -0.1474 -0.0905 369 ILE A CB  
491  C CG1 . ILE A 73  ? 1.0894 1.6980 1.1511 -0.4351 -0.1512 -0.0944 369 ILE A CG1 
492  C CG2 . ILE A 73  ? 0.9647 1.6456 1.1111 -0.3273 -0.1503 -0.0926 369 ILE A CG2 
493  C CD1 . ILE A 73  ? 1.0686 1.5995 1.0997 -0.4283 -0.1639 -0.1046 369 ILE A CD1 
494  N N   . LYS A 74  ? 1.1316 1.9712 1.2483 -0.4647 -0.1185 -0.0720 370 LYS A N   
495  C CA  . LYS A 74  ? 1.2028 2.1019 1.2968 -0.5186 -0.1134 -0.0677 370 LYS A CA  
496  C C   . LYS A 74  ? 1.2805 2.1264 1.3201 -0.5741 -0.1230 -0.0715 370 LYS A C   
497  O O   . LYS A 74  ? 1.3434 2.2662 1.3758 -0.6058 -0.1250 -0.0716 370 LYS A O   
498  C CB  . LYS A 74  ? 1.1756 2.2237 1.3120 -0.4939 -0.1090 -0.0666 370 LYS A CB  
499  C CG  . LYS A 74  ? 1.1002 2.1899 1.2869 -0.4187 -0.1050 -0.0666 370 LYS A CG  
500  C CD  . LYS A 74  ? 1.0996 2.2656 1.3048 -0.4068 -0.0912 -0.0609 370 LYS A CD  
501  C CE  . LYS A 74  ? 1.0732 2.2718 1.3175 -0.3289 -0.0887 -0.0619 370 LYS A CE  
502  N NZ  . LYS A 74  ? 1.0534 2.2962 1.3099 -0.3115 -0.0756 -0.0572 370 LYS A NZ  
503  N N   . ARG A 75  ? 1.2875 1.9992 1.2837 -0.5852 -0.1291 -0.0750 371 ARG A N   
504  C CA  . ARG A 75  ? 1.3465 1.9795 1.2759 -0.6357 -0.1381 -0.0791 371 ARG A CA  
505  C C   . ARG A 75  ? 1.4255 1.9090 1.2874 -0.6608 -0.1365 -0.0771 371 ARG A C   
506  O O   . ARG A 75  ? 1.4440 1.8166 1.2553 -0.6659 -0.1453 -0.0839 371 ARG A O   
507  C CB  . ARG A 75  ? 1.3040 1.9249 1.2404 -0.6103 -0.1518 -0.0895 371 ARG A CB  
508  C CG  . ARG A 75  ? 1.2644 2.0229 1.2506 -0.5922 -0.1552 -0.0911 371 ARG A CG  
509  C CD  . ARG A 75  ? 1.2307 1.9961 1.2556 -0.5301 -0.1637 -0.0979 371 ARG A CD  
510  N NE  . ARG A 75  ? 1.2745 2.0590 1.2870 -0.5383 -0.1769 -0.1053 371 ARG A NE  
511  C CZ  . ARG A 75  ? 1.3525 2.0365 1.3149 -0.5568 -0.1875 -0.1135 371 ARG A CZ  
512  N NH1 . ARG A 75  ? 1.3902 1.9451 1.3068 -0.5666 -0.1863 -0.1158 371 ARG A NH1 
513  N NH2 . ARG A 75  ? 1.3630 2.0752 1.3168 -0.5629 -0.1996 -0.1202 371 ARG A NH2 
514  N N   . PHE A 76  ? 1.4294 1.9065 1.2848 -0.6734 -0.1252 -0.0680 372 PHE A N   
515  C CA  . PHE A 76  ? 1.5045 1.8434 1.2872 -0.6994 -0.1229 -0.0639 372 PHE A CA  
516  C C   . PHE A 76  ? 1.5811 1.8574 1.2771 -0.7644 -0.1277 -0.0626 372 PHE A C   
517  O O   . PHE A 76  ? 1.5960 1.9532 1.2853 -0.8096 -0.1245 -0.0573 372 PHE A O   
518  C CB  . PHE A 76  ? 1.5386 1.9055 1.3365 -0.7010 -0.1099 -0.0537 372 PHE A CB  
519  C CG  . PHE A 76  ? 1.5964 1.8217 1.3266 -0.7134 -0.1072 -0.0486 372 PHE A CG  
520  C CD1 . PHE A 76  ? 1.6876 1.7784 1.3221 -0.7476 -0.1136 -0.0491 372 PHE A CD1 
521  C CD2 . PHE A 76  ? 1.6316 1.8575 1.3887 -0.6884 -0.0982 -0.0426 372 PHE A CD2 
522  C CE1 . PHE A 76  ? 1.7644 1.7235 1.3303 -0.7517 -0.1114 -0.0438 372 PHE A CE1 
523  C CE2 . PHE A 76  ? 1.7287 1.8277 1.4221 -0.6964 -0.0961 -0.0373 372 PHE A CE2 
524  C CZ  . PHE A 76  ? 1.7725 1.7370 1.3688 -0.7259 -0.1028 -0.0378 372 PHE A CZ  
525  N N   . GLY A 77  ? 1.6514 1.7824 1.2753 -0.7685 -0.1352 -0.0673 373 GLY A N   
526  C CA  . GLY A 77  ? 1.7419 1.7855 1.2669 -0.8277 -0.1400 -0.0654 373 GLY A CA  
527  C C   . GLY A 77  ? 1.7661 1.8561 1.2856 -0.8532 -0.1496 -0.0721 373 GLY A C   
528  O O   . GLY A 77  ? 1.8939 1.9089 1.3259 -0.9055 -0.1545 -0.0707 373 GLY A O   
529  N N   . SER A 78  ? 1.6551 1.8614 1.2590 -0.8177 -0.1531 -0.0790 374 SER A N   
530  C CA  . SER A 78  ? 1.6125 1.8651 1.2142 -0.8363 -0.1635 -0.0861 374 SER A CA  
531  C C   . SER A 78  ? 1.6535 1.7612 1.1820 -0.8346 -0.1746 -0.0956 374 SER A C   
532  O O   . SER A 78  ? 1.6990 1.6772 1.1825 -0.8126 -0.1735 -0.0969 374 SER A O   
533  C CB  . SER A 78  ? 1.5200 1.9131 1.2223 -0.7866 -0.1657 -0.0913 374 SER A CB  
534  O OG  . SER A 78  ? 1.5055 1.8585 1.2444 -0.7225 -0.1673 -0.0974 374 SER A OG  
535  N N   . LYS A 79  ? 1.6468 1.7758 1.1597 -0.8552 -0.1852 -0.1027 375 LYS A N   
536  C CA  . LYS A 79  ? 1.6859 1.6792 1.1239 -0.8532 -0.1958 -0.1129 375 LYS A CA  
537  C C   . LYS A 79  ? 1.6357 1.5872 1.1075 -0.7811 -0.1988 -0.1235 375 LYS A C   
538  O O   . LYS A 79  ? 1.6895 1.4986 1.0953 -0.7626 -0.2003 -0.1285 375 LYS A O   
539  C CB  . LYS A 79  ? 1.6951 1.7352 1.1175 -0.8890 -0.2069 -0.1187 375 LYS A CB  
540  C CG  . LYS A 79  ? 1.7769 1.6795 1.1184 -0.8863 -0.2183 -0.1303 375 LYS A CG  
541  C CD  . LYS A 79  ? 1.9156 1.7239 1.1442 -0.9581 -0.2215 -0.1255 375 LYS A CD  
542  C CE  . LYS A 79  ? 1.9881 1.6204 1.1173 -0.9447 -0.2294 -0.1352 375 LYS A CE  
543  N NZ  . LYS A 79  ? 2.0634 1.5739 1.1615 -0.8971 -0.2222 -0.1342 375 LYS A NZ  
544  N N   . ALA A 80  ? 1.5548 1.6284 1.1234 -0.7378 -0.1994 -0.1265 376 ALA A N   
545  C CA  . ALA A 80  ? 1.5396 1.5815 1.1375 -0.6737 -0.2025 -0.1360 376 ALA A CA  
546  C C   . ALA A 80  ? 1.5433 1.4951 1.1250 -0.6479 -0.1934 -0.1324 376 ALA A C   
547  O O   . ALA A 80  ? 1.5570 1.4098 1.1059 -0.6118 -0.1958 -0.1409 376 ALA A O   
548  C CB  . ALA A 80  ? 1.4186 1.6078 1.1168 -0.6338 -0.2041 -0.1365 376 ALA A CB  
549  N N   . HIS A 81  ? 1.5303 1.5155 1.1302 -0.6651 -0.1827 -0.1199 377 HIS A N   
550  C CA  . HIS A 81  ? 1.5573 1.4538 1.1346 -0.6457 -0.1744 -0.1152 377 HIS A CA  
551  C C   . HIS A 81  ? 1.6799 1.4058 1.1445 -0.6597 -0.1768 -0.1174 377 HIS A C   
552  O O   . HIS A 81  ? 1.6781 1.3052 1.1130 -0.6178 -0.1765 -0.1227 377 HIS A O   
553  C CB  . HIS A 81  ? 1.5367 1.5003 1.1435 -0.6695 -0.1630 -0.1012 377 HIS A CB  
554  C CG  . HIS A 81  ? 1.5462 1.4241 1.1289 -0.6529 -0.1550 -0.0951 377 HIS A CG  
555  N ND1 . HIS A 81  ? 1.5679 1.4700 1.1511 -0.6784 -0.1449 -0.0826 377 HIS A ND1 
556  C CD2 . HIS A 81  ? 1.5339 1.3058 1.0897 -0.6115 -0.1555 -0.0998 377 HIS A CD2 
557  C CE1 . HIS A 81  ? 1.5567 1.3690 1.1151 -0.6541 -0.1404 -0.0794 377 HIS A CE1 
558  N NE2 . HIS A 81  ? 1.5401 1.2739 1.0822 -0.6123 -0.1466 -0.0896 377 HIS A NE2 
559  N N   . MET A 82  ? 1.7676 1.4561 1.1626 -0.7168 -0.1788 -0.1126 378 MET A N   
560  C CA  . MET A 82  ? 1.8778 1.3972 1.1531 -0.7300 -0.1814 -0.1128 378 MET A CA  
561  C C   . MET A 82  ? 1.9036 1.3396 1.1438 -0.6886 -0.1897 -0.1277 378 MET A C   
562  O O   . MET A 82  ? 2.0038 1.3056 1.1741 -0.6560 -0.1887 -0.1302 378 MET A O   
563  C CB  . MET A 82  ? 1.9607 1.4663 1.1666 -0.8040 -0.1839 -0.1054 378 MET A CB  
564  C CG  . MET A 82  ? 2.0299 1.6067 1.2532 -0.8475 -0.1745 -0.0906 378 MET A CG  
565  S SD  . MET A 82  ? 2.2154 1.6737 1.3834 -0.8313 -0.1654 -0.0799 378 MET A SD  
566  C CE  . MET A 82  ? 1.9604 1.5512 1.2635 -0.7803 -0.1561 -0.0789 378 MET A CE  
567  N N   . ASP A 83  ? 1.8192 1.3351 1.1044 -0.6851 -0.1976 -0.1378 379 ASP A N   
568  C CA  . ASP A 83  ? 1.8338 1.2745 1.0812 -0.6481 -0.2052 -0.1527 379 ASP A CA  
569  C C   . ASP A 83  ? 1.8030 1.2301 1.0889 -0.5781 -0.2011 -0.1595 379 ASP A C   
570  O O   . ASP A 83  ? 1.8309 1.1427 1.0534 -0.5391 -0.2012 -0.1674 379 ASP A O   
571  C CB  . ASP A 83  ? 1.7986 1.3330 1.0830 -0.6635 -0.2154 -0.1612 379 ASP A CB  
572  C CG  . ASP A 83  ? 1.8827 1.3973 1.1029 -0.7298 -0.2212 -0.1576 379 ASP A CG  
573  O OD1 . ASP A 83  ? 1.9805 1.3549 1.0943 -0.7495 -0.2212 -0.1552 379 ASP A OD1 
574  O OD2 . ASP A 83  ? 1.8670 1.5056 1.1388 -0.7612 -0.2258 -0.1565 379 ASP A OD2 
575  N N   . ARG A 84  ? 1.6866 1.2320 1.0722 -0.5599 -0.1971 -0.1560 380 ARG A N   
576  C CA  . ARG A 84  ? 1.6165 1.1536 1.0374 -0.5000 -0.1931 -0.1607 380 ARG A CA  
577  C C   . ARG A 84  ? 1.6876 1.1078 1.0523 -0.4799 -0.1849 -0.1553 380 ARG A C   
578  O O   . ARG A 84  ? 1.7082 1.0663 1.0569 -0.4262 -0.1823 -0.1619 380 ARG A O   
579  C CB  . ARG A 84  ? 1.4900 1.1740 1.0211 -0.4909 -0.1906 -0.1552 380 ARG A CB  
580  C CG  . ARG A 84  ? 1.3965 1.0786 0.9637 -0.4369 -0.1871 -0.1582 380 ARG A CG  
581  C CD  . ARG A 84  ? 1.3443 1.0609 0.9328 -0.4039 -0.1946 -0.1699 380 ARG A CD  
582  N NE  . ARG A 84  ? 1.2771 0.9905 0.9039 -0.3351 -0.1813 -0.1642 380 ARG A NE  
583  C CZ  . ARG A 84  ? 1.3118 0.9423 0.8957 -0.2885 -0.1758 -0.1698 380 ARG A CZ  
584  N NH1 . ARG A 84  ? 1.4411 0.9760 0.9368 -0.2997 -0.1842 -0.1838 380 ARG A NH1 
585  N NH2 . ARG A 84  ? 1.2452 0.8916 0.8726 -0.2300 -0.1618 -0.1616 380 ARG A NH2 
586  N N   . LEU A 85  ? 1.7561 1.1494 1.0886 -0.5202 -0.1805 -0.1425 381 LEU A N   
587  C CA  . LEU A 85  ? 1.7978 1.0708 1.0627 -0.5022 -0.1743 -0.1358 381 LEU A CA  
588  C C   . LEU A 85  ? 1.9232 1.0496 1.0807 -0.4772 -0.1779 -0.1431 381 LEU A C   
589  O O   . LEU A 85  ? 1.9394 0.9884 1.0667 -0.4192 -0.1743 -0.1466 381 LEU A O   
590  C CB  . LEU A 85  ? 1.8229 1.0960 1.0631 -0.5570 -0.1700 -0.1203 381 LEU A CB  
591  C CG  . LEU A 85  ? 1.7925 1.0189 1.0234 -0.5356 -0.1617 -0.1103 381 LEU A CG  
592  C CD1 . LEU A 85  ? 1.6757 1.0180 1.0183 -0.5086 -0.1569 -0.1103 381 LEU A CD1 
593  C CD2 . LEU A 85  ? 1.8537 1.0605 1.0368 -0.5926 -0.1583 -0.0956 381 LEU A CD2 
594  N N   . GLU A 86  ? 1.9928 1.0827 1.0895 -0.5181 -0.1848 -0.1450 382 GLU A N   
595  C CA  . GLU A 86  ? 2.1333 1.0845 1.1228 -0.4947 -0.1888 -0.1517 382 GLU A CA  
596  C C   . GLU A 86  ? 2.0693 1.0278 1.0832 -0.4333 -0.1898 -0.1678 382 GLU A C   
597  O O   . GLU A 86  ? 2.1590 1.0131 1.1057 -0.3801 -0.1876 -0.1727 382 GLU A O   
598  C CB  . GLU A 86  ? 2.3005 1.2216 1.2243 -0.5578 -0.1969 -0.1505 382 GLU A CB  
599  C CG  . GLU A 86  ? 2.4959 1.2617 1.2939 -0.5401 -0.2017 -0.1554 382 GLU A CG  
600  C CD  . GLU A 86  ? 2.6942 1.3253 1.3788 -0.5548 -0.2004 -0.1418 382 GLU A CD  
601  O OE1 . GLU A 86  ? 2.7121 1.3643 1.4182 -0.5676 -0.1944 -0.1296 382 GLU A OE1 
602  O OE2 . GLU A 86  ? 2.8709 1.3716 1.4389 -0.5529 -0.2060 -0.1431 382 GLU A OE2 
603  N N   . GLU A 87  ? 1.9292 1.0135 1.0351 -0.4369 -0.1928 -0.1753 383 GLU A N   
604  C CA  . GLU A 87  ? 1.8552 0.9543 0.9837 -0.3816 -0.1934 -0.1899 383 GLU A CA  
605  C C   . GLU A 87  ? 1.8711 0.9411 1.0117 -0.3146 -0.1839 -0.1904 383 GLU A C   
606  O O   . GLU A 87  ? 1.8498 0.8568 0.9487 -0.2570 -0.1803 -0.1992 383 GLU A O   
607  C CB  . GLU A 87  ? 1.7464 0.9920 0.9712 -0.3998 -0.1993 -0.1945 383 GLU A CB  
608  C CG  . GLU A 87  ? 1.7124 0.9898 0.9690 -0.3453 -0.1993 -0.2070 383 GLU A CG  
609  C CD  . GLU A 87  ? 1.6090 1.0215 0.9436 -0.3650 -0.2080 -0.2098 383 GLU A CD  
610  O OE1 . GLU A 87  ? 1.5096 1.0283 0.9241 -0.3827 -0.2079 -0.2005 383 GLU A OE1 
611  O OE2 . GLU A 87  ? 1.5557 0.9692 0.8697 -0.3591 -0.2147 -0.2204 383 GLU A OE2 
612  N N   . VAL A 88  ? 1.8388 0.9592 1.0363 -0.3191 -0.1789 -0.1804 384 VAL A N   
613  C CA  . VAL A 88  ? 1.8156 0.9164 1.0286 -0.2579 -0.1704 -0.1800 384 VAL A CA  
614  C C   . VAL A 88  ? 1.9481 0.9189 1.0694 -0.2259 -0.1654 -0.1743 384 VAL A C   
615  O O   . VAL A 88  ? 1.9421 0.8718 1.0434 -0.1573 -0.1591 -0.1785 384 VAL A O   
616  C CB  . VAL A 88  ? 1.6919 0.8881 0.9931 -0.2751 -0.1679 -0.1708 384 VAL A CB  
617  C CG1 . VAL A 88  ? 1.6785 0.8483 0.9901 -0.2168 -0.1571 -0.1638 384 VAL A CG1 
618  C CG2 . VAL A 88  ? 1.5613 0.9015 0.9656 -0.2744 -0.1683 -0.1709 384 VAL A CG2 
619  N N   . ASN A 89  ? 2.0150 0.9263 1.0783 -0.2722 -0.1679 -0.1633 385 ASN A N   
620  C CA  . ASN A 89  ? 2.1183 0.8959 1.0768 -0.2439 -0.1661 -0.1569 385 ASN A CA  
621  C C   . ASN A 89  ? 2.1806 0.8817 1.0689 -0.1950 -0.1675 -0.1678 385 ASN A C   
622  O O   . ASN A 89  ? 2.2658 0.9081 1.1138 -0.1262 -0.1624 -0.1680 385 ASN A O   
623  C CB  . ASN A 89  ? 2.2278 0.9505 1.1211 -0.3119 -0.1706 -0.1444 385 ASN A CB  
624  C CG  . ASN A 89  ? 2.3733 0.9619 1.1588 -0.2860 -0.1697 -0.1343 385 ASN A CG  
625  O OD1 . ASN A 89  ? 2.3896 0.9679 1.1862 -0.2371 -0.1640 -0.1296 385 ASN A OD1 
626  N ND2 . ASN A 89  ? 2.5054 0.9897 1.1809 -0.3182 -0.1763 -0.1307 385 ASN A ND2 
627  N N   . LYS A 90  ? 2.1707 0.8816 1.0469 -0.2268 -0.1742 -0.1768 386 LYS A N   
628  C CA  . LYS A 90  ? 2.2107 0.8506 1.0189 -0.1822 -0.1752 -0.1873 386 LYS A CA  
629  C C   . LYS A 90  ? 2.1586 0.8551 1.0218 -0.1078 -0.1668 -0.1979 386 LYS A C   
630  O O   . LYS A 90  ? 2.2157 0.8510 1.0230 -0.0442 -0.1624 -0.2017 386 LYS A O   
631  C CB  . LYS A 90  ? 2.2435 0.8876 1.0298 -0.2365 -0.1848 -0.1946 386 LYS A CB  
632  C CG  . LYS A 90  ? 2.3767 0.9265 1.0670 -0.2966 -0.1924 -0.1849 386 LYS A CG  
633  C CD  . LYS A 90  ? 2.3835 0.9509 1.0592 -0.3529 -0.2023 -0.1920 386 LYS A CD  
634  C CE  . LYS A 90  ? 2.4841 0.9663 1.0659 -0.4203 -0.2092 -0.1807 386 LYS A CE  
635  N NZ  . LYS A 90  ? 2.5587 1.0853 1.1431 -0.4862 -0.2187 -0.1856 386 LYS A NZ  
636  N N   . GLU A 91  ? 2.0498 0.8651 1.0182 -0.1128 -0.1643 -0.2017 387 GLU A N   
637  C CA  . GLU A 91  ? 1.9886 0.8583 1.0036 -0.0443 -0.1553 -0.2104 387 GLU A CA  
638  C C   . GLU A 91  ? 2.0305 0.8814 1.0454 0.0190  -0.1450 -0.2028 387 GLU A C   
639  O O   . GLU A 91  ? 2.0338 0.8975 1.0495 0.0892  -0.1356 -0.2075 387 GLU A O   
640  C CB  . GLU A 91  ? 1.8350 0.8289 0.9507 -0.0673 -0.1574 -0.2154 387 GLU A CB  
641  C CG  . GLU A 91  ? 1.7472 0.8171 0.9219 0.0008  -0.1447 -0.2173 387 GLU A CG  
642  C CD  . GLU A 91  ? 1.6305 0.8562 0.9312 -0.0169 -0.1410 -0.2061 387 GLU A CD  
643  O OE1 . GLU A 91  ? 1.5988 0.8708 0.9384 -0.0756 -0.1496 -0.2007 387 GLU A OE1 
644  O OE2 . GLU A 91  ? 1.5688 0.8708 0.9257 0.0295  -0.1290 -0.2022 387 GLU A OE2 
645  N N   . ILE A 92  ? 2.0474 0.8787 1.0638 -0.0038 -0.1459 -0.1901 388 ILE A N   
646  C CA  . ILE A 92  ? 2.0459 0.8510 1.0496 0.0558  -0.1381 -0.1815 388 ILE A CA  
647  C C   . ILE A 92  ? 2.1786 0.8728 1.0730 0.0975  -0.1389 -0.1788 388 ILE A C   
648  O O   . ILE A 92  ? 2.2066 0.8949 1.0874 0.1675  -0.1323 -0.1751 388 ILE A O   
649  C CB  . ILE A 92  ? 2.0037 0.8149 1.0330 0.0176  -0.1397 -0.1682 388 ILE A CB  
650  C CG1 . ILE A 92  ? 1.8683 0.7924 1.0038 -0.0182 -0.1399 -0.1707 388 ILE A CG1 
651  C CG2 . ILE A 92  ? 2.0298 0.8201 1.0474 0.0798  -0.1331 -0.1588 388 ILE A CG2 
652  C CD1 . ILE A 92  ? 1.8504 0.7909 1.0159 -0.0602 -0.1410 -0.1574 388 ILE A CD1 
653  N N   . GLU A 93  ? 2.2415 0.8518 1.0550 0.0571  -0.1477 -0.1801 389 GLU A N   
654  C CA  . GLU A 93  ? 2.3785 0.8786 1.0798 0.1007  -0.1498 -0.1793 389 GLU A CA  
655  C C   . GLU A 93  ? 2.3616 0.8974 1.0730 0.1674  -0.1428 -0.1908 389 GLU A C   
656  O O   . GLU A 93  ? 2.3902 0.9202 1.0796 0.2425  -0.1365 -0.1883 389 GLU A O   
657  C CB  . GLU A 93  ? 2.4893 0.8904 1.0991 0.0364  -0.1612 -0.1779 389 GLU A CB  
658  C CG  . GLU A 93  ? 2.5213 0.8945 1.1166 -0.0339 -0.1665 -0.1649 389 GLU A CG  
659  C CD  . GLU A 93  ? 2.6780 0.9574 1.1916 -0.0025 -0.1670 -0.1518 389 GLU A CD  
660  O OE1 . GLU A 93  ? 2.7374 0.9446 1.1743 0.0648  -0.1669 -0.1528 389 GLU A OE1 
661  O OE2 . GLU A 93  ? 2.7040 0.9850 1.2276 -0.0435 -0.1676 -0.1404 389 GLU A OE2 
662  N N   . SER A 94  ? 2.3316 0.9156 1.0787 0.1409  -0.1437 -0.2031 390 SER A N   
663  C CA  . SER A 94  ? 2.3630 0.9679 1.1026 0.1963  -0.1375 -0.2139 390 SER A CA  
664  C C   . SER A 94  ? 2.3061 1.0212 1.1289 0.2624  -0.1231 -0.2145 390 SER A C   
665  O O   . SER A 94  ? 2.3135 1.0407 1.1170 0.3293  -0.1151 -0.2170 390 SER A O   
666  C CB  . SER A 94  ? 2.3434 0.9794 1.1033 0.1476  -0.1426 -0.2263 390 SER A CB  
667  O OG  . SER A 94  ? 2.3150 1.0762 1.1835 0.1402  -0.1372 -0.2317 390 SER A OG  
668  N N   . THR A 95  ? 2.2120 1.0139 1.1273 0.2437  -0.1194 -0.2114 391 THR A N   
669  C CA  . THR A 95  ? 2.1412 1.0606 1.1434 0.2948  -0.1057 -0.2119 391 THR A CA  
670  C C   . THR A 95  ? 2.0706 1.0223 1.1127 0.3177  -0.1013 -0.1996 391 THR A C   
671  O O   . THR A 95  ? 1.9989 1.0526 1.1116 0.3622  -0.0895 -0.1974 391 THR A O   
672  C CB  . THR A 95  ? 2.0613 1.0722 1.1442 0.2578  -0.1049 -0.2212 391 THR A CB  
673  O OG1 . THR A 95  ? 2.0789 1.0486 1.1203 0.2141  -0.1146 -0.2310 391 THR A OG1 
674  C CG2 . THR A 95  ? 1.9876 1.1121 1.1365 0.3148  -0.0889 -0.2240 391 THR A CG2 
675  N N   . SER A 96  ? 2.1225 0.9952 1.1205 0.2877  -0.1100 -0.1902 392 SER A N   
676  C CA  . SER A 96  ? 2.1076 1.0053 1.1396 0.3030  -0.1074 -0.1781 392 SER A CA  
677  C C   . SER A 96  ? 1.9857 0.9940 1.1293 0.2849  -0.1022 -0.1789 392 SER A C   
678  O O   . SER A 96  ? 1.9375 1.0136 1.1361 0.3216  -0.0949 -0.1712 392 SER A O   
679  C CB  . SER A 96  ? 2.2154 1.1268 1.2252 0.3845  -0.1006 -0.1714 392 SER A CB  
680  O OG  . SER A 96  ? 2.2101 1.2303 1.2800 0.4326  -0.0885 -0.1765 392 SER A OG  
681  N N   . THR A 97  ? 1.9016 0.9373 1.0801 0.2273  -0.1070 -0.1860 393 THR A N   
682  C CA  . THR A 97  ? 1.7109 0.8869 1.0174 0.1897  -0.1028 -0.1724 393 THR A CA  
683  C C   . THR A 97  ? 1.6826 0.8663 0.9982 0.1225  -0.1120 -0.1775 393 THR A C   
684  O O   . THR A 97  ? 1.7592 0.8424 0.9847 0.1011  -0.1218 -0.1907 393 THR A O   
685  C CB  . THR A 97  ? 1.5647 0.8704 0.9582 0.2347  -0.0888 -0.1669 393 THR A CB  
686  O OG1 . THR A 97  ? 1.4466 0.8652 0.9482 0.1989  -0.0861 -0.1529 393 THR A OG1 
687  C CG2 . THR A 97  ? 1.5944 0.9152 0.9737 0.2476  -0.0857 -0.1788 393 THR A CG2 
688  N N   . TYR A 98  ? 1.4901 0.7918 0.9092 0.0899  -0.1098 -0.1673 394 TYR A N   
689  C CA  . TYR A 98  ? 1.4564 0.7881 0.8934 0.0346  -0.1186 -0.1715 394 TYR A CA  
690  C C   . TYR A 98  ? 1.3307 0.8011 0.8796 0.0330  -0.1120 -0.1611 394 TYR A C   
691  O O   . TYR A 98  ? 1.2796 0.8142 0.8871 0.0657  -0.1012 -0.1508 394 TYR A O   
692  C CB  . TYR A 98  ? 1.4826 0.7645 0.8879 -0.0313 -0.1307 -0.1705 394 TYR A CB  
693  C CG  . TYR A 98  ? 1.4055 0.7539 0.8828 -0.0510 -0.1273 -0.1549 394 TYR A CG  
694  C CD1 . TYR A 98  ? 1.4285 0.7377 0.8912 -0.0252 -0.1221 -0.1470 394 TYR A CD1 
695  C CD2 . TYR A 98  ? 1.3310 0.7810 0.8864 -0.0921 -0.1297 -0.1484 394 TYR A CD2 
696  C CE1 . TYR A 98  ? 1.3474 0.7157 0.8725 -0.0435 -0.1190 -0.1333 394 TYR A CE1 
697  C CE2 . TYR A 98  ? 1.2459 0.7546 0.8618 -0.1066 -0.1259 -0.1353 394 TYR A CE2 
698  C CZ  . TYR A 98  ? 1.2520 0.7183 0.8525 -0.0844 -0.1204 -0.1280 394 TYR A CZ  
699  O OH  . TYR A 98  ? 1.2221 0.7463 0.8801 -0.0994 -0.1167 -0.1155 394 TYR A OH  
700  N N   . GLN A 99  ? 1.2912 0.8036 0.8621 -0.0056 -0.1197 -0.1642 395 GLN A N   
701  C CA  . GLN A 99  ? 1.2007 0.8274 0.8590 -0.0060 -0.1158 -0.1558 395 GLN A CA  
702  C C   . GLN A 99  ? 1.1255 0.8034 0.8250 -0.0576 -0.1251 -0.1506 395 GLN A C   
703  O O   . GLN A 99  ? 1.1649 0.8109 0.8240 -0.1006 -0.1374 -0.1587 395 GLN A O   
704  C CB  . GLN A 99  ? 1.1648 0.8053 0.8091 0.0077  -0.1162 -0.1645 395 GLN A CB  
705  C CG  . GLN A 99  ? 1.1678 0.7754 0.7748 0.0620  -0.1051 -0.1702 395 GLN A CG  
706  C CD  . GLN A 99  ? 1.1407 0.8211 0.8111 0.0989  -0.0901 -0.1572 395 GLN A CD  
707  O OE1 . GLN A 99  ? 1.1166 0.8772 0.8584 0.0861  -0.0877 -0.1452 395 GLN A OE1 
708  N NE2 . GLN A 99  ? 1.1770 0.8293 0.8167 0.1452  -0.0807 -0.1597 395 GLN A NE2 
709  N N   . LEU A 100 ? 1.0388 0.7990 0.8149 -0.0533 -0.1194 -0.1375 396 LEU A N   
710  C CA  . LEU A 100 ? 1.0094 0.8324 0.8290 -0.0917 -0.1264 -0.1323 396 LEU A CA  
711  C C   . LEU A 100 ? 0.9931 0.8725 0.8296 -0.1028 -0.1346 -0.1363 396 LEU A C   
712  O O   . LEU A 100 ? 0.9610 0.8612 0.8086 -0.0732 -0.1304 -0.1360 396 LEU A O   
713  C CB  . LEU A 100 ? 0.9563 0.8406 0.8429 -0.0768 -0.1178 -0.1182 396 LEU A CB  
714  C CG  . LEU A 100 ? 0.9375 0.7783 0.8135 -0.0683 -0.1113 -0.1128 396 LEU A CG  
715  C CD1 . LEU A 100 ? 0.8912 0.7922 0.8300 -0.0488 -0.1027 -0.1001 396 LEU A CD1 
716  C CD2 . LEU A 100 ? 1.0001 0.8066 0.8455 -0.1131 -0.1187 -0.1146 396 LEU A CD2 
717  N N   . LYS A 101 ? 0.9657 0.8756 0.8034 -0.1466 -0.1466 -0.1393 397 LYS A N   
718  C CA  . LYS A 101 ? 0.9462 0.9369 0.8170 -0.1534 -0.1551 -0.1396 397 LYS A CA  
719  C C   . LYS A 101 ? 0.8781 0.9430 0.8162 -0.1232 -0.1477 -0.1266 397 LYS A C   
720  O O   . LYS A 101 ? 0.8769 0.9483 0.8431 -0.1157 -0.1393 -0.1178 397 LYS A O   
721  C CB  . LYS A 101 ? 0.9571 0.9857 0.8232 -0.2071 -0.1690 -0.1442 397 LYS A CB  
722  C CG  . LYS A 101 ? 1.0572 1.0081 0.8462 -0.2475 -0.1792 -0.1576 397 LYS A CG  
723  C CD  . LYS A 101 ? 1.1247 1.0574 0.8809 -0.2346 -0.1859 -0.1679 397 LYS A CD  
724  C CE  . LYS A 101 ? 1.2125 1.0444 0.8770 -0.2685 -0.1953 -0.1827 397 LYS A CE  
725  N NZ  . LYS A 101 ? 1.2280 1.0260 0.8568 -0.2400 -0.1967 -0.1922 397 LYS A NZ  
726  N N   . ASP A 102 ? 0.8133 0.9272 0.7695 -0.1060 -0.1517 -0.1254 398 ASP A N   
727  C CA  . ASP A 102 ? 0.8156 0.9902 0.8211 -0.0793 -0.1475 -0.1136 398 ASP A CA  
728  C C   . ASP A 102 ? 0.7689 0.9946 0.8107 -0.0938 -0.1485 -0.1081 398 ASP A C   
729  O O   . ASP A 102 ? 0.7454 0.9787 0.8152 -0.0744 -0.1393 -0.0986 398 ASP A O   
730  C CB  . ASP A 102 ? 0.8482 1.0696 0.8563 -0.0672 -0.1570 -0.1143 398 ASP A CB  
731  C CG  . ASP A 102 ? 0.9249 1.1086 0.9092 -0.0405 -0.1510 -0.1140 398 ASP A CG  
732  O OD1 . ASP A 102 ? 0.9276 1.0539 0.8898 -0.0339 -0.1408 -0.1163 398 ASP A OD1 
733  O OD2 . ASP A 102 ? 0.9410 1.1564 0.9266 -0.0242 -0.1564 -0.1109 398 ASP A OD2 
734  N N   . THR A 103 ? 0.7646 1.0294 0.8040 -0.1305 -0.1597 -0.1141 399 THR A N   
735  C CA  . THR A 103 ? 0.7638 1.0911 0.8377 -0.1460 -0.1598 -0.1092 399 THR A CA  
736  C C   . THR A 103 ? 0.7945 1.0718 0.8663 -0.1540 -0.1485 -0.1046 399 THR A C   
737  O O   . THR A 103 ? 0.7541 1.0642 0.8597 -0.1403 -0.1416 -0.0963 399 THR A O   
738  C CB  . THR A 103 ? 0.7773 1.1602 0.8442 -0.1926 -0.1736 -0.1170 399 THR A CB  
739  O OG1 . THR A 103 ? 0.8390 1.1429 0.8510 -0.2310 -0.1772 -0.1263 399 THR A OG1 
740  C CG2 . THR A 103 ? 0.7355 1.1872 0.8121 -0.1788 -0.1861 -0.1202 399 THR A CG2 
741  N N   . GLU A 104 ? 0.8203 1.0137 0.8461 -0.1734 -0.1472 -0.1103 400 GLU A N   
742  C CA  . GLU A 104 ? 0.8309 0.9693 0.8466 -0.1764 -0.1377 -0.1056 400 GLU A CA  
743  C C   . GLU A 104 ? 0.7876 0.9146 0.8291 -0.1308 -0.1258 -0.0968 400 GLU A C   
744  O O   . GLU A 104 ? 0.7693 0.8946 0.8280 -0.1269 -0.1185 -0.0895 400 GLU A O   
745  C CB  . GLU A 104 ? 0.9223 0.9608 0.8700 -0.1964 -0.1400 -0.1139 400 GLU A CB  
746  C CG  . GLU A 104 ? 0.9740 1.0067 0.8824 -0.2535 -0.1522 -0.1223 400 GLU A CG  
747  C CD  . GLU A 104 ? 1.0546 0.9793 0.8818 -0.2657 -0.1576 -0.1337 400 GLU A CD  
748  O OE1 . GLU A 104 ? 1.0450 0.9084 0.8507 -0.2234 -0.1509 -0.1354 400 GLU A OE1 
749  O OE2 . GLU A 104 ? 1.1112 1.0135 0.8919 -0.3182 -0.1687 -0.1413 400 GLU A OE2 
750  N N   . LEU A 105 ? 0.7972 0.9177 0.8387 -0.0999 -0.1240 -0.0973 401 LEU A N   
751  C CA  . LEU A 105 ? 0.7773 0.8953 0.8412 -0.0643 -0.1135 -0.0885 401 LEU A CA  
752  C C   . LEU A 105 ? 0.7078 0.8843 0.8139 -0.0547 -0.1120 -0.0797 401 LEU A C   
753  O O   . LEU A 105 ? 0.6763 0.8465 0.7983 -0.0444 -0.1044 -0.0725 401 LEU A O   
754  C CB  . LEU A 105 ? 0.7685 0.8754 0.8199 -0.0405 -0.1119 -0.0903 401 LEU A CB  
755  C CG  . LEU A 105 ? 0.7338 0.8317 0.7962 -0.0113 -0.1005 -0.0823 401 LEU A CG  
756  C CD1 . LEU A 105 ? 0.7282 0.7784 0.7706 -0.0034 -0.0932 -0.0839 401 LEU A CD1 
757  C CD2 . LEU A 105 ? 0.7258 0.8316 0.7781 0.0044  -0.1000 -0.0825 401 LEU A CD2 
758  N N   . ILE A 106 ? 0.6960 0.9292 0.8158 -0.0558 -0.1201 -0.0808 402 ILE A N   
759  C CA  . ILE A 106 ? 0.6684 0.9538 0.8186 -0.0389 -0.1194 -0.0737 402 ILE A CA  
760  C C   . ILE A 106 ? 0.6350 0.9420 0.8020 -0.0572 -0.1163 -0.0718 402 ILE A C   
761  O O   . ILE A 106 ? 0.6223 0.9374 0.8063 -0.0406 -0.1101 -0.0650 402 ILE A O   
762  C CB  . ILE A 106 ? 0.6193 0.9647 0.7747 -0.0301 -0.1302 -0.0762 402 ILE A CB  
763  C CG1 . ILE A 106 ? 0.6295 0.9468 0.7629 -0.0117 -0.1324 -0.0767 402 ILE A CG1 
764  C CG2 . ILE A 106 ? 0.6005 0.9959 0.7780 -0.0042 -0.1299 -0.0698 402 ILE A CG2 
765  C CD1 . ILE A 106 ? 0.6254 0.9946 0.7555 -0.0032 -0.1451 -0.0799 402 ILE A CD1 
766  N N   . TYR A 107 ? 0.6592 0.9730 0.8158 -0.0945 -0.1208 -0.0777 403 TYR A N   
767  C CA  . TYR A 107 ? 0.6398 0.9673 0.8050 -0.1181 -0.1167 -0.0751 403 TYR A CA  
768  C C   . TYR A 107 ? 0.6808 0.9417 0.8372 -0.1090 -0.1069 -0.0697 403 TYR A C   
769  O O   . TYR A 107 ? 0.6137 0.8897 0.7890 -0.1008 -0.1005 -0.0633 403 TYR A O   
770  C CB  . TYR A 107 ? 0.6816 1.0114 0.8230 -0.1683 -0.1237 -0.0819 403 TYR A CB  
771  C CG  . TYR A 107 ? 0.7417 1.0723 0.8808 -0.2000 -0.1185 -0.0781 403 TYR A CG  
772  C CD1 . TYR A 107 ? 0.7816 1.0256 0.8904 -0.2055 -0.1123 -0.0753 403 TYR A CD1 
773  C CD2 . TYR A 107 ? 0.7325 1.1544 0.8971 -0.2224 -0.1196 -0.0769 403 TYR A CD2 
774  C CE1 . TYR A 107 ? 0.7935 1.0309 0.8935 -0.2343 -0.1077 -0.0708 403 TYR A CE1 
775  C CE2 . TYR A 107 ? 0.7428 1.1667 0.9021 -0.2546 -0.1136 -0.0726 403 TYR A CE2 
776  C CZ  . TYR A 107 ? 0.7946 1.1204 0.9195 -0.2614 -0.1077 -0.0692 403 TYR A CZ  
777  O OH  . TYR A 107 ? 0.8131 1.1332 0.9261 -0.2932 -0.1018 -0.0637 403 TYR A OH  
778  N N   . GLY A 108 ? 0.7226 0.9122 0.8474 -0.1083 -0.1061 -0.0727 404 GLY A N   
779  C CA  . GLY A 108 ? 0.7262 0.8604 0.8410 -0.0956 -0.0982 -0.0679 404 GLY A CA  
780  C C   . GLY A 108 ? 0.6825 0.8365 0.8275 -0.0648 -0.0917 -0.0599 404 GLY A C   
781  O O   . GLY A 108 ? 0.6250 0.7742 0.7791 -0.0627 -0.0866 -0.0541 404 GLY A O   
782  N N   . ALA A 109 ? 0.6370 0.8092 0.7917 -0.0432 -0.0926 -0.0593 405 ALA A N   
783  C CA  . ALA A 109 ? 0.6191 0.7958 0.7893 -0.0195 -0.0873 -0.0516 405 ALA A CA  
784  C C   . ALA A 109 ? 0.5763 0.7892 0.7658 -0.0165 -0.0866 -0.0476 405 ALA A C   
785  O O   . ALA A 109 ? 0.5782 0.7794 0.7731 -0.0082 -0.0815 -0.0419 405 ALA A O   
786  C CB  . ALA A 109 ? 0.5688 0.7493 0.7340 -0.0020 -0.0888 -0.0511 405 ALA A CB  
787  N N   . LYS A 110 ? 0.5721 0.8341 0.7704 -0.0214 -0.0918 -0.0508 406 LYS A N   
788  C CA  . LYS A 110 ? 0.5455 0.8499 0.7597 -0.0111 -0.0903 -0.0478 406 LYS A CA  
789  C C   . LYS A 110 ? 0.5693 0.8694 0.7889 -0.0290 -0.0845 -0.0456 406 LYS A C   
790  O O   . LYS A 110 ? 0.5468 0.8537 0.7730 -0.0153 -0.0799 -0.0414 406 LYS A O   
791  C CB  . LYS A 110 ? 0.5514 0.9262 0.7760 -0.0111 -0.0973 -0.0523 406 LYS A CB  
792  C CG  . LYS A 110 ? 0.5719 0.9568 0.7889 0.0203  -0.1031 -0.0520 406 LYS A CG  
793  C CD  . LYS A 110 ? 0.5378 1.0032 0.7661 0.0227  -0.1116 -0.0567 406 LYS A CD  
794  C CE  . LYS A 110 ? 0.5722 1.0386 0.7850 0.0509  -0.1196 -0.0569 406 LYS A CE  
795  N NZ  . LYS A 110 ? 0.5960 1.1513 0.8205 0.0707  -0.1274 -0.0594 406 LYS A NZ  
796  N N   . HIS A 111 ? 0.5717 0.8516 0.7804 -0.0593 -0.0850 -0.0483 407 HIS A N   
797  C CA  . HIS A 111 ? 0.5834 0.8517 0.7884 -0.0794 -0.0801 -0.0453 407 HIS A CA  
798  C C   . HIS A 111 ? 0.6190 0.8279 0.8136 -0.0676 -0.0754 -0.0404 407 HIS A C   
799  O O   . HIS A 111 ? 0.5902 0.7942 0.7859 -0.0712 -0.0707 -0.0358 407 HIS A O   
800  C CB  . HIS A 111 ? 0.5909 0.8525 0.7758 -0.1196 -0.0837 -0.0495 407 HIS A CB  
801  C CG  . HIS A 111 ? 0.6164 0.9592 0.8177 -0.1407 -0.0865 -0.0522 407 HIS A CG  
802  N ND1 . HIS A 111 ? 0.5874 0.9837 0.8014 -0.1335 -0.0938 -0.0572 407 HIS A ND1 
803  C CD2 . HIS A 111 ? 0.6015 0.9930 0.8105 -0.1665 -0.0828 -0.0500 407 HIS A CD2 
804  C CE1 . HIS A 111 ? 0.5819 1.0619 0.8125 -0.1537 -0.0953 -0.0586 407 HIS A CE1 
805  N NE2 . HIS A 111 ? 0.6106 1.0914 0.8392 -0.1757 -0.0879 -0.0542 407 HIS A NE2 
806  N N   . ALA A 112 ? 0.5695 0.7411 0.7544 -0.0529 -0.0765 -0.0411 408 ALA A N   
807  C CA  . ALA A 112 ? 0.5923 0.7307 0.7747 -0.0371 -0.0726 -0.0360 408 ALA A CA  
808  C C   . ALA A 112 ? 0.6083 0.7680 0.8071 -0.0226 -0.0697 -0.0309 408 ALA A C   
809  O O   . ALA A 112 ? 0.5985 0.7450 0.7969 -0.0213 -0.0667 -0.0264 408 ALA A O   
810  C CB  . ALA A 112 ? 0.5989 0.7155 0.7727 -0.0225 -0.0732 -0.0376 408 ALA A CB  
811  N N   . TRP A 113 ? 0.5697 0.7562 0.7756 -0.0100 -0.0715 -0.0318 409 TRP A N   
812  C CA  . TRP A 113 ? 0.5486 0.7428 0.7560 0.0057  -0.0697 -0.0282 409 TRP A CA  
813  C C   . TRP A 113 ? 0.5717 0.7946 0.7867 0.0004  -0.0667 -0.0283 409 TRP A C   
814  O O   . TRP A 113 ? 0.5262 0.7366 0.7376 0.0048  -0.0633 -0.0249 409 TRP A O   
815  C CB  . TRP A 113 ? 0.5838 0.7905 0.7849 0.0249  -0.0733 -0.0293 409 TRP A CB  
816  C CG  . TRP A 113 ? 0.5861 0.7824 0.7720 0.0460  -0.0727 -0.0264 409 TRP A CG  
817  C CD1 . TRP A 113 ? 0.6348 0.8090 0.8128 0.0467  -0.0694 -0.0232 409 TRP A CD1 
818  C CD2 . TRP A 113 ? 0.6272 0.8250 0.7940 0.0714  -0.0766 -0.0267 409 TRP A CD2 
819  N NE1 . TRP A 113 ? 0.6374 0.7936 0.7886 0.0699  -0.0707 -0.0224 409 TRP A NE1 
820  C CE2 . TRP A 113 ? 0.6388 0.8068 0.7808 0.0875  -0.0751 -0.0242 409 TRP A CE2 
821  C CE3 . TRP A 113 ? 0.5946 0.8121 0.7569 0.0841  -0.0820 -0.0291 409 TRP A CE3 
822  C CZ2 . TRP A 113 ? 0.6663 0.8143 0.7727 0.1183  -0.0788 -0.0239 409 TRP A CZ2 
823  C CZ3 . TRP A 113 ? 0.6421 0.8478 0.7744 0.1157  -0.0859 -0.0280 409 TRP A CZ3 
824  C CH2 . TRP A 113 ? 0.7032 0.8703 0.8048 0.1340  -0.0841 -0.0255 409 TRP A CH2 
825  N N   . ARG A 114 ? 0.5444 0.8108 0.7687 -0.0115 -0.0680 -0.0322 410 ARG A N   
826  C CA  . ARG A 114 ? 0.5383 0.8458 0.7709 -0.0213 -0.0637 -0.0319 410 ARG A CA  
827  C C   . ARG A 114 ? 0.5624 0.8347 0.7868 -0.0375 -0.0589 -0.0275 410 ARG A C   
828  O O   . ARG A 114 ? 0.5030 0.7909 0.7288 -0.0340 -0.0537 -0.0251 410 ARG A O   
829  C CB  . ARG A 114 ? 0.5331 0.8930 0.7745 -0.0454 -0.0663 -0.0362 410 ARG A CB  
830  C CG  . ARG A 114 ? 0.5491 0.9797 0.8038 -0.0529 -0.0617 -0.0363 410 ARG A CG  
831  C CD  . ARG A 114 ? 0.5306 1.0175 0.7921 -0.0873 -0.0654 -0.0402 410 ARG A CD  
832  N NE  . ARG A 114 ? 0.5173 1.0924 0.7954 -0.0962 -0.0600 -0.0399 410 ARG A NE  
833  C CZ  . ARG A 114 ? 0.5163 1.1724 0.8066 -0.1245 -0.0628 -0.0431 410 ARG A CZ  
834  N NH1 . ARG A 114 ? 0.5376 1.1888 0.8213 -0.1489 -0.0721 -0.0474 410 ARG A NH1 
835  N NH2 . ARG A 114 ? 0.4821 1.2212 0.7853 -0.1272 -0.0554 -0.0418 410 ARG A NH2 
836  N N   . ASN A 115 ? 0.5615 0.7849 0.7732 -0.0506 -0.0608 -0.0264 411 ASN A N   
837  C CA  . ASN A 115 ? 0.5804 0.7659 0.7770 -0.0636 -0.0581 -0.0220 411 ASN A CA  
838  C C   . ASN A 115 ? 0.5953 0.7498 0.7893 -0.0443 -0.0575 -0.0176 411 ASN A C   
839  O O   . ASN A 115 ? 0.5870 0.7128 0.7679 -0.0497 -0.0563 -0.0133 411 ASN A O   
840  C CB  . ASN A 115 ? 0.6057 0.7489 0.7789 -0.0823 -0.0615 -0.0236 411 ASN A CB  
841  C CG  . ASN A 115 ? 0.6250 0.7932 0.7916 -0.1139 -0.0628 -0.0272 411 ASN A CG  
842  O OD1 . ASN A 115 ? 0.6061 0.8314 0.7885 -0.1248 -0.0594 -0.0269 411 ASN A OD1 
843  N ND2 . ASN A 115 ? 0.6577 0.7870 0.7980 -0.1295 -0.0677 -0.0312 411 ASN A ND2 
844  N N   . ALA A 116 ? 0.5533 0.7118 0.7548 -0.0244 -0.0590 -0.0181 412 ALA A N   
