data_9CVQ
# 
_entry.id   9CVQ 
# 
_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   9CVQ         pdb_00009cvq 10.2210/pdb9cvq/pdb 
WWPDB D_1000286183 ?            ?                   
# 
_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                        9CVQ 
_pdbx_database_status.recvd_initial_deposition_date   2024-07-29 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    RCSB 
_pdbx_database_status.process_site                    RCSB 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           N 
# 
_pdbx_contact_author.id                 2 
_pdbx_contact_author.email              poulos@uci.edu 
_pdbx_contact_author.name_first         Thomas 
_pdbx_contact_author.name_last          Poulos 
_pdbx_contact_author.name_mi            L 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0002-5648-3510 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Li, H.'       1 0000-0003-4867-367X 
'Poulos, T.L.' 2 0000-0002-5648-3510 
# 
_citation.abstract                  ? 
_citation.abstract_id_CAS           ? 
_citation.book_id_ISBN              ? 
_citation.book_publisher            ? 
_citation.book_publisher_city       ? 
_citation.book_title                ? 
_citation.coordinate_linkage        ? 
_citation.country                   UK 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            Bioorg.Med.Chem. 
_citation.journal_id_ASTM           BMECEP 
_citation.journal_id_CSD            1200 
_citation.journal_id_ISSN           1464-3391 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            124 
_citation.language                  ? 
_citation.page_first                118193 
_citation.page_last                 118193 
_citation.title                     
;Truncated pyridinylbenzylamines: Potent, selective, and highly membrane permeable inhibitors of human neuronal nitric oxide synthase.
;
_citation.year                      2025 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1016/j.bmc.2025.118193 
_citation.pdbx_database_id_PubMed   40252563 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Vasu, D.'        1 ? 
primary 'Do, H.T.'        2 ? 
primary 'Li, H.'          3 ? 
primary 'Hardy, C.D.'     4 ? 
primary 'Poulos, T.L.'    5 ? 
primary 'Silverman, R.B.' 6 ? 
# 
loop_
_entity.id 
_entity.type 
_entity.src_method 
_entity.pdbx_description 
_entity.formula_weight 
_entity.pdbx_number_of_molecules 
_entity.pdbx_ec 
_entity.pdbx_mutation 
_entity.pdbx_fragment 
_entity.details 
1 polymer     man 'Nitric oxide synthase, brain'                                                              48726.410 1  
1.14.13.39 R349A ? ? 
2 non-polymer syn 'PROTOPORPHYRIN IX CONTAINING FE'                                                           616.487   1  ? ?     
? ? 
3 non-polymer syn 5,6,7,8-TETRAHYDROBIOPTERIN                                                                 241.247   1  ? ?     
? ? 
4 non-polymer syn 'ZINC ION'                                                                                  65.409    1  ? ?     
? ? 
5 non-polymer syn '(6M)-6-{5-[(3,3-difluoroazetidin-1-yl)methyl]-2,3-difluorophenyl}-4-methylpyridin-2-amine' 325.304   1  ? ?     
? ? 
6 water       nat water                                                                                       18.015    52 ? ?     
? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        'BNOS,Constitutive NOS,NC-NOS,NOS type I,Neuronal NOS,nNOS,Peptidyl-cysteine S-nitrosylase NOS1' 
# 
_entity_poly.entity_id                      1 
_entity_poly.type                           'polypeptide(L)' 
_entity_poly.nstd_linkage                   no 
_entity_poly.nstd_monomer                   no 
_entity_poly.pdbx_seq_one_letter_code       
;CPRFLKVKNWETDVVLTDTLHLKSTLETGCTEHICMGSIMLPSQHTRKPEDVATKDQLFPLAKEFLDQYYSSIKRFGSKA
HMDRLEEVNKEIESTSTYQLKDTELIYGAKHAWRNASRCVGRIQWSKLQVFDARDCTTAHGMFNYICNHVKYATNKGNLR
SAITIFPQRTDGKHDFRVWNSQLIRYAGYKQPDGSTLGDPANVQFTEICIQQGWKAPRGRFDVLPLLLQANGNDPELFQI
PPELVLEVPIRHPKFDWFKDLGLKWYGLPAVSNMLLEIGGLEFSACPFSGWYMGTEIGVRDYCDNSRYNILEEVAKKMDL
DMRKTSSLWKDQALVEINIAVLYSFQSDKVTIVDHHSATESFIKHMENEYRCRGGCPADWVWIVPPMSGSITPVFHQEML
NYRLTPSFEYQPDPWNTHVWKG
;
_entity_poly.pdbx_seq_one_letter_code_can   
;CPRFLKVKNWETDVVLTDTLHLKSTLETGCTEHICMGSIMLPSQHTRKPEDVATKDQLFPLAKEFLDQYYSSIKRFGSKA
HMDRLEEVNKEIESTSTYQLKDTELIYGAKHAWRNASRCVGRIQWSKLQVFDARDCTTAHGMFNYICNHVKYATNKGNLR
SAITIFPQRTDGKHDFRVWNSQLIRYAGYKQPDGSTLGDPANVQFTEICIQQGWKAPRGRFDVLPLLLQANGNDPELFQI
PPELVLEVPIRHPKFDWFKDLGLKWYGLPAVSNMLLEIGGLEFSACPFSGWYMGTEIGVRDYCDNSRYNILEEVAKKMDL
DMRKTSSLWKDQALVEINIAVLYSFQSDKVTIVDHHSATESFIKHMENEYRCRGGCPADWVWIVPPMSGSITPVFHQEML
NYRLTPSFEYQPDPWNTHVWKG
;
_entity_poly.pdbx_strand_id                 A 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 'PROTOPORPHYRIN IX CONTAINING FE'                                                           HEM   
3 5,6,7,8-TETRAHYDROBIOPTERIN                                                                 H4B   
4 'ZINC ION'                                                                                  ZN    
5 '(6M)-6-{5-[(3,3-difluoroazetidin-1-yl)methyl]-2,3-difluorophenyl}-4-methylpyridin-2-amine' A1A0D 
6 water                                                                                       HOH   
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   CYS n 
1 2   PRO n 
1 3   ARG n 
1 4   PHE n 
1 5   LEU n 
1 6   LYS n 
1 7   VAL n 
1 8   LYS n 
1 9   ASN n 
1 10  TRP n 
1 11  GLU n 
1 12  THR n 
1 13  ASP n 
1 14  VAL n 
1 15  VAL n 
1 16  LEU n 
1 17  THR n 
1 18  ASP n 
1 19  THR n 
1 20  LEU n 
1 21  HIS n 
1 22  LEU n 
1 23  LYS n 
1 24  SER n 
1 25  THR n 
1 26  LEU n 
1 27  GLU n 
1 28  THR n 
1 29  GLY n 
1 30  CYS n 
1 31  THR n 
1 32  GLU n 
1 33  HIS n 
1 34  ILE n 
1 35  CYS n 
1 36  MET n 
1 37  GLY n 
1 38  SER n 
1 39  ILE n 
1 40  MET n 
1 41  LEU n 
1 42  PRO n 
1 43  SER n 
1 44  GLN n 
1 45  HIS n 
1 46  THR n 
1 47  ARG n 
1 48  LYS n 
1 49  PRO n 
1 50  GLU n 
1 51  ASP n 
1 52  VAL n 
1 53  ALA n 
1 54  THR n 
1 55  LYS n 
1 56  ASP n 
1 57  GLN n 
1 58  LEU n 
1 59  PHE n 
1 60  PRO n 
1 61  LEU n 
1 62  ALA n 
1 63  LYS n 
1 64  GLU n 
1 65  PHE n 
1 66  LEU n 
1 67  ASP n 
1 68  GLN n 
1 69  TYR n 
1 70  TYR n 
1 71  SER n 
1 72  SER n 
1 73  ILE n 
1 74  LYS n 
1 75  ARG n 
1 76  PHE n 
1 77  GLY n 
1 78  SER n 
1 79  LYS n 
1 80  ALA n 
1 81  HIS n 
1 82  MET n 
1 83  ASP n 
1 84  ARG n 
1 85  LEU n 
1 86  GLU n 
1 87  GLU n 
1 88  VAL n 
1 89  ASN n 
1 90  LYS n 
1 91  GLU n 
1 92  ILE n 
1 93  GLU n 
1 94  SER n 
1 95  THR n 
1 96  SER n 
1 97  THR n 
1 98  TYR n 
1 99  GLN n 
1 100 LEU n 
1 101 LYS n 
1 102 ASP n 
1 103 THR n 
1 104 GLU n 
1 105 LEU n 
1 106 ILE n 
1 107 TYR n 
1 108 GLY n 
1 109 ALA n 
1 110 LYS n 
1 111 HIS n 
1 112 ALA n 
1 113 TRP n 
1 114 ARG n 
1 115 ASN n 
1 116 ALA n 
1 117 SER n 
1 118 ARG n 
1 119 CYS n 
1 120 VAL n 
1 121 GLY n 
1 122 ARG n 
1 123 ILE n 
1 124 GLN n 
1 125 TRP n 
1 126 SER n 
1 127 LYS n 
1 128 LEU n 
1 129 GLN n 
1 130 VAL n 
1 131 PHE n 
1 132 ASP n 
1 133 ALA n 
1 134 ARG n 
1 135 ASP n 
1 136 CYS n 
1 137 THR n 
1 138 THR n 
1 139 ALA n 
1 140 HIS n 
1 141 GLY n 
1 142 MET n 
1 143 PHE n 
1 144 ASN n 
1 145 TYR n 
1 146 ILE n 
1 147 CYS n 
1 148 ASN n 
1 149 HIS n 
1 150 VAL n 
1 151 LYS n 
1 152 TYR n 
1 153 ALA n 
1 154 THR n 
1 155 ASN n 
1 156 LYS n 
1 157 GLY n 
1 158 ASN n 
1 159 LEU n 
1 160 ARG n 
1 161 SER n 
1 162 ALA n 
1 163 ILE n 
1 164 THR n 
1 165 ILE n 
1 166 PHE n 
1 167 PRO n 
1 168 GLN n 
1 169 ARG n 
1 170 THR n 
1 171 ASP n 
1 172 GLY n 
1 173 LYS n 
1 174 HIS n 
1 175 ASP n 
1 176 PHE n 
1 177 ARG n 
1 178 VAL n 
1 179 TRP n 
1 180 ASN n 
1 181 SER n 
1 182 GLN n 
1 183 LEU n 
1 184 ILE n 
1 185 ARG n 
1 186 TYR n 
1 187 ALA n 
1 188 GLY n 
1 189 TYR n 
1 190 LYS n 
1 191 GLN n 
1 192 PRO n 
1 193 ASP n 
1 194 GLY n 
1 195 SER n 
1 196 THR n 
1 197 LEU n 
1 198 GLY n 
1 199 ASP n 
1 200 PRO n 
1 201 ALA n 
1 202 ASN n 
1 203 VAL n 
1 204 GLN n 
1 205 PHE n 
1 206 THR n 
1 207 GLU n 
1 208 ILE n 
1 209 CYS n 
1 210 ILE n 
1 211 GLN n 
1 212 GLN n 
1 213 GLY n 
1 214 TRP n 
1 215 LYS n 
1 216 ALA n 
1 217 PRO n 
1 218 ARG n 
1 219 GLY n 
1 220 ARG n 
1 221 PHE n 
1 222 ASP n 
1 223 VAL n 
1 224 LEU n 
1 225 PRO n 
1 226 LEU n 
1 227 LEU n 
1 228 LEU n 
1 229 GLN n 
1 230 ALA n 
1 231 ASN n 
1 232 GLY n 
1 233 ASN n 
1 234 ASP n 
1 235 PRO n 
1 236 GLU n 
1 237 LEU n 
1 238 PHE n 
1 239 GLN n 
1 240 ILE n 
1 241 PRO n 
1 242 PRO n 
1 243 GLU n 
1 244 LEU n 
1 245 VAL n 
1 246 LEU n 
1 247 GLU n 
1 248 VAL n 
1 249 PRO n 
1 250 ILE n 
1 251 ARG n 
1 252 HIS n 
1 253 PRO n 
1 254 LYS n 
1 255 PHE n 
1 256 ASP n 
1 257 TRP n 
1 258 PHE n 
1 259 LYS n 
1 260 ASP n 
1 261 LEU n 
1 262 GLY n 
1 263 LEU n 
1 264 LYS n 
1 265 TRP n 
1 266 TYR n 
1 267 GLY n 
1 268 LEU n 
1 269 PRO n 
1 270 ALA n 
1 271 VAL n 
1 272 SER n 
1 273 ASN n 
1 274 MET n 
1 275 LEU n 
1 276 LEU n 
1 277 GLU n 
1 278 ILE n 
1 279 GLY n 
1 280 GLY n 
1 281 LEU n 
1 282 GLU n 
1 283 PHE n 
1 284 SER n 
1 285 ALA n 
1 286 CYS n 
1 287 PRO n 
1 288 PHE n 
1 289 SER n 
1 290 GLY n 
1 291 TRP n 
1 292 TYR n 
1 293 MET n 
1 294 GLY n 
1 295 THR n 
1 296 GLU n 
1 297 ILE n 
1 298 GLY n 
1 299 VAL n 
1 300 ARG n 
1 301 ASP n 
1 302 TYR n 
1 303 CYS n 
1 304 ASP n 
1 305 ASN n 
1 306 SER n 
1 307 ARG n 
1 308 TYR n 
1 309 ASN n 
1 310 ILE n 
1 311 LEU n 
1 312 GLU n 
1 313 GLU n 
1 314 VAL n 
1 315 ALA n 
1 316 LYS n 
1 317 LYS n 
1 318 MET n 
1 319 ASP n 
1 320 LEU n 
1 321 ASP n 
1 322 MET n 
1 323 ARG n 
1 324 LYS n 
1 325 THR n 
1 326 SER n 
1 327 SER n 
1 328 LEU n 
1 329 TRP n 
1 330 LYS n 
1 331 ASP n 
1 332 GLN n 
1 333 ALA n 
1 334 LEU n 
1 335 VAL n 
1 336 GLU n 
1 337 ILE n 
1 338 ASN n 
1 339 ILE n 
1 340 ALA n 
1 341 VAL n 
1 342 LEU n 
1 343 TYR n 
1 344 SER n 
1 345 PHE n 
1 346 GLN n 
1 347 SER n 
1 348 ASP n 
1 349 LYS n 
1 350 VAL n 
1 351 THR n 
1 352 ILE n 
1 353 VAL n 
1 354 ASP n 
1 355 HIS n 
1 356 HIS n 
1 357 SER n 
1 358 ALA n 
1 359 THR n 
1 360 GLU n 
1 361 SER n 
1 362 PHE n 
1 363 ILE n 
1 364 LYS n 
1 365 HIS n 
1 366 MET n 
1 367 GLU n 
1 368 ASN n 
1 369 GLU n 
1 370 TYR n 
1 371 ARG n 
1 372 CYS n 
1 373 ARG n 
1 374 GLY n 
1 375 GLY n 
1 376 CYS n 
1 377 PRO n 
1 378 ALA n 
1 379 ASP n 
1 380 TRP n 
1 381 VAL n 
1 382 TRP n 
1 383 ILE n 
1 384 VAL n 
1 385 PRO n 
1 386 PRO n 
1 387 MET n 
1 388 SER n 
1 389 GLY n 
1 390 SER n 
1 391 ILE n 
1 392 THR n 
1 393 PRO n 
1 394 VAL n 
1 395 PHE n 
1 396 HIS n 
1 397 GLN n 
1 398 GLU n 
1 399 MET n 
1 400 LEU n 
1 401 ASN n 
1 402 TYR n 
1 403 ARG n 
1 404 LEU n 
1 405 THR n 
1 406 PRO n 
1 407 SER n 
1 408 PHE n 
1 409 GLU n 
1 410 TYR n 
1 411 GLN n 
1 412 PRO n 
1 413 ASP n 
1 414 PRO n 
1 415 TRP n 
1 416 ASN n 
1 417 THR n 
1 418 HIS n 
1 419 VAL n 
1 420 TRP n 
1 421 LYS n 
1 422 GLY n 
# 
_entity_src_gen.entity_id                          1 
_entity_src_gen.pdbx_src_id                        1 
_entity_src_gen.pdbx_alt_source_flag               sample 
_entity_src_gen.pdbx_seq_type                      'Biological sequence' 
_entity_src_gen.pdbx_beg_seq_num                   1 
_entity_src_gen.pdbx_end_seq_num                   422 
_entity_src_gen.gene_src_common_name               'Norway rat' 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 'Nos1, Bnos' 
_entity_src_gen.gene_src_species                   ? 
_entity_src_gen.gene_src_strain                    ? 
_entity_src_gen.gene_src_tissue                    ? 
_entity_src_gen.gene_src_tissue_fraction           ? 
_entity_src_gen.gene_src_details                   ? 
_entity_src_gen.pdbx_gene_src_fragment             ? 
_entity_src_gen.pdbx_gene_src_scientific_name      'Rattus norvegicus' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     10116 
_entity_src_gen.pdbx_gene_src_variant              ? 
_entity_src_gen.pdbx_gene_src_cell_line            ? 
_entity_src_gen.pdbx_gene_src_atcc                 ? 
_entity_src_gen.pdbx_gene_src_organ                brain 
_entity_src_gen.pdbx_gene_src_organelle            ? 
_entity_src_gen.pdbx_gene_src_cell                 ? 
_entity_src_gen.pdbx_gene_src_cellular_location    ? 
_entity_src_gen.host_org_common_name               ? 
_entity_src_gen.pdbx_host_org_scientific_name      'Escherichia coli BL21(DE3)' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     469008 
_entity_src_gen.host_org_genus                     ? 
_entity_src_gen.pdbx_host_org_gene                 ? 
_entity_src_gen.pdbx_host_org_organ                ? 
_entity_src_gen.host_org_species                   ? 
_entity_src_gen.pdbx_host_org_tissue               ? 
_entity_src_gen.pdbx_host_org_tissue_fraction      ? 
_entity_src_gen.pdbx_host_org_strain               ? 
_entity_src_gen.pdbx_host_org_variant              ? 
_entity_src_gen.pdbx_host_org_cell_line            ? 
_entity_src_gen.pdbx_host_org_atcc                 ? 
_entity_src_gen.pdbx_host_org_culture_collection   ? 
_entity_src_gen.pdbx_host_org_cell                 ? 
_entity_src_gen.pdbx_host_org_organelle            ? 
_entity_src_gen.pdbx_host_org_cellular_location    ? 
_entity_src_gen.pdbx_host_org_vector_type          plasmid 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       pET22b 
_entity_src_gen.plasmid_details                    ? 
_entity_src_gen.pdbx_description                   ? 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
A1A0D non-polymer         . '(6M)-6-{5-[(3,3-difluoroazetidin-1-yl)methyl]-2,3-difluorophenyl}-4-methylpyridin-2-amine' ?    
'C16 H15 F4 N3'    325.304 
ALA   'L-peptide linking' y ALANINE                                                                                     ?    
'C3 H7 N O2'       89.093  
ARG   'L-peptide linking' y ARGININE                                                                                    ?    
'C6 H15 N4 O2 1'   175.209 
ASN   'L-peptide linking' y ASPARAGINE                                                                                  ?    
'C4 H8 N2 O3'      132.118 
ASP   'L-peptide linking' y 'ASPARTIC ACID'                                                                             ?    
'C4 H7 N O4'       133.103 
CYS   'L-peptide linking' y CYSTEINE                                                                                    ?    
'C3 H7 N O2 S'     121.158 
GLN   'L-peptide linking' y GLUTAMINE                                                                                   ?    
'C5 H10 N2 O3'     146.144 
GLU   'L-peptide linking' y 'GLUTAMIC ACID'                                                                             ?    
'C5 H9 N O4'       147.129 
GLY   'peptide linking'   y GLYCINE                                                                                     ?    
'C2 H5 N O2'       75.067  
H4B   non-polymer         . 5,6,7,8-TETRAHYDROBIOPTERIN                                                                 ?    
'C9 H15 N5 O3'     241.247 
HEM   non-polymer         . 'PROTOPORPHYRIN IX CONTAINING FE'                                                           HEME 
'C34 H32 Fe N4 O4' 616.487 
HIS   'L-peptide linking' y HISTIDINE                                                                                   ?    
'C6 H10 N3 O2 1'   156.162 
HOH   non-polymer         . WATER                                                                                       ?    
'H2 O'             18.015  
ILE   'L-peptide linking' y ISOLEUCINE                                                                                  ?    
'C6 H13 N O2'      131.173 
LEU   'L-peptide linking' y LEUCINE                                                                                     ?    
'C6 H13 N O2'      131.173 
LYS   'L-peptide linking' y LYSINE                                                                                      ?    
'C6 H15 N2 O2 1'   147.195 
MET   'L-peptide linking' y METHIONINE                                                                                  ?    
'C5 H11 N O2 S'    149.211 
PHE   'L-peptide linking' y PHENYLALANINE                                                                               ?    
'C9 H11 N O2'      165.189 
PRO   'L-peptide linking' y PROLINE                                                                                     ?    
'C5 H9 N O2'       115.130 
SER   'L-peptide linking' y SERINE                                                                                      ?    
'C3 H7 N O3'       105.093 
THR   'L-peptide linking' y THREONINE                                                                                   ?    
'C4 H9 N O3'       119.119 
TRP   'L-peptide linking' y TRYPTOPHAN                                                                                  ?    
'C11 H12 N2 O2'    204.225 
TYR   'L-peptide linking' y TYROSINE                                                                                    ?    
'C9 H11 N O3'      181.189 
VAL   'L-peptide linking' y VALINE                                                                                      ?    
'C5 H11 N O2'      117.146 
ZN    non-polymer         . 'ZINC ION'                                                                                  ?    
'Zn 2'             65.409  
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   CYS 1   297 ?   ?   ?   A . n 
A 1 2   PRO 2   298 ?   ?   ?   A . n 
A 1 3   ARG 3   299 299 ARG ARG A . n 
A 1 4   PHE 4   300 300 PHE PHE A . n 
A 1 5   LEU 5   301 301 LEU LEU A . n 
A 1 6   LYS 6   302 302 LYS LYS A . n 
A 1 7   VAL 7   303 303 VAL VAL A . n 
A 1 8   LYS 8   304 304 LYS LYS A . n 
A 1 9   ASN 9   305 305 ASN ASN A . n 
A 1 10  TRP 10  306 306 TRP TRP A . n 
A 1 11  GLU 11  307 307 GLU GLU A . n 
A 1 12  THR 12  308 308 THR THR A . n 
A 1 13  ASP 13  309 309 ASP ASP A . n 
A 1 14  VAL 14  310 310 VAL VAL A . n 
A 1 15  VAL 15  311 311 VAL VAL A . n 
A 1 16  LEU 16  312 312 LEU LEU A . n 
A 1 17  THR 17  313 313 THR THR A . n 
A 1 18  ASP 18  314 314 ASP ASP A . n 
A 1 19  THR 19  315 315 THR THR A . n 
A 1 20  LEU 20  316 316 LEU LEU A . n 
A 1 21  HIS 21  317 317 HIS HIS A . n 
A 1 22  LEU 22  318 318 LEU LEU A . n 
A 1 23  LYS 23  319 319 LYS LYS A . n 
A 1 24  SER 24  320 320 SER SER A . n 
A 1 25  THR 25  321 321 THR THR A . n 
A 1 26  LEU 26  322 322 LEU LEU A . n 
A 1 27  GLU 27  323 323 GLU GLU A . n 
A 1 28  THR 28  324 324 THR THR A . n 
A 1 29  GLY 29  325 325 GLY GLY A . n 
A 1 30  CYS 30  326 326 CYS CYS A . n 
A 1 31  THR 31  327 327 THR THR A . n 
A 1 32  GLU 32  328 328 GLU GLU A . n 
A 1 33  HIS 33  329 329 HIS HIS A . n 
A 1 34  ILE 34  330 330 ILE ILE A . n 
A 1 35  CYS 35  331 331 CYS CYS A . n 
A 1 36  MET 36  332 332 MET MET A . n 
A 1 37  GLY 37  333 333 GLY GLY A . n 
A 1 38  SER 38  334 334 SER SER A . n 
A 1 39  ILE 39  335 335 ILE ILE A . n 
A 1 40  MET 40  336 336 MET MET A . n 
A 1 41  LEU 41  337 337 LEU LEU A . n 
A 1 42  PRO 42  338 338 PRO PRO A . n 
A 1 43  SER 43  339 339 SER SER A . n 
A 1 44  GLN 44  340 340 GLN GLN A . n 
A 1 45  HIS 45  341 341 HIS HIS A . n 
A 1 46  THR 46  342 342 THR THR A . n 
A 1 47  ARG 47  343 343 ARG ARG A . n 
A 1 48  LYS 48  344 ?   ?   ?   A . n 
A 1 49  PRO 49  345 ?   ?   ?   A . n 
A 1 50  GLU 50  346 ?   ?   ?   A . n 
A 1 51  ASP 51  347 ?   ?   ?   A . n 
A 1 52  VAL 52  348 348 VAL VAL A . n 
A 1 53  ALA 53  349 349 ALA ALA A . n 
A 1 54  THR 54  350 350 THR THR A . n 
A 1 55  LYS 55  351 351 LYS LYS A . n 
A 1 56  ASP 56  352 352 ASP ASP A . n 
A 1 57  GLN 57  353 353 GLN GLN A . n 
A 1 58  LEU 58  354 354 LEU LEU A . n 
A 1 59  PHE 59  355 355 PHE PHE A . n 
A 1 60  PRO 60  356 356 PRO PRO A . n 
A 1 61  LEU 61  357 357 LEU LEU A . n 
A 1 62  ALA 62  358 358 ALA ALA A . n 
A 1 63  LYS 63  359 359 LYS LYS A . n 
A 1 64  GLU 64  360 360 GLU GLU A . n 
A 1 65  PHE 65  361 361 PHE PHE A . n 
A 1 66  LEU 66  362 362 LEU LEU A . n 
A 1 67  ASP 67  363 363 ASP ASP A . n 
A 1 68  GLN 68  364 364 GLN GLN A . n 
A 1 69  TYR 69  365 365 TYR TYR A . n 
A 1 70  TYR 70  366 366 TYR TYR A . n 
A 1 71  SER 71  367 367 SER SER A . n 
A 1 72  SER 72  368 368 SER SER A . n 
A 1 73  ILE 73  369 369 ILE ILE A . n 
A 1 74  LYS 74  370 370 LYS LYS A . n 
A 1 75  ARG 75  371 371 ARG ARG A . n 
A 1 76  PHE 76  372 372 PHE PHE A . n 
A 1 77  GLY 77  373 373 GLY GLY A . n 
A 1 78  SER 78  374 374 SER SER A . n 
A 1 79  LYS 79  375 375 LYS LYS A . n 
A 1 80  ALA 80  376 376 ALA ALA A . n 
A 1 81  HIS 81  377 377 HIS HIS A . n 
A 1 82  MET 82  378 378 MET MET A . n 
A 1 83  ASP 83  379 379 ASP ASP A . n 
A 1 84  ARG 84  380 380 ARG ARG A . n 
A 1 85  LEU 85  381 381 LEU LEU A . n 
A 1 86  GLU 86  382 382 GLU GLU A . n 
A 1 87  GLU 87  383 383 GLU GLU A . n 
A 1 88  VAL 88  384 384 VAL VAL A . n 
A 1 89  ASN 89  385 385 ASN ASN A . n 
A 1 90  LYS 90  386 386 LYS LYS A . n 
A 1 91  GLU 91  387 387 GLU GLU A . n 
A 1 92  ILE 92  388 388 ILE ILE A . n 
A 1 93  GLU 93  389 389 GLU GLU A . n 
A 1 94  SER 94  390 390 SER SER A . n 
A 1 95  THR 95  391 391 THR THR A . n 
A 1 96  SER 96  392 392 SER SER A . n 
A 1 97  THR 97  393 393 THR THR A . n 
A 1 98  TYR 98  394 394 TYR TYR A . n 
A 1 99  GLN 99  395 395 GLN GLN A . n 
A 1 100 LEU 100 396 396 LEU LEU A . n 
A 1 101 LYS 101 397 397 LYS LYS A . n 
A 1 102 ASP 102 398 398 ASP ASP A . n 
A 1 103 THR 103 399 399 THR THR A . n 
A 1 104 GLU 104 400 400 GLU GLU A . n 
A 1 105 LEU 105 401 401 LEU LEU A . n 
A 1 106 ILE 106 402 402 ILE ILE A . n 
A 1 107 TYR 107 403 403 TYR TYR A . n 
A 1 108 GLY 108 404 404 GLY GLY A . n 
A 1 109 ALA 109 405 405 ALA ALA A . n 
A 1 110 LYS 110 406 406 LYS LYS A . n 
A 1 111 HIS 111 407 407 HIS HIS A . n 
A 1 112 ALA 112 408 408 ALA ALA A . n 
A 1 113 TRP 113 409 409 TRP TRP A . n 
A 1 114 ARG 114 410 410 ARG ARG A . n 
A 1 115 ASN 115 411 411 ASN ASN A . n 
A 1 116 ALA 116 412 412 ALA ALA A . n 
A 1 117 SER 117 413 413 SER SER A . n 
A 1 118 ARG 118 414 414 ARG ARG A . n 
A 1 119 CYS 119 415 415 CYS CYS A . n 
A 1 120 VAL 120 416 416 VAL VAL A . n 
A 1 121 GLY 121 417 417 GLY GLY A . n 
A 1 122 ARG 122 418 418 ARG ARG A . n 
A 1 123 ILE 123 419 419 ILE ILE A . n 
A 1 124 GLN 124 420 420 GLN GLN A . n 
A 1 125 TRP 125 421 421 TRP TRP A . n 
A 1 126 SER 126 422 422 SER SER A . n 
A 1 127 LYS 127 423 423 LYS LYS A . n 
A 1 128 LEU 128 424 424 LEU LEU A . n 
A 1 129 GLN 129 425 425 GLN GLN A . n 
A 1 130 VAL 130 426 426 VAL VAL A . n 
A 1 131 PHE 131 427 427 PHE PHE A . n 
A 1 132 ASP 132 428 428 ASP ASP A . n 
A 1 133 ALA 133 429 429 ALA ALA A . n 
A 1 134 ARG 134 430 430 ARG ARG A . n 
A 1 135 ASP 135 431 431 ASP ASP A . n 
A 1 136 CYS 136 432 432 CYS CYS A . n 
A 1 137 THR 137 433 433 THR THR A . n 
A 1 138 THR 138 434 434 THR THR A . n 
A 1 139 ALA 139 435 435 ALA ALA A . n 
A 1 140 HIS 140 436 436 HIS HIS A . n 
A 1 141 GLY 141 437 437 GLY GLY A . n 
A 1 142 MET 142 438 438 MET MET A . n 
A 1 143 PHE 143 439 439 PHE PHE A . n 
A 1 144 ASN 144 440 440 ASN ASN A . n 
A 1 145 TYR 145 441 441 TYR TYR A . n 
A 1 146 ILE 146 442 442 ILE ILE A . n 
A 1 147 CYS 147 443 443 CYS CYS A . n 
A 1 148 ASN 148 444 444 ASN ASN A . n 
A 1 149 HIS 149 445 445 HIS HIS A . n 
A 1 150 VAL 150 446 446 VAL VAL A . n 
A 1 151 LYS 151 447 447 LYS LYS A . n 
A 1 152 TYR 152 448 448 TYR TYR A . n 
A 1 153 ALA 153 449 449 ALA ALA A . n 
A 1 154 THR 154 450 450 THR THR A . n 
A 1 155 ASN 155 451 451 ASN ASN A . n 
A 1 156 LYS 156 452 452 LYS LYS A . n 
A 1 157 GLY 157 453 453 GLY GLY A . n 
A 1 158 ASN 158 454 454 ASN ASN A . n 
A 1 159 LEU 159 455 455 LEU LEU A . n 
A 1 160 ARG 160 456 456 ARG ARG A . n 
A 1 161 SER 161 457 457 SER SER A . n 
A 1 162 ALA 162 458 458 ALA ALA A . n 
A 1 163 ILE 163 459 459 ILE ILE A . n 
A 1 164 THR 164 460 460 THR THR A . n 
A 1 165 ILE 165 461 461 ILE ILE A . n 
A 1 166 PHE 166 462 462 PHE PHE A . n 
A 1 167 PRO 167 463 463 PRO PRO A . n 
A 1 168 GLN 168 464 464 GLN GLN A . n 
A 1 169 ARG 169 465 465 ARG ARG A . n 
A 1 170 THR 170 466 466 THR THR A . n 
A 1 171 ASP 171 467 467 ASP ASP A . n 
A 1 172 GLY 172 468 468 GLY GLY A . n 
A 1 173 LYS 173 469 469 LYS LYS A . n 
A 1 174 HIS 174 470 470 HIS HIS A . n 
A 1 175 ASP 175 471 471 ASP ASP A . n 
A 1 176 PHE 176 472 472 PHE PHE A . n 
A 1 177 ARG 177 473 473 ARG ARG A . n 
A 1 178 VAL 178 474 474 VAL VAL A . n 
A 1 179 TRP 179 475 475 TRP TRP A . n 
A 1 180 ASN 180 476 476 ASN ASN A . n 
A 1 181 SER 181 477 477 SER SER A . n 
A 1 182 GLN 182 478 478 GLN GLN A . n 
A 1 183 LEU 183 479 479 LEU LEU A . n 
A 1 184 ILE 184 480 480 ILE ILE A . n 
A 1 185 ARG 185 481 481 ARG ARG A . n 
A 1 186 TYR 186 482 482 TYR TYR A . n 
A 1 187 ALA 187 483 483 ALA ALA A . n 
A 1 188 GLY 188 484 484 GLY GLY A . n 
A 1 189 TYR 189 485 485 TYR TYR A . n 
A 1 190 LYS 190 486 486 LYS LYS A . n 
A 1 191 GLN 191 487 487 GLN GLN A . n 
A 1 192 PRO 192 488 488 PRO PRO A . n 
A 1 193 ASP 193 489 489 ASP ASP A . n 
A 1 194 GLY 194 490 490 GLY GLY A . n 
A 1 195 SER 195 491 491 SER SER A . n 
A 1 196 THR 196 492 492 THR THR A . n 
A 1 197 LEU 197 493 493 LEU LEU A . n 
A 1 198 GLY 198 494 494 GLY GLY A . n 
A 1 199 ASP 199 495 495 ASP ASP A . n 
A 1 200 PRO 200 496 496 PRO PRO A . n 
A 1 201 ALA 201 497 497 ALA ALA A . n 
A 1 202 ASN 202 498 498 ASN ASN A . n 
A 1 203 VAL 203 499 499 VAL VAL A . n 
A 1 204 GLN 204 500 500 GLN GLN A . n 
A 1 205 PHE 205 501 501 PHE PHE A . n 
A 1 206 THR 206 502 502 THR THR A . n 
A 1 207 GLU 207 503 503 GLU GLU A . n 
A 1 208 ILE 208 504 504 ILE ILE A . n 
A 1 209 CYS 209 505 505 CYS CYS A . n 
A 1 210 ILE 210 506 506 ILE ILE A . n 
A 1 211 GLN 211 507 507 GLN GLN A . n 
A 1 212 GLN 212 508 508 GLN GLN A . n 
A 1 213 GLY 213 509 509 GLY GLY A . n 
A 1 214 TRP 214 510 510 TRP TRP A . n 
A 1 215 LYS 215 511 511 LYS LYS A . n 
A 1 216 ALA 216 512 512 ALA ALA A . n 
A 1 217 PRO 217 513 513 PRO PRO A . n 
A 1 218 ARG 218 514 514 ARG ARG A . n 
A 1 219 GLY 219 515 515 GLY GLY A . n 
A 1 220 ARG 220 516 516 ARG ARG A . n 
A 1 221 PHE 221 517 517 PHE PHE A . n 
A 1 222 ASP 222 518 518 ASP ASP A . n 
A 1 223 VAL 223 519 519 VAL VAL A . n 
A 1 224 LEU 224 520 520 LEU LEU A . n 
A 1 225 PRO 225 521 521 PRO PRO A . n 
A 1 226 LEU 226 522 522 LEU LEU A . n 
A 1 227 LEU 227 523 523 LEU LEU A . n 
A 1 228 LEU 228 524 524 LEU LEU A . n 
A 1 229 GLN 229 525 525 GLN GLN A . n 
A 1 230 ALA 230 526 526 ALA ALA A . n 
A 1 231 ASN 231 527 527 ASN ASN A . n 
A 1 232 GLY 232 528 528 GLY GLY A . n 
A 1 233 ASN 233 529 529 ASN ASN A . n 
A 1 234 ASP 234 530 530 ASP ASP A . n 
A 1 235 PRO 235 531 531 PRO PRO A . n 
A 1 236 GLU 236 532 532 GLU GLU A . n 
A 1 237 LEU 237 533 533 LEU LEU A . n 
A 1 238 PHE 238 534 534 PHE PHE A . n 
A 1 239 GLN 239 535 535 GLN GLN A . n 
A 1 240 ILE 240 536 536 ILE ILE A . n 
A 1 241 PRO 241 537 537 PRO PRO A . n 
A 1 242 PRO 242 538 538 PRO PRO A . n 
A 1 243 GLU 243 539 539 GLU GLU A . n 
A 1 244 LEU 244 540 540 LEU LEU A . n 
A 1 245 VAL 245 541 541 VAL VAL A . n 
A 1 246 LEU 246 542 542 LEU LEU A . n 
A 1 247 GLU 247 543 543 GLU GLU A . n 
A 1 248 VAL 248 544 544 VAL VAL A . n 
A 1 249 PRO 249 545 545 PRO PRO A . n 
A 1 250 ILE 250 546 546 ILE ILE A . n 
A 1 251 ARG 251 547 547 ARG ARG A . n 
A 1 252 HIS 252 548 548 HIS HIS A . n 
A 1 253 PRO 253 549 549 PRO PRO A . n 
A 1 254 LYS 254 550 550 LYS LYS A . n 
A 1 255 PHE 255 551 551 PHE PHE A . n 
A 1 256 ASP 256 552 552 ASP ASP A . n 
A 1 257 TRP 257 553 553 TRP TRP A . n 
A 1 258 PHE 258 554 554 PHE PHE A . n 
A 1 259 LYS 259 555 555 LYS LYS A . n 
A 1 260 ASP 260 556 556 ASP ASP A . n 
A 1 261 LEU 261 557 557 LEU LEU A . n 
A 1 262 GLY 262 558 558 GLY GLY A . n 
A 1 263 LEU 263 559 559 LEU LEU A . n 
A 1 264 LYS 264 560 560 LYS LYS A . n 
A 1 265 TRP 265 561 561 TRP TRP A . n 
A 1 266 TYR 266 562 562 TYR TYR A . n 
A 1 267 GLY 267 563 563 GLY GLY A . n 
A 1 268 LEU 268 564 564 LEU LEU A . n 
A 1 269 PRO 269 565 565 PRO PRO A . n 
A 1 270 ALA 270 566 566 ALA ALA A . n 
A 1 271 VAL 271 567 567 VAL VAL A . n 
A 1 272 SER 272 568 568 SER SER A . n 
A 1 273 ASN 273 569 569 ASN ASN A . n 
A 1 274 MET 274 570 570 MET MET A . n 
A 1 275 LEU 275 571 571 LEU LEU A . n 
A 1 276 LEU 276 572 572 LEU LEU A . n 
A 1 277 GLU 277 573 573 GLU GLU A . n 
A 1 278 ILE 278 574 574 ILE ILE A . n 
A 1 279 GLY 279 575 575 GLY GLY A . n 
A 1 280 GLY 280 576 576 GLY GLY A . n 
A 1 281 LEU 281 577 577 LEU LEU A . n 
A 1 282 GLU 282 578 578 GLU GLU A . n 
A 1 283 PHE 283 579 579 PHE PHE A . n 
A 1 284 SER 284 580 580 SER SER A . n 
A 1 285 ALA 285 581 581 ALA ALA A . n 
A 1 286 CYS 286 582 582 CYS CYS A . n 
A 1 287 PRO 287 583 583 PRO PRO A . n 
A 1 288 PHE 288 584 584 PHE PHE A . n 
A 1 289 SER 289 585 585 SER SER A . n 
A 1 290 GLY 290 586 586 GLY GLY A . n 
A 1 291 TRP 291 587 587 TRP TRP A . n 
A 1 292 TYR 292 588 588 TYR TYR A . n 
A 1 293 MET 293 589 589 MET MET A . n 
A 1 294 GLY 294 590 590 GLY GLY A . n 
A 1 295 THR 295 591 591 THR THR A . n 
A 1 296 GLU 296 592 592 GLU GLU A . n 
A 1 297 ILE 297 593 593 ILE ILE A . n 
A 1 298 GLY 298 594 594 GLY GLY A . n 
A 1 299 VAL 299 595 595 VAL VAL A . n 
A 1 300 ARG 300 596 596 ARG ARG A . n 
A 1 301 ASP 301 597 597 ASP ASP A . n 
A 1 302 TYR 302 598 598 TYR TYR A . n 
A 1 303 CYS 303 599 599 CYS CYS A . n 
A 1 304 ASP 304 600 600 ASP ASP A . n 
A 1 305 ASN 305 601 601 ASN ASN A . n 
A 1 306 SER 306 602 602 SER SER A . n 
A 1 307 ARG 307 603 603 ARG ARG A . n 
A 1 308 TYR 308 604 604 TYR TYR A . n 
A 1 309 ASN 309 605 605 ASN ASN A . n 
A 1 310 ILE 310 606 606 ILE ILE A . n 
A 1 311 LEU 311 607 607 LEU LEU A . n 
A 1 312 GLU 312 608 608 GLU GLU A . n 
A 1 313 GLU 313 609 609 GLU GLU A . n 
A 1 314 VAL 314 610 610 VAL VAL A . n 
A 1 315 ALA 315 611 611 ALA ALA A . n 
A 1 316 LYS 316 612 612 LYS LYS A . n 
A 1 317 LYS 317 613 613 LYS LYS A . n 
A 1 318 MET 318 614 614 MET MET A . n 
A 1 319 ASP 319 615 615 ASP ASP A . n 
A 1 320 LEU 320 616 616 LEU LEU A . n 
A 1 321 ASP 321 617 617 ASP ASP A . n 
A 1 322 MET 322 618 618 MET MET A . n 
A 1 323 ARG 323 619 619 ARG ARG A . n 
A 1 324 LYS 324 620 620 LYS LYS A . n 
A 1 325 THR 325 621 621 THR THR A . n 
A 1 326 SER 326 622 622 SER SER A . n 
A 1 327 SER 327 623 623 SER SER A . n 
A 1 328 LEU 328 624 624 LEU LEU A . n 
A 1 329 TRP 329 625 625 TRP TRP A . n 
A 1 330 LYS 330 626 626 LYS LYS A . n 
A 1 331 ASP 331 627 627 ASP ASP A . n 
A 1 332 GLN 332 628 628 GLN GLN A . n 
A 1 333 ALA 333 629 629 ALA ALA A . n 
A 1 334 LEU 334 630 630 LEU LEU A . n 
A 1 335 VAL 335 631 631 VAL VAL A . n 
A 1 336 GLU 336 632 632 GLU GLU A . n 
A 1 337 ILE 337 633 633 ILE ILE A . n 
A 1 338 ASN 338 634 634 ASN ASN A . n 
A 1 339 ILE 339 635 635 ILE ILE A . n 
A 1 340 ALA 340 636 636 ALA ALA A . n 
A 1 341 VAL 341 637 637 VAL VAL A . n 
A 1 342 LEU 342 638 638 LEU LEU A . n 
A 1 343 TYR 343 639 639 TYR TYR A . n 
A 1 344 SER 344 640 640 SER SER A . n 
A 1 345 PHE 345 641 641 PHE PHE A . n 
A 1 346 GLN 346 642 642 GLN GLN A . n 
A 1 347 SER 347 643 643 SER SER A . n 
A 1 348 ASP 348 644 644 ASP ASP A . n 
A 1 349 LYS 349 645 645 LYS LYS A . n 
A 1 350 VAL 350 646 646 VAL VAL A . n 
A 1 351 THR 351 647 647 THR THR A . n 
A 1 352 ILE 352 648 648 ILE ILE A . n 
A 1 353 VAL 353 649 649 VAL VAL A . n 
A 1 354 ASP 354 650 650 ASP ASP A . n 
A 1 355 HIS 355 651 651 HIS HIS A . n 
A 1 356 HIS 356 652 652 HIS HIS A . n 
A 1 357 SER 357 653 653 SER SER A . n 
A 1 358 ALA 358 654 654 ALA ALA A . n 
A 1 359 THR 359 655 655 THR THR A . n 
A 1 360 GLU 360 656 656 GLU GLU A . n 
A 1 361 SER 361 657 657 SER SER A . n 
A 1 362 PHE 362 658 658 PHE PHE A . n 
A 1 363 ILE 363 659 659 ILE ILE A . n 
A 1 364 LYS 364 660 660 LYS LYS A . n 
A 1 365 HIS 365 661 661 HIS HIS A . n 
A 1 366 MET 366 662 662 MET MET A . n 
A 1 367 GLU 367 663 663 GLU GLU A . n 
A 1 368 ASN 368 664 664 ASN ASN A . n 
A 1 369 GLU 369 665 665 GLU GLU A . n 
A 1 370 TYR 370 666 666 TYR TYR A . n 
A 1 371 ARG 371 667 667 ARG ARG A . n 
A 1 372 CYS 372 668 668 CYS CYS A . n 
A 1 373 ARG 373 669 669 ARG ARG A . n 
A 1 374 GLY 374 670 670 GLY GLY A . n 
A 1 375 GLY 375 671 671 GLY GLY A . n 
A 1 376 CYS 376 672 672 CYS CYS A . n 
A 1 377 PRO 377 673 673 PRO PRO A . n 
A 1 378 ALA 378 674 674 ALA ALA A . n 
A 1 379 ASP 379 675 675 ASP ASP A . n 
A 1 380 TRP 380 676 676 TRP TRP A . n 
A 1 381 VAL 381 677 677 VAL VAL A . n 
A 1 382 TRP 382 678 678 TRP TRP A . n 
A 1 383 ILE 383 679 679 ILE ILE A . n 
A 1 384 VAL 384 680 680 VAL VAL A . n 
A 1 385 PRO 385 681 681 PRO PRO A . n 
A 1 386 PRO 386 682 682 PRO PRO A . n 
A 1 387 MET 387 683 683 MET MET A . n 
A 1 388 SER 388 684 684 SER SER A . n 
A 1 389 GLY 389 685 685 GLY GLY A . n 
A 1 390 SER 390 686 686 SER SER A . n 
A 1 391 ILE 391 687 687 ILE ILE A . n 
A 1 392 THR 392 688 688 THR THR A . n 
A 1 393 PRO 393 689 689 PRO PRO A . n 
A 1 394 VAL 394 690 690 VAL VAL A . n 
A 1 395 PHE 395 691 691 PHE PHE A . n 
A 1 396 HIS 396 692 692 HIS HIS A . n 
A 1 397 GLN 397 693 693 GLN GLN A . n 
A 1 398 GLU 398 694 694 GLU GLU A . n 
A 1 399 MET 399 695 695 MET MET A . n 
A 1 400 LEU 400 696 696 LEU LEU A . n 
A 1 401 ASN 401 697 697 ASN ASN A . n 
A 1 402 TYR 402 698 698 TYR TYR A . n 
A 1 403 ARG 403 699 699 ARG ARG A . n 
A 1 404 LEU 404 700 700 LEU LEU A . n 
A 1 405 THR 405 701 701 THR THR A . n 
A 1 406 PRO 406 702 702 PRO PRO A . n 
A 1 407 SER 407 703 703 SER SER A . n 
A 1 408 PHE 408 704 704 PHE PHE A . n 
A 1 409 GLU 409 705 705 GLU GLU A . n 
A 1 410 TYR 410 706 706 TYR TYR A . n 
A 1 411 GLN 411 707 707 GLN GLN A . n 
A 1 412 PRO 412 708 708 PRO PRO A . n 
A 1 413 ASP 413 709 709 ASP ASP A . n 
A 1 414 PRO 414 710 710 PRO PRO A . n 
A 1 415 TRP 415 711 711 TRP TRP A . n 
A 1 416 ASN 416 712 712 ASN ASN A . n 
A 1 417 THR 417 713 713 THR THR A . n 
A 1 418 HIS 418 714 714 HIS HIS A . n 
A 1 419 VAL 419 715 715 VAL VAL A . n 
A 1 420 TRP 420 716 716 TRP TRP A . n 
A 1 421 LYS 421 717 717 LYS LYS A . n 
A 1 422 GLY 422 718 ?   ?   ?   A . n 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        A1A0D 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   A1A0D 
_pdbx_entity_instance_feature.auth_asym_id   ? 
_pdbx_entity_instance_feature.auth_seq_num   ? 
_pdbx_entity_instance_feature.feature_type   'SUBJECT OF INVESTIGATION' 
_pdbx_entity_instance_feature.details        ? 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
B 2 HEM   1  801 750 HEM   HEM A . 
C 3 H4B   1  802 760 H4B   BH4 A . 
D 4 ZN    1  803 900 ZN    ZN  A . 
E 5 A1A0D 1  804 800 A1A0D 2V3 A . 
F 6 HOH   1  901 10  HOH   HOH A . 
F 6 HOH   2  902 48  HOH   HOH A . 
F 6 HOH   3  903 25  HOH   HOH A . 
F 6 HOH   4  904 5   HOH   HOH A . 
F 6 HOH   5  905 41  HOH   HOH A . 
F 6 HOH   6  906 47  HOH   HOH A . 
F 6 HOH   7  907 23  HOH   HOH A . 
F 6 HOH   8  908 17  HOH   HOH A . 
F 6 HOH   9  909 50  HOH   HOH A . 
F 6 HOH   10 910 37  HOH   HOH A . 
F 6 HOH   11 911 43  HOH   HOH A . 
F 6 HOH   12 912 8   HOH   HOH A . 
F 6 HOH   13 913 30  HOH   HOH A . 
F 6 HOH   14 914 26  HOH   HOH A . 
F 6 HOH   15 915 49  HOH   HOH A . 
F 6 HOH   16 916 36  HOH   HOH A . 
F 6 HOH   17 917 34  HOH   HOH A . 
F 6 HOH   18 918 9   HOH   HOH A . 
F 6 HOH   19 919 16  HOH   HOH A . 
F 6 HOH   20 920 19  HOH   HOH A . 
F 6 HOH   21 921 27  HOH   HOH A . 
F 6 HOH   22 922 2   HOH   HOH A . 
F 6 HOH   23 923 1   HOH   HOH A . 
F 6 HOH   24 924 24  HOH   HOH A . 
F 6 HOH   25 925 14  HOH   HOH A . 
F 6 HOH   26 926 11  HOH   HOH A . 
F 6 HOH   27 927 22  HOH   HOH A . 
F 6 HOH   28 928 6   HOH   HOH A . 
F 6 HOH   29 929 3   HOH   HOH A . 
F 6 HOH   30 930 4   HOH   HOH A . 
F 6 HOH   31 931 29  HOH   HOH A . 
F 6 HOH   32 932 20  HOH   HOH A . 
F 6 HOH   33 933 33  HOH   HOH A . 
F 6 HOH   34 934 38  HOH   HOH A . 
F 6 HOH   35 935 13  HOH   HOH A . 
F 6 HOH   36 936 40  HOH   HOH A . 
F 6 HOH   37 937 46  HOH   HOH A . 
F 6 HOH   38 938 15  HOH   HOH A . 
F 6 HOH   39 939 31  HOH   HOH A . 
F 6 HOH   40 940 52  HOH   HOH A . 
F 6 HOH   41 941 7   HOH   HOH A . 
F 6 HOH   42 942 21  HOH   HOH A . 
F 6 HOH   43 943 42  HOH   HOH A . 
F 6 HOH   44 944 28  HOH   HOH A . 
F 6 HOH   45 945 12  HOH   HOH A . 
F 6 HOH   46 946 39  HOH   HOH A . 
F 6 HOH   47 947 18  HOH   HOH A . 
F 6 HOH   48 948 44  HOH   HOH A . 
F 6 HOH   49 949 51  HOH   HOH A . 
F 6 HOH   50 950 35  HOH   HOH A . 
F 6 HOH   51 951 32  HOH   HOH A . 