845  C CA  . ALA A 116 ? 0.5574 0.6918 0.7543 -0.0133 -0.0598 -0.0142 412 ALA A CA  
846  C C   . ALA A 116 ? 0.5551 0.6924 0.7475 -0.0109 -0.0569 -0.0117 412 ALA A C   
847  O O   . ALA A 116 ? 0.5437 0.6915 0.7327 0.0013  -0.0560 -0.0133 412 ALA A O   
848  C CB  . ALA A 116 ? 0.5704 0.7034 0.7670 -0.0010 -0.0622 -0.0150 412 ALA A CB  
849  N N   . SER A 117 ? 0.5671 0.6897 0.7527 -0.0197 -0.0558 -0.0080 413 SER A N   
850  C CA  . SER A 117 ? 0.5565 0.6839 0.7354 -0.0192 -0.0522 -0.0061 413 SER A CA  
851  C C   . SER A 117 ? 0.5747 0.6878 0.7442 -0.0069 -0.0547 -0.0055 413 SER A C   
852  O O   . SER A 117 ? 0.5633 0.6787 0.7218 -0.0009 -0.0518 -0.0062 413 SER A O   
853  C CB  . SER A 117 ? 0.5732 0.6810 0.7401 -0.0320 -0.0513 -0.0012 413 SER A CB  
854  O OG  . SER A 117 ? 0.5887 0.6694 0.7495 -0.0265 -0.0569 0.0019  413 SER A OG  
855  N N   . ARG A 118 ? 0.5683 0.6670 0.7372 -0.0048 -0.0597 -0.0046 414 ARG A N   
856  C CA  . ARG A 118 ? 0.5768 0.6570 0.7291 -0.0028 -0.0633 -0.0036 414 ARG A CA  
857  C C   . ARG A 118 ? 0.6184 0.6866 0.7544 0.0071  -0.0638 -0.0068 414 ARG A C   
858  O O   . ARG A 118 ? 0.6050 0.6437 0.7140 0.0054  -0.0673 -0.0062 414 ARG A O   
859  C CB  . ARG A 118 ? 0.6120 0.6909 0.7684 -0.0108 -0.0684 0.0002  414 ARG A CB  
860  C CG  . ARG A 118 ? 0.6298 0.7138 0.7914 -0.0127 -0.0701 0.0039  414 ARG A CG  
861  C CD  . ARG A 118 ? 0.6517 0.7507 0.8189 -0.0147 -0.0756 0.0071  414 ARG A CD  
862  N NE  . ARG A 118 ? 0.6437 0.7480 0.8071 -0.0128 -0.0799 0.0113  414 ARG A NE  
863  C CZ  . ARG A 118 ? 0.7239 0.8548 0.8944 -0.0082 -0.0850 0.0144  414 ARG A CZ  
864  N NH1 . ARG A 118 ? 0.7284 0.8852 0.9113 -0.0073 -0.0849 0.0138  414 ARG A NH1 
865  N NH2 . ARG A 118 ? 0.7284 0.8652 0.8922 -0.0023 -0.0903 0.0183  414 ARG A NH2 
866  N N   . CYS A 119 ? 0.5673 0.6536 0.7124 0.0169  -0.0613 -0.0100 415 CYS A N   
867  C CA  . CYS A 119 ? 0.6074 0.6801 0.7326 0.0320  -0.0630 -0.0125 415 CYS A CA  
868  C C   . CYS A 119 ? 0.6183 0.6999 0.7289 0.0539  -0.0597 -0.0165 415 CYS A C   
869  O O   . CYS A 119 ? 0.5798 0.7069 0.7126 0.0570  -0.0552 -0.0186 415 CYS A O   
870  C CB  . CYS A 119 ? 0.5880 0.6808 0.7298 0.0336  -0.0639 -0.0137 415 CYS A CB  
871  S SG  . CYS A 119 ? 0.5714 0.6506 0.6846 0.0591  -0.0667 -0.0162 415 CYS A SG  
872  N N   . VAL A 120 ? 0.6687 0.7067 0.7366 0.0688  -0.0620 -0.0177 416 VAL A N   
873  C CA  . VAL A 120 ? 0.6779 0.7201 0.7222 0.0992  -0.0587 -0.0225 416 VAL A CA  
874  C C   . VAL A 120 ? 0.6763 0.7331 0.7110 0.1290  -0.0600 -0.0257 416 VAL A C   
875  O O   . VAL A 120 ? 0.6664 0.7465 0.6875 0.1618  -0.0569 -0.0303 416 VAL A O   
876  C CB  . VAL A 120 ? 0.7080 0.6827 0.6970 0.1048  -0.0615 -0.0235 416 VAL A CB  
877  C CG1 . VAL A 120 ? 0.7588 0.6639 0.6975 0.1063  -0.0689 -0.0221 416 VAL A CG1 
878  C CG2 . VAL A 120 ? 0.7342 0.7169 0.6988 0.1383  -0.0562 -0.0293 416 VAL A CG2 
879  N N   . GLY A 121 ? 0.6912 0.7422 0.7328 0.1215  -0.0644 -0.0234 417 GLY A N   
880  C CA  . GLY A 121 ? 0.7082 0.7654 0.7332 0.1513  -0.0677 -0.0256 417 GLY A CA  
881  C C   . GLY A 121 ? 0.7018 0.8402 0.7747 0.1520  -0.0663 -0.0279 417 GLY A C   
882  O O   . GLY A 121 ? 0.7077 0.8596 0.7737 0.1719  -0.0707 -0.0292 417 GLY A O   
883  N N   . ARG A 122 ? 0.6203 0.8104 0.7355 0.1292  -0.0611 -0.0284 418 ARG A N   
884  C CA  . ARG A 122 ? 0.6550 0.9098 0.8103 0.1143  -0.0612 -0.0300 418 ARG A CA  
885  C C   . ARG A 122 ? 0.6643 0.9937 0.8288 0.1402  -0.0609 -0.0346 418 ARG A C   
886  O O   . ARG A 122 ? 0.6197 1.0086 0.8145 0.1239  -0.0623 -0.0364 418 ARG A O   
887  C CB  . ARG A 122 ? 0.5947 0.8683 0.7789 0.0784  -0.0565 -0.0284 418 ARG A CB  
888  C CG  . ARG A 122 ? 0.5812 0.8023 0.7645 0.0550  -0.0582 -0.0243 418 ARG A CG  
889  C CD  . ARG A 122 ? 0.5535 0.7857 0.7538 0.0273  -0.0545 -0.0226 418 ARG A CD  
890  N NE  . ARG A 122 ? 0.5730 0.7952 0.7642 0.0279  -0.0499 -0.0204 418 ARG A NE  
891  C CZ  . ARG A 122 ? 0.5432 0.7763 0.7408 0.0078  -0.0455 -0.0180 418 ARG A CZ  
892  N NH1 . ARG A 122 ? 0.5223 0.7745 0.7312 -0.0163 -0.0451 -0.0180 418 ARG A NH1 
893  N NH2 . ARG A 122 ? 0.5580 0.7755 0.7431 0.0100  -0.0421 -0.0156 418 ARG A NH2 
894  N N   . ILE A 123 ? 0.6605 0.9909 0.7962 0.1809  -0.0597 -0.0371 419 ILE A N   
895  C CA  . ILE A 123 ? 0.6377 1.0525 0.7828 0.2128  -0.0600 -0.0416 419 ILE A CA  
896  C C   . ILE A 123 ? 0.6973 1.1247 0.8434 0.2226  -0.0694 -0.0422 419 ILE A C   
897  O O   . ILE A 123 ? 0.6066 1.1233 0.7751 0.2351  -0.0718 -0.0456 419 ILE A O   
898  C CB  . ILE A 123 ? 0.7190 1.1212 0.8209 0.2660  -0.0576 -0.0449 419 ILE A CB  
899  C CG1 . ILE A 123 ? 0.6784 1.1963 0.7996 0.3001  -0.0556 -0.0499 419 ILE A CG1 
900  C CG2 . ILE A 123 ? 0.7882 1.0890 0.8280 0.2965  -0.0655 -0.0436 419 ILE A CG2 
901  C CD1 . ILE A 123 ? 0.7577 1.2835 0.8419 0.3541  -0.0500 -0.0543 419 ILE A CD1 
902  N N   . GLN A 124 ? 0.7439 1.0899 0.8665 0.2143  -0.0748 -0.0386 420 GLN A N   
903  C CA  . GLN A 124 ? 0.7541 1.0938 0.8674 0.2236  -0.0834 -0.0381 420 GLN A CA  
904  C C   . GLN A 124 ? 0.7091 1.0729 0.8611 0.1800  -0.0851 -0.0380 420 GLN A C   
905  O O   . GLN A 124 ? 0.6833 1.0359 0.8271 0.1825  -0.0918 -0.0375 420 GLN A O   
906  C CB  . GLN A 124 ? 0.8455 1.0782 0.9023 0.2362  -0.0871 -0.0334 420 GLN A CB  
907  C CG  . GLN A 124 ? 0.9814 1.1695 0.9769 0.2878  -0.0894 -0.0342 420 GLN A CG  
908  C CD  . GLN A 124 ? 1.0322 1.2312 0.9985 0.3315  -0.0983 -0.0348 420 GLN A CD  
909  O OE1 . GLN A 124 ? 1.0350 1.2887 1.0339 0.3216  -0.1029 -0.0353 420 GLN A OE1 
910  N NE2 . GLN A 124 ? 1.1471 1.2884 1.0444 0.3824  -0.1018 -0.0351 420 GLN A NE2 
911  N N   . TRP A 125 ? 0.6227 1.0121 0.8086 0.1418  -0.0794 -0.0385 421 TRP A N   
912  C CA  . TRP A 125 ? 0.6050 0.9786 0.8086 0.1020  -0.0805 -0.0380 421 TRP A CA  
913  C C   . TRP A 125 ? 0.5795 1.0005 0.7955 0.0967  -0.0880 -0.0420 421 TRP A C   
914  O O   . TRP A 125 ? 0.5935 0.9821 0.8068 0.0790  -0.0910 -0.0420 421 TRP A O   
915  C CB  . TRP A 125 ? 0.5595 0.9449 0.7846 0.0668  -0.0740 -0.0377 421 TRP A CB  
916  C CG  . TRP A 125 ? 0.5571 1.0280 0.8056 0.0542  -0.0731 -0.0412 421 TRP A CG  
917  C CD1 . TRP A 125 ? 0.5359 1.0634 0.7918 0.0676  -0.0677 -0.0419 421 TRP A CD1 
918  C CD2 . TRP A 125 ? 0.5554 1.0715 0.8198 0.0232  -0.0777 -0.0448 421 TRP A CD2 
919  N NE1 . TRP A 125 ? 0.4889 1.1038 0.7690 0.0439  -0.0680 -0.0448 421 TRP A NE1 
920  C CE2 . TRP A 125 ? 0.5328 1.1387 0.8164 0.0137  -0.0750 -0.0467 421 TRP A CE2 
921  C CE3 . TRP A 125 ? 0.5046 0.9937 0.7648 0.0010  -0.0839 -0.0471 421 TRP A CE3 
922  C CZ2 . TRP A 125 ? 0.4577 1.1274 0.7559 -0.0235 -0.0792 -0.0503 421 TRP A CZ2 
923  C CZ3 . TRP A 125 ? 0.5222 1.0633 0.7921 -0.0323 -0.0885 -0.0515 421 TRP A CZ3 
924  C CH2 . TRP A 125 ? 0.4878 1.1181 0.7763 -0.0474 -0.0867 -0.0528 421 TRP A CH2 
925  N N   . SER A 126 ? 0.5618 1.0651 0.7905 0.1122  -0.0913 -0.0457 422 SER A N   
926  C CA  . SER A 126 ? 0.5581 1.1156 0.7983 0.1049  -0.1003 -0.0498 422 SER A CA  
927  C C   . SER A 126 ? 0.5994 1.1284 0.8119 0.1410  -0.1084 -0.0487 422 SER A C   
928  O O   . SER A 126 ? 0.6134 1.1635 0.8287 0.1322  -0.1165 -0.0515 422 SER A O   
929  C CB  . SER A 126 ? 0.5149 1.1881 0.7814 0.1058  -0.1016 -0.0539 422 SER A CB  
930  O OG  . SER A 126 ? 0.5715 1.2595 0.8158 0.1569  -0.0997 -0.0528 422 SER A OG  
931  N N   . LYS A 127 ? 0.6452 1.1209 0.8236 0.1799  -0.1071 -0.0447 423 LYS A N   
932  C CA  . LYS A 127 ? 0.6805 1.1053 0.8188 0.2097  -0.1142 -0.0416 423 LYS A CA  
933  C C   . LYS A 127 ? 0.6858 1.0173 0.8060 0.1846  -0.1099 -0.0365 423 LYS A C   
934  O O   . LYS A 127 ? 0.7087 0.9699 0.7968 0.1928  -0.1059 -0.0315 423 LYS A O   
935  C CB  . LYS A 127 ? 0.7442 1.1535 0.8412 0.2656  -0.1163 -0.0399 423 LYS A CB  
936  C CG  . LYS A 127 ? 0.7589 1.2681 0.8692 0.2962  -0.1191 -0.0449 423 LYS A CG  
937  C CD  . LYS A 127 ? 0.9155 1.3940 0.9700 0.3447  -0.1245 -0.0435 423 LYS A CD  
938  C CE  . LYS A 127 ? 0.9078 1.4605 0.9787 0.3402  -0.1293 -0.0472 423 LYS A CE  
939  N NZ  . LYS A 127 ? 0.9881 1.4927 1.0329 0.3457  -0.1404 -0.0437 423 LYS A NZ  
940  N N   . LEU A 128 ? 0.6554 0.9905 0.7946 0.1518  -0.1107 -0.0383 424 LEU A N   
941  C CA  . LEU A 128 ? 0.6659 0.9333 0.7928 0.1301  -0.1063 -0.0343 424 LEU A CA  
942  C C   . LEU A 128 ? 0.6476 0.9153 0.7654 0.1274  -0.1123 -0.0355 424 LEU A C   
943  O O   . LEU A 128 ? 0.6298 0.9505 0.7681 0.1172  -0.1178 -0.0419 424 LEU A O   
944  C CB  . LEU A 128 ? 0.6076 0.8727 0.7629 0.0949  -0.0990 -0.0359 424 LEU A CB  
945  C CG  . LEU A 128 ? 0.6053 0.8191 0.7538 0.0756  -0.0939 -0.0328 424 LEU A CG  
946  C CD1 . LEU A 128 ? 0.6495 0.8106 0.7712 0.0831  -0.0901 -0.0252 424 LEU A CD1 
947  C CD2 . LEU A 128 ? 0.5610 0.7782 0.7327 0.0491  -0.0891 -0.0356 424 LEU A CD2 
948  N N   . GLN A 129 ? 0.6434 0.8528 0.7265 0.1334  -0.1116 -0.0295 425 GLN A N   
949  C CA  . GLN A 129 ? 0.6683 0.8735 0.7375 0.1316  -0.1161 -0.0299 425 GLN A CA  
950  C C   . GLN A 129 ? 0.6609 0.8479 0.7435 0.1002  -0.1086 -0.0311 425 GLN A C   
951  O O   . GLN A 129 ? 0.6426 0.7898 0.7165 0.0900  -0.1006 -0.0255 425 GLN A O   
952  C CB  . GLN A 129 ? 0.7470 0.8986 0.7629 0.1553  -0.1192 -0.0217 425 GLN A CB  
953  C CG  . GLN A 129 ? 0.7242 0.8719 0.7224 0.1539  -0.1235 -0.0214 425 GLN A CG  
954  C CD  . GLN A 129 ? 0.7593 0.9755 0.7777 0.1638  -0.1344 -0.0297 425 GLN A CD  
955  O OE1 . GLN A 129 ? 0.7867 1.0485 0.8128 0.1877  -0.1416 -0.0323 425 GLN A OE1 
956  N NE2 . GLN A 129 ? 0.7696 0.9979 0.7945 0.1452  -0.1360 -0.0345 425 GLN A NE2 
957  N N   . VAL A 130 ? 0.6395 0.8573 0.7396 0.0855  -0.1116 -0.0390 426 VAL A N   
958  C CA  . VAL A 130 ? 0.6350 0.8348 0.7419 0.0632  -0.1050 -0.0421 426 VAL A CA  
959  C C   . VAL A 130 ? 0.6545 0.8376 0.7364 0.0664  -0.1058 -0.0417 426 VAL A C   
960  O O   . VAL A 130 ? 0.6287 0.8329 0.7017 0.0724  -0.1148 -0.0460 426 VAL A O   
961  C CB  . VAL A 130 ? 0.6314 0.8575 0.7590 0.0429  -0.1077 -0.0516 426 VAL A CB  
962  C CG1 . VAL A 130 ? 0.6255 0.8188 0.7483 0.0286  -0.1008 -0.0549 426 VAL A CG1 
963  C CG2 . VAL A 130 ? 0.5888 0.8381 0.7387 0.0389  -0.1067 -0.0508 426 VAL A CG2 
964  N N   . PHE A 131 ? 0.6658 0.8178 0.7357 0.0619  -0.0964 -0.0362 427 PHE A N   
965  C CA  . PHE A 131 ? 0.6826 0.8218 0.7280 0.0626  -0.0941 -0.0353 427 PHE A CA  
966  C C   . PHE A 131 ? 0.6533 0.7947 0.7076 0.0521  -0.0880 -0.0431 427 PHE A C   
967  O O   . PHE A 131 ? 0.6362 0.7731 0.7032 0.0466  -0.0794 -0.0415 427 PHE A O   
968  C CB  . PHE A 131 ? 0.6833 0.7926 0.7031 0.0622  -0.0869 -0.0231 427 PHE A CB  
969  C CG  . PHE A 131 ? 0.7128 0.7992 0.7030 0.0773  -0.0941 -0.0156 427 PHE A CG  
970  C CD1 . PHE A 131 ? 0.7391 0.8257 0.7036 0.0940  -0.1034 -0.0160 427 PHE A CD1 
971  C CD2 . PHE A 131 ? 0.6959 0.7560 0.6769 0.0778  -0.0924 -0.0086 427 PHE A CD2 
972  C CE1 . PHE A 131 ? 0.7772 0.8366 0.7054 0.1161  -0.1109 -0.0090 427 PHE A CE1 
973  C CE2 . PHE A 131 ? 0.7508 0.7771 0.6920 0.0976  -0.0994 -0.0024 427 PHE A CE2 
974  C CZ  . PHE A 131 ? 0.7835 0.8085 0.6971 0.1192  -0.1087 -0.0024 427 PHE A CZ  
975  N N   . ASP A 132 ? 0.6706 0.8173 0.7135 0.0518  -0.0935 -0.0521 428 ASP A N   
976  C CA  . ASP A 132 ? 0.6621 0.7983 0.6994 0.0467  -0.0895 -0.0617 428 ASP A CA  
977  C C   . ASP A 132 ? 0.6810 0.8101 0.6990 0.0542  -0.0790 -0.0582 428 ASP A C   
978  O O   . ASP A 132 ? 0.7230 0.8514 0.7179 0.0585  -0.0813 -0.0583 428 ASP A O   
979  C CB  . ASP A 132 ? 0.6447 0.7840 0.6697 0.0388  -0.1013 -0.0737 428 ASP A CB  
980  C CG  . ASP A 132 ? 0.7216 0.8313 0.7254 0.0345  -0.0985 -0.0849 428 ASP A CG  
981  O OD1 . ASP A 132 ? 0.7257 0.8201 0.7259 0.0451  -0.0869 -0.0833 428 ASP A OD1 
982  O OD2 . ASP A 132 ? 0.8090 0.9101 0.7943 0.0212  -0.1086 -0.0957 428 ASP A OD2 
983  N N   . ALA A 133 ? 0.6814 0.8123 0.7087 0.0559  -0.0674 -0.0546 429 ALA A N   
984  C CA  . ALA A 133 ? 0.6514 0.7923 0.6647 0.0619  -0.0552 -0.0515 429 ALA A CA  
985  C C   . ALA A 133 ? 0.6815 0.8182 0.6862 0.0751  -0.0497 -0.0625 429 ALA A C   
986  O O   . ALA A 133 ? 0.6748 0.8335 0.6788 0.0851  -0.0375 -0.0603 429 ALA A O   
987  C CB  . ALA A 133 ? 0.6790 0.8376 0.7056 0.0536  -0.0461 -0.0381 429 ALA A CB  
988  N N   . ARG A 134 ? 0.6750 0.7834 0.6676 0.0756  -0.0588 -0.0745 430 ARG A N   
989  C CA  . ARG A 134 ? 0.7296 0.8144 0.6979 0.0915  -0.0549 -0.0858 430 ARG A CA  
990  C C   . ARG A 134 ? 0.7546 0.8375 0.6884 0.1068  -0.0492 -0.0925 430 ARG A C   
991  O O   . ARG A 134 ? 0.7920 0.8561 0.6990 0.1284  -0.0437 -0.1016 430 ARG A O   
992  C CB  . ARG A 134 ? 0.7554 0.7972 0.7080 0.0807  -0.0670 -0.0963 430 ARG A CB  
993  C CG  . ARG A 134 ? 0.7521 0.7932 0.7325 0.0707  -0.0690 -0.0908 430 ARG A CG  
994  C CD  . ARG A 134 ? 0.7826 0.7840 0.7435 0.0516  -0.0804 -0.0997 430 ARG A CD  
995  N NE  . ARG A 134 ? 0.8121 0.8291 0.7747 0.0303  -0.0917 -0.1023 430 ARG A NE  
996  C CZ  . ARG A 134 ? 0.8426 0.8387 0.7848 0.0057  -0.1032 -0.1109 430 ARG A CZ  
997  N NH1 . ARG A 134 ? 0.8789 0.8223 0.7898 -0.0039 -0.1050 -0.1174 430 ARG A NH1 
998  N NH2 . ARG A 134 ? 0.8206 0.8493 0.7693 -0.0107 -0.1139 -0.1128 430 ARG A NH2 
999  N N   . ASP A 135 ? 0.7401 0.8393 0.6682 0.1000  -0.0500 -0.0879 431 ASP A N   
1000 C CA  . ASP A 135 ? 0.7832 0.8864 0.6784 0.1147  -0.0422 -0.0927 431 ASP A CA  
1001 C C   . ASP A 135 ? 0.8007 0.9522 0.7084 0.1224  -0.0248 -0.0817 431 ASP A C   
1002 O O   . ASP A 135 ? 0.8035 0.9707 0.6867 0.1339  -0.0152 -0.0836 431 ASP A O   
1003 C CB  . ASP A 135 ? 0.7975 0.8937 0.6721 0.1043  -0.0518 -0.0934 431 ASP A CB  
1004 C CG  . ASP A 135 ? 0.8076 0.9249 0.7032 0.0897  -0.0547 -0.0775 431 ASP A CG  
1005 O OD1 . ASP A 135 ? 0.7808 0.9176 0.7014 0.0846  -0.0467 -0.0656 431 ASP A OD1 
1006 O OD2 . ASP A 135 ? 0.8443 0.9549 0.7260 0.0842  -0.0663 -0.0774 431 ASP A OD2 
1007 N N   . CYS A 136 ? 0.7237 0.9024 0.6666 0.1132  -0.0205 -0.0703 432 CYS A N   
1008 C CA  . CYS A 136 ? 0.7446 0.9770 0.6997 0.1104  -0.0052 -0.0586 432 CYS A CA  
1009 C C   . CYS A 136 ? 0.7749 1.0402 0.7237 0.1401  0.0076  -0.0661 432 CYS A C   
1010 O O   . CYS A 136 ? 0.7691 1.0089 0.7113 0.1627  0.0041  -0.0772 432 CYS A O   
1011 C CB  . CYS A 136 ? 0.7028 0.9509 0.6918 0.0899  -0.0064 -0.0459 432 CYS A CB  
1012 S SG  . CYS A 136 ? 0.6743 0.9830 0.6699 0.0678  0.0089  -0.0287 432 CYS A SG  
1013 N N   . THR A 137 ? 0.8053 1.1264 0.7495 0.1416  0.0229  -0.0599 433 THR A N   
1014 C CA  . THR A 137 ? 0.7518 1.1199 0.6883 0.1762  0.0369  -0.0671 433 THR A CA  
1015 C C   . THR A 137 ? 0.7413 1.2042 0.7054 0.1671  0.0528  -0.0541 433 THR A C   
1016 O O   . THR A 137 ? 0.7469 1.2645 0.7156 0.1998  0.0631  -0.0592 433 THR A O   
1017 C CB  . THR A 137 ? 0.8457 1.2000 0.7374 0.1970  0.0422  -0.0778 433 THR A CB  
1018 O OG1 . THR A 137 ? 0.8098 1.1894 0.6958 0.1688  0.0483  -0.0659 433 THR A OG1 
1019 C CG2 . THR A 137 ? 0.8606 1.1253 0.7191 0.2034  0.0255  -0.0925 433 THR A CG2 
1020 N N   . THR A 138 ? 0.7320 1.2163 0.7084 0.1243  0.0547  -0.0379 434 THR A N   
1021 C CA  . THR A 138 ? 0.7179 1.2936 0.7132 0.1031  0.0696  -0.0245 434 THR A CA  
1022 C C   . THR A 138 ? 0.7117 1.2796 0.7292 0.0604  0.0621  -0.0104 434 THR A C   
1023 O O   . THR A 138 ? 0.6968 1.1887 0.7104 0.0484  0.0473  -0.0099 434 THR A O   
1024 C CB  . THR A 138 ? 0.7405 1.3476 0.7080 0.0848  0.0827  -0.0170 434 THR A CB  
1025 O OG1 . THR A 138 ? 0.7979 1.3287 0.7394 0.0551  0.0721  -0.0101 434 THR A OG1 
1026 C CG2 . THR A 138 ? 0.7768 1.3975 0.7186 0.1292  0.0918  -0.0316 434 THR A CG2 
1027 N N   . ALA A 139 ? 0.6695 1.3214 0.7081 0.0375  0.0725  0.0006  435 ALA A N   
1028 C CA  . ALA A 139 ? 0.6485 1.2897 0.6985 -0.0076 0.0656  0.0139  435 ALA A CA  
1029 C C   . ALA A 139 ? 0.6816 1.2596 0.6926 -0.0490 0.0622  0.0256  435 ALA A C   
1030 O O   . ALA A 139 ? 0.6877 1.1985 0.6903 -0.0701 0.0497  0.0310  435 ALA A O   
1031 C CB  . ALA A 139 ? 0.6878 1.4395 0.7646 -0.0287 0.0767  0.0228  435 ALA A CB  
1032 N N   . HIS A 140 ? 0.7176 1.3132 0.6986 -0.0574 0.0733  0.0297  436 HIS A N   
1033 C CA  . HIS A 140 ? 0.7731 1.2953 0.7054 -0.0877 0.0689  0.0402  436 HIS A CA  
1034 C C   . HIS A 140 ? 0.7572 1.1807 0.6775 -0.0638 0.0508  0.0318  436 HIS A C   
1035 O O   . HIS A 140 ? 0.8065 1.1589 0.6979 -0.0846 0.0402  0.0404  436 HIS A O   
1036 C CB  . HIS A 140 ? 0.8512 1.4076 0.7524 -0.0907 0.0837  0.0433  436 HIS A CB  
1037 C CG  . HIS A 140 ? 0.8670 1.5019 0.7596 -0.1382 0.1002  0.0591  436 HIS A CG  
1038 N ND1 . HIS A 140 ? 0.8324 1.5861 0.7663 -0.1372 0.1132  0.0582  436 HIS A ND1 
1039 C CD2 . HIS A 140 ? 0.8837 1.4967 0.7271 -0.1909 0.1053  0.0768  436 HIS A CD2 
1040 C CE1 . HIS A 140 ? 0.8452 1.6581 0.7610 -0.1912 0.1262  0.0744  436 HIS A CE1 
1041 N NE2 . HIS A 140 ? 0.8770 1.5996 0.7344 -0.2270 0.1219  0.0862  436 HIS A NE2 
1042 N N   . GLY A 141 ? 0.7115 1.1295 0.6479 -0.0201 0.0467  0.0151  437 GLY A N   
1043 C CA  . GLY A 141 ? 0.7550 1.0959 0.6858 -0.0025 0.0291  0.0069  437 GLY A CA  
1044 C C   . GLY A 141 ? 0.7336 1.0454 0.6875 -0.0110 0.0176  0.0090  437 GLY A C   
1045 O O   . GLY A 141 ? 0.7599 1.0109 0.6977 -0.0158 0.0048  0.0118  437 GLY A O   
1046 N N   . MET A 142 ? 0.7373 1.0953 0.7272 -0.0092 0.0219  0.0076  438 MET A N   
1047 C CA  . MET A 142 ? 0.6883 1.0225 0.6982 -0.0193 0.0122  0.0103  438 MET A CA  
1048 C C   . MET A 142 ? 0.7174 1.0164 0.6985 -0.0578 0.0094  0.0254  438 MET A C   
1049 O O   . MET A 142 ? 0.7142 0.9518 0.6839 -0.0587 -0.0028 0.0266  438 MET A O   
1050 C CB  . MET A 142 ? 0.6576 1.0554 0.7053 -0.0131 0.0180  0.0082  438 MET A CB  
1051 C CG  . MET A 142 ? 0.6605 1.0804 0.7238 0.0295  0.0204  -0.0064 438 MET A CG  
1052 S SD  . MET A 142 ? 0.6399 1.1372 0.7404 0.0427  0.0262  -0.0068 438 MET A SD  
1053 C CE  . MET A 142 ? 0.6528 1.1010 0.7706 0.0262  0.0117  -0.0035 438 MET A CE  
1054 N N   . PHE A 143 ? 0.6892 1.0250 0.6520 -0.0900 0.0208  0.0372  439 PHE A N   
1055 C CA  . PHE A 143 ? 0.7333 1.0208 0.6515 -0.1319 0.0182  0.0524  439 PHE A CA  
1056 C C   . PHE A 143 ? 0.7956 0.9918 0.6678 -0.1215 0.0070  0.0538  439 PHE A C   
1057 O O   . PHE A 143 ? 0.8098 0.9376 0.6541 -0.1296 -0.0036 0.0589  439 PHE A O   
1058 C CB  . PHE A 143 ? 0.7930 1.1352 0.6899 -0.1713 0.0334  0.0646  439 PHE A CB  
1059 C CG  . PHE A 143 ? 0.8697 1.1446 0.7008 -0.2192 0.0311  0.0812  439 PHE A CG  
1060 C CD1 . PHE A 143 ? 0.8942 1.1275 0.7096 -0.2487 0.0230  0.0877  439 PHE A CD1 
1061 C CD2 . PHE A 143 ? 0.9045 1.1485 0.6804 -0.2346 0.0365  0.0903  439 PHE A CD2 
1062 C CE1 . PHE A 143 ? 0.9981 1.1531 0.7390 -0.2925 0.0200  0.1024  439 PHE A CE1 
1063 C CE2 . PHE A 143 ? 0.9821 1.1480 0.6835 -0.2790 0.0336  0.1065  439 PHE A CE2 
1064 C CZ  . PHE A 143 ? 1.0315 1.1481 0.7123 -0.3081 0.0250  0.1123  439 PHE A CZ  
1065 N N   . ASN A 144 ? 0.7875 0.9827 0.6476 -0.0999 0.0087  0.0489  440 ASN A N   
1066 C CA  . ASN A 144 ? 0.7892 0.9095 0.6072 -0.0851 -0.0032 0.0498  440 ASN A CA  
1067 C C   . ASN A 144 ? 0.7910 0.8781 0.6317 -0.0563 -0.0187 0.0400  440 ASN A C   
1068 O O   . ASN A 144 ? 0.8370 0.8606 0.6429 -0.0513 -0.0302 0.0446  440 ASN A O   
1069 C CB  . ASN A 144 ? 0.8574 0.9941 0.6650 -0.0656 0.0006  0.0439  440 ASN A CB  
1070 C CG  . ASN A 144 ? 0.8832 0.9502 0.6366 -0.0568 -0.0105 0.0488  440 ASN A CG  
1071 O OD1 . ASN A 144 ? 0.9184 0.9366 0.6154 -0.0811 -0.0100 0.0638  440 ASN A OD1 
1072 N ND2 . ASN A 144 ? 0.8814 0.9403 0.6461 -0.0230 -0.0220 0.0365  440 ASN A ND2 
1073 N N   . TYR A 145 ? 0.7749 0.9040 0.6684 -0.0352 -0.0191 0.0264  441 TYR A N   
1074 C CA  . TYR A 145 ? 0.7882 0.8958 0.7052 -0.0140 -0.0322 0.0176  441 TYR A CA  
1075 C C   . TYR A 145 ? 0.7478 0.8281 0.6633 -0.0277 -0.0363 0.0245  441 TYR A C   
1076 O O   . TYR A 145 ? 0.7554 0.7970 0.6622 -0.0137 -0.0477 0.0232  441 TYR A O   
1077 C CB  . TYR A 145 ? 0.7493 0.8984 0.7123 0.0040  -0.0306 0.0034  441 TYR A CB  
1078 C CG  . TYR A 145 ? 0.6959 0.8416 0.6555 0.0258  -0.0366 -0.0085 441 TYR A CG  
1079 C CD1 . TYR A 145 ? 0.7110 0.8294 0.6647 0.0371  -0.0509 -0.0127 441 TYR A CD1 
1080 C CD2 . TYR A 145 ? 0.6803 0.8536 0.6409 0.0356  -0.0285 -0.0165 441 TYR A CD2 
1081 C CE1 . TYR A 145 ? 0.7169 0.8371 0.6666 0.0506  -0.0580 -0.0238 441 TYR A CE1 
1082 C CE2 . TYR A 145 ? 0.7261 0.8882 0.6759 0.0518  -0.0353 -0.0286 441 TYR A CE2 
1083 C CZ  . TYR A 145 ? 0.7525 0.8888 0.6977 0.0557  -0.0507 -0.0319 441 TYR A CZ  
1084 O OH  . TYR A 145 ? 0.7801 0.9099 0.7134 0.0655  -0.0594 -0.0439 441 TYR A OH  
1085 N N   . ILE A 146 ? 0.7543 0.8598 0.6774 -0.0542 -0.0273 0.0313  442 ILE A N   
1086 C CA  . ILE A 146 ? 0.7583 0.8353 0.6751 -0.0708 -0.0316 0.0371  442 ILE A CA  
1087 C C   . ILE A 146 ? 0.8179 0.8172 0.6658 -0.0852 -0.0371 0.0486  442 ILE A C   
1088 O O   . ILE A 146 ? 0.8433 0.7891 0.6706 -0.0766 -0.0467 0.0492  442 ILE A O   
1089 C CB  . ILE A 146 ? 0.7218 0.8551 0.6638 -0.0980 -0.0220 0.0409  442 ILE A CB  
1090 C CG1 . ILE A 146 ? 0.6508 0.8434 0.6518 -0.0735 -0.0197 0.0290  442 ILE A CG1 
1091 C CG2 . ILE A 146 ? 0.7542 0.8503 0.6743 -0.1252 -0.0266 0.0487  442 ILE A CG2 
1092 C CD1 . ILE A 146 ? 0.6461 0.9106 0.6742 -0.0898 -0.0103 0.0318  442 ILE A CD1 
1093 N N   . CYS A 147 ? 0.8559 0.8415 0.6599 -0.1031 -0.0314 0.0578  443 CYS A N   
1094 C CA  . CYS A 147 ? 0.8608 0.7560 0.5847 -0.1149 -0.0376 0.0696  443 CYS A CA  
1095 C C   . CYS A 147 ? 0.8898 0.7344 0.5958 -0.0707 -0.0518 0.0641  443 CYS A C   
1096 O O   . CYS A 147 ? 0.9720 0.7417 0.6274 -0.0636 -0.0609 0.0687  443 CYS A O   
1097 C CB  . CYS A 147 ? 0.9570 0.8442 0.6324 -0.1417 -0.0289 0.0810  443 CYS A CB  
1098 S SG  . CYS A 147 ? 1.0536 0.9851 0.7211 -0.2058 -0.0138 0.0931  443 CYS A SG  
1099 N N   . ASN A 148 ? 0.8790 0.7657 0.6224 -0.0396 -0.0542 0.0535  444 ASN A N   
1100 C CA  . ASN A 148 ? 0.8621 0.7214 0.5944 0.0009  -0.0683 0.0479  444 ASN A CA  
1101 C C   . ASN A 148 ? 0.8598 0.7251 0.6264 0.0182  -0.0750 0.0403  444 ASN A C   
1102 O O   . ASN A 148 ? 0.8718 0.6975 0.6095 0.0461  -0.0860 0.0402  444 ASN A O   
1103 C CB  . ASN A 148 ? 0.8862 0.7945 0.6491 0.0216  -0.0701 0.0380  444 ASN A CB  
1104 C CG  . ASN A 148 ? 0.9316 0.8251 0.6490 0.0118  -0.0652 0.0457  444 ASN A CG  
1105 O OD1 . ASN A 148 ? 0.9904 0.8250 0.6430 -0.0057 -0.0634 0.0597  444 ASN A OD1 
1106 N ND2 . ASN A 148 ? 0.9447 0.8849 0.6883 0.0218  -0.0634 0.0365  444 ASN A ND2 
1107 N N   . HIS A 149 ? 0.7732 0.6894 0.5978 0.0048  -0.0684 0.0342  445 HIS A N   
1108 C CA  . HIS A 149 ? 0.8006 0.7204 0.6535 0.0147  -0.0728 0.0287  445 HIS A CA  
1109 C C   . HIS A 149 ? 0.8246 0.6736 0.6224 0.0063  -0.0760 0.0377  445 HIS A C   
1110 O O   . HIS A 149 ? 0.8860 0.7018 0.6639 0.0340  -0.0849 0.0355  445 HIS A O   
1111 C CB  . HIS A 149 ? 0.7191 0.6971 0.6316 -0.0011 -0.0645 0.0230  445 HIS A CB  
1112 C CG  . HIS A 149 ? 0.7261 0.7099 0.6677 0.0053  -0.0678 0.0182  445 HIS A CG  
1113 N ND1 . HIS A 149 ? 0.6672 0.6984 0.6624 0.0135  -0.0671 0.0083  445 HIS A ND1 
1114 C CD2 . HIS A 149 ? 0.7393 0.6819 0.6568 0.0040  -0.0716 0.0219  445 HIS A CD2 
1115 C CE1 . HIS A 149 ? 0.6702 0.6952 0.6774 0.0159  -0.0697 0.0070  445 HIS A CE1 
1116 N NE2 . HIS A 149 ? 0.7064 0.6804 0.6688 0.0115  -0.0723 0.0145  445 HIS A NE2 
1117 N N   . VAL A 150 ? 0.8503 0.6765 0.6184 -0.0325 -0.0689 0.0475  446 VAL A N   
1118 C CA  . VAL A 150 ? 0.9322 0.6767 0.6330 -0.0488 -0.0725 0.0563  446 VAL A CA  
1119 C C   . VAL A 150 ? 1.0179 0.6781 0.6427 -0.0182 -0.0828 0.0605  446 VAL A C   
1120 O O   . VAL A 150 ? 1.0723 0.6786 0.6626 0.0059  -0.0909 0.0588  446 VAL A O   
1121 C CB  . VAL A 150 ? 0.9707 0.7078 0.6421 -0.1039 -0.0637 0.0677  446 VAL A CB  
1122 C CG1 . VAL A 150 ? 1.0260 0.6591 0.6083 -0.1275 -0.0692 0.0772  446 VAL A CG1 
1123 C CG2 . VAL A 150 ? 0.8769 0.7050 0.6222 -0.1265 -0.0550 0.0633  446 VAL A CG2 
1124 N N   . LYS A 151 ? 1.0177 0.6651 0.6111 -0.0143 -0.0829 0.0657  447 LYS A N   
1125 C CA  . LYS A 151 ? 1.1149 0.6765 0.6258 0.0178  -0.0937 0.0711  447 LYS A CA  
1126 C C   . LYS A 151 ? 1.0986 0.6825 0.6357 0.0755  -0.1045 0.0601  447 LYS A C   
1127 O O   . LYS A 151 ? 1.1659 0.6800 0.6428 0.1073  -0.1136 0.0616  447 LYS A O   
1128 C CB  . LYS A 151 ? 1.0964 0.6511 0.5751 0.0138  -0.0921 0.0782  447 LYS A CB  
1129 C CG  . LYS A 151 ? 1.2134 0.6558 0.5818 0.0364  -0.1025 0.0886  447 LYS A CG  
1130 C CD  . LYS A 151 ? 1.2229 0.6599 0.5590 0.0256  -0.0995 0.0968  447 LYS A CD  
1131 C CE  . LYS A 151 ? 1.3162 0.6217 0.5226 0.0304  -0.1070 0.1119  447 LYS A CE  
1132 N NZ  . LYS A 151 ? 1.3792 0.6852 0.5559 0.0158  -0.1026 0.1206  447 LYS A NZ  
1133 N N   . TYR A 152 ? 0.9882 0.6697 0.6104 0.0892  -0.1035 0.0488  448 TYR A N   
1134 C CA  . TYR A 152 ? 0.9939 0.7138 0.6460 0.1360  -0.1131 0.0386  448 TYR A CA  
1135 C C   . TYR A 152 ? 1.0256 0.7325 0.6837 0.1446  -0.1137 0.0350  448 TYR A C   
1136 O O   . TYR A 152 ? 1.0684 0.7410 0.6865 0.1859  -0.1224 0.0339  448 TYR A O   
1137 C CB  . TYR A 152 ? 0.9314 0.7526 0.6681 0.1360  -0.1116 0.0274  448 TYR A CB  
1138 C CG  . TYR A 152 ? 0.9236 0.7993 0.6980 0.1723  -0.1203 0.0170  448 TYR A CG  
1139 C CD1 . TYR A 152 ? 0.9494 0.8445 0.7076 0.2108  -0.1321 0.0146  448 TYR A CD1 
1140 C CD2 . TYR A 152 ? 0.8846 0.7978 0.7086 0.1670  -0.1167 0.0103  448 TYR A CD2 
1141 C CE1 . TYR A 152 ? 0.8977 0.8588 0.6924 0.2410  -0.1397 0.0055  448 TYR A CE1 
1142 C CE2 . TYR A 152 ? 0.8533 0.8236 0.7102 0.1952  -0.1231 0.0018  448 TYR A CE2 
1143 C CZ  . TYR A 152 ? 0.9175 0.9164 0.7616 0.2308  -0.1343 -0.0007 448 TYR A CZ  
1144 O OH  . TYR A 152 ? 0.9291 1.0014 0.8094 0.2552  -0.1400 -0.0090 448 TYR A OH  
1145 N N   . ALA A 153 ? 0.9470 0.6814 0.6508 0.1091  -0.1047 0.0330  449 ALA A N   
1146 C CA  . ALA A 153 ? 0.9684 0.6989 0.6843 0.1151  -0.1047 0.0286  449 ALA A CA  
1147 C C   . ALA A 153 ? 1.0984 0.7218 0.7225 0.1217  -0.1092 0.0357  449 ALA A C   
1148 O O   . ALA A 153 ? 1.1405 0.7459 0.7511 0.1500  -0.1131 0.0310  449 ALA A O   
1149 C CB  . ALA A 153 ? 0.8773 0.6542 0.6527 0.0750  -0.0952 0.0266  449 ALA A CB  
1150 N N   . THR A 154 ? 1.0807 0.6282 0.6348 0.0942  -0.1083 0.0469  450 THR A N   
1151 C CA  . THR A 154 ? 1.2249 0.6513 0.6749 0.0949  -0.1136 0.0540  450 THR A CA  
1152 C C   . THR A 154 ? 1.3359 0.7031 0.7171 0.1574  -0.1250 0.0537  450 THR A C   
1153 O O   . THR A 154 ? 1.3682 0.6753 0.6972 0.1909  -0.1308 0.0508  450 THR A O   
1154 C CB  . THR A 154 ? 1.2562 0.6194 0.6462 0.0387  -0.1091 0.0671  450 THR A CB  
1155 O OG1 . THR A 154 ? 1.2150 0.6448 0.6694 -0.0140 -0.0992 0.0668  450 THR A OG1 
1156 C CG2 . THR A 154 ? 1.3839 0.6032 0.6488 0.0344  -0.1160 0.0749  450 THR A CG2 
1157 N N   . ASN A 155 ? 1.3042 0.6872 0.6794 0.1773  -0.1287 0.0565  451 ASN A N   
1158 C CA  . ASN A 155 ? 1.3524 0.7095 0.6792 0.2449  -0.1408 0.0549  451 ASN A CA  
1159 C C   . ASN A 155 ? 1.4914 0.7044 0.6904 0.2711  -0.1485 0.0609  451 ASN A C   
1160 O O   . ASN A 155 ? 1.5703 0.7700 0.7436 0.3300  -0.1557 0.0544  451 ASN A O   
1161 C CB  . ASN A 155 ? 1.2751 0.7457 0.6882 0.2872  -0.1432 0.0412  451 ASN A CB  
1162 C CG  . ASN A 155 ? 1.3466 0.8275 0.7279 0.3570  -0.1558 0.0388  451 ASN A CG  
1163 O OD1 . ASN A 155 ? 1.3637 0.8054 0.6922 0.3708  -0.1624 0.0460  451 ASN A OD1 
1164 N ND2 . ASN A 155 ? 1.3278 0.8661 0.7387 0.4031  -0.1592 0.0290  451 ASN A ND2 
1165 N N   . LYS A 156 ? 1.5752 0.6776 0.6873 0.2259  -0.1467 0.0733  452 LYS A N   
1166 C CA  . LYS A 156 ? 1.6834 0.6482 0.6728 0.2358  -0.1502 0.0728  452 LYS A CA  
1167 C C   . LYS A 156 ? 1.7226 0.6625 0.7016 0.2454  -0.1492 0.0616  452 LYS A C   
1168 O O   . LYS A 156 ? 1.7966 0.6627 0.6970 0.2764  -0.1513 0.0503  452 LYS A O   
1169 C CB  . LYS A 156 ? 1.7672 0.7147 0.7113 0.2978  -0.1557 0.0639  452 LYS A CB  
1170 C CG  . LYS A 156 ? 1.8412 0.7713 0.7576 0.2845  -0.1569 0.0742  452 LYS A CG  
1171 C CD  . LYS A 156 ? 1.9348 0.8124 0.7775 0.3408  -0.1623 0.0645  452 LYS A CD  
1172 C CE  . LYS A 156 ? 1.9673 0.9596 0.8797 0.3992  -0.1678 0.0586  452 LYS A CE  
1173 N NZ  . LYS A 156 ? 1.9845 0.9979 0.9052 0.3840  -0.1700 0.0697  452 LYS A NZ  
1174 N N   . GLY A 157 ? 1.6708 0.6696 0.7230 0.2207  -0.1463 0.0642  453 GLY A N   
1175 C CA  . GLY A 157 ? 1.7027 0.6889 0.7544 0.2283  -0.1450 0.0540  453 GLY A CA  
1176 C C   . GLY A 157 ? 1.6488 0.7339 0.7738 0.2919  -0.1462 0.0417  453 GLY A C   
1177 O O   . GLY A 157 ? 1.5816 0.6790 0.7263 0.2961  -0.1438 0.0344  453 GLY A O   
1178 N N   . ASN A 158 ? 1.5433 0.7055 0.7088 0.3378  -0.1493 0.0382  454 ASN A N   
1179 C CA  . ASN A 158 ? 1.4732 0.7580 0.7234 0.3862  -0.1491 0.0264  454 ASN A CA  
1180 C C   . ASN A 158 ? 1.3483 0.7626 0.7269 0.3436  -0.1418 0.0245  454 ASN A C   
1181 O O   . ASN A 158 ? 1.2977 0.8052 0.7400 0.3519  -0.1429 0.0221  454 ASN A O   
1182 C CB  . ASN A 158 ? 1.5113 0.8383 0.7513 0.4414  -0.1519 0.0181  454 ASN A CB  
1183 C CG  . ASN A 158 ? 1.4929 0.9574 0.8174 0.4820  -0.1497 0.0055  454 ASN A CG  
1184 O OD1 . ASN A 158 ? 1.4465 0.9592 0.8228 0.4753  -0.1452 0.0013  454 ASN A OD1 
1185 N ND2 . ASN A 158 ? 1.5033 1.0347 0.8407 0.5201  -0.1523 -0.0004 454 ASN A ND2 
1186 N N   . LEU A 159 ? 1.3051 0.7228 0.7173 0.2938  -0.1335 0.0235  455 LEU A N   
1187 C CA  . LEU A 159 ? 1.2075 0.7246 0.7251 0.2432  -0.1245 0.0216  455 LEU A CA  
1188 C C   . LEU A 159 ? 1.1061 0.7530 0.7191 0.2676  -0.1235 0.0120  455 LEU A C   
1189 O O   . LEU A 159 ? 1.0969 0.7775 0.7146 0.3141  -0.1265 0.0051  455 LEU A O   
1190 C CB  . LEU A 159 ? 1.2196 0.7224 0.7516 0.2006  -0.1180 0.0208  455 LEU A CB  
1191 C CG  . LEU A 159 ? 1.2593 0.6902 0.7468 0.1402  -0.1153 0.0303  455 LEU A CG  
1192 C CD1 . LEU A 159 ? 1.3764 0.6928 0.7544 0.1428  -0.1216 0.0401  455 LEU A CD1 
1193 C CD2 . LEU A 159 ? 1.2711 0.6648 0.7410 0.1173  -0.1138 0.0281  455 LEU A CD2 
1194 N N   . ARG A 160 ? 1.0032 0.7236 0.6889 0.2331  -0.1188 0.0115  456 ARG A N   
1195 C CA  . ARG A 160 ? 0.9075 0.7407 0.6746 0.2431  -0.1188 0.0033  456 ARG A CA  
1196 C C   . ARG A 160 ? 0.8396 0.7211 0.6761 0.1939  -0.1099 0.0015  456 ARG A C   
1197 O O   . ARG A 160 ? 0.8675 0.7174 0.6957 0.1576  -0.1055 0.0074  456 ARG A O   
1198 C CB  . ARG A 160 ? 0.9218 0.7804 0.6843 0.2609  -0.1259 0.0043  456 ARG A CB  
1199 C CG  . ARG A 160 ? 1.0007 0.8234 0.6960 0.3188  -0.1365 0.0058  456 ARG A CG  
1200 C CD  . ARG A 160 ? 1.0463 0.9040 0.7413 0.3363  -0.1449 0.0066  456 ARG A CD  
1201 N NE  . ARG A 160 ? 1.0260 0.8134 0.6755 0.3098  -0.1441 0.0161  456 ARG A NE  
1202 C CZ  . ARG A 160 ? 1.1155 0.8981 0.7341 0.3297  -0.1523 0.0196  456 ARG A CZ  
1203 N NH1 . ARG A 160 ? 1.1456 0.9893 0.7723 0.3779  -0.1634 0.0143  456 ARG A NH1 
1204 N NH2 . ARG A 160 ? 1.1008 0.8227 0.6793 0.3001  -0.1495 0.0288  456 ARG A NH2 
1205 N N   . SER A 161 ? 0.7877 0.7472 0.6883 0.1937  -0.1074 -0.0062 457 SER A N   
1206 C CA  . SER A 161 ? 0.7674 0.7650 0.7255 0.1539  -0.0999 -0.0083 457 SER A CA  
1207 C C   . SER A 161 ? 0.7136 0.7465 0.7005 0.1372  -0.1000 -0.0096 457 SER A C   
1208 O O   . SER A 161 ? 0.7201 0.7876 0.7113 0.1557  -0.1063 -0.0130 457 SER A O   
1209 C CB  . SER A 161 ? 0.7280 0.7864 0.7334 0.1572  -0.0974 -0.0152 457 SER A CB  
1210 O OG  . SER A 161 ? 0.7701 0.8044 0.7435 0.1853  -0.0982 -0.0157 457 SER A OG  
1211 N N   . ALA A 162 ? 0.6873 0.7157 0.6925 0.1042  -0.0934 -0.0076 458 ALA A N   
1212 C CA  . ALA A 162 ? 0.6791 0.7291 0.6995 0.0913  -0.0924 -0.0090 458 ALA A CA  
1213 C C   . ALA A 162 ? 0.6588 0.7243 0.7119 0.0637  -0.0844 -0.0100 458 ALA A C   
1214 O O   . ALA A 162 ? 0.6600 0.7085 0.7122 0.0502  -0.0799 -0.0060 458 ALA A O   
1215 C CB  . ALA A 162 ? 0.7072 0.7115 0.6779 0.0928  -0.0937 -0.0014 458 ALA A CB  
1216 N N   . ILE A 163 ? 0.5846 0.6810 0.6612 0.0578  -0.0837 -0.0157 459 ILE A N   
1217 C CA  . ILE A 163 ? 0.5864 0.6942 0.6841 0.0409  -0.0766 -0.0173 459 ILE A CA  
1218 C C   . ILE A 163 ? 0.6236 0.7383 0.7137 0.0403  -0.0755 -0.0200 459 ILE A C   
1219 O O   . ILE A 163 ? 0.6422 0.7661 0.7271 0.0492  -0.0819 -0.0249 459 ILE A O   
1220 C CB  . ILE A 163 ? 0.5879 0.7173 0.7168 0.0370  -0.0767 -0.0240 459 ILE A CB  
1221 C CG1 . ILE A 163 ? 0.5655 0.6983 0.7059 0.0283  -0.0705 -0.0256 459 ILE A CG1 
1222 C CG2 . ILE A 163 ? 0.5338 0.6869 0.6705 0.0411  -0.0836 -0.0320 459 ILE A CG2 
1223 C CD1 . ILE A 163 ? 0.5743 0.7105 0.7328 0.0239  -0.0701 -0.0289 459 ILE A CD1 
1224 N N   . THR A 164 ? 0.6066 0.7228 0.6947 0.0306  -0.0674 -0.0168 460 THR A N   
1225 C CA  . THR A 164 ? 0.6167 0.7427 0.6965 0.0321  -0.0639 -0.0201 460 THR A CA  
1226 C C   . THR A 164 ? 0.5916 0.7349 0.6909 0.0334  -0.0587 -0.0267 460 THR A C   
1227 O O   . THR A 164 ? 0.6332 0.7878 0.7452 0.0289  -0.0531 -0.0229 460 THR A O   
1228 C CB  . THR A 164 ? 0.6169 0.7365 0.6712 0.0226  -0.0574 -0.0104 460 THR A CB  
1229 O OG1 . THR A 164 ? 0.6530 0.7399 0.6752 0.0252  -0.0637 -0.0042 460 THR A OG1 
1230 C CG2 . THR A 164 ? 0.6321 0.7684 0.6779 0.0263  -0.0520 -0.0144 460 THR A CG2 
1231 N N   . ILE A 165 ? 0.6095 0.7511 0.7051 0.0404  -0.0616 -0.0367 461 ILE A N   
1232 C CA  . ILE A 165 ? 0.5978 0.7367 0.6973 0.0463  -0.0590 -0.0444 461 ILE A CA  
1233 C C   . ILE A 165 ? 0.6468 0.7905 0.7273 0.0578  -0.0525 -0.0489 461 ILE A C   
1234 O O   . ILE A 165 ? 0.6507 0.7846 0.7113 0.0600  -0.0560 -0.0548 461 ILE A O   
1235 C CB  . ILE A 165 ? 0.5951 0.7159 0.6930 0.0415  -0.0680 -0.0533 461 ILE A CB  
1236 C CG1 . ILE A 165 ? 0.6245 0.7516 0.7429 0.0324  -0.0722 -0.0485 461 ILE A CG1 
1237 C CG2 . ILE A 165 ? 0.6693 0.7678 0.7555 0.0478  -0.0659 -0.0603 461 ILE A CG2 
1238 C CD1 . ILE A 165 ? 0.6337 0.7586 0.7527 0.0211  -0.0804 -0.0555 461 ILE A CD1 
1239 N N   . PHE A 166 ? 0.6291 0.7937 0.7149 0.0669  -0.0432 -0.0464 462 PHE A N   
1240 C CA  . PHE A 166 ? 0.6333 0.8143 0.7022 0.0836  -0.0345 -0.0506 462 PHE A CA  
1241 C C   . PHE A 166 ? 0.6798 0.8304 0.7278 0.1047  -0.0362 -0.0630 462 PHE A C   
1242 O O   . PHE A 166 ? 0.7171 0.8357 0.7651 0.1015  -0.0434 -0.0663 462 PHE A O   
1243 C CB  . PHE A 166 ? 0.6195 0.8527 0.7043 0.0831  -0.0235 -0.0410 462 PHE A CB  
1244 C CG  . PHE A 166 ? 0.6421 0.8902 0.7276 0.0585  -0.0212 -0.0292 462 PHE A CG  
1245 C CD1 . PHE A 166 ? 0.6400 0.8887 0.7024 0.0555  -0.0177 -0.0282 462 PHE A CD1 
1246 C CD2 . PHE A 166 ? 0.5837 0.8338 0.6833 0.0379  -0.0236 -0.0193 462 PHE A CD2 
1247 C CE1 . PHE A 166 ? 0.6751 0.9227 0.7253 0.0320  -0.0164 -0.0162 462 PHE A CE1 
1248 C CE2 . PHE A 166 ? 0.5946 0.8397 0.6793 0.0142  -0.0226 -0.0084 462 PHE A CE2 
1249 C CZ  . PHE A 166 ? 0.6422 0.8833 0.7001 0.0109  -0.0190 -0.0063 462 PHE A CZ  
1250 N N   . PRO A 167 ? 0.7253 0.8777 0.7467 0.1263  -0.0300 -0.0704 463 PRO A N   
1251 C CA  . PRO A 167 ? 0.7505 0.8546 0.7344 0.1494  -0.0327 -0.0836 463 PRO A CA  
1252 C C   . PRO A 167 ? 0.7630 0.8531 0.7508 0.1617  -0.0339 -0.0828 463 PRO A C   
1253 O O   . PRO A 167 ? 0.7335 0.8724 0.7520 0.1667  -0.0282 -0.0737 463 PRO A O   
1254 C CB  . PRO A 167 ? 0.7378 0.8661 0.6982 0.1788  -0.0214 -0.0887 463 PRO A CB  
1255 C CG  . PRO A 167 ? 0.7303 0.8921 0.7024 0.1586  -0.0183 -0.0821 463 PRO A CG  
1256 C CD  . PRO A 167 ? 0.7041 0.8908 0.7172 0.1291  -0.0211 -0.0680 463 PRO A CD  
1257 N N   . GLN A 168 ? 0.8131 0.8335 0.7641 0.1636  -0.0424 -0.0921 464 GLN A N   
1258 C CA  . GLN A 168 ? 0.8266 0.8173 0.7684 0.1752  -0.0449 -0.0913 464 GLN A CA  
1259 C C   . GLN A 168 ? 0.8657 0.8671 0.7843 0.2232  -0.0368 -0.0945 464 GLN A C   
1260 O O   . GLN A 168 ? 0.8987 0.9046 0.7898 0.2492  -0.0307 -0.1021 464 GLN A O   
1261 C CB  . GLN A 168 ? 0.8584 0.7626 0.7542 0.1590  -0.0561 -0.0999 464 GLN A CB  
1262 C CG  . GLN A 168 ? 0.9450 0.7864 0.7743 0.1738  -0.0584 -0.1146 464 GLN A CG  
1263 C CD  . GLN A 168 ? 1.0178 0.7885 0.8080 0.1369  -0.0712 -0.1222 464 GLN A CD  
1264 O OE1 . GLN A 168 ? 1.0091 0.8093 0.8342 0.0989  -0.0769 -0.1183 464 GLN A OE1 
1265 N NE2 . GLN A 168 ? 1.1040 0.7807 0.8163 0.1478  -0.0762 -0.1332 464 GLN A NE2 
1266 N N   . ARG A 169 ? 0.8322 0.8442 0.7618 0.2379  -0.0368 -0.0887 465 ARG A N   
1267 C CA  . ARG A 169 ? 0.9164 0.9322 0.8163 0.2904  -0.0319 -0.0924 465 ARG A CA  
1268 C C   . ARG A 169 ? 1.0132 0.9303 0.8311 0.3172  -0.0358 -0.1072 465 ARG A C   
1269 O O   . ARG A 169 ? 1.0481 0.8791 0.8292 0.2896  -0.0457 -0.1123 465 ARG A O   
1270 C CB  . ARG A 169 ? 0.9397 0.9592 0.8525 0.2983  -0.0357 -0.0845 465 ARG A CB  
1271 C CG  . ARG A 169 ? 1.0296 1.0368 0.8994 0.3585  -0.0341 -0.0889 465 ARG A CG  
1272 C CD  . ARG A 169 ? 1.0254 1.0547 0.9156 0.3664  -0.0381 -0.0793 465 ARG A CD  
1273 N NE  . ARG A 169 ? 0.9909 1.1422 0.9538 0.3547  -0.0321 -0.0683 465 ARG A NE  
1274 C CZ  . ARG A 169 ? 0.9384 1.1174 0.9472 0.3161  -0.0359 -0.0580 465 ARG A CZ  
1275 N NH1 . ARG A 169 ? 0.9813 1.0868 0.9786 0.2876  -0.0442 -0.0566 465 ARG A NH1 
1276 N NH2 . ARG A 169 ? 0.8423 1.1256 0.9056 0.3041  -0.0311 -0.0490 465 ARG A NH2 
1277 N N   . THR A 170 ? 1.0776 1.0087 0.8626 0.3697  -0.0281 -0.1143 466 THR A N   
1278 C CA  . THR A 170 ? 1.1667 0.9930 0.8598 0.4033  -0.0317 -0.1296 466 THR A CA  
1279 C C   . THR A 170 ? 1.2630 1.0661 0.9105 0.4667  -0.0310 -0.1317 466 THR A C   
1280 O O   . THR A 170 ? 1.3497 1.0681 0.9553 0.4672  -0.0406 -0.1310 466 THR A O   
1281 C CB  . THR A 170 ? 1.1914 1.0361 0.8658 0.4181  -0.0238 -0.1393 466 THR A CB  
1282 O OG1 . THR A 170 ? 1.1464 1.1189 0.8762 0.4409  -0.0095 -0.1324 466 THR A OG1 
1283 C CG2 . THR A 170 ? 1.1346 0.9643 0.8261 0.3594  -0.0294 -0.1401 466 THR A CG2 
1284 N N   . ASP A 171 ? 1.2375 1.1202 0.8913 0.5214  -0.0194 -0.1336 467 ASP A N   
1285 C CA  . ASP A 171 ? 1.3032 1.1890 0.9234 0.5718  -0.0207 -0.1292 467 ASP A CA  
1286 C C   . ASP A 171 ? 1.2951 1.2717 0.9841 0.5653  -0.0207 -0.1146 467 ASP A C   
1287 O O   . ASP A 171 ? 1.3791 1.3281 1.0360 0.5885  -0.0273 -0.1094 467 ASP A O   
1288 C CB  . ASP A 171 ? 1.3360 1.2872 0.9403 0.6130  -0.0115 -0.1303 467 ASP A CB  
1289 C CG  . ASP A 171 ? 1.2812 1.3926 0.9753 0.6006  0.0020  -0.1223 467 ASP A CG  
1290 O OD1 . ASP A 171 ? 1.2282 1.3848 0.9893 0.5579  0.0047  -0.1183 467 ASP A OD1 
1291 O OD2 . ASP A 171 ? 1.2983 1.4894 0.9915 0.6317  0.0092  -0.1193 467 ASP A OD2 
1292 N N   . GLY A 172 ? 1.2173 1.3005 0.9950 0.5330  -0.0142 -0.1076 468 GLY A N   
1293 C CA  . GLY A 172 ? 1.1493 1.3308 0.9920 0.5213  -0.0141 -0.0931 468 GLY A CA  
1294 C C   . GLY A 172 ? 1.1377 1.4656 1.0361 0.5176  -0.0022 -0.0855 468 GLY A C   
1295 O O   . GLY A 172 ? 1.0576 1.4745 1.0230 0.4837  -0.0006 -0.0742 468 GLY A O   
1296 N N   . LYS A 173 ? 1.1547 1.5052 1.0207 0.5484  0.0056  -0.0910 469 LYS A N   
1297 C CA  . LYS A 173 ? 1.1246 1.6107 1.0348 0.5419  0.0173  -0.0841 469 LYS A CA  
1298 C C   . LYS A 173 ? 1.1026 1.6155 1.0378 0.5125  0.0276  -0.0869 469 LYS A C   
1299 O O   . LYS A 173 ? 1.0584 1.6707 1.0172 0.5061  0.0384  -0.0820 469 LYS A O   
1300 C CB  . LYS A 173 ? 1.1934 1.7053 1.0546 0.5962  0.0194  -0.0867 469 LYS A CB  
1301 C CG  . LYS A 173 ? 1.1961 1.8558 1.1016 0.5936  0.0251  -0.0757 469 LYS A CG  
1302 C CD  . LYS A 173 ? 1.1764 1.8798 1.1343 0.5581  0.0197  -0.0648 469 LYS A CD  
1303 C CE  . LYS A 173 ? 1.1189 1.9353 1.1479 0.4997  0.0276  -0.0541 469 LYS A CE  
1304 N NZ  . LYS A 173 ? 1.0896 1.9122 1.1650 0.4534  0.0211  -0.0452 469 LYS A NZ  
1305 N N   . HIS A 174 ? 1.0749 1.5017 1.0014 0.4938  0.0240  -0.0948 470 HIS A N   
1306 C CA  . HIS A 174 ? 1.0558 1.4931 1.0026 0.4482  0.0295  -0.0935 470 HIS A CA  
1307 C C   . HIS A 174 ? 1.0362 1.4349 1.0179 0.3825  0.0191  -0.0840 470 HIS A C   
1308 O O   . HIS A 174 ? 1.1209 1.4411 1.0842 0.3531  0.0127  -0.0880 470 HIS A O   
1309 C CB  . HIS A 174 ? 1.1219 1.4692 1.0028 0.4688  0.0297  -0.1089 470 HIS A CB  
1310 C CG  . HIS A 174 ? 1.1554 1.5349 0.9951 0.5303  0.0397  -0.1172 470 HIS A CG  
1311 N ND1 . HIS A 174 ? 1.2340 1.5126 0.9948 0.5731  0.0312  -0.1269 470 HIS A ND1 
1312 C CD2 . HIS A 174 ? 1.1347 1.6237 0.9953 0.5364  0.0516  -0.1104 470 HIS A CD2 
1313 C CE1 . HIS A 174 ? 1.2818 1.6097 1.0189 0.6091  0.0374  -0.1263 470 HIS A CE1 
1314 N NE2 . HIS A 174 ? 1.2300 1.6885 1.0286 0.5878  0.0499  -0.1168 470 HIS A NE2 
1315 N N   . ASP A 175 ? 0.9335 1.3907 0.9631 0.3617  0.0169  -0.0720 471 ASP A N   
1316 C CA  . ASP A 175 ? 0.8551 1.2832 0.9161 0.3053  0.0081  -0.0628 471 ASP A CA  
1317 C C   . ASP A 175 ? 0.7964 1.2740 0.8885 0.2580  0.0142  -0.0539 471 ASP A C   
1318 O O   . ASP A 175 ? 0.7932 1.3660 0.9056 0.2563  0.0254  -0.0481 471 ASP A O   
1319 C CB  . ASP A 175 ? 0.8178 1.2832 0.9098 0.3021  0.0028  -0.0541 471 ASP A CB  
1320 C CG  . ASP A 175 ? 0.8859 1.2802 0.9412 0.3402  -0.0060 -0.0605 471 ASP A CG  
1321 O OD1 . ASP A 175 ? 0.9534 1.2597 0.9547 0.3641  -0.0086 -0.0718 471 ASP A OD1 
1322 O OD2 . ASP A 175 ? 0.8648 1.2855 0.9389 0.3443  -0.0109 -0.0540 471 ASP A OD2 
1323 N N   . PHE A 176 ? 0.7307 1.1445 0.8226 0.2195  0.0066  -0.0522 472 PHE A N   
1324 C CA  . PHE A 176 ? 0.7048 1.1468 0.8201 0.1727  0.0088  -0.0413 472 PHE A CA  
1325 C C   . PHE A 176 ? 0.6367 1.0942 0.7831 0.1449  0.0029  -0.0311 472 PHE A C   
1326 O O   . PHE A 176 ? 0.6415 1.0445 0.7872 0.1452  -0.0069 -0.0332 472 PHE A O   
1327 C CB  . PHE A 176 ? 0.6820 1.0525 0.7777 0.1525  0.0026  -0.0448 472 PHE A CB  
1328 C CG  . PHE A 176 ? 0.7338 1.0985 0.7992 0.1698  0.0088  -0.0529 472 PHE A CG  
1329 C CD1 . PHE A 176 ? 0.7647 1.0967 0.7960 0.2105  0.0090  -0.0665 472 PHE A CD1 
1330 C CD2 . PHE A 176 ? 0.7260 1.1101 0.7884 0.1458  0.0141  -0.0468 472 PHE A CD2 
1331 C CE1 . PHE A 176 ? 0.8083 1.1308 0.8058 0.2272  0.0147  -0.0752 472 PHE A CE1 
1332 C CE2 . PHE A 176 ? 0.7194 1.0991 0.7519 0.1615  0.0200  -0.0541 472 PHE A CE2 
1333 C CZ  . PHE A 176 ? 0.7569 1.1079 0.7581 0.2025  0.0204  -0.0689 472 PHE A CZ  
1334 N N   . ARG A 177 ? 0.6321 1.1623 0.8007 0.1181  0.0090  -0.0200 473 ARG A N   
1335 C CA  . ARG A 177 ? 0.6094 1.1554 0.8010 0.0892  0.0032  -0.0107 473 ARG A CA  
1336 C C   . ARG A 177 ? 0.6134 1.1759 0.8052 0.0387  0.0058  0.0009  473 ARG A C   
1337 O O   . ARG A 177 ? 0.6183 1.2354 0.8058 0.0266  0.0162  0.0053  473 ARG A O   
1338 C CB  . ARG A 177 ? 0.6176 1.2460 0.8307 0.1103  0.0055  -0.0092 473 ARG A CB  
1339 C CG  . ARG A 177 ? 0.6397 1.2339 0.8432 0.1586  -0.0003 -0.0183 473 ARG A CG  
1340 C CD  . ARG A 177 ? 0.6201 1.1274 0.8192 0.1448  -0.0123 -0.0188 473 ARG A CD  
1341 N NE  . ARG A 177 ? 0.6192 1.1458 0.8409 0.1063  -0.0172 -0.0088 473 ARG A NE  
1342 C CZ  . ARG A 177 ? 0.6559 1.2254 0.8942 0.1111  -0.0213 -0.0048 473 ARG A CZ  
1343 N NH1 . ARG A 177 ? 0.6358 1.2396 0.8723 0.1564  -0.0210 -0.0089 473 ARG A NH1 
1344 N NH2 . ARG A 177 ? 0.6308 1.2053 0.8820 0.0721  -0.0266 0.0031  473 ARG A NH2 
1345 N N   . VAL A 178 ? 0.5856 1.0959 0.7750 0.0097  -0.0031 0.0059  474 VAL A N   
1346 C CA  . VAL A 178 ? 0.5997 1.1195 0.7806 -0.0390 -0.0028 0.0179  474 VAL A CA  
1347 C C   . VAL A 178 ? 0.6049 1.1864 0.8084 -0.0528 -0.0048 0.0229  474 VAL A C   
1348 O O   . VAL A 178 ? 0.6276 1.1823 0.8414 -0.0437 -0.0136 0.0205  474 VAL A O   
1349 C CB  . VAL A 178 ? 0.5965 1.0234 0.7529 -0.0577 -0.0119 0.0199  474 VAL A CB  
1350 C CG1 . VAL A 178 ? 0.6247 1.0423 0.7538 -0.1069 -0.0117 0.0322  474 VAL A CG1 
1351 C CG2 . VAL A 178 ? 0.6292 1.0037 0.7671 -0.0389 -0.0124 0.0138  474 VAL A CG2 
1352 N N   . TRP A 179 ? 0.5945 1.2658 0.8057 -0.0759 0.0032  0.0301  475 TRP A N   
1353 C CA  . TRP A 179 ? 0.6127 1.3613 0.8483 -0.0888 0.0005  0.0345  475 TRP A CA  
1354 C C   . TRP A 179 ? 0.6284 1.3283 0.8475 -0.1363 -0.0095 0.0416  475 TRP A C   
1355 O O   . TRP A 179 ? 0.6310 1.3631 0.8672 -0.1406 -0.0166 0.0426  475 TRP A O   
1356 C CB  . TRP A 179 ? 0.5914 1.4650 0.8410 -0.1042 0.0120  0.0404  475 TRP A CB  
1357 C CG  . TRP A 179 ? 0.5798 1.5181 0.8489 -0.0445 0.0203  0.0316  475 TRP A CG  
1358 C CD1 . TRP A 179 ? 0.5944 1.4701 0.8517 0.0045  0.0216  0.0208  475 TRP A CD1 
1359 C CD2 . TRP A 179 ? 0.6022 1.6292 0.8760 -0.0227 0.0251  0.0310  475 TRP A CD2 
1360 N NE1 . TRP A 179 ? 0.6080 1.5596 0.8769 0.0559  0.0293  0.0140  475 TRP A NE1 
1361 C CE2 . TRP A 179 ? 0.6154 1.6461 0.8875 0.0418  0.0307  0.0202  475 TRP A CE2 
1362 C CE3 . TRP A 179 ? 0.5902 1.6857 0.8608 -0.0509 0.0239  0.0380  475 TRP A CE3 
1363 C CZ2 . TRP A 179 ? 0.6641 1.7624 0.9299 0.0808  0.0349  0.0167  475 TRP A CZ2 
1364 C CZ3 . TRP A 179 ? 0.6197 1.7952 0.8912 -0.0129 0.0281  0.0348  475 TRP A CZ3 
1365 C CH2 . TRP A 179 ? 0.6658 1.8415 0.9344 0.0535  0.0335  0.0245  475 TRP A CH2 
1366 N N   . ASN A 180 ? 0.6355 1.2541 0.8155 -0.1687 -0.0110 0.0463  476 ASN A N   
1367 C CA  . ASN A 180 ? 0.6501 1.2014 0.8009 -0.2064 -0.0210 0.0513  476 ASN A CA  
1368 C C   . ASN A 180 ? 0.6499 1.1411 0.8113 -0.1733 -0.0305 0.0434  476 ASN A C   
1369 O O   . ASN A 180 ? 0.6002 1.0578 0.7718 -0.1318 -0.0302 0.0354  476 ASN A O   
1370 C CB  . ASN A 180 ? 0.7049 1.1684 0.8003 -0.2362 -0.0208 0.0572  476 ASN A CB  
1371 C CG  . ASN A 180 ? 0.7660 1.2791 0.8446 -0.2686 -0.0099 0.0656  476 ASN A CG  
1372 O OD1 . ASN A 180 ? 0.7211 1.3062 0.8288 -0.2432 0.0000  0.0625  476 ASN A OD1 
1373 N ND2 . ASN A 180 ? 0.8059 1.2773 0.8308 -0.3257 -0.0115 0.0764  476 ASN A ND2 
1374 N N   . SER A 181 ? 0.6569 1.1358 0.8124 -0.1956 -0.0392 0.0458  477 SER A N   
1375 C CA  . SER A 181 ? 0.6176 1.0367 0.7771 -0.1697 -0.0474 0.0395  477 SER A CA  
1376 C C   . SER A 181 ? 0.6524 0.9668 0.7739 -0.1676 -0.0504 0.0380  477 SER A C   
1377 O O   . SER A 181 ? 0.6368 0.9112 0.7674 -0.1348 -0.0531 0.0311  477 SER A O   
1378 C CB  . SER A 181 ? 0.6509 1.0870 0.8103 -0.1941 -0.0557 0.0423  477 SER A CB  
1379 O OG  . SER A 181 ? 0.7025 1.1262 0.8222 -0.2500 -0.0578 0.0504  477 SER A OG  
1380 N N   . GLN A 182 ? 0.7089 0.9795 0.7835 -0.2022 -0.0502 0.0447  478 GLN A N   
1381 C CA  . GLN A 182 ? 0.7298 0.9070 0.7615 -0.1937 -0.0525 0.0440  478 GLN A CA  
1382 C C   . GLN A 182 ? 0.7729 0.9446 0.7725 -0.2158 -0.0465 0.0510  478 GLN A C   
1383 O O   . GLN A 182 ? 0.8143 1.0331 0.8064 -0.2557 -0.0423 0.0587  478 GLN A O   
1384 C CB  . GLN A 182 ? 0.8090 0.9013 0.7884 -0.2116 -0.0613 0.0459  478 GLN A CB  
1385 C CG  . GLN A 182 ? 0.8107 0.8925 0.8088 -0.1916 -0.0672 0.0395  478 GLN A CG  
1386 C CD  . GLN A 182 ? 0.9001 0.9178 0.8427 -0.2225 -0.0750 0.0425  478 GLN A CD  
1387 O OE1 . GLN A 182 ? 0.9458 0.8802 0.8207 -0.2375 -0.0779 0.0462  478 GLN A OE1 
1388 N NE2 . GLN A 182 ? 0.8650 0.9146 0.8275 -0.2316 -0.0793 0.0409  478 GLN A NE2 
1389 N N   . LEU A 183 ? 0.7688 0.8874 0.7477 -0.1916 -0.0463 0.0489  479 LEU A N   
1390 C CA  . LEU A 183 ? 0.8061 0.9096 0.7479 -0.2092 -0.0410 0.0560  479 LEU A CA  
1391 C C   . LEU A 183 ? 0.8762 0.9300 0.7509 -0.2626 -0.0430 0.0675  479 LEU A C   
1392 O O   . LEU A 183 ? 0.9185 1.0030 0.7749 -0.2992 -0.0358 0.0762  479 LEU A O   
1393 C CB  . LEU A 183 ? 0.7942 0.8365 0.7151 -0.1734 -0.0442 0.0521  479 LEU A CB  
1394 C CG  . LEU A 183 ? 0.7436 0.8249 0.7188 -0.1284 -0.0433 0.0408  479 LEU A CG  
1395 C CD1 . LEU A 183 ? 0.7682 0.7990 0.7180 -0.1009 -0.0476 0.0381  479 LEU A CD1 
1396 C CD2 . LEU A 183 ? 0.7348 0.9018 0.7511 -0.1279 -0.0334 0.0391  479 LEU A CD2 
1397 N N   . ILE A 184 ? 0.9269 0.8992 0.7568 -0.2694 -0.0524 0.0678  480 ILE A N   
1398 C CA  . ILE A 184 ? 1.0000 0.8974 0.7472 -0.3205 -0.0565 0.0778  480 ILE A CA  
1399 C C   . ILE A 184 ? 1.0480 0.9565 0.7988 -0.3483 -0.0625 0.0766  480 ILE A C   
1400 O O   . ILE A 184 ? 1.0303 0.8955 0.7801 -0.3210 -0.0698 0.0694  480 ILE A O   
1401 C CB  . ILE A 184 ? 1.0649 0.8313 0.7307 -0.3006 -0.0638 0.0791  480 ILE A CB  
1402 C CG1 . ILE A 184 ? 1.1014 0.8660 0.7635 -0.2762 -0.0588 0.0811  480 ILE A CG1 
1403 C CG2 . ILE A 184 ? 1.1812 0.8502 0.7457 -0.3544 -0.0692 0.0892  480 ILE A CG2 
1404 C CD1 . ILE A 184 ? 1.1845 0.8286 0.7631 -0.2525 -0.0665 0.0836  480 ILE A CD1 
1405 N N   . ARG A 185 ? 1.0016 0.9799 0.7603 -0.4019 -0.0592 0.0835  481 ARG A N   
1406 C CA  . ARG A 185 ? 1.0421 1.0360 0.7949 -0.4404 -0.0662 0.0841  481 ARG A CA  
1407 C C   . ARG A 185 ? 1.1218 1.1134 0.8150 -0.5196 -0.0656 0.0965  481 ARG A C   
1408 O O   . ARG A 185 ? 1.1504 1.1833 0.8409 -0.5422 -0.0562 0.1043  481 ARG A O   
1409 C CB  . ARG A 185 ? 0.9796 1.1051 0.8270 -0.4214 -0.0638 0.0782  481 ARG A CB  
1410 C CG  . ARG A 185 ? 0.9326 1.0705 0.8393 -0.3507 -0.0631 0.0671  481 ARG A CG  
1411 C CD  . ARG A 185 ? 0.8440 1.0609 0.8093 -0.3389 -0.0665 0.0621  481 ARG A CD  
1412 N NE  . ARG A 185 ? 0.9411 1.0999 0.8686 -0.3606 -0.0773 0.0612  481 ARG A NE  
1413 C CZ  . ARG A 185 ? 0.9142 1.1201 0.8769 -0.3541 -0.0828 0.0573  481 ARG A CZ  
1414 N NH1 . ARG A 185 ? 0.8368 1.1440 0.8697 -0.3243 -0.0791 0.0545  481 ARG A NH1 
1415 N NH2 . ARG A 185 ? 0.9972 1.1405 0.9165 -0.3753 -0.0927 0.0561  481 ARG A NH2 
1416 N N   . TYR A 186 ? 1.1959 1.1405 0.8379 -0.5513 -0.0752 0.0961  482 TYR A N   
1417 C CA  . TYR A 186 ? 1.2605 1.2064 0.8417 -0.6032 -0.0763 0.1019  482 TYR A CA  
1418 C C   . TYR A 186 ? 1.1849 1.2881 0.8346 -0.6179 -0.0718 0.1023  482 TYR A C   
1419 O O   . TYR A 186 ? 1.1184 1.3019 0.8436 -0.5881 -0.0718 0.0966  482 TYR A O   
1420 C CB  . TYR A 186 ? 1.3661 1.1877 0.8524 -0.6227 -0.0891 0.0999  482 TYR A CB  
1421 C CG  . TYR A 186 ? 1.4606 1.1219 0.8637 -0.6005 -0.0938 0.0991  482 TYR A CG  
1422 C CD1 . TYR A 186 ? 1.5217 1.1246 0.8668 -0.6110 -0.0904 0.1054  482 TYR A CD1 
1423 C CD2 . TYR A 186 ? 1.4500 1.0218 0.8321 -0.5626 -0.1016 0.0917  482 TYR A CD2 
1424 C CE1 . TYR A 186 ? 1.5888 1.0463 0.8537 -0.5809 -0.0953 0.1046  482 TYR A CE1 
1425 C CE2 . TYR A 186 ? 1.5174 0.9474 0.8199 -0.5307 -0.1059 0.0904  482 TYR A CE2 
1426 C CZ  . TYR A 186 ? 1.5852 0.9590 0.8292 -0.5376 -0.1030 0.0970  482 TYR A CZ  
1427 O OH  . TYR A 186 ? 1.6279 0.8663 0.7912 -0.4965 -0.1079 0.0954  482 TYR A OH  
1428 N N   . ALA A 187 ? 1.2385 1.3835 0.8562 -0.6616 -0.0685 0.1088  483 ALA A N   
1429 C CA  . ALA A 187 ? 1.1759 1.4728 0.8492 -0.6739 -0.0638 0.1101  483 ALA A CA  
1430 C C   . ALA A 187 ? 1.2160 1.5287 0.8785 -0.6929 -0.0732 0.1085  483 ALA A C   
1431 O O   . ALA A 187 ? 1.2891 1.4896 0.8765 -0.7162 -0.0834 0.1083  483 ALA A O   
1432 C CB  . ALA A 187 ? 1.2452 1.5789 0.8784 -0.7205 -0.0591 0.1173  483 ALA A CB  
1433 N N   . GLY A 188 ? 1.1183 1.5700 0.8517 -0.6797 -0.0695 0.1073  484 GLY A N   
1434 C CA  . GLY A 188 ? 1.1694 1.6613 0.8935 -0.7040 -0.0769 0.1080  484 GLY A CA  
1435 C C   . GLY A 188 ? 1.1669 1.7893 0.9006 -0.7361 -0.0726 0.1136  484 GLY A C   
1436 O O   . GLY A 188 ? 1.1036 1.8381 0.9010 -0.7065 -0.0628 0.1128  484 GLY A O   
1437 N N   . TYR A 189 ? 1.2943 1.9032 0.9598 -0.7964 -0.0801 0.1189  485 TYR A N   
1438 C CA  . TYR A 189 ? 1.3228 2.0588 0.9889 -0.8352 -0.0778 0.1246  485 TYR A CA  
1439 C C   . TYR A 189 ? 1.4082 2.1771 1.0597 -0.8620 -0.0862 0.1263  485 TYR A C   
1440 O O   . TYR A 189 ? 1.4875 2.1475 1.0614 -0.9017 -0.0961 0.1280  485 TYR A O   
1441 C CB  . TYR A 189 ? 1.3857 2.0801 0.9681 -0.8988 -0.0788 0.1313  485 TYR A CB  
1442 C CG  . TYR A 189 ? 1.3526 1.9709 0.9217 -0.8837 -0.0731 0.1306  485 TYR A CG  
1443 C CD1 . TYR A 189 ? 1.3371 2.0521 0.9566 -0.8654 -0.0617 0.1313  485 TYR A CD1 
1444 C CD2 . TYR A 189 ? 1.4246 1.8732 0.9244 -0.8874 -0.0792 0.1293  485 TYR A CD2 
1445 C CE1 . TYR A 189 ? 1.3547 2.0004 0.9599 -0.8539 -0.0561 0.1314  485 TYR A CE1 
1446 C CE2 . TYR A 189 ? 1.4802 1.8584 0.9634 -0.8736 -0.0741 0.1293  485 TYR A CE2 
1447 C CZ  . TYR A 189 ? 1.4059 1.8837 0.9433 -0.8591 -0.0624 0.1308  485 TYR A CZ  
1448 O OH  . TYR A 189 ? 1.4286 1.8348 0.9472 -0.8468 -0.0570 0.1316  485 TYR A OH  
1449 N N   . LYS A 190 ? 1.3996 2.3150 1.1199 -0.8387 -0.0824 0.1256  486 LYS A N   
1450 C CA  . LYS A 190 ? 1.5180 2.4923 1.2192 -0.8764 -0.0893 0.1293  486 LYS A CA  
1451 C C   . LYS A 190 ? 1.6279 2.6159 1.2486 -0.9584 -0.0922 0.1381  486 LYS A C   
1452 O O   . LYS A 190 ? 1.6683 2.6735 1.2730 -0.9761 -0.0869 0.1408  486 LYS A O   
1453 C CB  . LYS A 190 ? 1.4554 2.5903 1.2435 -0.8302 -0.0843 0.1268  486 LYS A CB  
1454 C CG  . LYS A 190 ? 1.4153 2.6432 1.2642 -0.7831 -0.0723 0.1244  486 LYS A CG  
1455 C CD  . LYS A 190 ? 1.3586 2.7364 1.2806 -0.7320 -0.0681 0.1214  486 LYS A CD  
1456 C CE  . LYS A 190 ? 1.3271 2.6692 1.3007 -0.6662 -0.0708 0.1133  486 LYS A CE  
1457 N NZ  . LYS A 190 ? 1.3021 2.6448 1.2647 -0.6843 -0.0810 0.1139  486 LYS A NZ  
1458 N N   . GLN A 191 ? 1.6369 2.6136 1.2025 -1.0112 -0.1013 0.1425  487 GLN A N   
1459 C CA  . GLN A 191 ? 1.7130 2.6752 1.1838 -1.0972 -0.1066 0.1509  487 GLN A CA  
1460 C C   . GLN A 191 ? 1.7012 2.8370 1.1906 -1.1318 -0.1056 0.1566  487 GLN A C   
1461 O O   . GLN A 191 ? 1.6343 2.8790 1.1970 -1.0920 -0.1034 0.1541  487 GLN A O   
1462 C CB  . GLN A 191 ? 1.8248 2.6245 1.1942 -1.1419 -0.1187 0.1525  487 GLN A CB  
1463 C CG  . GLN A 191 ? 1.8311 2.4494 1.1462 -1.1268 -0.1210 0.1486  487 GLN A CG  
1464 C CD  . GLN A 191 ? 1.9074 2.4824 1.1539 -1.1701 -0.1199 0.1525  487 GLN A CD  
1465 O OE1 . GLN A 191 ? 1.8169 2.4834 1.1171 -1.1530 -0.1106 0.1525  487 GLN A OE1 
1466 N NE2 . GLN A 191 ? 2.0273 2.4568 1.1492 -1.2251 -0.1299 0.1554  487 GLN A NE2 
1467 N N   . PRO A 192 ? 1.7593 2.9282 1.1811 -1.2058 -0.1076 0.1641  488 PRO A N   
1468 C CA  . PRO A 192 ? 1.7287 3.0657 1.1586 -1.2471 -0.1077 0.1702  488 PRO A CA  
1469 C C   . PRO A 192 ? 1.7706 3.1054 1.1770 -1.2744 -0.1163 0.1728  488 PRO A C   
1470 O O   . PRO A 192 ? 1.7488 3.2361 1.1806 -1.2930 -0.1158 0.1767  488 PRO A O   
1471 C CB  . PRO A 192 ? 1.8198 3.1518 1.1606 -1.3311 -0.1106 0.1775  488 PRO A CB  
1472 C CG  . PRO A 192 ? 1.8719 2.9971 1.1329 -1.3446 -0.1156 0.1757  488 PRO A CG  
1473 C CD  . PRO A 192 ? 1.8408 2.9083 1.1797 -1.2521 -0.1094 0.1668  488 PRO A CD  
1474 N N   . ASP A 193 ? 1.8631 3.0326 1.2203 -1.2761 -0.1242 0.1705  489 ASP A N   
1475 C CA  . ASP A 193 ? 1.8740 3.0274 1.2135 -1.2932 -0.1325 0.1717  489 ASP A CA  
1476 C C   . ASP A 193 ? 1.7442 2.8823 1.1689 -1.2092 -0.1313 0.1627  489 ASP A C   
1477 O O   . ASP A 193 ? 1.7979 2.8713 1.2004 -1.2149 -0.1395 0.1615  489 ASP A O   
1478 C CB  . ASP A 193 ? 2.0341 3.0102 1.2431 -1.3606 -0.1438 0.1758  489 ASP A CB  
1479 C CG  . ASP A 193 ? 2.0757 2.8681 1.2461 -1.3303 -0.1448 0.1702  489 ASP A CG  
1480 O OD1 . ASP A 193 ? 2.0657 2.8469 1.2315 -1.3266 -0.1395 0.1698  489 ASP A OD1 
1481 O OD2 . ASP A 193 ? 2.1302 2.7934 1.2752 -1.3085 -0.1509 0.1659  489 ASP A OD2 
1482 N N   . GLY A 194 ? 1.6486 2.8400 1.1648 -1.1329 -0.1219 0.1560  490 GLY A N   
1483 C CA  . GLY A 194 ? 1.5341 2.7332 1.1342 -1.0536 -0.1208 0.1474  490 GLY A CA  
1484 C C   . GLY A 194 ? 1.5662 2.5935 1.1516 -1.0197 -0.1249 0.1406  490 GLY A C   
1485 O O   . GLY A 194 ? 1.4260 2.4564 1.0804 -0.9534 -0.1244 0.1328  490 GLY A O   
1486 N N   . SER A 195 ? 1.6684 2.5456 1.1620 -1.0611 -0.1295 0.1428  491 SER A N   
1487 C CA  . SER A 195 ? 1.7030 2.4192 1.1774 -1.0259 -0.1332 0.1360  491 SER A CA  
1488 C C   . SER A 195 ? 1.6510 2.3505 1.1694 -0.9761 -0.1240 0.1316  491 SER A C   
1489 O O   . SER A 195 ? 1.5879 2.4114 1.1723 -0.9527 -0.1147 0.1320  491 SER A O   
1490 C CB  . SER A 195 ? 1.8122 2.3686 1.1589 -1.0865 -0.1430 0.1399  491 SER A CB  
1491 O OG  . SER A 195 ? 1.9193 2.4378 1.1961 -1.1323 -0.1413 0.1454  491 SER A OG  
1492 N N   . THR A 196 ? 1.6775 2.2254 1.1576 -0.9576 -0.1264 0.1273  492 THR A N   
1493 C CA  . THR A 196 ? 1.6095 2.1351 1.1306 -0.9100 -0.1182 0.1230  492 THR A CA  
1494 C C   . THR A 196 ? 1.6622 2.0262 1.0870 -0.9342 -0.1217 0.1240  492 THR A C   
1495 O O   . THR A 196 ? 1.7535 1.9876 1.0974 -0.9535 -0.1310 0.1232  492 THR A O   
1496 C CB  . THR A 196 ? 1.5137 2.0386 1.1176 -0.8348 -0.1167 0.1137  492 THR A CB  
1497 O OG1 . THR A 196 ? 1.4293 2.0984 1.1149 -0.8082 -0.1145 0.1123  492 THR A OG1 
1498 C CG2 . THR A 196 ? 1.4000 1.9070 1.0448 -0.7892 -0.1081 0.1099  492 THR A CG2 
1499 N N   . LEU A 197 ? 1.6178 1.9885 1.0466 -0.9309 -0.1143 0.1254  493 LEU A N   
1500 C CA  . LEU A 197 ? 1.6541 1.8761 1.0016 -0.9405 -0.1165 0.1253  493 LEU A CA  
1501 C C   . LEU A 197 ? 1.5623 1.7540 0.9713 -0.8729 -0.1099 0.1188  493 LEU A C   
1502 O O   . LEU A 197 ? 1.4685 1.7749 0.9764 -0.8327 -0.1006 0.1167  493 LEU A O   
1503 C CB  . LEU A 197 ? 1.6471 1.8884 0.9398 -0.9951 -0.1144 0.1321  493 LEU A CB  
1504 C CG  . LEU A 197 ? 1.7757 1.8567 0.9634 -1.0149 -0.1186 0.1326  493 LEU A CG  
1505 C CD1 . LEU A 197 ? 1.8419 1.7573 0.9300 -1.0233 -0.1306 0.1301  493 LEU A CD1 
1506 C CD2 . LEU A 197 ? 1.8049 1.9137 0.9288 -1.0826 -0.1192 0.1395  493 LEU A CD2 
1507 N N   . GLY A 198 ? 1.6442 1.6793 0.9887 -0.8588 -0.1150 0.1153  494 GLY A N   
1508 C CA  . GLY A 198 ? 1.5570 1.5553 0.9487 -0.7996 -0.1096 0.1099  494 GLY A CA  
1509 C C   . GLY A 198 ? 1.4026 1.4323 0.8735 -0.7473 -0.1102 0.1024  494 GLY A C   
1510 O O   . GLY A 198 ? 1.4688 1.4506 0.9127 -0.7491 -0.1187 0.0992  494 GLY A O   
1511 N N   . ASP A 199 ? 1.3055 1.4165 0.8720 -0.7007 -0.1016 0.0992  495 ASP A N   
1512 C CA  . ASP A 199 ? 1.2312 1.3679 0.8709 -0.6491 -0.1029 0.0911  495 ASP A CA  
1513 C C   . ASP A 199 ? 1.1374 1.4314 0.8641 -0.6361 -0.0991 0.0908  495 ASP A C   
1514 O O   . ASP A 199 ? 1.0390 1.4327 0.8258 -0.6173 -0.0894 0.0919  495 ASP A O   
1515 C CB  . ASP A 199 ? 1.1988 1.3032 0.8757 -0.6023 -0.0979 0.0868  495 ASP A CB  
1516 C CG  . ASP A 199 ? 1.1508 1.2322 0.8692 -0.5565 -0.1031 0.0775  495 ASP A CG  
1517 O OD1 . ASP A 199 ? 1.1313 1.2569 0.8757 -0.5530 -0.1084 0.0743  495 ASP A OD1 
1518 O OD2 . ASP A 199 ? 1.1386 1.1586 0.8615 -0.5248 -0.1026 0.0735  495 ASP A OD2 
1519 N N   . PRO A 200 ? 1.1314 1.4505 0.8645 -0.6407 -0.1062 0.0888  496 PRO A N   
1520 C CA  . PRO A 200 ? 1.0529 1.5194 0.8609 -0.6244 -0.1031 0.0888  496 PRO A CA  
1521 C C   . PRO A 200 ? 0.9495 1.4804 0.8473 -0.5592 -0.0975 0.0824  496 PRO A C   
1522 O O   . PRO A 200 ? 0.8943 1.5467 0.8482 -0.5379 -0.0917 0.0830  496 PRO A O   
1523 C CB  . PRO A 200 ? 1.0461 1.4964 0.8322 -0.6399 -0.1137 0.0873  496 PRO A CB  
1524 C CG  . PRO A 200 ? 1.1409 1.4467 0.8228 -0.6827 -0.1210 0.0893  496 PRO A CG  
1525 C CD  . PRO A 200 ? 1.1392 1.3523 0.8060 -0.6588 -0.1174 0.0865  496 PRO A CD  
1526 N N   . ALA A 201 ? 0.9574 1.4085 0.8638 -0.5259 -0.0994 0.0763  497 ALA A N   
1527 C CA  . ALA A 201 ? 0.9071 1.4110 0.8903 -0.4665 -0.0953 0.0703  497 ALA A CA  
1528 C C   . ALA A 201 ? 0.8616 1.4418 0.8806 -0.4511 -0.0829 0.0728  497 ALA A C   
1529 O O   . ALA A 201 ? 0.8355 1.4859 0.9159 -0.4018 -0.0784 0.0687  497 ALA A O   
1530 C CB  . ALA A 201 ? 0.9268 1.3277 0.9023 -0.4428 -0.1002 0.0640  497 ALA A CB  
1531 N N   . ASN A 202 ? 0.8958 1.4585 0.8710 -0.4906 -0.0776 0.0794  498 ASN A N   
1532 C CA  . ASN A 202 ? 0.9017 1.5222 0.9036 -0.4769 -0.0657 0.0814  498 ASN A CA  
1533 C C   . ASN A 202 ? 0.9103 1.6409 0.9144 -0.4999 -0.0596 0.0870  498 ASN A C   
1534 O O   . ASN A 202 ? 0.9214 1.6950 0.9308 -0.5011 -0.0500 0.0898  498 ASN A O   
1535 C CB  . ASN A 202 ? 0.9179 1.4375 0.8689 -0.4996 -0.0637 0.0847  498 ASN A CB  
1536 C CG  . ASN A 202 ? 0.8969 1.3119 0.8425 -0.4751 -0.0701 0.0791  498 ASN A CG  
1537 O OD1 . ASN A 202 ? 0.8471 1.2910 0.8512 -0.4278 -0.0705 0.0723  498 ASN A OD1 
1538 N ND2 . ASN A 202 ? 0.9703 1.2593 0.8384 -0.5052 -0.0759 0.0817  498 ASN A ND2 
1539 N N   . VAL A 203 ? 0.9324 1.7148 0.9325 -0.5179 -0.0651 0.0886  499 VAL A N   
1540 C CA  . VAL A 203 ? 0.9210 1.8041 0.9103 -0.5511 -0.0611 0.0948  499 VAL A CA  
1541 C C   . VAL A 203 ? 0.9370 1.9431 0.9881 -0.5025 -0.0508 0.0923  499 VAL A C   
1542 O O   . VAL A 203 ? 0.9379 2.0170 0.9818 -0.5211 -0.0437 0.0966  499 VAL A O   
1543 C CB  . VAL A 203 ? 0.9236 1.8336 0.8915 -0.5832 -0.0702 0.0973  499 VAL A CB  
1544 C CG1 . VAL A 203 ? 1.0416 2.0789 1.0076 -0.6118 -0.0662 0.1032  499 VAL A CG1 
1545 C CG2 . VAL A 203 ? 1.0118 1.7938 0.9006 -0.6365 -0.0797 0.1003  499 VAL A CG2 
1546 N N   . GLN A 204 ? 0.8604 1.8880 0.9662 -0.4386 -0.0505 0.0848  500 GLN A N   
1547 C CA  . GLN A 204 ? 0.8732 1.9972 1.0252 -0.3854 -0.0409 0.0812  500 GLN A CA  
1548 C C   . GLN A 204 ? 0.8612 1.9567 1.0151 -0.3738 -0.0314 0.0804  500 GLN A C   
1549 O O   . GLN A 204 ? 0.8554 2.0296 1.0175 -0.3651 -0.0220 0.0816  500 GLN A O   
1550 C CB  . GLN A 204 ? 0.9093 2.0456 1.1058 -0.3190 -0.0441 0.0733  500 GLN A CB  
1551 C CG  . GLN A 204 ? 0.8675 2.0981 1.0979 -0.2599 -0.0354 0.0691  500 GLN A CG  
1552 C CD  . GLN A 204 ? 0.9248 2.1387 1.1859 -0.1908 -0.0388 0.0610  500 GLN A CD  