F 6 HOH   52 952 45  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                     9CVQ 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     48.638 
_cell.length_a_esd                 ? 
_cell.length_b                     113.175 
_cell.length_b_esd                 ? 
_cell.length_c                     163.242 
_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                         9CVQ 
_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                   9CVQ 
_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                     CCD 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'ADSC QUANTUM 315' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2022-09-17 
_diffrn_detector.pdbx_frequency               ? 
_diffrn_detector.id                           ? 
_diffrn_detector.number_of_axes               ? 
# 
_diffrn_radiation.collimation                      ? 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.filter_edge                      ? 
_diffrn_radiation.inhomogeneity                    ? 
_diffrn_radiation.monochromator                    'DOUBLE CRYSTAL SI(III)' 
_diffrn_radiation.polarisn_norm                    ? 
_diffrn_radiation.polarisn_ratio                   ? 
_diffrn_radiation.probe                            ? 
_diffrn_radiation.type                             ? 
_diffrn_radiation.xray_symbol                      ? 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.pdbx_wavelength_list             ? 
_diffrn_radiation.pdbx_wavelength                  ? 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_analyzer                    ? 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   1.000 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.current                     ? 
_diffrn_source.details                     ? 
_diffrn_source.diffrn_id                   1 
_diffrn_source.power                       ? 
_diffrn_source.size                        ? 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.target                      ? 
_diffrn_source.type                        'ALS BEAMLINE 8.2.1' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        1.000 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   8.2.1 
_diffrn_source.pdbx_synchrotron_site       ALS 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       9CVQ 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              1.95 
_reflns.d_resolution_low                               29.81 
_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                                     32337 
_reflns.observed_criterion                             ? 
_reflns.observed_criterion_F_max                       ? 
_reflns.observed_criterion_F_min                       ? 
_reflns.observed_criterion_I_max                       ? 
_reflns.observed_criterion_I_min                       ? 
_reflns.observed_criterion_sigma_F                     ? 
_reflns.observed_criterion_sigma_I                     ? 
_reflns.percent_possible_obs                           97.2 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                12.0 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          15.3 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               ? 
_reflns.pdbx_scaling_rejects                           ? 
_reflns.pdbx_d_res_high_opt                            ? 
_reflns.pdbx_d_res_low_opt                             ? 
_reflns.pdbx_d_res_opt_method                          ? 
_reflns.phase_calculation_details                      ? 
_reflns.pdbx_Rrim_I_all                                0.164 
_reflns.pdbx_Rpim_I_all                                0.047 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       388707 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.999 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              0.157 
_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                                    1.95 
_reflns_shell.d_res_low                                     2.00 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           ? 
_reflns_shell.number_measured_all                           25602 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             2225 
_reflns_shell.percent_possible_obs                          97.1 
_reflns_shell.Rmerge_F_all                                  ? 
_reflns_shell.Rmerge_F_obs                                  ? 
_reflns_shell.meanI_over_sigI_gt                            ? 
_reflns_shell.meanI_over_uI_all                             ? 
_reflns_shell.meanI_over_uI_gt                              ? 
_reflns_shell.number_measured_gt                            ? 
_reflns_shell.number_unique_gt                              ? 
_reflns_shell.percent_possible_gt                           ? 
_reflns_shell.Rmerge_F_gt                                   ? 
_reflns_shell.Rmerge_I_gt                                   ? 
_reflns_shell.pdbx_redundancy                               11.5 
_reflns_shell.pdbx_chi_squared                              ? 
_reflns_shell.pdbx_netI_over_sigmaI_all                     ? 
_reflns_shell.pdbx_netI_over_sigmaI_obs                     0.9 
_reflns_shell.pdbx_Rrim_I_all                               9.590 
_reflns_shell.pdbx_Rpim_I_all                               2.797 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.499 
_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                                  9.162 
_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                                 9CVQ 
_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                            1.95 
_refine.ls_d_res_low                             29.81 
_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                     31959 
_refine.ls_number_reflns_R_free                  1626 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    95.84 
_refine.ls_percent_reflns_R_free                 5.09 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.2339 
_refine.ls_R_factor_R_free                       0.2687 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.2320 
_refine.ls_R_Fsqd_factor_obs                     ? 
_refine.ls_R_I_factor_obs                        ? 
_refine.ls_redundancy_reflns_all                 ? 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.ls_restrained_S_all                      ? 
_refine.ls_restrained_S_obs                      ? 
_refine.ls_shift_over_esd_max                    ? 
_refine.ls_shift_over_esd_mean                   ? 
_refine.ls_structure_factor_coef                 ? 
_refine.ls_weighting_details                     ? 
_refine.ls_weighting_scheme                      ? 
_refine.ls_wR_factor_all                         ? 
_refine.ls_wR_factor_obs                         ? 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_wR_factor_R_work                      ? 
_refine.occupancy_max                            ? 
_refine.occupancy_min                            ? 
_refine.solvent_model_details                    'FLAT BULK SOLVENT MODEL' 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.pdbx_R_complete                          ? 
_refine.ls_R_factor_gt                           ? 
_refine.ls_goodness_of_fit_gt                    ? 
_refine.ls_goodness_of_fit_ref                   ? 
_refine.ls_shift_over_su_max                     ? 
_refine.ls_shift_over_su_max_lt                  ? 
_refine.ls_shift_over_su_mean                    ? 
_refine.ls_shift_over_su_mean_lt                 ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          1.33 
_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                 43.80 
_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                            0.33 
_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                       1.95 
_refine_hist.d_res_low                        29.81 
_refine_hist.number_atoms_solvent             52 
_refine_hist.number_atoms_total               3514 
_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        3378 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         84 
_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' ? 0.007  ? 3569 ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 1.162  ? 4863 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 17.122 ? 1297 ? f_dihedral_angle_d ? ? 
'X-RAY DIFFRACTION' ? 0.051  ? 505  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.007  ? 613  ? 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' 1.95 2.01  . . 133 2471 96.00 . . . . 0.5530 . . . . . . . . . . . 0.5885 
'X-RAY DIFFRACTION' 2.01 2.07  . . 104 2486 95.00 . . . . 0.5079 . . . . . . . . . . . 0.5150 
'X-RAY DIFFRACTION' 2.07 2.15  . . 144 2362 92.00 . . . . 0.4444 . . . . . . . . . . . 0.4894 
'X-RAY DIFFRACTION' 2.15 2.23  . . 145 2503 96.00 . . . . 0.4160 . . . . . . . . . . . 0.4592 
'X-RAY DIFFRACTION' 2.23 2.33  . . 126 2507 96.00 . . . . 0.3597 . . . . . . . . . . . 0.4150 
'X-RAY DIFFRACTION' 2.33 2.46  . . 138 2526 96.00 . . . . 0.3174 . . . . . . . . . . . 0.4047 
'X-RAY DIFFRACTION' 2.46 2.61  . . 116 2415 93.00 . . . . 0.2843 . . . . . . . . . . . 0.3349 
'X-RAY DIFFRACTION' 2.61 2.81  . . 129 2590 97.00 . . . . 0.2867 . . . . . . . . . . . 0.3348 
'X-RAY DIFFRACTION' 2.81 3.09  . . 124 2595 98.00 . . . . 0.2668 . . . . . . . . . . . 0.2973 
'X-RAY DIFFRACTION' 3.09 3.54  . . 161 2554 97.00 . . . . 0.2384 . . . . . . . . . . . 0.2508 
'X-RAY DIFFRACTION' 3.54 4.46  . . 148 2644 99.00 . . . . 0.1810 . . . . . . . . . . . 0.2125 
'X-RAY DIFFRACTION' 4.46 29.81 . . 158 2680 96.00 . . . . 0.1626 . . . . . . . . . . . 0.2181 
# 
_struct.entry_id                     9CVQ 
_struct.title                        
;Structure of rat neuronal nitric oxide synthase R349A mutant heme domain bound with 6-(5-((3,3-difluoroazetidin-1-yl)methyl)-2,3-difluorophenyl)-4-methylpyridin-2-amine dihydrochloride
;
_struct.pdbx_model_details           ? 
_struct.pdbx_formula_weight          ? 
_struct.pdbx_formula_weight_method   ? 
_struct.pdbx_model_type_details      ? 
_struct.pdbx_CASP_flag               N 
# 
_struct_keywords.entry_id        9CVQ 
_struct_keywords.text            'nitric oxide synthase inhibitor binding, OXIDOREDUCTASE' 
_struct_keywords.pdbx_keywords   OXIDOREDUCTASE 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 2 ? 
C N N 3 ? 
D N N 4 ? 
E N N 5 ? 
F N N 6 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    NOS1_RAT 
_struct_ref.pdbx_db_accession          P29476 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;CPRFLKVKNWETDVVLTDTLHLKSTLETGCTEHICMGSIMLPSQHTRKPEDVRTKDQLFPLAKEFLDQYYSSIKRFGSKA
HMDRLEEVNKEIESTSTYQLKDTELIYGAKHAWRNASRCVGRIQWSKLQVFDARDCTTAHGMFNYICNHVKYATNKGNLR
SAITIFPQRTDGKHDFRVWNSQLIRYAGYKQPDGSTLGDPANVQFTEICIQQGWKAPRGRFDVLPLLLQANGNDPELFQI
PPELVLEVPIRHPKFDWFKDLGLKWYGLPAVSNMLLEIGGLEFSACPFSGWYMGTEIGVRDYCDNSRYNILEEVAKKMDL
DMRKTSSLWKDQALVEINIAVLYSFQSDKVTIVDHHSATESFIKHMENEYRCRGGCPADWVWIVPPMSGSITPVFHQEML
NYRLTPSFEYQPDPWNTHVWKG
;
_struct_ref.pdbx_align_begin           297 
# 
_struct_ref_seq.align_id                      1 
_struct_ref_seq.ref_id                        1 
_struct_ref_seq.pdbx_PDB_id_code              9CVQ 
_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             9CVQ 
_struct_ref_seq_dif.mon_id                       ALA 
_struct_ref_seq_dif.pdbx_pdb_strand_id           A 
_struct_ref_seq_dif.seq_num                      53 
_struct_ref_seq_dif.pdbx_pdb_ins_code            ? 
_struct_ref_seq_dif.pdbx_seq_db_name             UNP 
_struct_ref_seq_dif.pdbx_seq_db_accession_code   P29476 
_struct_ref_seq_dif.db_mon_id                    ARG 
_struct_ref_seq_dif.pdbx_seq_db_seq_num          349 
_struct_ref_seq_dif.details                      'engineered mutation' 
_struct_ref_seq_dif.pdbx_auth_seq_num            349 
_struct_ref_seq_dif.pdbx_ordinal                 1 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_defined_assembly 
_pdbx_struct_assembly.method_details       ? 
_pdbx_struct_assembly.oligomeric_details   monomeric 
_pdbx_struct_assembly.oligomeric_count     1 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,D,E,F 
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   'gel filtration' 
_pdbx_struct_assembly_auth_evidence.details                ? 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1  AA1 THR A 19  ? SER A 24  ? THR A 315 SER A 320 5 ? 6  
HELX_P HELX_P2  AA2 THR A 54  ? ILE A 73  ? THR A 350 ILE A 369 1 ? 20 
HELX_P HELX_P3  AA3 SER A 78  ? THR A 95  ? SER A 374 THR A 391 1 ? 18 
HELX_P HELX_P4  AA4 LYS A 101 ? ASN A 115 ? LYS A 397 ASN A 411 1 ? 15 
HELX_P HELX_P5  AA5 GLY A 121 ? TRP A 125 ? GLY A 417 TRP A 421 5 ? 5  
HELX_P HELX_P6  AA6 THR A 138 ? ASN A 155 ? THR A 434 ASN A 451 1 ? 18 
HELX_P HELX_P7  AA7 LYS A 156 ? ASN A 158 ? LYS A 452 ASN A 454 5 ? 3  
HELX_P HELX_P8  AA8 ASN A 202 ? GLN A 212 ? ASN A 498 GLN A 508 1 ? 11 
HELX_P HELX_P9  AA9 PRO A 241 ? VAL A 245 ? PRO A 537 VAL A 541 5 ? 5  
HELX_P HELX_P10 AB1 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 ? ASP A 319 ? ILE A 606 ASP A 615 1 ? 10 
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 ? ARG A 373 ? ASP A 650 ARG A 669 1 ? 20 
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 ? THR A 392 ? SER A 684 THR A 688 5 ? 5  
HELX_P HELX_P19 AC1 ASP A 413 ? THR A 417 ? ASP A 709 THR A 713 5 ? 5  
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_conn.id 
_struct_conn.conn_type_id 
_struct_conn.pdbx_leaving_atom_flag 
_struct_conn.pdbx_PDB_id 
_struct_conn.ptnr1_label_asym_id 
_struct_conn.ptnr1_label_comp_id 
_struct_conn.ptnr1_label_seq_id 
_struct_conn.ptnr1_label_atom_id 
_struct_conn.pdbx_ptnr1_label_alt_id 
_struct_conn.pdbx_ptnr1_PDB_ins_code 
_struct_conn.pdbx_ptnr1_standard_comp_id 
_struct_conn.ptnr1_symmetry 
_struct_conn.ptnr2_label_asym_id 
_struct_conn.ptnr2_label_comp_id 
_struct_conn.ptnr2_label_seq_id 
_struct_conn.ptnr2_label_atom_id 
_struct_conn.pdbx_ptnr2_label_alt_id 
_struct_conn.pdbx_ptnr2_PDB_ins_code 
_struct_conn.ptnr1_auth_asym_id 
_struct_conn.ptnr1_auth_comp_id 
_struct_conn.ptnr1_auth_seq_id 
_struct_conn.ptnr2_auth_asym_id 
_struct_conn.ptnr2_auth_comp_id 
_struct_conn.ptnr2_auth_seq_id 
_struct_conn.ptnr2_symmetry 
_struct_conn.pdbx_ptnr3_label_atom_id 
_struct_conn.pdbx_ptnr3_label_seq_id 
_struct_conn.pdbx_ptnr3_label_comp_id 
_struct_conn.pdbx_ptnr3_label_asym_id 
_struct_conn.pdbx_ptnr3_label_alt_id 
_struct_conn.pdbx_ptnr3_PDB_ins_code 
_struct_conn.details 
_struct_conn.pdbx_dist_value 
_struct_conn.pdbx_value_order 
_struct_conn.pdbx_role 
metalc1 metalc ? ? A CYS 30  SG ? ? ? 1_555 D ZN  . ZN ? ? A CYS 326 A ZN  803 1_555 ? ? ? ? ? ? ? 2.303 ? ? 
metalc2 metalc ? ? A CYS 30  SG ? ? ? 1_555 D ZN  . ZN ? ? A CYS 326 A ZN  803 3_455 ? ? ? ? ? ? ? 2.278 ? ? 
metalc3 metalc ? ? A CYS 35  SG ? ? ? 1_555 D ZN  . ZN ? ? A CYS 331 A ZN  803 1_555 ? ? ? ? ? ? ? 2.267 ? ? 
metalc4 metalc ? ? A CYS 35  SG ? ? ? 1_555 D ZN  . ZN ? ? A CYS 331 A ZN  803 3_455 ? ? ? ? ? ? ? 2.259 ? ? 
metalc5 metalc ? ? A CYS 119 SG ? ? ? 1_555 B HEM . FE ? ? A CYS 415 A HEM 801 1_555 ? ? ? ? ? ? ? 2.375 ? ? 
# 
_struct_conn_type.id          metalc 
_struct_conn_type.criteria    ? 
_struct_conn_type.reference   ? 
# 
loop_
_pdbx_struct_conn_angle.id 
_pdbx_struct_conn_angle.ptnr1_label_atom_id 
_pdbx_struct_conn_angle.ptnr1_label_alt_id 
_pdbx_struct_conn_angle.ptnr1_label_asym_id 
_pdbx_struct_conn_angle.ptnr1_label_comp_id 
_pdbx_struct_conn_angle.ptnr1_label_seq_id 
_pdbx_struct_conn_angle.ptnr1_auth_atom_id 
_pdbx_struct_conn_angle.ptnr1_auth_asym_id 
_pdbx_struct_conn_angle.ptnr1_auth_comp_id 
_pdbx_struct_conn_angle.ptnr1_auth_seq_id 
_pdbx_struct_conn_angle.ptnr1_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr1_symmetry 
_pdbx_struct_conn_angle.ptnr2_label_atom_id 
_pdbx_struct_conn_angle.ptnr2_label_alt_id 
_pdbx_struct_conn_angle.ptnr2_label_asym_id 
_pdbx_struct_conn_angle.ptnr2_label_comp_id 
_pdbx_struct_conn_angle.ptnr2_label_seq_id 
_pdbx_struct_conn_angle.ptnr2_auth_atom_id 
_pdbx_struct_conn_angle.ptnr2_auth_asym_id 
_pdbx_struct_conn_angle.ptnr2_auth_comp_id 
_pdbx_struct_conn_angle.ptnr2_auth_seq_id 
_pdbx_struct_conn_angle.ptnr2_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr2_symmetry 
_pdbx_struct_conn_angle.ptnr3_label_atom_id 
_pdbx_struct_conn_angle.ptnr3_label_alt_id 
_pdbx_struct_conn_angle.ptnr3_label_asym_id 
_pdbx_struct_conn_angle.ptnr3_label_comp_id 
_pdbx_struct_conn_angle.ptnr3_label_seq_id 
_pdbx_struct_conn_angle.ptnr3_auth_atom_id 
_pdbx_struct_conn_angle.ptnr3_auth_asym_id 
_pdbx_struct_conn_angle.ptnr3_auth_comp_id 
_pdbx_struct_conn_angle.ptnr3_auth_seq_id 
_pdbx_struct_conn_angle.ptnr3_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr3_symmetry 
_pdbx_struct_conn_angle.value 
_pdbx_struct_conn_angle.value_esd 
1  SG ? A CYS 30  ? A CYS 326 ? 1_555 ZN ? D ZN  . ? A ZN  803 ? 1_555 SG ? A CYS 30 ? A CYS 326 ? 1_555 0.0   ? 
2  SG ? A CYS 30  ? A CYS 326 ? 1_555 ZN ? D ZN  . ? A ZN  803 ? 1_555 SG ? A CYS 35 ? A CYS 331 ? 1_555 112.5 ? 
3  SG ? A CYS 30  ? A CYS 326 ? 1_555 ZN ? D ZN  . ? A ZN  803 ? 1_555 SG ? A CYS 35 ? A CYS 331 ? 1_555 112.5 ? 
4  SG ? A CYS 30  ? A CYS 326 ? 1_555 ZN ? D ZN  . ? A ZN  803 ? 1_555 SG ? A CYS 35 ? A CYS 331 ? 1_555 112.5 ? 
5  SG ? A CYS 30  ? A CYS 326 ? 1_555 ZN ? D ZN  . ? A ZN  803 ? 1_555 SG ? A CYS 35 ? A CYS 331 ? 1_555 112.5 ? 
6  SG ? A CYS 35  ? A CYS 331 ? 1_555 ZN ? D ZN  . ? A ZN  803 ? 1_555 SG ? A CYS 35 ? A CYS 331 ? 1_555 0.0   ? 
7  SG ? A CYS 119 ? A CYS 415 ? 1_555 FE ? B HEM . ? A HEM 801 ? 1_555 NA ? B HEM .  ? A HEM 801 ? 1_555 100.7 ? 
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 98.2  ? 
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 86.5  ? 
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_555 100.9 ? 
11 NA ? B HEM .   ? A HEM 801 ? 1_555 FE ? B HEM . ? A HEM 801 ? 1_555 NC ? B HEM .  ? A HEM 801 ? 1_555 158.0 ? 
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 86.2  ? 
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_555 107.8 ? 
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 88.4  ? 
15 NB ? B HEM .   ? A HEM 801 ? 1_555 FE ? B HEM . ? A HEM 801 ? 1_555 ND ? B HEM .  ? A HEM 801 ? 1_555 154.0 ? 
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 89.0  ? 
# 
_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       -1.02 
# 
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                   9CVQ 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.has_protein_modification   N 
# 
_pdbx_validate_close_contact.id               1 
_pdbx_validate_close_contact.PDB_model_num    1 
_pdbx_validate_close_contact.auth_atom_id_1   OE1 
_pdbx_validate_close_contact.auth_asym_id_1   A 
_pdbx_validate_close_contact.auth_comp_id_1   GLN 
_pdbx_validate_close_contact.auth_seq_id_1    478 
_pdbx_validate_close_contact.PDB_ins_code_1   ? 
_pdbx_validate_close_contact.label_alt_id_1   ? 
_pdbx_validate_close_contact.auth_atom_id_2   O 
_pdbx_validate_close_contact.auth_asym_id_2   A 
_pdbx_validate_close_contact.auth_comp_id_2   HOH 
_pdbx_validate_close_contact.auth_seq_id_2    901 
_pdbx_validate_close_contact.PDB_ins_code_2   ? 
_pdbx_validate_close_contact.label_alt_id_2   ? 
_pdbx_validate_close_contact.dist             2.09 
# 
_pdbx_validate_symm_contact.id                1 
_pdbx_validate_symm_contact.PDB_model_num     1 
_pdbx_validate_symm_contact.auth_atom_id_1    OD2 
_pdbx_validate_symm_contact.auth_asym_id_1    A 
_pdbx_validate_symm_contact.auth_comp_id_1    ASP 
_pdbx_validate_symm_contact.auth_seq_id_1     627 
_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    OG 
_pdbx_validate_symm_contact.auth_asym_id_2    A 
_pdbx_validate_symm_contact.auth_comp_id_2    SER 
_pdbx_validate_symm_contact.auth_seq_id_2     684 
_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              2.17 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1  1 THR A 321 ? ? -126.30 -57.73  
2  1 LEU A 337 ? ? -110.32 74.38   
3  1 HIS A 341 ? ? -69.24  5.16    
4  1 SER A 374 ? ? -67.21  -177.98 
5  1 SER A 392 ? ? 57.67   17.74   
6  1 THR A 466 ? ? -118.08 -87.21  
7  1 HIS A 470 ? ? -117.54 76.07   
8  1 PRO A 513 ? ? -85.29  44.46   
9  1 ARG A 514 ? ? -17.70  72.09   
10 1 ARG A 516 ? ? -77.18  -82.15  
11 1 PHE A 517 ? ? -92.92  56.19   
12 1 LYS A 550 ? ? -131.27 -52.07  
13 1 CYS A 582 ? ? -149.81 53.05   
14 1 VAL A 595 ? ? -106.35 -60.19  
15 1 ARG A 603 ? ? -120.21 -141.50 
16 1 ASP A 615 ? ? 54.82   76.33   
17 1 ASP A 617 ? ? -68.44  90.77   
18 1 ARG A 669 ? ? -144.18 -16.32  
19 1 VAL A 715 ? ? -57.65  106.28  
# 
_pdbx_struct_special_symmetry.id              1 
_pdbx_struct_special_symmetry.PDB_model_num   1 
_pdbx_struct_special_symmetry.auth_asym_id    A 
_pdbx_struct_special_symmetry.auth_comp_id    ZN 
_pdbx_struct_special_symmetry.auth_seq_id     803 
_pdbx_struct_special_symmetry.PDB_ins_code    ? 
_pdbx_struct_special_symmetry.label_asym_id   D 
_pdbx_struct_special_symmetry.label_comp_id   ZN 
_pdbx_struct_special_symmetry.label_seq_id    . 
# 
_pdbx_refine_tls.id               1 
_pdbx_refine_tls.pdbx_refine_id   'X-RAY DIFFRACTION' 
_pdbx_refine_tls.details          ? 
_pdbx_refine_tls.method           refined 
_pdbx_refine_tls.origin_x         -23.4521 
_pdbx_refine_tls.origin_y         -5.0387 
_pdbx_refine_tls.origin_z         22.2526 
_pdbx_refine_tls.T[1][1]          0.3512 
_pdbx_refine_tls.T[1][1]_esd      ? 
_pdbx_refine_tls.T[1][2]          -0.0335 
_pdbx_refine_tls.T[1][2]_esd      ? 
_pdbx_refine_tls.T[1][3]          -0.0773 
_pdbx_refine_tls.T[1][3]_esd      ? 
_pdbx_refine_tls.T[2][2]          0.4535 
_pdbx_refine_tls.T[2][2]_esd      ? 
_pdbx_refine_tls.T[2][3]          -0.0174 
_pdbx_refine_tls.T[2][3]_esd      ? 
_pdbx_refine_tls.T[3][3]          0.4899 
_pdbx_refine_tls.T[3][3]_esd      ? 
_pdbx_refine_tls.L[1][1]          1.3096 
_pdbx_refine_tls.L[1][1]_esd      ? 
_pdbx_refine_tls.L[1][2]          -0.0000 
_pdbx_refine_tls.L[1][2]_esd      ? 
_pdbx_refine_tls.L[1][3]          0.4258 
_pdbx_refine_tls.L[1][3]_esd      ? 
_pdbx_refine_tls.L[2][2]          1.7048 
_pdbx_refine_tls.L[2][2]_esd      ? 
_pdbx_refine_tls.L[2][3]          -0.1596 
_pdbx_refine_tls.L[2][3]_esd      ? 
_pdbx_refine_tls.L[3][3]          9.4310 
_pdbx_refine_tls.L[3][3]_esd      ? 
_pdbx_refine_tls.S[1][1]          -0.0692 
_pdbx_refine_tls.S[1][1]_esd      ? 
_pdbx_refine_tls.S[1][2]          0.2084 
_pdbx_refine_tls.S[1][2]_esd      ? 
_pdbx_refine_tls.S[1][3]          -0.0197 
_pdbx_refine_tls.S[1][3]_esd      ? 
_pdbx_refine_tls.S[2][1]          -0.0269 
_pdbx_refine_tls.S[2][1]_esd      ? 
_pdbx_refine_tls.S[2][2]          -0.0678 
_pdbx_refine_tls.S[2][2]_esd      ? 
_pdbx_refine_tls.S[2][3]          -0.1128 
_pdbx_refine_tls.S[2][3]_esd      ? 
_pdbx_refine_tls.S[3][1]          -0.5680 
_pdbx_refine_tls.S[3][1]_esd      ? 
_pdbx_refine_tls.S[3][2]          0.2945 
_pdbx_refine_tls.S[3][2]_esd      ? 
_pdbx_refine_tls.S[3][3]          0.0971 
_pdbx_refine_tls.S[3][3]_esd      ? 
# 
_pdbx_refine_tls_group.id                  1 
_pdbx_refine_tls_group.pdbx_refine_id      'X-RAY DIFFRACTION' 
_pdbx_refine_tls_group.refine_tls_id       1 
_pdbx_refine_tls_group.beg_label_asym_id   ? 
_pdbx_refine_tls_group.beg_label_seq_id    ? 
_pdbx_refine_tls_group.beg_auth_asym_id    ? 
_pdbx_refine_tls_group.beg_auth_seq_id     ? 
_pdbx_refine_tls_group.beg_PDB_ins_code    ? 
_pdbx_refine_tls_group.end_label_asym_id   ? 
_pdbx_refine_tls_group.end_label_seq_id    ? 
_pdbx_refine_tls_group.end_auth_asym_id    ? 
_pdbx_refine_tls_group.end_auth_seq_id     ? 
_pdbx_refine_tls_group.end_PDB_ins_code    ? 
_pdbx_refine_tls_group.selection           ? 
_pdbx_refine_tls_group.selection_details   '(chain A and resid 299:716)' 
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1 1 Y 1 A CYS 297 ? A CYS 1   
2 1 Y 1 A PRO 298 ? A PRO 2   
3 1 Y 1 A LYS 344 ? A LYS 48  
4 1 Y 1 A PRO 345 ? A PRO 49  
5 1 Y 1 A GLU 346 ? A GLU 50  
6 1 Y 1 A ASP 347 ? A ASP 51  
7 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 
A1A0D C11  C  Y N 1   
A1A0D C12  C  Y N 2   
A1A0D C13  C  Y N 3   
A1A0D C15  C  Y N 4   
A1A0D C16  C  Y N 5   
A1A0D C17  C  N N 6   
A1A0D C19  C  N N 7   
A1A0D C20  C  N N 8   
A1A0D C21  C  N N 9   
A1A0D C02  C  Y N 10  
A1A0D C03  C  Y N 11  
A1A0D C04  C  Y N 12  
A1A0D C05  C  Y N 13  
A1A0D C06  C  Y N 14  
A1A0D C07  C  N N 15  
A1A0D C14  C  Y N 16  
A1A0D F12  F  N N 17  
A1A0D F13  F  N N 18  
A1A0D F22  F  N N 19  
A1A0D F23  F  N N 20  
A1A0D N01  N  Y N 21  
A1A0D N02  N  N N 22  
A1A0D N18  N  N N 23  
A1A0D H1   H  N N 24  
A1A0D H2   H  N N 25  
A1A0D H3   H  N N 26  
A1A0D H4   H  N N 27  
A1A0D H5   H  N N 28  
A1A0D H6   H  N N 29  
A1A0D H7   H  N N 30  
A1A0D H8   H  N N 31  
A1A0D H9   H  N N 32  
A1A0D H10  H  N N 33  
A1A0D H11  H  N N 34  
A1A0D H12  H  N N 35  
A1A0D H13  H  N N 36  
A1A0D H14  H  N N 37  
A1A0D H15  H  N N 38  
ALA   N    N  N N 39  
ALA   CA   C  N S 40  
ALA   C    C  N N 41  
ALA   O    O  N N 42  
ALA   CB   C  N N 43  
ALA   OXT  O  N N 44  
ALA   H    H  N N 45  
ALA   H2   H  N N 46  
ALA   HA   H  N N 47  
ALA   HB1  H  N N 48  
ALA   HB2  H  N N 49  
ALA   HB3  H  N N 50  
ALA   HXT  H  N N 51  
ARG   N    N  N N 52  
ARG   CA   C  N S 53  
ARG   C    C  N N 54  
ARG   O    O  N N 55  
ARG   CB   C  N N 56  
ARG   CG   C  N N 57  
ARG   CD   C  N N 58  
ARG   NE   N  N N 59  
ARG   CZ   C  N N 60  
ARG   NH1  N  N N 61  
ARG   NH2  N  N N 62  
ARG   OXT  O  N N 63  
ARG   H    H  N N 64  
ARG   H2   H  N N 65  
ARG   HA   H  N N 66  
ARG   HB2  H  N N 67  
ARG   HB3  H  N N 68  
ARG   HG2  H  N N 69  
ARG   HG3  H  N N 70  
ARG   HD2  H  N N 71  
ARG   HD3  H  N N 72  
ARG   HE   H  N N 73  
ARG   HH11 H  N N 74  
ARG   HH12 H  N N 75  
ARG   HH21 H  N N 76  
ARG   HH22 H  N N 77  
ARG   HXT  H  N N 78  
ASN   N    N  N N 79  
ASN   CA   C  N S 80  
ASN   C    C  N N 81  
ASN   O    O  N N 82  
ASN   CB   C  N N 83  
ASN   CG   C  N N 84  
ASN   OD1  O  N N 85  
ASN   ND2  N  N N 86  
ASN   OXT  O  N N 87  
ASN   H    H  N N 88  
ASN   H2   H  N N 89  
ASN   HA   H  N N 90  
ASN   HB2  H  N N 91  
ASN   HB3  H  N N 92  
ASN   HD21 H  N N 93  
ASN   HD22 H  N N 94  
ASN   HXT  H  N N 95  
ASP   N    N  N N 96  
ASP   CA   C  N S 97  
ASP   C    C  N N 98  
ASP   O    O  N N 99  
ASP   CB   C  N N 100 
ASP   CG   C  N N 101 
ASP   OD1  O  N N 102 
ASP   OD2  O  N N 103 
ASP   OXT  O  N N 104 
ASP   H    H  N N 105 
ASP   H2   H  N N 106 
ASP   HA   H  N N 107 
ASP   HB2  H  N N 108 
ASP   HB3  H  N N 109 
ASP   HD2  H  N N 110 
ASP   HXT  H  N N 111 
CYS   N    N  N N 112 
CYS   CA   C  N R 113 
CYS   C    C  N N 114 
CYS   O    O  N N 115 
CYS   CB   C  N N 116 
CYS   SG   S  N N 117 
CYS   OXT  O  N N 118 
CYS   H    H  N N 119 
CYS   H2   H  N N 120 
CYS   HA   H  N N 121 
CYS   HB2  H  N N 122 
CYS   HB3  H  N N 123 
CYS   HG   H  N N 124 
CYS   HXT  H  N N 125 
GLN   N    N  N N 126 
GLN   CA   C  N S 127 
GLN   C    C  N N 128 
GLN   O    O  N N 129 
GLN   CB   C  N N 130 
GLN   CG   C  N N 131 
GLN   CD   C  N N 132 
GLN   OE1  O  N N 133 
GLN   NE2  N  N N 134 
GLN   OXT  O  N N 135 
GLN   H    H  N N 136 
GLN   H2   H  N N 137 
GLN   HA   H  N N 138 
GLN   HB2  H  N N 139 
GLN   HB3  H  N N 140 
GLN   HG2  H  N N 141 
GLN   HG3  H  N N 142 
GLN   HE21 H  N N 143 
GLN   HE22 H  N N 144 
GLN   HXT  H  N N 145 
GLU   N    N  N N 146 
GLU   CA   C  N S 147 
GLU   C    C  N N 148 
GLU   O    O  N N 149 
GLU   CB   C  N N 150 
GLU   CG   C  N N 151 
GLU   CD   C  N N 152 
GLU   OE1  O  N N 153 
GLU   OE2  O  N N 154 
GLU   OXT  O  N N 155 
GLU   H    H  N N 156 
GLU   H2   H  N N 157 
GLU   HA   H  N N 158 
GLU   HB2  H  N N 159 
GLU   HB3  H  N N 160 
GLU   HG2  H  N N 161 
GLU   HG3  H  N N 162 
GLU   HE2  H  N N 163 
GLU   HXT  H  N N 164 
GLY   N    N  N N 165 
GLY   CA   C  N N 166 
GLY   C    C  N N 167 
GLY   O    O  N N 168 
GLY   OXT  O  N N 169 
GLY   H    H  N N 170 
GLY   H2   H  N N 171 
GLY   HA2  H  N N 172 
GLY   HA3  H  N N 173 
GLY   HXT  H  N N 174 
H4B   N1   N  Y N 175 
H4B   C2   C  Y N 176 
H4B   N2   N  N N 177 
H4B   N3   N  Y N 178 
H4B   C4   C  Y N 179 
H4B   O4   O  N N 180 
H4B   C4A  C  Y N 181 
H4B   C8A  C  Y N 182 
H4B   N5   N  N N 183 
H4B   N8   N  N N 184 
H4B   C6   C  N R 185 
H4B   C7   C  N N 186 
H4B   C9   C  N R 187 
H4B   O9   O  N N 188 
H4B   C10  C  N S 189 
H4B   C11  C  N N 190 
H4B   O10  O  N N 191 
H4B   HN21 H  N N 192 
H4B   HN22 H  N N 193 
H4B   HN3  H  N N 194 
H4B   HN5  H  N N 195 
H4B   HN8  H  N N 196 
H4B   H6   H  N N 197 
H4B   H71  H  N N 198 
H4B   H72  H  N N 199 
H4B   H9   H  N N 200 
H4B   HO9  H  N N 201 
H4B   H10  H  N N 202 
H4B   H111 H  N N 203 
H4B   H112 H  N N 204 
H4B   H113 H  N N 205 
H4B   HO0  H  N N 206 
HEM   CHA  C  N N 207 
HEM   CHB  C  N N 208 
HEM   CHC  C  N N 209 
HEM   CHD  C  N N 210 
HEM   C1A  C  Y N 211 
HEM   C2A  C  Y N 212 
HEM   C3A  C  Y N 213 
HEM   C4A  C  Y N 214 
HEM   CMA  C  N N 215 
HEM   CAA  C  N N 216 
HEM   CBA  C  N N 217 
HEM   CGA  C  N N 218 
HEM   O1A  O  N N 219 
HEM   O2A  O  N N 220 
HEM   C1B  C  N N 221 
HEM   C2B  C  N N 222 
HEM   C3B  C  N N 223 
HEM   C4B  C  N N 224 
HEM   CMB  C  N N 225 
HEM   CAB  C  N N 226 
HEM   CBB  C  N N 227 
HEM   C1C  C  Y N 228 
HEM   C2C  C  Y N 229 
HEM   C3C  C  Y N 230 
HEM   C4C  C  Y N 231 
HEM   CMC  C  N N 232 
HEM   CAC  C  N N 233 
HEM   CBC  C  N N 234 
HEM   C1D  C  N N 235 
HEM   C2D  C  N N 236 
HEM   C3D  C  N N 237 
HEM   C4D  C  N N 238 
HEM   CMD  C  N N 239 
HEM   CAD  C  N N 240 
HEM   CBD  C  N N 241 
HEM   CGD  C  N N 242 
HEM   O1D  O  N N 243 
HEM   O2D  O  N N 244 
HEM   NA   N  Y N 245 
HEM   NB   N  N N 246 
HEM   NC   N  Y N 247 
HEM   ND   N  N N 248 
HEM   FE   FE N N 249 
HEM   HHB  H  N N 250 
HEM   HHC  H  N N 251 
HEM   HHD  H  N N 252 
HEM   HMA  H  N N 253 
HEM   HMAA H  N N 254 
HEM   HMAB H  N N 255 
HEM   HAA  H  N N 256 
HEM   HAAA H  N N 257 
HEM   HBA  H  N N 258 
HEM   HBAA H  N N 259 
HEM   HMB  H  N N 260 
HEM   HMBA H  N N 261 
HEM   HMBB H  N N 262 
HEM   HAB  H  N N 263 
HEM   HBB  H  N N 264 
HEM   HBBA H  N N 265 
HEM   HMC  H  N N 266 
HEM   HMCA H  N N 267 
HEM   HMCB H  N N 268 
HEM   HAC  H  N N 269 
HEM   HBC  H  N N 270 
HEM   HBCA H  N N 271 
HEM   HMD  H  N N 272 
HEM   HMDA H  N N 273 
HEM   HMDB H  N N 274 
HEM   HAD  H  N N 275 
HEM   HADA H  N N 276 
HEM   HBD  H  N N 277 
HEM   HBDA H  N N 278 
HEM   H2A  H  N N 279 
HEM   H2D  H  N N 280 
HEM   HHA  H  N N 281 
HIS   N    N  N N 282 
HIS   CA   C  N S 283 
HIS   C    C  N N 284 
HIS   O    O  N N 285 
HIS   CB   C  N N 286 
HIS   CG   C  Y N 287 
HIS   ND1  N  Y N 288 
HIS   CD2  C  Y N 289 
HIS   CE1  C  Y N 290 
HIS   NE2  N  Y N 291 
HIS   OXT  O  N N 292 
HIS   H    H  N N 293 
HIS   H2   H  N N 294 
HIS   HA   H  N N 295 
HIS   HB2  H  N N 296 
HIS   HB3  H  N N 297 
HIS   HD1  H  N N 298 
HIS   HD2  H  N N 299 
HIS   HE1  H  N N 300 
HIS   HE2  H  N N 301 
HIS   HXT  H  N N 302 
HOH   O    O  N N 303 
HOH   H1   H  N N 304 
HOH   H2   H  N N 305 
ILE   N    N  N N 306 
ILE   CA   C  N S 307 
ILE   C    C  N N 308 
ILE   O    O  N N 309 
ILE   CB   C  N S 310 
ILE   CG1  C  N N 311 
ILE   CG2  C  N N 312 
ILE   CD1  C  N N 313 
ILE   OXT  O  N N 314 
ILE   H    H  N N 315 
ILE   H2   H  N N 316 
ILE   HA   H  N N 317 
ILE   HB   H  N N 318 
ILE   HG12 H  N N 319 
ILE   HG13 H  N N 320 
ILE   HG21 H  N N 321 
ILE   HG22 H  N N 322 
ILE   HG23 H  N N 323 
ILE   HD11 H  N N 324 
ILE   HD12 H  N N 325 
ILE   HD13 H  N N 326 
ILE   HXT  H  N N 327 
LEU   N    N  N N 328 
LEU   CA   C  N S 329 
LEU   C    C  N N 330 
LEU   O    O  N N 331 
LEU   CB   C  N N 332 
LEU   CG   C  N N 333 
LEU   CD1  C  N N 334 
LEU   CD2  C  N N 335 
LEU   OXT  O  N N 336 
LEU   H    H  N N 337 
LEU   H2   H  N N 338 
LEU   HA   H  N N 339 
LEU   HB2  H  N N 340 
LEU   HB3  H  N N 341 
LEU   HG   H  N N 342 
LEU   HD11 H  N N 343 
LEU   HD12 H  N N 344 
LEU   HD13 H  N N 345 
LEU   HD21 H  N N 346 
LEU   HD22 H  N N 347 
LEU   HD23 H  N N 348 
LEU   HXT  H  N N 349 
LYS   N    N  N N 350 
LYS   CA   C  N S 351 
LYS   C    C  N N 352 
LYS   O    O  N N 353 
LYS   CB   C  N N 354 
LYS   CG   C  N N 355 
LYS   CD   C  N N 356 
LYS   CE   C  N N 357 
LYS   NZ   N  N N 358 
LYS   OXT  O  N N 359 
LYS   H    H  N N 360 
LYS   H2   H  N N 361 
LYS   HA   H  N N 362 
LYS   HB2  H  N N 363 
LYS   HB3  H  N N 364 
LYS   HG2  H  N N 365 
LYS   HG3  H  N N 366 
LYS   HD2  H  N N 367 
LYS   HD3  H  N N 368 
LYS   HE2  H  N N 369 
LYS   HE3  H  N N 370 
LYS   HZ1  H  N N 371 
LYS   HZ2  H  N N 372 
LYS   HZ3  H  N N 373 
LYS   HXT  H  N N 374 
MET   N    N  N N 375 
MET   CA   C  N S 376 
MET   C    C  N N 377 
MET   O    O  N N 378 
MET   CB   C  N N 379 
MET   CG   C  N N 380 
MET   SD   S  N N 381 
MET   CE   C  N N 382 
MET   OXT  O  N N 383 
MET   H    H  N N 384 
MET   H2   H  N N 385 
MET   HA   H  N N 386 
MET   HB2  H  N N 387 
MET   HB3  H  N N 388 
MET   HG2  H  N N 389 
MET   HG3  H  N N 390 
MET   HE1  H  N N 391 
MET   HE2  H  N N 392 
MET   HE3  H  N N 393 
MET   HXT  H  N N 394 
PHE   N    N  N N 395 
PHE   CA   C  N S 396 
PHE   C    C  N N 397 
PHE   O    O  N N 398 
PHE   CB   C  N N 399 
PHE   CG   C  Y N 400 
PHE   CD1  C  Y N 401 
PHE   CD2  C  Y N 402 