1553 O OE1 . GLN A 204 ? 0.9238 2.0487 1.1911 -0.1731 -0.0423 0.0567  500 GLN A OE1 
1554 N NE2 . GLN A 204 ? 0.9729 2.2720 1.2481 -0.1514 -0.0383 0.0590  500 GLN A NE2 
1555 N N   . PHE A 205 ? 0.8714 1.8580 1.0157 -0.3738 -0.0338 0.0785  501 PHE A N   
1556 C CA  . PHE A 205 ? 0.8372 1.7951 0.9808 -0.3656 -0.0249 0.0783  501 PHE A CA  
1557 C C   . PHE A 205 ? 0.8669 1.8281 0.9632 -0.4242 -0.0204 0.0870  501 PHE A C   
1558 O O   . PHE A 205 ? 0.8283 1.8284 0.9305 -0.4161 -0.0100 0.0880  501 PHE A O   
1559 C CB  . PHE A 205 ? 0.8231 1.6670 0.9619 -0.3570 -0.0297 0.0751  501 PHE A CB  
1560 C CG  . PHE A 205 ? 0.8775 1.6934 1.0156 -0.3481 -0.0209 0.0752  501 PHE A CG  
1561 C CD1 . PHE A 205 ? 0.7997 1.6629 0.9815 -0.2908 -0.0130 0.0684  501 PHE A CD1 
1562 C CD2 . PHE A 205 ? 0.8761 1.6124 0.9614 -0.3961 -0.0206 0.0823  501 PHE A CD2 
1563 C CE1 . PHE A 205 ? 0.7406 1.5827 0.9208 -0.2833 -0.0045 0.0684  501 PHE A CE1 
1564 C CE2 . PHE A 205 ? 0.8301 1.5423 0.9125 -0.3888 -0.0120 0.0836  501 PHE A CE2 
1565 C CZ  . PHE A 205 ? 0.7709 1.5427 0.9045 -0.3335 -0.0035 0.0766  501 PHE A CZ  
1566 N N   . THR A 206 ? 0.9138 1.8285 0.9568 -0.4838 -0.0285 0.0932  502 THR A N   
1567 C CA  . THR A 206 ? 0.9692 1.8763 0.9559 -0.5429 -0.0262 0.1014  502 THR A CA  
1568 C C   . THR A 206 ? 0.9849 2.0319 0.9903 -0.5463 -0.0193 0.1037  502 THR A C   
1569 O O   . THR A 206 ? 0.9583 2.0298 0.9440 -0.5688 -0.0125 0.1078  502 THR A O   
1570 C CB  . THR A 206 ? 0.9997 1.8207 0.9146 -0.6041 -0.0379 0.1064  502 THR A CB  
1571 O OG1 . THR A 206 ? 1.0027 1.6890 0.8935 -0.5963 -0.0441 0.1038  502 THR A OG1 
1572 C CG2 . THR A 206 ? 1.0459 1.8515 0.8922 -0.6675 -0.0372 0.1145  502 THR A CG2 
1573 N N   . GLU A 207 ? 0.9830 2.1245 1.0247 -0.5219 -0.0213 0.1008  503 GLU A N   
1574 C CA  . GLU A 207 ? 0.9805 2.2631 1.0403 -0.5174 -0.0152 0.1024  503 GLU A CA  
1575 C C   . GLU A 207 ? 0.9194 2.2530 1.0221 -0.4570 -0.0034 0.0969  503 GLU A C   
1576 O O   . GLU A 207 ? 0.9419 2.3625 1.0435 -0.4631 0.0037  0.0993  503 GLU A O   
1577 C CB  . GLU A 207 ? 0.9997 2.3661 1.0824 -0.5026 -0.0207 0.1009  503 GLU A CB  
1578 C CG  . GLU A 207 ? 1.1440 2.4948 1.1779 -0.5714 -0.0308 0.1075  503 GLU A CG  
1579 C CD  . GLU A 207 ? 1.1943 2.5911 1.2525 -0.5510 -0.0375 0.1051  503 GLU A CD  
1580 O OE1 . GLU A 207 ? 1.1537 2.6004 1.2643 -0.4826 -0.0343 0.0985  503 GLU A OE1 
1581 O OE2 . GLU A 207 ? 1.2634 2.6410 1.2830 -0.6031 -0.0463 0.1097  503 GLU A OE2 
1582 N N   . ILE A 208 ? 0.8606 2.1409 0.9976 -0.3990 -0.0018 0.0893  504 ILE A N   
1583 C CA  . ILE A 208 ? 0.8155 2.1275 0.9845 -0.3402 0.0089  0.0832  504 ILE A CA  
1584 C C   . ILE A 208 ? 0.8394 2.1208 0.9829 -0.3702 0.0169  0.0876  504 ILE A C   
1585 O O   . ILE A 208 ? 0.8155 2.1700 0.9670 -0.3532 0.0264  0.0869  504 ILE A O   
1586 C CB  . ILE A 208 ? 0.7439 1.9897 0.9444 -0.2802 0.0070  0.0742  504 ILE A CB  
1587 C CG1 . ILE A 208 ? 0.6719 1.9733 0.9001 -0.2318 0.0024  0.0686  504 ILE A CG1 
1588 C CG2 . ILE A 208 ? 0.6989 1.9333 0.9143 -0.2362 0.0174  0.0686  504 ILE A CG2 
1589 C CD1 . ILE A 208 ? 0.7289 1.9545 0.9790 -0.1830 -0.0028 0.0606  504 ILE A CD1 
1590 N N   . CYS A 209 ? 0.8801 2.0491 0.9881 -0.4131 0.0130  0.0921  505 CYS A N   
1591 C CA  . CYS A 209 ? 0.8828 2.0112 0.9540 -0.4497 0.0195  0.0982  505 CYS A CA  
1592 C C   . CYS A 209 ? 0.9479 2.1582 0.9908 -0.4975 0.0213  0.1049  505 CYS A C   
1593 O O   . CYS A 209 ? 0.9470 2.1912 0.9841 -0.5008 0.0309  0.1070  505 CYS A O   
1594 C CB  . CYS A 209 ? 0.8995 1.8864 0.9211 -0.4920 0.0120  0.1030  505 CYS A CB  
1595 S SG  . CYS A 209 ? 0.8358 1.7287 0.8869 -0.4421 0.0096  0.0959  505 CYS A SG  
1596 N N   . ILE A 210 ? 0.9199 2.1667 0.9438 -0.5363 0.0121  0.1084  506 ILE A N   
1597 C CA  . ILE A 210 ? 0.9445 2.2783 0.9398 -0.5869 0.0123  0.1147  506 ILE A CA  
1598 C C   . ILE A 210 ? 0.8863 2.3669 0.9289 -0.5399 0.0213  0.1108  506 ILE A C   
1599 O O   . ILE A 210 ? 0.8450 2.3934 0.8751 -0.5626 0.0271  0.1145  506 ILE A O   
1600 C CB  . ILE A 210 ? 0.9568 2.2943 0.9170 -0.6400 -0.0002 0.1191  506 ILE A CB  
1601 C CG1 . ILE A 210 ? 1.0191 2.2007 0.9126 -0.6919 -0.0091 0.1232  506 ILE A CG1 
1602 C CG2 . ILE A 210 ? 0.9883 2.4432 0.9266 -0.6882 -0.0006 0.1248  506 ILE A CG2 
1603 C CD1 . ILE A 210 ? 1.1325 2.3008 0.9810 -0.7450 -0.0217 0.1269  506 ILE A CD1 
1604 N N   . GLN A 211 ? 0.8490 2.3754 0.9417 -0.4716 0.0222  0.1030  507 GLN A N   
1605 C CA  . GLN A 211 ? 0.8116 2.4609 0.9411 -0.4147 0.0302  0.0979  507 GLN A CA  
1606 C C   . GLN A 211 ? 0.8079 2.4422 0.9459 -0.3825 0.0421  0.0946  507 GLN A C   
1607 O O   . GLN A 211 ? 0.7573 2.4915 0.9045 -0.3627 0.0494  0.0937  507 GLN A O   
1608 C CB  . GLN A 211 ? 0.8039 2.4755 0.9722 -0.3453 0.0274  0.0896  507 GLN A CB  
1609 C CG  . GLN A 211 ? 0.8043 2.5369 0.9700 -0.3661 0.0180  0.0925  507 GLN A CG  
1610 C CD  . GLN A 211 ? 0.7922 2.6775 0.9758 -0.3303 0.0207  0.0908  507 GLN A CD  
1611 O OE1 . GLN A 211 ? 0.7958 2.7182 1.0025 -0.2601 0.0273  0.0836  507 GLN A OE1 
1612 N NE2 . GLN A 211 ? 0.7818 2.7551 0.9492 -0.3779 0.0152  0.0973  507 GLN A NE2 
1613 N N   . GLN A 212 ? 0.8327 2.3470 0.9663 -0.3760 0.0444  0.0930  508 GLN A N   
1614 C CA  . GLN A 212 ? 0.8458 2.3370 0.9818 -0.3510 0.0563  0.0906  508 GLN A CA  
1615 C C   . GLN A 212 ? 0.8656 2.3291 0.9575 -0.4185 0.0600  0.1002  508 GLN A C   
1616 O O   . GLN A 212 ? 0.8575 2.3019 0.9454 -0.4049 0.0710  0.0997  508 GLN A O   
1617 C CB  . GLN A 212 ? 0.8608 2.2441 1.0111 -0.3109 0.0574  0.0842  508 GLN A CB  
1618 C CG  . GLN A 212 ? 0.8432 2.2452 1.0320 -0.2378 0.0546  0.0734  508 GLN A CG  
1619 C CD  . GLN A 212 ? 0.8772 2.3869 1.0827 -0.1831 0.0611  0.0673  508 GLN A CD  
1620 O OE1 . GLN A 212 ? 0.8797 2.4135 1.0808 -0.1663 0.0715  0.0655  508 GLN A OE1 
1621 N NE2 . GLN A 212 ? 0.8610 2.4351 1.0811 -0.1540 0.0548  0.0643  508 GLN A NE2 
1622 N N   . GLY A 213 ? 0.9061 2.3610 0.9585 -0.4907 0.0510  0.1086  509 GLY A N   
1623 C CA  . GLY A 213 ? 0.8950 2.3275 0.8961 -0.5579 0.0527  0.1177  509 GLY A CA  
1624 C C   . GLY A 213 ? 0.9873 2.2725 0.9275 -0.6160 0.0448  0.1244  509 GLY A C   
1625 O O   . GLY A 213 ? 1.0529 2.2971 0.9402 -0.6691 0.0460  0.1317  509 GLY A O   
1626 N N   . TRP A 214 ? 1.0369 2.2365 0.9768 -0.6069 0.0360  0.1220  510 TRP A N   
1627 C CA  . TRP A 214 ? 1.1108 2.1619 0.9837 -0.6564 0.0274  0.1278  510 TRP A CA  
1628 C C   . TRP A 214 ? 1.1655 2.2169 0.9747 -0.7337 0.0172  0.1344  510 TRP A C   
1629 O O   . TRP A 214 ? 1.1145 2.2512 0.9362 -0.7469 0.0109  0.1336  510 TRP A O   
1630 C CB  . TRP A 214 ? 1.0674 2.0351 0.9526 -0.6299 0.0192  0.1234  510 TRP A CB  
1631 C CG  . TRP A 214 ? 1.1379 1.9404 0.9506 -0.6658 0.0116  0.1284  510 TRP A CG  
1632 C CD1 . TRP A 214 ? 1.1725 1.8832 0.9416 -0.6749 0.0168  0.1334  510 TRP A CD1 
1633 C CD2 . TRP A 214 ? 1.1823 1.8868 0.9498 -0.6922 -0.0028 0.1287  510 TRP A CD2 
1634 N NE1 . TRP A 214 ? 1.2335 1.7922 0.9301 -0.7016 0.0057  0.1366  510 TRP A NE1 
1635 C CE2 . TRP A 214 ? 1.2283 1.7799 0.9225 -0.7124 -0.0064 0.1331  510 TRP A CE2 
1636 C CE3 . TRP A 214 ? 1.1797 1.9078 0.9570 -0.6975 -0.0128 0.1257  510 TRP A CE3 
1637 C CZ2 . TRP A 214 ? 1.2562 1.6771 0.8846 -0.7342 -0.0201 0.1333  510 TRP A CZ2 
1638 C CZ3 . TRP A 214 ? 1.1928 1.7940 0.9084 -0.7236 -0.0255 0.1264  510 TRP A CZ3 
1639 C CH2 . TRP A 214 ? 1.2989 1.7476 0.9401 -0.7399 -0.0292 0.1295  510 TRP A CH2 
1640 N N   . LYS A 215 ? 1.2665 2.2226 1.0025 -0.7845 0.0156  0.1409  511 LYS A N   
1641 C CA  . LYS A 215 ? 1.3558 2.2809 1.0131 -0.8630 0.0043  0.1466  511 LYS A CA  
1642 C C   . LYS A 215 ? 1.3388 2.1120 0.9367 -0.8808 -0.0092 0.1463  511 LYS A C   
1643 O O   . LYS A 215 ? 1.3845 2.0151 0.9342 -0.8779 -0.0106 0.1477  511 LYS A O   
1644 C CB  . LYS A 215 ? 1.4340 2.3311 1.0358 -0.9069 0.0092  0.1530  511 LYS A CB  
1645 C CG  . LYS A 215 ? 1.4481 2.5005 1.1068 -0.8885 0.0230  0.1531  511 LYS A CG  
1646 C CD  . LYS A 215 ? 1.5199 2.6921 1.1618 -0.9459 0.0181  0.1563  511 LYS A CD  
1647 C CE  . LYS A 215 ? 1.4998 2.7870 1.1921 -0.9266 0.0126  0.1520  511 LYS A CE  
1648 N NZ  . LYS A 215 ? 1.6314 2.9636 1.2700 -1.0028 0.0009  0.1567  511 LYS A NZ  
1649 N N   . ALA A 216 ? 1.3765 2.1799 0.9755 -0.8950 -0.0189 0.1445  512 ALA A N   
1650 C CA  . ALA A 216 ? 1.3484 2.0237 0.9066 -0.8965 -0.0305 0.1425  512 ALA A CA  
1651 C C   . ALA A 216 ? 1.4755 2.0287 0.9147 -0.9683 -0.0430 0.1468  512 ALA A C   
1652 O O   . ALA A 216 ? 1.5045 2.1172 0.9059 -1.0270 -0.0473 0.1506  512 ALA A O   
1653 C CB  . ALA A 216 ? 1.3389 2.0960 0.9480 -0.8777 -0.0349 0.1388  512 ALA A CB  
1654 N N   . PRO A 217 ? 1.5390 1.9214 0.9118 -0.9645 -0.0494 0.1460  513 PRO A N   
1655 C CA  . PRO A 217 ? 1.6588 1.9081 0.9066 -1.0256 -0.0632 0.1480  513 PRO A CA  
1656 C C   . PRO A 217 ? 1.7467 1.9751 0.9666 -1.0442 -0.0751 0.1460  513 PRO A C   
1657 O O   . PRO A 217 ? 1.8655 1.9403 0.9911 -1.0605 -0.0864 0.1446  513 PRO A O   
1658 C CB  . PRO A 217 ? 1.7544 1.8305 0.9460 -0.9970 -0.0649 0.1467  513 PRO A CB  
1659 C CG  . PRO A 217 ? 1.6746 1.7858 0.9652 -0.9214 -0.0558 0.1433  513 PRO A CG  
1660 C CD  . PRO A 217 ? 1.5464 1.8487 0.9456 -0.9047 -0.0435 0.1436  513 PRO A CD  
1661 N N   . ARG A 218 ? 1.6982 2.0775 0.9933 -1.0399 -0.0725 0.1460  514 ARG A N   
1662 C CA  . ARG A 218 ? 1.6860 2.0749 0.9821 -1.0445 -0.0807 0.1444  514 ARG A CA  
1663 C C   . ARG A 218 ? 1.7699 1.9812 0.9573 -1.0687 -0.0943 0.1433  514 ARG A C   
1664 O O   . ARG A 218 ? 1.8962 2.0846 1.0053 -1.1292 -0.1040 0.1466  514 ARG A O   
1665 C CB  . ARG A 218 ? 1.7050 2.2370 1.0076 -1.0947 -0.0821 0.1490  514 ARG A CB  
1666 C CG  . ARG A 218 ? 1.5936 2.3151 1.0118 -1.0550 -0.0701 0.1483  514 ARG A CG  
1667 C CD  . ARG A 218 ? 1.5997 2.4436 1.0523 -1.0644 -0.0730 0.1494  514 ARG A CD  
1668 N NE  . ARG A 218 ? 1.5659 2.5337 1.1337 -0.9913 -0.0633 0.1447  514 ARG A NE  
1669 C CZ  . ARG A 218 ? 1.5219 2.6477 1.1498 -0.9744 -0.0544 0.1452  514 ARG A CZ  
1670 N NH1 . ARG A 218 ? 1.6059 2.8034 1.1982 -1.0291 -0.0539 0.1506  514 ARG A NH1 
1671 N NH2 . ARG A 218 ? 1.4662 2.6776 1.1871 -0.8999 -0.0464 0.1395  514 ARG A NH2 
1672 N N   . GLY A 219 ? 1.7924 1.8780 0.9699 -1.0209 -0.0951 0.1387  515 GLY A N   
1673 C CA  . GLY A 219 ? 1.9037 1.8220 0.9844 -1.0267 -0.1074 0.1359  515 GLY A CA  
1674 C C   . GLY A 219 ? 1.8643 1.7621 1.0034 -0.9654 -0.1076 0.1300  515 GLY A C   
1675 O O   . GLY A 219 ? 1.7506 1.7760 0.9998 -0.9316 -0.1006 0.1284  515 GLY A O   
1676 N N   . ARG A 220 ? 2.0004 1.7368 1.0631 -0.9476 -0.1161 0.1258  516 ARG A N   
1677 C CA  . ARG A 220 ? 1.9746 1.6807 1.0822 -0.8917 -0.1176 0.1195  516 ARG A CA  
1678 C C   . ARG A 220 ? 1.8963 1.5978 1.0724 -0.8274 -0.1093 0.1159  516 ARG A C   
1679 O O   . ARG A 220 ? 1.8067 1.6303 1.0972 -0.7943 -0.1006 0.1147  516 ARG A O   
1680 C CB  . ARG A 220 ? 2.1130 1.6515 1.1025 -0.8982 -0.1304 0.1162  516 ARG A CB  
1681 C CG  . ARG A 220 ? 2.0519 1.5614 1.0787 -0.8471 -0.1332 0.1094  516 ARG A CG  
1682 C CD  . ARG A 220 ? 2.0364 1.6094 1.0778 -0.8753 -0.1378 0.1106  516 ARG A CD  
1683 N NE  . ARG A 220 ? 2.1766 1.6102 1.1137 -0.8811 -0.1491 0.1077  516 ARG A NE  
1684 C CZ  . ARG A 220 ? 2.1937 1.6442 1.1395 -0.8858 -0.1541 0.1064  516 ARG A CZ  
1685 N NH1 . ARG A 220 ? 2.0806 1.6809 1.1330 -0.8852 -0.1497 0.1073  516 ARG A NH1 
1686 N NH2 . ARG A 220 ? 2.2985 1.6102 1.1400 -0.8876 -0.1639 0.1038  516 ARG A NH2 
1687 N N   . PHE A 221 ? 1.8618 1.4231 0.9641 -0.8081 -0.1122 0.1142  517 PHE A N   
1688 C CA  . PHE A 221 ? 1.7559 1.2899 0.9062 -0.7456 -0.1063 0.1112  517 PHE A CA  
1689 C C   . PHE A 221 ? 1.7405 1.3262 0.9214 -0.7476 -0.0956 0.1168  517 PHE A C   
1690 O O   . PHE A 221 ? 1.7907 1.2774 0.9147 -0.7321 -0.0955 0.1181  517 PHE A O   
1691 C CB  . PHE A 221 ? 1.8104 1.1676 0.8635 -0.7128 -0.1154 0.1059  517 PHE A CB  
1692 C CG  . PHE A 221 ? 1.8620 1.1644 0.8809 -0.7062 -0.1251 0.0999  517 PHE A CG  
1693 C CD1 . PHE A 221 ? 1.7475 1.1102 0.8546 -0.6690 -0.1234 0.0950  517 PHE A CD1 
1694 C CD2 . PHE A 221 ? 1.9841 1.1702 0.8769 -0.7375 -0.1359 0.0990  517 PHE A CD2 
1695 C CE1 . PHE A 221 ? 1.8190 1.1304 0.8936 -0.6620 -0.1317 0.0895  517 PHE A CE1 
1696 C CE2 . PHE A 221 ? 2.0409 1.1746 0.8983 -0.7302 -0.1440 0.0942  517 PHE A CE2 
1697 C CZ  . PHE A 221 ? 1.9185 1.1173 0.8693 -0.6921 -0.1415 0.0896  517 PHE A CZ  
1698 N N   . ASP A 222 ? 1.6493 1.3955 0.9193 -0.7634 -0.0863 0.1201  518 ASP A N   
1699 C CA  . ASP A 222 ? 1.5651 1.3866 0.8785 -0.7624 -0.0742 0.1251  518 ASP A CA  
1700 C C   . ASP A 222 ? 1.4613 1.3400 0.8745 -0.7025 -0.0646 0.1231  518 ASP A C   
1701 O O   . ASP A 222 ? 1.3472 1.3321 0.8487 -0.6816 -0.0619 0.1190  518 ASP A O   
1702 C CB  . ASP A 222 ? 1.5372 1.5071 0.8893 -0.8050 -0.0691 0.1286  518 ASP A CB  
1703 C CG  . ASP A 222 ? 1.6846 1.6112 0.9402 -0.8711 -0.0796 0.1310  518 ASP A CG  
1704 O OD1 . ASP A 222 ? 1.8017 1.5727 0.9511 -0.8844 -0.0899 0.1298  518 ASP A OD1 
1705 O OD2 . ASP A 222 ? 1.6799 1.7279 0.9611 -0.9082 -0.0779 0.1338  518 ASP A OD2 
1706 N N   . VAL A 223 ? 1.4562 1.2626 0.8502 -0.6745 -0.0602 0.1260  519 VAL A N   
1707 C CA  . VAL A 223 ? 1.3466 1.2045 0.8260 -0.6233 -0.0510 0.1254  519 VAL A CA  
1708 C C   . VAL A 223 ? 1.2488 1.2806 0.8233 -0.6251 -0.0379 0.1260  519 VAL A C   
1709 O O   . VAL A 223 ? 1.2615 1.3391 0.8214 -0.6535 -0.0310 0.1311  519 VAL A O   
1710 C CB  . VAL A 223 ? 1.4049 1.1535 0.8321 -0.5965 -0.0487 0.1315  519 VAL A CB  
1711 C CG1 . VAL A 223 ? 1.2686 1.0660 0.7809 -0.5248 -0.0439 0.1239  519 VAL A CG1 
1712 C CG2 . VAL A 223 ? 1.5374 1.1113 0.8531 -0.5894 -0.0630 0.1293  519 VAL A CG2 
1713 N N   . LEU A 224 ? 1.1338 1.2625 0.8022 -0.5910 -0.0352 0.1193  520 LEU A N   
1714 C CA  . LEU A 224 ? 1.0603 1.3493 0.8149 -0.5766 -0.0233 0.1174  520 LEU A CA  
1715 C C   . LEU A 224 ? 1.0349 1.3423 0.8129 -0.5507 -0.0097 0.1208  520 LEU A C   
1716 O O   . LEU A 224 ? 1.0828 1.2883 0.8370 -0.5063 -0.0143 0.1160  520 LEU A O   
1717 C CB  . LEU A 224 ? 0.9776 1.3519 0.8166 -0.5380 -0.0259 0.1078  520 LEU A CB  
1718 C CG  . LEU A 224 ? 1.0095 1.4188 0.8448 -0.5592 -0.0349 0.1054  520 LEU A CG  
1719 C CD1 . LEU A 224 ? 0.9325 1.3224 0.8062 -0.5235 -0.0433 0.0972  520 LEU A CD1 
1720 C CD2 . LEU A 224 ? 0.9552 1.5155 0.8380 -0.5597 -0.0279 0.1054  520 LEU A CD2 
1721 N N   . PRO A 225 ? 0.9762 1.4025 0.7953 -0.5475 0.0024  0.1210  521 PRO A N   
1722 C CA  . PRO A 225 ? 0.9564 1.4058 0.8008 -0.5070 0.0146  0.1195  521 PRO A CA  
1723 C C   . PRO A 225 ? 0.8940 1.3844 0.8150 -0.4291 0.0129  0.1036  521 PRO A C   
1724 O O   . PRO A 225 ? 0.8464 1.3888 0.8142 -0.4153 0.0077  0.0975  521 PRO A O   
1725 C CB  . PRO A 225 ? 0.9736 1.5421 0.8321 -0.5314 0.0270  0.1237  521 PRO A CB  
1726 C CG  . PRO A 225 ? 0.9548 1.6040 0.8423 -0.5411 0.0185  0.1183  521 PRO A CG  
1727 C CD  . PRO A 225 ? 0.9956 1.5320 0.8297 -0.5716 0.0032  0.1201  521 PRO A CD  
1728 N N   . LEU A 226 ? 0.8738 1.3343 0.8003 -0.3805 0.0166  0.0974  522 LEU A N   
1729 C CA  . LEU A 226 ? 0.8240 1.3214 0.8129 -0.3121 0.0165  0.0828  522 LEU A CA  
1730 C C   . LEU A 226 ? 0.7537 1.3923 0.7958 -0.2977 0.0295  0.0800  522 LEU A C   
1731 O O   . LEU A 226 ? 0.7760 1.4727 0.8069 -0.3197 0.0422  0.0867  522 LEU A O   
1732 C CB  . LEU A 226 ? 0.8188 1.2391 0.7899 -0.2708 0.0151  0.0767  522 LEU A CB  
1733 C CG  . LEU A 226 ? 0.8343 1.1252 0.7599 -0.2647 0.0017  0.0766  522 LEU A CG  
1734 C CD1 . LEU A 226 ? 0.8587 1.0973 0.7629 -0.2318 0.0014  0.0731  522 LEU A CD1 
1735 C CD2 . LEU A 226 ? 0.8328 1.1067 0.7930 -0.2356 -0.0087 0.0670  522 LEU A CD2 
1736 N N   . LEU A 227 ? 0.7079 1.4016 0.8032 -0.2585 0.0264  0.0704  523 LEU A N   
1737 C CA  . LEU A 227 ? 0.6547 1.4699 0.7968 -0.2229 0.0371  0.0645  523 LEU A CA  
1738 C C   . LEU A 227 ? 0.6562 1.4269 0.8139 -0.1544 0.0347  0.0500  523 LEU A C   
1739 O O   . LEU A 227 ? 0.6068 1.3385 0.7814 -0.1264 0.0243  0.0427  523 LEU A O   
1740 C CB  . LEU A 227 ? 0.6041 1.5181 0.7857 -0.2290 0.0343  0.0654  523 LEU A CB  
1741 C CG  . LEU A 227 ? 0.6162 1.6345 0.7956 -0.2487 0.0411  0.0703  523 LEU A CG  
1742 C CD1 . LEU A 227 ? 0.6578 1.7346 0.8634 -0.2190 0.0337  0.0649  523 LEU A CD1 
1743 C CD2 . LEU A 227 ? 0.6426 1.7187 0.8239 -0.2222 0.0560  0.0677  523 LEU A CD2 
1744 N N   . LEU A 228 ? 0.6557 1.4287 0.8021 -0.1315 0.0441  0.0461  524 LEU A N   
1745 C CA  . LEU A 228 ? 0.6497 1.3600 0.7946 -0.0780 0.0407  0.0328  524 LEU A CA  
1746 C C   . LEU A 228 ? 0.6438 1.4327 0.8082 -0.0286 0.0511  0.0231  524 LEU A C   
1747 O O   . LEU A 228 ? 0.6484 1.5137 0.8095 -0.0342 0.0651  0.0266  524 LEU A O   
1748 C CB  . LEU A 228 ? 0.6810 1.3089 0.7849 -0.0894 0.0400  0.0346  524 LEU A CB  
1749 C CG  . LEU A 228 ? 0.7157 1.2659 0.7871 -0.1349 0.0308  0.0454  524 LEU A CG  
1750 C CD1 . LEU A 228 ? 0.7064 1.1810 0.7328 -0.1390 0.0296  0.0478  524 LEU A CD1 
1751 C CD2 . LEU A 228 ? 0.6744 1.1677 0.7594 -0.1236 0.0165  0.0406  524 LEU A CD2 
1752 N N   . GLN A 229 ? 0.6187 1.3841 0.7968 0.0200  0.0445  0.0113  525 GLN A N   
1753 C CA  . GLN A 229 ? 0.6352 1.4462 0.8177 0.0779  0.0515  -0.0002 525 GLN A CA  
1754 C C   . GLN A 229 ? 0.6450 1.3563 0.7981 0.1101  0.0464  -0.0128 525 GLN A C   
1755 O O   . GLN A 229 ? 0.6423 1.2675 0.7907 0.1111  0.0335  -0.0169 525 GLN A O   
1756 C CB  . GLN A 229 ? 0.6008 1.4535 0.8089 0.1082  0.0462  -0.0033 525 GLN A CB  
1757 C CG  . GLN A 229 ? 0.6243 1.4614 0.8188 0.1781  0.0462  -0.0178 525 GLN A CG  
1758 C CD  . GLN A 229 ? 0.7021 1.5622 0.9131 0.2079  0.0384  -0.0193 525 GLN A CD  
1759 O OE1 . GLN A 229 ? 0.6361 1.5223 0.8729 0.1746  0.0320  -0.0102 525 GLN A OE1 
1760 N NE2 . GLN A 229 ? 0.7590 1.6017 0.9475 0.2718  0.0382  -0.0308 525 GLN A NE2 
1761 N N   . ALA A 230 ? 0.6889 1.4160 0.8207 0.1336  0.0566  -0.0191 526 ALA A N   
1762 C CA  . ALA A 230 ? 0.7214 1.3598 0.8191 0.1605  0.0518  -0.0319 526 ALA A CA  
1763 C C   . ALA A 230 ? 0.7650 1.4191 0.8447 0.2223  0.0571  -0.0460 526 ALA A C   
1764 O O   . ALA A 230 ? 0.7566 1.5054 0.8420 0.2446  0.0710  -0.0456 526 ALA A O   
1765 C CB  . ALA A 230 ? 0.7207 1.3436 0.7942 0.1370  0.0574  -0.0288 526 ALA A CB  
1766 N N   . ASN A 231 ? 0.8072 1.3677 0.8601 0.2493  0.0460  -0.0583 527 ASN A N   
1767 C CA  . ASN A 231 ? 0.8614 1.3990 0.8762 0.3096  0.0481  -0.0734 527 ASN A CA  
1768 C C   . ASN A 231 ? 0.9005 1.5299 0.9322 0.3495  0.0559  -0.0721 527 ASN A C   
1769 O O   . ASN A 231 ? 0.9098 1.5804 0.9174 0.4003  0.0663  -0.0805 527 ASN A O   
1770 C CB  . ASN A 231 ? 0.8794 1.4064 0.8549 0.3271  0.0567  -0.0826 527 ASN A CB  
1771 C CG  . ASN A 231 ? 0.9576 1.4050 0.8734 0.3806  0.0528  -0.1010 527 ASN A CG  
1772 O OD1 . ASN A 231 ? 1.0131 1.3653 0.9060 0.3812  0.0386  -0.1072 527 ASN A OD1 
1773 N ND2 . ASN A 231 ? 1.0137 1.4963 0.8973 0.4250  0.0657  -0.1100 527 ASN A ND2 
1774 N N   . GLY A 232 ? 0.9247 1.5901 0.9961 0.3290  0.0504  -0.0618 528 GLY A N   
1775 C CA  . GLY A 232 ? 0.9260 1.6871 1.0181 0.3637  0.0549  -0.0593 528 GLY A CA  
1776 C C   . GLY A 232 ? 0.9088 1.7884 1.0177 0.3497  0.0667  -0.0500 528 GLY A C   
1777 O O   . GLY A 232 ? 0.9351 1.8727 1.0456 0.3655  0.0642  -0.0454 528 GLY A O   
1778 N N   . ASN A 233 ? 0.8078 1.7234 0.9241 0.3185  0.0786  -0.0465 529 ASN A N   
1779 C CA  . ASN A 233 ? 0.8084 1.8319 0.9363 0.2957  0.0885  -0.0360 529 ASN A CA  
1780 C C   . ASN A 233 ? 0.7782 1.8652 0.9458 0.2367  0.0849  -0.0199 529 ASN A C   
1781 O O   . ASN A 233 ? 0.7470 1.7926 0.9351 0.2069  0.0769  -0.0159 529 ASN A O   
1782 C CB  . ASN A 233 ? 0.7880 1.8194 0.9029 0.2757  0.1025  -0.0360 529 ASN A CB  
1783 C CG  . ASN A 233 ? 0.7726 1.7503 0.8397 0.3326  0.1065  -0.0523 529 ASN A CG  
1784 O OD1 . ASN A 233 ? 0.8199 1.8418 0.8673 0.3672  0.1097  -0.0547 529 ASN A OD1 
1785 N ND2 . ASN A 233 ? 0.7841 1.6523 0.8245 0.3370  0.1015  -0.0626 529 ASN A ND2 
1786 N N   . ASP A 234 ? 0.7561 1.9429 0.9302 0.2191  0.0895  -0.0111 530 ASP A N   
1787 C CA  . ASP A 234 ? 0.7323 1.9762 0.9322 0.1575  0.0856  0.0033  530 ASP A CA  
1788 C C   . ASP A 234 ? 0.6906 1.8882 0.8979 0.0940  0.0876  0.0118  530 ASP A C   
1789 O O   . ASP A 234 ? 0.7042 1.8712 0.8968 0.0884  0.0974  0.0102  530 ASP A O   
1790 C CB  . ASP A 234 ? 0.7777 2.1362 0.9762 0.1414  0.0915  0.0108  530 ASP A CB  
1791 C CG  . ASP A 234 ? 0.8572 2.2760 1.0476 0.2019  0.0878  0.0047  530 ASP A CG  
1792 O OD1 . ASP A 234 ? 0.8656 2.2375 1.0510 0.2459  0.0792  -0.0026 530 ASP A OD1 
1793 O OD2 . ASP A 234 ? 0.9032 2.4178 1.0889 0.2048  0.0933  0.0078  530 ASP A OD2 
1794 N N   . PRO A 235 ? 0.6568 1.8431 0.8797 0.0468  0.0785  0.0208  531 PRO A N   
1795 C CA  . PRO A 235 ? 0.6369 1.7646 0.8577 -0.0097 0.0782  0.0291  531 PRO A CA  
1796 C C   . PRO A 235 ? 0.6425 1.8073 0.8437 -0.0751 0.0856  0.0430  531 PRO A C   
1797 O O   . PRO A 235 ? 0.6571 1.9023 0.8559 -0.0888 0.0867  0.0475  531 PRO A O   
1798 C CB  . PRO A 235 ? 0.6108 1.7055 0.8480 -0.0276 0.0631  0.0320  531 PRO A CB  
1799 C CG  . PRO A 235 ? 0.6141 1.7860 0.8569 -0.0170 0.0596  0.0330  531 PRO A CG  
1800 C CD  . PRO A 235 ? 0.6907 1.9042 0.9276 0.0479  0.0669  0.0229  531 PRO A CD  
1801 N N   . GLU A 236 ? 0.6429 1.7401 0.8227 -0.1167 0.0888  0.0502  532 GLU A N   
1802 C CA  . GLU A 236 ? 0.6585 1.7659 0.8038 -0.1760 0.0978  0.0636  532 GLU A CA  
1803 C C   . GLU A 236 ? 0.6863 1.6948 0.7967 -0.2388 0.0870  0.0754  532 GLU A C   
1804 O O   . GLU A 236 ? 0.6940 1.5890 0.7946 -0.2230 0.0722  0.0701  532 GLU A O   
1805 C CB  . GLU A 236 ? 0.6851 1.7618 0.8032 -0.1512 0.1087  0.0592  532 GLU A CB  
1806 C CG  . GLU A 236 ? 0.6604 1.8274 0.7989 -0.0896 0.1200  0.0473  532 GLU A CG  
1807 C CD  . GLU A 236 ? 0.7633 1.8611 0.8773 -0.0416 0.1236  0.0352  532 GLU A CD  
1808 O OE1 . GLU A 236 ? 0.6649 1.6965 0.7394 -0.0692 0.1250  0.0408  532 GLU A OE1 
1809 O OE2 . GLU A 236 ? 0.8039 1.8996 0.9297 0.0242  0.1217  0.0195  532 GLU A OE2 
1810 N N   . LEU A 237 ? 0.7193 1.7471 0.7978 -0.3043 0.0893  0.0890  533 LEU A N   
1811 C CA  . LEU A 237 ? 0.7650 1.6997 0.7991 -0.3669 0.0790  0.1007  533 LEU A CA  
1812 C C   . LEU A 237 ? 0.8337 1.6505 0.8037 -0.3860 0.0803  0.1080  533 LEU A C   
1813 O O   . LEU A 237 ? 0.8503 1.6935 0.7992 -0.3921 0.0935  0.1124  533 LEU A O   
1814 C CB  . LEU A 237 ? 0.8092 1.7841 0.8201 -0.4210 0.0714  0.1072  533 LEU A CB  
1815 C CG  . LEU A 237 ? 0.8001 1.8461 0.8480 -0.4095 0.0609  0.1012  533 LEU A CG  
1816 C CD1 . LEU A 237 ? 0.8705 1.9711 0.8886 -0.4660 0.0561  0.1082  533 LEU A CD1 
1817 C CD2 . LEU A 237 ? 0.7738 1.7369 0.8235 -0.4106 0.0483  0.0997  533 LEU A CD2 
1818 N N   . PHE A 238 ? 0.8888 1.5694 0.8229 -0.3888 0.0642  0.1080  534 PHE A N   
1819 C CA  . PHE A 238 ? 0.9613 1.5142 0.8224 -0.4040 0.0601  0.1152  534 PHE A CA  
1820 C C   . PHE A 238 ? 1.0428 1.4825 0.8502 -0.4419 0.0452  0.1224  534 PHE A C   
1821 O O   . PHE A 238 ? 0.9584 1.3796 0.7935 -0.4236 0.0339  0.1148  534 PHE A O   
1822 C CB  . PHE A 238 ? 0.9329 1.4211 0.8012 -0.3369 0.0548  0.1026  534 PHE A CB  
1823 C CG  . PHE A 238 ? 0.8541 1.4348 0.7729 -0.2883 0.0661  0.0912  534 PHE A CG  
1824 C CD1 . PHE A 238 ? 0.8107 1.4524 0.7926 -0.2432 0.0644  0.0776  534 PHE A CD1 
1825 C CD2 . PHE A 238 ? 0.8643 1.4606 0.7584 -0.2854 0.0780  0.0937  534 PHE A CD2 
1826 C CE1 . PHE A 238 ? 0.7755 1.4864 0.7899 -0.1945 0.0741  0.0663  534 PHE A CE1 
1827 C CE2 . PHE A 238 ? 0.8149 1.4870 0.7460 -0.2374 0.0883  0.0817  534 PHE A CE2 
1828 C CZ  . PHE A 238 ? 0.7608 1.4864 0.7494 -0.1908 0.0861  0.0677  534 PHE A CZ  
1829 N N   . GLN A 239 ? 1.2040 1.5609 0.9269 -0.4931 0.0452  0.1369  535 GLN A N   
1830 C CA  . GLN A 239 ? 1.2582 1.4822 0.9069 -0.5262 0.0308  0.1439  535 GLN A CA  
1831 C C   . GLN A 239 ? 1.3140 1.4063 0.9230 -0.4745 0.0194  0.1389  535 GLN A C   
1832 O O   . GLN A 239 ? 1.3186 1.3755 0.8920 -0.4622 0.0235  0.1429  535 GLN A O   
1833 C CB  . GLN A 239 ? 1.3505 1.5387 0.9161 -0.6045 0.0334  0.1598  535 GLN A CB  
1834 C CG  . GLN A 239 ? 1.4927 1.5049 0.9558 -0.6233 0.0164  0.1639  535 GLN A CG  
1835 C CD  . GLN A 239 ? 1.6387 1.5913 1.0171 -0.6736 0.0123  0.1686  535 GLN A CD  
1836 O OE1 . GLN A 239 ? 1.6965 1.5330 0.9973 -0.6674 0.0096  0.1748  535 GLN A OE1 
1837 N NE2 . GLN A 239 ? 1.7212 1.7532 1.1097 -0.7224 0.0105  0.1655  535 GLN A NE2 
1838 N N   . ILE A 240 ? 1.2030 1.2293 0.8163 -0.4448 0.0051  0.1306  536 ILE A N   
1839 C CA  . ILE A 240 ? 1.2490 1.1548 0.8196 -0.3985 -0.0073 0.1266  536 ILE A CA  
1840 C C   . ILE A 240 ? 1.3636 1.1445 0.8155 -0.4388 -0.0110 0.1421  536 ILE A C   
1841 O O   . ILE A 240 ? 1.4001 1.1362 0.7954 -0.4965 -0.0135 0.1515  536 ILE A O   
1842 C CB  . ILE A 240 ? 1.2208 1.0900 0.8145 -0.3670 -0.0202 0.1160  536 ILE A CB  
1843 C CG1 . ILE A 240 ? 1.1319 1.1179 0.8333 -0.3334 -0.0165 0.1024  536 ILE A CG1 
1844 C CG2 . ILE A 240 ? 1.2175 0.9796 0.7698 -0.3160 -0.0324 0.1116  536 ILE A CG2 
1845 C CD1 . ILE A 240 ? 1.0626 1.0939 0.7922 -0.3630 -0.0183 0.1017  536 ILE A CD1 
1846 N N   . PRO A 241 ? 1.3521 1.0708 0.7566 -0.4136 -0.0120 0.1458  537 PRO A N   
1847 C CA  . PRO A 241 ? 1.4552 1.0379 0.7328 -0.4476 -0.0169 0.1616  537 PRO A CA  
1848 C C   . PRO A 241 ? 1.5072 0.9684 0.7173 -0.4510 -0.0318 0.1620  537 PRO A C   
1849 O O   . PRO A 241 ? 1.4868 0.9215 0.7233 -0.3917 -0.0425 0.1497  537 PRO A O   
1850 C CB  . PRO A 241 ? 1.4259 0.9625 0.6802 -0.3921 -0.0208 0.1601  537 PRO A CB  
1851 C CG  . PRO A 241 ? 1.3272 0.9984 0.6981 -0.3494 -0.0132 0.1456  537 PRO A CG  
1852 C CD  . PRO A 241 ? 1.2769 1.0251 0.7318 -0.3458 -0.0133 0.1342  537 PRO A CD  
1853 N N   . PRO A 242 ? 1.5620 0.9589 0.6925 -0.5177 -0.0332 0.1719  538 PRO A N   
1854 C CA  . PRO A 242 ? 1.6222 0.9281 0.7090 -0.5159 -0.0482 0.1630  538 PRO A CA  
1855 C C   . PRO A 242 ? 1.6866 0.8516 0.6995 -0.4530 -0.0621 0.1599  538 PRO A C   
1856 O O   . PRO A 242 ? 1.6718 0.7830 0.6723 -0.4265 -0.0724 0.1518  538 PRO A O   
1857 C CB  . PRO A 242 ? 1.6617 0.9420 0.6877 -0.5834 -0.0516 0.1601  538 PRO A CB  
1858 C CG  . PRO A 242 ? 1.6444 1.0525 0.7231 -0.6245 -0.0363 0.1668  538 PRO A CG  
1859 C CD  . PRO A 242 ? 1.5573 0.9919 0.6669 -0.5786 -0.0262 0.1745  538 PRO A CD  
1860 N N   . GLU A 243 ? 1.6895 0.8029 0.6570 -0.4225 -0.0629 0.1649  539 GLU A N   
1861 C CA  . GLU A 243 ? 1.7392 0.7414 0.6471 -0.3509 -0.0767 0.1600  539 GLU A CA  
1862 C C   . GLU A 243 ? 1.6927 0.7508 0.6805 -0.2835 -0.0809 0.1522  539 GLU A C   
1863 O O   . GLU A 243 ? 1.7393 0.7194 0.6862 -0.2233 -0.0935 0.1465  539 GLU A O   
1864 C CB  . GLU A 243 ? 1.8969 0.8565 0.7533 -0.3314 -0.0765 0.1658  539 GLU A CB  
1865 C CG  . GLU A 243 ? 1.7584 0.8212 0.6808 -0.3158 -0.0665 0.1751  539 GLU A CG  
1866 C CD  . GLU A 243 ? 1.6778 0.8109 0.6129 -0.3813 -0.0502 0.1836  539 GLU A CD  
1867 O OE1 . GLU A 243 ? 1.6588 0.8465 0.6214 -0.4423 -0.0425 0.1829  539 GLU A OE1 
1868 O OE2 . GLU A 243 ? 1.6748 0.8191 0.5967 -0.3700 -0.0454 0.1897  539 GLU A OE2 
1869 N N   . LEU A 244 ? 1.5829 0.7969 0.7027 -0.2839 -0.0709 0.1427  540 LEU A N   
1870 C CA  . LEU A 244 ? 1.4829 0.7781 0.7047 -0.2240 -0.0742 0.1254  540 LEU A CA  
1871 C C   . LEU A 244 ? 1.4701 0.7795 0.7250 -0.2335 -0.0767 0.1177  540 LEU A C   
1872 O O   . LEU A 244 ? 1.4125 0.7646 0.7317 -0.1844 -0.0809 0.1046  540 LEU A O   
1873 C CB  . LEU A 244 ? 1.3856 0.8257 0.7202 -0.2166 -0.0631 0.1185  540 LEU A CB  
1874 C CG  . LEU A 244 ? 1.3890 0.8414 0.7179 -0.1910 -0.0614 0.1206  540 LEU A CG  
1875 C CD1 . LEU A 244 ? 1.2282 0.8144 0.6721 -0.1678 -0.0540 0.1078  540 LEU A CD1 
1876 C CD2 . LEU A 244 ? 1.4143 0.7709 0.6765 -0.1348 -0.0761 0.1202  540 LEU A CD2 
1877 N N   . VAL A 245 ? 1.5086 0.7861 0.7194 -0.2979 -0.0745 0.1257  541 VAL A N   
1878 C CA  . VAL A 245 ? 1.5163 0.8056 0.7519 -0.3124 -0.0777 0.1190  541 VAL A CA  
1879 C C   . VAL A 245 ? 1.5834 0.7129 0.7003 -0.3009 -0.0907 0.1207  541 VAL A C   
1880 O O   . VAL A 245 ? 1.6651 0.6984 0.6806 -0.3510 -0.0936 0.1294  541 VAL A O   
1881 C CB  . VAL A 245 ? 1.5042 0.8642 0.7634 -0.3899 -0.0693 0.1255  541 VAL A CB  
1882 C CG1 . VAL A 245 ? 1.4628 0.8403 0.7505 -0.4016 -0.0743 0.1178  541 VAL A CG1 
1883 C CG2 . VAL A 245 ? 1.3850 0.8974 0.7493 -0.3919 -0.0559 0.1237  541 VAL A CG2 
1884 N N   . LEU A 246 ? 1.6007 0.7103 0.7325 -0.2323 -0.0985 0.1091  542 LEU A N   
1885 C CA  . LEU A 246 ? 1.6777 0.6402 0.6978 -0.2068 -0.1105 0.1083  542 LEU A CA  
1886 C C   . LEU A 246 ? 1.7025 0.6488 0.7153 -0.2430 -0.1129 0.1041  542 LEU A C   
1887 O O   . LEU A 246 ? 1.6021 0.6548 0.7181 -0.2336 -0.1094 0.0940  542 LEU A O   
1888 C CB  . LEU A 246 ? 1.6753 0.6407 0.7176 -0.1161 -0.1169 0.0971  542 LEU A CB  
1889 C CG  . LEU A 246 ? 1.7614 0.6078 0.7110 -0.0698 -0.1278 0.0901  542 LEU A CG  
1890 C CD1 . LEU A 246 ? 1.8402 0.5782 0.6749 -0.0751 -0.1317 0.0864  542 LEU A CD1 
1891 C CD2 . LEU A 246 ? 1.7539 0.6468 0.7522 0.0176  -0.1321 0.0802  542 LEU A CD2 
1892 N N   . GLU A 247 ? 1.7602 0.6214 0.6802 -0.2740 -0.1181 0.0982  543 GLU A N   
1893 C CA  . GLU A 247 ? 1.8155 0.6670 0.7200 -0.3087 -0.1219 0.0908  543 GLU A CA  
1894 C C   . GLU A 247 ? 1.9165 0.6438 0.7157 -0.2667 -0.1323 0.0783  543 GLU A C   
1895 O O   . GLU A 247 ? 1.9243 0.5632 0.6397 -0.2358 -0.1366 0.0755  543 GLU A O   
1896 C CB  . GLU A 247 ? 1.8429 0.7241 0.7292 -0.3955 -0.1193 0.0960  543 GLU A CB  
1897 C CG  . GLU A 247 ? 1.7568 0.7897 0.7609 -0.4367 -0.1080 0.1048  543 GLU A CG  
1898 C CD  . GLU A 247 ? 1.8583 0.9365 0.8454 -0.5125 -0.1043 0.1103  543 GLU A CD  
1899 O OE1 . GLU A 247 ? 1.9198 0.9474 0.8449 -0.5256 -0.1037 0.1146  543 GLU A OE1 
1900 O OE2 . GLU A 247 ? 1.8464 1.0162 0.8825 -0.5570 -0.1026 0.1100  543 GLU A OE2 
1901 N N   . VAL A 248 ? 1.8923 0.6170 0.6955 -0.2635 -0.1359 0.0706  544 VAL A N   
1902 C CA  . VAL A 248 ? 2.0304 0.6507 0.7396 -0.2223 -0.1443 0.0586  544 VAL A CA  
1903 C C   . VAL A 248 ? 2.0767 0.6549 0.7181 -0.2868 -0.1496 0.0576  544 VAL A C   
1904 O O   . VAL A 248 ? 2.0232 0.6755 0.7289 -0.3228 -0.1478 0.0592  544 VAL A O   
1905 C CB  . VAL A 248 ? 1.9910 0.6476 0.7608 -0.1560 -0.1438 0.0505  544 VAL A CB  
1906 C CG1 . VAL A 248 ? 2.0651 0.6209 0.7330 -0.1142 -0.1510 0.0386  544 VAL A CG1 
1907 C CG2 . VAL A 248 ? 1.9054 0.6149 0.7425 -0.0941 -0.1399 0.0524  544 VAL A CG2 
1908 N N   . PRO A 249 ? 2.1888 0.6526 0.6996 -0.3056 -0.1568 0.0554  545 PRO A N   
1909 C CA  . PRO A 249 ? 2.2772 0.6881 0.7074 -0.3605 -0.1640 0.0545  545 PRO A CA  
1910 C C   . PRO A 249 ? 2.3002 0.6722 0.7077 -0.3140 -0.1682 0.0457  545 PRO A C   
1911 O O   . PRO A 249 ? 2.3338 0.6475 0.7036 -0.2389 -0.1699 0.0374  545 PRO A O   
1912 C CB  . PRO A 249 ? 2.4362 0.7173 0.7202 -0.3788 -0.1713 0.0534  545 PRO A CB  
1913 C CG  . PRO A 249 ? 2.4405 0.6848 0.7156 -0.3059 -0.1695 0.0492  545 PRO A CG  
1914 C CD  . PRO A 249 ? 2.2840 0.6624 0.7116 -0.2832 -0.1592 0.0547  545 PRO A CD  
1915 N N   . ILE A 250 ? 2.3095 0.7241 0.7443 -0.3564 -0.1695 0.0476  546 ILE A N   
1916 C CA  . ILE A 250 ? 2.2840 0.6800 0.7150 -0.3171 -0.1721 0.0403  546 ILE A CA  
1917 C C   . ILE A 250 ? 2.4461 0.7039 0.7203 -0.3286 -0.1824 0.0378  546 ILE A C   
1918 O O   . ILE A 250 ? 2.5055 0.7404 0.7231 -0.4017 -0.1874 0.0442  546 ILE A O   
1919 C CB  . ILE A 250 ? 2.2254 0.7404 0.7700 -0.3526 -0.1682 0.0433  546 ILE A CB  
1920 C CG1 . ILE A 250 ? 2.1152 0.7623 0.8037 -0.3500 -0.1585 0.0471  546 ILE A CG1 
1921 C CG2 . ILE A 250 ? 2.2022 0.6993 0.7485 -0.3055 -0.1700 0.0348  546 ILE A CG2 
1922 C CD1 . ILE A 250 ? 2.0303 0.6883 0.7698 -0.2679 -0.1541 0.0407  546 ILE A CD1 
1923 N N   . ARG A 251 ? 2.5429 0.7120 0.7437 -0.2554 -0.1857 0.0289  547 ARG A N   
1924 C CA  . ARG A 251 ? 2.6851 0.7160 0.7314 -0.2522 -0.1955 0.0261  547 ARG A CA  
1925 C C   . ARG A 251 ? 2.7047 0.7310 0.7598 -0.1880 -0.1950 0.0189  547 ARG A C   
1926 O O   . ARG A 251 ? 2.5926 0.7040 0.7534 -0.1310 -0.1876 0.0136  547 ARG A O   
1927 C CB  . ARG A 251 ? 2.8404 0.7443 0.7525 -0.2228 -0.2010 0.0222  547 ARG A CB  
1928 C CG  . ARG A 251 ? 2.8074 0.7160 0.7420 -0.1250 -0.1968 0.0133  547 ARG A CG  
1929 C CD  . ARG A 251 ? 2.6966 0.6919 0.7319 -0.1245 -0.1894 0.0161  547 ARG A CD  
1930 N NE  . ARG A 251 ? 2.7144 0.6850 0.7293 -0.0423 -0.1881 0.0088  547 ARG A NE  
1931 C CZ  . ARG A 251 ? 2.6279 0.6696 0.7260 -0.0251 -0.1820 0.0110  547 ARG A CZ  
1932 N NH1 . ARG A 251 ? 2.4928 0.6381 0.7059 -0.0781 -0.1756 0.0203  547 ARG A NH1 
1933 N NH2 . ARG A 251 ? 2.6667 0.6743 0.7255 0.0466  -0.1826 0.0044  547 ARG A NH2 
1934 N N   . HIS A 252 ? 2.8026 0.7294 0.7425 -0.1995 -0.2031 0.0192  548 HIS A N   
1935 C CA  . HIS A 252 ? 2.8885 0.7996 0.8209 -0.1341 -0.2028 0.0125  548 HIS A CA  
1936 C C   . HIS A 252 ? 3.0213 0.8112 0.8270 -0.0631 -0.2070 0.0060  548 HIS A C   
1937 O O   . HIS A 252 ? 3.0972 0.7876 0.7993 -0.0815 -0.2122 0.0075  548 HIS A O   
1938 C CB  . HIS A 252 ? 2.8414 0.7351 0.7478 -0.1824 -0.2075 0.0172  548 HIS A CB  
1939 C CG  . HIS A 252 ? 2.8797 0.8079 0.8343 -0.1250 -0.2039 0.0106  548 HIS A CG  
1940 N ND1 . HIS A 252 ? 2.9577 0.7807 0.7982 -0.0752 -0.2091 0.0072  548 HIS A ND1 
1941 C CD2 . HIS A 252 ? 2.6946 0.7496 0.7953 -0.1068 -0.1953 0.0062  548 HIS A CD2 
1942 C CE1 . HIS A 252 ? 2.8514 0.7414 0.7705 -0.0303 -0.2034 0.0012  548 HIS A CE1 
1943 N NE2 . HIS A 252 ? 2.6978 0.7263 0.7731 -0.0493 -0.1951 -0.0002 548 HIS A NE2 
1944 N N   . PRO A 253 ? 2.9506 0.7573 0.7744 0.0211  -0.2036 -0.0019 549 PRO A N   
1945 C CA  . PRO A 253 ? 3.0848 0.7956 0.8048 0.0956  -0.2061 -0.0083 549 PRO A CA  
1946 C C   . PRO A 253 ? 3.2584 0.8401 0.8467 0.0856  -0.2140 -0.0069 549 PRO A C   
1947 O O   . PRO A 253 ? 3.3989 0.8763 0.8749 0.1331  -0.2182 -0.0107 549 PRO A O   
1948 C CB  . PRO A 253 ? 2.9825 0.7860 0.7851 0.1841  -0.1987 -0.0163 549 PRO A CB  
1949 C CG  . PRO A 253 ? 2.8604 0.7695 0.7791 0.1503  -0.1942 -0.0141 549 PRO A CG  
1950 C CD  . PRO A 253 ? 2.8037 0.7448 0.7725 0.0580  -0.1946 -0.0062 549 PRO A CD  
1951 N N   . LYS A 254 ? 3.2409 0.8239 0.8346 0.0269  -0.2167 -0.0016 550 LYS A N   
1952 C CA  . LYS A 254 ? 3.4145 0.8706 0.8786 0.0065  -0.2251 0.0009  550 LYS A CA  
1953 C C   . LYS A 254 ? 3.4925 0.8961 0.9000 -0.0979 -0.2320 0.0103  550 LYS A C   
1954 O O   . LYS A 254 ? 3.6812 0.9489 0.9479 -0.1154 -0.2403 0.0121  550 LYS A O   
1955 C CB  . LYS A 254 ? 3.4171 0.9038 0.9132 0.0253  -0.2238 -0.0005 550 LYS A CB  
1956 C CG  . LYS A 254 ? 3.3961 0.9609 0.9656 0.1206  -0.2159 -0.0091 550 LYS A CG  
1957 C CD  . LYS A 254 ? 3.5392 1.0250 1.0145 0.2074  -0.2172 -0.0158 550 LYS A CD  
1958 C CE  . LYS A 254 ? 3.5164 1.0957 1.0666 0.2998  -0.2091 -0.0236 550 LYS A CE  
1959 N NZ  . LYS A 254 ? 3.6196 1.1274 1.0720 0.3876  -0.2110 -0.0295 550 LYS A NZ  
1960 N N   . PHE A 255 ? 3.3594 0.8689 0.8689 -0.1680 -0.2291 0.0165  551 PHE A N   
1961 C CA  . PHE A 255 ? 3.4172 0.9062 0.8888 -0.2709 -0.2351 0.0263  551 PHE A CA  
1962 C C   . PHE A 255 ? 3.4600 0.9433 0.9144 -0.3175 -0.2357 0.0302  551 PHE A C   
1963 O O   . PHE A 255 ? 3.3339 0.9332 0.8996 -0.3401 -0.2296 0.0324  551 PHE A O   
1964 C CB  . PHE A 255 ? 3.2936 0.9104 0.8844 -0.3193 -0.2319 0.0314  551 PHE A CB  
1965 C CG  . PHE A 255 ? 3.2683 0.8903 0.8751 -0.2797 -0.2316 0.0278  551 PHE A CG  
1966 C CD1 . PHE A 255 ? 3.3662 0.9027 0.8801 -0.3115 -0.2392 0.0312  551 PHE A CD1 
1967 C CD2 . PHE A 255 ? 3.1589 0.8718 0.8717 -0.2135 -0.2238 0.0211  551 PHE A CD2 
1968 C CE1 . PHE A 255 ? 3.3451 0.8857 0.8728 -0.2753 -0.2388 0.0278  551 PHE A CE1 
1969 C CE2 . PHE A 255 ? 3.1149 0.8349 0.8417 -0.1782 -0.2231 0.0176  551 PHE A CE2 
1970 C CZ  . PHE A 255 ? 3.1968 0.8302 0.8318 -0.2081 -0.2305 0.0208  551 PHE A CZ  
1971 N N   . ASP A 256 ? 3.6375 0.9818 0.9470 -0.3333 -0.2432 0.0311  552 ASP A N   
1972 C CA  . ASP A 256 ? 3.6769 1.0062 0.9600 -0.3751 -0.2439 0.0341  552 ASP A CA  
1973 C C   . ASP A 256 ? 3.6191 1.0327 0.9541 -0.4806 -0.2440 0.0443  552 ASP A C   
1974 O O   . ASP A 256 ? 3.5764 1.0377 0.9465 -0.5136 -0.2411 0.0469  552 ASP A O   
1975 C CB  . ASP A 256 ? 3.9120 1.0643 1.0173 -0.3705 -0.2527 0.0327  552 ASP A CB  
1976 C CG  . ASP A 256 ? 3.9929 1.0912 1.0641 -0.2732 -0.2508 0.0234  552 ASP A CG  
1977 O OD1 . ASP A 256 ? 4.0318 1.0932 1.0773 -0.1945 -0.2509 0.0169  552 ASP A OD1 
1978 O OD2 . ASP A 256 ? 4.0128 1.1115 1.0841 -0.2748 -0.2491 0.0226  552 ASP A OD2 
1979 N N   . TRP A 257 ? 3.6187 1.0575 0.9599 -0.5332 -0.2471 0.0502  553 TRP A N   
1980 C CA  . TRP A 257 ? 3.5452 1.0927 0.9531 -0.6273 -0.2461 0.0600  553 TRP A CA  
1981 C C   . TRP A 257 ? 3.3173 1.0369 0.8969 -0.6167 -0.2362 0.0601  553 TRP A C   
1982 O O   . TRP A 257 ? 3.2437 1.0695 0.8893 -0.6862 -0.2340 0.0679  553 TRP A O   
1983 C CB  . TRP A 257 ? 3.5963 1.1371 0.9732 -0.6808 -0.2518 0.0662  553 TRP A CB  
1984 C CG  . TRP A 257 ? 3.5193 1.0827 0.9474 -0.6213 -0.2497 0.0613  553 TRP A CG  
1985 C CD1 . TRP A 257 ? 3.6337 1.0789 0.9692 -0.5700 -0.2545 0.0560  553 TRP A CD1 
1986 C CD2 . TRP A 257 ? 3.3216 1.0339 0.9021 -0.6055 -0.2423 0.0610  553 TRP A CD2 
1987 N NE1 . TRP A 257 ? 3.5111 1.0262 0.9348 -0.5245 -0.2502 0.0523  553 TRP A NE1 
1988 C CE2 . TRP A 257 ? 3.3266 1.0021 0.8989 -0.5466 -0.2430 0.0552  553 TRP A CE2 
1989 C CE3 . TRP A 257 ? 3.1834 1.0545 0.9017 -0.6350 -0.2354 0.0651  553 TRP A CE3 
1990 C CZ2 . TRP A 257 ? 3.2120 0.9998 0.9068 -0.5191 -0.2373 0.0532  553 TRP A CZ2 
1991 C CZ3 . TRP A 257 ? 3.0515 1.0378 0.9039 -0.6044 -0.2290 0.0618  553 TRP A CZ3 
1992 C CH2 . TRP A 257 ? 3.0470 0.9904 0.8874 -0.5484 -0.2300 0.0555  553 TRP A CH2 
1993 N N   . PHE A 258 ? 3.2108 0.9623 0.8605 -0.5314 -0.2304 0.0520  554 PHE A N   
1994 C CA  . PHE A 258 ? 3.0557 0.9612 0.8611 -0.5201 -0.2219 0.0521  554 PHE A CA  
1995 C C   . PHE A 258 ? 3.0376 0.9988 0.8876 -0.5462 -0.2174 0.0545  554 PHE A C   
1996 O O   . PHE A 258 ? 2.9296 1.0357 0.9153 -0.5782 -0.2098 0.0588  554 PHE A O   
1997 C CB  . PHE A 258 ? 2.9483 0.8686 0.8134 -0.4218 -0.2164 0.0419  554 PHE A CB  
1998 C CG  . PHE A 258 ? 2.7549 0.8348 0.7989 -0.4119 -0.2068 0.0403  554 PHE A CG  
1999 C CD1 . PHE A 258 ? 2.6281 0.8159 0.7927 -0.4040 -0.1981 0.0400  554 PHE A CD1 
2000 C CD2 . PHE A 258 ? 2.7427 0.8601 0.8292 -0.4114 -0.2069 0.0392  554 PHE A CD2 
2001 C CE1 . PHE A 258 ? 2.4835 0.8108 0.8037 -0.3952 -0.1901 0.0384  554 PHE A CE1 
2002 C CE2 . PHE A 258 ? 2.5182 0.7763 0.7616 -0.4028 -0.1989 0.0364  554 PHE A CE2 
2003 C CZ  . PHE A 258 ? 2.4460 0.8073 0.8040 -0.3947 -0.1908 0.0360  554 PHE A CZ  
2004 N N   . LYS A 259 ? 3.0778 0.9317 0.8272 -0.5307 -0.2205 0.0515  555 LYS A N   
2005 C CA  . LYS A 259 ? 3.1542 1.0482 0.9273 -0.5633 -0.2174 0.0545  555 LYS A CA  
2006 C C   . LYS A 259 ? 3.1759 1.1302 0.9528 -0.6669 -0.2191 0.0651  555 LYS A C   
2007 O O   . LYS A 259 ? 3.1022 1.1626 0.9661 -0.7000 -0.2127 0.0694  555 LYS A O   
2008 C CB  . LYS A 259 ? 3.2326 0.9899 0.8870 -0.5319 -0.2211 0.0494  555 LYS A CB  
2009 C CG  . LYS A 259 ? 3.3204 0.9821 0.9186 -0.4347 -0.2225 0.0396  555 LYS A CG  
2010 C CD  . LYS A 259 ? 3.4418 0.9585 0.9026 -0.4130 -0.2278 0.0359  555 LYS A CD  
2011 C CE  . LYS A 259 ? 3.5957 1.0005 0.9662 -0.3327 -0.2318 0.0282  555 LYS A CE  
2012 N NZ  . LYS A 259 ? 3.4760 0.9679 0.9522 -0.2544 -0.2252 0.0219  555 LYS A NZ  
2013 N N   . ASP A 260 ? 3.2285 1.1267 0.9246 -0.7164 -0.2261 0.0696  556 ASP A N   
2014 C CA  . ASP A 260 ? 3.2639 1.2239 0.9568 -0.8159 -0.2282 0.0799  556 ASP A CA  
2015 C C   . ASP A 260 ? 3.0697 1.2173 0.9191 -0.8411 -0.2208 0.0854  556 ASP A C   
2016 O O   . ASP A 260 ? 3.0201 1.2667 0.9108 -0.9104 -0.2184 0.0931  556 ASP A O   
2017 C CB  . ASP A 260 ? 3.3806 1.2362 0.9497 -0.8607 -0.2378 0.0836  556 ASP A CB  
2018 C CG  . ASP A 260 ? 3.6010 1.2831 1.0065 -0.8667 -0.2454 0.0814  556 ASP A CG  
2019 O OD1 . ASP A 260 ? 3.6336 1.3050 1.0219 -0.8784 -0.2439 0.0810  556 ASP A OD1 
2020 O OD2 . ASP A 260 ? 3.7602 1.3129 1.0501 -0.8592 -0.2533 0.0800  556 ASP A OD2 
2021 N N   . LEU A 261 ? 3.0061 1.2141 0.9603 -0.7811 -0.2153 0.0805  557 LEU A N   
2022 C CA  . LEU A 261 ? 2.8246 1.2169 0.9539 -0.7883 -0.2056 0.0832  557 LEU A CA  
2023 C C   . LEU A 261 ? 2.7944 1.2854 1.0123 -0.7954 -0.1968 0.0853  557 LEU A C   
2024 O O   . LEU A 261 ? 2.6831 1.3256 1.0117 -0.8316 -0.1903 0.0910  557 LEU A O   
2025 C CB  . LEU A 261 ? 2.7043 1.1240 0.9192 -0.7134 -0.2014 0.0752  557 LEU A CB  
2026 C CG  . LEU A 261 ? 2.7427 1.0928 0.8916 -0.7116 -0.2088 0.0740  557 LEU A CG  
2027 C CD1 . LEU A 261 ? 2.6043 0.9727 0.8279 -0.6341 -0.2048 0.0644  557 LEU A CD1 
2028 C CD2 . LEU A 261 ? 2.7389 1.1797 0.9182 -0.7889 -0.2106 0.0828  557 LEU A CD2 
2029 N N   . GLY A 262 ? 3.0031 1.4109 1.1695 -0.7600 -0.1966 0.0809  558 GLY A N   
2030 C CA  . GLY A 262 ? 2.9356 1.4235 1.1742 -0.7672 -0.1885 0.0836  558 GLY A CA  
2031 C C   . GLY A 262 ? 2.7224 1.3505 1.1303 -0.7236 -0.1770 0.0826  558 GLY A C   
2032 O O   . GLY A 262 ? 2.6835 1.4313 1.1827 -0.7481 -0.1689 0.0880  558 GLY A O   
2033 N N   . LEU A 263 ? 2.4994 1.1152 0.9468 -0.6600 -0.1763 0.0756  559 LEU A N   
2034 C CA  . LEU A 263 ? 2.2732 1.0064 0.8693 -0.6165 -0.1667 0.0735  559 LEU A CA  
2035 C C   . LEU A 263 ? 2.2386 0.9426 0.8491 -0.5611 -0.1617 0.0706  559 LEU A C   
2036 O O   . LEU A 263 ? 2.2935 0.8706 0.7986 -0.5305 -0.1667 0.0663  559 LEU A O   
2037 C CB  . LEU A 263 ? 2.2431 0.9777 0.8739 -0.5745 -0.1683 0.0666  559 LEU A CB  
2038 C CG  . LEU A 263 ? 2.2187 0.9927 0.8442 -0.6295 -0.1729 0.0704  559 LEU A CG  
2039 C CD1 . LEU A 263 ? 2.1701 0.9168 0.8019 -0.5895 -0.1761 0.0629  559 LEU A CD1 
2040 C CD2 . LEU A 263 ? 2.0725 1.0164 0.8183 -0.6744 -0.1660 0.0772  559 LEU A CD2 
2041 N N   . LYS A 264 ? 2.0510 0.8757 0.7897 -0.5484 -0.1519 0.0733  560 LYS A N   
2042 C CA  . LYS A 264 ? 2.0356 0.8520 0.8073 -0.4934 -0.1464 0.0721  560 LYS A CA  
2043 C C   . LYS A 264 ? 1.8724 0.8218 0.7906 -0.4737 -0.1376 0.0733  560 LYS A C   
2044 O O   . LYS A 264 ? 1.7924 0.8502 0.7865 -0.5100 -0.1349 0.0755  560 LYS A O   
2045 C CB  . LYS A 264 ? 2.0380 0.8348 0.7688 -0.5208 -0.1440 0.0787  560 LYS A CB  
2046 C CG  . LYS A 264 ? 1.9988 0.9224 0.7978 -0.5874 -0.1370 0.0881  560 LYS A CG  
2047 C CD  . LYS A 264 ? 2.0349 0.9535 0.8203 -0.5956 -0.1316 0.0941  560 LYS A CD  
2048 C CE  . LYS A 264 ? 2.0590 1.0464 0.8385 -0.6740 -0.1292 0.1015  560 LYS A CE  
2049 N NZ  . LYS A 264 ? 2.0067 1.0289 0.8075 -0.6813 -0.1206 0.1083  560 LYS A NZ  
2050 N N   . TRP A 265 ? 1.8113 0.7513 0.7644 -0.4126 -0.1339 0.0712  561 TRP A N   
2051 C CA  . TRP A 265 ? 1.6807 0.7355 0.7619 -0.3950 -0.1263 0.0726  561 TRP A CA  
2052 C C   . TRP A 265 ? 1.6763 0.7229 0.7722 -0.3563 -0.1213 0.0778  561 TRP A C   
2053 O O   . TRP A 265 ? 1.7287 0.6778 0.7393 -0.3284 -0.1249 0.0774  561 TRP A O   
2054 C CB  . TRP A 265 ? 1.6118 0.6742 0.7343 -0.3528 -0.1292 0.0626  561 TRP A CB  
2055 C CG  . TRP A 265 ? 1.4706 0.6767 0.7265 -0.3588 -0.1232 0.0616  561 TRP A CG  
2056 C CD1 . TRP A 265 ? 1.3684 0.6621 0.7213 -0.2968 -0.1166 0.0548  561 TRP A CD1 
2057 C CD2 . TRP A 265 ? 1.4257 0.7363 0.7407 -0.4174 -0.1218 0.0648  561 TRP A CD2 
2058 N NE1 . TRP A 265 ? 1.2957 0.7264 0.7562 -0.3110 -0.1112 0.0534  561 TRP A NE1 
2059 C CE2 . TRP A 265 ? 1.3180 0.7663 0.7598 -0.3804 -0.1143 0.0595  561 TRP A CE2 
2060 C CE3 . TRP A 265 ? 1.4755 0.8114 0.7601 -0.4745 -0.1237 0.0691  561 TRP A CE3 
2061 C CZ2 . TRP A 265 ? 1.2558 0.8297 0.7771 -0.4124 -0.1120 0.0606  561 TRP A CZ2 
2062 C CZ3 . TRP A 265 ? 1.3978 0.8707 0.7684 -0.5058 -0.1206 0.0707  561 TRP A CZ3 
2063 C CH2 . TRP A 265 ? 1.2865 0.8670 0.7696 -0.4813 -0.1164 0.0669  561 TRP A CH2 
2064 N N   . TYR A 266 ? 1.5471 0.7160 0.7571 -0.3483 -0.1130 0.0799  562 TYR A N   
2065 C CA  . TYR A 266 ? 1.4978 0.6989 0.7442 -0.3004 -0.1074 0.0805  562 TYR A CA  
2066 C C   . TYR A 266 ? 1.4483 0.6584 0.7337 -0.2193 -0.1094 0.0683  562 TYR A C   
2067 O O   . TYR A 266 ? 1.3658 0.6187 0.7012 -0.2029 -0.1101 0.0593  562 TYR A O   
2068 C CB  . TYR A 266 ? 1.3950 0.7455 0.7503 -0.3199 -0.0963 0.0831  562 TYR A CB  
2069 C CG  . TYR A 266 ? 1.2818 0.7542 0.7405 -0.3255 -0.0930 0.0760  562 TYR A CG  
2070 C CD1 . TYR A 266 ? 1.1985 0.7439 0.7456 -0.2691 -0.0905 0.0655  562 TYR A CD1 
2071 C CD2 . TYR A 266 ? 1.3001 0.8143 0.7626 -0.3888 -0.0933 0.0804  562 TYR A CD2 
2072 C CE1 . TYR A 266 ? 1.1393 0.7826 0.7689 -0.2723 -0.0881 0.0601  562 TYR A CE1 
2073 C CE2 . TYR A 266 ? 1.2247 0.8479 0.7755 -0.3886 -0.0916 0.0745  562 TYR A CE2 
2074 C CZ  . TYR A 266 ? 1.1485 0.8293 0.7792 -0.3286 -0.0891 0.0646  562 TYR A CZ  
2075 O OH  . TYR A 266 ? 1.0876 0.8661 0.7968 -0.3260 -0.0880 0.0597  562 TYR A OH  
2076 N N   . GLY A 267 ? 1.4107 0.5873 0.6731 -0.1699 -0.1104 0.0687  563 GLY A N   
2077 C CA  . GLY A 267 ? 1.3726 0.5609 0.6630 -0.0953 -0.1130 0.0578  563 GLY A CA  
2078 C C   . GLY A 267 ? 1.2653 0.5981 0.6879 -0.0714 -0.1059 0.0500  563 GLY A C   
2079 O O   . GLY A 267 ? 1.2714 0.6336 0.7299 -0.0252 -0.1070 0.0404  563 GLY A O   
2080 N N   . LEU A 268 ? 1.1550 0.5761 0.6448 -0.1030 -0.0985 0.0540  564 LEU A N   
2081 C CA  . LEU A 268 ? 1.0706 0.6072 0.6657 -0.0762 -0.0928 0.0472  564 LEU A CA  
2082 C C   . LEU A 268 ? 1.0050 0.6321 0.6808 -0.1016 -0.0874 0.0436  564 LEU A C   
2083 O O   . LEU A 268 ? 0.9782 0.6495 0.6743 -0.1444 -0.0823 0.0494  564 LEU A O   
2084 C CB  . LEU A 268 ? 1.0230 0.5897 0.6298 -0.0806 -0.0886 0.0525  564 LEU A CB  
2085 C CG  . LEU A 268 ? 0.9600 0.6269 0.6588 -0.0495 -0.0847 0.0441  564 LEU A CG  
2086 C CD1 . LEU A 268 ? 1.0282 0.6804 0.7215 0.0064  -0.0914 0.0369  564 LEU A CD1 
2087 C CD2 . LEU A 268 ? 0.9575 0.6637 0.6731 -0.0616 -0.0792 0.0483  564 LEU A CD2 
2088 N N   . PRO A 269 ? 0.9907 0.6527 0.7129 -0.0748 -0.0882 0.0347  565 PRO A N   
2089 C CA  . PRO A 269 ? 0.9069 0.6543 0.7045 -0.0916 -0.0838 0.0316  565 PRO A CA  
2090 C C   . PRO A 269 ? 0.7998 0.6312 0.6719 -0.0732 -0.0782 0.0277  565 PRO A C   
2091 O O   . PRO A 269 ? 0.7761 0.6204 0.6699 -0.0361 -0.0791 0.0213  565 PRO A O   
2092 C CB  . PRO A 269 ? 0.9137 0.6455 0.7128 -0.0698 -0.0872 0.0247  565 PRO A CB  
2093 C CG  . PRO A 269 ? 0.9457 0.6377 0.7154 -0.0219 -0.0901 0.0203  565 PRO A CG  
2094 C CD  . PRO A 269 ? 0.9872 0.6125 0.6886 -0.0270 -0.0929 0.0276  565 PRO A CD  
2095 N N   . ALA A 270 ? 0.7732 0.6638 0.6809 -0.0983 -0.0726 0.0309  566 ALA A N   
2096 C CA  . ALA A 270 ? 0.7276 0.6799 0.6869 -0.0809 -0.0675 0.0271  566 ALA A CA  
2097 C C   . ALA A 270 ? 0.7084 0.7346 0.7201 -0.0942 -0.0627 0.0263  566 ALA A C   
2098 O O   . ALA A 270 ? 0.7127 0.7694 0.7222 -0.1229 -0.0586 0.0323  566 ALA A O   
2099 C CB  . ALA A 270 ? 0.7512 0.6886 0.6807 -0.0868 -0.0651 0.0324  566 ALA A CB  
2100 N N   . VAL A 271 ? 0.6760 0.7319 0.7302 -0.0730 -0.0631 0.0194  567 VAL A N   
2101 C CA  . VAL A 271 ? 0.6470 0.7642 0.7434 -0.0761 -0.0601 0.0182  567 VAL A CA  
2102 C C   . VAL A 271 ? 0.6220 0.7823 0.7427 -0.0633 -0.0542 0.0156  567 VAL A C   
2103 O O   . VAL A 271 ? 0.6196 0.7698 0.7475 -0.0412 -0.0544 0.0096  567 VAL A O   
2104 C CB  . VAL A 271 ? 0.6334 0.7523 0.7539 -0.0581 -0.0630 0.0127  567 VAL A CB  
2105 C CG1 . VAL A 271 ? 0.6052 0.7777 0.7629 -0.0485 -0.0603 0.0104  567 VAL A CG1 
2106 C CG2 . VAL A 271 ? 0.6278 0.7166 0.7251 -0.0740 -0.0679 0.0155  567 VAL A CG2 
2107 N N   . SER A 272 ? 0.6275 0.8412 0.7603 -0.0765 -0.0492 0.0193  568 SER A N   
2108 C CA  . SER A 272 ? 0.6119 0.8655 0.7595 -0.0619 -0.0424 0.0165  568 SER A CA  
2109 C C   . SER A 272 ? 0.5802 0.8946 0.7600 -0.0437 -0.0393 0.0131  568 SER A C   
2110 O O   . SER A 272 ? 0.5883 0.9363 0.7750 -0.0269 -0.0331 0.0099  568 SER A O   
2111 C CB  . SER A 272 ? 0.6243 0.8913 0.7481 -0.0879 -0.0368 0.0241  568 SER A CB  
2112 O OG  . SER A 272 ? 0.6733 0.9665 0.7884 -0.1239 -0.0366 0.0324  568 SER A OG  
2113 N N   . ASN A 273 ? 0.5671 0.8933 0.7614 -0.0420 -0.0438 0.0133  569 ASN A N   
2114 C CA  . ASN A 273 ? 0.5373 0.9198 0.7550 -0.0197 -0.0422 0.0111  569 ASN A CA  
2115 C C   . ASN A 273 ? 0.5415 0.8890 0.7634 0.0112  -0.0462 0.0041  569 ASN A C   
2116 O O   . ASN A 273 ? 0.5538 0.9323 0.7850 0.0346  -0.0467 0.0025  569 ASN A O   
2117 C CB  . ASN A 273 ? 0.5394 0.9744 0.7673 -0.0413 -0.0450 0.0179  569 ASN A CB  
2118 C CG  . ASN A 273 ? 0.5480 0.9354 0.7666 -0.0575 -0.0534 0.0195  569 ASN A CG  
2119 O OD1 . ASN A 273 ? 0.5410 0.8627 0.7480 -0.0503 -0.0560 0.0158  569 ASN A OD1 
2120 N ND2 . ASN A 273 ? 0.5913 1.0184 0.8141 -0.0793 -0.0577 0.0246  569 ASN A ND2 
2121 N N   . MET A 274 ? 0.5589 0.8449 0.7702 0.0116  -0.0494 0.0003  570 MET A N   
2122 C CA  . MET A 274 ? 0.5560 0.8086 0.7660 0.0313  -0.0529 -0.0051 570 MET A CA  
2123 C C   . MET A 274 ? 0.6088 0.8422 0.8073 0.0525  -0.0506 -0.0129 570 MET A C   
2124 O O   . MET A 274 ? 0.5880 0.8337 0.7819 0.0538  -0.0464 -0.0146 570 MET A O   
2125 C CB  . MET A 274 ? 0.5803 0.7894 0.7857 0.0179  -0.0573 -0.0050 570 MET A CB  
2126 C CG  . MET A 274 ? 0.5825 0.7997 0.7906 0.0012  -0.0605 0.0011  570 MET A CG  
2127 S SD  . MET A 274 ? 0.5510 0.7217 0.7505 -0.0049 -0.0643 0.0000  570 MET A SD  
2128 C CE  . MET A 274 ? 0.5662 0.7281 0.7703 0.0116  -0.0656 -0.0027 570 MET A CE  
2129 N N   . LEU A 275 ? 0.6003 0.7981 0.7870 0.0675  -0.0538 -0.0175 571 LEU A N   
2130 C CA  . LEU A 275 ? 0.6481 0.8126 0.8112 0.0852  -0.0534 -0.0257 571 LEU A CA  
2131 C C   . LEU A 275 ? 0.6645 0.7805 0.8168 0.0691  -0.0579 -0.0295 571 LEU A C   
2132 O O   . LEU A 275 ? 0.6391 0.7377 0.7927 0.0599  -0.0610 -0.0269 571 LEU A O   
2133 C CB  . LEU A 275 ? 0.6701 0.8246 0.8130 0.1165  -0.0540 -0.0280 571 LEU A CB  
2134 C CG  . LEU A 275 ? 0.7105 0.8253 0.8162 0.1391  -0.0530 -0.0376 571 LEU A CG  
2135 C CD1 . LEU A 275 ? 0.7386 0.8844 0.8322 0.1800  -0.0491 -0.0392 571 LEU A CD1 
2136 C CD2 . LEU A 275 ? 0.7814 0.8173 0.8499 0.1342  -0.0591 -0.0421 571 LEU A CD2 
2137 N N   . LEU A 276 ? 0.6483 0.7495 0.7897 0.0646  -0.0581 -0.0355 572 LEU A N   
2138 C CA  . LEU A 276 ? 0.6758 0.7462 0.8079 0.0469  -0.0630 -0.0397 572 LEU A CA  
2139 C C   . LEU A 276 ? 0.7524 0.7710 0.8452 0.0528  -0.0658 -0.0473 572 LEU A C   
2140 O O   . LEU A 276 ? 0.7496 0.7532 0.8186 0.0689  -0.0646 -0.0536 572 LEU A O   
2141 C CB  . LEU A 276 ? 0.6773 0.7644 0.8167 0.0373  -0.0638 -0.0417 572 LEU A CB  
2142 C CG  . LEU A 276 ? 0.6805 0.7535 0.8107 0.0210  -0.0698 -0.0477 572 LEU A CG  
2143 C CD1 . LEU A 276 ? 0.6516 0.7268 0.7925 0.0053  -0.0721 -0.0449 572 LEU A CD1 
2144 C CD2 . LEU A 276 ? 0.6228 0.7202 0.7604 0.0191  -0.0714 -0.0482 572 LEU A CD2 
2145 N N   . GLU A 277 ? 0.7215 0.7075 0.8005 0.0390  -0.0693 -0.0467 573 GLU A N   
2146 C CA  . GLU A 277 ? 0.8000 0.7195 0.8282 0.0368  -0.0731 -0.0526 573 GLU A CA  
2147 C C   . GLU A 277 ? 0.8133 0.7220 0.8329 0.0010  -0.0780 -0.0571 573 GLU A C   
2148 O O   . GLU A 277 ? 0.7931 0.7304 0.8378 -0.0215 -0.0784 -0.0528 573 GLU A O   
2149 C CB  . GLU A 277 ? 0.8533 0.7402 0.8630 0.0424  -0.0738 -0.0471 573 GLU A CB  
2150 C CG  . GLU A 277 ? 0.9529 0.7740 0.9046 0.0701  -0.0756 -0.0510 573 GLU A CG  
2151 C CD  . GLU A 277 ? 1.0811 0.8196 0.9747 0.0481  -0.0808 -0.0522 573 GLU A CD  
2152 O OE1 . GLU A 277 ? 1.0718 0.7865 0.9465 0.0137  -0.0842 -0.0577 573 GLU A OE1 
2153 O OE2 . GLU A 277 ? 1.1798 0.8780 1.0432 0.0631  -0.0821 -0.0471 573 GLU A OE2 
2154 N N   . ILE A 278 ? 0.8749 0.7475 0.8575 -0.0040 -0.0818 -0.0663 574 ILE A N   
2155 C CA  . ILE A 278 ? 0.8764 0.7443 0.8464 -0.0418 -0.0881 -0.0716 574 ILE A CA  
2156 C C   . ILE A 278 ? 0.9881 0.7683 0.8842 -0.0504 -0.0935 -0.0803 574 ILE A C   
2157 O O   . ILE A 278 ? 1.0119 0.7584 0.8767 -0.0242 -0.0932 -0.0871 574 ILE A O   
2158 C CB  . ILE A 278 ? 0.8267 0.7505 0.8278 -0.0443 -0.0898 -0.0749 574 ILE A CB  
2159 C CG1 . ILE A 278 ? 0.7587 0.7521 0.8175 -0.0362 -0.0857 -0.0664 574 ILE A CG1 
2160 C CG2 . ILE A 278 ? 0.8574 0.7836 0.8425 -0.0831 -0.0981 -0.0813 574 ILE A CG2 
2161 C CD1 . ILE A 278 ? 0.7142 0.7507 0.7942 -0.0283 -0.0869 -0.0678 574 ILE A CD1 
2162 N N   . GLY A 279 ? 1.0001 0.7407 0.8625 -0.0880 -0.0980 -0.0800 575 GLY A N   
2163 C CA  . GLY A 279 ? 1.0945 0.7337 0.8711 -0.1040 -0.1045 -0.0879 575 GLY A CA  
2164 C C   . GLY A 279 ? 1.1612 0.7232 0.8845 -0.0565 -0.1025 -0.0905 575 GLY A C   
2165 O O   . GLY A 279 ? 1.2546 0.7391 0.9083 -0.0503 -0.1071 -0.1007 575 GLY A O   
2166 N N   . GLY A 280 ? 1.1398 0.7235 0.8911 -0.0203 -0.0962 -0.0820 576 GLY A N   
2167 C CA  . GLY A 280 ? 1.1911 0.7224 0.8989 0.0325  -0.0942 -0.0839 576 GLY A CA  
2168 C C   . GLY A 280 ? 1.1393 0.7170 0.8715 0.0741  -0.0891 -0.0892 576 GLY A C   
2169 O O   . GLY A 280 ? 1.1791 0.7371 0.8850 0.1241  -0.0860 -0.0905 576 GLY A O   
2170 N N   . LEU A 281 ? 1.0886 0.7305 0.8673 0.0571  -0.0880 -0.0919 577 LEU A N   
2171 C CA  . LEU A 281 ? 1.0717 0.7692 0.8802 0.0907  -0.0815 -0.0943 577 LEU A CA  
2172 C C   . LEU A 281 ? 0.9894 0.7772 0.8720 0.1023  -0.0745 -0.0828 577 LEU A C   
2173 O O   . LEU A 281 ? 0.9607 0.7846 0.8857 0.0747  -0.0754 -0.0752 577 LEU A O   
2174 C CB  . LEU A 281 ? 1.0482 0.7686 0.8666 0.0666  -0.0843 -0.1011 577 LEU A CB  
2175 C CG  . LEU A 281 ? 1.1389 0.7723 0.8809 0.0476  -0.0929 -0.1136 577 LEU A CG  
2176 C CD1 . LEU A 281 ? 1.0756 0.7425 0.8304 0.0257  -0.0969 -0.1204 577 LEU A CD1 
2177 C CD2 . LEU A 281 ? 1.1998 0.7539 0.8680 0.0927  -0.0911 -0.1216 577 LEU A CD2 
2178 N N   . GLU A 282 ? 0.9411 0.7667 0.8352 0.1422  -0.0674 -0.0819 578 GLU A N   
2179 C CA  . GLU A 282 ? 0.8880 0.7940 0.8416 0.1506  -0.0616 -0.0712 578 GLU A CA  
2180 C C   . GLU A 282 ? 0.8203 0.7953 0.8120 0.1496  -0.0553 -0.0700 578 GLU A C   
2181 O O   . GLU A 282 ? 0.8083 0.7902 0.7805 0.1750  -0.0504 -0.0759 578 GLU A O   
2182 C CB  . GLU A 282 ? 0.9320 0.8405 0.8696 0.1935  -0.0590 -0.0689 578 GLU A CB  
2183 C CG  . GLU A 282 ? 1.0332 0.8635 0.9236 0.1970  -0.0656 -0.0685 578 GLU A CG  
2184 C CD  . GLU A 282 ? 1.0980 0.9398 0.9758 0.2436  -0.0645 -0.0648 578 GLU A CD  
2185 O OE1 . GLU A 282 ? 1.0738 0.9438 0.9406 0.2865  -0.0596 -0.0692 578 GLU A OE1 
2186 O OE2 . GLU A 282 ? 1.1740 1.0032 1.0531 0.2393  -0.0684 -0.0573 578 GLU A OE2 
2187 N N   . PHE A 283 ? 0.7714 0.7923 0.8102 0.1218  -0.0551 -0.0622 579 PHE A N   
2188 C CA  . PHE A 283 ? 0.7141 0.7893 0.7815 0.1149  -0.0501 -0.0587 579 PHE A CA  
2189 C C   . PHE A 283 ? 0.6721 0.8078 0.7749 0.1174  -0.0447 -0.0484 579 PHE A C   
2190 O O   . PHE A 283 ? 0.6704 0.8190 0.7983 0.0965  -0.0470 -0.0410 579 PHE A O   
2191 C CB  . PHE A 283 ? 0.6952 0.7662 0.7750 0.0845  -0.0555 -0.0582 579 PHE A CB  
2192 C CG  . PHE A 283 ? 0.7654 0.7914 0.8116 0.0768  -0.0617 -0.0687 579 PHE A CG  
2193 C CD1 . PHE A 283 ? 0.7436 0.7681 0.7697 0.0855  -0.0602 -0.0752 579 PHE A CD1 
2194 C CD2 . PHE A 283 ? 0.7869 0.7735 0.8177 0.0575  -0.0692 -0.0720 579 PHE A CD2 
2195 C CE1 . PHE A 283 ? 0.8251 0.8074 0.8159 0.0749  -0.0676 -0.0857 579 PHE A CE1 
2196 C CE2 . PHE A 283 ? 0.8068 0.7547 0.8027 0.0428  -0.0762 -0.0817 579 PHE A CE2 
2197 C CZ  . PHE A 283 ? 0.8440 0.7882 0.8193 0.0516  -0.0761 -0.0891 579 PHE A CZ  
2198 N N   . SER A 284 ? 0.7005 0.8763 0.8017 0.1429  -0.0375 -0.0483 580 SER A N   
2199 C CA  . SER A 284 ? 0.6754 0.9184 0.8069 0.1437  -0.0332 -0.0391 580 SER A CA  
2200 C C   . SER A 284 ? 0.6494 0.9334 0.8063 0.1111  -0.0301 -0.0304 580 SER A C   
2201 O O   . SER A 284 ? 0.6251 0.9539 0.8039 0.0975  -0.0290 -0.0220 580 SER A O   
2202 C CB  . SER A 284 ? 0.7088 0.9970 0.8307 0.1821  -0.0259 -0.0421 580 SER A CB  
2203 O OG  . SER A 284 ? 0.7213 1.0127 0.8255 0.1909  -0.0196 -0.0482 580 SER A OG  
2204 N N   . ALA A 285 ? 0.6109 0.8757 0.7582 0.0977  -0.0295 -0.0322 581 ALA A N   
2205 C CA  . ALA A 285 ? 0.5787 0.8622 0.7345 0.0687  -0.0276 -0.0237 581 ALA A CA  
2206 C C   . ALA A 285 ? 0.5946 0.8258 0.7419 0.0552  -0.0355 -0.0256 581 ALA A C   
2207 O O   . ALA A 285 ? 0.6096 0.8159 0.7404 0.0619  -0.0376 -0.0327 581 ALA A O   
2208 C CB  . ALA A 285 ? 0.5838 0.9052 0.7303 0.0708  -0.0183 -0.0228 581 ALA A CB  
2209 N N   . CYS A 286 ? 0.5754 0.7943 0.7320 0.0381  -0.0403 -0.0198 582 CYS A N   
2210 C CA  . CYS A 286 ? 0.5740 0.7558 0.7247 0.0317  -0.0477 -0.0219 582 CYS A CA  
2211 C C   . CYS A 286 ? 0.5809 0.7543 0.7297 0.0149  -0.0500 -0.0133 582 CYS A C   
2212 O O   . CYS A 286 ? 0.5938 0.7497 0.7477 0.0135  -0.0551 -0.0137 582 CYS A O   
2213 C CB  . CYS A 286 ? 0.5858 0.7455 0.7413 0.0382  -0.0529 -0.0285 582 CYS A CB  
2214 S SG  . CYS A 286 ? 0.5318 0.6995 0.7029 0.0382  -0.0526 -0.0240 582 CYS A SG  
2215 N N   . PRO A 287 ? 0.5961 0.7763 0.7303 0.0011  -0.0463 -0.0057 583 PRO A N   
2216 C CA  . PRO A 287 ? 0.5856 0.7410 0.7030 -0.0161 -0.0493 0.0023  583 PRO A CA  
2217 C C   . PRO A 287 ? 0.6178 0.7349 0.7236 -0.0056 -0.0570 -0.0004 583 PRO A C   
2218 O O   . PRO A 287 ? 0.5828 0.6925 0.6807 0.0062  -0.0598 -0.0043 583 PRO A O   
2219 C CB  . PRO A 287 ? 0.5942 0.7501 0.6840 -0.0339 -0.0446 0.0102  583 PRO A CB  
2220 C CG  . PRO A 287 ? 0.5985 0.7703 0.6894 -0.0190 -0.0411 0.0048  583 PRO A CG  
2221 C CD  . PRO A 287 ? 0.5832 0.7827 0.7050 -0.0002 -0.0399 -0.0042 583 PRO A CD  
2222 N N   . PHE A 288 ? 0.5723 0.6712 0.6764 -0.0082 -0.0605 0.0012  584 PHE A N   
2223 C CA  . PHE A 288 ? 0.6028 0.6761 0.6962 0.0063  -0.0667 -0.0014 584 PHE A CA  
2224 C C   . PHE A 288 ? 0.6766 0.7066 0.7333 0.0001  -0.0692 0.0048  584 PHE A C   
2225 O O   . PHE A 288 ? 0.6466 0.6719 0.6988 -0.0194 -0.0674 0.0092  584 PHE A O   
2226 C CB  . PHE A 288 ? 0.6071 0.7005 0.7316 0.0154  -0.0682 -0.0082 584 PHE A CB  
2227 C CG  . PHE A 288 ? 0.6264 0.7276 0.7669 0.0059  -0.0658 -0.0067 584 PHE A CG  
2228 C CD1 . PHE A 288 ? 0.6177 0.6996 0.7476 0.0036  -0.0677 -0.0043 584 PHE A CD1 
2229 C CD2 . PHE A 288 ? 0.6074 0.7330 0.7690 0.0040  -0.0626 -0.0086 584 PHE A CD2 
2230 C CE1 . PHE A 288 ? 0.5987 0.6895 0.7419 -0.0047 -0.0667 -0.0030 584 PHE A CE1 
2231 C CE2 . PHE A 288 ? 0.5769 0.7114 0.7505 -0.0002 -0.0619 -0.0069 584 PHE A CE2 
2232 C CZ  . PHE A 288 ? 0.5781 0.6971 0.7443 -0.0064 -0.0642 -0.0038 584 PHE A CZ  
2233 N N   . SER A 289 ? 0.6640 0.6607 0.6891 0.0181  -0.0744 0.0047  585 SER A N   
2234 C CA  . SER A 289 ? 0.7324 0.6696 0.7055 0.0172  -0.0777 0.0098  585 SER A CA  
2235 C C   . SER A 289 ? 0.7370 0.6610 0.6976 0.0507  -0.0829 0.0050  585 SER A C   
2236 O O   . SER A 289 ? 0.7113 0.6709 0.6935 0.0732  -0.0852 -0.0003 585 SER A O   
2237 C CB  . SER A 289 ? 0.7667 0.6546 0.6839 0.0063  -0.0786 0.0179  585 SER A CB  
2238 O OG  . SER A 289 ? 0.7947 0.6863 0.7047 0.0288  -0.0815 0.0164  585 SER A OG  
2239 N N   . GLY A 290 ? 0.7466 0.6213 0.6677 0.0536  -0.0849 0.0067  586 GLY A N   
2240 C CA  . GLY A 290 ? 0.8397 0.6944 0.7336 0.0915  -0.0894 0.0027  586 GLY A CA  
2241 C C   . GLY A 290 ? 0.9514 0.7102 0.7595 0.0971  -0.0939 0.0075  586 GLY A C   
2242 O O   . GLY A 290 ? 0.9345 0.6413 0.6935 0.0871  -0.0962 0.0142  586 GLY A O   
2243 N N   . TRP A 291 ? 0.9037 0.6307 0.6844 0.1126  -0.0951 0.0042  587 TRP A N   
2244 C CA  . TRP A 291 ? 1.0413 0.6613 0.7295 0.1120  -0.0998 0.0078  587 TRP A CA  
2245 C C   . TRP A 291 ? 0.9951 0.6033 0.6844 0.0896  -0.0980 0.0057  587 TRP A C   
2246 O O   . TRP A 291 ? 0.8986 0.5800 0.6562 0.0869  -0.0934 0.0012  587 TRP A O   
2247 C CB  . TRP A 291 ? 1.1119 0.6806 0.7355 0.1694  -0.1056 0.0046  587 TRP A CB  
2248 C CG  . TRP A 291 ? 1.0948 0.7379 0.7645 0.2129  -0.1036 -0.0044 587 TRP A CG  
2249 C CD1 . TRP A 291 ? 1.1052 0.7535 0.7751 0.2278  -0.1008 -0.0105 587 TRP A CD1 
2250 C CD2 . TRP A 291 ? 1.0619 0.7908 0.7815 0.2443  -0.1040 -0.0081 587 TRP A CD2 
2251 N NE1 . TRP A 291 ? 1.0977 0.8355 0.8170 0.2657  -0.0982 -0.0172 587 TRP A NE1 
2252 C CE2 . TRP A 291 ? 1.0957 0.8858 0.8466 0.2745  -0.1008 -0.0160 587 TRP A CE2 
2253 C CE3 . TRP A 291 ? 1.0416 0.8042 0.7802 0.2477  -0.1070 -0.0058 587 TRP A CE3 
2254 C CZ2 . TRP A 291 ? 1.0850 0.9754 0.8876 0.3030  -0.1007 -0.0210 587 TRP A CZ2 
2255 C CZ3 . TRP A 291 ? 1.0247 0.8808 0.8128 0.2779  -0.1083 -0.0116 587 TRP A CZ3 
2256 C CH2 . TRP A 291 ? 1.0454 0.9674 0.8659 0.3029  -0.1052 -0.0189 587 TRP A CH2 
2257 N N   . TYR A 292 ? 1.0804 0.5911 0.6875 0.0702  -0.1025 0.0093  588 TYR A N   
2258 C CA  . TYR A 292 ? 1.0966 0.5936 0.6994 0.0410  -0.1025 0.0077  588 TYR A CA  
2259 C C   . TYR A 292 ? 1.1458 0.6222 0.7256 0.0832  -0.1030 -0.0009 588 TYR A C   
2260 O O   . TYR A 292 ? 1.1628 0.5827 0.6808 0.1301  -0.1062 -0.0041 588 TYR A O   
2261 C CB  . TYR A 292 ? 1.1615 0.5619 0.6795 -0.0053 -0.1080 0.0146  588 TYR A CB  