PHE   CE1  C  Y N 403 
PHE   CE2  C  Y N 404 
PHE   CZ   C  Y N 405 
PHE   OXT  O  N N 406 
PHE   H    H  N N 407 
PHE   H2   H  N N 408 
PHE   HA   H  N N 409 
PHE   HB2  H  N N 410 
PHE   HB3  H  N N 411 
PHE   HD1  H  N N 412 
PHE   HD2  H  N N 413 
PHE   HE1  H  N N 414 
PHE   HE2  H  N N 415 
PHE   HZ   H  N N 416 
PHE   HXT  H  N N 417 
PRO   N    N  N N 418 
PRO   CA   C  N S 419 
PRO   C    C  N N 420 
PRO   O    O  N N 421 
PRO   CB   C  N N 422 
PRO   CG   C  N N 423 
PRO   CD   C  N N 424 
PRO   OXT  O  N N 425 
PRO   H    H  N N 426 
PRO   HA   H  N N 427 
PRO   HB2  H  N N 428 
PRO   HB3  H  N N 429 
PRO   HG2  H  N N 430 
PRO   HG3  H  N N 431 
PRO   HD2  H  N N 432 
PRO   HD3  H  N N 433 
PRO   HXT  H  N N 434 
SER   N    N  N N 435 
SER   CA   C  N S 436 
SER   C    C  N N 437 
SER   O    O  N N 438 
SER   CB   C  N N 439 
SER   OG   O  N N 440 
SER   OXT  O  N N 441 
SER   H    H  N N 442 
SER   H2   H  N N 443 
SER   HA   H  N N 444 
SER   HB2  H  N N 445 
SER   HB3  H  N N 446 
SER   HG   H  N N 447 
SER   HXT  H  N N 448 
THR   N    N  N N 449 
THR   CA   C  N S 450 
THR   C    C  N N 451 
THR   O    O  N N 452 
THR   CB   C  N R 453 
THR   OG1  O  N N 454 
THR   CG2  C  N N 455 
THR   OXT  O  N N 456 
THR   H    H  N N 457 
THR   H2   H  N N 458 
THR   HA   H  N N 459 
THR   HB   H  N N 460 
THR   HG1  H  N N 461 
THR   HG21 H  N N 462 
THR   HG22 H  N N 463 
THR   HG23 H  N N 464 
THR   HXT  H  N N 465 
TRP   N    N  N N 466 
TRP   CA   C  N S 467 
TRP   C    C  N N 468 
TRP   O    O  N N 469 
TRP   CB   C  N N 470 
TRP   CG   C  Y N 471 
TRP   CD1  C  Y N 472 
TRP   CD2  C  Y N 473 
TRP   NE1  N  Y N 474 
TRP   CE2  C  Y N 475 
TRP   CE3  C  Y N 476 
TRP   CZ2  C  Y N 477 
TRP   CZ3  C  Y N 478 
TRP   CH2  C  Y N 479 
TRP   OXT  O  N N 480 
TRP   H    H  N N 481 
TRP   H2   H  N N 482 
TRP   HA   H  N N 483 
TRP   HB2  H  N N 484 
TRP   HB3  H  N N 485 
TRP   HD1  H  N N 486 
TRP   HE1  H  N N 487 
TRP   HE3  H  N N 488 
TRP   HZ2  H  N N 489 
TRP   HZ3  H  N N 490 
TRP   HH2  H  N N 491 
TRP   HXT  H  N N 492 
TYR   N    N  N N 493 
TYR   CA   C  N S 494 
TYR   C    C  N N 495 
TYR   O    O  N N 496 
TYR   CB   C  N N 497 
TYR   CG   C  Y N 498 
TYR   CD1  C  Y N 499 
TYR   CD2  C  Y N 500 
TYR   CE1  C  Y N 501 
TYR   CE2  C  Y N 502 
TYR   CZ   C  Y N 503 
TYR   OH   O  N N 504 
TYR   OXT  O  N N 505 
TYR   H    H  N N 506 
TYR   H2   H  N N 507 
TYR   HA   H  N N 508 
TYR   HB2  H  N N 509 
TYR   HB3  H  N N 510 
TYR   HD1  H  N N 511 
TYR   HD2  H  N N 512 
TYR   HE1  H  N N 513 
TYR   HE2  H  N N 514 
TYR   HH   H  N N 515 
TYR   HXT  H  N N 516 
VAL   N    N  N N 517 
VAL   CA   C  N S 518 
VAL   C    C  N N 519 
VAL   O    O  N N 520 
VAL   CB   C  N N 521 
VAL   CG1  C  N N 522 
VAL   CG2  C  N N 523 
VAL   OXT  O  N N 524 
VAL   H    H  N N 525 
VAL   H2   H  N N 526 
VAL   HA   H  N N 527 
VAL   HB   H  N N 528 
VAL   HG11 H  N N 529 
VAL   HG12 H  N N 530 
VAL   HG13 H  N N 531 
VAL   HG21 H  N N 532 
VAL   HG22 H  N N 533 
VAL   HG23 H  N N 534 
VAL   HXT  H  N N 535 
ZN    ZN   ZN N N 536 
# 
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 
A1A0D C07 C04  sing N N 1   
A1A0D C04 C03  doub Y N 2   
A1A0D C04 C05  sing Y N 3   
A1A0D C03 C02  sing Y N 4   
A1A0D C05 C06  doub Y N 5   
A1A0D C02 N01  doub Y N 6   
A1A0D C02 N02  sing N N 7   
A1A0D F12 C12  sing N N 8   
A1A0D C06 N01  sing Y N 9   
A1A0D C06 C11  sing N N 10  
A1A0D F23 C20  sing N N 11  
A1A0D C12 C11  doub Y N 12  
A1A0D C12 C13  sing Y N 13  
A1A0D C11 C16  sing Y N 14  
A1A0D F13 C13  sing N N 15  
A1A0D C13 C14  doub Y N 16  
A1A0D C16 C15  doub Y N 17  
A1A0D N18 C19  sing N N 18  
A1A0D N18 C21  sing N N 19  
A1A0D N18 C17  sing N N 20  
A1A0D C19 C20  sing N N 21  
A1A0D C14 C15  sing Y N 22  
A1A0D C15 C17  sing N N 23  
A1A0D C21 C20  sing N N 24  
A1A0D C20 F22  sing N N 25  
A1A0D C16 H1   sing N N 26  
A1A0D C17 H2   sing N N 27  
A1A0D C17 H3   sing N N 28  
A1A0D C19 H4   sing N N 29  
A1A0D C19 H5   sing N N 30  
A1A0D C21 H6   sing N N 31  
A1A0D C21 H7   sing N N 32  
A1A0D C03 H8   sing N N 33  
A1A0D C05 H9   sing N N 34  
A1A0D C07 H10  sing N N 35  
A1A0D C07 H11  sing N N 36  
A1A0D C07 H12  sing N N 37  
A1A0D C14 H13  sing N N 38  
A1A0D N02 H14  sing N N 39  
A1A0D N02 H15  sing N N 40  
ALA   N   CA   sing N N 41  
ALA   N   H    sing N N 42  
ALA   N   H2   sing N N 43  
ALA   CA  C    sing N N 44  
ALA   CA  CB   sing N N 45  
ALA   CA  HA   sing N N 46  
ALA   C   O    doub N N 47  
ALA   C   OXT  sing N N 48  
ALA   CB  HB1  sing N N 49  
ALA   CB  HB2  sing N N 50  
ALA   CB  HB3  sing N N 51  
ALA   OXT HXT  sing N N 52  
ARG   N   CA   sing N N 53  
ARG   N   H    sing N N 54  
ARG   N   H2   sing N N 55  
ARG   CA  C    sing N N 56  
ARG   CA  CB   sing N N 57  
ARG   CA  HA   sing N N 58  
ARG   C   O    doub N N 59  
ARG   C   OXT  sing N N 60  
ARG   CB  CG   sing N N 61  
ARG   CB  HB2  sing N N 62  
ARG   CB  HB3  sing N N 63  
ARG   CG  CD   sing N N 64  
ARG   CG  HG2  sing N N 65  
ARG   CG  HG3  sing N N 66  
ARG   CD  NE   sing N N 67  
ARG   CD  HD2  sing N N 68  
ARG   CD  HD3  sing N N 69  
ARG   NE  CZ   sing N N 70  
ARG   NE  HE   sing N N 71  
ARG   CZ  NH1  sing N N 72  
ARG   CZ  NH2  doub N N 73  
ARG   NH1 HH11 sing N N 74  
ARG   NH1 HH12 sing N N 75  
ARG   NH2 HH21 sing N N 76  
ARG   NH2 HH22 sing N N 77  
ARG   OXT HXT  sing N N 78  
ASN   N   CA   sing N N 79  
ASN   N   H    sing N N 80  
ASN   N   H2   sing N N 81  
ASN   CA  C    sing N N 82  
ASN   CA  CB   sing N N 83  
ASN   CA  HA   sing N N 84  
ASN   C   O    doub N N 85  
ASN   C   OXT  sing N N 86  
ASN   CB  CG   sing N N 87  
ASN   CB  HB2  sing N N 88  
ASN   CB  HB3  sing N N 89  
ASN   CG  OD1  doub N N 90  
ASN   CG  ND2  sing N N 91  
ASN   ND2 HD21 sing N N 92  
ASN   ND2 HD22 sing N N 93  
ASN   OXT HXT  sing N N 94  
ASP   N   CA   sing N N 95  
ASP   N   H    sing N N 96  
ASP   N   H2   sing N N 97  
ASP   CA  C    sing N N 98  
ASP   CA  CB   sing N N 99  
ASP   CA  HA   sing N N 100 
ASP   C   O    doub N N 101 
ASP   C   OXT  sing N N 102 
ASP   CB  CG   sing N N 103 
ASP   CB  HB2  sing N N 104 
ASP   CB  HB3  sing N N 105 
ASP   CG  OD1  doub N N 106 
ASP   CG  OD2  sing N N 107 
ASP   OD2 HD2  sing N N 108 
ASP   OXT HXT  sing N N 109 
CYS   N   CA   sing N N 110 
CYS   N   H    sing N N 111 
CYS   N   H2   sing N N 112 
CYS   CA  C    sing N N 113 
CYS   CA  CB   sing N N 114 
CYS   CA  HA   sing N N 115 
CYS   C   O    doub N N 116 
CYS   C   OXT  sing N N 117 
CYS   CB  SG   sing N N 118 
CYS   CB  HB2  sing N N 119 
CYS   CB  HB3  sing N N 120 
CYS   SG  HG   sing N N 121 
CYS   OXT HXT  sing N N 122 
GLN   N   CA   sing N N 123 
GLN   N   H    sing N N 124 
GLN   N   H2   sing N N 125 
GLN   CA  C    sing N N 126 
GLN   CA  CB   sing N N 127 
GLN   CA  HA   sing N N 128 
GLN   C   O    doub N N 129 
GLN   C   OXT  sing N N 130 
GLN   CB  CG   sing N N 131 
GLN   CB  HB2  sing N N 132 
GLN   CB  HB3  sing N N 133 
GLN   CG  CD   sing N N 134 
GLN   CG  HG2  sing N N 135 
GLN   CG  HG3  sing N N 136 
GLN   CD  OE1  doub N N 137 
GLN   CD  NE2  sing N N 138 
GLN   NE2 HE21 sing N N 139 
GLN   NE2 HE22 sing N N 140 
GLN   OXT HXT  sing N N 141 
GLU   N   CA   sing N N 142 
GLU   N   H    sing N N 143 
GLU   N   H2   sing N N 144 
GLU   CA  C    sing N N 145 
GLU   CA  CB   sing N N 146 
GLU   CA  HA   sing N N 147 
GLU   C   O    doub N N 148 
GLU   C   OXT  sing N N 149 
GLU   CB  CG   sing N N 150 
GLU   CB  HB2  sing N N 151 
GLU   CB  HB3  sing N N 152 
GLU   CG  CD   sing N N 153 
GLU   CG  HG2  sing N N 154 
GLU   CG  HG3  sing N N 155 
GLU   CD  OE1  doub N N 156 
GLU   CD  OE2  sing N N 157 
GLU   OE2 HE2  sing N N 158 
GLU   OXT HXT  sing N N 159 
GLY   N   CA   sing N N 160 
GLY   N   H    sing N N 161 
GLY   N   H2   sing N N 162 
GLY   CA  C    sing N N 163 
GLY   CA  HA2  sing N N 164 
GLY   CA  HA3  sing N N 165 
GLY   C   O    doub N N 166 
GLY   C   OXT  sing N N 167 
GLY   OXT HXT  sing N N 168 
H4B   N1  C2   doub Y N 169 
H4B   N1  C8A  sing Y N 170 
H4B   C2  N2   sing N N 171 
H4B   C2  N3   sing Y N 172 
H4B   N2  HN21 sing N N 173 
H4B   N2  HN22 sing N N 174 
H4B   N3  C4   sing Y N 175 
H4B   N3  HN3  sing N N 176 
H4B   C4  O4   doub N N 177 
H4B   C4  C4A  sing Y N 178 
H4B   C4A C8A  doub Y N 179 
H4B   C4A N5   sing N N 180 
H4B   C8A N8   sing N N 181 
H4B   N5  C6   sing N N 182 
H4B   N5  HN5  sing N N 183 
H4B   N8  C7   sing N N 184 
H4B   N8  HN8  sing N N 185 
H4B   C6  C7   sing N N 186 
H4B   C6  C9   sing N N 187 
H4B   C6  H6   sing N N 188 
H4B   C7  H71  sing N N 189 
H4B   C7  H72  sing N N 190 
H4B   C9  O9   sing N N 191 
H4B   C9  C10  sing N N 192 
H4B   C9  H9   sing N N 193 
H4B   O9  HO9  sing N N 194 
H4B   C10 C11  sing N N 195 
H4B   C10 O10  sing N N 196 
H4B   C10 H10  sing N N 197 
H4B   C11 H111 sing N N 198 
H4B   C11 H112 sing N N 199 
H4B   C11 H113 sing N N 200 
H4B   O10 HO0  sing N N 201 
HEM   CHA C1A  sing N N 202 
HEM   CHA C4D  doub N N 203 
HEM   CHA HHA  sing N N 204 
HEM   CHB C4A  sing N N 205 
HEM   CHB C1B  doub N N 206 
HEM   CHB HHB  sing N N 207 
HEM   CHC C4B  sing N N 208 
HEM   CHC C1C  doub N N 209 
HEM   CHC HHC  sing N N 210 
HEM   CHD C4C  doub N N 211 
HEM   CHD C1D  sing N N 212 
HEM   CHD HHD  sing N N 213 
HEM   C1A C2A  doub Y N 214 
HEM   C1A NA   sing Y N 215 
HEM   C2A C3A  sing Y N 216 
HEM   C2A CAA  sing N N 217 
HEM   C3A C4A  doub Y N 218 
HEM   C3A CMA  sing N N 219 
HEM   C4A NA   sing Y N 220 
HEM   CMA HMA  sing N N 221 
HEM   CMA HMAA sing N N 222 
HEM   CMA HMAB sing N N 223 
HEM   CAA CBA  sing N N 224 
HEM   CAA HAA  sing N N 225 
HEM   CAA HAAA sing N N 226 
HEM   CBA CGA  sing N N 227 
HEM   CBA HBA  sing N N 228 
HEM   CBA HBAA sing N N 229 
HEM   CGA O1A  doub N N 230 
HEM   CGA O2A  sing N N 231 
HEM   C1B C2B  sing N N 232 
HEM   C1B NB   sing N N 233 
HEM   C2B C3B  doub N N 234 
HEM   C2B CMB  sing N N 235 
HEM   C3B C4B  sing N N 236 
HEM   C3B CAB  sing N N 237 
HEM   C4B NB   doub N N 238 
HEM   CMB HMB  sing N N 239 
HEM   CMB HMBA sing N N 240 
HEM   CMB HMBB sing N N 241 
HEM   CAB CBB  doub N N 242 
HEM   CAB HAB  sing N N 243 
HEM   CBB HBB  sing N N 244 
HEM   CBB HBBA sing N N 245 
HEM   C1C C2C  sing Y N 246 
HEM   C1C NC   sing Y N 247 
HEM   C2C C3C  doub Y N 248 
HEM   C2C CMC  sing N N 249 
HEM   C3C C4C  sing Y N 250 
HEM   C3C CAC  sing N N 251 
HEM   C4C NC   sing Y N 252 
HEM   CMC HMC  sing N N 253 
HEM   CMC HMCA sing N N 254 
HEM   CMC HMCB sing N N 255 
HEM   CAC CBC  doub N N 256 
HEM   CAC HAC  sing N N 257 
HEM   CBC HBC  sing N N 258 
HEM   CBC HBCA sing N N 259 
HEM   C1D C2D  sing N N 260 
HEM   C1D ND   doub N N 261 
HEM   C2D C3D  doub N N 262 
HEM   C2D CMD  sing N N 263 
HEM   C3D C4D  sing N N 264 
HEM   C3D CAD  sing N N 265 
HEM   C4D ND   sing N N 266 
HEM   CMD HMD  sing N N 267 
HEM   CMD HMDA sing N N 268 
HEM   CMD HMDB sing N N 269 
HEM   CAD CBD  sing N N 270 
HEM   CAD HAD  sing N N 271 
HEM   CAD HADA sing N N 272 
HEM   CBD CGD  sing N N 273 
HEM   CBD HBD  sing N N 274 
HEM   CBD HBDA sing N N 275 
HEM   CGD O1D  doub N N 276 
HEM   CGD O2D  sing N N 277 
HEM   O2A H2A  sing N N 278 
HEM   O2D H2D  sing N N 279 
HEM   FE  NA   sing N N 280 
HEM   FE  NB   sing N N 281 
HEM   FE  NC   sing N N 282 
HEM   FE  ND   sing N N 283 
HIS   N   CA   sing N N 284 
HIS   N   H    sing N N 285 
HIS   N   H2   sing N N 286 
HIS   CA  C    sing N N 287 
HIS   CA  CB   sing N N 288 
HIS   CA  HA   sing N N 289 
HIS   C   O    doub N N 290 
HIS   C   OXT  sing N N 291 
HIS   CB  CG   sing N N 292 
HIS   CB  HB2  sing N N 293 
HIS   CB  HB3  sing N N 294 
HIS   CG  ND1  sing Y N 295 
HIS   CG  CD2  doub Y N 296 
HIS   ND1 CE1  doub Y N 297 
HIS   ND1 HD1  sing N N 298 
HIS   CD2 NE2  sing Y N 299 
HIS   CD2 HD2  sing N N 300 
HIS   CE1 NE2  sing Y N 301 
HIS   CE1 HE1  sing N N 302 
HIS   NE2 HE2  sing N N 303 
HIS   OXT HXT  sing N N 304 
HOH   O   H1   sing N N 305 
HOH   O   H2   sing N N 306 
ILE   N   CA   sing N N 307 
ILE   N   H    sing N N 308 
ILE   N   H2   sing N N 309 
ILE   CA  C    sing N N 310 
ILE   CA  CB   sing N N 311 
ILE   CA  HA   sing N N 312 
ILE   C   O    doub N N 313 
ILE   C   OXT  sing N N 314 
ILE   CB  CG1  sing N N 315 
ILE   CB  CG2  sing N N 316 
ILE   CB  HB   sing N N 317 
ILE   CG1 CD1  sing N N 318 
ILE   CG1 HG12 sing N N 319 
ILE   CG1 HG13 sing N N 320 
ILE   CG2 HG21 sing N N 321 
ILE   CG2 HG22 sing N N 322 
ILE   CG2 HG23 sing N N 323 
ILE   CD1 HD11 sing N N 324 
ILE   CD1 HD12 sing N N 325 
ILE   CD1 HD13 sing N N 326 
ILE   OXT HXT  sing N N 327 
LEU   N   CA   sing N N 328 
LEU   N   H    sing N N 329 
LEU   N   H2   sing N N 330 
LEU   CA  C    sing N N 331 
LEU   CA  CB   sing N N 332 
LEU   CA  HA   sing N N 333 
LEU   C   O    doub N N 334 
LEU   C   OXT  sing N N 335 
LEU   CB  CG   sing N N 336 
LEU   CB  HB2  sing N N 337 
LEU   CB  HB3  sing N N 338 
LEU   CG  CD1  sing N N 339 
LEU   CG  CD2  sing N N 340 
LEU   CG  HG   sing N N 341 
LEU   CD1 HD11 sing N N 342 
LEU   CD1 HD12 sing N N 343 
LEU   CD1 HD13 sing N N 344 
LEU   CD2 HD21 sing N N 345 
LEU   CD2 HD22 sing N N 346 
LEU   CD2 HD23 sing N N 347 
LEU   OXT HXT  sing N N 348 
LYS   N   CA   sing N N 349 
LYS   N   H    sing N N 350 
LYS   N   H2   sing N N 351 
LYS   CA  C    sing N N 352 
LYS   CA  CB   sing N N 353 
LYS   CA  HA   sing N N 354 
LYS   C   O    doub N N 355 
LYS   C   OXT  sing N N 356 
LYS   CB  CG   sing N N 357 
LYS   CB  HB2  sing N N 358 
LYS   CB  HB3  sing N N 359 
LYS   CG  CD   sing N N 360 
LYS   CG  HG2  sing N N 361 
LYS   CG  HG3  sing N N 362 
LYS   CD  CE   sing N N 363 
LYS   CD  HD2  sing N N 364 
LYS   CD  HD3  sing N N 365 
LYS   CE  NZ   sing N N 366 
LYS   CE  HE2  sing N N 367 
LYS   CE  HE3  sing N N 368 
LYS   NZ  HZ1  sing N N 369 
LYS   NZ  HZ2  sing N N 370 
LYS   NZ  HZ3  sing N N 371 
LYS   OXT HXT  sing N N 372 
MET   N   CA   sing N N 373 
MET   N   H    sing N N 374 
MET   N   H2   sing N N 375 
MET   CA  C    sing N N 376 
MET   CA  CB   sing N N 377 
MET   CA  HA   sing N N 378 
MET   C   O    doub N N 379 
MET   C   OXT  sing N N 380 
MET   CB  CG   sing N N 381 
MET   CB  HB2  sing N N 382 
MET   CB  HB3  sing N N 383 
MET   CG  SD   sing N N 384 
MET   CG  HG2  sing N N 385 
MET   CG  HG3  sing N N 386 
MET   SD  CE   sing N N 387 
MET   CE  HE1  sing N N 388 
MET   CE  HE2  sing N N 389 
MET   CE  HE3  sing N N 390 
MET   OXT HXT  sing N N 391 
PHE   N   CA   sing N N 392 
PHE   N   H    sing N N 393 
PHE   N   H2   sing N N 394 
PHE   CA  C    sing N N 395 
PHE   CA  CB   sing N N 396 
PHE   CA  HA   sing N N 397 
PHE   C   O    doub N N 398 
PHE   C   OXT  sing N N 399 
PHE   CB  CG   sing N N 400 
PHE   CB  HB2  sing N N 401 
PHE   CB  HB3  sing N N 402 
PHE   CG  CD1  doub Y N 403 
PHE   CG  CD2  sing Y N 404 
PHE   CD1 CE1  sing Y N 405 
PHE   CD1 HD1  sing N N 406 
PHE   CD2 CE2  doub Y N 407 
PHE   CD2 HD2  sing N N 408 
PHE   CE1 CZ   doub Y N 409 
PHE   CE1 HE1  sing N N 410 
PHE   CE2 CZ   sing Y N 411 
PHE   CE2 HE2  sing N N 412 
PHE   CZ  HZ   sing N N 413 
PHE   OXT HXT  sing N N 414 
PRO   N   CA   sing N N 415 
PRO   N   CD   sing N N 416 
PRO   N   H    sing N N 417 
PRO   CA  C    sing N N 418 
PRO   CA  CB   sing N N 419 
PRO   CA  HA   sing N N 420 
PRO   C   O    doub N N 421 
PRO   C   OXT  sing N N 422 
PRO   CB  CG   sing N N 423 
PRO   CB  HB2  sing N N 424 
PRO   CB  HB3  sing N N 425 
PRO   CG  CD   sing N N 426 
PRO   CG  HG2  sing N N 427 
PRO   CG  HG3  sing N N 428 
PRO   CD  HD2  sing N N 429 
PRO   CD  HD3  sing N N 430 
PRO   OXT HXT  sing N N 431 
SER   N   CA   sing N N 432 
SER   N   H    sing N N 433 
SER   N   H2   sing N N 434 
SER   CA  C    sing N N 435 
SER   CA  CB   sing N N 436 
SER   CA  HA   sing N N 437 
SER   C   O    doub N N 438 
SER   C   OXT  sing N N 439 
SER   CB  OG   sing N N 440 
SER   CB  HB2  sing N N 441 
SER   CB  HB3  sing N N 442 
SER   OG  HG   sing N N 443 
SER   OXT HXT  sing N N 444 
THR   N   CA   sing N N 445 
THR   N   H    sing N N 446 
THR   N   H2   sing N N 447 
THR   CA  C    sing N N 448 
THR   CA  CB   sing N N 449 
THR   CA  HA   sing N N 450 
THR   C   O    doub N N 451 
THR   C   OXT  sing N N 452 
THR   CB  OG1  sing N N 453 
THR   CB  CG2  sing N N 454 
THR   CB  HB   sing N N 455 
THR   OG1 HG1  sing N N 456 
THR   CG2 HG21 sing N N 457 
THR   CG2 HG22 sing N N 458 
THR   CG2 HG23 sing N N 459 
THR   OXT HXT  sing N N 460 
TRP   N   CA   sing N N 461 
TRP   N   H    sing N N 462 
TRP   N   H2   sing N N 463 
TRP   CA  C    sing N N 464 
TRP   CA  CB   sing N N 465 
TRP   CA  HA   sing N N 466 
TRP   C   O    doub N N 467 
TRP   C   OXT  sing N N 468 
TRP   CB  CG   sing N N 469 
TRP   CB  HB2  sing N N 470 
TRP   CB  HB3  sing N N 471 
TRP   CG  CD1  doub Y N 472 
TRP   CG  CD2  sing Y N 473 
TRP   CD1 NE1  sing Y N 474 
TRP   CD1 HD1  sing N N 475 
TRP   CD2 CE2  doub Y N 476 
TRP   CD2 CE3  sing Y N 477 
TRP   NE1 CE2  sing Y N 478 
TRP   NE1 HE1  sing N N 479 
TRP   CE2 CZ2  sing Y N 480 
TRP   CE3 CZ3  doub Y N 481 
TRP   CE3 HE3  sing N N 482 
TRP   CZ2 CH2  doub Y N 483 
TRP   CZ2 HZ2  sing N N 484 
TRP   CZ3 CH2  sing Y N 485 
TRP   CZ3 HZ3  sing N N 486 
TRP   CH2 HH2  sing N N 487 
TRP   OXT HXT  sing N N 488 
TYR   N   CA   sing N N 489 
TYR   N   H    sing N N 490 
TYR   N   H2   sing N N 491 
TYR   CA  C    sing N N 492 
TYR   CA  CB   sing N N 493 
TYR   CA  HA   sing N N 494 
TYR   C   O    doub N N 495 
TYR   C   OXT  sing N N 496 
TYR   CB  CG   sing N N 497 
TYR   CB  HB2  sing N N 498 
TYR   CB  HB3  sing N N 499 
TYR   CG  CD1  doub Y N 500 
TYR   CG  CD2  sing Y N 501 
TYR   CD1 CE1  sing Y N 502 
TYR   CD1 HD1  sing N N 503 
TYR   CD2 CE2  doub Y N 504 
TYR   CD2 HD2  sing N N 505 
TYR   CE1 CZ   doub Y N 506 
TYR   CE1 HE1  sing N N 507 
TYR   CE2 CZ   sing Y N 508 
TYR   CE2 HE2  sing N N 509 
TYR   CZ  OH   sing N N 510 
TYR   OH  HH   sing N N 511 
TYR   OXT HXT  sing N N 512 
VAL   N   CA   sing N N 513 
VAL   N   H    sing N N 514 
VAL   N   H2   sing N N 515 
VAL   CA  C    sing N N 516 
VAL   CA  CB   sing N N 517 
VAL   CA  HA   sing N N 518 
VAL   C   O    doub N N 519 
VAL   C   OXT  sing N N 520 
VAL   CB  CG1  sing N N 521 
VAL   CB  CG2  sing N N 522 
VAL   CB  HB   sing N N 523 
VAL   CG1 HG11 sing N N 524 
VAL   CG1 HG12 sing N N 525 
VAL   CG1 HG13 sing N N 526 
VAL   CG2 HG21 sing N N 527 
VAL   CG2 HG22 sing N N 528 
VAL   CG2 HG23 sing N N 529 
VAL   OXT HXT  sing N N 530 
# 
_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                    9CVQ 
_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]   0.020560 
_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]   0.008836 
_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]   0.006126 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
_atom_sites.solution_primary            ? 
_atom_sites.solution_secondary          ? 
_atom_sites.solution_hydrogens          ? 
_atom_sites.special_details             ? 
# 
loop_
_atom_type.symbol 
C  
F  
FE 
N  
O  
S  
ZN 
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N  N   . ARG   A 1 3   ? -38.165 -24.725 41.491 1.00 150.15 ? 299 ARG   A N   1 
ATOM   2    C  CA  . ARG   A 1 3   ? -37.979 -24.948 40.061 1.00 152.82 ? 299 ARG   A CA  1 
ATOM   3    C  C   . ARG   A 1 3   ? -38.953 -24.109 39.246 1.00 144.83 ? 299 ARG   A C   1 
ATOM   4    O  O   . ARG   A 1 3   ? -39.169 -24.357 38.058 1.00 147.67 ? 299 ARG   A O   1 
ATOM   5    C  CB  . ARG   A 1 3   ? -38.156 -26.425 39.724 1.00 160.36 ? 299 ARG   A CB  1 
ATOM   6    C  CG  . ARG   A 1 3   ? -37.166 -26.954 38.701 1.00 160.95 ? 299 ARG   A CG  1 
ATOM   7    C  CD  . ARG   A 1 3   ? -35.732 -26.754 39.172 1.00 163.82 ? 299 ARG   A CD  1 
ATOM   8    N  NE  . ARG   A 1 3   ? -35.019 -25.774 38.362 1.00 152.68 ? 299 ARG   A NE  1 
ATOM   9    C  CZ  . ARG   A 1 3   ? -34.357 -26.066 37.251 1.00 153.64 ? 299 ARG   A CZ  1 
ATOM   10   N  NH1 . ARG   A 1 3   ? -34.295 -27.306 36.790 1.00 157.54 ? 299 ARG   A NH1 1 
ATOM   11   N  NH2 . ARG   A 1 3   ? -33.745 -25.091 36.583 1.00 144.99 ? 299 ARG   A NH2 1 
ATOM   12   N  N   . PHE   A 1 4   ? -39.556 -23.121 39.909 1.00 126.63 ? 300 PHE   A N   1 
ATOM   13   C  CA  . PHE   A 1 4   ? -40.486 -22.154 39.339 1.00 118.07 ? 300 PHE   A CA  1 
ATOM   14   C  C   . PHE   A 1 4   ? -40.262 -20.865 40.137 1.00 112.91 ? 300 PHE   A C   1 
ATOM   15   O  O   . PHE   A 1 4   ? -41.099 -20.426 40.932 1.00 111.07 ? 300 PHE   A O   1 
ATOM   16   C  CB  . PHE   A 1 4   ? -41.938 -22.634 39.416 1.00 121.38 ? 300 PHE   A CB  1 
ATOM   17   C  CG  . PHE   A 1 4   ? -42.082 -24.130 39.539 1.00 129.43 ? 300 PHE   A CG  1 
ATOM   18   C  CD1 . PHE   A 1 4   ? -42.102 -24.736 40.788 1.00 129.47 ? 300 PHE   A CD1 1 
ATOM   19   C  CD2 . PHE   A 1 4   ? -42.198 -24.931 38.410 1.00 128.27 ? 300 PHE   A CD2 1 
ATOM   20   C  CE1 . PHE   A 1 4   ? -42.235 -26.112 40.909 1.00 130.95 ? 300 PHE   A CE1 1 
ATOM   21   C  CE2 . PHE   A 1 4   ? -42.332 -26.306 38.527 1.00 130.60 ? 300 PHE   A CE2 1 
ATOM   22   C  CZ  . PHE   A 1 4   ? -42.353 -26.897 39.782 1.00 131.77 ? 300 PHE   A CZ  1 
ATOM   23   N  N   . LEU   A 1 5   ? -39.103 -20.246 39.906 1.00 105.75 ? 301 LEU   A N   1 
ATOM   24   C  CA  . LEU   A 1 5   ? -38.489 -19.304 40.835 1.00 98.90  ? 301 LEU   A CA  1 
ATOM   25   C  C   . LEU   A 1 5   ? -39.149 -17.929 40.784 1.00 95.01  ? 301 LEU   A C   1 
ATOM   26   O  O   . LEU   A 1 5   ? -39.700 -17.502 39.765 1.00 93.54  ? 301 LEU   A O   1 
ATOM   27   C  CB  . LEU   A 1 5   ? -36.996 -19.166 40.537 1.00 93.87  ? 301 LEU   A CB  1 
ATOM   28   C  CG  . LEU   A 1 5   ? -36.196 -20.463 40.692 1.00 99.10  ? 301 LEU   A CG  1 
ATOM   29   C  CD1 . LEU   A 1 5   ? -34.990 -20.456 39.784 1.00 90.17  ? 301 LEU   A CD1 1 
ATOM   30   C  CD2 . LEU   A 1 5   ? -35.780 -20.660 42.131 1.00 95.74  ? 301 LEU   A CD2 1 
ATOM   31   N  N   . LYS   A 1 6   ? -39.058 -17.225 41.910 1.00 93.92  ? 302 LYS   A N   1 
ATOM   32   C  CA  . LYS   A 1 6   ? -39.642 -15.905 42.093 1.00 91.38  ? 302 LYS   A CA  1 
ATOM   33   C  C   . LYS   A 1 6   ? -38.554 -14.843 42.174 1.00 86.66  ? 302 LYS   A C   1 
ATOM   34   O  O   . LYS   A 1 6   ? -37.551 -15.020 42.873 1.00 83.37  ? 302 LYS   A O   1 
ATOM   35   C  CB  . LYS   A 1 6   ? -40.476 -15.846 43.374 1.00 90.90  ? 302 LYS   A CB  1 
ATOM   36   C  CG  . LYS   A 1 6   ? -41.556 -16.898 43.489 1.00 96.77  ? 302 LYS   A CG  1 
ATOM   37   C  CD  . LYS   A 1 6   ? -42.749 -16.537 42.629 1.00 96.06  ? 302 LYS   A CD  1 
ATOM   38   C  CE  . LYS   A 1 6   ? -43.951 -17.423 42.947 1.00 100.94 ? 302 LYS   A CE  1 
ATOM   39   N  NZ  . LYS   A 1 6   ? -44.418 -17.287 44.355 1.00 97.35  ? 302 LYS   A NZ  1 
ATOM   40   N  N   . VAL   A 1 7   ? -38.766 -13.734 41.471 1.00 83.41  ? 303 VAL   A N   1 
ATOM   41   C  CA  . VAL   A 1 7   ? -37.941 -12.540 41.597 1.00 77.86  ? 303 VAL   A CA  1 
ATOM   42   C  C   . VAL   A 1 7   ? -38.820 -11.430 42.153 1.00 79.58  ? 303 VAL   A C   1 
ATOM   43   O  O   . VAL   A 1 7   ? -39.986 -11.307 41.760 1.00 82.42  ? 303 VAL   A O   1 
ATOM   44   C  CB  . VAL   A 1 7   ? -37.312 -12.134 40.252 1.00 75.82  ? 303 VAL   A CB  1 
ATOM   45   C  CG1 . VAL   A 1 7   ? -36.555 -13.298 39.676 1.00 76.00  ? 303 VAL   A CG1 1 
ATOM   46   C  CG2 . VAL   A 1 7   ? -38.376 -11.690 39.264 1.00 79.21  ? 303 VAL   A CG2 1 
ATOM   47   N  N   . LYS   A 1 8   ? -38.285 -10.657 43.098 1.00 78.30  ? 304 LYS   A N   1 
ATOM   48   C  CA  . LYS   A 1 8   ? -39.030 -9.557  43.685 1.00 76.52  ? 304 LYS   A CA  1 
ATOM   49   C  C   . LYS   A 1 8   ? -38.447 -8.219  43.254 1.00 73.96  ? 304 LYS   A C   1 
ATOM   50   O  O   . LYS   A 1 8   ? -37.254 -8.097  42.978 1.00 70.82  ? 304 LYS   A O   1 
ATOM   51   C  CB  . LYS   A 1 8   ? -39.034 -9.636  45.221 1.00 78.18  ? 304 LYS   A CB  1 
ATOM   52   C  CG  . LYS   A 1 8   ? -40.066 -8.722  45.870 1.00 80.62  ? 304 LYS   A CG  1 
ATOM   53   C  CD  . LYS   A 1 8   ? -40.193 -8.943  47.376 1.00 83.04  ? 304 LYS   A CD  1 
ATOM   54   C  CE  . LYS   A 1 8   ? -41.159 -7.929  47.986 1.00 87.76  ? 304 LYS   A CE  1 
ATOM   55   N  NZ  . LYS   A 1 8   ? -41.013 -7.843  49.451 1.00 89.57  ? 304 LYS   A NZ  1 
ATOM   56   N  N   . ASN   A 1 9   ? -39.311 -7.215  43.199 1.00 79.08  ? 305 ASN   A N   1 
ATOM   57   C  CA  . ASN   A 1 9   ? -38.899 -5.820  43.186 1.00 78.94  ? 305 ASN   A CA  1 
ATOM   58   C  C   . ASN   A 1 9   ? -39.110 -5.262  44.587 1.00 83.15  ? 305 ASN   A C   1 
ATOM   59   O  O   . ASN   A 1 9   ? -40.215 -5.347  45.127 1.00 85.78  ? 305 ASN   A O   1 
ATOM   60   C  CB  . ASN   A 1 9   ? -39.696 -5.005  42.163 1.00 79.44  ? 305 ASN   A CB  1 
ATOM   61   C  CG  . ASN   A 1 9   ? -39.191 -3.576  42.034 1.00 80.32  ? 305 ASN   A CG  1 
ATOM   62   O  OD1 . ASN   A 1 9   ? -39.273 -2.794  42.981 1.00 85.30  ? 305 ASN   A OD1 1 
ATOM   63   N  ND2 . ASN   A 1 9   ? -38.670 -3.226  40.854 1.00 77.29  ? 305 ASN   A ND2 1 
ATOM   64   N  N   . TRP   A 1 10  ? -38.057 -4.702  45.173 1.00 77.75  ? 306 TRP   A N   1 
ATOM   65   C  CA  . TRP   A 1 10  ? -38.121 -4.196  46.541 1.00 81.69  ? 306 TRP   A CA  1 
ATOM   66   C  C   . TRP   A 1 10  ? -38.420 -2.706  46.619 1.00 84.40  ? 306 TRP   A C   1 
ATOM   67   O  O   . TRP   A 1 10  ? -38.467 -2.155  47.723 1.00 88.15  ? 306 TRP   A O   1 
ATOM   68   C  CB  . TRP   A 1 10  ? -36.818 -4.499  47.277 1.00 79.55  ? 306 TRP   A CB  1 
ATOM   69   C  CG  . TRP   A 1 10  ? -36.598 -5.950  47.442 1.00 77.53  ? 306 TRP   A CG  1 
ATOM   70   C  CD1 . TRP   A 1 10  ? -35.917 -6.768  46.601 1.00 75.64  ? 306 TRP   A CD1 1 
ATOM   71   C  CD2 . TRP   A 1 10  ? -37.073 -6.772  48.511 1.00 78.08  ? 306 TRP   A CD2 1 
ATOM   72   N  NE1 . TRP   A 1 10  ? -35.926 -8.052  47.081 1.00 73.73  ? 306 TRP   A NE1 1 
ATOM   73   C  CE2 . TRP   A 1 10  ? -36.628 -8.081  48.255 1.00 77.36  ? 306 TRP   A CE2 1 
ATOM   74   C  CE3 . TRP   A 1 10  ? -37.826 -6.527  49.659 1.00 78.57  ? 306 TRP   A CE3 1 
ATOM   75   C  CZ2 . TRP   A 1 10  ? -36.914 -9.144  49.094 1.00 77.18  ? 306 TRP   A CZ2 1 
ATOM   76   C  CZ3 . TRP   A 1 10  ? -38.110 -7.587  50.500 1.00 79.17  ? 306 TRP   A CZ3 1 
ATOM   77   C  CH2 . TRP   A 1 10  ? -37.655 -8.881  50.214 1.00 78.31  ? 306 TRP   A CH2 1 
ATOM   78   N  N   . GLU   A 1 11  ? -38.600 -2.039  45.483 1.00 83.37  ? 307 GLU   A N   1 
ATOM   79   C  CA  . GLU   A 1 11  ? -39.172 -0.700  45.477 1.00 87.17  ? 307 GLU   A CA  1 
ATOM   80   C  C   . GLU   A 1 11  ? -40.684 -0.742  45.318 1.00 89.66  ? 307 GLU   A C   1 
ATOM   81   O  O   . GLU   A 1 11  ? -41.377 0.148   45.816 1.00 91.25  ? 307 GLU   A O   1 
ATOM   82   C  CB  . GLU   A 1 11  ? -38.548 0.144   44.351 1.00 85.24  ? 307 GLU   A CB  1 
ATOM   83   C  CG  . GLU   A 1 11  ? -38.831 1.662   44.407 1.00 85.63  ? 307 GLU   A CG  1 
ATOM   84   C  CD  . GLU   A 1 11  ? -38.718 2.349   43.025 1.00 91.92  ? 307 GLU   A CD  1 
ATOM   85   O  OE1 . GLU   A 1 11  ? -38.012 1.830   42.124 1.00 86.14  ? 307 GLU   A OE1 1 
ATOM   86   O  OE2 . GLU   A 1 11  ? -39.356 3.415   42.835 1.00 95.84  ? 307 GLU   A OE2 1 
ATOM   87   N  N   . THR   A 1 12  ? -41.217 -1.769  44.643 1.00 91.06  ? 308 THR   A N   1 
ATOM   88   C  CA  . THR   A 1 12  ? -42.641 -1.837  44.344 1.00 93.67  ? 308 THR   A CA  1 
ATOM   89   C  C   . THR   A 1 12  ? -43.354 -3.052  44.920 1.00 96.49  ? 308 THR   A C   1 
ATOM   90   O  O   . THR   A 1 12  ? -44.580 -3.136  44.784 1.00 97.43  ? 308 THR   A O   1 
ATOM   91   C  CB  . THR   A 1 12  ? -42.876 -1.813  42.825 1.00 91.94  ? 308 THR   A CB  1 
ATOM   92   O  OG1 . THR   A 1 12  ? -42.417 -3.041  42.239 1.00 91.72  ? 308 THR   A OG1 1 
ATOM   93   C  CG2 . THR   A 1 12  ? -42.134 -0.649  42.195 1.00 94.14  ? 308 THR   A CG2 1 
ATOM   94   N  N   . ASP   A 1 13  ? -42.639 -3.992  45.540 1.00 100.38 ? 309 ASP   A N   1 
ATOM   95   C  CA  . ASP   A 1 13  ? -43.220 -5.223  46.080 1.00 99.45  ? 309 ASP   A CA  1 
ATOM   96   C  C   . ASP   A 1 13  ? -43.829 -6.105  44.989 1.00 99.45  ? 309 ASP   A C   1 
ATOM   97   O  O   . ASP   A 1 13  ? -44.610 -7.014  45.282 1.00 104.61 ? 309 ASP   A O   1 
ATOM   98   C  CB  . ASP   A 1 13  ? -44.270 -4.926  47.158 1.00 105.55 ? 309 ASP   A CB  1 
ATOM   99   C  CG  . ASP   A 1 13  ? -43.655 -4.424  48.457 1.00 111.08 ? 309 ASP   A CG  1 
ATOM   100  O  OD1 . ASP   A 1 13  ? -42.749 -5.107  48.983 1.00 114.11 ? 309 ASP   A OD1 1 
ATOM   101  O  OD2 . ASP   A 1 13  ? -44.083 -3.358  48.964 1.00 115.15 ? 309 ASP   A OD2 1 
ATOM   102  N  N   . VAL   A 1 14  ? -43.500 -5.859  43.727 1.00 94.60  ? 310 VAL   A N   1 
ATOM   103  C  CA  . VAL   A 1 14  ? -44.024 -6.675  42.640 1.00 92.29  ? 310 VAL   A CA  1 
ATOM   104  C  C   . VAL   A 1 14  ? -43.195 -7.947  42.535 1.00 89.95  ? 310 VAL   A C   1 
ATOM   105  O  O   . VAL   A 1 14  ? -41.960 -7.893  42.485 1.00 87.65  ? 310 VAL   A O   1 
ATOM   106  C  CB  . VAL   A 1 14  ? -44.013 -5.897  41.317 1.00 91.99  ? 310 VAL   A CB  1 
ATOM   107  C  CG1 . VAL   A 1 14  ? -44.245 -6.841  40.162 1.00 93.06  ? 310 VAL   A CG1 1 
ATOM   108  C  CG2 . VAL   A 1 14  ? -45.077 -4.826  41.323 1.00 94.32  ? 310 VAL   A CG2 1 
ATOM   109  N  N   . VAL   A 1 15  ? -43.868 -9.094  42.491 1.00 90.22  ? 311 VAL   A N   1 
ATOM   110  C  CA  . VAL   A 1 15  ? -43.219 -10.387 42.317 1.00 89.60  ? 311 VAL   A CA  1 
ATOM   111  C  C   . VAL   A 1 15  ? -43.580 -10.942 40.945 1.00 92.85  ? 311 VAL   A C   1 
ATOM   112  O  O   . VAL   A 1 15  ? -44.708 -10.772 40.465 1.00 97.11  ? 311 VAL   A O   1 
ATOM   113  C  CB  . VAL   A 1 15  ? -43.615 -11.370 43.433 1.00 89.16  ? 311 VAL   A CB  1 
ATOM   114  C  CG1 . VAL   A 1 15  ? -42.843 -12.681 43.297 1.00 90.09  ? 311 VAL   A CG1 1 
ATOM   115  C  CG2 . VAL   A 1 15  ? -43.356 -10.741 44.780 1.00 88.28  ? 311 VAL   A CG2 1 
ATOM   116  N  N   . LEU   A 1 16  ? -42.610 -11.588 40.307 1.00 89.12  ? 312 LEU   A N   1 
ATOM   117  C  CA  . LEU   A 1 16  ? -42.807 -12.276 39.042 1.00 89.44  ? 312 LEU   A CA  1 
ATOM   118  C  C   . LEU   A 1 16  ? -42.268 -13.691 39.179 1.00 90.18  ? 312 LEU   A C   1 
ATOM   119  O  O   . LEU   A 1 16  ? -41.304 -13.933 39.913 1.00 88.11  ? 312 LEU   A O   1 
ATOM   120  C  CB  . LEU   A 1 16  ? -42.107 -11.545 37.906 1.00 88.65  ? 312 LEU   A CB  1 
ATOM   121  C  CG  . LEU   A 1 16  ? -42.608 -10.117 37.699 1.00 90.14  ? 312 LEU   A CG  1 
ATOM   122  C  CD1 . LEU   A 1 16  ? -41.702 -9.362  36.747 1.00 86.24  ? 312 LEU   A CD1 1 
ATOM   123  C  CD2 . LEU   A 1 16  ? -44.038 -10.143 37.176 1.00 95.60  ? 312 LEU   A CD2 1 
ATOM   124  N  N   . THR   A 1 17  ? -42.914 -14.634 38.498 1.00 91.06  ? 313 THR   A N   1 
ATOM   125  C  CA  . THR   A 1 17  ? -42.515 -16.035 38.546 1.00 91.09  ? 313 THR   A CA  1 
ATOM   126  C  C   . THR   A 1 17  ? -41.784 -16.392 37.262 1.00 90.18  ? 313 THR   A C   1 
ATOM   127  O  O   . THR   A 1 17  ? -42.322 -16.209 36.164 1.00 89.54  ? 313 THR   A O   1 
ATOM   128  C  CB  . THR   A 1 17  ? -43.717 -16.955 38.732 1.00 93.94  ? 313 THR   A CB  1 
ATOM   129  O  OG1 . THR   A 1 17  ? -44.390 -16.630 39.953 1.00 96.15  ? 313 THR   A OG1 1 
ATOM   130  C  CG2 . THR   A 1 17  ? -43.256 -18.407 38.787 1.00 96.48  ? 313 THR   A CG2 1 
ATOM   131  N  N   . ASP   A 1 18  ? -40.568 -16.909 37.402 1.00 90.75  ? 314 ASP   A N   1 
ATOM   132  C  CA  . ASP   A 1 18  ? -39.727 -17.253 36.262 1.00 90.16  ? 314 ASP   A CA  1 
ATOM   133  C  C   . ASP   A 1 18  ? -39.786 -18.756 36.045 1.00 90.65  ? 314 ASP   A C   1 
ATOM   134  O  O   . ASP   A 1 18  ? -39.291 -19.527 36.870 1.00 94.71  ? 314 ASP   A O   1 
ATOM   135  C  CB  . ASP   A 1 18  ? -38.287 -16.798 36.486 1.00 87.65  ? 314 ASP   A CB  1 
ATOM   136  C  CG  . ASP   A 1 18  ? -37.425 -16.950 35.238 1.00 84.16  ? 314 ASP   A CG  1 
ATOM   137  O  OD1 . ASP   A 1 18  ? -37.171 -18.107 34.829 1.00 81.71  ? 314 ASP   A OD1 1 
ATOM   138  O  OD2 . ASP   A 1 18  ? -37.013 -15.914 34.671 1.00 79.16  ? 314 ASP   A OD2 1 
ATOM   139  N  N   . THR   A 1 19  ? -40.401 -19.172 34.938 1.00 85.54  ? 315 THR   A N   1 
ATOM   140  C  CA  . THR   A 1 19  ? -40.316 -20.551 34.481 1.00 86.62  ? 315 THR   A CA  1 
ATOM   141  C  C   . THR   A 1 19  ? -39.457 -20.705 33.236 1.00 83.54  ? 315 THR   A C   1 
ATOM   142  O  O   . THR   A 1 19  ? -39.045 -21.827 32.928 1.00 82.83  ? 315 THR   A O   1 
ATOM   143  C  CB  . THR   A 1 19  ? -41.713 -21.113 34.187 1.00 86.94  ? 315 THR   A CB  1 
ATOM   144  O  OG1 . THR   A 1 19  ? -42.299 -20.386 33.100 1.00 87.59  ? 315 THR   A OG1 1 
ATOM   145  C  CG2 . THR   A 1 19  ? -42.602 -20.985 35.410 1.00 93.13  ? 315 THR   A CG2 1 
ATOM   146  N  N   . LEU   A 1 20  ? -39.164 -19.602 32.540 1.00 82.36  ? 316 LEU   A N   1 
ATOM   147  C  CA  . LEU   A 1 20  ? -38.347 -19.648 31.334 1.00 84.04  ? 316 LEU   A CA  1 
ATOM   148  C  C   . LEU   A 1 20  ? -36.971 -20.244 31.600 1.00 82.77  ? 316 LEU   A C   1 
ATOM   149  O  O   . LEU   A 1 20  ? -36.394 -20.887 30.713 1.00 83.02  ? 316 LEU   A O   1 
ATOM   150  C  CB  . LEU   A 1 20  ? -38.212 -18.238 30.747 1.00 81.37  ? 316 LEU   A CB  1 
ATOM   151  C  CG  . LEU   A 1 20  ? -37.446 -18.074 29.426 1.00 79.04  ? 316 LEU   A CG  1 
ATOM   152  C  CD1 . LEU   A 1 20  ? -38.105 -18.861 28.296 1.00 76.85  ? 316 LEU   A CD1 1 
ATOM   153  C  CD2 . LEU   A 1 20  ? -37.314 -16.600 29.048 1.00 75.76  ? 316 LEU   A CD2 1 
ATOM   154  N  N   . HIS   A 1 21  ? -36.426 -20.041 32.803 1.00 82.06  ? 317 HIS   A N   1 
ATOM   155  C  CA  . HIS   A 1 21  ? -35.088 -20.531 33.114 1.00 81.42  ? 317 HIS   A CA  1 
ATOM   156  C  C   . HIS   A 1 21  ? -34.980 -22.038 32.968 1.00 85.88  ? 317 HIS   A C   1 
ATOM   157  O  O   . HIS   A 1 21  ? -33.864 -22.561 32.890 1.00 85.39  ? 317 HIS   A O   1 
ATOM   158  C  CB  . HIS   A 1 21  ? -34.697 -20.130 34.542 1.00 81.25  ? 317 HIS   A CB  1 
ATOM   159  C  CG  . HIS   A 1 21  ? -35.436 -20.883 35.595 1.00 86.02  ? 317 HIS   A CG  1 
ATOM   160  N  ND1 . HIS   A 1 21  ? -36.758 -20.637 35.892 1.00 87.53  ? 317 HIS   A ND1 1 
ATOM   161  C  CD2 . HIS   A 1 21  ? -35.048 -21.894 36.407 1.00 92.22  ? 317 HIS   A CD2 1 
ATOM   162  C  CE1 . HIS   A 1 21  ? -37.150 -21.458 36.850 1.00 96.07  ? 317 HIS   A CE1 1 
ATOM   163  N  NE2 . HIS   A 1 21  ? -36.131 -22.230 37.182 1.00 100.81 ? 317 HIS   A NE2 1 
ATOM   164  N  N   . LEU   A 1 22  ? -36.110 -22.748 32.951 1.00 85.48  ? 318 LEU   A N   1 
ATOM   165  C  CA  . LEU   A 1 22  ? -36.087 -24.184 32.684 1.00 87.54  ? 318 LEU   A CA  1 
ATOM   166  C  C   . LEU   A 1 22  ? -35.624 -24.487 31.261 1.00 87.32  ? 318 LEU   A C   1 
ATOM   167  O  O   . LEU   A 1 22  ? -34.959 -25.504 31.020 1.00 89.89  ? 318 LEU   A O   1 
ATOM   168  C  CB  . LEU   A 1 22  ? -37.471 -24.788 32.913 1.00 88.50  ? 318 LEU   A CB  1 
ATOM   169  C  CG  . LEU   A 1 22  ? -38.149 -24.657 34.278 1.00 92.59  ? 318 LEU   A CG  1 
ATOM   170  C  CD1 . LEU   A 1 22  ? -39.508 -25.340 34.219 1.00 91.53  ? 318 LEU   A CD1 1 
ATOM   171  C  CD2 . LEU   A 1 22  ? -37.298 -25.232 35.409 1.00 108.15 ? 318 LEU   A CD2 1 
ATOM   172  N  N   . LYS   A 1 23  ? -35.999 -23.647 30.293 1.00 85.64  ? 319 LYS   A N   1 
ATOM   173  C  CA  . LYS   A 1 23  ? -35.537 -23.890 28.925 1.00 87.76  ? 319 LYS   A CA  1 
ATOM   174  C  C   . LYS   A 1 23  ? -34.053 -23.581 28.761 1.00 88.28  ? 319 LYS   A C   1 
ATOM   175  O  O   . LYS   A 1 23  ? -33.507 -23.841 27.686 1.00 90.54  ? 319 LYS   A O   1 
ATOM   176  C  CB  . LYS   A 1 23  ? -36.345 -23.073 27.894 1.00 88.44  ? 319 LYS   A CB  1 
ATOM   177  C  CG  . LYS   A 1 23  ? -37.893 -23.155 27.976 1.00 90.37  ? 319 LYS   A CG  1 
ATOM   178  C  CD  . LYS   A 1 23  ? -38.472 -24.542 27.704 1.00 96.87  ? 319 LYS   A CD  1 
ATOM   179  C  CE  . LYS   A 1 23  ? -38.802 -24.771 26.227 1.00 108.18 ? 319 LYS   A CE  1 
ATOM   180  N  NZ  . LYS   A 1 23  ? -40.042 -24.070 25.764 1.00 110.41 ? 319 LYS   A NZ  1 
ATOM   181  N  N   . SER   A 1 24  ? -33.391 -23.050 29.791 1.00 89.25  ? 320 SER   A N   1 
ATOM   182  C  CA  . SER   A 1 24  ? -31.969 -22.749 29.702 1.00 92.03  ? 320 SER   A CA  1 
ATOM   183  C  C   . SER   A 1 24  ? -31.150 -24.008 29.465 1.00 99.70  ? 320 SER   A C   1 
ATOM   184  O  O   . SER   A 1 24  ? -31.498 -25.107 29.909 1.00 98.57  ? 320 SER   A O   1 
ATOM   185  C  CB  . SER   A 1 24  ? -31.460 -22.069 30.969 1.00 86.65  ? 320 SER   A CB  1 
ATOM   186  O  OG  . SER   A 1 24  ? -30.050 -22.222 31.051 1.00 88.13  ? 320 SER   A OG  1 
ATOM   187  N  N   . THR   A 1 25  ? -30.034 -23.824 28.771 1.00 114.98 ? 321 THR   A N   1 
ATOM   188  C  CA  . THR   A 1 25  ? -29.188 -24.934 28.370 1.00 117.13 ? 321 THR   A CA  1 
ATOM   189  C  C   . THR   A 1 25  ? -27.762 -24.681 28.838 1.00 117.13 ? 321 THR   A C   1 
ATOM   190  O  O   . THR   A 1 25  ? -27.202 -25.474 29.607 1.00 113.89 ? 321 THR   A O   1 
ATOM   191  C  CB  . THR   A 1 25  ? -29.263 -25.128 26.844 1.00 118.95 ? 321 THR   A CB  1 
ATOM   192  O  OG1 . THR   A 1 25  ? -28.108 -25.834 26.374 1.00 122.37 ? 321 THR   A OG1 1 
ATOM   193  C  CG2 . THR   A 1 25  ? -29.392 -23.778 26.113 1.00 116.23 ? 321 THR   A CG2 1 
ATOM   194  N  N   . LEU   A 1 26  ? -27.188 -23.559 28.405 1.00 107.75 ? 322 LEU   A N   1 
ATOM   195  C  CA  . LEU   A 1 26  ? -25.807 -23.236 28.713 1.00 105.36 ? 322 LEU   A CA  1 
ATOM   196  C  C   . LEU   A 1 26  ? -25.618 -23.034 30.215 1.00 105.05 ? 322 LEU   A C   1 
ATOM   197  O  O   . LEU   A 1 26  ? -26.573 -22.916 30.989 1.00 97.81  ? 322 LEU   A O   1 
ATOM   198  C  CB  . LEU   A 1 26  ? -25.375 -21.984 27.959 1.00 101.89 ? 322 LEU   A CB  1 
ATOM   199  C  CG  . LEU   A 1 26  ? -24.865 -22.167 26.535 1.00 106.66 ? 322 LEU   A CG  1 
ATOM   200  C  CD1 . LEU   A 1 26  ? -25.377 -21.049 25.642 1.00 101.47 ? 322 LEU   A CD1 1 
ATOM   201  C  CD2 . LEU   A 1 26  ? -23.346 -22.191 26.567 1.00 110.39 ? 322 LEU   A CD2 1 
ATOM   202  N  N   . GLU   A 1 27  ? -24.356 -23.001 30.621 1.00 103.55 ? 323 GLU   A N   1 
ATOM   203  C  CA  . GLU   A 1 27  ? -23.993 -22.840 32.016 1.00 100.38 ? 323 GLU   A CA  1 
ATOM   204  C  C   . GLU   A 1 27  ? -23.570 -21.401 32.295 1.00 98.79  ? 323 GLU   A C   1 
ATOM   205  O  O   . GLU   A 1 27  ? -23.219 -20.638 31.386 1.00 97.57  ? 323 GLU   A O   1 
ATOM   206  C  CB  . GLU   A 1 27  ? -22.881 -23.818 32.404 1.00 104.21 ? 323 GLU   A CB  1 
ATOM   207  C  CG  . GLU   A 1 27  ? -23.287 -25.273 32.259 1.00 106.07 ? 323 GLU   A CG  1 
ATOM   208  C  CD  . GLU   A 1 27  ? -22.291 -26.222 32.896 1.00 115.32 ? 323 GLU   A CD  1 
ATOM   209  O  OE1 . GLU   A 1 27  ? -21.328 -25.727 33.518 1.00 116.39 ? 323 GLU   A OE1 1 
ATOM   210  O  OE2 . GLU   A 1 27  ? -22.470 -27.459 32.784 1.00 118.19 ? 323 GLU   A OE2 1 
ATOM   211  N  N   . THR   A 1 28  ? -23.619 -21.042 33.582 1.00 96.02  ? 324 THR   A N   1 
ATOM   212  C  CA  . THR   A 1 28  ? -23.430 -19.672 34.042 1.00 91.62  ? 324 THR   A CA  1 
ATOM   213  C  C   . THR   A 1 28  ? -22.057 -19.407 34.644 1.00 94.54  ? 324 THR   A C   1 
ATOM   214  O  O   . THR   A 1 28  ? -21.631 -18.248 34.689 1.00 91.07  ? 324 THR   A O   1 
ATOM   215  C  CB  . THR   A 1 28  ? -24.481 -19.316 35.101 1.00 88.90  ? 324 THR   A CB  1 
ATOM   216  O  OG1 . THR   A 1 28  ? -24.307 -20.159 36.257 1.00 83.97  ? 324 THR   A OG1 1 
ATOM   217  C  CG2 . THR   A 1 28  ? -25.876 -19.503 34.545 1.00 85.24  ? 324 THR   A CG2 1 
ATOM   218  N  N   . GLY   A 1 29  ? -21.365 -20.437 35.125 1.00 87.94  ? 325 GLY   A N   1 
ATOM   219  C  CA  . GLY   A 1 29  ? -20.153 -20.272 35.884 1.00 84.56  ? 325 GLY   A CA  1 
ATOM   220  C  C   . GLY   A 1 29  ? -20.357 -20.404 37.379 1.00 79.52  ? 325 GLY   A C   1 
ATOM   221  O  O   . GLY   A 1 29  ? -19.434 -20.823 38.088 1.00 81.89  ? 325 GLY   A O   1 
ATOM   222  N  N   . CYS   A 1 30  ? -21.544 -20.077 37.876 1.00 78.11  ? 326 CYS   A N   1 
ATOM   223  C  CA  . CYS   A 1 30  ? -21.786 -20.267 39.299 1.00 77.01  ? 326 CYS   A CA  1 
ATOM   224  C  C   . CYS   A 1 30  ? -21.991 -21.748 39.612 1.00 80.47  ? 326 CYS   A C   1 
ATOM   225  O  O   . CYS   A 1 30  ? -22.340 -22.557 38.749 1.00 83.34  ? 326 CYS   A O   1 
ATOM   226  C  CB  . CYS   A 1 30  ? -23.008 -19.476 39.753 1.00 73.62  ? 326 CYS   A CB  1 
ATOM   227  S  SG  . CYS   A 1 30  ? -22.980 -17.728 39.350 1.00 67.31  ? 326 CYS   A SG  1 
ATOM   228  N  N   . THR   A 1 31  ? -21.765 -22.100 40.864 1.00 83.42  ? 327 THR   A N   1 
ATOM   229  C  CA  . THR   A 1 31  ? -22.108 -23.425 41.353 1.00 86.45  ? 327 THR   A CA  1 
ATOM   230  C  C   . THR   A 1 31  ? -23.018 -23.267 42.561 1.00 88.56  ? 327 THR   A C   1 
ATOM   231  O  O   . THR   A 1 31  ? -23.344 -22.157 42.981 1.00 88.41  ? 327 THR   A O   1 
ATOM   232  C  CB  . THR   A 1 31  ? -20.861 -24.239 41.709 1.00 85.37  ? 327 THR   A CB  1 
ATOM   233  O  OG1 . THR   A 1 31  ? -20.239 -23.671 42.861 1.00 85.48  ? 327 THR   A OG1 1 
ATOM   234  C  CG2 . THR   A 1 31  ? -19.865 -24.240 40.578 1.00 82.29  ? 327 THR   A CG2 1 
ATOM   235  N  N   . GLU   A 1 32  ? -23.436 -24.393 43.125 1.00 92.87  ? 328 GLU   A N   1 
ATOM   236  C  CA  . GLU   A 1 32  ? -24.179 -24.330 44.374 1.00 93.30  ? 328 GLU   A CA  1 
ATOM   237  C  C   . GLU   A 1 32  ? -23.389 -23.609 45.461 1.00 91.08  ? 328 GLU   A C   1 
ATOM   238  O  O   . GLU   A 1 32  ? -23.993 -23.064 46.391 1.00 94.43  ? 328 GLU   A O   1 
ATOM   239  C  CB  . GLU   A 1 32  ? -24.570 -25.743 44.839 1.00 101.67 ? 328 GLU   A CB  1 
ATOM   240  C  CG  . GLU   A 1 32  ? -25.752 -26.382 44.086 1.00 102.90 ? 328 GLU   A CG  1 
ATOM   241  C  CD  . GLU   A 1 32  ? -25.328 -27.202 42.869 1.00 110.53 ? 328 GLU   A CD  1 
ATOM   242  O  OE1 . GLU   A 1 32  ? -24.433 -26.748 42.116 1.00 108.74 ? 328 GLU   A OE1 1 
ATOM   243  O  OE2 . GLU   A 1 32  ? -25.894 -28.304 42.664 1.00 116.56 ? 328 GLU   A OE2 1 
ATOM   244  N  N   . HIS   A 1 33  ? -22.056 -23.560 45.355 1.00 87.15  ? 329 HIS   A N   1 
ATOM   245  C  CA  . HIS   A 1 33  ? -21.232 -23.033 46.431 1.00 88.51  ? 329 HIS   A CA  1 
ATOM   246  C  C   . HIS   A 1 33  ? -20.401 -21.807 46.066 1.00 83.95  ? 329 HIS   A C   1 
ATOM   247  O  O   . HIS   A 1 33  ? -19.655 -21.321 46.929 1.00 80.38  ? 329 HIS   A O   1 
ATOM   248  C  CB  . HIS   A 1 33  ? -20.294 -24.126 46.960 1.00 93.49  ? 329 HIS   A CB  1 
ATOM   249  C  CG  . HIS   A 1 33  ? -20.972 -25.441 47.209 1.00 98.91  ? 329 HIS   A CG  1 
ATOM   250  N  ND1 . HIS   A 1 33  ? -21.183 -26.372 46.213 1.00 100.49 ? 329 HIS   A ND1 1 
ATOM   251  C  CD2 . HIS   A 1 33  ? -21.487 -25.981 48.342 1.00 102.78 ? 329 HIS   A CD2 1 
ATOM   252  C  CE1 . HIS   A 1 33  ? -21.794 -27.429 46.720 1.00 104.88 ? 329 HIS   A CE1 1 
ATOM   253  N  NE2 . HIS   A 1 33  ? -21.990 -27.217 48.010 1.00 104.05 ? 329 HIS   A NE2 1 
ATOM   254  N  N   . ILE   A 1 34  ? -20.497 -21.285 44.840 1.00 80.20  ? 330 ILE   A N   1 
ATOM   255  C  CA  . ILE   A 1 34  ? -19.759 -20.077 44.478 1.00 74.55  ? 330 ILE   A CA  1 
ATOM   256  C  C   . ILE   A 1 34  ? -20.530 -19.306 43.415 1.00 74.57  ? 330 ILE   A C   1 
ATOM   257  O  O   . ILE   A 1 34  ? -21.012 -19.877 42.432 1.00 73.52  ? 330 ILE   A O   1 
ATOM   258  C  CB  . ILE   A 1 34  ? -18.329 -20.396 44.007 1.00 75.11  ? 330 ILE   A CB  1 
ATOM   259  C  CG1 . ILE   A 1 34  ? -17.548 -19.102 43.799 1.00 72.77  ? 330 ILE   A CG1 1 
ATOM   260  C  CG2 . ILE   A 1 34  ? -18.343 -21.197 42.693 1.00 83.59  ? 330 ILE   A CG2 1 
ATOM   261  C  CD1 . ILE   A 1 34  ? -16.083 -19.250 44.165 1.00 75.75  ? 330 ILE   A CD1 1 
ATOM   262  N  N   . CYS   A 1 35  ? -20.657 -18.001 43.608 1.00 71.55  ? 331 CYS   A N   1 
ATOM   263  C  CA  . CYS   A 1 35  ? -21.369 -17.160 42.662 1.00 68.66  ? 331 CYS   A CA  1 
ATOM   264  C  C   . CYS   A 1 35  ? -20.363 -16.352 41.859 1.00 68.73  ? 331 CYS   A C   1 
ATOM   265  O  O   . CYS   A 1 35  ? -19.554 -15.612 42.437 1.00 64.60  ? 331 CYS   A O   1 
ATOM   266  C  CB  . CYS   A 1 35  ? -22.360 -16.228 43.351 1.00 65.37  ? 331 CYS   A CB  1 
ATOM   267  S  SG  . CYS   A 1 35  ? -23.166 -15.161 42.145 1.00 56.56  ? 331 CYS   A SG  1 
ATOM   268  N  N   . MET   A 1 36  ? -20.415 -16.514 40.534 1.00 65.86  ? 332 MET   A N   1 
ATOM   269  C  CA  . MET   A 1 36  ? -19.550 -15.825 39.581 1.00 67.63  ? 332 MET   A CA  1 
ATOM   270  C  C   . MET   A 1 36  ? -20.231 -14.630 38.927 1.00 64.60  ? 332 MET   A C   1 
ATOM   271  O  O   . MET   A 1 36  ? -19.747 -14.132 37.902 1.00 60.70  ? 332 MET   A O   1 
ATOM   272  C  CB  . MET   A 1 36  ? -19.093 -16.787 38.481 1.00 70.21  ? 332 MET   A CB  1 
ATOM   273  C  CG  . MET   A 1 36  ? -18.524 -18.082 38.982 1.00 75.46  ? 332 MET   A CG  1 
ATOM   274  S  SD  . MET   A 1 36  ? -16.732 -18.196 38.882 1.00 87.64  ? 332 MET   A SD  1 
ATOM   275  C  CE  . MET   A 1 36  ? -16.479 -19.478 40.102 1.00 85.37  ? 332 MET   A CE  1 
ATOM   276  N  N   . GLY   A 1 37  ? -21.349 -14.165 39.483 1.00 61.71  ? 333 GLY   A N   1 
ATOM   277  C  CA  . GLY   A 1 37  ? -22.126 -13.122 38.827 1.00 61.24  ? 333 GLY   A CA  1 
ATOM   278  C  C   . GLY   A 1 37  ? -21.425 -11.798 38.594 1.00 60.90  ? 333 GLY   A C   1 
ATOM   279  O  O   . GLY   A 1 37  ? -22.010 -10.946 37.922 1.00 60.29  ? 333 GLY   A O   1 
ATOM   280  N  N   . SER   A 1 38  ? -20.219 -11.569 39.121 1.00 61.83  ? 334 SER   A N   1 
ATOM   281  C  CA  . SER   A 1 38  ? -19.484 -10.347 38.804 1.00 57.89  ? 334 SER   A CA  1 
ATOM   282  C  C   . SER   A 1 38  ? -18.178 -10.627 38.066 1.00 60.04  ? 334 SER   A C   1 
ATOM   283  O  O   . SER   A 1 38  ? -17.343 -9.721  37.940 1.00 59.88  ? 334 SER   A O   1 
ATOM   284  C  CB  . SER   A 1 38  ? -19.197 -9.527  40.064 1.00 59.86  ? 334 SER   A CB  1 
ATOM   285  O  OG  . SER   A 1 38  ? -18.145 -10.112 40.826 1.00 62.11  ? 334 SER   A OG  1 
ATOM   286  N  N   . ILE   A 1 39  ? -17.972 -11.856 37.601 1.00 60.63  ? 335 ILE   A N   1 
ATOM   287  C  CA  . ILE   A 1 39  ? -16.856 -12.174 36.718 1.00 65.27  ? 335 ILE   A CA  1 
ATOM   288  C  C   . ILE   A 1 39  ? -17.203 -11.691 35.316 1.00 67.80  ? 335 ILE   A C   1 
ATOM   289  O  O   . ILE   A 1 39  ? -18.258 -12.039 34.773 1.00 68.68  ? 335 ILE   A O   1 
ATOM   290  C  CB  . ILE   A 1 39  ? -16.569 -13.683 36.725 1.00 66.76  ? 335 ILE   A CB  1 
ATOM   291  C  CG1 . ILE   A 1 39  ? -16.350 -14.200 38.163 1.00 68.79  ? 335 ILE   A CG1 1 
ATOM   292  C  CG2 . ILE   A 1 39  ? -15.375 -13.989 35.843 1.00 71.13  ? 335 ILE   A CG2 1 
ATOM   293  C  CD1 . ILE   A 1 39  ? -15.240 -13.478 38.929 1.00 67.57  ? 335 ILE   A CD1 1 
ATOM   294  N  N   . MET   A 1 40  ? -16.314 -10.893 34.722 1.00 69.03  ? 336 MET   A N   1 
ATOM   295  C  CA  . MET   A 1 40  ? -16.663 -10.183 33.489 1.00 70.87  ? 336 MET   A CA  1 
ATOM   296  C  C   . MET   A 1 40  ? -16.816 -11.135 32.303 1.00 77.95  ? 336 MET   A C   1 
ATOM   297  O  O   . MET   A 1 40  ? -17.872 -11.185 31.658 1.00 76.19  ? 336 MET   A O   1 
ATOM   298  C  CB  . MET   A 1 40  ? -15.611 -9.120  33.176 1.00 73.52  ? 336 MET   A CB  1 
ATOM   299  C  CG  . MET   A 1 40  ? -15.776 -8.530  31.796 1.00 76.92  ? 336 MET   A CG  1 
ATOM   300  S  SD  . MET   A 1 40  ? -16.360 -6.828  31.876 1.00 80.44  ? 336 MET   A SD  1 
ATOM   301  C  CE  . MET   A 1 40  ? -14.966 -6.068  32.683 1.00 68.97  ? 336 MET   A CE  1 
ATOM   302  N  N   . LEU   A 1 41  ? -15.759 -11.867 31.975 1.00 75.51  ? 337 LEU   A N   1 
ATOM   303  C  CA  . LEU   A 1 41  ? -15.782 -12.823 30.877 1.00 84.61  ? 337 LEU   A CA  1 
ATOM   304  C  C   . LEU   A 1 41  ? -15.719 -14.229 31.443 1.00 92.11  ? 337 LEU   A C   1 
ATOM   305  O  O   . LEU   A 1 41  ? -14.661 -14.868 31.374 1.00 97.09  ? 337 LEU   A O   1 
ATOM   306  C  CB  . LEU   A 1 41  ? -14.602 -12.604 29.921 1.00 86.13  ? 337 LEU   A CB  1 
ATOM   307  C  CG  . LEU   A 1 41  ? -14.098 -11.163 29.681 1.00 84.33  ? 337 LEU   A CG  1 
ATOM   308  C  CD1 . LEU   A 1 41  ? -12.658 -11.205 29.199 1.00 86.66  ? 337 LEU   A CD1 1 
ATOM   309  C  CD2 . LEU   A 1 41  ? -14.982 -10.440 28.688 1.00 81.32  ? 337 LEU   A CD2 1 
ATOM   310  N  N   . PRO   A 1 42  ? -16.803 -14.739 32.024 1.00 96.04  ? 338 PRO   A N   1 
ATOM   311  C  CA  . PRO   A 1 42  ? -16.724 -16.061 32.646 1.00 104.39 ? 338 PRO   A CA  1 
ATOM   312  C  C   . PRO   A 1 42  ? -16.410 -17.109 31.589 1.00 119.38 ? 338 PRO   A C   1 
ATOM   313  O  O   . PRO   A 1 42  ? -16.727 -16.941 30.408 1.00 119.58 ? 338 PRO   A O   1 
ATOM   314  C  CB  . PRO   A 1 42  ? -18.115 -16.253 33.250 1.00 103.01 ? 338 PRO   A CB  1 
ATOM   315  C  CG  . PRO   A 1 42  ? -19.010 -15.430 32.386 1.00 100.59 ? 338 PRO   A CG  1 
ATOM   316  C  CD  . PRO   A 1 42  ? -18.192 -14.244 31.930 1.00 93.35  ? 338 PRO   A CD  1 
ATOM   317  N  N   . SER   A 1 43  ? -15.754 -18.188 32.026 1.00 130.71 ? 339 SER   A N   1 
ATOM   318  C  CA  . SER   A 1 43  ? -15.284 -19.222 31.109 1.00 135.62 ? 339 SER   A CA  1 
ATOM   319  C  C   . SER   A 1 43  ? -16.384 -19.730 30.189 1.00 137.59 ? 339 SER   A C   1 
ATOM   320  O  O   . SER   A 1 43  ? -16.082 -20.296 29.131 1.00 136.11 ? 339 SER   A O   1 
ATOM   321  C  CB  . SER   A 1 43  ? -14.695 -20.388 31.909 1.00 138.50 ? 339 SER   A CB  1 
ATOM   322  O  OG  . SER   A 1 43  ? -14.208 -21.399 31.046 1.00 144.77 ? 339 SER   A OG  1 
ATOM   323  N  N   . GLN   A 1 44  ? -17.650 -19.521 30.563 1.00 130.30 ? 340 GLN   A N   1 
ATOM   324  C  CA  . GLN   A 1 44  ? -18.782 -19.975 29.761 1.00 130.35 ? 340 GLN   A CA  1 
ATOM   325  C  C   . GLN   A 1 44  ? -19.162 -18.975 28.666 1.00 132.03 ? 340 GLN   A C   1 
ATOM   326  O  O   . GLN   A 1 44  ? -19.520 -19.385 27.556 1.00 130.64 ? 340 GLN   A O   1 
ATOM   327  C  CB  . GLN   A 1 44  ? -19.989 -20.236 30.666 1.00 121.32 ? 340 GLN   A CB  1 
ATOM   328  C  CG  . GLN   A 1 44  ? -20.021 -21.615 31.331 1.00 117.59 ? 340 GLN   A CG  1 
ATOM   329  C  CD  . GLN   A 1 44  ? -19.028 -21.772 32.469 1.00 119.82 ? 340 GLN   A CD  1 
ATOM   330  O  OE1 . GLN   A 1 44  ? -18.184 -20.904 32.713 1.00 123.44 ? 340 GLN   A OE1 1 
ATOM   331  N  NE2 . GLN   A 1 44  ? -19.124 -22.897 33.174 1.00 114.67 ? 340 GLN   A NE2 1 
ATOM   332  N  N   . HIS   A 1 45  ? -19.108 -17.666 28.955 1.00 133.14 ? 341 HIS   A N   1 
ATOM   333  C  CA  . HIS   A 1 45  ? -19.581 -16.604 28.063 1.00 129.64 ? 341 HIS   A CA  1 
ATOM   334  C  C   . HIS   A 1 45  ? -18.721 -16.425 26.800 1.00 128.19 ? 341 HIS   A C   1 
ATOM   335  O  O   . HIS   A 1 45  ? -18.990 -15.508 26.012 1.00 124.59 ? 341 HIS   A O   1 
ATOM   336  C  CB  . HIS   A 1 45  ? -19.663 -15.287 28.851 1.00 123.92 ? 341 HIS   A CB  1 
ATOM   337  C  CG  . HIS   A 1 45  ? -20.680 -14.317 28.325 1.00 121.00 ? 341 HIS   A CG  1 
ATOM   338  N  ND1 . HIS   A 1 45  ? -21.175 -14.381 27.040 1.00 116.39 ? 341 HIS   A ND1 1 
ATOM   339  C  CD2 . HIS   A 1 45  ? -21.289 -13.256 28.907 1.00 114.04 ? 341 HIS   A CD2 1 
ATOM   340  C  CE1 . HIS   A 1 45  ? -22.043 -13.402 26.852 1.00 111.23 ? 341 HIS   A CE1 1 
ATOM   341  N  NE2 . HIS   A 1 45  ? -22.129 -12.704 27.969 1.00 110.92 ? 341 HIS   A NE2 1 
ATOM   342  N  N   . THR   A 1 46  ? -17.721 -17.274 26.561 1.00 143.68 ? 342 THR   A N   1 
ATOM   343  C  CA  . THR   A 1 46  ? -16.823 -17.143 25.419 1.00 143.06 ? 342 THR   A CA  1 
ATOM   344  C  C   . THR   A 1 46  ? -16.924 -18.386 24.544 1.00 145.07 ? 342 THR   A C   1 
ATOM   345  O  O   . THR   A 1 46  ? -17.046 -19.506 25.051 1.00 148.58 ? 342 THR   A O   1 
ATOM   346  C  CB  . THR   A 1 46  ? -15.360 -16.933 25.884 1.00 144.33 ? 342 THR   A CB  1 
ATOM   347  O  OG1 . THR   A 1 46  ? -15.278 -15.764 26.707 1.00 141.50 ? 342 THR   A OG1 1 
ATOM   348  C  CG2 . THR   A 1 46  ? -14.428 -16.769 24.695 1.00 143.76 ? 342 THR   A CG2 1 
ATOM   349  N  N   . ARG   A 1 47  ? -16.893 -18.175 23.230 1.00 129.12 ? 343 ARG   A N   1 
ATOM   350  C  CA  . ARG   A 1 47  ? -16.854 -19.268 22.256 1.00 134.87 ? 343 ARG   A CA  1 
ATOM   351  C  C   . ARG   A 1 47  ? -15.422 -19.574 21.842 1.00 134.61 ? 343 ARG   A C   1 
ATOM   352  O  O   . ARG   A 1 47  ? -14.852 -18.884 21.000 1.00 130.81 ? 343 ARG   A O   1 
ATOM   353  C  CB  . ARG   A 1 47  ? -17.696 -18.930 21.020 1.00 124.98 ? 343 ARG   A CB  1 
ATOM   354  C  CG  . ARG   A 1 47  ? -19.190 -19.101 21.223 1.00 123.57 ? 343 ARG   A CG  1 
ATOM   355  C  CD  . ARG   A 1 47  ? -19.469 -20.173 22.269 1.00 132.50 ? 343 ARG   A CD  1 
ATOM   356  N  NE  . ARG   A 1 47  ? -20.896 -20.360 22.490 1.00 129.31 ? 343 ARG   A NE  1 
ATOM   357  C  CZ  . ARG   A 1 47  ? -21.417 -20.993 23.532 1.00 131.05 ? 343 ARG   A CZ  1 
ATOM   358  N  NH1 . ARG   A 1 47  ? -20.655 -21.491 24.493 1.00 134.31 ? 343 ARG   A NH1 1 
ATOM   359  N  NH2 . ARG   A 1 47  ? -22.738 -21.125 23.613 1.00 132.00 ? 343 ARG   A NH2 1 
ATOM   360  N  N   . VAL   A 1 52  ? -13.864 -25.789 17.530 1.00 138.83 ? 348 VAL   A N   1 
ATOM   361  C  CA  . VAL   A 1 52  ? -14.594 -26.409 16.427 1.00 142.93 ? 348 VAL   A CA  1 
ATOM   362  C  C   . VAL   A 1 52  ? -15.738 -27.261 16.987 1.00 143.49 ? 348 VAL   A C   1 
ATOM   363  O  O   . VAL   A 1 52  ? -15.639 -27.796 18.097 1.00 140.85 ? 348 VAL   A O   1 
ATOM   364  C  CB  . VAL   A 1 52  ? -13.639 -27.241 15.512 1.00 140.60 ? 348 VAL   A CB  1 
ATOM   365  C  CG1 . VAL   A 1 52  ? -13.174 -28.518 16.203 1.00 139.73 ? 348 VAL   A CG1 1 
ATOM   366  C  CG2 . VAL   A 1 52  ? -14.285 -27.543 14.153 1.00 137.23 ? 348 VAL   A CG2 1 
ATOM   367  N  N   . ALA   A 1 53  ? -16.830 -27.364 16.225 1.00 144.38 ? 349 ALA   A N   1 
ATOM   368  C  CA  . ALA   A 1 53  ? -18.013 -28.123 16.611 1.00 140.45 ? 349 ALA   A CA  1 
ATOM   369  C  C   . ALA   A 1 53  ? -18.317 -29.181 15.556 1.00 136.36 ? 349 ALA   A C   1 
ATOM   370  O  O   . ALA   A 1 53  ? -18.206 -28.918 14.354 1.00 138.32 ? 349 ALA   A O   1 
ATOM   371  C  CB  . ALA   A 1 53  ? -19.225 -27.202 16.800 1.00 137.46 ? 349 ALA   A CB  1 
ATOM   372  N  N   . THR   A 1 54  ? -18.714 -30.371 16.010 1.00 134.05 ? 350 THR   A N   1 
ATOM   373  C  CA  . THR   A 1 54  ? -18.869 -31.535 15.148 1.00 133.43 ? 350 THR   A CA  1 
ATOM   374  C  C   . THR   A 1 54  ? -20.323 -31.745 14.730 1.00 131.26 ? 350 THR   A C   1 
ATOM   375  O  O   . THR   A 1 54  ? -21.247 -31.076 15.196 1.00 128.54 ? 350 THR   A O   1 
ATOM   376  C  CB  . THR   A 1 54  ? -18.354 -32.798 15.840 1.00 132.59 ? 350 THR   A CB  1 
ATOM   377  O  OG1 . THR   A 1 54  ? -19.446 -33.459 16.490 1.00 134.81 ? 350 THR   A OG1 1 
ATOM   378  C  CG2 . THR   A 1 54  ? -17.298 -32.440 16.872 1.00 130.65 ? 350 THR   A CG2 1 
ATOM   379  N  N   . LYS   A 1 55  ? -20.510 -32.727 13.846 1.00 134.38 ? 351 LYS   A N   1 
ATOM   380  C  CA  . LYS   A 1 55  ? -21.815 -32.959 13.235 1.00 134.35 ? 351 LYS   A CA  1 
ATOM   381  C  C   . LYS   A 1 55  ? -22.808 -33.566 14.217 1.00 132.52 ? 351 LYS   A C   1 
ATOM   382  O  O   . LYS   A 1 55  ? -24.011 -33.292 14.130 1.00 126.42 ? 351 LYS   A O   1 
ATOM   383  C  CB  . LYS   A 1 55  ? -21.655 -33.861 12.011 1.00 136.55 ? 351 LYS   A CB  1 
ATOM   384  C  CG  . LYS   A 1 55  ? -20.606 -34.945 12.196 1.00 141.28 ? 351 LYS   A CG  1 
ATOM   385  C  CD  . LYS   A 1 55  ? -20.408 -35.777 10.935 1.00 148.45 ? 351 LYS   A CD  1 
ATOM   386  C  CE  . LYS   A 1 55  ? -19.395 -36.892 11.183 1.00 154.36 ? 351 LYS   A CE  1 
ATOM   387  N  NZ  . LYS   A 1 55  ? -19.451 -37.968 10.154 1.00 153.72 ? 351 LYS   A NZ  1 
ATOM   388  N  N   . ASP   A 1 56  ? -22.332 -34.394 15.146 1.00 137.45 ? 352 ASP   A N   1 
ATOM   389  C  CA  . ASP   A 1 56  ? -23.231 -35.019 16.111 1.00 139.67 ? 352 ASP   A CA  1 
ATOM   390  C  C   . ASP   A 1 56  ? -23.872 -33.975 17.015 1.00 133.28 ? 352 ASP   A C   1 
ATOM   391  O  O   . ASP   A 1 56  ? -25.079 -34.023 17.282 1.00 134.16 ? 352 ASP   A O   1 
ATOM   392  C  CB  . ASP   A 1 56  ? -22.459 -36.049 16.935 1.00 147.58 ? 352 ASP   A CB  1 
ATOM   393  C  CG  . ASP   A 1 56  ? -21.379 -36.746 16.124 1.00 154.60 ? 352 ASP   A CG  1 
ATOM   394  O  OD1 . ASP   A 1 56  ? -20.347 -36.100 15.843 1.00 156.41 ? 352 ASP   A OD1 1 
ATOM   395  O  OD2 . ASP   A 1 56  ? -21.568 -37.926 15.754 1.00 159.43 ? 352 ASP   A OD2 1 
ATOM   396  N  N   . GLN   A 1 57  ? -23.083 -33.012 17.481 1.00 126.71 ? 353 GLN   A N   1 
ATOM   397  C  CA  . GLN   A 1 57  ? -23.618 -31.963 18.333 1.00 123.10 ? 353 GLN   A CA  1 
ATOM   398  C  C   . GLN   A 1 57  ? -24.588 -31.048 17.598 1.00 117.86 ? 353 GLN   A C   1 
ATOM   399  O  O   . GLN   A 1 57  ? -25.379 -30.362 18.254 1.00 110.83 ? 353 GLN   A O   1 
ATOM   400  C  CB  . GLN   A 1 57  ? -22.468 -31.145 18.903 1.00 122.29 ? 353 GLN   A CB  1 
ATOM   401  C  CG  . GLN   A 1 57  ? -21.236 -31.975 19.209 1.00 126.46 ? 353 GLN   A CG  1 
ATOM   402  C  CD  . GLN   A 1 57  ? -19.950 -31.188 19.048 1.00 128.66 ? 353 GLN   A CD  1 
ATOM   403  O  OE1 . GLN   A 1 57  ? -19.810 -30.391 18.119 1.00 130.85 ? 353 GLN   A OE1 1 
ATOM   404  N  NE2 . GLN   A 1 57  ? -19.001 -31.405 19.958 1.00 127.08 ? 353 GLN   A NE2 1 
ATOM   405  N  N   . LEU   A 1 58  ? -24.558 -31.036 16.259 1.00 118.21 ? 354 LEU   A N   1 
ATOM   406  C  CA  . LEU   A 1 58  ? -25.255 -29.987 15.520 1.00 114.11 ? 354 LEU   A CA  1 
ATOM   407  C  C   . LEU   A 1 58  ? -26.760 -30.230 15.460 1.00 112.21 ? 354 LEU   A C   1 
ATOM   408  O  O   . LEU   A 1 58  ? -27.546 -29.276 15.532 1.00 105.56 ? 354 LEU   A O   1 
ATOM   409  C  CB  . LEU   A 1 58  ? -24.680 -29.861 14.110 1.00 114.28 ? 354 LEU   A CB  1 
ATOM   410  C  CG  . LEU   A 1 58  ? -24.067 -28.517 13.721 1.00 109.73 ? 354 LEU   A CG  1 
ATOM   411  C  CD1 . LEU   A 1 58  ? -22.858 -28.180 14.585 1.00 109.85 ? 354 LEU   A CD1 1 
ATOM   412  C  CD2 . LEU   A 1 58  ? -23.682 -28.531 12.256 1.00 107.41 ? 354 LEU   A CD2 1 
ATOM   413  N  N   . PHE   A 1 59  ? -27.190 -31.492 15.330 1.00 113.95 ? 355 PHE   A N   1 
ATOM   414  C  CA  . PHE   A 1 59  ? -28.622 -31.701 15.129 1.00 114.36 ? 355 PHE   A CA  1 
ATOM   415  C  C   . PHE   A 1 59  ? -29.467 -31.413 16.369 1.00 113.91 ? 355 PHE   A C   1 
ATOM   416  O  O   . PHE   A 1 59  ? -30.550 -30.830 16.230 1.00 113.75 ? 355 PHE   A O   1 
ATOM   417  C  CB  . PHE   A 1 59  ? -28.933 -33.111 14.643 1.00 125.11 ? 355 PHE   A CB  1 
ATOM   418  C  CG  . PHE   A 1 59  ? -30.324 -33.242 14.096 1.00 133.49 ? 355 PHE   A CG  1 
ATOM   419  C  CD1 . PHE   A 1 59  ? -30.691 -32.548 12.948 1.00 131.08 ? 355 PHE   A CD1 1 
ATOM   420  C  CD2 . PHE   A 1 59  ? -31.276 -34.018 14.741 1.00 134.27 ? 355 PHE   A CD2 1 
ATOM   421  C  CE1 . PHE   A 1 59  ? -31.975 -32.635 12.443 1.00 130.64 ? 355 PHE   A CE1 1 
ATOM   422  C  CE2 . PHE   A 1 59  ? -32.564 -34.118 14.232 1.00 137.52 ? 355 PHE   A CE2 1 
ATOM   423  C  CZ  . PHE   A 1 59  ? -32.911 -33.426 13.077 1.00 135.89 ? 355 PHE   A CZ  1 
ATOM   424  N  N   . PRO   A 1 60  ? -29.055 -31.811 17.582 1.00 112.21 ? 356 PRO   A N   1 
ATOM   425  C  CA  . PRO   A 1 60  ? -29.801 -31.349 18.770 1.00 107.44 ? 356 PRO   A CA  1 
ATOM   426  C  C   . PRO   A 1 60  ? -29.957 -29.840 18.832 1.00 101.46 ? 356 PRO   A C   1 
ATOM   427  O  O   . PRO   A 1 60  ? -31.041 -29.344 19.165 1.00 96.78  ? 356 PRO   A O   1 
ATOM   428  C  CB  . PRO   A 1 60  ? -28.969 -31.889 19.948 1.00 107.88 ? 356 PRO   A CB  1 
ATOM   429  C  CG  . PRO   A 1 60  ? -27.679 -32.389 19.344 1.00 113.17 ? 356 PRO   A CG  1 
ATOM   430  C  CD  . PRO   A 1 60  ? -28.026 -32.798 17.950 1.00 113.39 ? 356 PRO   A CD  1 
ATOM   431  N  N   . LEU   A 1 61  ? -28.898 -29.100 18.496 1.00 101.85 ? 357 LEU   A N   1 
ATOM   432  C  CA  . LEU   A 1 61  ? -28.967 -27.642 18.467 1.00 94.32  ? 357 LEU   A CA  1 
ATOM   433  C  C   . LEU   A 1 61  ? -29.886 -27.140 17.357 1.00 96.76  ? 357 LEU   A C   1 
ATOM   434  O  O   . LEU   A 1 61  ? -30.587 -26.136 17.537 1.00 94.22  ? 357 LEU   A O   1 
ATOM   435  C  CB  . LEU   A 1 61  ? -27.565 -27.069 18.298 1.00 91.16  ? 357 LEU   A CB  1 
ATOM   436  C  CG  . LEU   A 1 61  ? -26.559 -27.629 19.293 1.00 97.73  ? 357 LEU   A CG  1 
ATOM   437  C  CD1 . LEU   A 1 61  ? -25.140 -27.223 18.949 1.00 96.35  ? 357 LEU   A CD1 1 
ATOM   438  C  CD2 . LEU   A 1 61  ? -26.922 -27.177 20.707 1.00 96.72  ? 357 LEU   A CD2 1 
ATOM   439  N  N   . ALA   A 1 62  ? -29.888 -27.812 16.197 1.00 97.31  ? 358 ALA   A N   1 
ATOM   440  C  CA  . ALA   A 1 62  ? -30.786 -27.410 15.118 1.00 94.96  ? 358 ALA   A CA  1 
ATOM   441  C  C   . ALA   A 1 62  ? -32.234 -27.710 15.473 1.00 95.07  ? 358 ALA   A C   1 
ATOM   442  O  O   . ALA   A 1 62  ? -33.115 -26.857 15.303 1.00 92.47  ? 358 ALA   A O   1 
ATOM   443  C  CB  . ALA   A 1 62  ? -30.404 -28.113 13.811 1.00 99.63  ? 358 ALA   A CB  1 
ATOM   444  N  N   . LYS   A 1 63  ? -32.492 -28.926 15.963 1.00 96.28  ? 359 LYS   A N   1 
ATOM   445  C  CA  . LYS   A 1 63  ? -33.847 -29.344 16.325 1.00 98.06  ? 359 LYS   A CA  1 
ATOM   446  C  C   . LYS   A 1 63  ? -34.420 -28.466 17.430 1.00 98.95  ? 359 LYS   A C   1 
ATOM   447  O  O   . LYS   A 1 63  ? -35.553 -27.978 17.331 1.00 100.08 ? 359 LYS   A O   1 
ATOM   448  C  CB  . LYS   A 1 63  ? -33.842 -30.810 16.768 1.00 101.59 ? 359 LYS   A CB  1 
ATOM   449  C  CG  . LYS   A 1 63  ? -35.142 -31.273 17.392 1.00 102.94 ? 359 LYS   A CG  1 
ATOM   450  C  CD  . LYS   A 1 63  ? -35.084 -32.732 17.817 1.00 107.44 ? 359 LYS   A CD  1 
ATOM   451  C  CE  . LYS   A 1 63  ? -36.438 -33.397 17.619 1.00 106.52 ? 359 LYS   A CE  1 
ATOM   452  N  NZ  . LYS   A 1 63  ? -37.525 -32.542 18.182 1.00 113.75 ? 359 LYS   A NZ  1 
ATOM   453  N  N   . GLU   A 1 64  ? -33.651 -28.272 18.500 1.00 93.77  ? 360 GLU   A N   1 
ATOM   454  C  CA  . GLU   A 1 64  ? -34.042 -27.336 19.543 1.00 95.30  ? 360 GLU   A CA  1 
ATOM   455  C  C   . GLU   A 1 64  ? -34.414 -25.972 18.957 1.00 93.09  ? 360 GLU   A C   1 
ATOM   456  O  O   . GLU   A 1 64  ? -35.506 -25.452 19.216 1.00 94.30  ? 360 GLU   A O   1 
ATOM   457  C  CB  . GLU   A 1 64  ? -32.903 -27.228 20.559 1.00 94.80  ? 360 GLU   A CB  1 
ATOM   458  C  CG  . GLU   A 1 64  ? -33.155 -26.320 21.726 1.00 96.00  ? 360 GLU   A CG  1 
ATOM   459  C  CD  . GLU   A 1 64  ? -31.887 -26.066 22.520 1.00 98.86  ? 360 GLU   A CD  1 
ATOM   460  O  OE1 . GLU   A 1 64  ? -31.107 -27.033 22.713 1.00 105.09 ? 360 GLU   A OE1 1 
ATOM   461  O  OE2 . GLU   A 1 64  ? -31.674 -24.903 22.935 1.00 94.80  ? 360 GLU   A OE2 1 
ATOM   462  N  N   . PHE   A 1 65  ? -33.530 -25.386 18.141 1.00 91.51  ? 361 PHE   A N   1 
ATOM   463  C  CA  . PHE   A 1 65  ? -33.823 -24.074 17.567 1.00 88.63  ? 361 PHE   A CA  1 
ATOM   464  C  C   . PHE   A 1 65  ? -35.053 -24.122 16.668 1.00 93.23  ? 361 PHE   A C   1 
ATOM   465  O  O   . PHE   A 1 65  ? -35.948 -23.276 16.780 1.00 92.46  ? 361 PHE   A O   1 
ATOM   466  C  CB  . PHE   A 1 65  ? -32.626 -23.543 16.782 1.00 84.99  ? 361 PHE   A CB  1 
ATOM   467  C  CG  . PHE   A 1 65  ? -32.925 -22.281 16.010 1.00 80.79  ? 361 PHE   A CG  1 
ATOM   468  C  CD1 . PHE   A 1 65  ? -33.023 -21.059 16.660 1.00 79.17  ? 361 PHE   A CD1 1 
ATOM   469  C  CD2 . PHE   A 1 65  ? -33.132 -22.316 14.641 1.00 80.42  ? 361 PHE   A CD2 1 
ATOM   470  C  CE1 . PHE   A 1 65  ? -33.301 -19.898 15.959 1.00 77.95  ? 361 PHE   A CE1 1 
ATOM   471  C  CE2 . PHE   A 1 65  ? -33.413 -21.152 13.928 1.00 78.75  ? 361 PHE   A CE2 1 
ATOM   472  C  CZ  . PHE   A 1 65  ? -33.495 -19.940 14.590 1.00 77.64  ? 361 PHE   A CZ  1 
ATOM   473  N  N   . LEU   A 1 66  ? -35.100 -25.094 15.747 1.00 93.58  ? 362 LEU   A N   1 
ATOM   474  C  CA  . LEU   A 1 66  ? -36.231 -25.183 14.830 1.00 93.64  ? 362 LEU   A CA  1 
ATOM   475  C  C   . LEU   A 1 66  ? -37.540 -25.377 15.577 1.00 98.69  ? 362 LEU   A C   1 
ATOM   476  O  O   . LEU   A 1 66  ? -38.575 -24.841 15.167 1.00 99.46  ? 362 LEU   A O   1 
ATOM   477  C  CB  . LEU   A 1 66  ? -36.018 -26.329 13.836 1.00 97.02  ? 362 LEU   A CB  1 
ATOM   478  C  CG  . LEU   A 1 66  ? -34.926 -26.121 12.771 1.00 94.85  ? 362 LEU   A CG  1 
ATOM   479  C  CD1 . LEU   A 1 66  ? -34.923 -27.244 11.765 1.00 96.06  ? 362 LEU   A CD1 1 
ATOM   480  C  CD2 . LEU   A 1 66  ? -35.068 -24.770 12.083 1.00 89.41  ? 362 LEU   A CD2 1 
ATOM   481  N  N   . ASP   A 1 67  ? -37.510 -26.123 16.684 1.00 97.81  ? 363 ASP   A N   1 
ATOM   482  C  CA  . ASP   A 1 67  ? -38.727 -26.364 17.455 1.00 101.22 ? 363 ASP   A CA  1 
ATOM   483  C  C   . ASP   A 1 67  ? -39.280 -25.071 18.049 1.00 100.50 ? 363 ASP   A C   1 
ATOM   484  O  O   . ASP   A 1 67  ? -40.501 -24.892 18.131 1.00 103.98 ? 363 ASP   A O   1 
ATOM   485  C  CB  . ASP   A 1 67  ? -38.451 -27.381 18.560 1.00 104.18 ? 363 ASP   A CB  1 
ATOM   486  C  CG  . ASP   A 1 67  ? -38.647 -28.809 18.104 1.00 111.51 ? 363 ASP   A CG  1 
ATOM   487  O  OD1 . ASP   A 1 67  ? -39.807 -29.209 17.857 1.00 118.93 ? 363 ASP   A OD1 1 
ATOM   488  O  OD2 . ASP   A 1 67  ? -37.640 -29.537 17.984 1.00 110.25 ? 363 ASP   A OD2 1 
ATOM   489  N  N   . GLN   A 1 68  ? -38.408 -24.165 18.486 1.00 96.67  ? 364 GLN   A N   1 
ATOM   490  C  CA  . GLN   A 1 68  ? -38.918 -22.927 19.061 1.00 97.26  ? 364 GLN   A CA  1 
ATOM   491  C  C   . GLN   A 1 68  ? -39.291 -21.932 17.972 1.00 97.19  ? 364 GLN   A C   1 
ATOM   492  O  O   . GLN   A 1 68  ? -40.241 -21.157 18.140 1.00 100.62 ? 364 GLN   A O   1 
ATOM   493  C  CB  . GLN   A 1 68  ? -37.899 -22.328 20.041 1.00 92.46  ? 364 GLN   A CB  1 
ATOM   494  C  CG  . GLN   A 1 68  ? -36.642 -21.778 19.391 1.00 90.76  ? 364 GLN   A CG  1 
ATOM   495  C  CD  . GLN   A 1 68  ? -35.502 -21.555 20.374 1.00 87.97  ? 364 GLN   A CD  1 
ATOM   496  O  OE1 . GLN   A 1 68  ? -34.903 -20.464 20.424 1.00 80.36  ? 364 GLN   A OE1 1 
ATOM   497  N  NE2 . GLN   A 1 68  ? -35.186 -22.590 21.154 1.00 88.02  ? 364 GLN   A NE2 1 
ATOM   498  N  N   . TYR   A 1 69  ? -38.592 -21.969 16.837 1.00 95.74  ? 365 TYR   A N   1 
ATOM   499  C  CA  . TYR   A 1 69  ? -38.967 -21.109 15.723 1.00 96.56  ? 365 TYR   A CA  1 
ATOM   500  C  C   . TYR   A 1 69  ? -40.364 -21.442 15.219 1.00 101.62 ? 365 TYR   A C   1 
ATOM   501  O  O   . TYR   A 1 69  ? -41.196 -20.548 15.031 1.00 103.79 ? 365 TYR   A O   1 
ATOM   502  C  CB  . TYR   A 1 69  ? -37.952 -21.223 14.590 1.00 93.22  ? 365 TYR   A CB  1 
ATOM   503  C  CG  . TYR   A 1 69  ? -38.445 -20.534 13.348 1.00 92.51  ? 365 TYR   A CG  1 
ATOM   504  C  CD1 . TYR   A 1 69  ? -38.767 -19.182 13.372 1.00 90.25  ? 365 TYR   A CD1 1 
ATOM   505  C  CD2 . TYR   A 1 69  ? -38.620 -21.236 12.158 1.00 94.97  ? 365 TYR   A CD2 1 
ATOM   506  C  CE1 . TYR   A 1 69  ? -39.238 -18.546 12.238 1.00 89.94  ? 365 TYR   A CE1 1 
ATOM   507  C  CE2 . TYR   A 1 69  ? -39.089 -20.600 11.021 1.00 92.41  ? 365 TYR   A CE2 1 
ATOM   508  C  CZ  . TYR   A 1 69  ? -39.393 -19.257 11.076 1.00 89.82  ? 365 TYR   A CZ  1 
ATOM   509  O  OH  . TYR   A 1 69  ? -39.862 -18.615 9.958  1.00 89.62  ? 365 TYR   A OH  1 
ATOM   510  N  N   . TYR   A 1 70  ? -40.635 -22.724 14.969 1.00 103.08 ? 366 TYR   A N   1 
ATOM   511  C  CA  . TYR   A 1 70  ? -41.967 -23.087 14.498 1.00 108.46 ? 366 TYR   A CA  1 