2262 C CG  . TYR A 292 ? 1.1627 0.6146 0.7224 -0.0660 -0.1055 0.0221  588 TYR A CG  
2263 C CD1 . TYR A 292 ? 1.1010 0.6322 0.7304 -0.0906 -0.1027 0.0204  588 TYR A CD1 
2264 C CD2 . TYR A 292 ? 1.1742 0.5981 0.6995 -0.0962 -0.1058 0.0311  588 TYR A CD2 
2265 C CE1 . TYR A 292 ? 1.0928 0.6811 0.7588 -0.1394 -0.1007 0.0268  588 TYR A CE1 
2266 C CE2 . TYR A 292 ? 1.1421 0.6257 0.7054 -0.1498 -0.1023 0.0378  588 TYR A CE2 
2267 C CZ  . TYR A 292 ? 1.0981 0.6680 0.7335 -0.1687 -0.0999 0.0352  588 TYR A CZ  
2268 O OH  . TYR A 292 ? 1.0745 0.7156 0.7484 -0.2146 -0.0965 0.0414  588 TYR A OH  
2269 N N   . MET A 293 ? 1.0529 0.5777 0.6799 0.0694  -0.0997 -0.0045 589 MET A N   
2270 C CA  . MET A 293 ? 1.1459 0.6255 0.7282 0.0893  -0.1009 -0.0111 589 MET A CA  
2271 C C   . MET A 293 ? 1.2100 0.5883 0.7088 0.0479  -0.1083 -0.0081 589 MET A C   
2272 O O   . MET A 293 ? 1.1964 0.5926 0.7158 -0.0069 -0.1098 -0.0017 589 MET A O   
2273 C CB  . MET A 293 ? 1.0532 0.6220 0.7142 0.0878  -0.0947 -0.0152 589 MET A CB  
2274 C CG  . MET A 293 ? 1.1017 0.6369 0.7217 0.1165  -0.0939 -0.0230 589 MET A CG  
2275 S SD  . MET A 293 ? 0.9912 0.6374 0.7017 0.1230  -0.0846 -0.0268 589 MET A SD  
2276 C CE  . MET A 293 ? 0.9717 0.6372 0.7185 0.0613  -0.0876 -0.0210 589 MET A CE  
2277 N N   . GLY A 294 ? 1.3093 0.5815 0.7085 0.0746  -0.1132 -0.0129 590 GLY A N   
2278 C CA  . GLY A 294 ? 1.3722 0.5254 0.6697 0.0329  -0.1220 -0.0102 590 GLY A CA  
2279 C C   . GLY A 294 ? 1.3502 0.5382 0.6806 -0.0290 -0.1239 -0.0083 590 GLY A C   
2280 O O   . GLY A 294 ? 1.3764 0.5231 0.6672 -0.0880 -0.1299 -0.0015 590 GLY A O   
2281 N N   . THR A 295 ? 1.2480 0.5159 0.6482 -0.0175 -0.1192 -0.0136 591 THR A N   
2282 C CA  . THR A 295 ? 1.2687 0.5646 0.6904 -0.0681 -0.1228 -0.0125 591 THR A CA  
2283 C C   . THR A 295 ? 1.1971 0.5780 0.6902 -0.1187 -0.1224 -0.0034 591 THR A C   
2284 O O   . THR A 295 ? 1.1905 0.5794 0.6777 -0.1710 -0.1286 -0.0003 591 THR A O   
2285 C CB  . THR A 295 ? 1.1774 0.5386 0.6551 -0.0405 -0.1174 -0.0192 591 THR A CB  
2286 O OG1 . THR A 295 ? 1.1011 0.5592 0.6680 -0.0060 -0.1077 -0.0189 591 THR A OG1 
2287 C CG2 . THR A 295 ? 1.2670 0.5399 0.6604 -0.0002 -0.1186 -0.0288 591 THR A CG2 
2288 N N   . GLU A 296 ? 1.1194 0.5689 0.6781 -0.1037 -0.1157 0.0005  592 GLU A N   
2289 C CA  . GLU A 296 ? 1.0813 0.6104 0.7012 -0.1456 -0.1145 0.0083  592 GLU A CA  
2290 C C   . GLU A 296 ? 1.1665 0.6379 0.7182 -0.2032 -0.1215 0.0152  592 GLU A C   
2291 O O   . GLU A 296 ? 1.1523 0.6805 0.7323 -0.2512 -0.1241 0.0198  592 GLU A O   
2292 C CB  . GLU A 296 ? 1.0582 0.6467 0.7375 -0.1198 -0.1069 0.0105  592 GLU A CB  
2293 C CG  . GLU A 296 ? 0.9969 0.6490 0.7433 -0.0740 -0.1003 0.0047  592 GLU A CG  
2294 C CD  . GLU A 296 ? 0.9590 0.6629 0.7545 -0.0561 -0.0948 0.0065  592 GLU A CD  
2295 O OE1 . GLU A 296 ? 0.8786 0.6489 0.7286 -0.0777 -0.0921 0.0104  592 GLU A OE1 
2296 O OE2 . GLU A 296 ? 0.9644 0.6424 0.7393 -0.0190 -0.0938 0.0036  592 GLU A OE2 
2297 N N   . ILE A 297 ? 1.2612 0.6205 0.7182 -0.1996 -0.1250 0.0163  593 ILE A N   
2298 C CA  . ILE A 297 ? 1.3366 0.6225 0.7108 -0.2601 -0.1319 0.0238  593 ILE A CA  
2299 C C   . ILE A 297 ? 1.4267 0.6319 0.7216 -0.2919 -0.1420 0.0198  593 ILE A C   
2300 O O   . ILE A 297 ? 1.4374 0.6708 0.7288 -0.3545 -0.1470 0.0244  593 ILE A O   
2301 C CB  . ILE A 297 ? 1.4210 0.6027 0.7112 -0.2422 -0.1325 0.0274  593 ILE A CB  
2302 C CG1 . ILE A 297 ? 1.3344 0.5911 0.7001 -0.1984 -0.1236 0.0287  593 ILE A CG1 
2303 C CG2 . ILE A 297 ? 1.5232 0.6471 0.7399 -0.3130 -0.1373 0.0380  593 ILE A CG2 
2304 C CD1 . ILE A 297 ? 1.3551 0.5114 0.6395 -0.1624 -0.1255 0.0304  593 ILE A CD1 
2305 N N   . GLY A 298 ? 1.4727 0.5839 0.7017 -0.2456 -0.1446 0.0109  594 GLY A N   
2306 C CA  . GLY A 298 ? 1.6105 0.6377 0.7485 -0.2652 -0.1521 0.0082  594 GLY A CA  
2307 C C   . GLY A 298 ? 1.5131 0.6114 0.7017 -0.2983 -0.1558 0.0053  594 GLY A C   
2308 O O   . GLY A 298 ? 1.5713 0.6545 0.7142 -0.3422 -0.1608 0.0102  594 GLY A O   
2309 N N   . VAL A 299 ? 1.4152 0.6146 0.7066 -0.2702 -0.1508 0.0005  595 VAL A N   
2310 C CA  . VAL A 299 ? 1.3951 0.6623 0.7324 -0.2902 -0.1545 -0.0024 595 VAL A CA  
2311 C C   . VAL A 299 ? 1.3015 0.6994 0.7294 -0.3340 -0.1542 0.0061  595 VAL A C   
2312 O O   . VAL A 299 ? 1.3297 0.7508 0.7460 -0.3905 -0.1633 0.0088  595 VAL A O   
2313 C CB  . VAL A 299 ? 1.3195 0.6305 0.7121 -0.2267 -0.1468 -0.0103 595 VAL A CB  
2314 C CG1 . VAL A 299 ? 1.2942 0.6571 0.7166 -0.2486 -0.1521 -0.0127 595 VAL A CG1 
2315 C CG2 . VAL A 299 ? 1.3859 0.5855 0.6940 -0.1748 -0.1454 -0.0192 595 VAL A CG2 
2316 N N   . ARG A 300 ? 1.2232 0.7111 0.7395 -0.3059 -0.1440 0.0099  596 ARG A N   
2317 C CA  . ARG A 300 ? 1.1573 0.7750 0.7626 -0.3316 -0.1424 0.0164  596 ARG A CA  
2318 C C   . ARG A 300 ? 1.2136 0.8405 0.7953 -0.3893 -0.1447 0.0255  596 ARG A C   
2319 O O   . ARG A 300 ? 1.1703 0.8525 0.7577 -0.4415 -0.1509 0.0300  596 ARG A O   
2320 C CB  . ARG A 300 ? 1.0677 0.7668 0.7657 -0.2789 -0.1309 0.0160  596 ARG A CB  
2321 C CG  . ARG A 300 ? 1.0345 0.7318 0.7558 -0.2279 -0.1272 0.0084  596 ARG A CG  
2322 C CD  . ARG A 300 ? 1.0449 0.7726 0.7760 -0.2436 -0.1342 0.0065  596 ARG A CD  
2323 N NE  . ARG A 300 ? 0.9675 0.7988 0.7589 -0.2717 -0.1373 0.0127  596 ARG A NE  
2324 C CZ  . ARG A 300 ? 0.8634 0.7827 0.7341 -0.2455 -0.1309 0.0150  596 ARG A CZ  
2325 N NH1 . ARG A 300 ? 0.7909 0.7091 0.6925 -0.1991 -0.1217 0.0119  596 ARG A NH1 
2326 N NH2 . ARG A 300 ? 0.8314 0.8421 0.7465 -0.2664 -0.1344 0.0203  596 ARG A NH2 
2327 N N   . ASP A 301 ? 1.2052 0.7871 0.7614 -0.3792 -0.1388 0.0290  597 ASP A N   
2328 C CA  . ASP A 301 ? 1.2300 0.8230 0.7628 -0.4347 -0.1390 0.0387  597 ASP A CA  
2329 C C   . ASP A 301 ? 1.3157 0.8554 0.7634 -0.4790 -0.1438 0.0435  597 ASP A C   
2330 O O   . ASP A 301 ? 1.3052 0.9237 0.7692 -0.5216 -0.1423 0.0514  597 ASP A O   
2331 C CB  . ASP A 301 ? 1.2225 0.7555 0.7250 -0.4095 -0.1321 0.0418  597 ASP A CB  
2332 C CG  . ASP A 301 ? 1.1604 0.7827 0.7601 -0.3544 -0.1211 0.0402  597 ASP A CG  
2333 O OD1 . ASP A 301 ? 1.0739 0.8168 0.7614 -0.3553 -0.1172 0.0411  597 ASP A OD1 
2334 O OD2 . ASP A 301 ? 1.2044 0.7749 0.7881 -0.3089 -0.1171 0.0377  597 ASP A OD2 
2335 N N   . TYR A 302 ? 1.3798 0.7916 0.7349 -0.4652 -0.1492 0.0387  598 TYR A N   
2336 C CA  . TYR A 302 ? 1.4741 0.8198 0.7333 -0.5059 -0.1543 0.0439  598 TYR A CA  
2337 C C   . TYR A 302 ? 1.4804 0.8680 0.7499 -0.5293 -0.1603 0.0426  598 TYR A C   
2338 O O   . TYR A 302 ? 1.5007 0.8980 0.7284 -0.5803 -0.1632 0.0505  598 TYR A O   
2339 C CB  . TYR A 302 ? 1.5886 0.7742 0.7322 -0.4761 -0.1577 0.0399  598 TYR A CB  
2340 C CG  . TYR A 302 ? 1.6862 0.8158 0.7829 -0.4718 -0.1542 0.0451  598 TYR A CG  
2341 C CD1 . TYR A 302 ? 1.6225 0.8248 0.7498 -0.5143 -0.1496 0.0548  598 TYR A CD1 
2342 C CD2 . TYR A 302 ? 1.7826 0.7918 0.8027 -0.4216 -0.1554 0.0400  598 TYR A CD2 
2343 C CE1 . TYR A 302 ? 1.7427 0.8912 0.8229 -0.5122 -0.1468 0.0594  598 TYR A CE1 
2344 C CE2 . TYR A 302 ? 1.8065 0.7632 0.7794 -0.4149 -0.1533 0.0445  598 TYR A CE2 
2345 C CZ  . TYR A 302 ? 1.8132 0.8357 0.8154 -0.4627 -0.1492 0.0542  598 TYR A CZ  
2346 O OH  . TYR A 302 ? 1.7911 0.7588 0.7433 -0.4571 -0.1475 0.0583  598 TYR A OH  
2347 N N   . CYS A 303 ? 1.4100 0.8231 0.7301 -0.4955 -0.1626 0.0330  599 CYS A N   
2348 C CA  . CYS A 303 ? 1.4665 0.8864 0.7723 -0.5120 -0.1697 0.0307  599 CYS A CA  
2349 C C   . CYS A 303 ? 1.3759 0.9359 0.7885 -0.5129 -0.1708 0.0294  599 CYS A C   
2350 O O   . CYS A 303 ? 1.3799 0.9572 0.7841 -0.5300 -0.1771 0.0286  599 CYS A O   
2351 C CB  . CYS A 303 ? 1.5028 0.8040 0.7415 -0.4713 -0.1736 0.0198  599 CYS A CB  
2352 S SG  . CYS A 303 ? 1.6286 0.7588 0.7236 -0.4620 -0.1740 0.0220  599 CYS A SG  
2353 N N   . ASP A 304 ? 1.2696 0.9276 0.7766 -0.4932 -0.1654 0.0296  600 ASP A N   
2354 C CA  . ASP A 304 ? 1.2291 1.0300 0.8289 -0.4964 -0.1660 0.0319  600 ASP A CA  
2355 C C   . ASP A 304 ? 1.2609 1.1184 0.8447 -0.5470 -0.1666 0.0417  600 ASP A C   
2356 O O   . ASP A 304 ? 1.3133 1.1398 0.8453 -0.5813 -0.1633 0.0492  600 ASP A O   
2357 C CB  . ASP A 304 ? 1.1518 1.0461 0.8404 -0.4719 -0.1586 0.0338  600 ASP A CB  
2358 C CG  . ASP A 304 ? 1.0719 0.9789 0.8154 -0.4204 -0.1594 0.0256  600 ASP A CG  
2359 O OD1 . ASP A 304 ? 1.0893 0.9206 0.7978 -0.3936 -0.1610 0.0184  600 ASP A OD1 
2360 O OD2 . ASP A 304 ? 0.9936 0.9893 0.8152 -0.3896 -0.1508 0.0285  600 ASP A OD2 
2361 N N   . ASN A 305 ? 1.2504 1.1918 0.8750 -0.5520 -0.1716 0.0418  601 ASN A N   
2362 C CA  . ASN A 305 ? 1.2604 1.2693 0.8744 -0.5990 -0.1725 0.0507  601 ASN A CA  
2363 C C   . ASN A 305 ? 1.1879 1.3089 0.8566 -0.6071 -0.1631 0.0586  601 ASN A C   
2364 O O   . ASN A 305 ? 1.1741 1.3299 0.8129 -0.6532 -0.1615 0.0671  601 ASN A O   
2365 C CB  . ASN A 305 ? 1.2480 1.3267 0.8968 -0.5957 -0.1803 0.0485  601 ASN A CB  
2366 C CG  . ASN A 305 ? 1.3582 1.3425 0.9243 -0.6223 -0.1895 0.0461  601 ASN A CG  
2367 O OD1 . ASN A 305 ? 1.4562 1.3637 0.9375 -0.6643 -0.1901 0.0514  601 ASN A OD1 
2368 N ND2 . ASN A 305 ? 1.3518 1.3370 0.9352 -0.5980 -0.1972 0.0386  601 ASN A ND2 
2369 N N   . SER A 306 ? 1.1169 1.2975 0.8620 -0.5633 -0.1571 0.0558  602 SER A N   
2370 C CA  . SER A 306 ? 1.0913 1.3781 0.8900 -0.5608 -0.1472 0.0618  602 SER A CA  
2371 C C   . SER A 306 ? 1.0953 1.3252 0.8680 -0.5653 -0.1395 0.0640  602 SER A C   
2372 O O   . SER A 306 ? 1.0496 1.3589 0.8645 -0.5595 -0.1305 0.0681  602 SER A O   
2373 C CB  . SER A 306 ? 1.0669 1.4538 0.9590 -0.5069 -0.1451 0.0579  602 SER A CB  
2374 O OG  . SER A 306 ? 1.0814 1.4050 0.9877 -0.4674 -0.1477 0.0501  602 SER A OG  
2375 N N   . ARG A 307 ? 1.1556 1.2478 0.8557 -0.5718 -0.1431 0.0612  603 ARG A N   
2376 C CA  . ARG A 307 ? 1.1979 1.2200 0.8575 -0.5776 -0.1374 0.0638  603 ARG A CA  
2377 C C   . ARG A 307 ? 1.2659 1.1972 0.8173 -0.6294 -0.1410 0.0700  603 ARG A C   
2378 O O   . ARG A 307 ? 1.3012 1.2828 0.8351 -0.6708 -0.1432 0.0760  603 ARG A O   
2379 C CB  . ARG A 307 ? 1.1761 1.1103 0.8347 -0.5336 -0.1385 0.0554  603 ARG A CB  
2380 C CG  . ARG A 307 ? 1.0908 1.1120 0.8490 -0.4868 -0.1362 0.0500  603 ARG A CG  
2381 C CD  . ARG A 307 ? 1.0363 1.1507 0.8551 -0.4778 -0.1259 0.0549  603 ARG A CD  
2382 N NE  . ARG A 307 ? 1.0329 1.0686 0.8069 -0.4847 -0.1214 0.0573  603 ARG A NE  
2383 C CZ  . ARG A 307 ? 1.0519 1.0088 0.8157 -0.4535 -0.1223 0.0519  603 ARG A CZ  
2384 N NH1 . ARG A 307 ? 1.0241 0.9803 0.8257 -0.3988 -0.1217 0.0441  603 ARG A NH1 
2385 N NH2 . ARG A 307 ? 1.1127 0.9902 0.8239 -0.4563 -0.1181 0.0552  603 ARG A NH2 
2386 N N   . TYR A 308 ? 1.3296 1.1264 0.8019 -0.6269 -0.1422 0.0689  604 TYR A N   
2387 C CA  . TYR A 308 ? 1.4091 1.1169 0.7697 -0.6751 -0.1457 0.0757  604 TYR A CA  
2388 C C   . TYR A 308 ? 1.5000 1.1560 0.7958 -0.7018 -0.1553 0.0753  604 TYR A C   
2389 O O   . TYR A 308 ? 1.5502 1.1859 0.7733 -0.7559 -0.1587 0.0829  604 TYR A O   
2390 C CB  . TYR A 308 ? 1.4921 1.0620 0.7771 -0.6560 -0.1455 0.0739  604 TYR A CB  
2391 C CG  . TYR A 308 ? 1.5469 1.1555 0.8550 -0.6604 -0.1370 0.0794  604 TYR A CG  
2392 C CD1 . TYR A 308 ? 1.4373 1.1266 0.8447 -0.6220 -0.1291 0.0769  604 TYR A CD1 
2393 C CD2 . TYR A 308 ? 1.7093 1.2719 0.9350 -0.7048 -0.1373 0.0870  604 TYR A CD2 
2394 C CE1 . TYR A 308 ? 1.4262 1.1509 0.8529 -0.6260 -0.1208 0.0822  604 TYR A CE1 
2395 C CE2 . TYR A 308 ? 1.6119 1.2104 0.8566 -0.7099 -0.1295 0.0917  604 TYR A CE2 
2396 C CZ  . TYR A 308 ? 1.5227 1.2030 0.8694 -0.6694 -0.1207 0.0896  604 TYR A CZ  
2397 O OH  . TYR A 308 ? 1.5340 1.2497 0.8988 -0.6732 -0.1123 0.0946  604 TYR A OH  
2398 N N   . ASN A 309 ? 1.4750 1.1086 0.7917 -0.6673 -0.1600 0.0665  605 ASN A N   
2399 C CA  . ASN A 309 ? 1.5000 1.1135 0.7777 -0.6896 -0.1684 0.0658  605 ASN A CA  
2400 C C   . ASN A 309 ? 1.6505 1.1226 0.7889 -0.7252 -0.1746 0.0699  605 ASN A C   
2401 O O   . ASN A 309 ? 1.7584 1.2412 0.8474 -0.7805 -0.1789 0.0775  605 ASN A O   
2402 C CB  . ASN A 309 ? 1.4529 1.2162 0.7960 -0.7225 -0.1679 0.0718  605 ASN A CB  
2403 C CG  . ASN A 309 ? 1.4912 1.2509 0.8128 -0.7390 -0.1768 0.0701  605 ASN A CG  
2404 O OD1 . ASN A 309 ? 1.4891 1.1740 0.7924 -0.7081 -0.1820 0.0613  605 ASN A OD1 
2405 N ND2 . ASN A 309 ? 1.5048 1.3460 0.8247 -0.7885 -0.1786 0.0782  605 ASN A ND2 
2406 N N   . ILE A 310 ? 1.7108 1.0479 0.7807 -0.6903 -0.1756 0.0645  606 ILE A N   
2407 C CA  . ILE A 310 ? 1.8487 1.0387 0.7756 -0.7141 -0.1815 0.0682  606 ILE A CA  
2408 C C   . ILE A 310 ? 1.9894 1.0761 0.8424 -0.7001 -0.1894 0.0625  606 ILE A C   
2409 O O   . ILE A 310 ? 2.1136 1.0684 0.8375 -0.7158 -0.1952 0.0654  606 ILE A O   
2410 C CB  . ILE A 310 ? 1.9172 1.0124 0.7937 -0.6820 -0.1783 0.0665  606 ILE A CB  
2411 C CG1 . ILE A 310 ? 1.9322 0.9651 0.8215 -0.6066 -0.1773 0.0546  606 ILE A CG1 
2412 C CG2 . ILE A 310 ? 1.7473 0.9438 0.7010 -0.6915 -0.1699 0.0714  606 ILE A CG2 
2413 C CD1 . ILE A 310 ? 1.8451 0.7919 0.6884 -0.5670 -0.1742 0.0526  606 ILE A CD1 
2414 N N   . LEU A 311 ? 1.9447 1.0822 0.8687 -0.6694 -0.1902 0.0543  607 LEU A N   
2415 C CA  . LEU A 311 ? 2.0053 1.0491 0.8587 -0.6571 -0.1973 0.0488  607 LEU A CA  
2416 C C   . LEU A 311 ? 2.1571 1.1593 0.9173 -0.7230 -0.2049 0.0583  607 LEU A C   
2417 O O   . LEU A 311 ? 2.2758 1.1439 0.9201 -0.7215 -0.2111 0.0576  607 LEU A O   
2418 C CB  . LEU A 311 ? 1.8089 0.9345 0.7571 -0.6272 -0.1978 0.0393  607 LEU A CB  
2419 C CG  . LEU A 311 ? 1.7505 0.8759 0.7577 -0.5558 -0.1928 0.0268  607 LEU A CG  
2420 C CD1 . LEU A 311 ? 1.7184 0.9301 0.8106 -0.5379 -0.1951 0.0184  607 LEU A CD1 
2421 C CD2 . LEU A 311 ? 1.7669 0.7409 0.6741 -0.5079 -0.1930 0.0201  607 LEU A CD2 
2422 N N   . GLU A 312 ? 2.2342 1.3507 1.0389 -0.7803 -0.2044 0.0676  608 GLU A N   
2423 C CA  . GLU A 312 ? 2.3912 1.4801 1.1072 -0.8515 -0.2112 0.0779  608 GLU A CA  
2424 C C   . GLU A 312 ? 2.5100 1.4364 1.0738 -0.8695 -0.2152 0.0828  608 GLU A C   
2425 O O   . GLU A 312 ? 2.6003 1.4043 1.0496 -0.8821 -0.2232 0.0837  608 GLU A O   
2426 C CB  . GLU A 312 ? 2.4355 1.6803 1.2232 -0.9038 -0.2075 0.0872  608 GLU A CB  
2427 C CG  . GLU A 312 ? 2.3230 1.7337 1.2565 -0.8823 -0.2039 0.0830  608 GLU A CG  
2428 C CD  . GLU A 312 ? 2.5046 1.9779 1.4416 -0.9234 -0.2107 0.0863  608 GLU A CD  
2429 O OE1 . GLU A 312 ? 2.5485 1.9150 1.3782 -0.9552 -0.2189 0.0886  608 GLU A OE1 
2430 O OE2 . GLU A 312 ? 2.4796 2.1078 1.5231 -0.9224 -0.2083 0.0867  608 GLU A OE2 
2431 N N   . GLU A 313 ? 2.4409 1.3610 0.9970 -0.8692 -0.2103 0.0859  609 GLU A N   
2432 C CA  . GLU A 313 ? 2.5718 1.3461 0.9795 -0.8922 -0.2152 0.0909  609 GLU A CA  
2433 C C   . GLU A 313 ? 2.6411 1.2525 0.9584 -0.8295 -0.2186 0.0827  609 GLU A C   
2434 O O   . GLU A 313 ? 2.7707 1.2399 0.9429 -0.8470 -0.2270 0.0857  609 GLU A O   
2435 C CB  . GLU A 313 ? 2.6339 1.4501 1.0637 -0.9038 -0.2091 0.0946  609 GLU A CB  
2436 C CG  . GLU A 313 ? 2.7171 1.5988 1.1207 -0.9887 -0.2103 0.1064  609 GLU A CG  
2437 C CD  . GLU A 313 ? 2.8981 1.6339 1.1255 -1.0443 -0.2210 0.1130  609 GLU A CD  
2438 O OE1 . GLU A 313 ? 2.9115 1.6006 1.0811 -1.0674 -0.2282 0.1151  609 GLU A OE1 
2439 O OE2 . GLU A 313 ? 2.9542 1.6183 1.0964 -1.0658 -0.2226 0.1158  609 GLU A OE2 
2440 N N   . VAL A 314 ? 2.5369 1.1672 0.9330 -0.7548 -0.2123 0.0723  610 VAL A N   
2441 C CA  . VAL A 314 ? 2.6064 1.0974 0.9229 -0.6866 -0.2142 0.0640  610 VAL A CA  
2442 C C   . VAL A 314 ? 2.6933 1.0991 0.9329 -0.6821 -0.2215 0.0619  610 VAL A C   
2443 O O   . VAL A 314 ? 2.8247 1.0793 0.9317 -0.6574 -0.2270 0.0609  610 VAL A O   
2444 C CB  . VAL A 314 ? 2.4651 1.0164 0.8941 -0.6112 -0.2055 0.0533  610 VAL A CB  
2445 C CG1 . VAL A 314 ? 2.5007 0.9290 0.8568 -0.5352 -0.2067 0.0439  610 VAL A CG1 
2446 C CG2 . VAL A 314 ? 2.3240 0.9269 0.8015 -0.6120 -0.1991 0.0559  610 VAL A CG2 
2447 N N   . ALA A 315 ? 2.5970 1.0970 0.9151 -0.7031 -0.2220 0.0610  611 ALA A N   
2448 C CA  . ALA A 315 ? 2.6935 1.1180 0.9438 -0.7008 -0.2290 0.0586  611 ALA A CA  
2449 C C   . ALA A 315 ? 2.8489 1.1613 0.9474 -0.7640 -0.2386 0.0697  611 ALA A C   
2450 O O   . ALA A 315 ? 3.0083 1.1830 0.9877 -0.7468 -0.2451 0.0685  611 ALA A O   
2451 C CB  . ALA A 315 ? 2.5454 1.1027 0.9131 -0.7152 -0.2285 0.0551  611 ALA A CB  
2452 N N   . LYS A 316 ? 2.8239 1.1940 0.9206 -0.8378 -0.2396 0.0805  612 LYS A N   
2453 C CA  . LYS A 316 ? 2.9813 1.2478 0.9281 -0.9064 -0.2489 0.0916  612 LYS A CA  
2454 C C   . LYS A 316 ? 3.1427 1.2206 0.9322 -0.8736 -0.2536 0.0908  612 LYS A C   
2455 O O   . LYS A 316 ? 3.2963 1.2334 0.9517 -0.8746 -0.2621 0.0924  612 LYS A O   
2456 C CB  . LYS A 316 ? 2.9588 1.3286 0.9350 -0.9838 -0.2473 0.1021  612 LYS A CB  
2457 C CG  . LYS A 316 ? 2.8771 1.4206 0.9720 -1.0293 -0.2453 0.1057  612 LYS A CG  
2458 C CD  . LYS A 316 ? 2.9074 1.5216 0.9825 -1.1154 -0.2459 0.1181  612 LYS A CD  
2459 C CE  . LYS A 316 ? 3.1294 1.5828 1.0132 -1.1738 -0.2564 0.1269  612 LYS A CE  
2460 N NZ  . LYS A 316 ? 3.1993 1.7148 1.0479 -1.2651 -0.2580 0.1390  612 LYS A NZ  
2461 N N   . LYS A 317 ? 3.1062 1.1785 0.9082 -0.8406 -0.2485 0.0879  613 LYS A N   
2462 C CA  . LYS A 317 ? 3.2621 1.1649 0.9178 -0.8060 -0.2532 0.0861  613 LYS A CA  
2463 C C   . LYS A 317 ? 3.2990 1.1007 0.9119 -0.7196 -0.2541 0.0760  613 LYS A C   
2464 O O   . LYS A 317 ? 3.4447 1.1047 0.9409 -0.6851 -0.2580 0.0712  613 LYS A O   
2465 C CB  . LYS A 317 ? 3.1976 1.1344 0.8978 -0.7814 -0.2466 0.0829  613 LYS A CB  
2466 C CG  . LYS A 317 ? 3.2332 1.2123 0.9203 -0.8608 -0.2473 0.0913  613 LYS A CG  
2467 C CD  . LYS A 317 ? 3.0762 1.2550 0.9305 -0.8917 -0.2387 0.0948  613 LYS A CD  
2468 C CE  . LYS A 317 ? 3.0622 1.2913 0.9195 -0.9430 -0.2364 0.1006  613 LYS A CE  
2469 N NZ  . LYS A 317 ? 3.2172 1.3940 0.9536 -1.0328 -0.2450 0.1106  613 LYS A NZ  
2470 N N   . MET A 318 ? 3.2179 1.0973 0.9349 -0.6801 -0.2495 0.0698  614 MET A N   
2471 C CA  . MET A 318 ? 3.2565 1.0473 0.9291 -0.5987 -0.2500 0.0608  614 MET A CA  
2472 C C   . MET A 318 ? 3.3682 1.0601 0.9335 -0.6204 -0.2591 0.0643  614 MET A C   
2473 O O   . MET A 318 ? 3.4809 1.0856 0.9905 -0.5534 -0.2601 0.0573  614 MET A O   
2474 C CB  . MET A 318 ? 3.0783 0.9967 0.9152 -0.5383 -0.2398 0.0492  614 MET A CB  
2475 C CG  . MET A 318 ? 3.0210 0.9790 0.9215 -0.4815 -0.2316 0.0431  614 MET A CG  
2476 S SD  . MET A 318 ? 2.7710 0.8718 0.8520 -0.4159 -0.2202 0.0298  614 MET A SD  
2477 C CE  . MET A 318 ? 2.8197 0.8278 0.8300 -0.3506 -0.2225 0.0213  614 MET A CE  
2478 N N   . ASP A 319 ? 3.4042 1.1114 0.9400 -0.7106 -0.2653 0.0744  615 ASP A N   
2479 C CA  . ASP A 319 ? 3.5598 1.1883 1.0054 -0.7419 -0.2742 0.0783  615 ASP A CA  
2480 C C   . ASP A 319 ? 3.4465 1.1589 1.0058 -0.7019 -0.2700 0.0679  615 ASP A C   
2481 O O   . ASP A 319 ? 3.5646 1.1863 1.0630 -0.6500 -0.2724 0.0618  615 ASP A O   
2482 C CB  . ASP A 319 ? 3.7622 1.1972 1.0395 -0.7092 -0.2813 0.0741  615 ASP A CB  
2483 C CG  . ASP A 319 ? 3.9416 1.2843 1.1151 -0.7461 -0.2913 0.0780  615 ASP A CG  
2484 O OD1 . ASP A 319 ? 4.0519 1.3823 1.1678 -0.8366 -0.2984 0.0880  615 ASP A OD1 
2485 O OD2 . ASP A 319 ? 3.9513 1.2343 1.0977 -0.6851 -0.2920 0.0712  615 ASP A OD2 
2486 N N   . LEU A 320 ? 3.2904 1.1793 1.0131 -0.7261 -0.2639 0.0655  616 LEU A N   
2487 C CA  . LEU A 320 ? 3.1219 1.1069 0.9649 -0.6892 -0.2597 0.0541  616 LEU A CA  
2488 C C   . LEU A 320 ? 3.0817 1.1425 0.9600 -0.7592 -0.2655 0.0579  616 LEU A C   
2489 O O   . LEU A 320 ? 3.1024 1.1931 0.9564 -0.8394 -0.2700 0.0697  616 LEU A O   
2490 C CB  . LEU A 320 ? 2.9618 1.0924 0.9689 -0.6495 -0.2487 0.0460  616 LEU A CB  
2491 C CG  . LEU A 320 ? 2.9585 1.0374 0.9569 -0.5673 -0.2419 0.0390  616 LEU A CG  
2492 C CD1 . LEU A 320 ? 2.7328 0.9602 0.8981 -0.5314 -0.2317 0.0301  616 LEU A CD1 
2493 C CD2 . LEU A 320 ? 3.0186 0.9735 0.9254 -0.4996 -0.2437 0.0315  616 LEU A CD2 
2494 N N   . ASP A 321 ? 2.9824 1.0818 0.9206 -0.7263 -0.2652 0.0470  617 ASP A N   
2495 C CA  . ASP A 321 ? 2.9757 1.1544 0.9569 -0.7805 -0.2713 0.0477  617 ASP A CA  
2496 C C   . ASP A 321 ? 2.7762 1.1528 0.9306 -0.7926 -0.2656 0.0451  617 ASP A C   
2497 O O   . ASP A 321 ? 2.7111 1.1647 0.9695 -0.7408 -0.2609 0.0327  617 ASP A O   
2498 C CB  . ASP A 321 ? 3.0032 1.1225 0.9570 -0.7371 -0.2745 0.0361  617 ASP A CB  
2499 C CG  . ASP A 321 ? 3.0401 1.2214 1.0167 -0.7941 -0.2829 0.0365  617 ASP A CG  
2500 O OD1 . ASP A 321 ? 3.0196 1.3099 1.0499 -0.8624 -0.2854 0.0453  617 ASP A OD1 
2501 O OD2 . ASP A 321 ? 3.0695 1.1938 1.0088 -0.7687 -0.2870 0.0277  617 ASP A OD2 
2502 N N   . MET A 322 ? 2.7467 1.2064 0.9267 -0.8610 -0.2664 0.0570  618 MET A N   
2503 C CA  . MET A 322 ? 2.6273 1.2767 0.9628 -0.8735 -0.2613 0.0566  618 MET A CA  
2504 C C   . MET A 322 ? 2.6617 1.4194 1.0519 -0.9191 -0.2681 0.0574  618 MET A C   
2505 O O   . MET A 322 ? 2.5629 1.4837 1.0749 -0.9316 -0.2652 0.0584  618 MET A O   
2506 C CB  . MET A 322 ? 2.6398 1.3367 0.9825 -0.9142 -0.2568 0.0684  618 MET A CB  
2507 C CG  . MET A 322 ? 2.5612 1.1939 0.8889 -0.8625 -0.2493 0.0659  618 MET A CG  
2508 S SD  . MET A 322 ? 2.6672 1.3764 1.0237 -0.9049 -0.2432 0.0773  618 MET A SD  
2509 C CE  . MET A 322 ? 2.6133 1.5178 1.0767 -0.9704 -0.2441 0.0840  618 MET A CE  
2510 N N   . ARG A 323 ? 2.7682 1.4401 1.0693 -0.9413 -0.2774 0.0568  619 ARG A N   
2511 C CA  . ARG A 323 ? 2.7658 1.5397 1.1169 -0.9816 -0.2849 0.0564  619 ARG A CA  
2512 C C   . ARG A 323 ? 2.6914 1.5471 1.1529 -0.9219 -0.2841 0.0410  619 ARG A C   
2513 O O   . ARG A 323 ? 2.6045 1.6168 1.1771 -0.9335 -0.2856 0.0401  619 ARG A O   
2514 C CB  . ARG A 323 ? 2.9504 1.5998 1.1626 -1.0287 -0.2959 0.0609  619 ARG A CB  
2515 C CG  . ARG A 323 ? 3.0801 1.6435 1.1674 -1.0970 -0.2986 0.0772  619 ARG A CG  
2516 C CD  . ARG A 323 ? 3.3041 1.6824 1.2228 -1.1176 -0.3083 0.0798  619 ARG A CD  
2517 N NE  . ARG A 323 ? 3.3516 1.5855 1.2088 -1.0375 -0.3056 0.0700  619 ARG A NE  
2518 C CZ  . ARG A 323 ? 3.5349 1.5948 1.2466 -1.0298 -0.3125 0.0697  619 ARG A CZ  
2519 N NH1 . ARG A 323 ? 3.6604 1.6556 1.2653 -1.1013 -0.3235 0.0786  619 ARG A NH1 
2520 N NH2 . ARG A 323 ? 3.5481 1.4981 1.2177 -0.9471 -0.3084 0.0603  619 ARG A NH2 
2521 N N   . LYS A 324 ? 2.6909 1.4455 1.1203 -0.8555 -0.2817 0.0290  620 LYS A N   
2522 C CA  . LYS A 324 ? 2.5537 1.3658 1.0647 -0.8009 -0.2815 0.0138  620 LYS A CA  
2523 C C   . LYS A 324 ? 2.4218 1.2898 1.0258 -0.7390 -0.2706 0.0071  620 LYS A C   
2524 O O   . LYS A 324 ? 2.4835 1.2648 1.0431 -0.7058 -0.2633 0.0072  620 LYS A O   
2525 C CB  . LYS A 324 ? 2.6500 1.3223 1.0631 -0.7674 -0.2852 0.0040  620 LYS A CB  
2526 C CG  . LYS A 324 ? 2.8566 1.5114 1.2145 -0.8183 -0.2978 0.0053  620 LYS A CG  
2527 C CD  . LYS A 324 ? 2.9958 1.5761 1.2437 -0.8935 -0.3039 0.0211  620 LYS A CD  
2528 C CE  . LYS A 324 ? 3.0517 1.6341 1.2561 -0.9502 -0.3169 0.0226  620 LYS A CE  
2529 N NZ  . LYS A 324 ? 3.2276 1.7460 1.3237 -1.0310 -0.3228 0.0391  620 LYS A NZ  
2530 N N   . THR A 325 ? 2.2281 1.2405 0.9564 -0.7234 -0.2704 0.0017  621 THR A N   
2531 C CA  . THR A 325 ? 2.0573 1.1284 0.8753 -0.6677 -0.2612 -0.0048 621 THR A CA  
2532 C C   . THR A 325 ? 2.0906 1.0535 0.8641 -0.5988 -0.2552 -0.0178 621 THR A C   
2533 O O   . THR A 325 ? 1.9797 0.9294 0.7752 -0.5566 -0.2459 -0.0207 621 THR A O   
2534 C CB  . THR A 325 ? 1.9098 1.1414 0.8510 -0.6618 -0.2646 -0.0079 621 THR A CB  
2535 O OG1 . THR A 325 ? 1.8323 1.1004 0.8447 -0.6033 -0.2571 -0.0159 621 THR A OG1 
2536 C CG2 . THR A 325 ? 1.9644 1.2002 0.8907 -0.6649 -0.2749 -0.0150 621 THR A CG2 
2537 N N   . SER A 326 ? 2.1320 1.0207 0.8418 -0.5851 -0.2598 -0.0258 622 SER A N   
2538 C CA  . SER A 326 ? 2.1368 0.9404 0.8077 -0.5157 -0.2533 -0.0393 622 SER A CA  
2539 C C   . SER A 326 ? 2.2243 0.8730 0.7778 -0.4919 -0.2486 -0.0373 622 SER A C   
2540 O O   . SER A 326 ? 2.2587 0.8379 0.7752 -0.4276 -0.2417 -0.0477 622 SER A O   
2541 C CB  . SER A 326 ? 2.1017 0.8976 0.7520 -0.5112 -0.2600 -0.0483 622 SER A CB  
2542 O OG  . SER A 326 ? 2.1604 0.9753 0.7874 -0.5797 -0.2720 -0.0396 622 SER A OG  
2543 N N   . SER A 327 ? 2.3062 0.9010 0.7956 -0.5388 -0.2520 -0.0236 623 SER A N   
2544 C CA  . SER A 327 ? 2.4169 0.8705 0.7978 -0.5088 -0.2479 -0.0203 623 SER A CA  
2545 C C   . SER A 327 ? 2.3393 0.8183 0.7730 -0.4570 -0.2369 -0.0231 623 SER A C   
2546 O O   . SER A 327 ? 2.4192 0.7923 0.7715 -0.4199 -0.2331 -0.0214 623 SER A O   
2547 C CB  . SER A 327 ? 2.5485 0.9336 0.8355 -0.5770 -0.2554 -0.0040 623 SER A CB  
2548 O OG  . SER A 327 ? 2.5138 0.9946 0.8708 -0.6166 -0.2531 0.0056  623 SER A OG  
2549 N N   . LEU A 328 ? 2.2042 0.8203 0.7680 -0.4529 -0.2326 -0.0270 624 LEU A N   
2550 C CA  . LEU A 328 ? 2.1621 0.8161 0.7868 -0.4100 -0.2226 -0.0298 624 LEU A CA  
2551 C C   . LEU A 328 ? 2.2151 0.8102 0.7840 -0.4282 -0.2216 -0.0178 624 LEU A C   
2552 O O   . LEU A 328 ? 2.1991 0.7613 0.7617 -0.3792 -0.2142 -0.0204 624 LEU A O   
2553 C CB  . LEU A 328 ? 2.1319 0.7438 0.7472 -0.3258 -0.2135 -0.0439 624 LEU A CB  
2554 C CG  . LEU A 328 ? 2.0975 0.7628 0.7593 -0.3015 -0.2127 -0.0569 624 LEU A CG  
2555 C CD1 . LEU A 328 ? 2.0188 0.6985 0.7142 -0.2225 -0.1997 -0.0698 624 LEU A CD1 
2556 C CD2 . LEU A 328 ? 2.0094 0.8094 0.7747 -0.3501 -0.2190 -0.0546 624 LEU A CD2 
2557 N N   . TRP A 329 ? 2.2787 0.8638 0.8042 -0.4993 -0.2290 -0.0046 625 TRP A N   
2558 C CA  . TRP A 329 ? 2.3055 0.8440 0.7782 -0.5231 -0.2282 0.0071  625 TRP A CA  
2559 C C   . TRP A 329 ? 2.2258 0.8644 0.8049 -0.5073 -0.2200 0.0064  625 TRP A C   
2560 O O   . TRP A 329 ? 2.2326 0.8173 0.7756 -0.4836 -0.2158 0.0089  625 TRP A O   
2561 C CB  . TRP A 329 ? 2.3876 0.9268 0.8109 -0.6092 -0.2363 0.0212  625 TRP A CB  
2562 C CG  . TRP A 329 ? 2.2910 0.9919 0.8295 -0.6589 -0.2377 0.0245  625 TRP A CG  
2563 C CD1 . TRP A 329 ? 2.2922 1.0598 0.8725 -0.6794 -0.2435 0.0211  625 TRP A CD1 
2564 C CD2 . TRP A 329 ? 2.2453 1.0646 0.8683 -0.6901 -0.2334 0.0322  625 TRP A CD2 
2565 N NE1 . TRP A 329 ? 2.2062 1.1288 0.8915 -0.7181 -0.2434 0.0264  625 TRP A NE1 
2566 C CE2 . TRP A 329 ? 2.1621 1.1199 0.8759 -0.7246 -0.2367 0.0334  625 TRP A CE2 
2567 C CE3 . TRP A 329 ? 2.1802 1.0034 0.8094 -0.6892 -0.2271 0.0378  625 TRP A CE3 
2568 C CZ2 . TRP A 329 ? 2.0455 1.1465 0.8547 -0.7542 -0.2331 0.0404  625 TRP A CZ2 
2569 C CZ3 . TRP A 329 ? 2.1001 1.0626 0.8244 -0.7229 -0.2234 0.0445  625 TRP A CZ3 
2570 C CH2 . TRP A 329 ? 2.0689 1.1694 0.8816 -0.7532 -0.2260 0.0459  625 TRP A CH2 
2571 N N   . LYS A 330 ? 2.0996 0.8815 0.8064 -0.5164 -0.2184 0.0029  626 LYS A N   
2572 C CA  . LYS A 330 ? 1.9821 0.8603 0.7907 -0.5014 -0.2112 0.0026  626 LYS A CA  
2573 C C   . LYS A 330 ? 1.9702 0.8041 0.7841 -0.4253 -0.2034 -0.0084 626 LYS A C   
2574 O O   . LYS A 330 ? 1.9691 0.7947 0.7894 -0.4087 -0.1980 -0.0058 626 LYS A O   
2575 C CB  . LYS A 330 ? 1.9013 0.9349 0.8359 -0.5183 -0.2124 0.0008  626 LYS A CB  
2576 C CG  . LYS A 330 ? 1.8875 1.0082 0.8473 -0.5882 -0.2169 0.0133  626 LYS A CG  
2577 C CD  . LYS A 330 ? 1.7556 1.0409 0.8497 -0.5886 -0.2159 0.0128  626 LYS A CD  
2578 C CE  . LYS A 330 ? 1.7382 1.1243 0.8600 -0.6505 -0.2190 0.0250  626 LYS A CE  
2579 N NZ  . LYS A 330 ? 1.6323 1.1779 0.8786 -0.6404 -0.2187 0.0243  626 LYS A NZ  
2580 N N   . ASP A 331 ? 1.9616 0.7768 0.7769 -0.3778 -0.2022 -0.0210 627 ASP A N   
2581 C CA  . ASP A 331 ? 1.9745 0.7562 0.7921 -0.3016 -0.1934 -0.0321 627 ASP A CA  
2582 C C   . ASP A 331 ? 2.0595 0.7190 0.7707 -0.2736 -0.1916 -0.0277 627 ASP A C   
2583 O O   . ASP A 331 ? 2.0673 0.7252 0.7943 -0.2331 -0.1849 -0.0294 627 ASP A O   
2584 C CB  . ASP A 331 ? 1.9528 0.7244 0.7665 -0.2581 -0.1917 -0.0454 627 ASP A CB  
2585 C CG  . ASP A 331 ? 1.8336 0.7166 0.7365 -0.2852 -0.1959 -0.0496 627 ASP A CG  
2586 O OD1 . ASP A 331 ? 1.7632 0.6707 0.6624 -0.3422 -0.2049 -0.0421 627 ASP A OD1 
2587 O OD2 . ASP A 331 ? 1.7378 0.6850 0.7102 -0.2480 -0.1906 -0.0598 627 ASP A OD2 
2588 N N   . GLN A 332 ? 2.0815 0.6374 0.6792 -0.2963 -0.1986 -0.0213 628 GLN A N   
2589 C CA  . GLN A 332 ? 2.2703 0.6972 0.7475 -0.2678 -0.1993 -0.0166 628 GLN A CA  
2590 C C   . GLN A 332 ? 2.2672 0.6978 0.7425 -0.2937 -0.1988 -0.0069 628 GLN A C   
2591 O O   . GLN A 332 ? 2.2605 0.6547 0.7141 -0.2433 -0.1942 -0.0087 628 GLN A O   
2592 C CB  . GLN A 332 ? 2.4368 0.7511 0.7879 -0.2979 -0.2087 -0.0105 628 GLN A CB  
2593 C CG  . GLN A 332 ? 2.5629 0.7430 0.7919 -0.2336 -0.2089 -0.0127 628 GLN A CG  
2594 C CD  . GLN A 332 ? 2.6906 0.7772 0.8198 -0.2441 -0.2164 -0.0120 628 GLN A CD  
2595 O OE1 . GLN A 332 ? 2.6895 0.7964 0.8228 -0.3108 -0.2232 -0.0076 628 GLN A OE1 
2596 N NE2 . GLN A 332 ? 2.8049 0.7922 0.8431 -0.1756 -0.2155 -0.0160 628 GLN A NE2 
2597 N N   . ALA A 333 ? 2.2289 0.7129 0.7301 -0.3706 -0.2031 0.0033  629 ALA A N   
2598 C CA  . ALA A 333 ? 2.2349 0.7300 0.7363 -0.3979 -0.2018 0.0122  629 ALA A CA  
2599 C C   . ALA A 333 ? 2.1606 0.7519 0.7787 -0.3616 -0.1928 0.0065  629 ALA A C   
2600 O O   . ALA A 333 ? 2.1167 0.6944 0.7245 -0.3563 -0.1900 0.0106  629 ALA A O   
2601 C CB  . ALA A 333 ? 2.2373 0.7874 0.7476 -0.4868 -0.2067 0.0242  629 ALA A CB  
2602 N N   . LEU A 334 ? 2.0304 0.7143 0.7537 -0.3371 -0.1887 -0.0031 630 LEU A N   
2603 C CA  . LEU A 334 ? 1.9300 0.7004 0.7589 -0.3046 -0.1809 -0.0084 630 LEU A CA  
2604 C C   . LEU A 334 ? 1.9786 0.6836 0.7710 -0.2275 -0.1749 -0.0154 630 LEU A C   
2605 O O   . LEU A 334 ? 1.9472 0.6810 0.7800 -0.2081 -0.1698 -0.0146 630 LEU A O   
2606 C CB  . LEU A 334 ? 1.8051 0.6824 0.7414 -0.2993 -0.1795 -0.0172 630 LEU A CB  
2607 C CG  . LEU A 334 ? 1.7392 0.7032 0.7797 -0.2708 -0.1727 -0.0221 630 LEU A CG  
2608 C CD1 . LEU A 334 ? 1.6275 0.6782 0.7317 -0.3248 -0.1732 -0.0107 630 LEU A CD1 
2609 C CD2 . LEU A 334 ? 1.6170 0.6500 0.7315 -0.2447 -0.1715 -0.0342 630 LEU A CD2 
2610 N N   . VAL A 335 ? 1.9946 0.6190 0.7122 -0.1802 -0.1752 -0.0220 631 VAL A N   
2611 C CA  . VAL A 335 ? 2.0798 0.6531 0.7579 -0.1004 -0.1695 -0.0280 631 VAL A CA  
2612 C C   . VAL A 335 ? 2.1890 0.6794 0.7787 -0.1027 -0.1730 -0.0190 631 VAL A C   
2613 O O   . VAL A 335 ? 2.1461 0.6511 0.7571 -0.0625 -0.1680 -0.0203 631 VAL A O   
2614 C CB  . VAL A 335 ? 2.1418 0.6537 0.7541 -0.0502 -0.1692 -0.0355 631 VAL A CB  
2615 C CG1 . VAL A 335 ? 2.2013 0.6643 0.7598 0.0322  -0.1644 -0.0391 631 VAL A CG1 