ATOM   512  C  C   . TYR   A 1 70  ? -42.998 -22.934 15.605 1.00 112.53 ? 366 TYR   A C   1 
ATOM   513  O  O   . TYR   A 1 70  ? -44.173 -22.673 15.325 1.00 118.66 ? 366 TYR   A O   1 
ATOM   514  C  CB  . TYR   A 1 70  ? -41.972 -24.510 13.935 1.00 112.20 ? 366 TYR   A CB  1 
ATOM   515  C  CG  . TYR   A 1 70  ? -41.406 -24.585 12.538 1.00 110.71 ? 366 TYR   A CG  1 
ATOM   516  C  CD1 . TYR   A 1 70  ? -42.209 -24.345 11.429 1.00 113.52 ? 366 TYR   A CD1 1 
ATOM   517  C  CD2 . TYR   A 1 70  ? -40.064 -24.875 12.326 1.00 107.63 ? 366 TYR   A CD2 1 
ATOM   518  C  CE1 . TYR   A 1 70  ? -41.696 -24.401 10.146 1.00 112.03 ? 366 TYR   A CE1 1 
ATOM   519  C  CE2 . TYR   A 1 70  ? -39.537 -24.937 11.045 1.00 106.72 ? 366 TYR   A CE2 1 
ATOM   520  C  CZ  . TYR   A 1 70  ? -40.359 -24.696 9.956  1.00 110.42 ? 366 TYR   A CZ  1 
ATOM   521  O  OH  . TYR   A 1 70  ? -39.849 -24.747 8.667  1.00 104.65 ? 366 TYR   A OH  1 
ATOM   522  N  N   . SER   A 1 71  ? -42.582 -23.088 16.860 1.00 109.64 ? 367 SER   A N   1 
ATOM   523  C  CA  . SER   A 1 71  ? -43.471 -22.739 17.959 1.00 113.70 ? 367 SER   A CA  1 
ATOM   524  C  C   . SER   A 1 71  ? -43.865 -21.269 17.892 1.00 112.26 ? 367 SER   A C   1 
ATOM   525  O  O   . SER   A 1 71  ? -45.009 -20.917 18.199 1.00 118.59 ? 367 SER   A O   1 
ATOM   526  C  CB  . SER   A 1 71  ? -42.805 -23.049 19.300 1.00 113.46 ? 367 SER   A CB  1 
ATOM   527  O  OG  . SER   A 1 71  ? -43.769 -23.360 20.293 1.00 114.48 ? 367 SER   A OG  1 
ATOM   528  N  N   . SER   A 1 72  ? -42.944 -20.403 17.461 1.00 109.22 ? 368 SER   A N   1 
ATOM   529  C  CA  . SER   A 1 72  ? -43.210 -18.970 17.440 1.00 107.85 ? 368 SER   A CA  1 
ATOM   530  C  C   . SER   A 1 72  ? -44.139 -18.551 16.302 1.00 114.17 ? 368 SER   A C   1 
ATOM   531  O  O   . SER   A 1 72  ? -44.864 -17.561 16.447 1.00 116.73 ? 368 SER   A O   1 
ATOM   532  C  CB  . SER   A 1 72  ? -41.891 -18.198 17.355 1.00 101.37 ? 368 SER   A CB  1 
ATOM   533  O  OG  . SER   A 1 72  ? -41.787 -17.475 16.140 1.00 101.67 ? 368 SER   A OG  1 
ATOM   534  N  N   . ILE   A 1 73  ? -44.138 -19.262 15.171 1.00 113.67 ? 369 ILE   A N   1 
ATOM   535  C  CA  . ILE   A 1 73  ? -45.061 -18.936 14.086 1.00 117.41 ? 369 ILE   A CA  1 
ATOM   536  C  C   . ILE   A 1 73  ? -46.322 -19.778 14.239 1.00 124.39 ? 369 ILE   A C   1 
ATOM   537  O  O   . ILE   A 1 73  ? -47.099 -19.933 13.291 1.00 126.66 ? 369 ILE   A O   1 
ATOM   538  C  CB  . ILE   A 1 73  ? -44.418 -19.128 12.694 1.00 115.69 ? 369 ILE   A CB  1 
ATOM   539  C  CG1 . ILE   A 1 73  ? -43.868 -20.543 12.529 1.00 116.47 ? 369 ILE   A CG1 1 
ATOM   540  C  CG2 . ILE   A 1 73  ? -43.313 -18.095 12.453 1.00 108.92 ? 369 ILE   A CG2 1 
ATOM   541  C  CD1 . ILE   A 1 73  ? -43.190 -20.774 11.189 1.00 110.86 ? 369 ILE   A CD1 1 
ATOM   542  N  N   . LYS   A 1 74  ? -46.536 -20.315 15.444 1.00 129.03 ? 370 LYS   A N   1 
ATOM   543  C  CA  . LYS   A 1 74  ? -47.758 -21.038 15.812 1.00 133.21 ? 370 LYS   A CA  1 
ATOM   544  C  C   . LYS   A 1 74  ? -48.045 -22.203 14.864 1.00 139.22 ? 370 LYS   A C   1 
ATOM   545  O  O   . LYS   A 1 74  ? -49.202 -22.588 14.660 1.00 147.87 ? 370 LYS   A O   1 
ATOM   546  C  CB  . LYS   A 1 74  ? -48.959 -20.086 15.891 1.00 135.09 ? 370 LYS   A CB  1 
ATOM   547  C  CG  . LYS   A 1 74  ? -48.586 -18.666 16.327 1.00 135.37 ? 370 LYS   A CG  1 
ATOM   548  C  CD  . LYS   A 1 74  ? -49.222 -18.228 17.640 1.00 135.23 ? 370 LYS   A CD  1 
ATOM   549  C  CE  . LYS   A 1 74  ? -48.510 -16.980 18.165 1.00 136.61 ? 370 LYS   A CE  1 
ATOM   550  N  NZ  . LYS   A 1 74  ? -49.307 -16.199 19.146 1.00 133.69 ? 370 LYS   A NZ  1 
ATOM   551  N  N   . ARG   A 1 75  ? -46.989 -22.762 14.270 1.00 131.97 ? 371 ARG   A N   1 
ATOM   552  C  CA  . ARG   A 1 75  ? -47.080 -24.001 13.509 1.00 131.67 ? 371 ARG   A CA  1 
ATOM   553  C  C   . ARG   A 1 75  ? -46.104 -25.019 14.084 1.00 129.20 ? 371 ARG   A C   1 
ATOM   554  O  O   . ARG   A 1 75  ? -45.287 -25.594 13.356 1.00 127.78 ? 371 ARG   A O   1 
ATOM   555  C  CB  . ARG   A 1 75  ? -46.795 -23.753 12.032 1.00 130.07 ? 371 ARG   A CB  1 
ATOM   556  C  CG  . ARG   A 1 75  ? -47.759 -22.781 11.393 1.00 132.09 ? 371 ARG   A CG  1 
ATOM   557  C  CD  . ARG   A 1 75  ? -47.002 -21.703 10.642 1.00 132.72 ? 371 ARG   A CD  1 
ATOM   558  N  NE  . ARG   A 1 75  ? -47.569 -21.470 9.320  1.00 135.71 ? 371 ARG   A NE  1 
ATOM   559  C  CZ  . ARG   A 1 75  ? -47.303 -22.213 8.257  1.00 140.28 ? 371 ARG   A CZ  1 
ATOM   560  N  NH1 . ARG   A 1 75  ? -46.489 -23.255 8.331  1.00 140.78 ? 371 ARG   A NH1 1 
ATOM   561  N  NH2 . ARG   A 1 75  ? -47.866 -21.904 7.090  1.00 140.94 ? 371 ARG   A NH2 1 
ATOM   562  N  N   . PHE   A 1 76  ? -46.180 -25.226 15.398 1.00 129.49 ? 372 PHE   A N   1 
ATOM   563  C  CA  . PHE   A 1 76  ? -45.308 -26.180 16.066 1.00 127.19 ? 372 PHE   A CA  1 
ATOM   564  C  C   . PHE   A 1 76  ? -45.632 -27.596 15.619 1.00 130.69 ? 372 PHE   A C   1 
ATOM   565  O  O   . PHE   A 1 76  ? -46.790 -28.022 15.653 1.00 130.55 ? 372 PHE   A O   1 
ATOM   566  C  CB  . PHE   A 1 76  ? -45.466 -26.071 17.585 1.00 123.41 ? 372 PHE   A CB  1 
ATOM   567  C  CG  . PHE   A 1 76  ? -44.516 -26.946 18.361 1.00 120.29 ? 372 PHE   A CG  1 
ATOM   568  C  CD1 . PHE   A 1 76  ? -44.697 -28.320 18.429 1.00 120.83 ? 372 PHE   A CD1 1 
ATOM   569  C  CD2 . PHE   A 1 76  ? -43.446 -26.389 19.030 1.00 119.91 ? 372 PHE   A CD2 1 
ATOM   570  C  CE1 . PHE   A 1 76  ? -43.823 -29.117 19.133 1.00 124.52 ? 372 PHE   A CE1 1 
ATOM   571  C  CE2 . PHE   A 1 76  ? -42.575 -27.184 19.750 1.00 123.99 ? 372 PHE   A CE2 1 
ATOM   572  C  CZ  . PHE   A 1 76  ? -42.765 -28.551 19.794 1.00 125.63 ? 372 PHE   A CZ  1 
ATOM   573  N  N   . GLY   A 1 77  ? -44.598 -28.336 15.234 1.00 137.53 ? 373 GLY   A N   1 
ATOM   574  C  CA  . GLY   A 1 77  ? -44.740 -29.752 14.962 1.00 147.18 ? 373 GLY   A CA  1 
ATOM   575  C  C   . GLY   A 1 77  ? -45.630 -30.080 13.781 1.00 149.98 ? 373 GLY   A C   1 
ATOM   576  O  O   . GLY   A 1 77  ? -46.020 -31.237 13.591 1.00 158.68 ? 373 GLY   A O   1 
ATOM   577  N  N   . SER   A 1 78  ? -45.959 -29.072 12.977 1.00 134.90 ? 374 SER   A N   1 
ATOM   578  C  CA  . SER   A 1 78  ? -46.737 -29.304 11.772 1.00 131.90 ? 374 SER   A CA  1 
ATOM   579  C  C   . SER   A 1 78  ? -45.916 -30.113 10.771 1.00 132.71 ? 374 SER   A C   1 
ATOM   580  O  O   . SER   A 1 78  ? -44.778 -30.520 11.032 1.00 130.87 ? 374 SER   A O   1 
ATOM   581  C  CB  . SER   A 1 78  ? -47.186 -27.976 11.163 1.00 129.70 ? 374 SER   A CB  1 
ATOM   582  O  OG  . SER   A 1 78  ? -46.074 -27.156 10.835 1.00 128.32 ? 374 SER   A OG  1 
ATOM   583  N  N   . LYS   A 1 79  ? -46.518 -30.352 9.602  1.00 128.28 ? 375 LYS   A N   1 
ATOM   584  C  CA  . LYS   A 1 79  ? -45.794 -30.999 8.514  1.00 128.70 ? 375 LYS   A CA  1 
ATOM   585  C  C   . LYS   A 1 79  ? -44.685 -30.097 7.988  1.00 123.45 ? 375 LYS   A C   1 
ATOM   586  O  O   . LYS   A 1 79  ? -43.581 -30.570 7.691  1.00 122.89 ? 375 LYS   A O   1 
ATOM   587  C  CB  . LYS   A 1 79  ? -46.763 -31.375 7.395  1.00 131.32 ? 375 LYS   A CB  1 
ATOM   588  C  CG  . LYS   A 1 79  ? -46.176 -32.271 6.311  1.00 136.40 ? 375 LYS   A CG  1 
ATOM   589  C  CD  . LYS   A 1 79  ? -46.253 -33.742 6.695  1.00 139.72 ? 375 LYS   A CD  1 
ATOM   590  C  CE  . LYS   A 1 79  ? -45.842 -34.628 5.531  1.00 141.32 ? 375 LYS   A CE  1 
ATOM   591  N  NZ  . LYS   A 1 79  ? -44.499 -34.242 5.006  1.00 136.44 ? 375 LYS   A NZ  1 
ATOM   592  N  N   . ALA   A 1 80  ? -44.954 -28.793 7.876  1.00 123.84 ? 376 ALA   A N   1 
ATOM   593  C  CA  . ALA   A 1 80  ? -43.917 -27.876 7.416  1.00 122.23 ? 376 ALA   A CA  1 
ATOM   594  C  C   . ALA   A 1 80  ? -42.732 -27.865 8.371  1.00 122.04 ? 376 ALA   A C   1 
ATOM   595  O  O   . ALA   A 1 80  ? -41.590 -27.671 7.938  1.00 120.40 ? 376 ALA   A O   1 
ATOM   596  C  CB  . ALA   A 1 80  ? -44.493 -26.470 7.237  1.00 118.96 ? 376 ALA   A CB  1 
ATOM   597  N  N   . HIS   A 1 81  ? -42.981 -28.098 9.664  1.00 121.67 ? 377 HIS   A N   1 
ATOM   598  C  CA  . HIS   A 1 81  ? -41.903 -28.206 10.644 1.00 121.26 ? 377 HIS   A CA  1 
ATOM   599  C  C   . HIS   A 1 81  ? -41.119 -29.502 10.465 1.00 123.48 ? 377 HIS   A C   1 
ATOM   600  O  O   . HIS   A 1 81  ? -39.888 -29.484 10.346 1.00 120.00 ? 377 HIS   A O   1 
ATOM   601  C  CB  . HIS   A 1 81  ? -42.483 -28.117 12.059 1.00 121.98 ? 377 HIS   A CB  1 
ATOM   602  C  CG  . HIS   A 1 81  ? -41.464 -28.242 13.156 1.00 120.27 ? 377 HIS   A CG  1 
ATOM   603  N  ND1 . HIS   A 1 81  ? -41.817 -28.350 14.485 1.00 119.18 ? 377 HIS   A ND1 1 
ATOM   604  C  CD2 . HIS   A 1 81  ? -40.109 -28.265 13.127 1.00 115.94 ? 377 HIS   A CD2 1 
ATOM   605  C  CE1 . HIS   A 1 81  ? -40.727 -28.442 15.224 1.00 114.38 ? 377 HIS   A CE1 1 
ATOM   606  N  NE2 . HIS   A 1 81  ? -39.677 -28.392 14.425 1.00 113.52 ? 377 HIS   A NE2 1 
ATOM   607  N  N   . MET   A 1 82  ? -41.819 -30.642 10.451 1.00 133.18 ? 378 MET   A N   1 
ATOM   608  C  CA  . MET   A 1 82  ? -41.144 -31.936 10.363 1.00 133.42 ? 378 MET   A CA  1 
ATOM   609  C  C   . MET   A 1 82  ? -40.342 -32.089 9.075  1.00 131.03 ? 378 MET   A C   1 
ATOM   610  O  O   . MET   A 1 82  ? -39.345 -32.822 9.053  1.00 132.02 ? 378 MET   A O   1 
ATOM   611  C  CB  . MET   A 1 82  ? -42.162 -33.071 10.486 1.00 140.51 ? 378 MET   A CB  1 
ATOM   612  C  CG  . MET   A 1 82  ? -42.551 -33.385 11.924 1.00 148.71 ? 378 MET   A CG  1 
ATOM   613  S  SD  . MET   A 1 82  ? -41.125 -33.886 12.914 1.00 150.14 ? 378 MET   A SD  1 
ATOM   614  C  CE  . MET   A 1 82  ? -40.534 -35.284 11.955 1.00 153.04 ? 378 MET   A CE  1 
ATOM   615  N  N   . ASP   A 1 83  ? -40.755 -31.427 7.992  1.00 122.53 ? 379 ASP   A N   1 
ATOM   616  C  CA  . ASP   A 1 83  ? -39.969 -31.508 6.768  1.00 121.44 ? 379 ASP   A CA  1 
ATOM   617  C  C   . ASP   A 1 83  ? -38.712 -30.661 6.867  1.00 115.84 ? 379 ASP   A C   1 
ATOM   618  O  O   . ASP   A 1 83  ? -37.649 -31.059 6.376  1.00 112.19 ? 379 ASP   A O   1 
ATOM   619  C  CB  . ASP   A 1 83  ? -40.816 -31.100 5.569  1.00 121.17 ? 379 ASP   A CB  1 
ATOM   620  C  CG  . ASP   A 1 83  ? -41.674 -32.231 5.078  1.00 123.43 ? 379 ASP   A CG  1 
ATOM   621  O  OD1 . ASP   A 1 83  ? -41.115 -33.309 4.783  1.00 129.06 ? 379 ASP   A OD1 1 
ATOM   622  O  OD2 . ASP   A 1 83  ? -42.910 -32.062 5.019  1.00 127.13 ? 379 ASP   A OD2 1 
ATOM   623  N  N   . ARG   A 1 84  ? -38.815 -29.497 7.512  1.00 116.44 ? 380 ARG   A N   1 
ATOM   624  C  CA  . ARG   A 1 84  ? -37.641 -28.680 7.794  1.00 109.40 ? 380 ARG   A CA  1 
ATOM   625  C  C   . ARG   A 1 84  ? -36.700 -29.366 8.777  1.00 109.36 ? 380 ARG   A C   1 
ATOM   626  O  O   . ARG   A 1 84  ? -35.481 -29.173 8.706  1.00 108.14 ? 380 ARG   A O   1 
ATOM   627  C  CB  . ARG   A 1 84  ? -38.074 -27.326 8.347  1.00 105.63 ? 380 ARG   A CB  1 
ATOM   628  C  CG  . ARG   A 1 84  ? -36.936 -26.391 8.621  1.00 99.06  ? 380 ARG   A CG  1 
ATOM   629  C  CD  . ARG   A 1 84  ? -36.586 -25.619 7.385  1.00 97.87  ? 380 ARG   A CD  1 
ATOM   630  N  NE  . ARG   A 1 84  ? -35.414 -24.782 7.608  1.00 93.17  ? 380 ARG   A NE  1 
ATOM   631  C  CZ  . ARG   A 1 84  ? -34.220 -25.050 7.102  1.00 91.83  ? 380 ARG   A CZ  1 
ATOM   632  N  NH1 . ARG   A 1 84  ? -34.022 -26.100 6.325  1.00 90.04  ? 380 ARG   A NH1 1 
ATOM   633  N  NH2 . ARG   A 1 84  ? -33.201 -24.242 7.378  1.00 84.13  ? 380 ARG   A NH2 1 
ATOM   634  N  N   . LEU   A 1 85  ? -37.243 -30.144 9.713  1.00 112.19 ? 381 LEU   A N   1 
ATOM   635  C  CA  . LEU   A 1 85  ? -36.395 -30.970 10.563 1.00 114.11 ? 381 LEU   A CA  1 
ATOM   636  C  C   . LEU   A 1 85  ? -35.684 -32.039 9.738  1.00 114.79 ? 381 LEU   A C   1 
ATOM   637  O  O   . LEU   A 1 85  ? -34.474 -32.249 9.882  1.00 113.75 ? 381 LEU   A O   1 
ATOM   638  C  CB  . LEU   A 1 85  ? -37.236 -31.606 11.671 1.00 116.86 ? 381 LEU   A CB  1 
ATOM   639  C  CG  . LEU   A 1 85  ? -36.634 -31.680 13.077 1.00 113.56 ? 381 LEU   A CG  1 
ATOM   640  C  CD1 . LEU   A 1 85  ? -36.650 -30.321 13.754 1.00 109.62 ? 381 LEU   A CD1 1 
ATOM   641  C  CD2 . LEU   A 1 85  ? -37.378 -32.704 13.921 1.00 116.96 ? 381 LEU   A CD2 1 
ATOM   642  N  N   . GLU   A 1 86  ? -36.425 -32.724 8.862  1.00 115.88 ? 382 GLU   A N   1 
ATOM   643  C  CA  . GLU   A 1 86  ? -35.808 -33.685 7.951  1.00 115.62 ? 382 GLU   A CA  1 
ATOM   644  C  C   . GLU   A 1 86  ? -34.808 -33.002 7.029  1.00 111.59 ? 382 GLU   A C   1 
ATOM   645  O  O   . GLU   A 1 86  ? -33.697 -33.504 6.817  1.00 115.29 ? 382 GLU   A O   1 
ATOM   646  C  CB  . GLU   A 1 86  ? -36.884 -34.386 7.122  1.00 120.98 ? 382 GLU   A CB  1 
ATOM   647  C  CG  . GLU   A 1 86  ? -36.361 -35.495 6.232  1.00 124.01 ? 382 GLU   A CG  1 
ATOM   648  C  CD  . GLU   A 1 86  ? -36.415 -36.852 6.910  1.00 130.56 ? 382 GLU   A CD  1 
ATOM   649  O  OE1 . GLU   A 1 86  ? -36.685 -36.884 8.127  1.00 132.02 ? 382 GLU   A OE1 1 
ATOM   650  O  OE2 . GLU   A 1 86  ? -36.199 -37.884 6.234  1.00 134.25 ? 382 GLU   A OE2 1 
ATOM   651  N  N   . GLU   A 1 87  ? -35.192 -31.855 6.470  1.00 107.64 ? 383 GLU   A N   1 
ATOM   652  C  CA  . GLU   A 1 87  ? -34.319 -31.133 5.555  1.00 104.74 ? 383 GLU   A CA  1 
ATOM   653  C  C   . GLU   A 1 87  ? -32.968 -30.826 6.194  1.00 109.15 ? 383 GLU   A C   1 
ATOM   654  O  O   . GLU   A 1 87  ? -31.921 -31.015 5.563  1.00 103.69 ? 383 GLU   A O   1 
ATOM   655  C  CB  . GLU   A 1 87  ? -35.015 -29.851 5.096  1.00 98.72  ? 383 GLU   A CB  1 
ATOM   656  C  CG  . GLU   A 1 87  ? -34.271 -29.076 4.031  1.00 100.32 ? 383 GLU   A CG  1 
ATOM   657  C  CD  . GLU   A 1 87  ? -35.111 -27.957 3.434  1.00 101.35 ? 383 GLU   A CD  1 
ATOM   658  O  OE1 . GLU   A 1 87  ? -35.739 -27.208 4.213  1.00 96.47  ? 383 GLU   A OE1 1 
ATOM   659  O  OE2 . GLU   A 1 87  ? -35.150 -27.835 2.178  1.00 99.87  ? 383 GLU   A OE2 1 
ATOM   660  N  N   . VAL   A 1 88  ? -32.965 -30.368 7.454  1.00 109.14 ? 384 VAL   A N   1 
ATOM   661  C  CA  . VAL   A 1 88  ? -31.711 -29.950 8.079  1.00 108.03 ? 384 VAL   A CA  1 
ATOM   662  C  C   . VAL   A 1 88  ? -30.887 -31.154 8.519  1.00 113.17 ? 384 VAL   A C   1 
ATOM   663  O  O   . VAL   A 1 88  ? -29.656 -31.151 8.399  1.00 110.82 ? 384 VAL   A O   1 
ATOM   664  C  CB  . VAL   A 1 88  ? -31.982 -28.989 9.251  1.00 101.97 ? 384 VAL   A CB  1 
ATOM   665  C  CG1 . VAL   A 1 88  ? -30.688 -28.689 9.990  1.00 101.00 ? 384 VAL   A CG1 1 
ATOM   666  C  CG2 . VAL   A 1 88  ? -32.601 -27.699 8.744  1.00 94.72  ? 384 VAL   A CG2 1 
ATOM   667  N  N   . ASN   A 1 89  ? -31.543 -32.190 9.047  1.00 119.02 ? 385 ASN   A N   1 
ATOM   668  C  CA  . ASN   A 1 89  ? -30.873 -33.464 9.294  1.00 120.19 ? 385 ASN   A CA  1 
ATOM   669  C  C   . ASN   A 1 89  ? -30.122 -33.936 8.047  1.00 119.52 ? 385 ASN   A C   1 
ATOM   670  O  O   . ASN   A 1 89  ? -28.916 -34.201 8.088  1.00 124.99 ? 385 ASN   A O   1 
ATOM   671  C  CB  . ASN   A 1 89  ? -31.907 -34.509 9.734  1.00 126.07 ? 385 ASN   A CB  1 
ATOM   672  C  CG  . ASN   A 1 89  ? -31.281 -35.696 10.462 1.00 133.09 ? 385 ASN   A CG  1 
ATOM   673  O  OD1 . ASN   A 1 89  ? -31.182 -36.797 9.913  1.00 137.42 ? 385 ASN   A OD1 1 
ATOM   674  N  ND2 . ASN   A 1 89  ? -30.870 -35.477 11.706 1.00 132.92 ? 385 ASN   A ND2 1 
ATOM   675  N  N   . LYS   A 1 90  ? -30.825 -34.018 6.917  1.00 117.55 ? 386 LYS   A N   1 
ATOM   676  C  CA  . LYS   A 1 90  ? -30.191 -34.488 5.689  1.00 120.86 ? 386 LYS   A CA  1 
ATOM   677  C  C   . LYS   A 1 90  ? -29.033 -33.585 5.269  1.00 119.55 ? 386 LYS   A C   1 
ATOM   678  O  O   . LYS   A 1 90  ? -27.993 -34.069 4.808  1.00 120.52 ? 386 LYS   A O   1 
ATOM   679  C  CB  . LYS   A 1 90  ? -31.233 -34.594 4.574  1.00 123.22 ? 386 LYS   A CB  1 
ATOM   680  C  CG  . LYS   A 1 90  ? -32.232 -35.732 4.773  1.00 128.49 ? 386 LYS   A CG  1 
ATOM   681  C  CD  . LYS   A 1 90  ? -33.271 -35.814 3.654  1.00 128.55 ? 386 LYS   A CD  1 
ATOM   682  C  CE  . LYS   A 1 90  ? -34.170 -37.032 3.868  1.00 131.36 ? 386 LYS   A CE  1 
ATOM   683  N  NZ  . LYS   A 1 90  ? -35.401 -37.007 3.024  1.00 136.52 ? 386 LYS   A NZ  1 
ATOM   684  N  N   . GLU   A 1 91  ? -29.180 -32.269 5.434  1.00 115.68 ? 387 GLU   A N   1 
ATOM   685  C  CA  . GLU   A 1 91  ? -28.079 -31.380 5.075  1.00 112.81 ? 387 GLU   A CA  1 
ATOM   686  C  C   . GLU   A 1 91  ? -26.896 -31.522 6.033  1.00 115.61 ? 387 GLU   A C   1 
ATOM   687  O  O   . GLU   A 1 91  ? -25.740 -31.441 5.600  1.00 116.73 ? 387 GLU   A O   1 
ATOM   688  C  CB  . GLU   A 1 91  ? -28.562 -29.931 5.033  1.00 107.24 ? 387 GLU   A CB  1 
ATOM   689  C  CG  . GLU   A 1 91  ? -27.546 -28.987 4.445  1.00 103.64 ? 387 GLU   A CG  1 
ATOM   690  C  CD  . GLU   A 1 91  ? -28.008 -27.551 4.450  1.00 99.85  ? 387 GLU   A CD  1 
ATOM   691  O  OE1 . GLU   A 1 91  ? -29.124 -27.270 4.945  1.00 96.19  ? 387 GLU   A OE1 1 
ATOM   692  O  OE2 . GLU   A 1 91  ? -27.241 -26.699 3.959  1.00 98.71  ? 387 GLU   A OE2 1 
ATOM   693  N  N   . ILE   A 1 92  ? -27.153 -31.735 7.328  1.00 116.45 ? 388 ILE   A N   1 
ATOM   694  C  CA  . ILE   A 1 92  ? -26.059 -32.053 8.244  1.00 118.25 ? 388 ILE   A CA  1 
ATOM   695  C  C   . ILE   A 1 92  ? -25.493 -33.447 7.976  1.00 122.28 ? 388 ILE   A C   1 
ATOM   696  O  O   . ILE   A 1 92  ? -24.357 -33.739 8.360  1.00 124.97 ? 388 ILE   A O   1 
ATOM   697  C  CB  . ILE   A 1 92  ? -26.511 -31.909 9.709  1.00 114.35 ? 388 ILE   A CB  1 
ATOM   698  C  CG1 . ILE   A 1 92  ? -26.981 -30.482 9.993  1.00 109.48 ? 388 ILE   A CG1 1 
ATOM   699  C  CG2 . ILE   A 1 92  ? -25.375 -32.232 10.670 1.00 116.59 ? 388 ILE   A CG2 1 
ATOM   700  C  CD1 . ILE   A 1 92  ? -27.659 -30.328 11.336 1.00 107.97 ? 388 ILE   A CD1 1 
ATOM   701  N  N   . GLU   A 1 93  ? -26.235 -34.327 7.321  1.00 121.73 ? 389 GLU   A N   1 
ATOM   702  C  CA  . GLU   A 1 93  ? -25.590 -35.541 6.842  1.00 125.94 ? 389 GLU   A CA  1 
ATOM   703  C  C   . GLU   A 1 93  ? -24.604 -35.147 5.751  1.00 124.63 ? 389 GLU   A C   1 
ATOM   704  O  O   . GLU   A 1 93  ? -23.384 -35.220 5.942  1.00 125.19 ? 389 GLU   A O   1 
ATOM   705  C  CB  . GLU   A 1 93  ? -26.620 -36.541 6.323  1.00 127.46 ? 389 GLU   A CB  1 
ATOM   706  C  CG  . GLU   A 1 93  ? -27.634 -36.982 7.361  1.00 130.91 ? 389 GLU   A CG  1 
ATOM   707  C  CD  . GLU   A 1 93  ? -27.086 -38.032 8.316  1.00 139.08 ? 389 GLU   A CD  1 
ATOM   708  O  OE1 . GLU   A 1 93  ? -26.120 -38.738 7.936  1.00 140.38 ? 389 GLU   A OE1 1 
ATOM   709  O  OE2 . GLU   A 1 93  ? -27.626 -38.150 9.443  1.00 139.93 ? 389 GLU   A OE2 1 
ATOM   710  N  N   . SER   A 1 94  ? -25.148 -34.680 4.625  1.00 127.57 ? 390 SER   A N   1 
ATOM   711  C  CA  . SER   A 1 94  ? -24.417 -34.290 3.424  1.00 122.66 ? 390 SER   A CA  1 
ATOM   712  C  C   . SER   A 1 94  ? -23.196 -33.416 3.694  1.00 124.79 ? 390 SER   A C   1 
ATOM   713  O  O   . SER   A 1 94  ? -22.065 -33.811 3.383  1.00 126.37 ? 390 SER   A O   1 
ATOM   714  C  CB  . SER   A 1 94  ? -25.371 -33.558 2.481  1.00 123.81 ? 390 SER   A CB  1 
ATOM   715  O  OG  . SER   A 1 94  ? -24.665 -32.796 1.520  1.00 132.15 ? 390 SER   A OG  1 
ATOM   716  N  N   . THR   A 1 95  ? -23.419 -32.225 4.251  1.00 123.66 ? 391 THR   A N   1 
ATOM   717  C  CA  . THR   A 1 95  ? -22.369 -31.229 4.434  1.00 122.67 ? 391 THR   A CA  1 
ATOM   718  C  C   . THR   A 1 95  ? -21.866 -31.133 5.870  1.00 122.99 ? 391 THR   A C   1 
ATOM   719  O  O   . THR   A 1 95  ? -20.975 -30.323 6.142  1.00 120.05 ? 391 THR   A O   1 
ATOM   720  C  CB  . THR   A 1 95  ? -22.859 -29.839 3.993  1.00 117.89 ? 391 THR   A CB  1 
ATOM   721  O  OG1 . THR   A 1 95  ? -23.808 -29.336 4.947  1.00 115.39 ? 391 THR   A OG1 1 
ATOM   722  C  CG2 . THR   A 1 95  ? -23.510 -29.899 2.617  1.00 115.21 ? 391 THR   A CG2 1 
ATOM   723  N  N   . SER   A 1 96  ? -22.418 -31.920 6.793  1.00 130.34 ? 392 SER   A N   1 
ATOM   724  C  CA  . SER   A 1 96  ? -22.070 -31.867 8.215  1.00 131.61 ? 392 SER   A CA  1 
ATOM   725  C  C   . SER   A 1 96  ? -22.295 -30.482 8.814  1.00 128.05 ? 392 SER   A C   1 
ATOM   726  O  O   . SER   A 1 96  ? -21.758 -30.161 9.879  1.00 131.72 ? 392 SER   A O   1 
ATOM   727  C  CB  . SER   A 1 96  ? -20.631 -32.336 8.462  1.00 136.58 ? 392 SER   A CB  1 
ATOM   728  O  OG  . SER   A 1 96  ? -19.692 -31.444 7.894  1.00 136.08 ? 392 SER   A OG  1 
ATOM   729  N  N   . THR   A 1 97  ? -23.080 -29.657 8.131  1.00 116.02 ? 393 THR   A N   1 
ATOM   730  C  CA  . THR   A 1 97  ? -23.540 -28.372 8.631  1.00 109.48 ? 393 THR   A CA  1 
ATOM   731  C  C   . THR   A 1 97  ? -24.858 -28.065 7.927  1.00 105.23 ? 393 THR   A C   1 
ATOM   732  O  O   . THR   A 1 97  ? -25.461 -28.943 7.301  1.00 106.87 ? 393 THR   A O   1 
ATOM   733  C  CB  . THR   A 1 97  ? -22.478 -27.285 8.421  1.00 104.80 ? 393 THR   A CB  1 
ATOM   734  O  OG1 . THR   A 1 97  ? -23.035 -26.003 8.737  1.00 100.52 ? 393 THR   A OG1 1 
ATOM   735  C  CG2 . THR   A 1 97  ? -21.980 -27.276 6.999  1.00 108.72 ? 393 THR   A CG2 1 
ATOM   736  N  N   . TYR   A 1 98  ? -25.327 -26.827 8.034  1.00 95.91  ? 394 TYR   A N   1 
ATOM   737  C  CA  . TYR   A 1 98  ? -26.563 -26.453 7.358  1.00 91.96  ? 394 TYR   A CA  1 
ATOM   738  C  C   . TYR   A 1 98  ? -26.636 -24.932 7.251  1.00 88.65  ? 394 TYR   A C   1 
ATOM   739  O  O   . TYR   A 1 98  ? -25.764 -24.205 7.735  1.00 87.35  ? 394 TYR   A O   1 
ATOM   740  C  CB  . TYR   A 1 98  ? -27.790 -27.047 8.066  1.00 92.65  ? 394 TYR   A CB  1 
ATOM   741  C  CG  . TYR   A 1 98  ? -28.120 -26.436 9.406  1.00 88.05  ? 394 TYR   A CG  1 
ATOM   742  C  CD1 . TYR   A 1 98  ? -27.480 -26.863 10.562 1.00 92.18  ? 394 TYR   A CD1 1 
ATOM   743  C  CD2 . TYR   A 1 98  ? -29.089 -25.445 9.520  1.00 87.64  ? 394 TYR   A CD2 1 
ATOM   744  C  CE1 . TYR   A 1 98  ? -27.784 -26.322 11.786 1.00 88.51  ? 394 TYR   A CE1 1 
ATOM   745  C  CE2 . TYR   A 1 98  ? -29.399 -24.882 10.749 1.00 83.35  ? 394 TYR   A CE2 1 
ATOM   746  C  CZ  . TYR   A 1 98  ? -28.744 -25.331 11.877 1.00 85.47  ? 394 TYR   A CZ  1 
ATOM   747  O  OH  . TYR   A 1 98  ? -29.044 -24.783 13.104 1.00 81.82  ? 394 TYR   A OH  1 
ATOM   748  N  N   . GLN   A 1 99  ? -27.696 -24.462 6.606  1.00 85.15  ? 395 GLN   A N   1 
ATOM   749  C  CA  . GLN   A 1 99  ? -27.875 -23.063 6.252  1.00 81.50  ? 395 GLN   A CA  1 
ATOM   750  C  C   . GLN   A 1 99  ? -29.265 -22.640 6.682  1.00 79.44  ? 395 GLN   A C   1 
ATOM   751  O  O   . GLN   A 1 99  ? -30.247 -23.336 6.403  1.00 78.08  ? 395 GLN   A O   1 
ATOM   752  C  CB  . GLN   A 1 99  ? -27.710 -22.838 4.731  1.00 80.28  ? 395 GLN   A CB  1 
ATOM   753  C  CG  . GLN   A 1 99  ? -26.334 -23.166 4.170  1.00 78.15  ? 395 GLN   A CG  1 
ATOM   754  C  CD  . GLN   A 1 99  ? -25.244 -22.232 4.667  1.00 77.67  ? 395 GLN   A CD  1 
ATOM   755  O  OE1 . GLN   A 1 99  ? -25.480 -21.042 4.912  1.00 82.01  ? 395 GLN   A OE1 1 
ATOM   756  N  NE2 . GLN   A 1 99  ? -24.043 -22.774 4.844  1.00 75.52  ? 395 GLN   A NE2 1 
ATOM   757  N  N   . LEU   A 1 100 ? -29.350 -21.490 7.326  1.00 78.71  ? 396 LEU   A N   1 
ATOM   758  C  CA  . LEU   A 1 100 ? -30.624 -20.992 7.812  1.00 75.67  ? 396 LEU   A CA  1 
ATOM   759  C  C   . LEU   A 1 100 ? -31.425 -20.358 6.688  1.00 75.39  ? 396 LEU   A C   1 
ATOM   760  O  O   . LEU   A 1 100 ? -30.864 -19.695 5.811  1.00 74.53  ? 396 LEU   A O   1 
ATOM   761  C  CB  . LEU   A 1 100 ? -30.393 -19.963 8.915  1.00 72.40  ? 396 LEU   A CB  1 
ATOM   762  C  CG  . LEU   A 1 100 ? -29.653 -20.456 10.160 1.00 74.36  ? 396 LEU   A CG  1 
ATOM   763  C  CD1 . LEU   A 1 100 ? -29.142 -19.269 10.961 1.00 72.64  ? 396 LEU   A CD1 1 
ATOM   764  C  CD2 . LEU   A 1 100 ? -30.577 -21.320 11.002 1.00 75.90  ? 396 LEU   A CD2 1 
ATOM   765  N  N   . LYS   A 1 101 ? -32.741 -20.566 6.723  1.00 77.49  ? 397 LYS   A N   1 
ATOM   766  C  CA  . LYS   A 1 101 ? -33.655 -19.732 5.958  1.00 78.53  ? 397 LYS   A CA  1 
ATOM   767  C  C   . LYS   A 1 101 ? -33.499 -18.278 6.373  1.00 77.12  ? 397 LYS   A C   1 
ATOM   768  O  O   . LYS   A 1 101 ? -33.081 -17.973 7.492  1.00 75.28  ? 397 LYS   A O   1 
ATOM   769  C  CB  . LYS   A 1 101 ? -35.098 -20.175 6.188  1.00 79.88  ? 397 LYS   A CB  1 
ATOM   770  C  CG  . LYS   A 1 101 ? -35.400 -21.571 5.725  1.00 80.72  ? 397 LYS   A CG  1 
ATOM   771  C  CD  . LYS   A 1 101 ? -35.572 -21.581 4.223  1.00 85.63  ? 397 LYS   A CD  1 
ATOM   772  C  CE  . LYS   A 1 101 ? -35.093 -22.875 3.624  1.00 87.05  ? 397 LYS   A CE  1 
ATOM   773  N  NZ  . LYS   A 1 101 ? -34.631 -22.635 2.224  1.00 81.46  ? 397 LYS   A NZ  1 
ATOM   774  N  N   . ASP   A 1 102 ? -33.847 -17.372 5.459  1.00 77.11  ? 398 ASP   A N   1 
ATOM   775  C  CA  . ASP   A 1 102 ? -33.871 -15.959 5.824  1.00 74.37  ? 398 ASP   A CA  1 
ATOM   776  C  C   . ASP   A 1 102 ? -34.753 -15.730 7.047  1.00 77.10  ? 398 ASP   A C   1 
ATOM   777  O  O   . ASP   A 1 102 ? -34.357 -15.031 7.987  1.00 70.67  ? 398 ASP   A O   1 
ATOM   778  C  CB  . ASP   A 1 102 ? -34.362 -15.111 4.652  1.00 80.81  ? 398 ASP   A CB  1 
ATOM   779  C  CG  . ASP   A 1 102 ? -33.362 -15.049 3.511  1.00 81.06  ? 398 ASP   A CG  1 
ATOM   780  O  OD1 . ASP   A 1 102 ? -32.323 -15.743 3.581  1.00 80.92  ? 398 ASP   A OD1 1 
ATOM   781  O  OD2 . ASP   A 1 102 ? -33.616 -14.297 2.548  1.00 84.09  ? 398 ASP   A OD2 1 
ATOM   782  N  N   . THR   A 1 103 ? -35.944 -16.335 7.064  1.00 76.84  ? 399 THR   A N   1 
ATOM   783  C  CA  . THR   A 1 103 ? -36.827 -16.193 8.219  1.00 76.13  ? 399 THR   A CA  1 
ATOM   784  C  C   . THR   A 1 103 ? -36.169 -16.716 9.493  1.00 76.10  ? 399 THR   A C   1 
ATOM   785  O  O   . THR   A 1 103 ? -36.237 -16.076 10.553 1.00 75.40  ? 399 THR   A O   1 
ATOM   786  C  CB  . THR   A 1 103 ? -38.132 -16.933 7.954  1.00 80.31  ? 399 THR   A CB  1 
ATOM   787  O  OG1 . THR   A 1 103 ? -37.839 -18.275 7.543  1.00 80.89  ? 399 THR   A OG1 1 
ATOM   788  C  CG2 . THR   A 1 103 ? -38.913 -16.233 6.857  1.00 75.54  ? 399 THR   A CG2 1 
ATOM   789  N  N   . GLU   A 1 104 ? -35.524 -17.880 9.406  1.00 78.50  ? 400 GLU   A N   1 
ATOM   790  C  CA  . GLU   A 1 104 ? -34.842 -18.447 10.564 1.00 75.50  ? 400 GLU   A CA  1 
ATOM   791  C  C   . GLU   A 1 104 ? -33.726 -17.535 11.053 1.00 72.82  ? 400 GLU   A C   1 
ATOM   792  O  O   . GLU   A 1 104 ? -33.479 -17.420 12.267 1.00 71.43  ? 400 GLU   A O   1 
ATOM   793  C  CB  . GLU   A 1 104 ? -34.296 -19.822 10.197 1.00 77.02  ? 400 GLU   A CB  1 
ATOM   794  C  CG  . GLU   A 1 104 ? -35.371 -20.854 10.006 1.00 80.09  ? 400 GLU   A CG  1 
ATOM   795  C  CD  . GLU   A 1 104 ? -34.856 -22.069 9.278  1.00 83.15  ? 400 GLU   A CD  1 
ATOM   796  O  OE1 . GLU   A 1 104 ? -33.643 -22.090 8.979  1.00 81.58  ? 400 GLU   A OE1 1 
ATOM   797  O  OE2 . GLU   A 1 104 ? -35.652 -22.994 9.003  1.00 86.14  ? 400 GLU   A OE2 1 
ATOM   798  N  N   . LEU   A 1 105 ? -33.051 -16.868 10.118 1.00 72.00  ? 401 LEU   A N   1 
ATOM   799  C  CA  . LEU   A 1 105 ? -31.950 -15.979 10.469 1.00 71.76  ? 401 LEU   A CA  1 
ATOM   800  C  C   . LEU   A 1 105 ? -32.458 -14.755 11.220 1.00 70.32  ? 401 LEU   A C   1 
ATOM   801  O  O   . LEU   A 1 105 ? -31.933 -14.408 12.283 1.00 65.46  ? 401 LEU   A O   1 
ATOM   802  C  CB  . LEU   A 1 105 ? -31.200 -15.561 9.202  1.00 69.12  ? 401 LEU   A CB  1 
ATOM   803  C  CG  . LEU   A 1 105 ? -29.864 -14.846 9.401  1.00 67.61  ? 401 LEU   A CG  1 
ATOM   804  C  CD1 . LEU   A 1 105 ? -28.782 -15.797 9.898  1.00 66.59  ? 401 LEU   A CD1 1 
ATOM   805  C  CD2 . LEU   A 1 105 ? -29.463 -14.189 8.087  1.00 65.12  ? 401 LEU   A CD2 1 
ATOM   806  N  N   . ILE   A 1 106 ? -33.519 -14.120 10.706 1.00 70.68  ? 402 ILE   A N   1 
ATOM   807  C  CA  . ILE   A 1 106 ? -34.087 -12.937 11.368 1.00 70.08  ? 402 ILE   A CA  1 
ATOM   808  C  C   . ILE   A 1 106 ? -34.621 -13.293 12.755 1.00 69.40  ? 402 ILE   A C   1 
ATOM   809  O  O   . ILE   A 1 106 ? -34.461 -12.527 13.723 1.00 67.41  ? 402 ILE   A O   1 
ATOM   810  C  CB  . ILE   A 1 106 ? -35.177 -12.316 10.466 1.00 68.84  ? 402 ILE   A CB  1 
ATOM   811  C  CG1 . ILE   A 1 106 ? -34.555 -11.873 9.139  1.00 65.69  ? 402 ILE   A CG1 1 
ATOM   812  C  CG2 . ILE   A 1 106 ? -35.841 -11.127 11.135 1.00 66.75  ? 402 ILE   A CG2 1 
ATOM   813  C  CD1 . ILE   A 1 106 ? -35.562 -11.547 8.034  1.00 65.85  ? 402 ILE   A CD1 1 
ATOM   814  N  N   . TYR   A 1 107 ? -35.256 -14.461 12.878 1.00 68.45  ? 403 TYR   A N   1 
ATOM   815  C  CA  . TYR   A 1 107 ? -35.745 -14.920 14.175 1.00 70.16  ? 403 TYR   A CA  1 
ATOM   816  C  C   . TYR   A 1 107 ? -34.587 -15.143 15.143 1.00 71.98  ? 403 TYR   A C   1 
ATOM   817  O  O   . TYR   A 1 107 ? -34.542 -14.557 16.234 1.00 66.63  ? 403 TYR   A O   1 
ATOM   818  C  CB  . TYR   A 1 107 ? -36.568 -16.203 14.011 1.00 72.87  ? 403 TYR   A CB  1 
ATOM   819  C  CG  . TYR   A 1 107 ? -36.950 -16.855 15.335 1.00 76.46  ? 403 TYR   A CG  1 
ATOM   820  C  CD1 . TYR   A 1 107 ? -36.066 -17.699 16.004 1.00 76.62  ? 403 TYR   A CD1 1 
ATOM   821  C  CD2 . TYR   A 1 107 ? -38.196 -16.638 15.905 1.00 79.91  ? 403 TYR   A CD2 1 
ATOM   822  C  CE1 . TYR   A 1 107 ? -36.403 -18.291 17.215 1.00 79.58  ? 403 TYR   A CE1 1 
ATOM   823  C  CE2 . TYR   A 1 107 ? -38.549 -17.233 17.122 1.00 82.51  ? 403 TYR   A CE2 1 
ATOM   824  C  CZ  . TYR   A 1 107 ? -37.644 -18.050 17.771 1.00 82.47  ? 403 TYR   A CZ  1 
ATOM   825  O  OH  . TYR   A 1 107 ? -37.984 -18.642 18.970 1.00 84.23  ? 403 TYR   A OH  1 
ATOM   826  N  N   . GLY   A 1 108 ? -33.641 -16.006 14.755 1.00 70.40  ? 404 GLY   A N   1 
ATOM   827  C  CA  . GLY   A 1 108 ? -32.474 -16.248 15.591 1.00 68.11  ? 404 GLY   A CA  1 
ATOM   828  C  C   . GLY   A 1 108 ? -31.799 -14.970 16.041 1.00 66.18  ? 404 GLY   A C   1 
ATOM   829  O  O   . GLY   A 1 108 ? -31.502 -14.791 17.220 1.00 63.80  ? 404 GLY   A O   1 
ATOM   830  N  N   . ALA   A 1 109 ? -31.574 -14.048 15.109 1.00 66.11  ? 405 ALA   A N   1 
ATOM   831  C  CA  . ALA   A 1 109 ? -30.902 -12.801 15.453 1.00 63.73  ? 405 ALA   A CA  1 
ATOM   832  C  C   . ALA   A 1 109 ? -31.700 -12.010 16.487 1.00 65.77  ? 405 ALA   A C   1 
ATOM   833  O  O   . ALA   A 1 109 ? -31.150 -11.547 17.498 1.00 60.84  ? 405 ALA   A O   1 
ATOM   834  C  CB  . ALA   A 1 109 ? -30.677 -11.980 14.182 1.00 64.58  ? 405 ALA   A CB  1 
ATOM   835  N  N   . LYS   A 1 110 ? -33.005 -11.846 16.255 1.00 65.93  ? 406 LYS   A N   1 
ATOM   836  C  CA  . LYS   A 1 110 ? -33.811 -11.061 17.185 1.00 65.99  ? 406 LYS   A CA  1 
ATOM   837  C  C   . LYS   A 1 110 ? -33.806 -11.680 18.569 1.00 65.10  ? 406 LYS   A C   1 
ATOM   838  O  O   . LYS   A 1 110 ? -33.800 -10.959 19.586 1.00 63.31  ? 406 LYS   A O   1 
ATOM   839  C  CB  . LYS   A 1 110 ? -35.246 -10.938 16.666 1.00 65.30  ? 406 LYS   A CB  1 
ATOM   840  C  CG  . LYS   A 1 110 ? -35.385 -9.975  15.505 1.00 66.11  ? 406 LYS   A CG  1 
ATOM   841  C  CD  . LYS   A 1 110 ? -36.835 -9.782  15.105 1.00 66.17  ? 406 LYS   A CD  1 
ATOM   842  C  CE  . LYS   A 1 110 ? -36.936 -8.845  13.925 1.00 66.78  ? 406 LYS   A CE  1 
ATOM   843  N  NZ  . LYS   A 1 110 ? -38.363 -8.524  13.615 1.00 68.95  ? 406 LYS   A NZ  1 
ATOM   844  N  N   . HIS   A 1 111 ? -33.786 -13.014 18.630 1.00 62.79  ? 407 HIS   A N   1 
ATOM   845  C  CA  . HIS   A 1 111 ? -33.836 -13.696 19.910 1.00 65.49  ? 407 HIS   A CA  1 
ATOM   846  C  C   . HIS   A 1 111 ? -32.480 -13.800 20.588 1.00 64.48  ? 407 HIS   A C   1 
ATOM   847  O  O   . HIS   A 1 111 ? -32.433 -13.928 21.816 1.00 61.71  ? 407 HIS   A O   1 
ATOM   848  C  CB  . HIS   A 1 111 ? -34.478 -15.065 19.721 1.00 66.43  ? 407 HIS   A CB  1 
ATOM   849  C  CG  . HIS   A 1 111 ? -35.969 -14.993 19.651 1.00 69.12  ? 407 HIS   A CG  1 
ATOM   850  N  ND1 . HIS   A 1 111 ? -36.638 -14.574 18.522 1.00 69.84  ? 407 HIS   A ND1 1 
ATOM   851  C  CD2 . HIS   A 1 111 ? -36.921 -15.228 20.588 1.00 70.36  ? 407 HIS   A CD2 1 
ATOM   852  C  CE1 . HIS   A 1 111 ? -37.939 -14.585 18.751 1.00 71.56  ? 407 HIS   A CE1 1 
ATOM   853  N  NE2 . HIS   A 1 111 ? -38.138 -14.980 19.997 1.00 71.27  ? 407 HIS   A NE2 1 
ATOM   854  N  N   . ALA   A 1 112 ? -31.383 -13.717 19.833 1.00 64.13  ? 408 ALA   A N   1 
ATOM   855  C  CA  . ALA   A 1 112 ? -30.079 -13.520 20.455 1.00 62.67  ? 408 ALA   A CA  1 
ATOM   856  C  C   . ALA   A 1 112 ? -30.042 -12.199 21.212 1.00 63.05  ? 408 ALA   A C   1 
ATOM   857  O  O   . ALA   A 1 112 ? -29.614 -12.137 22.376 1.00 64.27  ? 408 ALA   A O   1 
ATOM   858  C  CB  . ALA   A 1 112 ? -28.983 -13.563 19.398 1.00 60.03  ? 408 ALA   A CB  1 
ATOM   859  N  N   . TRP   A 1 113 ? -30.524 -11.130 20.581 1.00 61.30  ? 409 TRP   A N   1 
ATOM   860  C  CA  . TRP   A 1 113 ? -30.699 -9.881  21.317 1.00 60.72  ? 409 TRP   A CA  1 
ATOM   861  C  C   . TRP   A 1 113 ? -31.655 -10.072 22.489 1.00 61.52  ? 409 TRP   A C   1 
ATOM   862  O  O   . TRP   A 1 113 ? -31.334 -9.726  23.630 1.00 58.92  ? 409 TRP   A O   1 
ATOM   863  C  CB  . TRP   A 1 113 ? -31.207 -8.791  20.382 1.00 59.55  ? 409 TRP   A CB  1 
ATOM   864  C  CG  . TRP   A 1 113 ? -31.346 -7.433  20.990 1.00 59.36  ? 409 TRP   A CG  1 
ATOM   865  C  CD1 . TRP   A 1 113 ? -30.883 -7.008  22.211 1.00 61.40  ? 409 TRP   A CD1 1 
ATOM   866  C  CD2 . TRP   A 1 113 ? -32.002 -6.313  20.399 1.00 61.51  ? 409 TRP   A CD2 1 
ATOM   867  N  NE1 . TRP   A 1 113 ? -31.215 -5.680  22.409 1.00 59.71  ? 409 TRP   A NE1 1 
ATOM   868  C  CE2 . TRP   A 1 113 ? -31.908 -5.237  21.311 1.00 60.90  ? 409 TRP   A CE2 1 
ATOM   869  C  CE3 . TRP   A 1 113 ? -32.668 -6.114  19.184 1.00 63.17  ? 409 TRP   A CE3 1 
ATOM   870  C  CZ2 . TRP   A 1 113 ? -32.448 -3.987  21.040 1.00 62.15  ? 409 TRP   A CZ2 1 
ATOM   871  C  CZ3 . TRP   A 1 113 ? -33.207 -4.875  18.923 1.00 64.73  ? 409 TRP   A CZ3 1 
ATOM   872  C  CH2 . TRP   A 1 113 ? -33.090 -3.826  19.842 1.00 63.58  ? 409 TRP   A CH2 1 
ATOM   873  N  N   . ARG   A 1 114 ? -32.831 -10.647 22.224 1.00 60.23  ? 410 ARG   A N   1 
ATOM   874  C  CA  . ARG   A 1 114 ? -33.834 -10.843 23.261 1.00 62.68  ? 410 ARG   A CA  1 
ATOM   875  C  C   . ARG   A 1 114 ? -33.269 -11.574 24.476 1.00 62.55  ? 410 ARG   A C   1 
ATOM   876  O  O   . ARG   A 1 114 ? -33.646 -11.270 25.617 1.00 59.64  ? 410 ARG   A O   1 
ATOM   877  C  CB  . ARG   A 1 114 ? -35.016 -11.610 22.678 1.00 64.12  ? 410 ARG   A CB  1 
ATOM   878  C  CG  . ARG   A 1 114 ? -36.241 -11.650 23.541 1.00 68.61  ? 410 ARG   A CG  1 
ATOM   879  C  CD  . ARG   A 1 114 ? -37.311 -12.545 22.923 1.00 69.57  ? 410 ARG   A CD  1 
ATOM   880  N  NE  . ARG   A 1 114 ? -38.527 -12.477 23.725 1.00 70.75  ? 410 ARG   A NE  1 
ATOM   881  C  CZ  . ARG   A 1 114 ? -39.690 -13.010 23.394 1.00 71.37  ? 410 ARG   A CZ  1 
ATOM   882  N  NH1 . ARG   A 1 114 ? -39.846 -13.686 22.263 1.00 73.72  ? 410 ARG   A NH1 1 
ATOM   883  N  NH2 . ARG   A 1 114 ? -40.728 -12.851 24.207 1.00 74.99  ? 410 ARG   A NH2 1 
ATOM   884  N  N   . ASN   A 1 115 ? -32.339 -12.502 24.258 1.00 59.61  ? 411 ASN   A N   1 
ATOM   885  C  CA  . ASN   A 1 115 ? -31.768 -13.304 25.327 1.00 62.95  ? 411 ASN   A CA  1 
ATOM   886  C  C   . ASN   A 1 115 ? -30.517 -12.692 25.958 1.00 60.74  ? 411 ASN   A C   1 
ATOM   887  O  O   . ASN   A 1 115 ? -29.922 -13.306 26.859 1.00 57.23  ? 411 ASN   A O   1 
ATOM   888  C  CB  . ASN   A 1 115 ? -31.455 -14.700 24.799 1.00 62.06  ? 411 ASN   A CB  1 
ATOM   889  C  CG  . ASN   A 1 115 ? -32.700 -15.454 24.416 1.00 66.00  ? 411 ASN   A CG  1 
ATOM   890  O  OD1 . ASN   A 1 115 ? -33.768 -15.230 24.988 1.00 65.40  ? 411 ASN   A OD1 1 
ATOM   891  N  ND2 . ASN   A 1 115 ? -32.581 -16.354 23.429 1.00 63.26  ? 411 ASN   A ND2 1 
ATOM   892  N  N   . ALA   A 1 116 ? -30.119 -11.499 25.531 1.00 59.55  ? 412 ALA   A N   1 
ATOM   893  C  CA  . ALA   A 1 116 ? -28.841 -10.911 25.916 1.00 57.11  ? 412 ALA   A CA  1 
ATOM   894  C  C   . ALA   A 1 116 ? -28.993 -10.338 27.313 1.00 56.26  ? 412 ALA   A C   1 
ATOM   895  O  O   . ALA   A 1 116 ? -29.487 -9.225  27.484 1.00 51.80  ? 412 ALA   A O   1 
ATOM   896  C  CB  . ALA   A 1 116 ? -28.435 -9.835  24.911 1.00 59.37  ? 412 ALA   A CB  1 
ATOM   897  N  N   . SER   A 1 117 ? -28.570 -11.094 28.326 1.00 57.18  ? 413 SER   A N   1 
ATOM   898  C  CA  . SER   A 1 117 ? -28.987 -10.755 29.678 1.00 52.42  ? 413 SER   A CA  1 
ATOM   899  C  C   . SER   A 1 117 ? -28.307 -9.486  30.192 1.00 53.83  ? 413 SER   A C   1 
ATOM   900  O  O   . SER   A 1 117 ? -28.825 -8.856  31.116 1.00 53.81  ? 413 SER   A O   1 
ATOM   901  C  CB  . SER   A 1 117 ? -28.757 -11.955 30.601 1.00 56.26  ? 413 SER   A CB  1 
ATOM   902  O  OG  . SER   A 1 117 ? -27.389 -12.148 30.887 1.00 56.95  ? 413 SER   A OG  1 
ATOM   903  N  N   . ARG   A 1 118 ? -27.201 -9.067  29.586 1.00 54.56  ? 414 ARG   A N   1 
ATOM   904  C  CA  . ARG   A 1 118 ? -26.504 -7.847  29.972 1.00 53.59  ? 414 ARG   A CA  1 
ATOM   905  C  C   . ARG   A 1 118 ? -27.013 -6.598  29.265 1.00 56.54  ? 414 ARG   A C   1 
ATOM   906  O  O   . ARG   A 1 118 ? -26.514 -5.503  29.548 1.00 49.48  ? 414 ARG   A O   1 
ATOM   907  C  CB  . ARG   A 1 118 ? -25.010 -8.012  29.715 1.00 56.16  ? 414 ARG   A CB  1 
ATOM   908  C  CG  . ARG   A 1 118 ? -24.411 -9.049  30.647 1.00 58.84  ? 414 ARG   A CG  1 
ATOM   909  C  CD  . ARG   A 1 118 ? -22.937 -9.227  30.431 1.00 63.58  ? 414 ARG   A CD  1 
ATOM   910  N  NE  . ARG   A 1 118 ? -22.396 -10.028 31.515 1.00 62.01  ? 414 ARG   A NE  1 
ATOM   911  C  CZ  . ARG   A 1 118 ? -21.112 -10.311 31.668 1.00 66.13  ? 414 ARG   A CZ  1 
ATOM   912  N  NH1 . ARG   A 1 118 ? -20.212 -9.928  30.774 1.00 64.21  ? 414 ARG   A NH1 1 
ATOM   913  N  NH2 . ARG   A 1 118 ? -20.721 -10.993 32.747 1.00 62.82  ? 414 ARG   A NH2 1 
ATOM   914  N  N   . CYS   A 1 119 ? -28.013 -6.716  28.389 1.00 53.21  ? 415 CYS   A N   1 
ATOM   915  C  CA  . CYS   A 1 119 ? -28.486 -5.587  27.587 1.00 56.64  ? 415 CYS   A CA  1 
ATOM   916  C  C   . CYS   A 1 119 ? -29.731 -4.963  28.210 1.00 55.60  ? 415 CYS   A C   1 
ATOM   917  O  O   . CYS   A 1 119 ? -30.778 -5.607  28.275 1.00 56.62  ? 415 CYS   A O   1 
ATOM   918  C  CB  . CYS   A 1 119 ? -28.802 -6.014  26.151 1.00 56.67  ? 415 CYS   A CB  1 
ATOM   919  S  SG  . CYS   A 1 119 ? -29.599 -4.670  25.212 1.00 50.19  ? 415 CYS   A SG  1 
ATOM   920  N  N   . VAL   A 1 120 ? -29.640 -3.689  28.611 1.00 57.37  ? 416 VAL   A N   1 
ATOM   921  C  CA  . VAL   A 1 120 ? -30.798 -3.023  29.208 1.00 53.14  ? 416 VAL   A CA  1 
ATOM   922  C  C   . VAL   A 1 120 ? -31.787 -2.503  28.175 1.00 56.49  ? 416 VAL   A C   1 
ATOM   923  O  O   . VAL   A 1 120 ? -32.896 -2.088  28.538 1.00 55.14  ? 416 VAL   A O   1 
ATOM   924  C  CB  . VAL   A 1 120 ? -30.320 -1.877  30.123 1.00 53.42  ? 416 VAL   A CB  1 
ATOM   925  C  CG1 . VAL   A 1 120 ? -29.832 -0.686  29.321 1.00 53.24  ? 416 VAL   A CG1 1 
ATOM   926  C  CG2 . VAL   A 1 120 ? -31.425 -1.470  31.144 1.00 56.36  ? 416 VAL   A CG2 1 
ATOM   927  N  N   . GLY   A 1 121 ? -31.444 -2.543  26.888 1.00 58.73  ? 417 GLY   A N   1 
ATOM   928  C  CA  . GLY   A 1 121 ? -32.325 -1.952  25.895 1.00 55.90  ? 417 GLY   A CA  1 
ATOM   929  C  C   . GLY   A 1 121 ? -33.258 -2.925  25.207 1.00 63.53  ? 417 GLY   A C   1 
ATOM   930  O  O   . GLY   A 1 121 ? -33.883 -2.578  24.202 1.00 62.87  ? 417 GLY   A O   1 
ATOM   931  N  N   . ARG   A 1 122 ? -33.381 -4.142  25.735 1.00 62.59  ? 418 ARG   A N   1 
ATOM   932  C  CA  . ARG   A 1 122 ? -34.052 -5.218  25.007 1.00 62.98  ? 418 ARG   A CA  1 
ATOM   933  C  C   . ARG   A 1 122 ? -35.539 -4.977  24.786 1.00 65.28  ? 418 ARG   A C   1 
ATOM   934  O  O   . ARG   A 1 122 ? -36.163 -5.752  24.055 1.00 66.62  ? 418 ARG   A O   1 
ATOM   935  C  CB  . ARG   A 1 122 ? -33.859 -6.550  25.730 1.00 60.87  ? 418 ARG   A CB  1 
ATOM   936  C  CG  . ARG   A 1 122 ? -32.514 -7.194  25.458 1.00 57.60  ? 418 ARG   A CG  1 
ATOM   937  C  CD  . ARG   A 1 122 ? -32.350 -8.421  26.278 1.00 59.00  ? 418 ARG   A CD  1 
ATOM   938  N  NE  . ARG   A 1 122 ? -32.161 -8.085  27.683 1.00 56.81  ? 418 ARG   A NE  1 
ATOM   939  C  CZ  . ARG   A 1 122 ? -32.214 -8.971  28.661 1.00 58.04  ? 418 ARG   A CZ  1 
ATOM   940  N  NH1 . ARG   A 1 122 ? -32.491 -10.241 28.415 1.00 52.78  ? 418 ARG   A NH1 1 
ATOM   941  N  NH2 . ARG   A 1 122 ? -31.978 -8.575  29.916 1.00 56.80  ? 418 ARG   A NH2 1 
ATOM   942  N  N   . ILE   A 1 123 ? -36.134 -3.928  25.357 1.00 65.81  ? 419 ILE   A N   1 
ATOM   943  C  CA  . ILE   A 1 123 ? -37.539 -3.627  25.092 1.00 65.91  ? 419 ILE   A CA  1 
ATOM   944  C  C   . ILE   A 1 123 ? -37.765 -3.537  23.576 1.00 69.52  ? 419 ILE   A C   1 
ATOM   945  O  O   . ILE   A 1 123 ? -38.870 -3.784  23.076 1.00 68.54  ? 419 ILE   A O   1 
ATOM   946  C  CB  . ILE   A 1 123 ? -37.971 -2.334  25.814 1.00 68.87  ? 419 ILE   A CB  1 
ATOM   947  C  CG1 . ILE   A 1 123 ? -39.496 -2.194  25.779 1.00 70.15  ? 419 ILE   A CG1 1 
ATOM   948  C  CG2 . ILE   A 1 123 ? -37.244 -1.090  25.260 1.00 64.04  ? 419 ILE   A CG2 1 
ATOM   949  C  CD1 . ILE   A 1 123 ? -39.996 -0.794  26.047 1.00 72.75  ? 419 ILE   A CD1 1 
ATOM   950  N  N   . GLN   A 1 124 ? -36.707 -3.212  22.842 1.00 69.62  ? 420 GLN   A N   1 
ATOM   951  C  CA  . GLN   A 1 124 ? -36.743 -3.006  21.404 1.00 70.58  ? 420 GLN   A CA  1 
ATOM   952  C  C   . GLN   A 1 124 ? -36.420 -4.264  20.603 1.00 69.54  ? 420 GLN   A C   1 
ATOM   953  O  O   . GLN   A 1 124 ? -36.248 -4.177  19.378 1.00 69.56  ? 420 GLN   A O   1 
ATOM   954  C  CB  . GLN   A 1 124 ? -35.759 -1.893  21.039 1.00 74.06  ? 420 GLN   A CB  1 
ATOM   955  C  CG  . GLN   A 1 124 ? -36.200 -0.514  21.477 1.00 80.18  ? 420 GLN   A CG  1 
ATOM   956  C  CD  . GLN   A 1 124 ? -37.037 0.178   20.422 1.00 85.72  ? 420 GLN   A CD  1 
ATOM   957  O  OE1 . GLN   A 1 124 ? -37.290 -0.371  19.343 1.00 84.70  ? 420 GLN   A OE1 1 
ATOM   958  N  NE2 . GLN   A 1 124 ? -37.465 1.399   20.722 1.00 90.62  ? 420 GLN   A NE2 1 
ATOM   959  N  N   . TRP   A 1 125 ? -36.363 -5.430  21.253 1.00 68.67  ? 421 TRP   A N   1 
ATOM   960  C  CA  . TRP   A 1 125 ? -35.719 -6.586  20.629 1.00 66.58  ? 421 TRP   A CA  1 
ATOM   961  C  C   . TRP   A 1 125 ? -36.403 -7.017  19.342 1.00 68.38  ? 421 TRP   A C   1 
ATOM   962  O  O   . TRP   A 1 125 ? -35.745 -7.604  18.479 1.00 66.66  ? 421 TRP   A O   1 
ATOM   963  C  CB  . TRP   A 1 125 ? -35.659 -7.776  21.587 1.00 66.26  ? 421 TRP   A CB  1 
ATOM   964  C  CG  . TRP   A 1 125 ? -36.996 -8.357  21.814 1.00 67.61  ? 421 TRP   A CG  1 
ATOM   965  C  CD1 . TRP   A 1 125 ? -37.894 -7.982  22.765 1.00 68.25  ? 421 TRP   A CD1 1 
ATOM   966  C  CD2 . TRP   A 1 125 ? -37.619 -9.401  21.061 1.00 70.10  ? 421 TRP   A CD2 1 
ATOM   967  N  NE1 . TRP   A 1 125 ? -39.034 -8.732  22.661 1.00 69.24  ? 421 TRP   A NE1 1 
ATOM   968  C  CE2 . TRP   A 1 125 ? -38.891 -9.615  21.624 1.00 69.07  ? 421 TRP   A CE2 1 
ATOM   969  C  CE3 . TRP   A 1 125 ? -37.222 -10.181 19.971 1.00 67.91  ? 421 TRP   A CE3 1 
ATOM   970  C  CZ2 . TRP   A 1 125 ? -39.766 -10.575 21.140 1.00 68.48  ? 421 TRP   A CZ2 1 
ATOM   971  C  CZ3 . TRP   A 1 125 ? -38.091 -11.137 19.496 1.00 67.78  ? 421 TRP   A CZ3 1 
ATOM   972  C  CH2 . TRP   A 1 125 ? -39.350 -11.320 20.069 1.00 71.58  ? 421 TRP   A CH2 1 
ATOM   973  N  N   . SER   A 1 126 ? -37.712 -6.782  19.199 1.00 67.60  ? 422 SER   A N   1 
ATOM   974  C  CA  . SER   A 1 126 ? -38.365 -7.192  17.957 1.00 71.67  ? 422 SER   A CA  1 
ATOM   975  C  C   . SER   A 1 126 ? -38.245 -6.162  16.839 1.00 71.98  ? 422 SER   A C   1 
ATOM   976  O  O   . SER   A 1 126 ? -38.617 -6.463  15.705 1.00 69.49  ? 422 SER   A O   1 
ATOM   977  C  CB  . SER   A 1 126 ? -39.850 -7.505  18.189 1.00 74.80  ? 422 SER   A CB  1 
ATOM   978  O  OG  . SER   A 1 126 ? -40.527 -6.427  18.821 1.00 77.68  ? 422 SER   A OG  1 
ATOM   979  N  N   . LYS   A 1 127 ? -37.763 -4.956  17.130 1.00 73.54  ? 423 LYS   A N   1 
ATOM   980  C  CA  . LYS   A 1 127 ? -37.525 -3.931  16.111 1.00 70.23  ? 423 LYS   A CA  1 
ATOM   981  C  C   . LYS   A 1 127 ? -36.048 -3.992  15.736 1.00 69.75  ? 423 LYS   A C   1 
ATOM   982  O  O   . LYS   A 1 127 ? -35.220 -3.190  16.182 1.00 69.35  ? 423 LYS   A O   1 
ATOM   983  C  CB  . LYS   A 1 127 ? -37.907 -2.550  16.628 1.00 77.03  ? 423 LYS   A CB  1 
ATOM   984  C  CG  . LYS   A 1 127 ? -39.101 -1.914  15.966 1.00 80.03  ? 423 LYS   A CG  1 
ATOM   985  C  CD  . LYS   A 1 127 ? -38.834 -0.445  15.641 1.00 81.92  ? 423 LYS   A CD  1 
ATOM   986  C  CE  . LYS   A 1 127 ? -40.050 0.216   15.029 1.00 89.08  ? 423 LYS   A CE  1 
ATOM   987  N  NZ  . LYS   A 1 127 ? -40.397 -0.390  13.712 1.00 97.35  ? 423 LYS   A NZ  1 
ATOM   988  N  N   . LEU   A 1 128 ? -35.709 -4.988  14.922 1.00 69.88  ? 424 LEU   A N   1 
ATOM   989  C  CA  . LEU   A 1 128 ? -34.324 -5.215  14.537 1.00 66.93  ? 424 LEU   A CA  1 
ATOM   990  C  C   . LEU   A 1 128 ? -34.263 -5.442  13.035 1.00 65.39  ? 424 LEU   A C   1 
ATOM   991  O  O   . LEU   A 1 128 ? -34.969 -6.304  12.500 1.00 65.73  ? 424 LEU   A O   1 
ATOM   992  C  CB  . LEU   A 1 128 ? -33.714 -6.403  15.288 1.00 63.53  ? 424 LEU   A CB  1 
ATOM   993  C  CG  . LEU   A 1 128 ? -32.255 -6.743  14.954 1.00 62.62  ? 424 LEU   A CG  1 
ATOM   994  C  CD1 . LEU   A 1 128 ? -31.316 -5.599  15.281 1.00 61.44  ? 424 LEU   A CD1 1 
ATOM   995  C  CD2 . LEU   A 1 128 ? -31.784 -8.021  15.657 1.00 62.47  ? 424 LEU   A CD2 1 
ATOM   996  N  N   . GLN   A 1 129 ? -33.439 -4.663  12.356 1.00 63.17  ? 425 GLN   A N   1 
ATOM   997  C  CA  . GLN   A 1 129 ? -33.216 -4.880  10.935 1.00 63.72  ? 425 GLN   A CA  1 
ATOM   998  C  C   . GLN   A 1 129 ? -32.063 -5.859  10.800 1.00 64.22  ? 425 GLN   A C   1 
ATOM   999  O  O   . GLN   A 1 129 ? -31.031 -5.714  11.463 1.00 63.48  ? 425 GLN   A O   1 
ATOM   1000 C  CB  . GLN   A 1 129 ? -32.915 -3.573  10.210 1.00 64.63  ? 425 GLN   A CB  1 
ATOM   1001 C  CG  . GLN   A 1 129 ? -32.630 -3.743  8.741  1.00 63.47  ? 425 GLN   A CG  1 
ATOM   1002 C  CD  . GLN   A 1 129 ? -33.825 -4.276  7.955  1.00 68.86  ? 425 GLN   A CD  1 
ATOM   1003 O  OE1 . GLN   A 1 129 ? -34.962 -4.284  8.447  1.00 73.64  ? 425 GLN   A OE1 1 
ATOM   1004 N  NE2 . GLN   A 1 129 ? -33.575 -4.707  6.719  1.00 69.22  ? 425 GLN   A NE2 1 
ATOM   1005 N  N   . VAL   A 1 130 ? -32.264 -6.889  9.995  1.00 64.44  ? 426 VAL   A N   1 
ATOM   1006 C  CA  . VAL   A 1 130 ? -31.268 -7.932  9.824  1.00 64.34  ? 426 VAL   A CA  1 
ATOM   1007 C  C   . VAL   A 1 130 ? -30.781 -7.824  8.396  1.00 63.40  ? 426 VAL   A C   1 
ATOM   1008 O  O   . VAL   A 1 130 ? -31.585 -7.861  7.461  1.00 61.92  ? 426 VAL   A O   1 
ATOM   1009 C  CB  . VAL   A 1 130 ? -31.839 -9.325  10.131 1.00 65.13  ? 426 VAL   A CB  1 
ATOM   1010 C  CG1 . VAL   A 1 130 ? -30.756 -10.391 9.967  1.00 61.75  ? 426 VAL   A CG1 1 
ATOM   1011 C  CG2 . VAL   A 1 130 ? -32.421 -9.353  11.548 1.00 62.45  ? 426 VAL   A CG2 1 
ATOM   1012 N  N   . PHE   A 1 131 ? -29.479 -7.624  8.226  1.00 60.87  ? 427 PHE   A N   1 
ATOM   1013 C  CA  . PHE   A 1 131 ? -28.876 -7.552  6.901  1.00 59.71  ? 427 PHE   A CA  1 
ATOM   1014 C  C   . PHE   A 1 131 ? -28.153 -8.866  6.676  1.00 61.08  ? 427 PHE   A C   1 
ATOM   1015 O  O   . PHE   A 1 131 ? -27.147 -9.156  7.335  1.00 59.48  ? 427 PHE   A O   1 
ATOM   1016 C  CB  . PHE   A 1 131 ? -27.940 -6.357  6.763  1.00 58.38  ? 427 PHE   A CB  1 
ATOM   1017 C  CG  . PHE   A 1 131 ? -28.656 -5.051  6.760  1.00 60.11  ? 427 PHE   A CG  1 
ATOM   1018 C  CD1 . PHE   A 1 131 ? -29.568 -4.757  5.771  1.00 61.82  ? 427 PHE   A CD1 1 
ATOM   1019 C  CD2 . PHE   A 1 131 ? -28.449 -4.129  7.762  1.00 58.41  ? 427 PHE   A CD2 1 
ATOM   1020 C  CE1 . PHE   A 1 131 ? -30.236 -3.555  5.773  1.00 62.80  ? 427 PHE   A CE1 1 
ATOM   1021 C  CE2 . PHE   A 1 131 ? -29.112 -2.930  7.760  1.00 59.68  ? 427 PHE   A CE2 1 
ATOM   1022 C  CZ  . PHE   A 1 131 ? -30.000 -2.638  6.786  1.00 61.97  ? 427 PHE   A CZ  1 
ATOM   1023 N  N   . ASP   A 1 132 ? -28.695 -9.663  5.769  1.00 62.70  ? 428 ASP   A N   1 
ATOM   1024 C  CA  . ASP   A 1 132 ? -28.121 -10.950 5.411  1.00 59.04  ? 428 ASP   A CA  1 
ATOM   1025 C  C   . ASP   A 1 132 ? -26.929 -10.676 4.512  1.00 60.84  ? 428 ASP   A C   1 
ATOM   1026 O  O   . ASP   A 1 132 ? -27.078 -10.326 3.338  1.00 64.06  ? 428 ASP   A O   1 
ATOM   1027 C  CB  . ASP   A 1 132 ? -29.175 -11.823 4.751  1.00 62.83  ? 428 ASP   A CB  1 
ATOM   1028 C  CG  . ASP   A 1 132 ? -28.674 -13.222 4.467  1.00 64.89  ? 428 ASP   A CG  1 
ATOM   1029 O  OD1 . ASP   A 1 132 ? -27.471 -13.496 4.683  1.00 65.66  ? 428 ASP   A OD1 1 
ATOM   1030 O  OD2 . ASP   A 1 132 ? -29.491 -14.049 4.017  1.00 66.33  ? 428 ASP   A OD2 1 
ATOM   1031 N  N   . ALA   A 1 133 ? -25.735 -10.809 5.080  1.00 60.91  ? 429 ALA   A N   1 
ATOM   1032 C  CA  . ALA   A 1 133 ? -24.486 -10.678 4.347  1.00 60.81  ? 429 ALA   A CA  1 
ATOM   1033 C  C   . ALA   A 1 133 ? -23.839 -12.021 4.118  1.00 60.46  ? 429 ALA   A C   1 
ATOM   1034 O  O   . ALA   A 1 133 ? -22.620 -12.093 3.924  1.00 60.95  ? 429 ALA   A O   1 
ATOM   1035 C  CB  . ALA   A 1 133 ? -23.516 -9.767  5.102  1.00 63.61  ? 429 ALA   A CB  1 
ATOM   1036 N  N   . ARG   A 1 134 ? -24.624 -13.093 4.147  1.00 61.53  ? 430 ARG   A N   1 
ATOM   1037 C  CA  . ARG   A 1 134 ? -24.019 -14.409 4.013  1.00 64.07  ? 430 ARG   A CA  1 
ATOM   1038 C  C   . ARG   A 1 134 ? -23.535 -14.727 2.598  1.00 65.74  ? 430 ARG   A C   1 
ATOM   1039 O  O   . ARG   A 1 134 ? -22.923 -15.785 2.426  1.00 66.84  ? 430 ARG   A O   1 
ATOM   1040 C  CB  . ARG   A 1 134 ? -24.997 -15.475 4.501  1.00 63.77  ? 430 ARG   A CB  1 
ATOM   1041 C  CG  . ARG   A 1 134 ? -25.120 -15.552 6.022  1.00 65.81  ? 430 ARG   A CG  1 
ATOM   1042 C  CD  . ARG   A 1 134 ? -26.202 -16.533 6.455  1.00 66.65  ? 430 ARG   A CD  1 
ATOM   1043 N  NE  . ARG   A 1 134 ? -27.499 -16.183 5.888  1.00 67.19  ? 430 ARG   A NE  1 
ATOM   1044 C  CZ  . ARG   A 1 134 ? -28.511 -17.030 5.771  1.00 70.32  ? 430 ARG   A CZ  1 
ATOM   1045 N  NH1 . ARG   A 1 134 ? -28.428 -18.270 6.234  1.00 71.92  ? 430 ARG   A NH1 1 
ATOM   1046 N  NH2 . ARG   A 1 134 ? -29.621 -16.632 5.152  1.00 65.41  ? 430 ARG   A NH2 1 
ATOM   1047 N  N   . ASP   A 1 135 ? -23.767 -13.859 1.590  1.00 63.92  ? 431 ASP   A N   1 
ATOM   1048 C  CA  . ASP   A 1 135 ? -23.186 -14.051 0.257  1.00 65.25  ? 431 ASP   A CA  1 
ATOM   1049 C  C   . ASP   A 1 135 ? -21.842 -13.352 0.104  1.00 65.85  ? 431 ASP   A C   1 
ATOM   1050 O  O   . ASP   A 1 135 ? -21.238 -13.411 -0.968 1.00 67.21  ? 431 ASP   A O   1 
ATOM   1051 C  CB  . ASP   A 1 135 ? -24.149 -13.573 -0.857 1.00 65.60  ? 431 ASP   A CB  1 
ATOM   1052 C  CG  . ASP   A 1 135 ? -24.587 -12.105 -0.695 1.00 66.88  ? 431 ASP   A CG  1 
ATOM   1053 O  OD1 . ASP   A 1 135 ? -24.178 -11.432 0.272  1.00 64.11  ? 431 ASP   A OD1 1 
ATOM   1054 O  OD2 . ASP   A 1 135 ? -25.372 -11.625 -1.544 1.00 63.67  ? 431 ASP   A OD2 1 
ATOM   1055 N  N   . CYS   A 1 136 ? -21.369 -12.698 1.151  1.00 64.95  ? 432 CYS   A N   1 
ATOM   1056 C  CA  . CYS   A 1 136 ? -20.137 -11.927 1.095  1.00 67.08  ? 432 CYS   A CA  1 
ATOM   1057 C  C   . CYS   A 1 136 ? -18.930 -12.853 0.967  1.00 68.74  ? 432 CYS   A C   1 
ATOM   1058 O  O   . CYS   A 1 136 ? -18.921 -13.965 1.505  1.00 72.27  ? 432 CYS   A O   1 
ATOM   1059 C  CB  . CYS   A 1 136 ? -20.032 -11.055 2.357  1.00 63.12  ? 432 CYS   A CB  1 
ATOM   1060 S  SG  . CYS   A 1 136 ? -18.676 -9.868  2.324  1.00 62.99  ? 432 CYS   A SG  1 
ATOM   1061 N  N   . THR   A 1 137 ? -17.908 -12.406 0.230  1.00 72.31  ? 433 THR   A N   1 
ATOM   1062 C  CA  . THR   A 1 137 ? -16.724 -13.233 0.001  1.00 70.19  ? 433 THR   A CA  1 
ATOM   1063 C  C   . THR   A 1 137 ? -15.399 -12.532 0.246  1.00 71.96  ? 433 THR   A C   1 
ATOM   1064 O  O   . THR   A 1 137 ? -14.380 -13.221 0.385  1.00 72.92  ? 433 THR   A O   1 
ATOM   1065 C  CB  . THR   A 1 137 ? -16.701 -13.781 -1.435 1.00 76.21  ? 433 THR   A CB  1 
ATOM   1066 O  OG1 . THR   A 1 137 ? -16.635 -12.688 -2.364 1.00 76.61  ? 433 THR   A OG1 1 
ATOM   1067 C  CG2 . THR   A 1 137 ? -17.933 -14.626 -1.725 1.00 75.09  ? 433 THR   A CG2 1 
ATOM   1068 N  N   . THR   A 1 138 ? -15.368 -11.207 0.313  1.00 76.14  ? 434 THR   A N   1 
ATOM   1069 C  CA  . THR   A 1 138 ? -14.124 -10.457 0.336  1.00 77.12  ? 434 THR   A CA  1 
ATOM   1070 C  C   . THR   A 1 138 ? -14.193 -9.408  1.428  1.00 73.23  ? 434 THR   A C   1 
ATOM   1071 O  O   . THR   A 1 138 ? -15.264 -9.098  1.960  1.00 74.30  ? 434 THR   A O   1 
ATOM   1072 C  CB  . THR   A 1 138 ? -13.841 -9.786  -1.025 1.00 76.64  ? 434 THR   A CB  1 
ATOM   1073 O  OG1 . THR   A 1 138 ? -15.056 -9.247  -1.549 1.00 78.11  ? 434 THR   A OG1 1 
ATOM   1074 C  CG2 . THR   A 1 138 ? -13.260 -10.783 -2.012 1.00 79.41  ? 434 THR   A CG2 1 
ATOM   1075 N  N   . ALA   A 1 139 ? -13.021 -8.878  1.776  1.00 77.33  ? 435 ALA   A N   1 
ATOM   1076 C  CA  . ALA   A 1 139 ? -12.983 -7.819  2.775  1.00 75.02  ? 435 ALA   A CA  1 
ATOM   1077 C  C   . ALA   A 1 139 ? -13.627 -6.553  2.231  1.00 74.09  ? 435 ALA   A C   1 
ATOM   1078 O  O   . ALA   A 1 139 ? -14.314 -5.833  2.964  1.00 73.58  ? 435 ALA   A O   1 
ATOM   1079 C  CB  . ALA   A 1 139 ? -11.544 -7.555  3.204  1.00 81.02  ? 435 ALA   A CB  1 
ATOM   1080 N  N   . HIS   A 1 140 ? -13.428 -6.282  0.938  1.00 80.01  ? 436 HIS   A N   1 
ATOM   1081 C  CA  . HIS   A 1 140 ? -14.148 -5.197  0.283  1.00 77.63  ? 436 HIS   A CA  1 
ATOM   1082 C  C   . HIS   A 1 140 ? -15.648 -5.439  0.314  1.00 72.52  ? 436 HIS   A C   1 
ATOM   1083 O  O   . HIS   A 1 140 ? -16.435 -4.498  0.450  1.00 72.99  ? 436 HIS   A O   1 
ATOM   1084 C  CB  . HIS   A 1 140 ? -13.684 -5.054  -1.166 1.00 82.54  ? 436 HIS   A CB  1 
ATOM   1085 C  CG  . HIS   A 1 140 ? -12.501 -4.157  -1.357 1.00 86.18  ? 436 HIS   A CG  1 
ATOM   1086 N  ND1 . HIS   A 1 140 ? -11.235 -4.476  -0.911 1.00 88.17  ? 436 HIS   A ND1 1 
ATOM   1087 C  CD2 . HIS   A 1 140 ? -12.385 -2.971  -2.001 1.00 86.07  ? 436 HIS   A CD2 1 
ATOM   1088 C  CE1 . HIS   A 1 140 ? -10.395 -3.518  -1.263 1.00 89.42  ? 436 HIS   A CE1 1 
ATOM   1089 N  NE2 . HIS   A 1 140 ? -11.068 -2.591  -1.922 1.00 88.12  ? 436 HIS   A NE2 1 
ATOM   1090 N  N   . GLY   A 1 141 ? -16.069 -6.688  0.138  1.00 72.13  ? 437 GLY   A N   1 
ATOM   1091 C  CA  . GLY   A 1 141 ? -17.478 -6.992  0.288  1.00 70.27  ? 437 GLY   A CA  1 
ATOM   1092 C  C   . GLY   A 1 141 ? -17.980 -6.621  1.664  1.00 70.08  ? 437 GLY   A C   1 
ATOM   1093 O  O   . GLY   A 1 141 ? -19.020 -5.976  1.800  1.00 69.03  ? 437 GLY   A O   1 
ATOM   1094 N  N   . MET   A 1 142 ? -17.226 -6.993  2.702  1.00 71.14  ? 438 MET   A N   1 
ATOM   1095 C  CA  . MET   A 1 142 ? -17.607 -6.658  4.071  1.00 66.98  ? 438 MET   A CA  1 
ATOM   1096 C  C   . MET   A 1 142 ? -17.680 -5.151  4.262  1.00 65.50  ? 438 MET   A C   1 
ATOM   1097 O  O   . MET   A 1 142 ? -18.666 -4.627  4.790  1.00 65.34  ? 438 MET   A O   1 
ATOM   1098 C  CB  . MET   A 1 142 ? -16.611 -7.270  5.051  1.00 68.42  ? 438 MET   A CB  1 
ATOM   1099 C  CG  . MET   A 1 142 ? -16.533 -8.774  5.014  1.00 67.39  ? 438 MET   A CG  1 
ATOM   1100 S  SD  . MET   A 1 142 ? -15.185 -9.385  6.062  1.00 72.77  ? 438 MET   A SD  1 
ATOM   1101 C  CE  . MET   A 1 142 ? -15.766 -8.860  7.660  1.00 67.06  ? 438 MET   A CE  1 
ATOM   1102 N  N   . PHE   A 1 143 ? -16.623 -4.442  3.870  1.00 64.53  ? 439 PHE   A N   1 
ATOM   1103 C  CA  . PHE   A 1 143 ? -16.639 -2.986  3.914  1.00 65.98  ? 439 PHE   A CA  1 
ATOM   1104 C  C   . PHE   A 1 143 ? -17.943 -2.437  3.359  1.00 68.66  ? 439 PHE   A C   1 
ATOM   1105 O  O   . PHE   A 1 143 ? -18.640 -1.665  4.027  1.00 63.30  ? 439 PHE   A O   1 
ATOM   1106 C  CB  . PHE   A 1 143 ? -15.450 -2.430  3.132  1.00 72.32  ? 439 PHE   A CB  1 
ATOM   1107 C  CG  . PHE   A 1 143 ? -15.412 -0.940  3.099  1.00 76.03  ? 439 PHE   A CG  1 
ATOM   1108 C  CD1 . PHE   A 1 143 ? -15.446 -0.218  4.279  1.00 75.45  ? 439 PHE   A CD1 1 
ATOM   1109 C  CD2 . PHE   A 1 143 ? -15.362 -0.253  1.904  1.00 74.20  ? 439 PHE   A CD2 1 
ATOM   1110 C  CE1 . PHE   A 1 143 ? -15.412 1.152   4.258  1.00 77.71  ? 439 PHE   A CE1 1 
ATOM   1111 C  CE2 . PHE   A 1 143 ? -15.334 1.125   1.890  1.00 77.59  ? 439 PHE   A CE2 1 
ATOM   1112 C  CZ  . PHE   A 1 143 ? -15.363 1.825   3.077  1.00 78.73  ? 439 PHE   A CZ  1 
ATOM   1113 N  N   . ASN   A 1 144 ? -18.297 -2.839  2.132  1.00 63.88  ? 440 ASN   A N   1 
ATOM   1114 C  CA  . ASN   A 1 144 ? -19.550 -2.379  1.548  1.00 62.92  ? 440 ASN   A CA  1 
ATOM   1115 C  C   . ASN   A 1 144 ? -20.731 -2.702  2.453  1.00 61.69  ? 440 ASN   A C   1 
ATOM   1116 O  O   . ASN   A 1 144 ? -21.559 -1.833  2.743  1.00 67.25  ? 440 ASN   A O   1 
ATOM   1117 C  CB  . ASN   A 1 144 ? -19.757 -2.994  0.167  1.00 65.75  ? 440 ASN   A CB  1 
ATOM   1118 C  CG  . ASN   A 1 144 ? -20.786 -2.234  -0.638 1.00 63.13  ? 440 ASN   A CG  1 
ATOM   1119 O  OD1 . ASN   A 1 144 ? -20.626 -1.044  -0.898 1.00 60.83  ? 440 ASN   A OD1 1 
ATOM   1120 N  ND2 . ASN   A 1 144 ? -21.865 -2.902  -0.990 1.00 62.05  ? 440 ASN   A ND2 1 
ATOM   1121 N  N   . TYR   A 1 145 ? -20.839 -3.950  2.902  1.00 58.28  ? 441 TYR   A N   1 
ATOM   1122 C  CA  . TYR   A 1 145 ? -21.972 -4.292  3.751  1.00 65.61  ? 441 TYR   A CA  1 
ATOM   1123 C  C   . TYR   A 1 145 ? -21.988 -3.436  5.009  1.00 62.08  ? 441 TYR   A C   1 
ATOM   1124 O  O   . TYR   A 1 145 ? -23.047 -2.958  5.437  1.00 64.46  ? 441 TYR   A O   1 
ATOM   1125 C  CB  . TYR   A 1 145 ? -21.931 -5.770  4.121  1.00 64.80  ? 441 TYR   A CB  1 
ATOM   1126 C  CG  . TYR   A 1 145 ? -22.721 -6.658  3.191  1.00 60.75  ? 441 TYR   A CG  1 
ATOM   1127 C  CD1 . TYR   A 1 145 ? -24.103 -6.647  3.213  1.00 61.68  ? 441 TYR   A CD1 1 
ATOM   1128 C  CD2 . TYR   A 1 145 ? -22.086 -7.528  2.332  1.00 63.52  ? 441 TYR   A CD2 1 
ATOM   1129 C  CE1 . TYR   A 1 145 ? -24.838 -7.458  2.390  1.00 59.15  ? 441 TYR   A CE1 1 
ATOM   1130 C  CE2 . TYR   A 1 145 ? -22.809 -8.361  1.476  1.00 59.26  ? 441 TYR   A CE2 1 
ATOM   1131 C  CZ  . TYR   A 1 145 ? -24.184 -8.320  1.518  1.00 59.98  ? 441 TYR   A CZ  1 
ATOM   1132 O  OH  . TYR   A 1 145 ? -24.902 -9.133  0.677  1.00 64.64  ? 441 TYR   A OH  1 
ATOM   1133 N  N   . ILE   A 1 146 ? -20.818 -3.220  5.609  1.00 61.23  ? 442 ILE   A N   1 
ATOM   1134 C  CA  . ILE   A 1 146 ? -20.759 -2.510  6.886  1.00 60.64  ? 442 ILE   A CA  1 
ATOM   1135 C  C   . ILE   A 1 146 ? -21.139 -1.041  6.693  1.00 62.89  ? 442 ILE   A C   1 
ATOM   1136 O  O   . ILE   A 1 146 ? -21.845 -0.453  7.525  1.00 62.97  ? 442 ILE   A O   1 
ATOM   1137 C  CB  . ILE   A 1 146 ? -19.358 -2.675  7.502  1.00 62.49  ? 442 ILE   A CB  1 
ATOM   1138 C  CG1 . ILE   A 1 146 ? -19.164 -4.092  8.053  1.00 63.66  ? 442 ILE   A CG1 1 
ATOM   1139 C  CG2 . ILE   A 1 146 ? -19.111 -1.649  8.596  1.00 61.77  ? 442 ILE   A CG2 1 
ATOM   1140 C  CD1 . ILE   A 1 146 ? -17.736 -4.385  8.476  1.00 59.90  ? 442 ILE   A CD1 1 
ATOM   1141 N  N   . CYS   A 1 147 ? -20.692 -0.435  5.579  1.00 62.09  ? 443 CYS   A N   1 
ATOM   1142 C  CA  . CYS   A 1 147 ? -21.081 0.933   5.234  1.00 61.07  ? 443 CYS   A CA  1 
ATOM   1143 C  C   . CYS   A 1 147 ? -22.589 1.065   5.080  1.00 62.07  ? 443 CYS   A C   1 
ATOM   1144 O  O   . CYS   A 1 147 ? -23.176 2.056   5.527  1.00 62.53  ? 443 CYS   A O   1 
ATOM   1145 C  CB  . CYS   A 1 147 ? -20.414 1.382   3.925  1.00 65.85  ? 443 CYS   A CB  1 
ATOM   1146 S  SG  . CYS   A 1 147 ? -18.682 1.828   4.017  1.00 73.80  ? 443 CYS   A SG  1 
ATOM   1147 N  N   . ASN   A 1 148 ? -23.221 0.125   4.366  1.00 60.91  ? 444 ASN   A N   1 
ATOM   1148 C  CA  . ASN   A 1 148 ? -24.677 0.147   4.259  1.00 61.97  ? 444 ASN   A CA  1 
ATOM   1149 C  C   . ASN   A 1 148 ? -25.316 0.028   5.631  1.00 62.02  ? 444 ASN   A C   1 
ATOM   1150 O  O   . ASN   A 1 148 ? -26.360 0.634   5.901  1.00 60.11  ? 444 ASN   A O   1 
ATOM   1151 C  CB  . ASN   A 1 148 ? -25.163 -0.993  3.376  1.00 65.12  ? 444 ASN   A CB  1 
ATOM   1152 C  CG  . ASN   A 1 148 ? -24.834 -0.782  1.920  1.00 64.96  ? 444 ASN   A CG  1 
ATOM   1153 O  OD1 . ASN   A 1 148 ? -24.341 0.282   1.531  1.00 66.32  ? 444 ASN   A OD1 1 
ATOM   1154 N  ND2 . ASN   A 1 148 ? -25.130 -1.781  1.097  1.00 62.64  ? 444 ASN   A ND2 1 
ATOM   1155 N  N   . HIS   A 1 149 ? -24.724 -0.790  6.490  1.00 60.94  ? 445 HIS   A N   1 
ATOM   1156 C  CA  . HIS   A 1 149 ? -25.229 -0.921  7.844  1.00 59.78  ? 445 HIS   A CA  1 
ATOM   1157 C  C   . HIS   A 1 149 ? -25.162 0.421   8.571  1.00 59.54  ? 445 HIS   A C   1 
ATOM   1158 O  O   . HIS   A 1 149 ? -26.183 0.937   9.029  1.00 61.55  ? 445 HIS   A O   1 
ATOM   1159 C  CB  . HIS   A 1 149 ? -24.440 -2.015  8.563  1.00 59.58  ? 445 HIS   A CB  1 
ATOM   1160 C  CG  . HIS   A 1 149 ? -24.849 -2.226  9.986  1.00 59.57  ? 445 HIS   A CG  1 
ATOM   1161 N  ND1 . HIS   A 1 149 ? -25.044 -3.478  10.530 1.00 58.60  ? 445 HIS   A ND1 1 
ATOM   1162 C  CD2 . HIS   A 1 149 ? -25.079 -1.341  10.985 1.00 54.12  ? 445 HIS   A CD2 1 
ATOM   1163 C  CE1 . HIS   A 1 149 ? -25.397 -3.355  11.798 1.00 56.28  ? 445 HIS   A CE1 1 
ATOM   1164 N  NE2 . HIS   A 1 149 ? -25.423 -2.069  12.099 1.00 59.40  ? 445 HIS   A NE2 1 
ATOM   1165 N  N   . VAL   A 1 150 ? -23.967 1.015   8.648  1.00 60.04  ? 446 VAL   A N   1 
ATOM   1166 C  CA  . VAL   A 1 150 ? -23.799 2.323   9.291  1.00 62.35  ? 446 VAL   A CA  1 
ATOM   1167 C  C   . VAL   A 1 150 ? -24.847 3.310   8.787  1.00 66.15  ? 446 VAL   A C   1 
ATOM   1168 O  O   . VAL   A 1 150 ? -25.628 3.869   9.561  1.00 70.85  ? 446 VAL   A O   1 
ATOM   1169 C  CB  . VAL   A 1 150 ? -22.383 2.867   9.042  1.00 63.35  ? 446 VAL   A CB  1 
ATOM   1170 C  CG1 . VAL   A 1 150 ? -22.278 4.318   9.507  1.00 67.98  ? 446 VAL   A CG1 1 
ATOM   1171 C  CG2 . VAL   A 1 150 ? -21.344 1.990   9.704  1.00 60.50  ? 446 VAL   A CG2 1 
ATOM   1172 N  N   . LYS   A 1 151 ? -24.887 3.521   7.476  1.00 65.00  ? 447 LYS   A N   1 
ATOM   1173 C  CA  . LYS   A 1 151 ? -25.792 4.527   6.925  1.00 68.94  ? 447 LYS   A CA  1 
ATOM   1174 C  C   . LYS   A 1 151 ? -27.247 4.232   7.281  1.00 69.97  ? 447 LYS   A C   1 
ATOM   1175 O  O   . LYS   A 1 151 ? -27.999 5.140   7.665  1.00 72.01  ? 447 LYS   A O   1 
ATOM   1176 C  CB  . LYS   A 1 151 ? -25.630 4.610   5.411  1.00 68.83  ? 447 LYS   A CB  1 
ATOM   1177 C  CG  . LYS   A 1 151 ? -26.325 5.809   4.820  1.00 71.12  ? 447 LYS   A CG  1 
ATOM   1178 C  CD  . LYS   A 1 151 ? -26.069 5.892   3.332  1.00 74.50  ? 447 LYS   A CD  1 
ATOM   1179 C  CE  . LYS   A 1 151 ? -26.196 7.303   2.822  1.00 73.04  ? 447 LYS   A CE  1 
ATOM   1180 N  NZ  . LYS   A 1 151 ? -25.800 7.408   1.377  1.00 70.08  ? 447 LYS   A NZ  1 
ATOM   1181 N  N   . TYR   A 1 152 ? -27.669 2.972   7.151  1.00 66.57  ? 448 TYR   A N   1 
ATOM   1182 C  CA  . TYR   A 1 152 ? -29.031 2.623   7.534  1.00 67.44  ? 448 TYR   A CA  1 
ATOM   1183 C  C   . TYR   A 1 152 ? -29.258 2.858   9.028  1.00 66.86  ? 448 TYR   A C   1 
ATOM   1184 O  O   . TYR   A 1 152 ? -30.201 3.546   9.427  1.00 66.23  ? 448 TYR   A O   1 
ATOM   1185 C  CB  . TYR   A 1 152 ? -29.331 1.170   7.180  1.00 67.06  ? 448 TYR   A CB  1 
ATOM   1186 C  CG  . TYR   A 1 152 ? -30.672 0.742   7.718  1.00 67.27  ? 448 TYR   A CG  1 
ATOM   1187 C  CD1 . TYR   A 1 152 ? -31.820 0.945   6.985  1.00 69.52  ? 448 TYR   A CD1 1 
ATOM   1188 C  CD2 . TYR   A 1 152 ? -30.791 0.156   8.970  1.00 66.55  ? 448 TYR   A CD2 1 
ATOM   1189 C  CE1 . TYR   A 1 152 ? -33.053 0.574   7.469  1.00 68.01  ? 448 TYR   A CE1 1 
ATOM   1190 C  CE2 . TYR   A 1 152 ? -32.019 -0.221  9.462  1.00 66.79  ? 448 TYR   A CE2 1 
ATOM   1191 C  CZ  . TYR   A 1 152 ? -33.142 -0.010  8.700  1.00 70.88  ? 448 TYR   A CZ  1 
ATOM   1192 O  OH  . TYR   A 1 152 ? -34.366 -0.388  9.187  1.00 76.05  ? 448 TYR   A OH  1 
ATOM   1193 N  N   . ALA   A 1 153 ? -28.421 2.256   9.870  1.00 64.63  ? 449 ALA   A N   1 
ATOM   1194 C  CA  . ALA   A 1 153 ? -28.662 2.323   11.305 1.00 65.91  ? 449 ALA   A CA  1 
ATOM   1195 C  C   . ALA   A 1 153 ? -28.619 3.757   11.815 1.00 68.93  ? 449 ALA   A C   1 
ATOM   1196 O  O   . ALA   A 1 153 ? -29.235 4.075   12.842 1.00 70.72  ? 449 ALA   A O   1 
ATOM   1197 C  CB  . ALA   A 1 153 ? -27.639 1.470   12.056 1.00 62.10  ? 449 ALA   A CB  1 
ATOM   1198 N  N   . THR   A 1 154 ? -27.877 4.627   11.133 1.00 63.38  ? 450 THR   A N   1 
ATOM   1199 C  CA  . THR   A 1 154 ? -27.740 6.000   11.597 1.00 68.87  ? 450 THR   A CA  1 
ATOM   1200 C  C   . THR   A 1 154 ? -28.963 6.820   11.221 1.00 73.53  ? 450 THR   A C   1 
ATOM   1201 O  O   . THR   A 1 154 ? -29.523 7.524   12.067 1.00 70.66  ? 450 THR   A O   1 
ATOM   1202 C  CB  . THR   A 1 154 ? -26.461 6.617   11.037 1.00 68.84  ? 450 THR   A CB  1 
ATOM   1203 O  OG1 . THR   A 1 154 ? -25.356 5.789   11.431 1.00 66.58  ? 450 THR   A OG1 1 
ATOM   1204 C  CG2 . THR   A 1 154 ? -26.271 8.022   11.569 1.00 68.79  ? 450 THR   A CG2 1 
ATOM   1205 N  N   . ASN   A 1 155 ? -29.392 6.739   9.957  1.00 71.65  ? 451 ASN   A N   1 
ATOM   1206 C  CA  . ASN   A 1 155 ? -30.676 7.290   9.538  1.00 71.14  ? 451 ASN   A CA  1 
ATOM   1207 C  C   . ASN   A 1 155 ? -30.779 8.756   9.964  1.00 77.69  ? 451 ASN   A C   1 
ATOM   1208 O  O   . ASN   A 1 155 ? -31.767 9.199   10.549 1.00 79.42  ? 451 ASN   A O   1 
ATOM   1209 C  CB  . ASN   A 1 155 ? -31.830 6.450   10.103 1.00 69.86  ? 451 ASN   A CB  1 
ATOM   1210 C  CG  . ASN   A 1 155 ? -33.186 6.857   9.560  1.00 76.28  ? 451 ASN   A CG  1 
ATOM   1211 O  OD1 . ASN   A 1 155 ? -33.294 7.457   8.482  1.00 76.44  ? 451 ASN   A OD1 1 
ATOM   1212 N  ND2 . ASN   A 1 155 ? -34.236 6.533   10.307 1.00 73.95  ? 451 ASN   A ND2 1 
ATOM   1213 N  N   . LYS   A 1 156 ? -29.707 9.500   9.689  1.00 78.13  ? 452 LYS   A N   1 
ATOM   1214 C  CA  . LYS   A 1 156 ? -29.654 10.941  9.885  1.00 78.15  ? 452 LYS   A CA  1 
ATOM   1215 C  C   . LYS   A 1 156 ? -29.876 11.303  11.354 1.00 84.09  ? 452 LYS   A C   1 
ATOM   1216 O  O   . LYS   A 1 156 ? -30.407 12.370  11.663 1.00 87.09  ? 452 LYS   A O   1 
ATOM   1217 C  CB  . LYS   A 1 156 ? -30.668 11.659  9.008  1.00 83.49  ? 452 LYS   A CB  1 
ATOM   1218 C  CG  . LYS   A 1 156 ? -30.625 11.274  7.490  1.00 91.08  ? 452 LYS   A CG  1 
ATOM   1219 C  CD  . LYS   A 1 156 ? -30.947 12.443  6.546  1.00 98.91  ? 452 LYS   A CD  1 
ATOM   1220 C  CE  . LYS   A 1 156 ? -32.238 13.175  6.927  1.00 108.82 ? 452 LYS   A CE  1 
ATOM   1221 N  NZ  . LYS   A 1 156 ? -33.330 12.227  7.281  1.00 110.68 ? 452 LYS   A NZ  1 
ATOM   1222 N  N   . GLY   A 1 157 ? -29.494 10.407  12.260 1.00 81.19  ? 453 GLY   A N   1 
ATOM   1223 C  CA  . GLY   A 1 157 ? -29.634 10.604  13.686 1.00 83.73  ? 453 GLY   A CA  1 
ATOM   1224 C  C   . GLY   A 1 157 ? -30.879 9.985   14.283 1.00 84.40  ? 453 GLY   A C   1 
ATOM   1225 O  O   . GLY   A 1 157 ? -30.928 9.787   15.496 1.00 81.47  ? 453 GLY   A O   1 
ATOM   1226 N  N   . ASN   A 1 158 ? -31.889 9.669   13.467 1.00 84.40  ? 454 ASN   A N   1 
ATOM   1227 C  CA  . ASN   A 1 158 ? -33.045 8.935   13.971 1.00 85.32  ? 454 ASN   A CA  1 