2616 C CG2 . VAL A 335 ? 2.0931 0.6925 0.7953 -0.0389 -0.1640 -0.0468 631 VAL A CG2 
2617 N N   . GLU A 336 ? 2.2281 0.6291 0.7124 -0.1505 -0.1818 -0.0100 632 GLU A N   
2618 C CA  . GLU A 336 ? 2.3398 0.6517 0.7247 -0.1583 -0.1862 -0.0023 632 GLU A CA  
2619 C C   . GLU A 336 ? 2.2754 0.6600 0.7354 -0.1850 -0.1823 0.0021  632 GLU A C   
2620 O O   . GLU A 336 ? 2.2928 0.6380 0.7150 -0.1541 -0.1813 0.0026  632 GLU A O   
2621 C CB  . GLU A 336 ? 2.4919 0.7110 0.7610 -0.2229 -0.1964 0.0074  632 GLU A CB  
2622 C CG  . GLU A 336 ? 2.6289 0.7676 0.8154 -0.2052 -0.2014 0.0050  632 GLU A CG  
2623 C CD  . GLU A 336 ? 2.7654 0.8088 0.8601 -0.1194 -0.2011 -0.0007 632 GLU A CD  
2624 O OE1 . GLU A 336 ? 2.7646 0.7643 0.8111 -0.0897 -0.2012 0.0001  632 GLU A OE1 
2625 O OE2 . GLU A 336 ? 2.8037 0.8214 0.8753 -0.0799 -0.2009 -0.0062 632 GLU A OE2 
2626 N N   . ILE A 337 ? 2.1646 0.6570 0.7283 -0.2412 -0.1805 0.0056  633 ILE A N   
2627 C CA  . ILE A 337 ? 2.1314 0.6989 0.7680 -0.2694 -0.1765 0.0112  633 ILE A CA  
2628 C C   . ILE A 337 ? 2.0719 0.6789 0.7758 -0.2013 -0.1686 0.0040  633 ILE A C   
2629 O O   . ILE A 337 ? 2.0444 0.6457 0.7452 -0.1940 -0.1665 0.0077  633 ILE A O   
2630 C CB  . ILE A 337 ? 1.9782 0.6672 0.7170 -0.3341 -0.1759 0.0159  633 ILE A CB  
2631 C CG1 . ILE A 337 ? 2.0745 0.7303 0.7397 -0.4066 -0.1834 0.0256  633 ILE A CG1 
2632 C CG2 . ILE A 337 ? 1.9739 0.7536 0.8006 -0.3519 -0.1701 0.0210  633 ILE A CG2 
2633 C CD1 . ILE A 337 ? 2.0266 0.8077 0.7842 -0.4638 -0.1836 0.0299  633 ILE A CD1 
2634 N N   . ASN A 338 ? 2.0163 0.6629 0.7767 -0.1499 -0.1643 -0.0064 634 ASN A N   
2635 C CA  . ASN A 338 ? 1.9672 0.6657 0.7983 -0.0863 -0.1564 -0.0131 634 ASN A CA  
2636 C C   . ASN A 338 ? 2.0391 0.6612 0.7887 -0.0137 -0.1555 -0.0169 634 ASN A C   
2637 O O   . ASN A 338 ? 1.9850 0.6417 0.7736 0.0302  -0.1504 -0.0183 634 ASN A O   
2638 C CB  . ASN A 338 ? 1.8605 0.6393 0.7820 -0.0636 -0.1517 -0.0233 634 ASN A CB  
2639 C CG  . ASN A 338 ? 1.7183 0.5988 0.7446 -0.1202 -0.1518 -0.0204 634 ASN A CG  
2640 O OD1 . ASN A 338 ? 1.6556 0.6141 0.7688 -0.1085 -0.1463 -0.0195 634 ASN A OD1 
2641 N ND2 . ASN A 338 ? 1.6912 0.5842 0.7111 -0.1812 -0.1578 -0.0163 634 ASN A ND2 
2642 N N   . ILE A 339 ? 2.1482 0.6710 0.7837 0.0016  -0.1608 -0.0180 635 ILE A N   
2643 C CA  . ILE A 339 ? 2.2081 0.6511 0.7483 0.0634  -0.1623 -0.0198 635 ILE A CA  
2644 C C   . ILE A 339 ? 2.2359 0.6348 0.7294 0.0348  -0.1660 -0.0122 635 ILE A C   
2645 O O   . ILE A 339 ? 2.2134 0.6044 0.6922 0.0854  -0.1641 -0.0143 635 ILE A O   
2646 C CB  . ILE A 339 ? 2.2957 0.6308 0.7109 0.0805  -0.1687 -0.0211 635 ILE A CB  
2647 C CG1 . ILE A 339 ? 2.2832 0.6675 0.7446 0.1287  -0.1629 -0.0302 635 ILE A CG1 
2648 C CG2 . ILE A 339 ? 2.3772 0.6125 0.6700 0.1334  -0.1730 -0.0214 635 ILE A CG2 
2649 C CD1 . ILE A 339 ? 2.3775 0.6600 0.7208 0.1494  -0.1687 -0.0307 635 ILE A CD1 
2650 N N   . ALA A 340 ? 2.2453 0.6283 0.7226 -0.0480 -0.1707 -0.0033 636 ALA A N   
2651 C CA  . ALA A 340 ? 2.3146 0.6530 0.7389 -0.0840 -0.1740 0.0041  636 ALA A CA  
2652 C C   . ALA A 340 ? 2.2158 0.6495 0.7497 -0.0811 -0.1669 0.0062  636 ALA A C   
2653 O O   . ALA A 340 ? 2.2290 0.6295 0.7270 -0.0608 -0.1670 0.0074  636 ALA A O   
2654 C CB  . ALA A 340 ? 2.3690 0.6802 0.7483 -0.1757 -0.1803 0.0135  636 ALA A CB  
2655 N N   . VAL A 341 ? 2.0665 0.6151 0.7292 -0.1026 -0.1612 0.0071  637 VAL A N   
2656 C CA  . VAL A 341 ? 2.0177 0.6526 0.7802 -0.0984 -0.1548 0.0104  637 VAL A CA  
2657 C C   . VAL A 341 ? 2.0231 0.6571 0.7910 -0.0120 -0.1513 0.0039  637 VAL A C   
2658 O O   . VAL A 341 ? 2.0201 0.6488 0.7819 0.0025  -0.1504 0.0076  637 VAL A O   
2659 C CB  . VAL A 341 ? 1.9216 0.6744 0.8133 -0.1275 -0.1503 0.0109  637 VAL A CB  
2660 C CG1 . VAL A 341 ? 1.7947 0.6273 0.7808 -0.1155 -0.1442 0.0149  637 VAL A CG1 
2661 C CG2 . VAL A 341 ? 1.9275 0.7050 0.8214 -0.2128 -0.1537 0.0182  637 VAL A CG2 
2662 N N   . LEU A 342 ? 2.0201 0.6647 0.7965 0.0471  -0.1493 -0.0059 638 LEU A N   
2663 C CA  . LEU A 342 ? 2.0110 0.6783 0.7977 0.1316  -0.1454 -0.0125 638 LEU A CA  
2664 C C   . LEU A 342 ? 2.1090 0.6806 0.7789 0.1602  -0.1505 -0.0125 638 LEU A C   
2665 O O   . LEU A 342 ? 2.0912 0.6843 0.7758 0.1917  -0.1491 -0.0116 638 LEU A O   
2666 C CB  . LEU A 342 ? 2.0123 0.7085 0.8147 0.1837  -0.1419 -0.0228 638 LEU A CB  
2667 C CG  . LEU A 342 ? 1.8850 0.6822 0.8064 0.1691  -0.1360 -0.0258 638 LEU A CG  
2668 C CD1 . LEU A 342 ? 1.8794 0.6959 0.8013 0.2169  -0.1319 -0.0363 638 LEU A CD1 
2669 C CD2 . LEU A 342 ? 1.6829 0.5790 0.7098 0.1879  -0.1306 -0.0235 638 LEU A CD2 
2670 N N   . TYR A 343 ? 2.2002 0.6615 0.7473 0.1496  -0.1574 -0.0136 639 TYR A N   
2671 C CA  . TYR A 343 ? 2.3452 0.6995 0.7630 0.1790  -0.1634 -0.0150 639 TYR A CA  
2672 C C   . TYR A 343 ? 2.3364 0.6698 0.7416 0.1405  -0.1651 -0.0081 639 TYR A C   
2673 O O   . TYR A 343 ? 2.3441 0.6438 0.7009 0.1842  -0.1664 -0.0107 639 TYR A O   
2674 C CB  . TYR A 343 ? 2.4899 0.7197 0.7714 0.1579  -0.1718 -0.0148 639 TYR A CB  
2675 C CG  . TYR A 343 ? 2.6330 0.7296 0.7595 0.1752  -0.1799 -0.0156 639 TYR A CG  
2676 C CD1 . TYR A 343 ? 2.6860 0.7421 0.7413 0.2610  -0.1813 -0.0234 639 TYR A CD1 
2677 C CD2 . TYR A 343 ? 2.7107 0.7240 0.7572 0.1054  -0.1863 -0.0089 639 TYR A CD2 
2678 C CE1 . TYR A 343 ? 2.8296 0.7585 0.7379 0.2799  -0.1890 -0.0251 639 TYR A CE1 
2679 C CE2 . TYR A 343 ? 2.8421 0.7235 0.7369 0.1203  -0.1942 -0.0108 639 TYR A CE2 
2680 C CZ  . TYR A 343 ? 2.9202 0.7612 0.7568 0.2086  -0.1947 -0.0188 639 TYR A CZ  
2681 O OH  . TYR A 343 ? 3.0954 0.8138 0.8032 0.2261  -0.2006 -0.0201 639 TYR A OH  
2682 N N   . SER A 344 ? 2.3254 0.6832 0.7725 0.0590  -0.1648 0.0009  640 SER A N   
2683 C CA  . SER A 344 ? 2.2799 0.6195 0.7106 0.0161  -0.1658 0.0084  640 SER A CA  
2684 C C   . SER A 344 ? 2.2371 0.6647 0.7656 0.0535  -0.1593 0.0101  640 SER A C   
2685 O O   . SER A 344 ? 2.2265 0.6158 0.7101 0.0705  -0.1608 0.0110  640 SER A O   
2686 C CB  . SER A 344 ? 2.2768 0.6438 0.7366 -0.0799 -0.1660 0.0181  640 SER A CB  
2687 O OG  . SER A 344 ? 2.3919 0.6951 0.7746 -0.1140 -0.1723 0.0173  640 SER A OG  
2688 N N   . PHE A 345 ? 2.0936 0.6363 0.7512 0.0659  -0.1529 0.0105  641 PHE A N   
2689 C CA  . PHE A 345 ? 2.0093 0.6384 0.7576 0.1037  -0.1480 0.0130  641 PHE A CA  
2690 C C   . PHE A 345 ? 2.0766 0.6903 0.7843 0.1899  -0.1491 0.0041  641 PHE A C   
2691 O O   . PHE A 345 ? 2.1209 0.7365 0.8223 0.2113  -0.1496 0.0065  641 PHE A O   
2692 C CB  . PHE A 345 ? 1.8673 0.6127 0.7472 0.1048  -0.1423 0.0137  641 PHE A CB  
2693 C CG  . PHE A 345 ? 1.7682 0.5665 0.7189 0.0308  -0.1396 0.0252  641 PHE A CG  
2694 C CD1 . PHE A 345 ? 1.7865 0.5552 0.7056 -0.0442 -0.1414 0.0290  641 PHE A CD1 
2695 C CD2 . PHE A 345 ? 1.6533 0.5459 0.7056 0.0375  -0.1353 0.0318  641 PHE A CD2 
2696 C CE1 . PHE A 345 ? 1.7190 0.5588 0.7099 -0.1109 -0.1378 0.0385  641 PHE A CE1 
2697 C CE2 . PHE A 345 ? 1.5478 0.5347 0.6845 -0.0271 -0.1292 0.0375  641 PHE A CE2 
2698 C CZ  . PHE A 345 ? 1.5886 0.5366 0.6878 -0.1003 -0.1312 0.0429  641 PHE A CZ  
2699 N N   . GLN A 346 ? 2.1087 0.7080 0.7824 0.2392  -0.1496 -0.0063 642 GLN A N   
2700 C CA  . GLN A 346 ? 2.1434 0.7505 0.7860 0.3236  -0.1497 -0.0153 642 GLN A CA  
2701 C C   . GLN A 346 ? 2.2472 0.7396 0.7601 0.3358  -0.1562 -0.0165 642 GLN A C   
2702 O O   . GLN A 346 ? 2.1597 0.6751 0.6712 0.3857  -0.1562 -0.0193 642 GLN A O   
2703 C CB  . GLN A 346 ? 2.1490 0.7599 0.7703 0.3680  -0.1486 -0.0247 642 GLN A CB  
2704 C CG  . GLN A 346 ? 2.0790 0.8178 0.8294 0.3793  -0.1410 -0.0270 642 GLN A CG  
2705 C CD  . GLN A 346 ? 2.1595 0.8817 0.8758 0.4032  -0.1400 -0.0342 642 GLN A CD  
2706 O OE1 . GLN A 346 ? 2.1838 0.8023 0.8094 0.3714  -0.1453 -0.0331 642 GLN A OE1 
2707 N NE2 . GLN A 346 ? 2.1655 0.9927 0.9510 0.4576  -0.1333 -0.0410 642 GLN A NE2 
2708 N N   . SER A 347 ? 2.3011 0.6698 0.6998 0.2908  -0.1623 -0.0150 643 SER A N   
2709 C CA  . SER A 347 ? 2.4420 0.6870 0.7033 0.2977  -0.1692 -0.0169 643 SER A CA  
2710 C C   . SER A 347 ? 2.4499 0.7065 0.7368 0.2716  -0.1683 -0.0099 643 SER A C   
2711 O O   . SER A 347 ? 2.5180 0.7005 0.7152 0.2994  -0.1725 -0.0131 643 SER A O   
2712 C CB  . SER A 347 ? 2.5691 0.6857 0.7076 0.2414  -0.1764 -0.0153 643 SER A CB  
2713 O OG  . SER A 347 ? 2.6100 0.7040 0.7107 0.2698  -0.1781 -0.0207 643 SER A OG  
2714 N N   . ASP A 348 ? 2.3614 0.7084 0.7650 0.2215  -0.1631 0.0000  644 ASP A N   
2715 C CA  . ASP A 348 ? 2.3569 0.7293 0.7964 0.1973  -0.1614 0.0090  644 ASP A CA  
2716 C C   . ASP A 348 ? 2.2677 0.7601 0.8178 0.2534  -0.1570 0.0094  644 ASP A C   
2717 O O   . ASP A 348 ? 2.2392 0.7711 0.8366 0.2350  -0.1553 0.0187  644 ASP A O   
2718 C CB  . ASP A 348 ? 2.3053 0.7065 0.7971 0.1053  -0.1584 0.0215  644 ASP A CB  
2719 C CG  . ASP A 348 ? 2.3795 0.6708 0.7584 0.0381  -0.1637 0.0227  644 ASP A CG  
2720 O OD1 . ASP A 348 ? 2.4628 0.6366 0.7100 0.0607  -0.1706 0.0150  644 ASP A OD1 
2721 O OD2 . ASP A 348 ? 2.2901 0.6174 0.7102 -0.0381 -0.1614 0.0312  644 ASP A OD2 
2722 N N   . LYS A 349 ? 2.2468 0.8050 0.8395 0.3183  -0.1552 0.0002  645 LYS A N   
2723 C CA  . LYS A 349 ? 2.1988 0.8864 0.8995 0.3687  -0.1518 -0.0006 645 LYS A CA  
2724 C C   . LYS A 349 ? 2.0622 0.8438 0.8843 0.3224  -0.1480 0.0113  645 LYS A C   
2725 O O   . LYS A 349 ? 1.9186 0.7754 0.8053 0.3377  -0.1477 0.0161  645 LYS A O   
2726 C CB  . LYS A 349 ? 2.3166 0.9882 0.9727 0.4148  -0.1551 -0.0030 645 LYS A CB  
2727 C CG  . LYS A 349 ? 2.3744 1.1611 1.0943 0.4906  -0.1535 -0.0114 645 LYS A CG  
2728 C CD  . LYS A 349 ? 2.5024 1.2348 1.1219 0.5556  -0.1559 -0.0247 645 LYS A CD  
2729 C CE  . LYS A 349 ? 2.5135 1.3611 1.1828 0.6282  -0.1546 -0.0325 645 LYS A CE  
2730 N NZ  . LYS A 349 ? 2.4547 1.4525 1.2517 0.6375  -0.1485 -0.0345 645 LYS A NZ  
2731 N N   . VAL A 350 ? 1.9828 0.7616 0.8324 0.2654  -0.1458 0.0162  646 VAL A N   
2732 C CA  . VAL A 350 ? 1.8444 0.7121 0.8043 0.2251  -0.1422 0.0269  646 VAL A CA  
2733 C C   . VAL A 350 ? 1.7426 0.6969 0.7862 0.2517  -0.1392 0.0198  646 VAL A C   
2734 O O   . VAL A 350 ? 1.7684 0.6873 0.7825 0.2456  -0.1384 0.0130  646 VAL A O   
2735 C CB  . VAL A 350 ? 1.8279 0.6471 0.7663 0.1369  -0.1410 0.0378  646 VAL A CB  
2736 C CG1 . VAL A 350 ? 1.6581 0.5825 0.7130 0.0994  -0.1360 0.0473  646 VAL A CG1 
2737 C CG2 . VAL A 350 ? 1.9301 0.6704 0.7852 0.1082  -0.1430 0.0439  646 VAL A CG2 
2738 N N   . THR A 351 ? 1.6218 0.6906 0.7665 0.2792  -0.1380 0.0210  647 THR A N   
2739 C CA  . THR A 351 ? 1.5272 0.7068 0.7642 0.3032  -0.1326 0.0105  647 THR A CA  
2740 C C   . THR A 351 ? 1.4832 0.6672 0.7491 0.2485  -0.1271 0.0087  647 THR A C   
2741 O O   . THR A 351 ? 1.4389 0.6350 0.7346 0.1828  -0.1240 0.0152  647 THR A O   
2742 C CB  . THR A 351 ? 1.3975 0.7284 0.7573 0.3050  -0.1278 0.0086  647 THR A CB  
2743 O OG1 . THR A 351 ? 1.4264 0.7520 0.7562 0.3470  -0.1345 0.0116  647 THR A OG1 
2744 C CG2 . THR A 351 ? 1.2692 0.7143 0.7132 0.3332  -0.1224 -0.0021 647 THR A CG2 
2745 N N   . ILE A 352 ? 1.4918 0.6698 0.7458 0.2785  -0.1261 -0.0002 648 ILE A N   
2746 C CA  . ILE A 352 ? 1.4393 0.6342 0.7262 0.2355  -0.1216 -0.0032 648 ILE A CA  
2747 C C   . ILE A 352 ? 1.4116 0.6505 0.7172 0.2886  -0.1181 -0.0144 648 ILE A C   
2748 O O   . ILE A 352 ? 1.4345 0.6417 0.6842 0.3559  -0.1211 -0.0194 648 ILE A O   
2749 C CB  . ILE A 352 ? 1.5220 0.5775 0.7026 0.1888  -0.1276 0.0016  648 ILE A CB  
2750 C CG1 . ILE A 352 ? 1.4813 0.5805 0.7157 0.1303  -0.1239 0.0005  648 ILE A CG1 
2751 C CG2 . ILE A 352 ? 1.6125 0.5641 0.6781 0.2332  -0.1320 -0.0056 648 ILE A CG2 
2752 C CD1 . ILE A 352 ? 1.5550 0.5536 0.7101 0.0634  -0.1298 0.0075  648 ILE A CD1 
2753 N N   . VAL A 353 ? 1.3296 0.6461 0.7124 0.2612  -0.1113 -0.0180 649 VAL A N   
2754 C CA  . VAL A 353 ? 1.3268 0.6959 0.7336 0.3034  -0.1059 -0.0277 649 VAL A CA  
2755 C C   . VAL A 353 ? 1.3706 0.6879 0.7472 0.2724  -0.1056 -0.0305 649 VAL A C   
2756 O O   . VAL A 353 ? 1.3303 0.6526 0.7366 0.2097  -0.1060 -0.0255 649 VAL A O   
2757 C CB  . VAL A 353 ? 1.2658 0.7917 0.7985 0.3043  -0.0977 -0.0294 649 VAL A CB  
2758 C CG1 . VAL A 353 ? 1.2082 0.7856 0.8177 0.2376  -0.0943 -0.0242 649 VAL A CG1 
2759 C CG2 . VAL A 353 ? 1.2616 0.8498 0.8159 0.3469  -0.0909 -0.0384 649 VAL A CG2 
2760 N N   . ASP A 354 ? 1.4149 0.6847 0.7289 0.3188  -0.1053 -0.0391 650 ASP A N   
2761 C CA  . ASP A 354 ? 1.4484 0.6658 0.7265 0.2932  -0.1057 -0.0431 650 ASP A CA  
2762 C C   . ASP A 354 ? 1.3631 0.7084 0.7493 0.2810  -0.0959 -0.0457 650 ASP A C   
2763 O O   . ASP A 354 ? 1.2926 0.7504 0.7566 0.3087  -0.0883 -0.0472 650 ASP A O   
2764 C CB  . ASP A 354 ? 1.5434 0.6538 0.7022 0.3466  -0.1089 -0.0512 650 ASP A CB  
2765 C CG  . ASP A 354 ? 1.5700 0.7737 0.7611 0.4164  -0.0999 -0.0591 650 ASP A CG  
2766 O OD1 . ASP A 354 ? 1.5268 0.8205 0.7937 0.4210  -0.0913 -0.0641 650 ASP A OD1 
2767 O OD2 . ASP A 354 ? 1.6293 0.8205 0.7654 0.4631  -0.1011 -0.0599 650 ASP A OD2 
2768 N N   . HIS A 355 ? 1.3664 0.6942 0.7541 0.2355  -0.0969 -0.0457 651 HIS A N   
2769 C CA  . HIS A 355 ? 1.2622 0.7033 0.7481 0.2186  -0.0886 -0.0461 651 HIS A CA  
2770 C C   . HIS A 355 ? 1.2350 0.7298 0.7319 0.2739  -0.0792 -0.0545 651 HIS A C   
2771 O O   . HIS A 355 ? 1.1641 0.7656 0.7461 0.2668  -0.0706 -0.0538 651 HIS A O   
2772 C CB  . HIS A 355 ? 1.2713 0.6829 0.7501 0.1634  -0.0931 -0.0442 651 HIS A CB  
2773 C CG  . HIS A 355 ? 1.3547 0.6427 0.7201 0.1678  -0.1000 -0.0505 651 HIS A CG  
2774 N ND1 . HIS A 355 ? 1.4166 0.5803 0.6815 0.1537  -0.1103 -0.0490 651 HIS A ND1 
2775 C CD2 . HIS A 355 ? 1.4009 0.6629 0.7297 0.1814  -0.0986 -0.0584 651 HIS A CD2 
2776 C CE1 . HIS A 355 ? 1.5706 0.6311 0.7378 0.1581  -0.1157 -0.0563 651 HIS A CE1 
2777 N NE2 . HIS A 355 ? 1.4898 0.6097 0.6951 0.1773  -0.1086 -0.0626 651 HIS A NE2 
2778 N N   . HIS A 356 ? 1.3031 0.7267 0.7113 0.3297  -0.0802 -0.0623 652 HIS A N   
2779 C CA  . HIS A 356 ? 1.3066 0.7966 0.7257 0.3888  -0.0700 -0.0705 652 HIS A CA  
2780 C C   . HIS A 356 ? 1.2279 0.8297 0.7141 0.4226  -0.0645 -0.0692 652 HIS A C   
2781 O O   . HIS A 356 ? 1.1480 0.8734 0.7155 0.4249  -0.0542 -0.0698 652 HIS A O   
2782 C CB  . HIS A 356 ? 1.4260 0.8018 0.7207 0.4448  -0.0731 -0.0802 652 HIS A CB  
2783 C CG  . HIS A 356 ? 1.4929 0.7502 0.7097 0.4090  -0.0801 -0.0827 652 HIS A CG  
2784 N ND1 . HIS A 356 ? 1.4812 0.7727 0.7274 0.3837  -0.0750 -0.0853 652 HIS A ND1 
2785 C CD2 . HIS A 356 ? 1.6044 0.7205 0.7170 0.3857  -0.0926 -0.0804 652 HIS A CD2 
2786 C CE1 . HIS A 356 ? 1.5691 0.7393 0.7295 0.3526  -0.0849 -0.0876 652 HIS A CE1 
2787 N NE2 . HIS A 356 ? 1.6522 0.7143 0.7299 0.3506  -0.0955 -0.0845 652 HIS A NE2 
2788 N N   . SER A 357 ? 1.2884 0.8491 0.7395 0.4439  -0.0719 -0.0668 653 SER A N   
2789 C CA  . SER A 357 ? 1.2216 0.8918 0.7348 0.4741  -0.0688 -0.0658 653 SER A CA  
2790 C C   . SER A 357 ? 1.0802 0.8523 0.7058 0.4161  -0.0656 -0.0585 653 SER A C   
2791 O O   . SER A 357 ? 1.0318 0.9259 0.7300 0.4264  -0.0593 -0.0592 653 SER A O   
2792 C CB  . SER A 357 ? 1.3134 0.9134 0.7592 0.5048  -0.0785 -0.0635 653 SER A CB  
2793 O OG  . SER A 357 ? 1.2867 1.0064 0.7872 0.5334  -0.0751 -0.0637 653 SER A OG  
2794 N N   . ALA A 358 ? 1.0991 0.8244 0.7363 0.3545  -0.0701 -0.0518 654 ALA A N   
2795 C CA  . ALA A 358 ? 1.0884 0.8981 0.8206 0.3059  -0.0676 -0.0455 654 ALA A CA  
2796 C C   . ALA A 358 ? 1.0002 0.8991 0.7981 0.2902  -0.0577 -0.0470 654 ALA A C   
2797 O O   . ALA A 358 ? 0.9007 0.8969 0.7711 0.2782  -0.0529 -0.0452 654 ALA A O   
2798 C CB  . ALA A 358 ? 1.0754 0.8206 0.8001 0.2503  -0.0741 -0.0384 654 ALA A CB  
2799 N N   . THR A 359 ? 1.0078 0.8694 0.7744 0.2876  -0.0551 -0.0499 655 THR A N   
2800 C CA  . THR A 359 ? 0.9552 0.8927 0.7759 0.2707  -0.0457 -0.0500 655 THR A CA  
2801 C C   . THR A 359 ? 0.9318 0.9612 0.7728 0.3136  -0.0357 -0.0553 655 THR A C   
2802 O O   . THR A 359 ? 0.8696 0.9941 0.7755 0.2937  -0.0277 -0.0530 655 THR A O   
2803 C CB  . THR A 359 ? 0.9341 0.8053 0.7122 0.2555  -0.0466 -0.0515 655 THR A CB  
2804 O OG1 . THR A 359 ? 1.0068 0.8039 0.6979 0.3014  -0.0481 -0.0593 655 THR A OG1 
2805 C CG2 . THR A 359 ? 0.8940 0.7036 0.6666 0.2061  -0.0565 -0.0452 655 THR A CG2 
2806 N N   . GLU A 360 ? 0.9519 0.9565 0.7342 0.3725  -0.0363 -0.0621 656 GLU A N   
2807 C CA  . GLU A 360 ? 0.9507 1.0619 0.7554 0.4183  -0.0269 -0.0674 656 GLU A CA  
2808 C C   . GLU A 360 ? 0.8904 1.1058 0.7692 0.4033  -0.0270 -0.0634 656 GLU A C   
2809 O O   . GLU A 360 ? 0.8294 1.1610 0.7679 0.3923  -0.0178 -0.0631 656 GLU A O   
2810 C CB  . GLU A 360 ? 1.0335 1.0953 0.7550 0.4935  -0.0294 -0.0755 656 GLU A CB  
2811 C CG  . GLU A 360 ? 1.0795 1.2645 0.8221 0.5408  -0.0196 -0.0803 656 GLU A CG  
2812 C CD  . GLU A 360 ? 1.1942 1.3416 0.8623 0.5897  -0.0274 -0.0813 656 GLU A CD  
2813 O OE1 . GLU A 360 ? 1.2150 1.2429 0.8167 0.5970  -0.0388 -0.0801 656 GLU A OE1 
2814 O OE2 . GLU A 360 ? 1.2519 1.4901 0.9236 0.6197  -0.0226 -0.0827 656 GLU A OE2 
2815 N N   . SER A 361 ? 0.9454 1.1183 0.8173 0.3980  -0.0375 -0.0601 657 SER A N   
2816 C CA  A SER A 361 ? 0.9280 1.1902 0.8638 0.3815  -0.0393 -0.0571 657 SER A CA  
2817 C CA  B SER A 361 ? 0.8774 1.1388 0.8132 0.3812  -0.0394 -0.0570 657 SER A CA  
2818 C C   . SER A 361 ? 0.8409 1.1544 0.8469 0.3167  -0.0346 -0.0517 657 SER A C   
2819 O O   . SER A 361 ? 0.7589 1.1738 0.8201 0.3012  -0.0315 -0.0511 657 SER A O   
2820 C CB  A SER A 361 ? 0.9298 1.1225 0.8376 0.3844  -0.0513 -0.0540 657 SER A CB  
2821 C CB  B SER A 361 ? 0.9325 1.1240 0.8417 0.3819  -0.0513 -0.0537 657 SER A CB  
2822 O OG  A SER A 361 ? 0.9566 1.0933 0.7887 0.4474  -0.0564 -0.0582 657 SER A OG  
2823 O OG  B SER A 361 ? 0.9497 1.0736 0.8664 0.3272  -0.0549 -0.0476 657 SER A OG  
2824 N N   . PHE A 362 ? 0.8025 1.0463 0.8016 0.2785  -0.0350 -0.0478 658 PHE A N   
2825 C CA  . PHE A 362 ? 0.7567 1.0364 0.8108 0.2238  -0.0317 -0.0425 658 PHE A CA  
2826 C C   . PHE A 362 ? 0.7169 1.0797 0.7991 0.2174  -0.0200 -0.0433 658 PHE A C   
2827 O O   . PHE A 362 ? 0.6793 1.1054 0.8079 0.1813  -0.0167 -0.0399 658 PHE A O   
2828 C CB  . PHE A 362 ? 0.7254 0.9198 0.7643 0.1905  -0.0359 -0.0379 658 PHE A CB  
2829 C CG  . PHE A 362 ? 0.6825 0.9037 0.7673 0.1436  -0.0336 -0.0324 658 PHE A CG  
2830 C CD1 . PHE A 362 ? 0.6331 0.8736 0.7515 0.1200  -0.0375 -0.0297 658 PHE A CD1 
2831 C CD2 . PHE A 362 ? 0.6775 0.9014 0.7651 0.1260  -0.0278 -0.0303 658 PHE A CD2 
2832 C CE1 . PHE A 362 ? 0.6218 0.8744 0.7697 0.0819  -0.0361 -0.0252 658 PHE A CE1 
2833 C CE2 . PHE A 362 ? 0.6458 0.8836 0.7645 0.0869  -0.0266 -0.0246 658 PHE A CE2 
2834 C CZ  . PHE A 362 ? 0.6041 0.8531 0.7505 0.0660  -0.0309 -0.0223 658 PHE A CZ  
2835 N N   . ILE A 363 ? 0.7464 1.1054 0.7948 0.2493  -0.0135 -0.0476 659 ILE A N   
2836 C CA  . ILE A 363 ? 0.7365 1.1879 0.8096 0.2470  -0.0006 -0.0484 659 ILE A CA  
2837 C C   . ILE A 363 ? 0.6900 1.2608 0.8022 0.2579  0.0026  -0.0504 659 ILE A C   
2838 O O   . ILE A 363 ? 0.6500 1.3027 0.8069 0.2183  0.0087  -0.0467 659 ILE A O   
2839 C CB  . ILE A 363 ? 0.7426 1.1703 0.7655 0.2893  0.0062  -0.0543 659 ILE A CB  
2840 C CG1 . ILE A 363 ? 0.7826 1.1032 0.7703 0.2672  0.0024  -0.0520 659 ILE A CG1 
2841 C CG2 . ILE A 363 ? 0.7529 1.2942 0.8016 0.2925  0.0215  -0.0554 659 ILE A CG2 
2842 C CD1 . ILE A 363 ? 0.7346 1.0790 0.7535 0.2187  0.0090  -0.0454 659 ILE A CD1 
2843 N N   . LYS A 364 ? 0.7230 1.3036 0.8137 0.3101  -0.0026 -0.0558 660 LYS A N   
2844 C CA  . LYS A 364 ? 0.7014 1.4024 0.8300 0.3226  -0.0024 -0.0579 660 LYS A CA  
2845 C C   . LYS A 364 ? 0.6357 1.3582 0.8119 0.2648  -0.0086 -0.0525 660 LYS A C   
2846 O O   . LYS A 364 ? 0.5800 1.3996 0.7942 0.2331  -0.0045 -0.0511 660 LYS A O   
2847 C CB  . LYS A 364 ? 0.7453 1.4112 0.8231 0.3802  -0.0107 -0.0621 660 LYS A CB  
2848 C CG  . LYS A 364 ? 0.7452 1.5073 0.8328 0.3867  -0.0110 -0.0629 660 LYS A CG  
2849 C CD  . LYS A 364 ? 0.8589 1.5720 0.9003 0.4306  -0.0222 -0.0651 660 LYS A CD  
2850 C CE  . LYS A 364 ? 0.8289 1.6323 0.8976 0.4192  -0.0259 -0.0649 660 LYS A CE  
2851 N NZ  . LYS A 364 ? 0.9949 1.7406 1.0252 0.4518  -0.0374 -0.0659 660 LYS A NZ  
2852 N N   . HIS A 365 ? 0.6205 1.2405 0.7843 0.2444  -0.0183 -0.0492 661 HIS A N   
2853 C CA  . HIS A 365 ? 0.6101 1.2358 0.8104 0.1915  -0.0235 -0.0449 661 HIS A CA  
2854 C C   . HIS A 365 ? 0.5947 1.2494 0.8219 0.1368  -0.0155 -0.0404 661 HIS A C   
2855 O O   . HIS A 365 ? 0.5752 1.2898 0.8335 0.0978  -0.0158 -0.0389 661 HIS A O   
2856 C CB  . HIS A 365 ? 0.6370 1.1494 0.8164 0.1807  -0.0327 -0.0419 661 HIS A CB  
2857 C CG  . HIS A 365 ? 0.6064 1.1145 0.8156 0.1312  -0.0369 -0.0383 661 HIS A CG  
2858 N ND1 . HIS A 365 ? 0.6158 1.0512 0.8217 0.0984  -0.0380 -0.0337 661 HIS A ND1 
2859 C CD2 . HIS A 365 ? 0.5605 1.1283 0.7983 0.1107  -0.0408 -0.0394 661 HIS A CD2 
2860 C CE1 . HIS A 365 ? 0.5737 1.0171 0.8007 0.0647  -0.0417 -0.0324 661 HIS A CE1 
2861 N NE2 . HIS A 365 ? 0.5731 1.0922 0.8182 0.0683  -0.0436 -0.0360 661 HIS A NE2 
2862 N N   . MET A 366 ? 0.6517 1.2563 0.8601 0.1309  -0.0093 -0.0379 662 MET A N   
2863 C CA  . MET A 366 ? 0.6229 1.2437 0.8466 0.0815  -0.0020 -0.0323 662 MET A CA  
2864 C C   . MET A 366 ? 0.6080 1.3529 0.8575 0.0688  0.0077  -0.0330 662 MET A C   
2865 O O   . MET A 366 ? 0.6244 1.4023 0.8923 0.0163  0.0094  -0.0287 662 MET A O   
2866 C CB  . MET A 366 ? 0.6213 1.1762 0.8165 0.0859  0.0026  -0.0300 662 MET A CB  
2867 C CG  . MET A 366 ? 0.6011 1.0737 0.7909 0.0489  -0.0024 -0.0236 662 MET A CG  
2868 S SD  . MET A 366 ? 0.6771 1.0897 0.8323 0.0592  0.0018  -0.0219 662 MET A SD  
2869 C CE  . MET A 366 ? 0.6769 1.0694 0.8375 0.0054  0.0039  -0.0122 662 MET A CE  
2870 N N   . GLU A 367 ? 0.5229 1.3382 0.7688 0.1162  0.0138  -0.0385 663 GLU A N   
2871 C CA  . GLU A 367 ? 0.5594 1.5063 0.8290 0.1061  0.0237  -0.0391 663 GLU A CA  
2872 C C   . GLU A 367 ? 0.5720 1.5556 0.8566 0.0720  0.0158  -0.0381 663 GLU A C   
2873 O O   . GLU A 367 ? 0.6066 1.6417 0.8992 0.0220  0.0203  -0.0342 663 GLU A O   
2874 C CB  . GLU A 367 ? 0.5889 1.5671 0.8293 0.1705  0.0279  -0.0451 663 GLU A CB  
2875 C CG  . GLU A 367 ? 0.6693 1.6117 0.8841 0.2045  0.0376  -0.0474 663 GLU A CG  
2876 C CD  . GLU A 367 ? 0.7350 1.6848 0.9064 0.2733  0.0384  -0.0543 663 GLU A CD  
2877 O OE1 . GLU A 367 ? 0.7761 1.7686 0.9415 0.2937  0.0315  -0.0563 663 GLU A OE1 
2878 O OE2 . GLU A 367 ? 0.8180 1.7272 0.9556 0.3075  0.0452  -0.0578 663 GLU A OE2 
2879 N N   . ASN A 368 ? 0.6048 1.5580 0.8868 0.0978  0.0038  -0.0417 664 ASN A N   
2880 C CA  . ASN A 368 ? 0.5978 1.5801 0.8911 0.0681  -0.0040 -0.0417 664 ASN A CA  
2881 C C   . ASN A 368 ? 0.6327 1.5823 0.9399 -0.0003 -0.0065 -0.0369 664 ASN A C   
2882 O O   . ASN A 368 ? 0.7035 1.6930 1.0128 -0.0451 -0.0066 -0.0353 664 ASN A O   
2883 C CB  . ASN A 368 ? 0.5885 1.5317 0.8721 0.1100  -0.0159 -0.0458 664 ASN A CB  
2884 C CG  . ASN A 368 ? 0.6198 1.5803 0.8740 0.1785  -0.0150 -0.0504 664 ASN A CG  
2885 O OD1 . ASN A 368 ? 0.6225 1.6494 0.8682 0.1933  -0.0067 -0.0517 664 ASN A OD1 
2886 N ND2 . ASN A 368 ? 0.6146 1.5111 0.8459 0.2204  -0.0243 -0.0528 664 ASN A ND2 
2887 N N   . GLU A 369 ? 0.6235 1.4966 0.9332 -0.0088 -0.0093 -0.0347 665 GLU A N   
2888 C CA  . GLU A 369 ? 0.6306 1.4482 0.9374 -0.0679 -0.0131 -0.0303 665 GLU A CA  
2889 C C   . GLU A 369 ? 0.6853 1.5333 0.9874 -0.1198 -0.0029 -0.0244 665 GLU A C   
2890 O O   . GLU A 369 ? 0.7025 1.5388 0.9922 -0.1721 -0.0054 -0.0218 665 GLU A O   
2891 C CB  . GLU A 369 ? 0.5928 1.2789 0.8754 -0.0569 -0.0178 -0.0277 665 GLU A CB  
2892 C CG  . GLU A 369 ? 0.6087 1.2515 0.8879 -0.0174 -0.0276 -0.0317 665 GLU A CG  
2893 C CD  . GLU A 369 ? 0.5804 1.2047 0.8641 -0.0425 -0.0375 -0.0333 665 GLU A CD  
2894 O OE1 . GLU A 369 ? 0.5177 1.2188 0.8177 -0.0631 -0.0401 -0.0361 665 GLU A OE1 
2895 O OE2 . GLU A 369 ? 0.6066 1.1437 0.8759 -0.0424 -0.0426 -0.0319 665 GLU A OE2 
2896 N N   . TYR A 370 ? 0.6724 1.5379 0.9695 -0.1052 0.0086  -0.0219 666 TYR A N   
2897 C CA  . TYR A 370 ? 0.6930 1.5861 0.9787 -0.1548 0.0192  -0.0153 666 TYR A CA  
2898 C C   . TYR A 370 ? 0.7406 1.7135 1.0217 -0.1755 0.0211  -0.0162 666 TYR A C   
2899 O O   . TYR A 370 ? 0.7631 1.7326 1.0242 -0.2339 0.0230  -0.0109 666 TYR A O   
2900 C CB  . TYR A 370 ? 0.6431 1.5402 0.9208 -0.1293 0.0316  -0.0130 666 TYR A CB  
2901 C CG  . TYR A 370 ? 0.6674 1.4292 0.9135 -0.1297 0.0281  -0.0082 666 TYR A CG  
2902 C CD1 . TYR A 370 ? 0.6359 1.3166 0.8749 -0.0874 0.0187  -0.0118 666 TYR A CD1 
2903 C CD2 . TYR A 370 ? 0.7128 1.4307 0.9330 -0.1743 0.0336  0.0008  666 TYR A CD2 
2904 C CE1 . TYR A 370 ? 0.6496 1.2239 0.8637 -0.0889 0.0146  -0.0075 666 TYR A CE1 
2905 C CE2 . TYR A 370 ? 0.7387 1.3418 0.9302 -0.1698 0.0289  0.0052  666 TYR A CE2 
2906 C CZ  . TYR A 370 ? 0.7014 1.2402 0.8936 -0.1271 0.0192  0.0007  666 TYR A CZ  
2907 O OH  . TYR A 370 ? 0.7467 1.1881 0.9140 -0.1236 0.0139  0.0051  666 TYR A OH  
2908 N N   . ARG A 371 ? 0.8480 1.8881 1.1405 -0.1294 0.0192  -0.0227 667 ARG A N   
2909 C CA  . ARG A 371 ? 0.8653 1.9942 1.1547 -0.1464 0.0197  -0.0239 667 ARG A CA  
2910 C C   . ARG A 371 ? 0.8720 1.9789 1.1550 -0.1946 0.0099  -0.0236 667 ARG A C   
2911 O O   . ARG A 371 ? 0.9058 2.0209 1.1696 -0.2540 0.0119  -0.0191 667 ARG A O   
2912 C CB  . ARG A 371 ? 0.9174 2.1142 1.2140 -0.0803 0.0182  -0.0309 667 ARG A CB  
2913 C CG  . ARG A 371 ? 1.0134 2.3205 1.3074 -0.0915 0.0190  -0.0324 667 ARG A CG  
2914 C CD  . ARG A 371 ? 1.0868 2.4432 1.3814 -0.0250 0.0139  -0.0393 667 ARG A CD  
2915 N NE  . ARG A 371 ? 1.0856 2.3753 1.3843 -0.0054 0.0026  -0.0424 667 ARG A NE  
2916 C CZ  . ARG A 371 ? 1.1174 2.4190 1.4204 -0.0300 -0.0061 -0.0437 667 ARG A CZ  
2917 N NH1 . ARG A 371 ? 1.1764 2.5529 1.4784 -0.0764 -0.0053 -0.0425 667 ARG A NH1 
2918 N NH2 . ARG A 371 ? 1.1012 2.3384 1.4064 -0.0086 -0.0161 -0.0463 667 ARG A NH2 
2919 N N   . CYS A 372 ? 0.9137 1.9865 1.2063 -0.1706 -0.0011 -0.0283 668 CYS A N   
2920 C CA  . CYS A 372 ? 0.9355 1.9994 1.2210 -0.2070 -0.0107 -0.0298 668 CYS A CA  
2921 C C   . CYS A 372 ? 0.9149 1.8691 1.1872 -0.2412 -0.0179 -0.0279 668 CYS A C   
2922 O O   . CYS A 372 ? 0.9620 1.8932 1.2256 -0.2629 -0.0274 -0.0306 668 CYS A O   
2923 C CB  . CYS A 372 ? 0.9987 2.1024 1.2979 -0.1604 -0.0187 -0.0364 668 CYS A CB  
2924 S SG  . CYS A 372 ? 1.1391 2.1652 1.4491 -0.0987 -0.0264 -0.0399 668 CYS A SG  
2925 N N   . ARG A 373 ? 0.8097 1.6966 1.0767 -0.2450 -0.0141 -0.0238 669 ARG A N   
2926 C CA  . ARG A 373 ? 0.7798 1.5610 1.0258 -0.2772 -0.0211 -0.0218 669 ARG A CA  
2927 C C   . ARG A 373 ? 0.7852 1.5109 1.0037 -0.3133 -0.0138 -0.0138 669 ARG A C   
2928 O O   . ARG A 373 ? 0.7562 1.3866 0.9425 -0.3447 -0.0195 -0.0114 669 ARG A O   
2929 C CB  . ARG A 373 ? 0.6854 1.4175 0.9503 -0.2340 -0.0292 -0.0259 669 ARG A CB  
2930 C CG  . ARG A 373 ? 0.6596 1.2992 0.9033 -0.2596 -0.0402 -0.0274 669 ARG A CG  
2931 C CD  . ARG A 373 ? 0.6422 1.1984 0.8839 -0.2075 -0.0433 -0.0280 669 ARG A CD  
2932 N NE  . ARG A 373 ? 0.6169 1.0858 0.8329 -0.2179 -0.0522 -0.0301 669 ARG A NE  
2933 C CZ  . ARG A 373 ? 0.6391 1.0290 0.8455 -0.1865 -0.0546 -0.0296 669 ARG A CZ  
2934 N NH1 . ARG A 373 ? 0.5889 0.9687 0.8069 -0.1481 -0.0503 -0.0268 669 ARG A NH1 
2935 N NH2 . ARG A 373 ? 0.6186 0.9403 0.8000 -0.1950 -0.0616 -0.0322 669 ARG A NH2 
2936 N N   . GLY A 374 ? 0.7747 1.5507 0.9986 -0.3073 -0.0017 -0.0097 670 GLY A N   
2937 C CA  . GLY A 374 ? 0.8101 1.5360 1.0047 -0.3405 0.0059  -0.0010 670 GLY A CA  
2938 C C   . GLY A 374 ? 0.7999 1.4577 0.9974 -0.3121 0.0065  0.0015  670 GLY A C   
2939 O O   . GLY A 374 ? 0.8144 1.4055 0.9760 -0.3336 0.0112  0.0096  670 GLY A O   
2940 N N   . GLY A 375 ? 0.7095 1.3508 0.9285 -0.2534 0.0009  -0.0045 671 GLY A N   
2941 C CA  . GLY A 375 ? 0.7024 1.2552 0.9074 -0.2162 0.0001  -0.0024 671 GLY A CA  
2942 C C   . GLY A 375 ? 0.6880 1.2072 0.9072 -0.1694 -0.0093 -0.0086 671 GLY A C   
2943 O O   . GLY A 375 ? 0.6802 1.2345 0.9171 -0.1638 -0.0157 -0.0144 671 GLY A O   
2944 N N   . CYS A 376 ? 0.6768 1.1284 0.8848 -0.1389 -0.0104 -0.0069 672 CYS A N   
2945 C CA  . CYS A 376 ? 0.6219 1.0339 0.8361 -0.0993 -0.0184 -0.0112 672 CYS A CA  
2946 C C   . CYS A 376 ? 0.6265 0.9537 0.8194 -0.0924 -0.0210 -0.0065 672 CYS A C   
2947 O O   . CYS A 376 ? 0.6298 0.9493 0.8145 -0.0767 -0.0167 -0.0046 672 CYS A O   
2948 C CB  . CYS A 376 ? 0.5925 1.0549 0.8204 -0.0558 -0.0159 -0.0165 672 CYS A CB  
2949 S SG  . CYS A 376 ? 0.5795 0.9805 0.8009 -0.0142 -0.0255 -0.0200 672 CYS A SG  
2950 N N   . PRO A 377 ? 0.6367 0.9024 0.8176 -0.1019 -0.0284 -0.0050 673 PRO A N   
2951 C CA  . PRO A 377 ? 0.6348 0.8342 0.7983 -0.0909 -0.0320 -0.0007 673 PRO A CA  
2952 C C   . PRO A 377 ? 0.6129 0.8104 0.7854 -0.0574 -0.0341 -0.0032 673 PRO A C   
2953 O O   . PRO A 377 ? 0.5491 0.7597 0.7341 -0.0407 -0.0374 -0.0080 673 PRO A O   
2954 C CB  . PRO A 377 ? 0.6608 0.8123 0.8132 -0.0979 -0.0395 -0.0009 673 PRO A CB  
2955 C CG  . PRO A 377 ? 0.6317 0.8215 0.8025 -0.1004 -0.0415 -0.0075 673 PRO A CG  
2956 C CD  . PRO A 377 ? 0.6054 0.8666 0.7898 -0.1134 -0.0348 -0.0088 673 PRO A CD  
2957 N N   . ALA A 378 ? 0.5863 0.7620 0.7454 -0.0498 -0.0329 0.0002  674 ALA A N   
2958 C CA  . ALA A 378 ? 0.5549 0.7211 0.7113 -0.0247 -0.0354 -0.0025 674 ALA A CA  
2959 C C   . ALA A 378 ? 0.5940 0.7193 0.7336 -0.0246 -0.0396 0.0021  674 ALA A C   
2960 O O   . ALA A 378 ? 0.6087 0.7250 0.7356 -0.0361 -0.0370 0.0070  674 ALA A O   
2961 C CB  . ALA A 378 ? 0.5806 0.7860 0.7348 -0.0086 -0.0282 -0.0067 674 ALA A CB  
2962 N N   . ASP A 379 ? 0.5729 0.6760 0.7098 -0.0140 -0.0467 0.0010  675 ASP A N   
2963 C CA  . ASP A 379 ? 0.5687 0.6452 0.6934 -0.0154 -0.0533 0.0048  675 ASP A CA  
2964 C C   . ASP A 379 ? 0.6155 0.6805 0.7197 -0.0066 -0.0539 0.0016  675 ASP A C   
2965 O O   . ASP A 379 ? 0.5637 0.6156 0.6598 -0.0007 -0.0577 -0.0018 675 ASP A O   
2966 C CB  . ASP A 379 ? 0.5823 0.6516 0.7168 -0.0155 -0.0608 0.0061  675 ASP A CB  
2967 C CG  . ASP A 379 ? 0.6174 0.6774 0.7434 -0.0169 -0.0684 0.0104  675 ASP A CG  
2968 O OD1 . ASP A 379 ? 0.6262 0.6776 0.7353 -0.0186 -0.0696 0.0114  675 ASP A OD1 
2969 O OD2 . ASP A 379 ? 0.5857 0.6523 0.7213 -0.0149 -0.0735 0.0125  675 ASP A OD2 