ATOM   1228 C  C   . ASN   A 1 158 ? -32.678 7.452   13.948 1.00 81.02  ? 454 ASN   A C   1 
ATOM   1229 O  O   . ASN   A 1 158 ? -33.157 6.669   13.127 1.00 79.25  ? 454 ASN   A O   1 
ATOM   1230 C  CB  . ASN   A 1 158 ? -34.295 9.237   13.162 1.00 84.80  ? 454 ASN   A CB  1 
ATOM   1231 C  CG  . ASN   A 1 158 ? -35.524 8.507   13.697 1.00 88.74  ? 454 ASN   A CG  1 
ATOM   1232 O  OD1 . ASN   A 1 158 ? -35.509 7.957   14.806 1.00 88.71  ? 454 ASN   A OD1 1 
ATOM   1233 N  ND2 . ASN   A 1 158 ? -36.595 8.493   12.905 1.00 91.98  ? 454 ASN   A ND2 1 
ATOM   1234 N  N   . LEU   A 1 159 ? -31.805 7.080   14.891 1.00 78.19  ? 455 LEU   A N   1 
ATOM   1235 C  CA  . LEU   A 1 159 ? -31.081 5.814   14.817 1.00 72.26  ? 455 LEU   A CA  1 
ATOM   1236 C  C   . LEU   A 1 159 ? -32.033 4.624   14.782 1.00 69.26  ? 455 LEU   A C   1 
ATOM   1237 O  O   . LEU   A 1 159 ? -33.158 4.672   15.289 1.00 71.02  ? 455 LEU   A O   1 
ATOM   1238 C  CB  . LEU   A 1 159 ? -30.120 5.674   16.006 1.00 74.14  ? 455 LEU   A CB  1 
ATOM   1239 C  CG  . LEU   A 1 159 ? -28.679 6.209   15.901 1.00 73.03  ? 455 LEU   A CG  1 
ATOM   1240 C  CD1 . LEU   A 1 159 ? -28.583 7.408   15.010 1.00 75.63  ? 455 LEU   A CD1 1 
ATOM   1241 C  CD2 . LEU   A 1 159 ? -28.135 6.575   17.283 1.00 70.30  ? 455 LEU   A CD2 1 
ATOM   1242 N  N   . ARG   A 1 160 ? -31.562 3.545   14.176 1.00 65.84  ? 456 ARG   A N   1 
ATOM   1243 C  CA  . ARG   A 1 160 ? -32.370 2.365   13.928 1.00 66.46  ? 456 ARG   A CA  1 
ATOM   1244 C  C   . ARG   A 1 160 ? -31.516 1.164   14.240 1.00 59.54  ? 456 ARG   A C   1 
ATOM   1245 O  O   . ARG   A 1 160 ? -30.324 1.140   13.928 1.00 63.36  ? 456 ARG   A O   1 
ATOM   1246 C  CB  . ARG   A 1 160 ? -32.867 2.267   12.454 1.00 65.08  ? 456 ARG   A CB  1 
ATOM   1247 C  CG  . ARG   A 1 160 ? -33.888 3.325   12.081 1.00 68.73  ? 456 ARG   A CG  1 
ATOM   1248 C  CD  . ARG   A 1 160 ? -34.443 3.152   10.645 1.00 68.42  ? 456 ARG   A CD  1 
ATOM   1249 N  NE  . ARG   A 1 160 ? -33.439 3.440   9.629  1.00 66.37  ? 456 ARG   A NE  1 
ATOM   1250 C  CZ  . ARG   A 1 160 ? -33.719 3.698   8.357  1.00 71.61  ? 456 ARG   A CZ  1 
ATOM   1251 N  NH1 . ARG   A 1 160 ? -34.970 3.712   7.910  1.00 68.06  ? 456 ARG   A NH1 1 
ATOM   1252 N  NH2 . ARG   A 1 160 ? -32.725 3.974   7.518  1.00 66.83  ? 456 ARG   A NH2 1 
ATOM   1253 N  N   . SER   A 1 161 ? -32.121 0.166   14.837 1.00 58.16  ? 457 SER   A N   1 
ATOM   1254 C  CA  . SER   A 1 161 ? -31.344 -0.974  15.280 1.00 64.59  ? 457 SER   A CA  1 
ATOM   1255 C  C   . SER   A 1 161 ? -31.144 -1.901  14.110 1.00 59.73  ? 457 SER   A C   1 
ATOM   1256 O  O   . SER   A 1 161 ? -32.037 -2.043  13.266 1.00 65.01  ? 457 SER   A O   1 
ATOM   1257 C  CB  . SER   A 1 161 ? -32.021 -1.695  16.446 1.00 60.77  ? 457 SER   A CB  1 
ATOM   1258 O  OG  . SER   A 1 161 ? -32.270 -0.768  17.490 1.00 63.03  ? 457 SER   A OG  1 
ATOM   1259 N  N   . ALA   A 1 162 ? -29.961 -2.511  14.042 1.00 56.23  ? 458 ALA   A N   1 
ATOM   1260 C  CA  . ALA   A 1 162 ? -29.666 -3.346  12.884 1.00 61.03  ? 458 ALA   A CA  1 
ATOM   1261 C  C   . ALA   A 1 162 ? -28.520 -4.296  13.196 1.00 60.21  ? 458 ALA   A C   1 
ATOM   1262 O  O   . ALA   A 1 162 ? -27.735 -4.069  14.119 1.00 54.18  ? 458 ALA   A O   1 
ATOM   1263 C  CB  . ALA   A 1 162 ? -29.332 -2.492  11.651 1.00 58.88  ? 458 ALA   A CB  1 
ATOM   1264 N  N   . ILE   A 1 163 ? -28.421 -5.360  12.393 1.00 54.24  ? 459 ILE   A N   1 
ATOM   1265 C  CA  . ILE   A 1 163 ? -27.329 -6.323  12.500 1.00 57.50  ? 459 ILE   A CA  1 
ATOM   1266 C  C   . ILE   A 1 163 ? -27.003 -6.825  11.101 1.00 57.45  ? 459 ILE   A C   1 
ATOM   1267 O  O   . ILE   A 1 163 ? -27.888 -6.928  10.242 1.00 59.58  ? 459 ILE   A O   1 
ATOM   1268 C  CB  . ILE   A 1 163 ? -27.681 -7.493  13.457 1.00 56.27  ? 459 ILE   A CB  1 
ATOM   1269 C  CG1 . ILE   A 1 163 ? -26.511 -8.460  13.619 1.00 54.64  ? 459 ILE   A CG1 1 
ATOM   1270 C  CG2 . ILE   A 1 163 ? -28.896 -8.238  12.947 1.00 58.25  ? 459 ILE   A CG2 1 
ATOM   1271 C  CD1 . ILE   A 1 163 ? -26.762 -9.551  14.723 1.00 56.25  ? 459 ILE   A CD1 1 
ATOM   1272 N  N   . THR   A 1 164 ? -25.721 -7.087  10.854 1.00 57.57  ? 460 THR   A N   1 
ATOM   1273 C  CA  . THR   A 1 164 ? -25.249 -7.576  9.560  1.00 57.87  ? 460 THR   A CA  1 
ATOM   1274 C  C   . THR   A 1 164 ? -24.519 -8.887  9.801  1.00 58.81  ? 460 THR   A C   1 
ATOM   1275 O  O   . THR   A 1 164 ? -23.538 -8.911  10.544 1.00 60.78  ? 460 THR   A O   1 
ATOM   1276 C  CB  . THR   A 1 164 ? -24.334 -6.564  8.876  1.00 56.88  ? 460 THR   A CB  1 
ATOM   1277 O  OG1 . THR   A 1 164 ? -25.073 -5.373  8.602  1.00 54.75  ? 460 THR   A OG1 1 
ATOM   1278 C  CG2 . THR   A 1 164 ? -23.861 -7.122  7.507  1.00 60.52  ? 460 THR   A CG2 1 
ATOM   1279 N  N   . ILE   A 1 165 ? -24.989 -9.972  9.176  1.00 58.55  ? 461 ILE   A N   1 
ATOM   1280 C  CA  . ILE   A 1 165 ? -24.556 -11.324 9.516  1.00 58.36  ? 461 ILE   A CA  1 
ATOM   1281 C  C   . ILE   A 1 165 ? -23.737 -11.873 8.360  1.00 60.94  ? 461 ILE   A C   1 
ATOM   1282 O  O   . ILE   A 1 165 ? -24.292 -12.245 7.326  1.00 61.17  ? 461 ILE   A O   1 
ATOM   1283 C  CB  . ILE   A 1 165 ? -25.750 -12.231 9.836  1.00 58.72  ? 461 ILE   A CB  1 
ATOM   1284 C  CG1 . ILE   A 1 165 ? -26.452 -11.773 11.127 1.00 57.47  ? 461 ILE   A CG1 1 
ATOM   1285 C  CG2 . ILE   A 1 165 ? -25.287 -13.646 10.034 1.00 61.74  ? 461 ILE   A CG2 1 
ATOM   1286 C  CD1 . ILE   A 1 165 ? -27.897 -12.203 11.209 1.00 60.06  ? 461 ILE   A CD1 1 
ATOM   1287 N  N   . PHE   A 1 166 ? -22.423 -11.930 8.541  1.00 59.61  ? 462 PHE   A N   1 
ATOM   1288 C  CA  . PHE   A 1 166 ? -21.501 -12.443 7.546  1.00 61.36  ? 462 PHE   A CA  1 
ATOM   1289 C  C   . PHE   A 1 166 ? -21.491 -13.966 7.596  1.00 64.54  ? 462 PHE   A C   1 
ATOM   1290 O  O   . PHE   A 1 166 ? -22.144 -14.560 8.455  1.00 65.34  ? 462 PHE   A O   1 
ATOM   1291 C  CB  . PHE   A 1 166 ? -20.132 -11.809 7.769  1.00 59.48  ? 462 PHE   A CB  1 
ATOM   1292 C  CG  . PHE   A 1 166 ? -20.108 -10.361 7.387  1.00 63.35  ? 462 PHE   A CG  1 
ATOM   1293 C  CD1 . PHE   A 1 166 ? -20.144 -9.991  6.042  1.00 62.07  ? 462 PHE   A CD1 1 
ATOM   1294 C  CD2 . PHE   A 1 166 ? -20.128 -9.362  8.359  1.00 60.71  ? 462 PHE   A CD2 1 
ATOM   1295 C  CE1 . PHE   A 1 166 ? -20.144 -8.651  5.681  1.00 64.25  ? 462 PHE   A CE1 1 
ATOM   1296 C  CE2 . PHE   A 1 166 ? -20.131 -8.016  7.989  1.00 60.61  ? 462 PHE   A CE2 1 
ATOM   1297 C  CZ  . PHE   A 1 166 ? -20.140 -7.658  6.669  1.00 65.33  ? 462 PHE   A CZ  1 
ATOM   1298 N  N   . PRO   A 1 167 ? -20.843 -14.629 6.626  1.00 64.68  ? 463 PRO   A N   1 
ATOM   1299 C  CA  . PRO   A 1 167 ? -20.946 -16.093 6.538  1.00 66.98  ? 463 PRO   A CA  1 
ATOM   1300 C  C   . PRO   A 1 167 ? -20.604 -16.782 7.855  1.00 69.68  ? 463 PRO   A C   1 
ATOM   1301 O  O   . PRO   A 1 167 ? -19.733 -16.343 8.611  1.00 68.30  ? 463 PRO   A O   1 
ATOM   1302 C  CB  . PRO   A 1 167 ? -19.951 -16.451 5.429  1.00 66.57  ? 463 PRO   A CB  1 
ATOM   1303 C  CG  . PRO   A 1 167 ? -19.978 -15.276 4.522  1.00 65.71  ? 463 PRO   A CG  1 
ATOM   1304 C  CD  . PRO   A 1 167 ? -20.166 -14.068 5.443  1.00 63.25  ? 463 PRO   A CD  1 
ATOM   1305 N  N   . GLN   A 1 168 ? -21.323 -17.860 8.138  1.00 74.53  ? 464 GLN   A N   1 
ATOM   1306 C  CA  . GLN   A 1 168 ? -21.100 -18.603 9.366  1.00 70.55  ? 464 GLN   A CA  1 
ATOM   1307 C  C   . GLN   A 1 168 ? -19.750 -19.306 9.317  1.00 75.65  ? 464 GLN   A C   1 
ATOM   1308 O  O   . GLN   A 1 168 ? -19.239 -19.647 8.243  1.00 72.37  ? 464 GLN   A O   1 
ATOM   1309 C  CB  . GLN   A 1 168 ? -22.201 -19.635 9.572  1.00 70.79  ? 464 GLN   A CB  1 
ATOM   1310 C  CG  . GLN   A 1 168 ? -22.248 -20.679 8.464  1.00 70.90  ? 464 GLN   A CG  1 
ATOM   1311 C  CD  . GLN   A 1 168 ? -23.640 -21.229 8.260  1.00 76.98  ? 464 GLN   A CD  1 
ATOM   1312 O  OE1 . GLN   A 1 168 ? -24.613 -20.478 8.173  1.00 72.63  ? 464 GLN   A OE1 1 
ATOM   1313 N  NE2 . GLN   A 1 168 ? -23.746 -22.558 8.180  1.00 78.34  ? 464 GLN   A NE2 1 
ATOM   1314 N  N   . ARG   A 1 169 ? -19.164 -19.509 10.499 1.00 73.55  ? 465 ARG   A N   1 
ATOM   1315 C  CA  . ARG   A 1 169 ? -17.959 -20.313 10.586 1.00 79.23  ? 465 ARG   A CA  1 
ATOM   1316 C  C   . ARG   A 1 169 ? -18.217 -21.674 9.956  1.00 82.97  ? 465 ARG   A C   1 
ATOM   1317 O  O   . ARG   A 1 169 ? -19.324 -22.212 10.037 1.00 82.62  ? 465 ARG   A O   1 
ATOM   1318 C  CB  . ARG   A 1 169 ? -17.525 -20.476 12.042 1.00 81.93  ? 465 ARG   A CB  1 
ATOM   1319 C  CG  . ARG   A 1 169 ? -16.418 -21.491 12.204 1.00 87.13  ? 465 ARG   A CG  1 
ATOM   1320 C  CD  . ARG   A 1 169 ? -15.920 -21.578 13.613 1.00 88.52  ? 465 ARG   A CD  1 
ATOM   1321 N  NE  . ARG   A 1 169 ? -15.222 -20.368 14.024 1.00 90.58  ? 465 ARG   A NE  1 
ATOM   1322 C  CZ  . ARG   A 1 169 ? -15.567 -19.623 15.064 1.00 84.81  ? 465 ARG   A CZ  1 
ATOM   1323 N  NH1 . ARG   A 1 169 ? -16.602 -19.938 15.828 1.00 84.47  ? 465 ARG   A NH1 1 
ATOM   1324 N  NH2 . ARG   A 1 169 ? -14.850 -18.539 15.349 1.00 85.19  ? 465 ARG   A NH2 1 
ATOM   1325 N  N   . THR   A 1 170 ? -17.204 -22.213 9.285  1.00 89.03  ? 466 THR   A N   1 
ATOM   1326 C  CA  . THR   A 1 170 ? -17.319 -23.546 8.706  1.00 91.72  ? 466 THR   A CA  1 
ATOM   1327 C  C   . THR   A 1 170 ? -16.284 -24.459 9.345  1.00 98.12  ? 466 THR   A C   1 
ATOM   1328 O  O   . THR   A 1 170 ? -16.561 -25.132 10.342 1.00 96.23  ? 466 THR   A O   1 
ATOM   1329 C  CB  . THR   A 1 170 ? -17.125 -23.516 7.189  1.00 92.19  ? 466 THR   A CB  1 
ATOM   1330 O  OG1 . THR   A 1 170 ? -16.003 -22.687 6.865  1.00 94.95  ? 466 THR   A OG1 1 
ATOM   1331 C  CG2 . THR   A 1 170 ? -18.382 -22.994 6.484  1.00 89.26  ? 466 THR   A CG2 1 
ATOM   1332 N  N   . ASP   A 1 171 ? -15.077 -24.468 8.778  1.00 100.04 ? 467 ASP   A N   1 
ATOM   1333 C  CA  . ASP   A 1 171 ? -13.992 -25.262 9.337  1.00 104.32 ? 467 ASP   A CA  1 
ATOM   1334 C  C   . ASP   A 1 171 ? -13.403 -24.615 10.581 1.00 107.97 ? 467 ASP   A C   1 
ATOM   1335 O  O   . ASP   A 1 171 ? -12.890 -25.321 11.455 1.00 115.11 ? 467 ASP   A O   1 
ATOM   1336 C  CB  . ASP   A 1 171 ? -12.898 -25.455 8.292  1.00 112.44 ? 467 ASP   A CB  1 
ATOM   1337 C  CG  . ASP   A 1 171 ? -12.264 -24.140 7.871  1.00 117.62 ? 467 ASP   A CG  1 
ATOM   1338 O  OD1 . ASP   A 1 171 ? -12.948 -23.092 7.948  1.00 118.85 ? 467 ASP   A OD1 1 
ATOM   1339 O  OD2 . ASP   A 1 171 ? -11.082 -24.154 7.465  1.00 121.66 ? 467 ASP   A OD2 1 
ATOM   1340 N  N   . GLY   A 1 172 ? -13.457 -23.286 10.681 1.00 107.49 ? 468 GLY   A N   1 
ATOM   1341 C  CA  . GLY   A 1 172 ? -12.792 -22.547 11.735 1.00 104.73 ? 468 GLY   A CA  1 
ATOM   1342 C  C   . GLY   A 1 172 ? -11.539 -21.824 11.286 1.00 107.31 ? 468 GLY   A C   1 
ATOM   1343 O  O   . GLY   A 1 172 ? -11.116 -20.874 11.953 1.00 104.74 ? 468 GLY   A O   1 
ATOM   1344 N  N   . LYS   A 1 173 ? -10.932 -22.248 10.178 1.00 109.80 ? 469 LYS   A N   1 
ATOM   1345 C  CA  . LYS   A 1 173 ? -9.792  -21.550 9.599  1.00 110.42 ? 469 LYS   A CA  1 
ATOM   1346 C  C   . LYS   A 1 173 ? -10.203 -20.554 8.526  1.00 110.84 ? 469 LYS   A C   1 
ATOM   1347 O  O   . LYS   A 1 173 ? -9.361  -19.781 8.056  1.00 108.42 ? 469 LYS   A O   1 
ATOM   1348 C  CB  . LYS   A 1 173 ? -8.796  -22.559 9.013  1.00 112.43 ? 469 LYS   A CB  1 
ATOM   1349 C  CG  . LYS   A 1 173 ? -8.069  -23.400 10.060 1.00 114.40 ? 469 LYS   A CG  1 
ATOM   1350 C  CD  . LYS   A 1 173 ? -6.776  -22.731 10.510 1.00 114.84 ? 469 LYS   A CD  1 
ATOM   1351 C  CE  . LYS   A 1 173 ? -5.772  -22.679 9.368  1.00 119.82 ? 469 LYS   A CE  1 
ATOM   1352 N  NZ  . LYS   A 1 173 ? -4.583  -21.844 9.690  1.00 120.00 ? 469 LYS   A NZ  1 
ATOM   1353 N  N   . HIS   A 1 174 ? -11.471 -20.558 8.129  1.00 107.62 ? 470 HIS   A N   1 
ATOM   1354 C  CA  . HIS   A 1 174 ? -12.016 -19.604 7.172  1.00 106.73 ? 470 HIS   A CA  1 
ATOM   1355 C  C   . HIS   A 1 174 ? -13.090 -18.816 7.911  1.00 105.18 ? 470 HIS   A C   1 
ATOM   1356 O  O   . HIS   A 1 174 ? -14.292 -19.041 7.748  1.00 106.49 ? 470 HIS   A O   1 
ATOM   1357 C  CB  . HIS   A 1 174 ? -12.555 -20.308 5.955  1.00 106.41 ? 470 HIS   A CB  1 
ATOM   1358 C  CG  . HIS   A 1 174 ? -11.528 -21.126 5.242  1.00 109.89 ? 470 HIS   A CG  1 
ATOM   1359 N  ND1 . HIS   A 1 174 ? -11.503 -22.502 5.302  1.00 113.13 ? 470 HIS   A ND1 1 
ATOM   1360 C  CD2 . HIS   A 1 174 ? -10.465 -20.760 4.488  1.00 111.70 ? 470 HIS   A CD2 1 
ATOM   1361 C  CE1 . HIS   A 1 174 ? -10.479 -22.951 4.598  1.00 119.27 ? 470 HIS   A CE1 1 
ATOM   1362 N  NE2 . HIS   A 1 174 ? -9.834  -21.914 4.093  1.00 120.12 ? 470 HIS   A NE2 1 
ATOM   1363 N  N   . ASP   A 1 175 ? -12.638 -17.893 8.751  1.00 102.00 ? 471 ASP   A N   1 
ATOM   1364 C  CA  . ASP   A 1 175 ? -13.514 -17.116 9.610  1.00 94.17  ? 471 ASP   A CA  1 
ATOM   1365 C  C   . ASP   A 1 175 ? -13.618 -15.685 9.115  1.00 91.37  ? 471 ASP   A C   1 
ATOM   1366 O  O   . ASP   A 1 175 ? -12.598 -15.030 8.877  1.00 94.27  ? 471 ASP   A O   1 
ATOM   1367 C  CB  . ASP   A 1 175 ? -13.002 -17.112 11.046 1.00 94.50  ? 471 ASP   A CB  1 
ATOM   1368 C  CG  . ASP   A 1 175 ? -13.501 -18.282 11.827 1.00 93.63  ? 471 ASP   A CG  1 
ATOM   1369 O  OD1 . ASP   A 1 175 ? -14.194 -19.132 11.234 1.00 96.57  ? 471 ASP   A OD1 1 
ATOM   1370 O  OD2 . ASP   A 1 175 ? -13.206 -18.353 13.027 1.00 94.15  ? 471 ASP   A OD2 1 
ATOM   1371 N  N   . PHE   A 1 176 ? -14.849 -15.200 8.985  1.00 84.53  ? 472 PHE   A N   1 
ATOM   1372 C  CA  . PHE   A 1 176 ? -15.089 -13.779 8.772  1.00 77.83  ? 472 PHE   A CA  1 
ATOM   1373 C  C   . PHE   A 1 176 ? -15.030 -13.070 10.112 1.00 75.40  ? 472 PHE   A C   1 
ATOM   1374 O  O   . PHE   A 1 176 ? -15.745 -13.452 11.039 1.00 70.60  ? 472 PHE   A O   1 
ATOM   1375 C  CB  . PHE   A 1 176 ? -16.446 -13.553 8.116  1.00 74.10  ? 472 PHE   A CB  1 
ATOM   1376 C  CG  . PHE   A 1 176 ? -16.464 -13.893 6.660  1.00 74.28  ? 472 PHE   A CG  1 
ATOM   1377 C  CD1 . PHE   A 1 176 ? -16.414 -15.212 6.249  1.00 75.26  ? 472 PHE   A CD1 1 
ATOM   1378 C  CD2 . PHE   A 1 176 ? -16.517 -12.897 5.709  1.00 74.19  ? 472 PHE   A CD2 1 
ATOM   1379 C  CE1 . PHE   A 1 176 ? -16.437 -15.531 4.897  1.00 75.77  ? 472 PHE   A CE1 1 
ATOM   1380 C  CE2 . PHE   A 1 176 ? -16.529 -13.211 4.360  1.00 72.12  ? 472 PHE   A CE2 1 
ATOM   1381 C  CZ  . PHE   A 1 176 ? -16.489 -14.532 3.962  1.00 71.71  ? 472 PHE   A CZ  1 
ATOM   1382 N  N   . ARG   A 1 177 ? -14.200 -12.035 10.210 1.00 74.27  ? 473 ARG   A N   1 
ATOM   1383 C  CA  . ARG   A 1 177 ? -14.065 -11.300 11.458 1.00 74.14  ? 473 ARG   A CA  1 
ATOM   1384 C  C   . ARG   A 1 177 ? -13.935 -9.815  11.174 1.00 72.92  ? 473 ARG   A C   1 
ATOM   1385 O  O   . ARG   A 1 177 ? -13.136 -9.411  10.323 1.00 74.35  ? 473 ARG   A O   1 
ATOM   1386 C  CB  . ARG   A 1 177 ? -12.843 -11.779 12.245 1.00 74.34  ? 473 ARG   A CB  1 
ATOM   1387 C  CG  . ARG   A 1 177 ? -12.983 -13.161 12.842 1.00 75.93  ? 473 ARG   A CG  1 
ATOM   1388 C  CD  . ARG   A 1 177 ? -14.158 -13.212 13.807 1.00 71.99  ? 473 ARG   A CD  1 
ATOM   1389 N  NE  . ARG   A 1 177 ? -14.024 -12.298 14.941 1.00 72.55  ? 473 ARG   A NE  1 
ATOM   1390 C  CZ  . ARG   A 1 177 ? -13.330 -12.564 16.041 1.00 76.30  ? 473 ARG   A CZ  1 
ATOM   1391 N  NH1 . ARG   A 1 177 ? -12.642 -13.690 16.167 1.00 76.42  ? 473 ARG   A NH1 1 
ATOM   1392 N  NH2 . ARG   A 1 177 ? -13.334 -11.681 17.045 1.00 74.46  ? 473 ARG   A NH2 1 
ATOM   1393 N  N   . VAL   A 1 178 ? -14.728 -9.012  11.874 1.00 71.04  ? 474 VAL   A N   1 
ATOM   1394 C  CA  . VAL   A 1 178 ? -14.391 -7.608  12.075 1.00 71.21  ? 474 VAL   A CA  1 
ATOM   1395 C  C   . VAL   A 1 178 ? -13.411 -7.543  13.236 1.00 74.00  ? 474 VAL   A C   1 
ATOM   1396 O  O   . VAL   A 1 178 ? -13.748 -7.926  14.362 1.00 74.45  ? 474 VAL   A O   1 
ATOM   1397 C  CB  . VAL   A 1 178 ? -15.637 -6.759  12.359 1.00 67.83  ? 474 VAL   A CB  1 
ATOM   1398 C  CG1 . VAL   A 1 178 ? -15.289 -5.286  12.284 1.00 69.02  ? 474 VAL   A CG1 1 
ATOM   1399 C  CG2 . VAL   A 1 178 ? -16.747 -7.085  11.373 1.00 69.10  ? 474 VAL   A CG2 1 
ATOM   1400 N  N   . TRP   A 1 179 ? -12.188 -7.092  12.963 1.00 75.51  ? 475 TRP   A N   1 
ATOM   1401 C  CA  . TRP   A 1 179 ? -11.190 -7.010  14.024 1.00 79.13  ? 475 TRP   A CA  1 
ATOM   1402 C  C   . TRP   A 1 179 ? -11.429 -5.842  14.970 1.00 78.16  ? 475 TRP   A C   1 
ATOM   1403 O  O   . TRP   A 1 179 ? -10.970 -5.895  16.117 1.00 79.26  ? 475 TRP   A O   1 
ATOM   1404 C  CB  . TRP   A 1 179 ? -9.782  -6.929  13.431 1.00 81.20  ? 475 TRP   A CB  1 
ATOM   1405 C  CG  . TRP   A 1 179 ? -9.310  -8.244  12.896 1.00 84.72  ? 475 TRP   A CG  1 
ATOM   1406 C  CD1 . TRP   A 1 179 ? -10.079 -9.220  12.329 1.00 82.69  ? 475 TRP   A CD1 1 
ATOM   1407 C  CD2 . TRP   A 1 179 ? -7.969  -8.745  12.904 1.00 87.92  ? 475 TRP   A CD2 1 
ATOM   1408 N  NE1 . TRP   A 1 179 ? -9.297  -10.292 11.966 1.00 85.22  ? 475 TRP   A NE1 1 
ATOM   1409 C  CE2 . TRP   A 1 179 ? -7.999  -10.025 12.311 1.00 89.76  ? 475 TRP   A CE2 1 
ATOM   1410 C  CE3 . TRP   A 1 179 ? -6.747  -8.232  13.342 1.00 90.68  ? 475 TRP   A CE3 1 
ATOM   1411 C  CZ2 . TRP   A 1 179 ? -6.855  -10.797 12.152 1.00 95.66  ? 475 TRP   A CZ2 1 
ATOM   1412 C  CZ3 . TRP   A 1 179 ? -5.619  -8.999  13.187 1.00 95.81  ? 475 TRP   A CZ3 1 
ATOM   1413 C  CH2 . TRP   A 1 179 ? -5.678  -10.268 12.597 1.00 102.38 ? 475 TRP   A CH2 1 
ATOM   1414 N  N   . ASN   A 1 180 ? -12.131 -4.802  14.523 1.00 75.82  ? 476 ASN   A N   1 
ATOM   1415 C  CA  . ASN   A 1 180 ? -12.538 -3.727  15.416 1.00 72.56  ? 476 ASN   A CA  1 
ATOM   1416 C  C   . ASN   A 1 180 ? -13.459 -4.281  16.491 1.00 71.11  ? 476 ASN   A C   1 
ATOM   1417 O  O   . ASN   A 1 180 ? -14.292 -5.154  16.224 1.00 67.83  ? 476 ASN   A O   1 
ATOM   1418 C  CB  . ASN   A 1 180 ? -13.276 -2.630  14.651 1.00 74.02  ? 476 ASN   A CB  1 
ATOM   1419 C  CG  . ASN   A 1 180 ? -12.528 -2.156  13.423 1.00 78.32  ? 476 ASN   A CG  1 
ATOM   1420 O  OD1 . ASN   A 1 180 ? -12.264 -2.935  12.500 1.00 76.45  ? 476 ASN   A OD1 1 
ATOM   1421 N  ND2 . ASN   A 1 180 ? -12.207 -0.864  13.389 1.00 80.28  ? 476 ASN   A ND2 1 
ATOM   1422 N  N   . SER   A 1 181 ? -13.308 -3.768  17.718 1.00 68.70  ? 477 SER   A N   1 
ATOM   1423 C  CA  . SER   A 1 181 ? -14.228 -4.154  18.787 1.00 66.61  ? 477 SER   A CA  1 
ATOM   1424 C  C   . SER   A 1 181 ? -15.610 -3.570  18.546 1.00 64.77  ? 477 SER   A C   1 
ATOM   1425 O  O   . SER   A 1 181 ? -16.627 -4.181  18.894 1.00 60.41  ? 477 SER   A O   1 
ATOM   1426 C  CB  . SER   A 1 181 ? -13.689 -3.703  20.147 1.00 66.54  ? 477 SER   A CB  1 
ATOM   1427 O  OG  . SER   A 1 181 ? -13.128 -2.392  20.064 1.00 67.58  ? 477 SER   A OG  1 
ATOM   1428 N  N   . GLN   A 1 182 ? -15.658 -2.388  17.941 1.00 65.12  ? 478 GLN   A N   1 
ATOM   1429 C  CA  . GLN   A 1 182 ? -16.892 -1.700  17.599 1.00 63.56  ? 478 GLN   A CA  1 
ATOM   1430 C  C   . GLN   A 1 182 ? -16.614 -0.947  16.307 1.00 64.27  ? 478 GLN   A C   1 
ATOM   1431 O  O   . GLN   A 1 182 ? -15.506 -0.442  16.115 1.00 67.78  ? 478 GLN   A O   1 
ATOM   1432 C  CB  . GLN   A 1 182 ? -17.350 -0.745  18.728 1.00 64.71  ? 478 GLN   A CB  1 
ATOM   1433 C  CG  . GLN   A 1 182 ? -17.868 -1.460  20.007 1.00 63.95  ? 478 GLN   A CG  1 
ATOM   1434 C  CD  . GLN   A 1 182 ? -17.445 -0.775  21.323 1.00 70.47  ? 478 GLN   A CD  1 
ATOM   1435 O  OE1 . GLN   A 1 182 ? -17.629 0.432   21.504 1.00 71.61  ? 478 GLN   A OE1 1 
ATOM   1436 N  NE2 . GLN   A 1 182 ? -16.876 -1.556  22.241 1.00 70.27  ? 478 GLN   A NE2 1 
ATOM   1437 N  N   . LEU   A 1 183 ? -17.611 -0.908  15.415 1.00 64.30  ? 479 LEU   A N   1 
ATOM   1438 C  CA  . LEU   A 1 183 ? -17.423 -0.352  14.077 1.00 63.52  ? 479 LEU   A CA  1 
ATOM   1439 C  C   . LEU   A 1 183 ? -16.817 1.039   14.112 1.00 65.64  ? 479 LEU   A C   1 
ATOM   1440 O  O   . LEU   A 1 183 ? -15.955 1.379   13.288 1.00 70.40  ? 479 LEU   A O   1 
ATOM   1441 C  CB  . LEU   A 1 183 ? -18.761 -0.306  13.344 1.00 63.88  ? 479 LEU   A CB  1 
ATOM   1442 C  CG  . LEU   A 1 183 ? -19.473 -1.626  13.043 1.00 64.03  ? 479 LEU   A CG  1 
ATOM   1443 C  CD1 . LEU   A 1 183 ? -20.618 -1.386  12.067 1.00 57.60  ? 479 LEU   A CD1 1 
ATOM   1444 C  CD2 . LEU   A 1 183 ? -18.483 -2.627  12.480 1.00 64.26  ? 479 LEU   A CD2 1 
ATOM   1445 N  N   . ILE   A 1 184 ? -17.276 1.872   15.035 1.00 65.36  ? 480 ILE   A N   1 
ATOM   1446 C  CA  . ILE   A 1 184 ? -16.803 3.234   15.162 1.00 65.70  ? 480 ILE   A CA  1 
ATOM   1447 C  C   . ILE   A 1 184 ? -16.218 3.385   16.560 1.00 73.18  ? 480 ILE   A C   1 
ATOM   1448 O  O   . ILE   A 1 184 ? -16.933 3.246   17.563 1.00 71.09  ? 480 ILE   A O   1 
ATOM   1449 C  CB  . ILE   A 1 184 ? -17.919 4.246   14.900 1.00 66.73  ? 480 ILE   A CB  1 
ATOM   1450 C  CG1 . ILE   A 1 184 ? -18.398 4.127   13.444 1.00 66.82  ? 480 ILE   A CG1 1 
ATOM   1451 C  CG2 . ILE   A 1 184 ? -17.416 5.656   15.133 1.00 71.32  ? 480 ILE   A CG2 1 
ATOM   1452 C  CD1 . ILE   A 1 184 ? -19.577 4.996   13.162 1.00 66.88  ? 480 ILE   A CD1 1 
ATOM   1453 N  N   . ARG   A 1 185 ? -14.908 3.616   16.622 1.00 73.68  ? 481 ARG   A N   1 
ATOM   1454 C  CA  . ARG   A 1 185 ? -14.198 3.873   17.865 1.00 75.49  ? 481 ARG   A CA  1 
ATOM   1455 C  C   . ARG   A 1 185 ? -13.077 4.854   17.572 1.00 82.68  ? 481 ARG   A C   1 
ATOM   1456 O  O   . ARG   A 1 185 ? -12.544 4.880   16.461 1.00 80.16  ? 481 ARG   A O   1 
ATOM   1457 C  CB  . ARG   A 1 185 ? -13.597 2.608   18.475 1.00 75.22  ? 481 ARG   A CB  1 
ATOM   1458 C  CG  . ARG   A 1 185 ? -14.572 1.491   18.732 1.00 74.13  ? 481 ARG   A CG  1 
ATOM   1459 C  CD  . ARG   A 1 185 ? -14.083 0.630   19.889 1.00 73.01  ? 481 ARG   A CD  1 
ATOM   1460 N  NE  . ARG   A 1 185 ? -13.939 1.404   21.113 1.00 76.98  ? 481 ARG   A NE  1 
ATOM   1461 C  CZ  . ARG   A 1 185 ? -13.582 0.884   22.280 1.00 76.39  ? 481 ARG   A CZ  1 
ATOM   1462 N  NH1 . ARG   A 1 185 ? -13.341 -0.412  22.414 1.00 70.93  ? 481 ARG   A NH1 1 
ATOM   1463 N  NH2 . ARG   A 1 185 ? -13.442 1.688   23.332 1.00 79.49  ? 481 ARG   A NH2 1 
ATOM   1464 N  N   . TYR   A 1 186 ? -12.711 5.644   18.580 1.00 81.02  ? 482 TYR   A N   1 
ATOM   1465 C  CA  . TYR   A 1 186 ? -11.603 6.571   18.459 1.00 89.18  ? 482 TYR   A CA  1 
ATOM   1466 C  C   . TYR   A 1 186 ? -10.276 5.872   18.722 1.00 90.64  ? 482 TYR   A C   1 
ATOM   1467 O  O   . TYR   A 1 186 ? -10.198 4.886   19.461 1.00 88.48  ? 482 TYR   A O   1 
ATOM   1468 C  CB  . TYR   A 1 186 ? -11.790 7.754   19.410 1.00 90.17  ? 482 TYR   A CB  1 
ATOM   1469 C  CG  . TYR   A 1 186 ? -13.066 8.498   19.106 1.00 91.89  ? 482 TYR   A CG  1 
ATOM   1470 C  CD1 . TYR   A 1 186 ? -13.309 9.009   17.835 1.00 93.04  ? 482 TYR   A CD1 1 
ATOM   1471 C  CD2 . TYR   A 1 186 ? -14.045 8.649   20.060 1.00 90.24  ? 482 TYR   A CD2 1 
ATOM   1472 C  CE1 . TYR   A 1 186 ? -14.483 9.686   17.548 1.00 92.10  ? 482 TYR   A CE1 1 
ATOM   1473 C  CE2 . TYR   A 1 186 ? -15.218 9.316   19.780 1.00 89.45  ? 482 TYR   A CE2 1 
ATOM   1474 C  CZ  . TYR   A 1 186 ? -15.437 9.831   18.531 1.00 89.45  ? 482 TYR   A CZ  1 
ATOM   1475 O  OH  . TYR   A 1 186 ? -16.620 10.489  18.284 1.00 87.46  ? 482 TYR   A OH  1 
ATOM   1476 N  N   . ALA   A 1 187 ? -9.234  6.385   18.077 1.00 92.99  ? 483 ALA   A N   1 
ATOM   1477 C  CA  . ALA   A 1 187 ? -7.908  5.800   18.181 1.00 96.84  ? 483 ALA   A CA  1 
ATOM   1478 C  C   . ALA   A 1 187 ? -7.301  6.043   19.557 1.00 99.24  ? 483 ALA   A C   1 
ATOM   1479 O  O   . ALA   A 1 187 ? -7.550  7.064   20.201 1.00 96.73  ? 483 ALA   A O   1 
ATOM   1480 C  CB  . ALA   A 1 187 ? -6.984  6.380   17.115 1.00 99.50  ? 483 ALA   A CB  1 
ATOM   1481 N  N   . GLY   A 1 188 ? -6.479  5.092   19.989 1.00 98.91  ? 484 GLY   A N   1 
ATOM   1482 C  CA  . GLY   A 1 188 ? -5.679  5.263   21.179 1.00 101.27 ? 484 GLY   A CA  1 
ATOM   1483 C  C   . GLY   A 1 188 ? -4.202  5.396   20.884 1.00 107.37 ? 484 GLY   A C   1 
ATOM   1484 O  O   . GLY   A 1 188 ? -3.582  4.471   20.350 1.00 107.35 ? 484 GLY   A O   1 
ATOM   1485 N  N   . TYR   A 1 189 ? -3.627  6.544   21.231 1.00 115.24 ? 485 TYR   A N   1 
ATOM   1486 C  CA  . TYR   A 1 189 ? -2.212  6.813   21.020 1.00 119.26 ? 485 TYR   A CA  1 
ATOM   1487 C  C   . TYR   A 1 189 ? -1.539  7.011   22.368 1.00 125.65 ? 485 TYR   A C   1 
ATOM   1488 O  O   . TYR   A 1 189 ? -1.862  7.959   23.094 1.00 127.31 ? 485 TYR   A O   1 
ATOM   1489 C  CB  . TYR   A 1 189 ? -1.994  8.053   20.152 1.00 119.83 ? 485 TYR   A CB  1 
ATOM   1490 C  CG  . TYR   A 1 189 ? -2.768  8.092   18.857 1.00 117.60 ? 485 TYR   A CG  1 
ATOM   1491 C  CD1 . TYR   A 1 189 ? -2.337  7.386   17.745 1.00 119.01 ? 485 TYR   A CD1 1 
ATOM   1492 C  CD2 . TYR   A 1 189 ? -3.915  8.865   18.743 1.00 116.07 ? 485 TYR   A CD2 1 
ATOM   1493 C  CE1 . TYR   A 1 189 ? -3.042  7.430   16.558 1.00 120.85 ? 485 TYR   A CE1 1 
ATOM   1494 C  CE2 . TYR   A 1 189 ? -4.623  8.921   17.568 1.00 118.56 ? 485 TYR   A CE2 1 
ATOM   1495 C  CZ  . TYR   A 1 189 ? -4.181  8.206   16.471 1.00 118.20 ? 485 TYR   A CZ  1 
ATOM   1496 O  OH  . TYR   A 1 189 ? -4.892  8.265   15.298 1.00 115.98 ? 485 TYR   A OH  1 
ATOM   1497 N  N   . LYS   A 1 190 ? -0.611  6.123   22.699 1.00 129.25 ? 486 LYS   A N   1 
ATOM   1498 C  CA  . LYS   A 1 190 ? 0.299   6.369   23.803 1.00 137.66 ? 486 LYS   A CA  1 
ATOM   1499 C  C   . LYS   A 1 190 ? 1.337   7.405   23.386 1.00 143.22 ? 486 LYS   A C   1 
ATOM   1500 O  O   . LYS   A 1 190 ? 1.737   7.477   22.220 1.00 144.40 ? 486 LYS   A O   1 
ATOM   1501 C  CB  . LYS   A 1 190 ? 0.975   5.068   24.228 1.00 139.17 ? 486 LYS   A CB  1 
ATOM   1502 C  CG  . LYS   A 1 190 ? 1.365   4.202   23.045 1.00 141.49 ? 486 LYS   A CG  1 
ATOM   1503 C  CD  . LYS   A 1 190 ? 2.336   3.105   23.435 1.00 143.52 ? 486 LYS   A CD  1 
ATOM   1504 C  CE  . LYS   A 1 190 ? 1.614   1.853   23.888 1.00 142.69 ? 486 LYS   A CE  1 
ATOM   1505 N  NZ  . LYS   A 1 190 ? 2.392   0.635   23.523 1.00 142.56 ? 486 LYS   A NZ  1 
ATOM   1506 N  N   . GLN   A 1 191 ? 1.766   8.218   24.346 1.00 144.10 ? 487 GLN   A N   1 
ATOM   1507 C  CA  . GLN   A 1 191 ? 2.642   9.348   24.068 1.00 147.05 ? 487 GLN   A CA  1 
ATOM   1508 C  C   . GLN   A 1 191 ? 4.092   9.013   24.386 1.00 151.56 ? 487 GLN   A C   1 
ATOM   1509 O  O   . GLN   A 1 191 ? 4.377   8.122   25.193 1.00 151.34 ? 487 GLN   A O   1 
ATOM   1510 C  CB  . GLN   A 1 191 ? 2.205   10.571  24.884 1.00 147.75 ? 487 GLN   A CB  1 
ATOM   1511 C  CG  . GLN   A 1 191 ? 0.870   11.169  24.462 1.00 142.97 ? 487 GLN   A CG  1 
ATOM   1512 C  CD  . GLN   A 1 191 ? 0.928   11.869  23.111 1.00 148.68 ? 487 GLN   A CD  1 
ATOM   1513 O  OE1 . GLN   A 1 191 ? 1.074   11.234  22.063 1.00 145.64 ? 487 GLN   A OE1 1 
ATOM   1514 N  NE2 . GLN   A 1 191 ? 0.811   13.191  23.133 1.00 154.69 ? 487 GLN   A NE2 1 
ATOM   1515 N  N   . PRO   A 1 192 ? 5.045   9.720   23.769 1.00 153.66 ? 488 PRO   A N   1 
ATOM   1516 C  CA  . PRO   A 1 192 ? 6.461   9.485   24.099 1.00 155.96 ? 488 PRO   A CA  1 
ATOM   1517 C  C   . PRO   A 1 192 ? 6.805   9.750   25.554 1.00 156.68 ? 488 PRO   A C   1 
ATOM   1518 O  O   . PRO   A 1 192 ? 7.882   9.337   26.003 1.00 159.67 ? 488 PRO   A O   1 
ATOM   1519 C  CB  . PRO   A 1 192 ? 7.207   10.447  23.162 1.00 160.09 ? 488 PRO   A CB  1 
ATOM   1520 C  CG  . PRO   A 1 192 ? 6.178   11.440  22.713 1.00 158.24 ? 488 PRO   A CG  1 
ATOM   1521 C  CD  . PRO   A 1 192 ? 4.891   10.690  22.672 1.00 155.98 ? 488 PRO   A CD  1 
ATOM   1522 N  N   . ASP   A 1 193 ? 5.930   10.418  26.308 1.00 155.61 ? 489 ASP   A N   1 
ATOM   1523 C  CA  . ASP   A 1 193 ? 6.116   10.615  27.739 1.00 152.36 ? 489 ASP   A CA  1 
ATOM   1524 C  C   . ASP   A 1 193 ? 5.249   9.680   28.572 1.00 149.66 ? 489 ASP   A C   1 
ATOM   1525 O  O   . ASP   A 1 193 ? 5.015   9.954   29.753 1.00 148.75 ? 489 ASP   A O   1 
ATOM   1526 C  CB  . ASP   A 1 193 ? 5.820   12.063  28.127 1.00 154.18 ? 489 ASP   A CB  1 
ATOM   1527 C  CG  . ASP   A 1 193 ? 4.381   12.448  27.858 1.00 152.56 ? 489 ASP   A CG  1 
ATOM   1528 O  OD1 . ASP   A 1 193 ? 4.004   12.537  26.665 1.00 151.98 ? 489 ASP   A OD1 1 
ATOM   1529 O  OD2 . ASP   A 1 193 ? 3.627   12.638  28.839 1.00 146.80 ? 489 ASP   A OD2 1 
ATOM   1530 N  N   . GLY   A 1 194 ? 4.745   8.600   27.979 1.00 147.52 ? 490 GLY   A N   1 
ATOM   1531 C  CA  . GLY   A 1 194 ? 4.031   7.578   28.708 1.00 146.45 ? 490 GLY   A CA  1 
ATOM   1532 C  C   . GLY   A 1 194 ? 2.521   7.729   28.757 1.00 143.58 ? 490 GLY   A C   1 
ATOM   1533 O  O   . GLY   A 1 194 ? 1.816   6.717   28.831 1.00 143.44 ? 490 GLY   A O   1 
ATOM   1534 N  N   . SER   A 1 195 ? 2.004   8.955   28.725 1.00 143.93 ? 491 SER   A N   1 
ATOM   1535 C  CA  . SER   A 1 195 ? 0.562   9.172   28.809 1.00 139.49 ? 491 SER   A CA  1 
ATOM   1536 C  C   . SER   A 1 195 ? -0.105  8.709   27.505 1.00 136.79 ? 491 SER   A C   1 
ATOM   1537 O  O   . SER   A 1 195 ? 0.511   8.068   26.650 1.00 136.44 ? 491 SER   A O   1 
ATOM   1538 C  CB  . SER   A 1 195 ? 0.265   10.631  29.145 1.00 135.95 ? 491 SER   A CB  1 
ATOM   1539 O  OG  . SER   A 1 195 ? 1.033   11.517  28.350 1.00 141.76 ? 491 SER   A OG  1 
ATOM   1540 N  N   . THR   A 1 196 ? -1.391  9.026   27.343 1.00 131.86 ? 492 THR   A N   1 
ATOM   1541 C  CA  . THR   A 1 196 ? -2.187  8.451   26.263 1.00 127.38 ? 492 THR   A CA  1 
ATOM   1542 C  C   . THR   A 1 196 ? -3.147  9.481   25.681 1.00 124.16 ? 492 THR   A C   1 
ATOM   1543 O  O   . THR   A 1 196 ? -3.887  10.131  26.425 1.00 125.42 ? 492 THR   A O   1 
ATOM   1544 C  CB  . THR   A 1 196 ? -2.970  7.228   26.765 1.00 122.98 ? 492 THR   A CB  1 
ATOM   1545 O  OG1 . THR   A 1 196 ? -2.059  6.266   27.315 1.00 122.86 ? 492 THR   A OG1 1 
ATOM   1546 C  CG2 . THR   A 1 196 ? -3.762  6.590   25.636 1.00 115.02 ? 492 THR   A CG2 1 
ATOM   1547 N  N   . LEU   A 1 197 ? -3.141  9.610   24.350 1.00 122.89 ? 493 LEU   A N   1 
ATOM   1548 C  CA  . LEU   A 1 197 ? -4.058  10.481  23.623 1.00 118.26 ? 493 LEU   A CA  1 
ATOM   1549 C  C   . LEU   A 1 197 ? -5.191  9.650   23.031 1.00 112.17 ? 493 LEU   A C   1 
ATOM   1550 O  O   . LEU   A 1 197 ? -4.987  8.499   22.627 1.00 111.16 ? 493 LEU   A O   1 
ATOM   1551 C  CB  . LEU   A 1 197 ? -3.329  11.246  22.511 1.00 117.90 ? 493 LEU   A CB  1 
ATOM   1552 C  CG  . LEU   A 1 197 ? -4.071  12.388  21.801 1.00 116.69 ? 493 LEU   A CG  1 
ATOM   1553 C  CD1 . LEU   A 1 197 ? -4.517  13.463  22.774 1.00 117.13 ? 493 LEU   A CD1 1 
ATOM   1554 C  CD2 . LEU   A 1 197 ? -3.209  13.011  20.700 1.00 124.64 ? 493 LEU   A CD2 1 
ATOM   1555 N  N   . GLY   A 1 198 ? -6.391  10.227  22.999 1.00 107.96 ? 494 GLY   A N   1 
ATOM   1556 C  CA  . GLY   A 1 198 ? -7.546  9.501   22.506 1.00 103.53 ? 494 GLY   A CA  1 
ATOM   1557 C  C   . GLY   A 1 198 ? -8.051  8.461   23.481 1.00 96.72  ? 494 GLY   A C   1 
ATOM   1558 O  O   . GLY   A 1 198 ? -8.094  8.711   24.694 1.00 100.73 ? 494 GLY   A O   1 
ATOM   1559 N  N   . ASP   A 1 199 ? -8.403  7.278   22.982 1.00 95.65  ? 495 ASP   A N   1 
ATOM   1560 C  CA  . ASP   A 1 199 ? -9.026  6.268   23.826 1.00 93.70  ? 495 ASP   A CA  1 
ATOM   1561 C  C   . ASP   A 1 199 ? -8.005  5.219   24.234 1.00 94.30  ? 495 ASP   A C   1 
ATOM   1562 O  O   . ASP   A 1 199 ? -7.596  4.412   23.389 1.00 94.43  ? 495 ASP   A O   1 
ATOM   1563 C  CB  . ASP   A 1 199 ? -10.190 5.609   23.093 1.00 92.17  ? 495 ASP   A CB  1 
ATOM   1564 C  CG  . ASP   A 1 199 ? -11.157 4.927   24.025 1.00 90.56  ? 495 ASP   A CG  1 
ATOM   1565 O  OD1 . ASP   A 1 199 ? -10.735 4.517   25.135 1.00 85.99  ? 495 ASP   A OD1 1 
ATOM   1566 O  OD2 . ASP   A 1 199 ? -12.348 4.804   23.649 1.00 87.58  ? 495 ASP   A OD2 1 
ATOM   1567 N  N   . PRO   A 1 200 ? -7.590  5.163   25.505 1.00 93.97  ? 496 PRO   A N   1 
ATOM   1568 C  CA  . PRO   A 1 200 ? -6.621  4.133   25.919 1.00 94.09  ? 496 PRO   A CA  1 
ATOM   1569 C  C   . PRO   A 1 200 ? -7.111  2.707   25.722 1.00 92.15  ? 496 PRO   A C   1 
ATOM   1570 O  O   . PRO   A 1 200 ? -6.282  1.790   25.684 1.00 92.85  ? 496 PRO   A O   1 
ATOM   1571 C  CB  . PRO   A 1 200 ? -6.385  4.443   27.406 1.00 94.22  ? 496 PRO   A CB  1 
ATOM   1572 C  CG  . PRO   A 1 200 ? -6.770  5.888   27.563 1.00 95.04  ? 496 PRO   A CG  1 
ATOM   1573 C  CD  . PRO   A 1 200 ? -7.919  6.088   26.598 1.00 91.74  ? 496 PRO   A CD  1 
ATOM   1574 N  N   . ALA   A 1 201 ? -8.421  2.485   25.587 1.00 89.00  ? 497 ALA   A N   1 
ATOM   1575 C  CA  . ALA   A 1 201 ? -8.921  1.135   25.335 1.00 90.95  ? 497 ALA   A CA  1 
ATOM   1576 C  C   . ALA   A 1 201 ? -8.370  0.568   24.035 1.00 92.17  ? 497 ALA   A C   1 
ATOM   1577 O  O   . ALA   A 1 201 ? -8.073  -0.628  23.946 1.00 94.86  ? 497 ALA   A O   1 
ATOM   1578 C  CB  . ALA   A 1 201 ? -10.451 1.129   25.290 1.00 87.26  ? 497 ALA   A CB  1 
ATOM   1579 N  N   . ASN   A 1 202 ? -8.223  1.412   23.018 1.00 92.58  ? 498 ASN   A N   1 
ATOM   1580 C  CA  . ASN   A 1 202 ? -7.911  0.973   21.665 1.00 94.84  ? 498 ASN   A CA  1 
ATOM   1581 C  C   . ASN   A 1 202 ? -6.439  1.140   21.319 1.00 98.34  ? 498 ASN   A C   1 
ATOM   1582 O  O   . ASN   A 1 202 ? -6.085  1.113   20.136 1.00 99.57  ? 498 ASN   A O   1 
ATOM   1583 C  CB  . ASN   A 1 202 ? -8.780  1.736   20.665 1.00 92.63  ? 498 ASN   A CB  1 
ATOM   1584 C  CG  . ASN   A 1 202 ? -10.238 1.758   21.078 1.00 86.34  ? 498 ASN   A CG  1 
ATOM   1585 O  OD1 . ASN   A 1 202 ? -10.779 0.734   21.499 1.00 84.29  ? 498 ASN   A OD1 1 