2970 N N   . TRP A 380 ? 0.5766 0.6396 0.6646 -0.0068 -0.0500 0.0027  676 TRP A N   
2971 C CA  . TRP A 380 ? 0.5744 0.6188 0.6334 0.0034  -0.0502 -0.0015 676 TRP A CA  
2972 C C   . TRP A 380 ? 0.5799 0.5926 0.6225 -0.0026 -0.0615 -0.0018 676 TRP A C   
2973 O O   . TRP A 380 ? 0.6157 0.6006 0.6307 0.0041  -0.0639 -0.0068 676 TRP A O   
2974 C CB  . TRP A 380 ? 0.6196 0.6657 0.6631 0.0005  -0.0454 0.0012  676 TRP A CB  
2975 C CG  . TRP A 380 ? 0.6386 0.6709 0.6491 0.0151  -0.0421 -0.0046 676 TRP A CG  
2976 C CD1 . TRP A 380 ? 0.6665 0.7249 0.6700 0.0316  -0.0304 -0.0090 676 TRP A CD1 
2977 C CD2 . TRP A 380 ? 0.6562 0.6462 0.6304 0.0153  -0.0504 -0.0074 676 TRP A CD2 
2978 N NE1 . TRP A 380 ? 0.7215 0.7498 0.6830 0.0478  -0.0305 -0.0149 676 TRP A NE1 
2979 C CE2 . TRP A 380 ? 0.7417 0.7219 0.6817 0.0354  -0.0432 -0.0141 676 TRP A CE2 
2980 C CE3 . TRP A 380 ? 0.6586 0.6227 0.6235 -0.0006 -0.0636 -0.0051 676 TRP A CE3 
2981 C CZ2 . TRP A 380 ? 0.7593 0.6890 0.6485 0.0394  -0.0494 -0.0194 676 TRP A CZ2 
2982 C CZ3 . TRP A 380 ? 0.7290 0.6522 0.6484 -0.0027 -0.0704 -0.0096 676 TRP A CZ3 
2983 C CH2 . TRP A 380 ? 0.7272 0.6261 0.6057 0.0168  -0.0636 -0.0169 676 TRP A CH2 
2984 N N   . VAL A 381 ? 0.5686 0.5850 0.6224 -0.0155 -0.0689 0.0039  677 VAL A N   
2985 C CA  . VAL A 381 ? 0.6106 0.6147 0.6523 -0.0273 -0.0801 0.0046  677 VAL A CA  
2986 C C   . VAL A 381 ? 0.6356 0.6288 0.6740 -0.0303 -0.0820 0.0014  677 VAL A C   
2987 O O   . VAL A 381 ? 0.6176 0.5840 0.6261 -0.0427 -0.0890 -0.0003 677 VAL A O   
2988 C CB  . VAL A 381 ? 0.5919 0.6212 0.6543 -0.0334 -0.0870 0.0113  677 VAL A CB  
2989 C CG1 . VAL A 381 ? 0.6015 0.6423 0.6621 -0.0484 -0.0979 0.0124  677 VAL A CG1 
2990 C CG2 . VAL A 381 ? 0.6421 0.6679 0.6913 -0.0314 -0.0879 0.0152  677 VAL A CG2 
2991 N N   . TRP A 382 ? 0.6156 0.6246 0.6782 -0.0219 -0.0765 0.0009  678 TRP A N   
2992 C CA  . TRP A 382 ? 0.6515 0.6493 0.7092 -0.0228 -0.0777 -0.0011 678 TRP A CA  
2993 C C   . TRP A 382 ? 0.6522 0.6263 0.6860 -0.0040 -0.0726 -0.0068 678 TRP A C   
2994 O O   . TRP A 382 ? 0.6670 0.6064 0.6708 -0.0042 -0.0760 -0.0086 678 TRP A O   
2995 C CB  . TRP A 382 ? 0.6274 0.6569 0.7220 -0.0225 -0.0760 0.0012  678 TRP A CB  
2996 C CG  . TRP A 382 ? 0.6462 0.6965 0.7540 -0.0359 -0.0823 0.0058  678 TRP A CG  
2997 C CD1 . TRP A 382 ? 0.6571 0.7267 0.7726 -0.0393 -0.0869 0.0097  678 TRP A CD1 
2998 C CD2 . TRP A 382 ? 0.6482 0.7104 0.7620 -0.0455 -0.0846 0.0071  678 TRP A CD2 
2999 N NE1 . TRP A 382 ? 0.6793 0.7807 0.8084 -0.0474 -0.0921 0.0128  678 TRP A NE1 
3000 C CE2 . TRP A 382 ? 0.6575 0.7561 0.7865 -0.0536 -0.0899 0.0114  678 TRP A CE2 
3001 C CE3 . TRP A 382 ? 0.6721 0.7203 0.7775 -0.0466 -0.0827 0.0056  678 TRP A CE3 
3002 C CZ2 . TRP A 382 ? 0.6420 0.7721 0.7814 -0.0647 -0.0918 0.0138  678 TRP A CZ2 
3003 C CZ3 . TRP A 382 ? 0.6695 0.7387 0.7817 -0.0604 -0.0846 0.0087  678 TRP A CZ3 
3004 C CH2 . TRP A 382 ? 0.6701 0.7841 0.8010 -0.0701 -0.0884 0.0126  678 TRP A CH2 
3005 N N   . ILE A 383 ? 0.6386 0.6322 0.6808 0.0128  -0.0646 -0.0093 679 ILE A N   
3006 C CA  . ILE A 383 ? 0.6371 0.6244 0.6596 0.0381  -0.0597 -0.0150 679 ILE A CA  
3007 C C   . ILE A 383 ? 0.7444 0.6765 0.7089 0.0491  -0.0625 -0.0195 679 ILE A C   
3008 O O   . ILE A 383 ? 0.7517 0.6465 0.6779 0.0681  -0.0640 -0.0236 679 ILE A O   
3009 C CB  . ILE A 383 ? 0.6119 0.6514 0.6609 0.0493  -0.0499 -0.0162 679 ILE A CB  
3010 C CG1 . ILE A 383 ? 0.5916 0.6707 0.6839 0.0363  -0.0486 -0.0130 679 ILE A CG1 
3011 C CG2 . ILE A 383 ? 0.6244 0.6723 0.6513 0.0825  -0.0446 -0.0228 679 ILE A CG2 
3012 C CD1 . ILE A 383 ? 0.6182 0.7033 0.7173 0.0462  -0.0509 -0.0154 679 ILE A CD1 
3013 N N   . VAL A 384 ? 0.7076 0.6265 0.6570 0.0389  -0.0640 -0.0191 680 VAL A N   
3014 C CA  . VAL A 384 ? 0.7580 0.6164 0.6431 0.0490  -0.0670 -0.0248 680 VAL A CA  
3015 C C   . VAL A 384 ? 0.8088 0.6059 0.6522 0.0298  -0.0780 -0.0243 680 VAL A C   
3016 O O   . VAL A 384 ? 0.7749 0.5836 0.6382 -0.0029 -0.0849 -0.0188 680 VAL A O   
3017 C CB  . VAL A 384 ? 0.7824 0.6415 0.6596 0.0387  -0.0674 -0.0242 680 VAL A CB  
3018 C CG1 . VAL A 384 ? 0.8560 0.6419 0.6581 0.0444  -0.0725 -0.0310 680 VAL A CG1 
3019 C CG2 . VAL A 384 ? 0.7753 0.6885 0.6821 0.0549  -0.0552 -0.0241 680 VAL A CG2 
3020 N N   . PRO A 385 ? 0.8751 0.6071 0.6561 0.0488  -0.0799 -0.0297 681 PRO A N   
3021 C CA  . PRO A 385 ? 0.9277 0.5893 0.6559 0.0238  -0.0904 -0.0282 681 PRO A CA  
3022 C C   . PRO A 385 ? 1.0129 0.6439 0.7116 -0.0156 -0.1000 -0.0272 681 PRO A C   
3023 O O   . PRO A 385 ? 0.9379 0.5741 0.6316 -0.0125 -0.0994 -0.0302 681 PRO A O   
3024 C CB  . PRO A 385 ? 1.0154 0.5985 0.6650 0.0612  -0.0900 -0.0354 681 PRO A CB  
3025 C CG  . PRO A 385 ? 1.0243 0.6684 0.7125 0.1067  -0.0789 -0.0386 681 PRO A CG  
3026 C CD  . PRO A 385 ? 0.9406 0.6636 0.6938 0.0968  -0.0723 -0.0367 681 PRO A CD  
3027 N N   . PRO A 386 ? 1.0290 0.6310 0.7046 -0.0554 -0.1094 -0.0228 682 PRO A N   
3028 C CA  . PRO A 386 ? 1.0413 0.6300 0.6931 -0.1004 -0.1203 -0.0213 682 PRO A CA  
3029 C C   . PRO A 386 ? 1.1430 0.6235 0.6908 -0.1088 -0.1283 -0.0282 682 PRO A C   
3030 O O   . PRO A 386 ? 1.1972 0.6569 0.7123 -0.1553 -0.1397 -0.0270 682 PRO A O   
3031 C CB  . PRO A 386 ? 1.0547 0.6687 0.7259 -0.1403 -0.1252 -0.0134 682 PRO A CB  
3032 C CG  . PRO A 386 ? 1.0452 0.5998 0.6762 -0.1202 -0.1217 -0.0144 682 PRO A CG  
3033 C CD  . PRO A 386 ? 1.0222 0.6076 0.6906 -0.0642 -0.1104 -0.0186 682 PRO A CD  
3034 N N   . MET A 387 ? 1.2075 0.6196 0.6981 -0.0646 -0.1233 -0.0358 683 MET A N   
3035 C CA  . MET A 387 ? 1.2884 0.5958 0.6766 -0.0583 -0.1291 -0.0448 683 MET A CA  
3036 C C   . MET A 387 ? 1.3080 0.6146 0.6889 0.0081  -0.1174 -0.0530 683 MET A C   
3037 O O   . MET A 387 ? 1.2402 0.6069 0.6765 0.0444  -0.1069 -0.0514 683 MET A O   
3038 C CB  . MET A 387 ? 1.4792 0.6629 0.7607 -0.0766 -0.1384 -0.0459 683 MET A CB  
3039 C CG  . MET A 387 ? 1.4166 0.5658 0.6760 -0.0251 -0.1313 -0.0471 683 MET A CG  
3040 S SD  . MET A 387 ? 1.7190 0.7091 0.8421 -0.0429 -0.1423 -0.0463 683 MET A SD  
3041 C CE  . MET A 387 ? 1.7169 0.5895 0.7190 -0.0513 -0.1509 -0.0535 683 MET A CE  
3042 N N   . SER A 388 ? 1.3844 0.6324 0.6989 0.0222  -0.1190 -0.0619 684 SER A N   
3043 C CA  . SER A 388 ? 1.3895 0.6281 0.6781 0.0882  -0.1077 -0.0710 684 SER A CA  
3044 C C   . SER A 388 ? 1.2672 0.6376 0.6640 0.1128  -0.0931 -0.0675 684 SER A C   
3045 O O   . SER A 388 ? 1.3185 0.7190 0.7239 0.1654  -0.0819 -0.0715 684 SER A O   
3046 C CB  . SER A 388 ? 1.4609 0.6220 0.6793 0.1321  -0.1069 -0.0753 684 SER A CB  
3047 O OG  . SER A 388 ? 1.6233 0.6395 0.7189 0.1122  -0.1202 -0.0793 684 SER A OG  
3048 N N   . GLY A 389 ? 1.1854 0.6352 0.6610 0.0741  -0.0939 -0.0595 685 GLY A N   
3049 C CA  . GLY A 389 ? 1.1211 0.6838 0.6931 0.0873  -0.0817 -0.0543 685 GLY A CA  
3050 C C   . GLY A 389 ? 1.1228 0.7179 0.6927 0.1369  -0.0674 -0.0607 685 GLY A C   
3051 O O   . GLY A 389 ? 1.0595 0.7185 0.6742 0.1649  -0.0571 -0.0598 685 GLY A O   
3052 N N   . SER A 390 ? 1.1561 0.7136 0.6729 0.1473  -0.0665 -0.0675 686 SER A N   
3053 C CA  . SER A 390 ? 1.1271 0.7386 0.6542 0.1882  -0.0509 -0.0721 686 SER A CA  
3054 C C   . SER A 390 ? 1.1928 0.7697 0.6584 0.2494  -0.0442 -0.0827 686 SER A C   
3055 O O   . SER A 390 ? 1.1696 0.8037 0.6431 0.2883  -0.0298 -0.0872 686 SER A O   
3056 C CB  . SER A 390 ? 1.1221 0.7192 0.6217 0.1767  -0.0509 -0.0746 686 SER A CB  
3057 O OG  . SER A 390 ? 1.2058 0.6889 0.6055 0.1798  -0.0617 -0.0839 686 SER A OG  
3058 N N   . ILE A 391 ? 1.2708 0.7562 0.6699 0.2614  -0.0539 -0.0867 687 ILE A N   
3059 C CA  . ILE A 391 ? 1.2613 0.7239 0.6076 0.3284  -0.0477 -0.0955 687 ILE A CA  
3060 C C   . ILE A 391 ? 1.2407 0.7743 0.6494 0.3433  -0.0441 -0.0899 687 ILE A C   
3061 O O   . ILE A 391 ? 1.3048 0.8245 0.6729 0.4002  -0.0414 -0.0958 687 ILE A O   
3062 C CB  . ILE A 391 ? 1.4300 0.7350 0.6442 0.3455  -0.0598 -0.1044 687 ILE A CB  
3063 C CG1 . ILE A 391 ? 1.5358 0.7696 0.7321 0.2981  -0.0751 -0.0972 687 ILE A CG1 
3064 C CG2 . ILE A 391 ? 1.5472 0.7797 0.6887 0.3364  -0.0631 -0.1124 687 ILE A CG2 
3065 C CD1 . ILE A 391 ? 1.6881 0.7531 0.7409 0.3079  -0.0877 -0.1050 687 ILE A CD1 
3066 N N   . THR A 392 ? 1.1867 0.7954 0.6882 0.2974  -0.0447 -0.0791 688 THR A N   
3067 C CA  . THR A 392 ? 1.1491 0.8456 0.7231 0.3053  -0.0399 -0.0738 688 THR A CA  
3068 C C   . THR A 392 ? 1.0422 0.8662 0.7014 0.2995  -0.0262 -0.0703 688 THR A C   
3069 O O   . THR A 392 ? 1.0336 0.8742 0.7146 0.2676  -0.0238 -0.0670 688 THR A O   
3070 C CB  . THR A 392 ? 1.1306 0.8149 0.7410 0.2571  -0.0501 -0.0645 688 THR A CB  
3071 O OG1 . THR A 392 ? 1.0519 0.7845 0.7268 0.2062  -0.0502 -0.0570 688 THR A OG1 
3072 C CG2 . THR A 392 ? 1.1561 0.7119 0.6795 0.2447  -0.0639 -0.0659 688 THR A CG2 
3073 N N   . PRO A 393 ? 0.9872 0.9027 0.6923 0.3263  -0.0179 -0.0702 689 PRO A N   
3074 C CA  . PRO A 393 ? 0.9321 0.9665 0.7042 0.3186  -0.0039 -0.0673 689 PRO A CA  
3075 C C   . PRO A 393 ? 0.8702 0.9440 0.7128 0.2574  -0.0051 -0.0566 689 PRO A C   
3076 O O   . PRO A 393 ? 0.8305 0.9703 0.7085 0.2398  0.0050  -0.0531 689 PRO A O   
3077 C CB  . PRO A 393 ? 0.9336 1.0530 0.7294 0.3605  0.0022  -0.0704 689 PRO A CB  
3078 C CG  . PRO A 393 ? 0.9303 0.9868 0.7089 0.3628  -0.0113 -0.0691 689 PRO A CG  
3079 C CD  . PRO A 393 ? 1.0105 0.9276 0.7047 0.3625  -0.0214 -0.0723 689 PRO A CD  
3080 N N   . VAL A 394 ? 0.8467 0.8790 0.7040 0.2259  -0.0166 -0.0512 690 VAL A N   
3081 C CA  . VAL A 394 ? 0.8164 0.8817 0.7325 0.1764  -0.0179 -0.0419 690 VAL A CA  
3082 C C   . VAL A 394 ? 0.8118 0.8453 0.7163 0.1490  -0.0195 -0.0385 690 VAL A C   
3083 O O   . VAL A 394 ? 0.7773 0.8470 0.7216 0.1182  -0.0170 -0.0312 690 VAL A O   
3084 C CB  . VAL A 394 ? 0.7867 0.8231 0.7194 0.1563  -0.0288 -0.0378 690 VAL A CB  
3085 C CG1 . VAL A 394 ? 0.7830 0.8618 0.7332 0.1807  -0.0273 -0.0401 690 VAL A CG1 
3086 C CG2 . VAL A 394 ? 0.8408 0.7814 0.7176 0.1527  -0.0401 -0.0395 690 VAL A CG2 
3087 N N   . PHE A 395 ? 0.8595 0.8202 0.7030 0.1595  -0.0247 -0.0437 691 PHE A N   
3088 C CA  . PHE A 395 ? 0.8831 0.8182 0.7122 0.1354  -0.0274 -0.0411 691 PHE A CA  
3089 C C   . PHE A 395 ? 0.8255 0.8244 0.6763 0.1367  -0.0138 -0.0389 691 PHE A C   
3090 O O   . PHE A 395 ? 0.8179 0.8261 0.6871 0.1071  -0.0147 -0.0316 691 PHE A O   
3091 C CB  . PHE A 395 ? 0.9301 0.7770 0.6799 0.1489  -0.0346 -0.0491 691 PHE A CB  
3092 C CG  . PHE A 395 ? 0.9311 0.7496 0.6605 0.1231  -0.0401 -0.0473 691 PHE A CG  
3093 C CD1 . PHE A 395 ? 0.9589 0.7956 0.6714 0.1368  -0.0303 -0.0500 691 PHE A CD1 
3094 C CD2 . PHE A 395 ? 0.9067 0.6867 0.6323 0.0856  -0.0551 -0.0430 691 PHE A CD2 
3095 C CE1 . PHE A 395 ? 0.9554 0.7641 0.6449 0.1142  -0.0366 -0.0483 691 PHE A CE1 
3096 C CE2 . PHE A 395 ? 0.9690 0.7312 0.6761 0.0631  -0.0620 -0.0413 691 PHE A CE2 
3097 C CZ  . PHE A 395 ? 0.9451 0.7167 0.6321 0.0778  -0.0534 -0.0441 691 PHE A CZ  
3098 N N   . HIS A 396 ? 0.8326 0.8786 0.6782 0.1716  -0.0011 -0.0446 692 HIS A N   
3099 C CA  . HIS A 396 ? 0.8363 0.9487 0.6949 0.1731  0.0139  -0.0429 692 HIS A CA  
3100 C C   . HIS A 396 ? 0.8058 1.0071 0.7276 0.1503  0.0223  -0.0353 692 HIS A C   
3101 O O   . HIS A 396 ? 0.7867 1.0547 0.7210 0.1461  0.0362  -0.0329 692 HIS A O   
3102 C CB  . HIS A 396 ? 0.9154 1.0405 0.7299 0.2254  0.0241  -0.0539 692 HIS A CB  
3103 C CG  . HIS A 396 ? 0.9723 0.9923 0.7095 0.2492  0.0145  -0.0630 692 HIS A CG  
3104 N ND1 . HIS A 396 ? 0.9960 0.9551 0.6950 0.2303  0.0089  -0.0631 692 HIS A ND1 
3105 C CD2 . HIS A 396 ? 1.0359 0.9927 0.7190 0.2870  0.0080  -0.0720 692 HIS A CD2 
3106 C CE1 . HIS A 396 ? 1.0678 0.9315 0.6920 0.2518  -0.0005 -0.0725 692 HIS A CE1 
3107 N NE2 . HIS A 396 ? 1.0647 0.9192 0.6744 0.2865  -0.0010 -0.0777 692 HIS A NE2 
3108 N N   . GLN A 397 ? 0.7631 0.9643 0.7197 0.1320  0.0141  -0.0313 693 GLN A N   
3109 C CA  . GLN A 397 ? 0.7287 1.0024 0.7368 0.1083  0.0196  -0.0254 693 GLN A CA  
3110 C C   . GLN A 397 ? 0.6864 0.9319 0.7125 0.0636  0.0133  -0.0152 693 GLN A C   
3111 O O   . GLN A 397 ? 0.6617 0.8551 0.6900 0.0545  0.0007  -0.0135 693 GLN A O   
3112 C CB  . GLN A 397 ? 0.7277 1.0190 0.7553 0.1241  0.0144  -0.0292 693 GLN A CB  
3113 C CG  . GLN A 397 ? 0.6754 1.0389 0.7512 0.0967  0.0182  -0.0243 693 GLN A CG  
3114 C CD  . GLN A 397 ? 0.6814 1.1466 0.7719 0.1021  0.0332  -0.0256 693 GLN A CD  
3115 O OE1 . GLN A 397 ? 0.6881 1.1983 0.7694 0.1453  0.0384  -0.0333 693 GLN A OE1 
3116 N NE2 . GLN A 397 ? 0.6796 1.1828 0.7885 0.0585  0.0404  -0.0176 693 GLN A NE2 
3117 N N   . GLU A 398 ? 0.6731 0.9520 0.7063 0.0375  0.0223  -0.0082 694 GLU A N   
3118 C CA  . GLU A 398 ? 0.6993 0.9524 0.7436 -0.0009 0.0169  0.0018  694 GLU A CA  
3119 C C   . GLU A 398 ? 0.6781 0.9474 0.7543 -0.0136 0.0122  0.0022  694 GLU A C   
3120 O O   . GLU A 398 ? 0.6556 0.9871 0.7524 -0.0081 0.0182  -0.0018 694 GLU A O   
3121 C CB  . GLU A 398 ? 0.6895 0.9726 0.7262 -0.0286 0.0286  0.0098  694 GLU A CB  
3122 C CG  . GLU A 398 ? 0.7507 1.0126 0.7520 -0.0185 0.0329  0.0104  694 GLU A CG  
3123 C CD  . GLU A 398 ? 0.7657 1.0672 0.7571 -0.0452 0.0471  0.0183  694 GLU A CD  
3124 O OE1 . GLU A 398 ? 0.7723 1.1213 0.7832 -0.0735 0.0539  0.0228  694 GLU A OE1 
3125 O OE2 . GLU A 398 ? 0.8188 1.1027 0.7789 -0.0415 0.0514  0.0204  694 GLU A OE2 
3126 N N   . MET A 399 ? 0.6665 0.8837 0.7450 -0.0280 0.0009  0.0066  695 MET A N   
3127 C CA  . MET A 399 ? 0.6723 0.8913 0.7740 -0.0381 -0.0049 0.0064  695 MET A CA  
3128 C C   . MET A 399 ? 0.7058 0.8845 0.7988 -0.0660 -0.0096 0.0149  695 MET A C   
3129 O O   . MET A 399 ? 0.7514 0.8831 0.8255 -0.0643 -0.0158 0.0194  695 MET A O   
3130 C CB  . MET A 399 ? 0.6105 0.7993 0.7174 -0.0159 -0.0154 0.0011  695 MET A CB  
3131 C CG  . MET A 399 ? 0.5955 0.8064 0.6997 0.0149  -0.0131 -0.0073 695 MET A CG  
3132 S SD  . MET A 399 ? 0.6096 0.7592 0.6974 0.0321  -0.0257 -0.0108 695 MET A SD  
3133 C CE  . MET A 399 ? 0.6044 0.7534 0.6587 0.0713  -0.0215 -0.0197 695 MET A CE  
3134 N N   . LEU A 400 ? 0.6713 0.8661 0.7724 -0.0901 -0.0077 0.0166  696 LEU A N   
3135 C CA  . LEU A 400 ? 0.7078 0.8493 0.7891 -0.1120 -0.0135 0.0233  696 LEU A CA  
3136 C C   . LEU A 400 ? 0.7042 0.8216 0.7993 -0.0992 -0.0237 0.0192  696 LEU A C   
3137 O O   . LEU A 400 ? 0.6667 0.8186 0.7852 -0.0965 -0.0236 0.0131  696 LEU A O   
3138 C CB  . LEU A 400 ? 0.7366 0.8954 0.8055 -0.1515 -0.0065 0.0273  696 LEU A CB  
3139 C CG  . LEU A 400 ? 0.7966 0.9777 0.8451 -0.1735 0.0049  0.0338  696 LEU A CG  
3140 C CD1 . LEU A 400 ? 0.8576 1.0614 0.8925 -0.2218 0.0113  0.0378  696 LEU A CD1 
3141 C CD2 . LEU A 400 ? 0.8287 0.9414 0.8397 -0.1698 0.0013  0.0420  696 LEU A CD2 
3142 N N   . ASN A 401 ? 0.7021 0.7671 0.7823 -0.0888 -0.0325 0.0227  697 ASN A N   
3143 C CA  . ASN A 401 ? 0.7056 0.7507 0.7951 -0.0766 -0.0410 0.0197  697 ASN A CA  
3144 C C   . ASN A 401 ? 0.7667 0.7660 0.8273 -0.0920 -0.0437 0.0232  697 ASN A C   
3145 O O   . ASN A 401 ? 0.8062 0.7617 0.8302 -0.0991 -0.0447 0.0304  697 ASN A O   
3146 C CB  . ASN A 401 ? 0.6867 0.7157 0.7782 -0.0533 -0.0491 0.0206  697 ASN A CB  
3147 C CG  . ASN A 401 ? 0.6770 0.7093 0.7869 -0.0402 -0.0550 0.0163  697 ASN A CG  
3148 O OD1 . ASN A 401 ? 0.6804 0.7292 0.8047 -0.0444 -0.0528 0.0114  697 ASN A OD1 
3149 N ND2 . ASN A 401 ? 0.6584 0.6820 0.7677 -0.0254 -0.0625 0.0182  697 ASN A ND2 
3150 N N   . TYR A 402 ? 0.7795 0.7817 0.8488 -0.0964 -0.0456 0.0179  698 TYR A N   
3151 C CA  . TYR A 402 ? 0.8124 0.7591 0.8456 -0.1077 -0.0496 0.0191  698 TYR A CA  
3152 C C   . TYR A 402 ? 0.8236 0.7808 0.8756 -0.0987 -0.0534 0.0112  698 TYR A C   
3153 O O   . TYR A 402 ? 0.7480 0.7581 0.8386 -0.0921 -0.0518 0.0060  698 TYR A O   
3154 C CB  . TYR A 402 ? 0.8468 0.7793 0.8478 -0.1488 -0.0443 0.0227  698 TYR A CB  
3155 C CG  . TYR A 402 ? 0.8261 0.8365 0.8607 -0.1710 -0.0366 0.0188  698 TYR A CG  
3156 C CD1 . TYR A 402 ? 0.7995 0.8371 0.8476 -0.1853 -0.0381 0.0120  698 TYR A CD1 
3157 C CD2 . TYR A 402 ? 0.7664 0.8278 0.8171 -0.1744 -0.0281 0.0214  698 TYR A CD2 
3158 C CE1 . TYR A 402 ? 0.7619 0.8819 0.8413 -0.2009 -0.0323 0.0085  698 TYR A CE1 
3159 C CE2 . TYR A 402 ? 0.7624 0.9056 0.8430 -0.1872 -0.0208 0.0174  698 TYR A CE2 
3160 C CZ  . TYR A 402 ? 0.7699 0.9455 0.8662 -0.1998 -0.0234 0.0111  698 TYR A CZ  
3161 O OH  . TYR A 402 ? 0.7382 1.0057 0.8650 -0.2085 -0.0176 0.0070  698 TYR A OH  
3162 N N   . ARG A 403 ? 0.8506 0.7509 0.8680 -0.0949 -0.0588 0.0105  699 ARG A N   
3163 C CA  . ARG A 403 ? 0.8681 0.7700 0.8968 -0.0784 -0.0628 0.0035  699 ARG A CA  
3164 C C   . ARG A 403 ? 0.9070 0.7946 0.9162 -0.1079 -0.0631 -0.0017 699 ARG A C   
3165 O O   . ARG A 403 ? 1.0098 0.8289 0.9639 -0.1230 -0.0659 -0.0007 699 ARG A O   
3166 C CB  . ARG A 403 ? 0.9921 0.8464 0.9934 -0.0463 -0.0686 0.0048  699 ARG A CB  
3167 C CG  . ARG A 403 ? 1.0154 0.8924 1.0349 -0.0211 -0.0702 0.0100  699 ARG A CG  
3168 C CD  . ARG A 403 ? 1.0495 0.9775 1.1109 0.0001  -0.0713 0.0063  699 ARG A CD  
3169 N NE  . ARG A 403 ? 1.1102 1.0242 1.1561 0.0320  -0.0761 0.0063  699 ARG A NE  
3170 C CZ  . ARG A 403 ? 1.0713 1.0259 1.1436 0.0496  -0.0767 0.0032  699 ARG A CZ  
3171 N NH1 . ARG A 403 ? 1.0049 1.0027 1.1139 0.0372  -0.0735 0.0001  699 ARG A NH1 
3172 N NH2 . ARG A 403 ? 1.1066 1.0594 1.1640 0.0820  -0.0803 0.0036  699 ARG A NH2 
3173 N N   . LEU A 404 ? 0.8203 0.7687 0.8680 -0.1166 -0.0612 -0.0071 700 LEU A N   
3174 C CA  . LEU A 404 ? 0.8178 0.7652 0.8529 -0.1423 -0.0636 -0.0133 700 LEU A CA  
3175 C C   . LEU A 404 ? 0.7980 0.7364 0.8385 -0.1180 -0.0682 -0.0201 700 LEU A C   
3176 O O   . LEU A 404 ? 0.7770 0.7354 0.8452 -0.0858 -0.0678 -0.0199 700 LEU A O   
3177 C CB  . LEU A 404 ? 0.7489 0.7781 0.8209 -0.1641 -0.0598 -0.0153 700 LEU A CB  
3178 C CG  . LEU A 404 ? 0.7732 0.8302 0.8446 -0.1882 -0.0531 -0.0091 700 LEU A CG  
3179 C CD1 . LEU A 404 ? 0.6927 0.8468 0.8062 -0.1956 -0.0491 -0.0122 700 LEU A CD1 
3180 C CD2 . LEU A 404 ? 0.8785 0.8768 0.8931 -0.2306 -0.0539 -0.0056 700 LEU A CD2 
3181 N N   . THR A 405 ? 0.8233 0.7294 0.8319 -0.1373 -0.0725 -0.0261 701 THR A N   
3182 C CA  . THR A 405 ? 0.7856 0.6872 0.7963 -0.1182 -0.0762 -0.0336 701 THR A CA  
3183 C C   . THR A 405 ? 0.7725 0.7183 0.7965 -0.1461 -0.0790 -0.0400 701 THR A C   
3184 O O   . THR A 405 ? 0.7992 0.7584 0.8122 -0.1857 -0.0794 -0.0394 701 THR A O   
3185 C CB  . THR A 405 ? 0.8754 0.6853 0.8231 -0.1067 -0.0803 -0.0365 701 THR A CB  
3186 O OG1 . THR A 405 ? 0.9243 0.7357 0.8756 -0.0817 -0.0822 -0.0437 701 THR A OG1 
3187 C CG2 . THR A 405 ? 0.9716 0.7182 0.8571 -0.1499 -0.0844 -0.0386 701 THR A CG2 
3188 N N   . PRO A 406 ? 0.7885 0.7665 0.8369 -0.1280 -0.0811 -0.0456 702 PRO A N   
3189 C CA  . PRO A 406 ? 0.7454 0.7269 0.8122 -0.0880 -0.0796 -0.0459 702 PRO A CA  
3190 C C   . PRO A 406 ? 0.7020 0.7140 0.8035 -0.0658 -0.0745 -0.0383 702 PRO A C   
3191 O O   . PRO A 406 ? 0.6663 0.7133 0.7887 -0.0757 -0.0720 -0.0343 702 PRO A O   
3192 C CB  . PRO A 406 ? 0.7038 0.7324 0.7931 -0.0885 -0.0827 -0.0515 702 PRO A CB  
3193 C CG  . PRO A 406 ? 0.7304 0.7554 0.7956 -0.1261 -0.0884 -0.0572 702 PRO A CG  
3194 C CD  . PRO A 406 ? 0.7697 0.7878 0.8239 -0.1540 -0.0861 -0.0521 702 PRO A CD  
3195 N N   . SER A 407 ? 0.7079 0.7107 0.8133 -0.0368 -0.0729 -0.0366 703 SER A N   
3196 C CA  . SER A 407 ? 0.6790 0.7031 0.8079 -0.0221 -0.0697 -0.0296 703 SER A CA  
3197 C C   . SER A 407 ? 0.6576 0.6988 0.7999 0.0011  -0.0684 -0.0290 703 SER A C   
3198 O O   . SER A 407 ? 0.6866 0.7141 0.8141 0.0129  -0.0687 -0.0333 703 SER A O   
3199 C CB  . SER A 407 ? 0.7230 0.7101 0.8290 -0.0196 -0.0696 -0.0249 703 SER A CB  
3200 O OG  . SER A 407 ? 0.7740 0.7238 0.8517 0.0022  -0.0712 -0.0267 703 SER A OG  
3201 N N   . PHE A 408 ? 0.6381 0.7088 0.8039 0.0054  -0.0666 -0.0237 704 PHE A N   
3202 C CA  . PHE A 408 ? 0.6087 0.6984 0.7838 0.0194  -0.0651 -0.0208 704 PHE A CA  
3203 C C   . PHE A 408 ? 0.6693 0.7555 0.8400 0.0300  -0.0655 -0.0165 704 PHE A C   
3204 O O   . PHE A 408 ? 0.6723 0.7533 0.8442 0.0235  -0.0665 -0.0127 704 PHE A O   
3205 C CB  . PHE A 408 ? 0.5747 0.6884 0.7653 0.0135  -0.0644 -0.0173 704 PHE A CB  
3206 C CG  . PHE A 408 ? 0.5919 0.7108 0.7824 0.0110  -0.0650 -0.0208 704 PHE A CG  
3207 C CD1 . PHE A 408 ? 0.5997 0.7244 0.7859 0.0164  -0.0639 -0.0225 704 PHE A CD1 
3208 C CD2 . PHE A 408 ? 0.5780 0.7017 0.7711 0.0058  -0.0666 -0.0223 704 PHE A CD2 
3209 C CE1 . PHE A 408 ? 0.5769 0.7048 0.7592 0.0157  -0.0656 -0.0252 704 PHE A CE1 
3210 C CE2 . PHE A 408 ? 0.5750 0.7093 0.7665 0.0083  -0.0688 -0.0252 704 PHE A CE2 
3211 C CZ  . PHE A 408 ? 0.6010 0.7337 0.7858 0.0127  -0.0688 -0.0265 704 PHE A CZ  
3212 N N   . GLU A 409 ? 0.6519 0.7452 0.8159 0.0492  -0.0649 -0.0171 705 GLU A N   
3213 C CA  . GLU A 409 ? 0.6674 0.7645 0.8243 0.0672  -0.0666 -0.0135 705 GLU A CA  
3214 C C   . GLU A 409 ? 0.6558 0.8116 0.8345 0.0737  -0.0651 -0.0097 705 GLU A C   
3215 O O   . GLU A 409 ? 0.5998 0.7819 0.7888 0.0692  -0.0615 -0.0109 705 GLU A O   
3216 C CB  . GLU A 409 ? 0.7227 0.7779 0.8427 0.0913  -0.0678 -0.0180 705 GLU A CB  
3217 C CG  . GLU A 409 ? 0.7864 0.7767 0.8739 0.0766  -0.0701 -0.0212 705 GLU A CG  
3218 C CD  . GLU A 409 ? 0.8581 0.8318 0.9417 0.0636  -0.0721 -0.0150 705 GLU A CD  
3219 O OE1 . GLU A 409 ? 0.8842 0.8778 0.9748 0.0780  -0.0738 -0.0094 705 GLU A OE1 
3220 O OE2 . GLU A 409 ? 0.8641 0.8112 0.9376 0.0378  -0.0720 -0.0157 705 GLU A OE2 
3221 N N   . TYR A 410 ? 0.6198 0.7992 0.8035 0.0811  -0.0682 -0.0045 706 TYR A N   
3222 C CA  . TYR A 410 ? 0.5986 0.8454 0.8008 0.0860  -0.0676 -0.0008 706 TYR A CA  
3223 C C   . TYR A 410 ? 0.6046 0.8739 0.7973 0.1209  -0.0650 -0.0044 706 TYR A C   
3224 O O   . TYR A 410 ? 0.6471 0.8679 0.8097 0.1468  -0.0660 -0.0090 706 TYR A O   
3225 C CB  . TYR A 410 ? 0.6324 0.9050 0.8412 0.0849  -0.0735 0.0051  706 TYR A CB  
3226 C CG  . TYR A 410 ? 0.6767 0.9467 0.8945 0.0511  -0.0759 0.0088  706 TYR A CG  
3227 C CD1 . TYR A 410 ? 0.6979 1.0072 0.9278 0.0253  -0.0753 0.0118  706 TYR A CD1 
3228 C CD2 . TYR A 410 ? 0.7554 0.9807 0.9621 0.0448  -0.0787 0.0096  706 TYR A CD2 
3229 C CE1 . TYR A 410 ? 0.7376 1.0299 0.9621 -0.0034 -0.0785 0.0144  706 TYR A CE1 
3230 C CE2 . TYR A 410 ? 0.7556 0.9749 0.9634 0.0196  -0.0807 0.0118  706 TYR A CE2 
3231 C CZ  . TYR A 410 ? 0.7278 0.9754 0.9416 -0.0029 -0.0812 0.0138  706 TYR A CZ  
3232 O OH  . TYR A 410 ? 0.7178 0.9441 0.9195 -0.0259 -0.0840 0.0150  706 TYR A OH  
3233 N N   . GLN A 411 ? 0.6332 0.9751 0.8457 0.1211  -0.0614 -0.0023 707 GLN A N   
3234 C CA  . GLN A 411 ? 0.6704 1.0486 0.8751 0.1592  -0.0574 -0.0060 707 GLN A CA  
3235 C C   . GLN A 411 ? 0.6501 1.1342 0.8833 0.1569  -0.0560 -0.0003 707 GLN A C   
3236 O O   . GLN A 411 ? 0.6398 1.1569 0.8938 0.1158  -0.0565 0.0056  707 GLN A O   
3237 C CB  . GLN A 411 ? 0.6641 1.0192 0.8576 0.1602  -0.0505 -0.0125 707 GLN A CB  
3238 C CG  . GLN A 411 ? 0.6487 1.0518 0.8650 0.1281  -0.0448 -0.0089 707 GLN A CG  
3239 C CD  . GLN A 411 ? 0.6378 1.0093 0.8393 0.1286  -0.0393 -0.0151 707 GLN A CD  
3240 O OE1 . GLN A 411 ? 0.6523 1.0037 0.8305 0.1616  -0.0371 -0.0226 707 GLN A OE1 
3241 N NE2 . GLN A 411 ? 0.5830 0.9435 0.7908 0.0940  -0.0382 -0.0121 707 GLN A NE2 
3242 N N   . PRO A 412 ? 0.6498 1.1890 0.8796 0.2003  -0.0547 -0.0019 708 PRO A N   
3243 C CA  . PRO A 412 ? 0.6736 1.3351 0.9344 0.1974  -0.0534 0.0037  708 PRO A CA  
3244 C C   . PRO A 412 ? 0.6769 1.3902 0.9577 0.1568  -0.0447 0.0065  708 PRO A C   
3245 O O   . PRO A 412 ? 0.6847 1.3618 0.9535 0.1562  -0.0374 0.0020  708 PRO A O   
3246 C CB  . PRO A 412 ? 0.7504 1.4300 0.9845 0.2545  -0.0493 -0.0012 708 PRO A CB  
3247 C CG  . PRO A 412 ? 0.7606 1.3413 0.9572 0.2957  -0.0559 -0.0070 708 PRO A CG  
3248 C CD  . PRO A 412 ? 0.7223 1.2125 0.9132 0.2554  -0.0554 -0.0089 708 PRO A CD  
3249 N N   . ASP A 413 ? 0.7005 1.4772 0.9973 0.1170  -0.0450 0.0139  709 ASP A N   
3250 C CA  . ASP A 413 ? 0.7259 1.5523 1.0294 0.0771  -0.0361 0.0181  709 ASP A CA  
3251 C C   . ASP A 413 ? 0.7430 1.6172 1.0376 0.1123  -0.0246 0.0139  709 ASP A C   
3252 O O   . ASP A 413 ? 0.7780 1.6857 1.0625 0.1527  -0.0240 0.0113  709 ASP A O   
3253 C CB  . ASP A 413 ? 0.7411 1.6193 1.0484 0.0300  -0.0387 0.0262  709 ASP A CB  
3254 C CG  . ASP A 413 ? 0.7642 1.5885 1.0712 -0.0144 -0.0487 0.0301  709 ASP A CG  
3255 O OD1 . ASP A 413 ? 0.7499 1.5038 1.0527 -0.0207 -0.0504 0.0281  709 ASP A OD1 
3256 O OD2 . ASP A 413 ? 0.7778 1.6236 1.0815 -0.0418 -0.0546 0.0346  709 ASP A OD2 
3257 N N   . PRO A 414 ? 0.7197 1.5976 1.0135 0.1003  -0.0157 0.0130  710 PRO A N   
3258 C CA  . PRO A 414 ? 0.7208 1.6324 1.0011 0.1408  -0.0050 0.0072  710 PRO A CA  
3259 C C   . PRO A 414 ? 0.7555 1.7654 1.0336 0.1414  0.0010  0.0111  710 PRO A C   
3260 O O   . PRO A 414 ? 0.7961 1.8351 1.0576 0.1879  0.0072  0.0054  710 PRO A O   
3261 C CB  . PRO A 414 ? 0.6611 1.5577 0.9429 0.1164  0.0027  0.0072  710 PRO A CB  
3262 C CG  . PRO A 414 ? 0.6365 1.5158 0.9301 0.0531  -0.0028 0.0162  710 PRO A CG  
3263 C CD  . PRO A 414 ? 0.6922 1.5324 0.9915 0.0552  -0.0159 0.0164  710 PRO A CD  
3264 N N   . TRP A 415 ? 0.7424 1.8039 1.0311 0.0918  -0.0014 0.0202  711 TRP A N   
3265 C CA  . TRP A 415 ? 0.7501 1.9152 1.0352 0.0907  0.0037  0.0238  711 TRP A CA  
3266 C C   . TRP A 415 ? 0.7747 1.9710 1.0541 0.1401  -0.0015 0.0203  711 TRP A C   
3267 O O   . TRP A 415 ? 0.7766 2.0668 1.0515 0.1497  0.0019  0.0222  711 TRP A O   
3268 C CB  . TRP A 415 ? 0.7098 1.9177 0.9987 0.0181  0.0023  0.0345  711 TRP A CB  
3269 C CG  . TRP A 415 ? 0.7162 1.8706 1.0096 -0.0165 -0.0091 0.0381  711 TRP A CG  
3270 C CD1 . TRP A 415 ? 0.7358 1.9140 1.0323 -0.0154 -0.0176 0.0396  711 TRP A CD1 
3271 C CD2 . TRP A 415 ? 0.7208 1.7898 1.0119 -0.0563 -0.0137 0.0405  711 TRP A CD2 
3272 N NE1 . TRP A 415 ? 0.7489 1.8596 1.0451 -0.0520 -0.0272 0.0424  711 TRP A NE1 
3273 C CE2 . TRP A 415 ? 0.7301 1.7726 1.0216 -0.0767 -0.0252 0.0429  711 TRP A CE2 
3274 C CE3 . TRP A 415 ? 0.6978 1.7118 0.9837 -0.0750 -0.0096 0.0408  711 TRP A CE3 
3275 C CZ2 . TRP A 415 ? 0.7525 1.7129 1.0362 -0.1134 -0.0329 0.0450  711 TRP A CZ2 
3276 C CZ3 . TRP A 415 ? 0.6933 1.6282 0.9724 -0.1114 -0.0175 0.0435  711 TRP A CZ3 
3277 C CH2 . TRP A 415 ? 0.7750 1.6823 1.0516 -0.1293 -0.0291 0.0452  711 TRP A CH2 
3278 N N   . ASN A 416 ? 0.7873 1.9089 1.0629 0.1718  -0.0100 0.0157  712 ASN A N   
3279 C CA  . ASN A 416 ? 0.8597 1.9937 1.1207 0.2242  -0.0153 0.0122  712 ASN A CA  
3280 C C   . ASN A 416 ? 0.9191 2.0070 1.1479 0.2931  -0.0124 0.0024  712 ASN A C   
3281 O O   . ASN A 416 ? 0.9604 2.0806 1.1656 0.3422  -0.0132 -0.0007 712 ASN A O   
3282 C CB  . ASN A 416 ? 0.8725 1.9480 1.1396 0.2159  -0.0277 0.0140  712 ASN A CB  
3283 C CG  . ASN A 416 ? 0.8497 1.9510 1.1388 0.1478  -0.0322 0.0225  712 ASN A CG  
3284 O OD1 . ASN A 416 ? 0.8361 2.0178 1.1307 0.1122  -0.0274 0.0279  712 ASN A OD1 
3285 N ND2 . ASN A 416 ? 0.8320 1.8621 1.1273 0.1284  -0.0418 0.0238  712 ASN A ND2 
3286 N N   . THR A 417 ? 0.9232 1.9331 1.1446 0.2982  -0.0096 -0.0029 713 THR A N   
3287 C CA  . THR A 417 ? 0.9943 1.9389 1.1749 0.3589  -0.0081 -0.0130 713 THR A CA  
3288 C C   . THR A 417 ? 1.0041 1.9860 1.1712 0.3751  0.0033  -0.0174 713 THR A C   
3289 O O   . THR A 417 ? 1.0657 2.0217 1.1897 0.4319  0.0048  -0.0254 713 THR A O   
3290 C CB  . THR A 417 ? 1.0381 1.8641 1.2106 0.3574  -0.0140 -0.0174 713 THR A CB  
3291 O OG1 . THR A 417 ? 0.9501 1.7785 1.1623 0.2970  -0.0146 -0.0113 713 THR A OG1 
3292 C CG2 . THR A 417 ? 1.0773 1.8370 1.2280 0.3832  -0.0256 -0.0180 713 THR A CG2 
3293 N N   . HIS A 418 ? 0.9671 2.0037 1.1633 0.3264  0.0109  -0.0120 714 HIS A N   
3294 C CA  . HIS A 418 ? 0.9737 2.0393 1.1577 0.3375  0.0220  -0.0156 714 HIS A CA  
3295 C C   . HIS A 418 ? 0.9879 2.1353 1.1488 0.3816  0.0257  -0.0173 714 HIS A C   
3296 O O   . HIS A 418 ? 0.9872 2.2065 1.1550 0.3825  0.0220  -0.0123 714 HIS A O   
3297 C CB  . HIS A 418 ? 0.9265 2.0414 1.1419 0.2714  0.0289  -0.0071 714 HIS A CB  
3298 C CG  . HIS A 418 ? 0.9241 2.0531 1.1276 0.2774  0.0404  -0.0106 714 HIS A CG  
3299 N ND1 . HIS A 418 ? 0.9478 1.9989 1.1231 0.3196  0.0427  -0.0219 714 HIS A ND1 
3300 C CD2 . HIS A 418 ? 0.9235 2.1321 1.1352 0.2446  0.0499  -0.0043 714 HIS A CD2 
3301 C CE1 . HIS A 418 ? 0.8953 1.9801 1.0643 0.3152  0.0538  -0.0228 714 HIS A CE1 
3302 N NE2 . HIS A 418 ? 0.8734 2.0547 1.0651 0.2698  0.0585  -0.0116 714 HIS A NE2 
3303 N N   . VAL A 419 ? 1.0109 2.1470 1.1408 0.4209  0.0323  -0.0249 715 VAL A N   
3304 C CA  . VAL A 419 ? 1.0127 2.2322 1.1184 0.4637  0.0365  -0.0265 715 VAL A CA  
3305 C C   . VAL A 419 ? 1.0117 2.3041 1.1346 0.4313  0.0478  -0.0226 715 VAL A C   
3306 O O   . VAL A 419 ? 1.0247 2.2647 1.1327 0.4391  0.0538  -0.0286 715 VAL A O   
3307 C CB  . VAL A 419 ? 1.0718 2.2125 1.1159 0.5399  0.0336  -0.0383 715 VAL A CB  
3308 C CG1 . VAL A 419 ? 1.0855 2.3153 1.1024 0.5859  0.0379  -0.0398 715 VAL A CG1 
3309 C CG2 . VAL A 419 ? 1.1059 2.1749 1.1265 0.5685  0.0221  -0.0405 715 VAL A CG2 
3310 N N   . TRP A 420 ? 0.9642 2.3751 1.1146 0.3925  0.0502  -0.0126 716 TRP A N   
3311 C CA  . TRP A 420 ? 0.9774 2.4519 1.1489 0.3385  0.0594  -0.0054 716 TRP A CA  
3312 C C   . TRP A 420 ? 1.0300 2.5515 1.1793 0.3722  0.0687  -0.0096 716 TRP A C   
3313 O O   . TRP A 420 ? 1.0954 2.5844 1.2080 0.4407  0.0681  -0.0194 716 TRP A O   
3314 C CB  . TRP A 420 ? 0.9320 2.5128 1.1301 0.2828  0.0572  0.0067  716 TRP A CB  
3315 C CG  . TRP A 420 ? 0.9361 2.4662 1.1585 0.2190  0.0518  0.0136  716 TRP A CG  
3316 C CD1 . TRP A 420 ? 0.9334 2.4131 1.1633 0.2209  0.0419  0.0132  716 TRP A CD1 
3317 C CD2 . TRP A 420 ? 0.9209 2.4398 1.1571 0.1454  0.0554  0.0220  716 TRP A CD2 
3318 N NE1 . TRP A 420 ? 0.9046 2.3451 1.1532 0.1544  0.0388  0.0205  716 TRP A NE1 
3319 C CE2 . TRP A 420 ? 0.9063 2.3665 1.1559 0.1076  0.0467  0.0261  716 TRP A CE2 
3320 C CE3 . TRP A 420 ? 0.9087 2.4575 1.1418 0.1080  0.0647  0.0269  716 TRP A CE3 
3321 C CZ2 . TRP A 420 ? 0.8666 2.2928 1.1216 0.0362  0.0465  0.0346  716 TRP A CZ2 
3322 C CZ3 . TRP A 420 ? 0.8938 2.4068 1.1314 0.0352  0.0649  0.0358  716 TRP A CZ3 
3323 C CH2 . TRP A 420 ? 0.8774 2.3273 1.1235 0.0010  0.0556  0.0395  716 TRP A CH2 
# 