ATOM   1586 N  ND2 . ASN   A 1 202 ? -10.877 2.925   20.983 1.00 83.94  ? 498 ASN   A ND2 1 
ATOM   1587 N  N   . VAL   A 1 203 ? -5.576  1.305   22.327 1.00 102.61 ? 499 VAL   A N   1 
ATOM   1588 C  CA  . VAL   A 1 203 ? -4.168  1.590   22.058 1.00 106.38 ? 499 VAL   A CA  1 
ATOM   1589 C  C   . VAL   A 1 203 ? -3.517  0.440   21.303 1.00 110.26 ? 499 VAL   A C   1 
ATOM   1590 O  O   . VAL   A 1 203 ? -2.747  0.658   20.361 1.00 114.96 ? 499 VAL   A O   1 
ATOM   1591 C  CB  . VAL   A 1 203 ? -3.421  1.905   23.366 1.00 104.14 ? 499 VAL   A CB  1 
ATOM   1592 C  CG1 . VAL   A 1 203 ? -1.922  1.803   23.159 1.00 113.11 ? 499 VAL   A CG1 1 
ATOM   1593 C  CG2 . VAL   A 1 203 ? -3.788  3.293   23.847 1.00 104.76 ? 499 VAL   A CG2 1 
ATOM   1594 N  N   . GLN   A 1 204 ? -3.815  -0.801  21.691 1.00 102.66 ? 500 GLN   A N   1 
ATOM   1595 C  CA  . GLN   A 1 204 ? -3.282  -1.930  20.935 1.00 106.73 ? 500 GLN   A CA  1 
ATOM   1596 C  C   . GLN   A 1 204 ? -3.871  -1.968  19.531 1.00 104.79 ? 500 GLN   A C   1 
ATOM   1597 O  O   . GLN   A 1 204 ? -3.135  -2.049  18.541 1.00 109.15 ? 500 GLN   A O   1 
ATOM   1598 C  CB  . GLN   A 1 204 ? -3.549  -3.252  21.657 1.00 107.53 ? 500 GLN   A CB  1 
ATOM   1599 C  CG  . GLN   A 1 204 ? -3.314  -4.471  20.758 1.00 106.93 ? 500 GLN   A CG  1 
ATOM   1600 C  CD  . GLN   A 1 204 ? -2.886  -5.723  21.515 1.00 107.78 ? 500 GLN   A CD  1 
ATOM   1601 O  OE1 . GLN   A 1 204 ? -3.190  -5.888  22.699 1.00 107.76 ? 500 GLN   A OE1 1 
ATOM   1602 N  NE2 . GLN   A 1 204 ? -2.171  -6.612  20.827 1.00 108.15 ? 500 GLN   A NE2 1 
ATOM   1603 N  N   . PHE   A 1 205 ? -5.201  -1.904  19.428 1.00 103.76 ? 501 PHE   A N   1 
ATOM   1604 C  CA  . PHE   A 1 205 ? -5.843  -1.965  18.118 1.00 101.55 ? 501 PHE   A CA  1 
ATOM   1605 C  C   . PHE   A 1 205 ? -5.357  -0.840  17.213 1.00 104.07 ? 501 PHE   A C   1 
ATOM   1606 O  O   . PHE   A 1 205 ? -5.116  -1.055  16.020 1.00 103.13 ? 501 PHE   A O   1 
ATOM   1607 C  CB  . PHE   A 1 205 ? -7.365  -1.917  18.258 1.00 95.10  ? 501 PHE   A CB  1 
ATOM   1608 C  CG  . PHE   A 1 205 ? -8.083  -1.991  16.944 1.00 94.65  ? 501 PHE   A CG  1 
ATOM   1609 C  CD1 . PHE   A 1 205 ? -8.296  -3.214  16.327 1.00 91.27  ? 501 PHE   A CD1 1 
ATOM   1610 C  CD2 . PHE   A 1 205 ? -8.522  -0.835  16.307 1.00 92.79  ? 501 PHE   A CD2 1 
ATOM   1611 C  CE1 . PHE   A 1 205 ? -8.945  -3.290  15.102 1.00 87.49  ? 501 PHE   A CE1 1 
ATOM   1612 C  CE2 . PHE   A 1 205 ? -9.172  -0.901  15.080 1.00 90.06  ? 501 PHE   A CE2 1 
ATOM   1613 C  CZ  . PHE   A 1 205 ? -9.383  -2.131  14.476 1.00 87.36  ? 501 PHE   A CZ  1 
ATOM   1614 N  N   . THR   A 1 206 ? -5.210  0.369   17.760 1.00 103.71 ? 502 THR   A N   1 
ATOM   1615 C  CA  . THR   A 1 206 ? -4.703  1.475   16.957 1.00 106.51 ? 502 THR   A CA  1 
ATOM   1616 C  C   . THR   A 1 206 ? -3.333  1.145   16.379 1.00 112.55 ? 502 THR   A C   1 
ATOM   1617 O  O   . THR   A 1 206 ? -3.043  1.473   15.222 1.00 115.46 ? 502 THR   A O   1 
ATOM   1618 C  CB  . THR   A 1 206 ? -4.645  2.756   17.792 1.00 105.72 ? 502 THR   A CB  1 
ATOM   1619 O  OG1 . THR   A 1 206 ? -5.972  3.135   18.177 1.00 101.82 ? 502 THR   A OG1 1 
ATOM   1620 C  CG2 . THR   A 1 206 ? -4.004  3.899   16.999 1.00 107.53 ? 502 THR   A CG2 1 
ATOM   1621 N  N   . GLU   A 1 207 ? -2.487  0.466   17.155 1.00 119.87 ? 503 GLU   A N   1 
ATOM   1622 C  CA  . GLU   A 1 207 ? -1.159  0.131   16.653 1.00 124.47 ? 503 GLU   A CA  1 
ATOM   1623 C  C   . GLU   A 1 207 ? -1.223  -0.987  15.619 1.00 125.07 ? 503 GLU   A C   1 
ATOM   1624 O  O   . GLU   A 1 207 ? -0.488  -0.959  14.624 1.00 132.62 ? 503 GLU   A O   1 
ATOM   1625 C  CB  . GLU   A 1 207 ? -0.233  -0.233  17.813 1.00 129.53 ? 503 GLU   A CB  1 
ATOM   1626 C  CG  . GLU   A 1 207 ? 0.470   0.984   18.411 1.00 138.10 ? 503 GLU   A CG  1 
ATOM   1627 C  CD  . GLU   A 1 207 ? 0.290   1.102   19.921 1.00 144.58 ? 503 GLU   A CD  1 
ATOM   1628 O  OE1 . GLU   A 1 207 ? -0.029  0.077   20.564 1.00 143.29 ? 503 GLU   A OE1 1 
ATOM   1629 O  OE2 . GLU   A 1 207 ? 0.468   2.218   20.467 1.00 149.01 ? 503 GLU   A OE2 1 
ATOM   1630 N  N   . ILE   A 1 208 ? -2.110  -1.965  15.825 1.00 116.62 ? 504 ILE   A N   1 
ATOM   1631 C  CA  . ILE   A 1 208 ? -2.287  -3.041  14.848 1.00 113.97 ? 504 ILE   A CA  1 
ATOM   1632 C  C   . ILE   A 1 208 ? -2.614  -2.471  13.471 1.00 116.80 ? 504 ILE   A C   1 
ATOM   1633 O  O   . ILE   A 1 208 ? -2.082  -2.925  12.450 1.00 117.45 ? 504 ILE   A O   1 
ATOM   1634 C  CB  . ILE   A 1 208 ? -3.374  -4.021  15.329 1.00 106.00 ? 504 ILE   A CB  1 
ATOM   1635 C  CG1 . ILE   A 1 208 ? -2.881  -4.808  16.540 1.00 104.58 ? 504 ILE   A CG1 1 
ATOM   1636 C  CG2 . ILE   A 1 208 ? -3.775  -4.973  14.225 1.00 100.71 ? 504 ILE   A CG2 1 
ATOM   1637 C  CD1 . ILE   A 1 208 ? -3.952  -5.669  17.197 1.00 102.48 ? 504 ILE   A CD1 1 
ATOM   1638 N  N   . CYS   A 1 209 ? -3.484  -1.461  13.424 1.00 112.51 ? 505 CYS   A N   1 
ATOM   1639 C  CA  . CYS   A 1 209 ? -3.833  -0.843  12.153 1.00 112.04 ? 505 CYS   A CA  1 
ATOM   1640 C  C   . CYS   A 1 209 ? -2.626  -0.171  11.514 1.00 119.87 ? 505 CYS   A C   1 
ATOM   1641 O  O   . CYS   A 1 209 ? -2.471  -0.196  10.286 1.00 118.83 ? 505 CYS   A O   1 
ATOM   1642 C  CB  . CYS   A 1 209 ? -4.966  0.160   12.355 1.00 106.53 ? 505 CYS   A CB  1 
ATOM   1643 S  SG  . CYS   A 1 209 ? -6.452  -0.589  13.026 1.00 98.19  ? 505 CYS   A SG  1 
ATOM   1644 N  N   . ILE   A 1 210 ? -1.752  0.428   12.326 1.00 117.43 ? 506 ILE   A N   1 
ATOM   1645 C  CA  . ILE   A 1 210 ? -0.566  1.059   11.757 1.00 121.50 ? 506 ILE   A CA  1 
ATOM   1646 C  C   . ILE   A 1 210 ? 0.411   0.003   11.247 1.00 122.27 ? 506 ILE   A C   1 
ATOM   1647 O  O   . ILE   A 1 210 ? 1.109   0.222   10.247 1.00 124.28 ? 506 ILE   A O   1 
ATOM   1648 C  CB  . ILE   A 1 210 ? 0.088   1.998   12.787 1.00 123.04 ? 506 ILE   A CB  1 
ATOM   1649 C  CG1 . ILE   A 1 210 ? -0.965  2.924   13.396 1.00 119.00 ? 506 ILE   A CG1 1 
ATOM   1650 C  CG2 . ILE   A 1 210 ? 1.172   2.836   12.120 1.00 127.56 ? 506 ILE   A CG2 1 
ATOM   1651 C  CD1 . ILE   A 1 210 ? -0.399  3.955   14.350 1.00 122.96 ? 506 ILE   A CD1 1 
ATOM   1652 N  N   . GLN   A 1 211 ? 0.466   -1.159  11.906 1.00 123.34 ? 507 GLN   A N   1 
ATOM   1653 C  CA  . GLN   A 1 211 ? 1.322   -2.241  11.430 1.00 125.50 ? 507 GLN   A CA  1 
ATOM   1654 C  C   . GLN   A 1 211 ? 0.821   -2.805  10.107 1.00 124.14 ? 507 GLN   A C   1 
ATOM   1655 O  O   . GLN   A 1 211 ? 1.623   -3.284  9.297  1.00 123.76 ? 507 GLN   A O   1 
ATOM   1656 C  CB  . GLN   A 1 211 ? 1.413   -3.344  12.487 1.00 128.81 ? 507 GLN   A CB  1 
ATOM   1657 C  CG  . GLN   A 1 211 ? 1.859   -2.855  13.864 1.00 132.98 ? 507 GLN   A CG  1 
ATOM   1658 C  CD  . GLN   A 1 211 ? 3.334   -2.488  13.921 1.00 143.22 ? 507 GLN   A CD  1 
ATOM   1659 O  OE1 . GLN   A 1 211 ? 4.175   -3.156  13.318 1.00 148.99 ? 507 GLN   A OE1 1 
ATOM   1660 N  NE2 . GLN   A 1 211 ? 3.655   -1.424  14.653 1.00 144.01 ? 507 GLN   A NE2 1 
ATOM   1661 N  N   . GLN   A 1 212 ? -0.491  -2.763  9.871  1.00 121.79 ? 508 GLN   A N   1 
ATOM   1662 C  CA  . GLN   A 1 212 ? -1.057  -3.101  8.572  1.00 121.09 ? 508 GLN   A CA  1 
ATOM   1663 C  C   . GLN   A 1 212 ? -1.126  -1.899  7.641  1.00 119.22 ? 508 GLN   A C   1 
ATOM   1664 O  O   . GLN   A 1 212 ? -1.552  -2.048  6.491  1.00 116.41 ? 508 GLN   A O   1 
ATOM   1665 C  CB  . GLN   A 1 212 ? -2.449  -3.717  8.733  1.00 117.61 ? 508 GLN   A CB  1 
ATOM   1666 C  CG  . GLN   A 1 212 ? -2.520  -4.849  9.751  1.00 119.73 ? 508 GLN   A CG  1 
ATOM   1667 C  CD  . GLN   A 1 212 ? -1.913  -6.156  9.261  1.00 126.38 ? 508 GLN   A CD  1 
ATOM   1668 O  OE1 . GLN   A 1 212 ? -2.621  -7.145  9.070  1.00 127.60 ? 508 GLN   A OE1 1 
ATOM   1669 N  NE2 . GLN   A 1 212 ? -0.596  -6.176  9.084  1.00 126.74 ? 508 GLN   A NE2 1 
ATOM   1670 N  N   . GLY   A 1 213 ? -0.727  -0.718  8.110  1.00 121.38 ? 509 GLY   A N   1 
ATOM   1671 C  CA  . GLY   A 1 213 ? -0.488  0.391   7.208  1.00 122.15 ? 509 GLY   A CA  1 
ATOM   1672 C  C   . GLY   A 1 213 ? -1.245  1.671   7.487  1.00 123.43 ? 509 GLY   A C   1 
ATOM   1673 O  O   . GLY   A 1 213 ? -1.151  2.618   6.702  1.00 123.66 ? 509 GLY   A O   1 
ATOM   1674 N  N   . TRP   A 1 214 ? -1.989  1.737   8.587  1.00 120.18 ? 510 TRP   A N   1 
ATOM   1675 C  CA  . TRP   A 1 214 ? -2.810  2.914   8.827  1.00 121.52 ? 510 TRP   A CA  1 
ATOM   1676 C  C   . TRP   A 1 214 ? -1.937  4.143   9.022  1.00 124.69 ? 510 TRP   A C   1 
ATOM   1677 O  O   . TRP   A 1 214 ? -0.840  4.075   9.588  1.00 126.97 ? 510 TRP   A O   1 
ATOM   1678 C  CB  . TRP   A 1 214 ? -3.718  2.733   10.043 1.00 118.54 ? 510 TRP   A CB  1 
ATOM   1679 C  CG  . TRP   A 1 214 ? -4.769  3.807   10.116 1.00 116.15 ? 510 TRP   A CG  1 
ATOM   1680 C  CD1 . TRP   A 1 214 ? -5.557  4.236   9.094  1.00 115.37 ? 510 TRP   A CD1 1 
ATOM   1681 C  CD2 . TRP   A 1 214 ? -5.142  4.589   11.264 1.00 116.37 ? 510 TRP   A CD2 1 
ATOM   1682 N  NE1 . TRP   A 1 214 ? -6.398  5.229   9.525  1.00 112.95 ? 510 TRP   A NE1 1 
ATOM   1683 C  CE2 . TRP   A 1 214 ? -6.164  5.468   10.853 1.00 113.89 ? 510 TRP   A CE2 1 
ATOM   1684 C  CE3 . TRP   A 1 214 ? -4.711  4.629   12.596 1.00 115.63 ? 510 TRP   A CE3 1 
ATOM   1685 C  CZ2 . TRP   A 1 214 ? -6.767  6.377   11.721 1.00 111.08 ? 510 TRP   A CZ2 1 
ATOM   1686 C  CZ3 . TRP   A 1 214 ? -5.313  5.537   13.464 1.00 113.49 ? 510 TRP   A CZ3 1 
ATOM   1687 C  CH2 . TRP   A 1 214 ? -6.330  6.397   13.022 1.00 113.23 ? 510 TRP   A CH2 1 
ATOM   1688 N  N   . LYS   A 1 215 ? -2.434  5.268   8.541  1.00 126.50 ? 511 LYS   A N   1 
ATOM   1689 C  CA  . LYS   A 1 215 ? -1.760  6.552   8.656  1.00 127.87 ? 511 LYS   A CA  1 
ATOM   1690 C  C   . LYS   A 1 215 ? -2.519  7.348   9.711  1.00 123.89 ? 511 LYS   A C   1 
ATOM   1691 O  O   . LYS   A 1 215 ? -3.599  7.879   9.445  1.00 124.54 ? 511 LYS   A O   1 
ATOM   1692 C  CB  . LYS   A 1 215 ? -1.723  7.242   7.299  1.00 130.51 ? 511 LYS   A CB  1 
ATOM   1693 C  CG  . LYS   A 1 215 ? -1.369  6.284   6.164  1.00 134.27 ? 511 LYS   A CG  1 
ATOM   1694 C  CD  . LYS   A 1 215 ? 0.126   6.291   5.829  1.00 140.15 ? 511 LYS   A CD  1 
ATOM   1695 C  CE  . LYS   A 1 215 ? 0.944   5.417   6.769  1.00 140.35 ? 511 LYS   A CE  1 
ATOM   1696 N  NZ  . LYS   A 1 215 ? 2.393   5.773   6.729  1.00 148.72 ? 511 LYS   A NZ  1 
ATOM   1697 N  N   . ALA   A 1 216 ? -1.962  7.411   10.905 1.00 126.85 ? 512 ALA   A N   1 
ATOM   1698 C  CA  . ALA   A 1 216 ? -2.688  7.968   12.037 1.00 121.60 ? 512 ALA   A CA  1 
ATOM   1699 C  C   . ALA   A 1 216 ? -2.637  9.493   12.010 1.00 120.23 ? 512 ALA   A C   1 
ATOM   1700 O  O   . ALA   A 1 216 ? -1.553  10.069  11.869 1.00 118.56 ? 512 ALA   A O   1 
ATOM   1701 C  CB  . ALA   A 1 216 ? -2.103  7.447   13.342 1.00 123.18 ? 512 ALA   A CB  1 
ATOM   1702 N  N   . PRO   A 1 217 ? -3.789  10.177  12.133 1.00 117.27 ? 513 PRO   A N   1 
ATOM   1703 C  CA  . PRO   A 1 217 ? -3.807  11.636  12.336 1.00 118.92 ? 513 PRO   A CA  1 
ATOM   1704 C  C   . PRO   A 1 217 ? -3.664  12.022  13.810 1.00 125.55 ? 513 PRO   A C   1 
ATOM   1705 O  O   . PRO   A 1 217 ? -4.375  12.906  14.304 1.00 126.78 ? 513 PRO   A O   1 
ATOM   1706 C  CB  . PRO   A 1 217 ? -5.162  12.038  11.767 1.00 116.02 ? 513 PRO   A CB  1 
ATOM   1707 C  CG  . PRO   A 1 217 ? -6.032  10.847  11.996 1.00 115.29 ? 513 PRO   A CG  1 
ATOM   1708 C  CD  . PRO   A 1 217 ? -5.141  9.632   11.926 1.00 115.95 ? 513 PRO   A CD  1 
ATOM   1709 N  N   . ARG   A 1 218 ? -2.728  11.366  14.510 1.00 133.52 ? 514 ARG   A N   1 
ATOM   1710 C  CA  . ARG   A 1 218 ? -2.525  11.378  15.962 1.00 130.36 ? 514 ARG   A CA  1 
ATOM   1711 C  C   . ARG   A 1 218 ? -3.183  12.520  16.729 1.00 129.67 ? 514 ARG   A C   1 
ATOM   1712 O  O   . ARG   A 1 218 ? -2.500  13.426  17.222 1.00 135.19 ? 514 ARG   A O   1 
ATOM   1713 C  CB  . ARG   A 1 218 ? -1.026  11.382  16.269 1.00 136.46 ? 514 ARG   A CB  1 
ATOM   1714 C  CG  . ARG   A 1 218 ? -0.332  10.111  15.837 1.00 136.39 ? 514 ARG   A CG  1 
ATOM   1715 C  CD  . ARG   A 1 218 ? 1.042   9.948   16.477 1.00 143.28 ? 514 ARG   A CD  1 
ATOM   1716 N  NE  . ARG   A 1 218 ? 1.236   8.587   16.964 1.00 142.26 ? 514 ARG   A NE  1 
ATOM   1717 C  CZ  . ARG   A 1 218 ? 1.366   7.520   16.184 1.00 141.83 ? 514 ARG   A CZ  1 
ATOM   1718 N  NH1 . ARG   A 1 218 ? 1.343   7.620   14.863 1.00 143.75 ? 514 ARG   A NH1 1 
ATOM   1719 N  NH2 . ARG   A 1 218 ? 1.511   6.322   16.743 1.00 142.36 ? 514 ARG   A NH2 1 
ATOM   1720 N  N   . GLY   A 1 219 ? -4.508  12.469  16.850 1.00 124.56 ? 515 GLY   A N   1 
ATOM   1721 C  CA  . GLY   A 1 219 ? -5.231  13.377  17.716 1.00 122.82 ? 515 GLY   A CA  1 
ATOM   1722 C  C   . GLY   A 1 219 ? -6.097  12.625  18.706 1.00 121.43 ? 515 GLY   A C   1 
ATOM   1723 O  O   . GLY   A 1 219 ? -5.837  11.455  19.008 1.00 119.33 ? 515 GLY   A O   1 
ATOM   1724 N  N   . ARG   A 1 220 ? -7.140  13.279  19.210 1.00 120.49 ? 516 ARG   A N   1 
ATOM   1725 C  CA  . ARG   A 1 220 ? -8.079  12.635  20.118 1.00 115.93 ? 516 ARG   A CA  1 
ATOM   1726 C  C   . ARG   A 1 220 ? -9.042  11.726  19.374 1.00 117.04 ? 516 ARG   A C   1 
ATOM   1727 O  O   . ARG   A 1 220 ? -8.838  10.507  19.285 1.00 112.73 ? 516 ARG   A O   1 
ATOM   1728 C  CB  . ARG   A 1 220 ? -8.887  13.683  20.876 1.00 116.91 ? 516 ARG   A CB  1 
ATOM   1729 C  CG  . ARG   A 1 220 ? -9.155  13.328  22.307 1.00 110.87 ? 516 ARG   A CG  1 
ATOM   1730 C  CD  . ARG   A 1 220 ? -8.153  14.024  23.188 1.00 116.10 ? 516 ARG   A CD  1 
ATOM   1731 N  NE  . ARG   A 1 220 ? -8.827  14.894  24.142 1.00 118.47 ? 516 ARG   A NE  1 
ATOM   1732 C  CZ  . ARG   A 1 220 ? -9.168  14.522  25.368 1.00 119.07 ? 516 ARG   A CZ  1 
ATOM   1733 N  NH1 . ARG   A 1 220 ? -8.852  13.326  25.837 1.00 116.72 ? 516 ARG   A NH1 1 
ATOM   1734 N  NH2 . ARG   A 1 220 ? -9.837  15.373  26.143 1.00 118.06 ? 516 ARG   A NH2 1 
ATOM   1735 N  N   . PHE   A 1 221 ? -10.088 12.338  18.817 1.00 111.60 ? 517 PHE   A N   1 
ATOM   1736 C  CA  . PHE   A 1 221 ? -11.260 11.624  18.318 1.00 103.20 ? 517 PHE   A CA  1 
ATOM   1737 C  C   . PHE   A 1 221 ? -11.107 11.308  16.828 1.00 103.56 ? 517 PHE   A C   1 
ATOM   1738 O  O   . PHE   A 1 221 ? -11.928 11.661  15.977 1.00 103.72 ? 517 PHE   A O   1 
ATOM   1739 C  CB  . PHE   A 1 221 ? -12.519 12.432  18.613 1.00 100.41 ? 517 PHE   A CB  1 
ATOM   1740 C  CG  . PHE   A 1 221 ? -12.661 12.830  20.078 1.00 101.71 ? 517 PHE   A CG  1 
ATOM   1741 C  CD1 . PHE   A 1 221 ? -13.045 11.906  21.028 1.00 94.41  ? 517 PHE   A CD1 1 
ATOM   1742 C  CD2 . PHE   A 1 221 ? -12.412 14.129  20.484 1.00 103.89 ? 517 PHE   A CD2 1 
ATOM   1743 C  CE1 . PHE   A 1 221 ? -13.184 12.275  22.351 1.00 97.63  ? 517 PHE   A CE1 1 
ATOM   1744 C  CE2 . PHE   A 1 221 ? -12.543 14.499  21.820 1.00 105.08 ? 517 PHE   A CE2 1 
ATOM   1745 C  CZ  . PHE   A 1 221 ? -12.929 13.568  22.747 1.00 100.49 ? 517 PHE   A CZ  1 
ATOM   1746 N  N   . ASP   A 1 222 ? -10.010 10.617  16.530 1.00 105.27 ? 518 ASP   A N   1 
ATOM   1747 C  CA  . ASP   A 1 222 ? -9.744  10.104  15.192 1.00 101.63 ? 518 ASP   A CA  1 
ATOM   1748 C  C   . ASP   A 1 222 ? -10.495 8.789   15.022 1.00 96.58  ? 518 ASP   A C   1 
ATOM   1749 O  O   . ASP   A 1 222 ? -10.173 7.795   15.683 1.00 92.82  ? 518 ASP   A O   1 
ATOM   1750 C  CB  . ASP   A 1 222 ? -8.244  9.910   14.990 1.00 106.29 ? 518 ASP   A CB  1 
ATOM   1751 C  CG  . ASP   A 1 222 ? -7.438  11.153  15.323 1.00 113.83 ? 518 ASP   A CG  1 
ATOM   1752 O  OD1 . ASP   A 1 222 ? -8.040  12.203  15.643 1.00 114.54 ? 518 ASP   A OD1 1 
ATOM   1753 O  OD2 . ASP   A 1 222 ? -6.191  11.076  15.271 1.00 117.08 ? 518 ASP   A OD2 1 
ATOM   1754 N  N   . VAL   A 1 223 ? -11.505 8.780   14.144 1.00 96.49  ? 519 VAL   A N   1 
ATOM   1755 C  CA  . VAL   A 1 223 ? -12.265 7.558   13.893 1.00 92.22  ? 519 VAL   A CA  1 
ATOM   1756 C  C   . VAL   A 1 223 ? -11.336 6.501   13.317 1.00 89.76  ? 519 VAL   A C   1 
ATOM   1757 O  O   . VAL   A 1 223 ? -10.622 6.748   12.340 1.00 91.05  ? 519 VAL   A O   1 
ATOM   1758 C  CB  . VAL   A 1 223 ? -13.439 7.848   12.947 1.00 89.96  ? 519 VAL   A CB  1 
ATOM   1759 C  CG1 . VAL   A 1 223 ? -14.213 6.577   12.644 1.00 83.32  ? 519 VAL   A CG1 1 
ATOM   1760 C  CG2 . VAL   A 1 223 ? -14.353 8.925   13.542 1.00 91.18  ? 519 VAL   A CG2 1 
ATOM   1761 N  N   . LEU   A 1 224 ? -11.318 5.326   13.932 1.00 87.98  ? 520 LEU   A N   1 
ATOM   1762 C  CA  . LEU   A 1 224 ? -10.430 4.277   13.456 1.00 88.81  ? 520 LEU   A CA  1 
ATOM   1763 C  C   . LEU   A 1 224 ? -10.914 3.706   12.128 1.00 87.38  ? 520 LEU   A C   1 
ATOM   1764 O  O   . LEU   A 1 224 ? -12.112 3.707   11.845 1.00 88.42  ? 520 LEU   A O   1 
ATOM   1765 C  CB  . LEU   A 1 224 ? -10.340 3.149   14.466 1.00 86.88  ? 520 LEU   A CB  1 
ATOM   1766 C  CG  . LEU   A 1 224 ? -9.422  3.379   15.664 1.00 88.36  ? 520 LEU   A CG  1 
ATOM   1767 C  CD1 . LEU   A 1 224 ? -10.066 2.705   16.827 1.00 85.13  ? 520 LEU   A CD1 1 
ATOM   1768 C  CD2 . LEU   A 1 224 ? -8.019  2.824   15.408 1.00 92.57  ? 520 LEU   A CD2 1 
ATOM   1769 N  N   . PRO   A 1 225 ? -10.007 3.182   11.314 1.00 89.98  ? 521 PRO   A N   1 
ATOM   1770 C  CA  . PRO   A 1 225 ? -10.420 2.459   10.112 1.00 87.60  ? 521 PRO   A CA  1 
ATOM   1771 C  C   . PRO   A 1 225 ? -10.904 1.070   10.494 1.00 85.87  ? 521 PRO   A C   1 
ATOM   1772 O  O   . PRO   A 1 225 ? -10.694 0.600   11.609 1.00 82.04  ? 521 PRO   A O   1 
ATOM   1773 C  CB  . PRO   A 1 225 ? -9.136  2.393   9.286  1.00 92.42  ? 521 PRO   A CB  1 
ATOM   1774 C  CG  . PRO   A 1 225 ? -8.059  2.328   10.347 1.00 95.69  ? 521 PRO   A CG  1 
ATOM   1775 C  CD  . PRO   A 1 225 ? -8.541  3.192   11.474 1.00 96.65  ? 521 PRO   A CD  1 
ATOM   1776 N  N   . LEU   A 1 226 ? -11.549 0.413   9.533  1.00 84.02  ? 522 LEU   A N   1 
ATOM   1777 C  CA  . LEU   A 1 226 ? -12.031 -0.946  9.718  1.00 80.81  ? 522 LEU   A CA  1 
ATOM   1778 C  C   . LEU   A 1 226 ? -10.952 -1.948  9.340  1.00 81.72  ? 522 LEU   A C   1 
ATOM   1779 O  O   . LEU   A 1 226 ? -10.272 -1.790  8.322  1.00 83.33  ? 522 LEU   A O   1 
ATOM   1780 C  CB  . LEU   A 1 226 ? -13.272 -1.199  8.867  1.00 81.09  ? 522 LEU   A CB  1 
ATOM   1781 C  CG  . LEU   A 1 226 ? -14.520 -0.380  9.185  1.00 77.42  ? 522 LEU   A CG  1 
ATOM   1782 C  CD1 . LEU   A 1 226 ? -15.582 -0.590  8.096  1.00 73.52  ? 522 LEU   A CD1 1 
ATOM   1783 C  CD2 . LEU   A 1 226 ? -15.061 -0.754  10.562 1.00 74.86  ? 522 LEU   A CD2 1 
ATOM   1784 N  N   . LEU   A 1 227 ? -10.807 -2.989  10.158 1.00 78.43  ? 523 LEU   A N   1 
ATOM   1785 C  CA  . LEU   A 1 227 ? -9.932  -4.117  9.846  1.00 80.86  ? 523 LEU   A CA  1 
ATOM   1786 C  C   . LEU   A 1 227 ? -10.828 -5.330  9.617  1.00 79.55  ? 523 LEU   A C   1 
ATOM   1787 O  O   . LEU   A 1 227 ? -11.305 -5.945  10.573 1.00 76.03  ? 523 LEU   A O   1 
ATOM   1788 C  CB  . LEU   A 1 227 ? -8.925  -4.373  10.959 1.00 80.86  ? 523 LEU   A CB  1 
ATOM   1789 C  CG  . LEU   A 1 227 ? -7.443  -4.350  10.581 1.00 85.70  ? 523 LEU   A CG  1 
ATOM   1790 C  CD1 . LEU   A 1 227 ? -6.633  -5.185  11.566 1.00 88.91  ? 523 LEU   A CD1 1 
ATOM   1791 C  CD2 . LEU   A 1 227 ? -7.191  -4.803  9.144  1.00 88.45  ? 523 LEU   A CD2 1 
ATOM   1792 N  N   . LEU   A 1 228 ? -11.051 -5.676  8.354  1.00 80.47  ? 524 LEU   A N   1 
ATOM   1793 C  CA  . LEU   A 1 228 ? -12.011 -6.709  8.000  1.00 78.02  ? 524 LEU   A CA  1 
ATOM   1794 C  C   . LEU   A 1 228 ? -11.270 -7.925  7.465  1.00 82.63  ? 524 LEU   A C   1 
ATOM   1795 O  O   . LEU   A 1 228 ? -10.448 -7.803  6.548  1.00 84.52  ? 524 LEU   A O   1 
ATOM   1796 C  CB  . LEU   A 1 228 ? -13.010 -6.184  6.972  1.00 77.34  ? 524 LEU   A CB  1 
ATOM   1797 C  CG  . LEU   A 1 228 ? -13.519 -4.802  7.382  1.00 78.66  ? 524 LEU   A CG  1 
ATOM   1798 C  CD1 . LEU   A 1 228 ? -14.473 -4.281  6.358  1.00 74.57  ? 524 LEU   A CD1 1 
ATOM   1799 C  CD2 . LEU   A 1 228 ? -14.179 -4.824  8.769  1.00 75.17  ? 524 LEU   A CD2 1 
ATOM   1800 N  N   . GLN   A 1 229 ? -11.567 -9.086  8.042  1.00 79.08  ? 525 GLN   A N   1 
ATOM   1801 C  CA  . GLN   A 1 229 ? -10.978 -10.366 7.675  1.00 82.72  ? 525 GLN   A CA  1 
ATOM   1802 C  C   . GLN   A 1 229 ? -12.055 -11.215 7.006  1.00 81.13  ? 525 GLN   A C   1 
ATOM   1803 O  O   . GLN   A 1 229 ? -13.085 -11.524 7.618  1.00 78.39  ? 525 GLN   A O   1 
ATOM   1804 C  CB  . GLN   A 1 229 ? -10.414 -11.066 8.913  1.00 84.40  ? 525 GLN   A CB  1 
ATOM   1805 C  CG  . GLN   A 1 229 ? -10.113 -12.549 8.751  1.00 87.52  ? 525 GLN   A CG  1 
ATOM   1806 C  CD  . GLN   A 1 229 ? -9.878  -13.264 10.084 1.00 88.86  ? 525 GLN   A CD  1 
ATOM   1807 O  OE1 . GLN   A 1 229 ? -9.710  -12.627 11.132 1.00 86.70  ? 525 GLN   A OE1 1 
ATOM   1808 N  NE2 . GLN   A 1 229 ? -9.874  -14.592 10.047 1.00 90.87  ? 525 GLN   A NE2 1 
ATOM   1809 N  N   . ALA   A 1 230 ? -11.827 -11.578 5.749  1.00 82.99  ? 526 ALA   A N   1 
ATOM   1810 C  CA  . ALA   A 1 230 ? -12.787 -12.340 4.964  1.00 80.68  ? 526 ALA   A CA  1 
ATOM   1811 C  C   . ALA   A 1 230 ? -12.273 -13.758 4.773  1.00 83.04  ? 526 ALA   A C   1 
ATOM   1812 O  O   . ALA   A 1 230 ? -11.105 -13.951 4.422  1.00 85.06  ? 526 ALA   A O   1 
ATOM   1813 C  CB  . ALA   A 1 230 ? -13.030 -11.678 3.607  1.00 75.54  ? 526 ALA   A CB  1 
ATOM   1814 N  N   . ASN   A 1 231 ? -13.140 -14.740 5.032  1.00 82.32  ? 527 ASN   A N   1 
ATOM   1815 C  CA  . ASN   A 1 231 ? -12.865 -16.148 4.751  1.00 87.20  ? 527 ASN   A CA  1 
ATOM   1816 C  C   . ASN   A 1 231 ? -11.504 -16.579 5.293  1.00 94.51  ? 527 ASN   A C   1 
ATOM   1817 O  O   . ASN   A 1 231 ? -10.786 -17.369 4.678  1.00 95.28  ? 527 ASN   A O   1 
ATOM   1818 C  CB  . ASN   A 1 231 ? -12.964 -16.426 3.253  1.00 87.30  ? 527 ASN   A CB  1 
ATOM   1819 C  CG  . ASN   A 1 231 ? -13.259 -17.876 2.956  1.00 91.92  ? 527 ASN   A CG  1 
ATOM   1820 O  OD1 . ASN   A 1 231 ? -13.901 -18.559 3.754  1.00 95.74  ? 527 ASN   A OD1 1 
ATOM   1821 N  ND2 . ASN   A 1 231 ? -12.797 -18.356 1.809  1.00 91.41  ? 527 ASN   A ND2 1 
ATOM   1822 N  N   . GLY   A 1 232 ? -11.142 -16.052 6.458  1.00 95.75  ? 528 GLY   A N   1 
ATOM   1823 C  CA  . GLY   A 1 232 ? -9.884  -16.387 7.089  1.00 99.15  ? 528 GLY   A CA  1 
ATOM   1824 C  C   . GLY   A 1 232 ? -8.662  -15.696 6.520  1.00 99.06  ? 528 GLY   A C   1 
ATOM   1825 O  O   . GLY   A 1 232 ? -7.562  -15.897 7.047  1.00 104.84 ? 528 GLY   A O   1 
ATOM   1826 N  N   . ASN   A 1 233 ? -8.806  -14.881 5.482  1.00 93.90  ? 529 ASN   A N   1 
ATOM   1827 C  CA  . ASN   A 1 233 ? -7.649  -14.217 4.898  1.00 97.36  ? 529 ASN   A CA  1 
ATOM   1828 C  C   . ASN   A 1 233 ? -7.212  -13.029 5.746  1.00 98.25  ? 529 ASN   A C   1 
ATOM   1829 O  O   . ASN   A 1 233 ? -8.017  -12.414 6.447  1.00 97.14  ? 529 ASN   A O   1 
ATOM   1830 C  CB  . ASN   A 1 233 ? -7.958  -13.759 3.471  1.00 90.13  ? 529 ASN   A CB  1 
ATOM   1831 C  CG  . ASN   A 1 233 ? -8.135  -14.915 2.526  1.00 92.10  ? 529 ASN   A CG  1 
ATOM   1832 O  OD1 . ASN   A 1 233 ? -7.184  -15.342 1.878  1.00 98.34  ? 529 ASN   A OD1 1 
ATOM   1833 N  ND2 . ASN   A 1 233 ? -9.353  -15.431 2.436  1.00 89.88  ? 529 ASN   A ND2 1 
ATOM   1834 N  N   . ASP   A 1 234 ? -5.919  -12.715 5.670  1.00 96.52  ? 530 ASP   A N   1 
ATOM   1835 C  CA  . ASP   A 1 234 ? -5.348  -11.614 6.434  1.00 103.03 ? 530 ASP   A CA  1 
ATOM   1836 C  C   . ASP   A 1 234 ? -6.194  -10.348 6.258  1.00 99.42  ? 530 ASP   A C   1 
ATOM   1837 O  O   . ASP   A 1 234 ? -6.532  -9.989  5.122  1.00 99.64  ? 530 ASP   A O   1 
ATOM   1838 C  CB  . ASP   A 1 234 ? -3.904  -11.359 5.985  1.00 109.47 ? 530 ASP   A CB  1 
ATOM   1839 C  CG  . ASP   A 1 234 ? -3.034  -12.619 6.025  1.00 117.18 ? 530 ASP   A CG  1 
ATOM   1840 O  OD1 . ASP   A 1 234 ? -3.368  -13.580 6.755  1.00 117.23 ? 530 ASP   A OD1 1 
ATOM   1841 O  OD2 . ASP   A 1 234 ? -1.999  -12.638 5.320  1.00 119.72 ? 530 ASP   A OD2 1 
ATOM   1842 N  N   . PRO   A 1 235 ? -6.555  -9.656  7.338  1.00 96.09  ? 531 PRO   A N   1 
ATOM   1843 C  CA  . PRO   A 1 235 ? -7.538  -8.572  7.223  1.00 91.19  ? 531 PRO   A CA  1 
ATOM   1844 C  C   . PRO   A 1 235 ? -6.964  -7.335  6.544  1.00 92.08  ? 531 PRO   A C   1 
ATOM   1845 O  O   . PRO   A 1 235 ? -5.751  -7.172  6.399  1.00 96.94  ? 531 PRO   A O   1 
ATOM   1846 C  CB  . PRO   A 1 235 ? -7.912  -8.288  8.679  1.00 88.67  ? 531 PRO   A CB  1 
ATOM   1847 C  CG  . PRO   A 1 235 ? -6.683  -8.623  9.423  1.00 92.71  ? 531 PRO   A CG  1 
ATOM   1848 C  CD  . PRO   A 1 235 ? -6.100  -9.829  8.726  1.00 98.42  ? 531 PRO   A CD  1 
ATOM   1849 N  N   . GLU   A 1 236 ? -7.870  -6.450  6.118  1.00 89.82  ? 532 GLU   A N   1 
ATOM   1850 C  CA  . GLU   A 1 236 ? -7.528  -5.330  5.245  1.00 88.89  ? 532 GLU   A CA  1 
ATOM   1851 C  C   . GLU   A 1 236 ? -8.182  -4.044  5.736  1.00 87.81  ? 532 GLU   A C   1 
ATOM   1852 O  O   . GLU   A 1 236 ? -9.302  -4.054  6.249  1.00 86.89  ? 532 GLU   A O   1 
ATOM   1853 C  CB  . GLU   A 1 236 ? -7.967  -5.609  3.792  1.00 89.86  ? 532 GLU   A CB  1 
ATOM   1854 C  CG  . GLU   A 1 236 ? -7.451  -6.924  3.233  1.00 90.33  ? 532 GLU   A CG  1 
ATOM   1855 C  CD  . GLU   A 1 236 ? -8.279  -7.424  2.062  1.00 93.77  ? 532 GLU   A CD  1 
ATOM   1856 O  OE1 . GLU   A 1 236 ? -8.649  -6.599  1.196  1.00 90.77  ? 532 GLU   A OE1 1 
ATOM   1857 O  OE2 . GLU   A 1 236 ? -8.568  -8.642  2.017  1.00 96.29  ? 532 GLU   A OE2 1 
ATOM   1858 N  N   . LEU   A 1 237 ? -7.480  -2.929  5.556  1.00 88.04  ? 533 LEU   A N   1 
ATOM   1859 C  CA  . LEU   A 1 237 ? -7.903  -1.650  6.114  1.00 87.70  ? 533 LEU   A CA  1 
ATOM   1860 C  C   . LEU   A 1 237 ? -8.861  -0.915  5.186  1.00 86.31  ? 533 LEU   A C   1 
ATOM   1861 O  O   . LEU   A 1 237 ? -8.637  -0.847  3.978  1.00 90.69  ? 533 LEU   A O   1 
ATOM   1862 C  CB  . LEU   A 1 237 ? -6.685  -0.770  6.392  1.00 89.62  ? 533 LEU   A CB  1 
ATOM   1863 C  CG  . LEU   A 1 237 ? -5.873  -1.219  7.606  1.00 93.68  ? 533 LEU   A CG  1 
ATOM   1864 C  CD1 . LEU   A 1 237 ? -4.579  -0.427  7.731  1.00 104.98 ? 533 LEU   A CD1 1 
ATOM   1865 C  CD2 . LEU   A 1 237 ? -6.733  -1.068  8.842  1.00 90.19  ? 533 LEU   A CD2 1 
ATOM   1866 N  N   . PHE   A 1 238 ? -9.920  -0.345  5.763  1.00 85.36  ? 534 PHE   A N   1 
ATOM   1867 C  CA  . PHE   A 1 238 ? -10.877 0.462   5.014  1.00 87.38  ? 534 PHE   A CA  1 
ATOM   1868 C  C   . PHE   A 1 238 ? -11.355 1.626   5.871  1.00 87.38  ? 534 PHE   A C   1 
ATOM   1869 O  O   . PHE   A 1 238 ? -11.740 1.429   7.029  1.00 85.61  ? 534 PHE   A O   1 
ATOM   1870 C  CB  . PHE   A 1 238 ? -12.089 -0.358  4.562  1.00 82.91  ? 534 PHE   A CB  1 
ATOM   1871 C  CG  . PHE   A 1 238 ? -11.741 -1.637  3.868  1.00 84.55  ? 534 PHE   A CG  1 
ATOM   1872 C  CD1 . PHE   A 1 238 ? -11.578 -2.805  4.596  1.00 83.11  ? 534 PHE   A CD1 1 
ATOM   1873 C  CD2 . PHE   A 1 238 ? -11.600 -1.678  2.485  1.00 84.25  ? 534 PHE   A CD2 1 
ATOM   1874 C  CE1 . PHE   A 1 238 ? -11.261 -3.991  3.960  1.00 83.08  ? 534 PHE   A CE1 1 
ATOM   1875 C  CE2 . PHE   A 1 238 ? -11.285 -2.861  1.843  1.00 84.00  ? 534 PHE   A CE2 1 
ATOM   1876 C  CZ  . PHE   A 1 238 ? -11.119 -4.021  2.580  1.00 82.74  ? 534 PHE   A CZ  1 
ATOM   1877 N  N   . GLN   A 1 239 ? -11.369 2.823   5.282  1.00 94.38  ? 535 GLN   A N   1 
ATOM   1878 C  CA  . GLN   A 1 239 ? -11.848 4.030   5.946  1.00 94.29  ? 535 GLN   A CA  1 
ATOM   1879 C  C   . GLN   A 1 239 ? -13.335 4.220   5.670  1.00 92.35  ? 535 GLN   A C   1 
ATOM   1880 O  O   . GLN   A 1 239 ? -13.743 4.413   4.517  1.00 93.13  ? 535 GLN   A O   1 
ATOM   1881 C  CB  . GLN   A 1 239 ? -11.083 5.260   5.466  1.00 98.47  ? 535 GLN   A CB  1 
ATOM   1882 C  CG  . GLN   A 1 239 ? -11.735 6.559   5.902  1.00 101.15 ? 535 GLN   A CG  1 
ATOM   1883 C  CD  . GLN   A 1 239 ? -11.343 7.735   5.038  1.00 109.50 ? 535 GLN   A CD  1 
ATOM   1884 O  OE1 . GLN   A 1 239 ? -12.165 8.607   4.745  1.00 112.28 ? 535 GLN   A OE1 1 
ATOM   1885 N  NE2 . GLN   A 1 239 ? -10.085 7.765   4.615  1.00 118.38 ? 535 GLN   A NE2 1 
ATOM   1886 N  N   . ILE   A 1 240 ? -14.129 4.185   6.730  1.00 89.64  ? 536 ILE   A N   1 
ATOM   1887 C  CA  . ILE   A 1 240 ? -15.560 4.502   6.682  1.00 85.46  ? 536 ILE   A CA  1 
ATOM   1888 C  C   . ILE   A 1 240 ? -15.724 5.918   6.160  1.00 89.07  ? 536 ILE   A C   1 
ATOM   1889 O  O   . ILE   A 1 240 ? -15.126 6.851   6.729  1.00 88.16  ? 536 ILE   A O   1 
ATOM   1890 C  CB  . ILE   A 1 240 ? -16.185 4.362   8.092  1.00 84.58  ? 536 ILE   A CB  1 
ATOM   1891 C  CG1 . ILE   A 1 240 ? -15.821 3.013   8.711  1.00 84.30  ? 536 ILE   A CG1 1 
ATOM   1892 C  CG2 . ILE   A 1 240 ? -17.697 4.547   8.055  1.00 79.37  ? 536 ILE   A CG2 1 
ATOM   1893 C  CD1 . ILE   A 1 240 ? -15.213 3.100   10.131 1.00 79.34  ? 536 ILE   A CD1 1 
ATOM   1894 N  N   . PRO   A 1 241 ? -16.467 6.142   5.076  1.00 85.85  ? 537 PRO   A N   1 
ATOM   1895 C  CA  . PRO   A 1 241 ? -16.627 7.511   4.564  1.00 85.35  ? 537 PRO   A CA  1 
ATOM   1896 C  C   . PRO   A 1 241 ? -17.040 8.439   5.689  1.00 84.10  ? 537 PRO   A C   1 
ATOM   1897 O  O   . PRO   A 1 241 ? -18.034 8.175   6.383  1.00 79.74  ? 537 PRO   A O   1 
ATOM   1898 C  CB  . PRO   A 1 241 ? -17.735 7.380   3.507  1.00 84.14  ? 537 PRO   A CB  1 
ATOM   1899 C  CG  . PRO   A 1 241 ? -17.701 5.942   3.113  1.00 83.26  ? 537 PRO   A CG  1 
ATOM   1900 C  CD  . PRO   A 1 241 ? -17.308 5.184   4.337  1.00 79.89  ? 537 PRO   A CD  1 
ATOM   1901 N  N   . PRO   A 1 242 ? -16.267 9.492   5.942  1.00 85.11  ? 538 PRO   A N   1 
ATOM   1902 C  CA  . PRO   A 1 242 ? -16.558 10.344  7.104  1.00 84.66  ? 538 PRO   A CA  1 
ATOM   1903 C  C   . PRO   A 1 242 ? -17.987 10.868  7.121  1.00 83.62  ? 538 PRO   A C   1 
ATOM   1904 O  O   . PRO   A 1 242 ? -18.582 10.946  8.204  1.00 84.32  ? 538 PRO   A O   1 
ATOM   1905 C  CB  . PRO   A 1 242 ? -15.522 11.467  6.971  1.00 85.64  ? 538 PRO   A CB  1 
ATOM   1906 C  CG  . PRO   A 1 242 ? -14.398 10.832  6.224  1.00 90.39  ? 538 PRO   A CG  1 
ATOM   1907 C  CD  . PRO   A 1 242 ? -15.056 9.923   5.228  1.00 88.23  ? 538 PRO   A CD  1 
ATOM   1908 N  N   . GLU   A 1 243 ? -18.586 11.148  5.955  1.00 82.50  ? 539 GLU   A N   1 
ATOM   1909 C  CA  . GLU   A 1 243 ? -19.970 11.613  5.921  1.00 78.60  ? 539 GLU   A CA  1 
ATOM   1910 C  C   . GLU   A 1 243 ? -20.940 10.578  6.480  1.00 80.51  ? 539 GLU   A C   1 
ATOM   1911 O  O   . GLU   A 1 243 ? -22.081 10.931  6.815  1.00 77.85  ? 539 GLU   A O   1 
ATOM   1912 C  CB  . GLU   A 1 243 ? -20.360 12.023  4.488  1.00 85.56  ? 539 GLU   A CB  1 
ATOM   1913 C  CG  . GLU   A 1 243 ? -20.355 10.910  3.402  1.00 80.50  ? 539 GLU   A CG  1 
ATOM   1914 C  CD  . GLU   A 1 243 ? -18.993 10.675  2.735  1.00 81.39  ? 539 GLU   A CD  1 
ATOM   1915 O  OE1 . GLU   A 1 243 ? -17.960 10.809  3.423  1.00 86.46  ? 539 GLU   A OE1 1 
ATOM   1916 O  OE2 . GLU   A 1 243 ? -18.952 10.332  1.529  1.00 81.63  ? 539 GLU   A OE2 1 
ATOM   1917 N  N   . LEU   A 1 244 ? -20.503 9.318   6.614  1.00 80.17  ? 540 LEU   A N   1 
ATOM   1918 C  CA  . LEU   A 1 244 ? -21.300 8.262   7.221  1.00 78.49  ? 540 LEU   A CA  1 
ATOM   1919 C  C   . LEU   A 1 244 ? -21.119 8.150   8.730  1.00 76.51  ? 540 LEU   A C   1 
ATOM   1920 O  O   . LEU   A 1 244 ? -21.929 7.482   9.382  1.00 68.39  ? 540 LEU   A O   1 
ATOM   1921 C  CB  . LEU   A 1 244 ? -20.957 6.902   6.609  1.00 78.30  ? 540 LEU   A CB  1 
ATOM   1922 C  CG  . LEU   A 1 244 ? -21.304 6.642   5.142  1.00 77.85  ? 540 LEU   A CG  1 
ATOM   1923 C  CD1 . LEU   A 1 244 ? -21.341 5.147   4.926  1.00 72.71  ? 540 LEU   A CD1 1 
ATOM   1924 C  CD2 . LEU   A 1 244 ? -22.629 7.273   4.765  1.00 75.79  ? 540 LEU   A CD2 1 
ATOM   1925 N  N   . VAL   A 1 245 ? -20.090 8.762   9.306  1.00 77.25  ? 541 VAL   A N   1 
ATOM   1926 C  CA  . VAL   A 1 245 ? -19.852 8.681   10.749 1.00 78.18  ? 541 VAL   A CA  1 
ATOM   1927 C  C   . VAL   A 1 245 ? -20.440 9.926   11.398 1.00 77.67  ? 541 VAL   A C   1 
ATOM   1928 O  O   . VAL   A 1 245 ? -19.848 11.003  11.341 1.00 79.56  ? 541 VAL   A O   1 
ATOM   1929 C  CB  . VAL   A 1 245 ? -18.366 8.522   11.078 1.00 77.59  ? 541 VAL   A CB  1 
ATOM   1930 C  CG1 . VAL   A 1 245 ? -18.145 8.568   12.620 1.00 80.66  ? 541 VAL   A CG1 1 
ATOM   1931 C  CG2 . VAL   A 1 245 ? -17.863 7.205   10.514 1.00 75.70  ? 541 VAL   A CG2 1 
ATOM   1932 N  N   . LEU   A 1 246 ? -21.576 9.766   12.081 1.00 78.88  ? 542 LEU   A N   1 
ATOM   1933 C  CA  . LEU   A 1 246 ? -22.269 10.897  12.694 1.00 77.91  ? 542 LEU   A CA  1 
ATOM   1934 C  C   . LEU   A 1 246 ? -21.719 11.152  14.090 1.00 80.16  ? 542 LEU   A C   1 
ATOM   1935 O  O   . LEU   A 1 246 ? -21.760 10.268  14.948 1.00 77.20  ? 542 LEU   A O   1 
ATOM   1936 C  CB  . LEU   A 1 246 ? -23.771 10.627  12.753 1.00 79.27  ? 542 LEU   A CB  1 
ATOM   1937 C  CG  . LEU   A 1 246 ? -24.696 11.623  13.444 1.00 83.01  ? 542 LEU   A CG  1 
ATOM   1938 C  CD1 . LEU   A 1 246 ? -24.787 12.879  12.625 1.00 85.67  ? 542 LEU   A CD1 1 
ATOM   1939 C  CD2 . LEU   A 1 246 ? -26.072 10.995  13.664 1.00 82.54  ? 542 LEU   A CD2 1 
ATOM   1940 N  N   . GLU   A 1 247 ? -21.231 12.362  14.323 1.00 79.23  ? 543 GLU   A N   1 
ATOM   1941 C  CA  . GLU   A 1 247 ? -20.628 12.722  15.594 1.00 83.82  ? 543 GLU   A CA  1 
ATOM   1942 C  C   . GLU   A 1 247 ? -21.380 13.884  16.228 1.00 84.63  ? 543 GLU   A C   1 
ATOM   1943 O  O   . GLU   A 1 247 ? -21.875 14.784  15.531 1.00 86.69  ? 543 GLU   A O   1 
ATOM   1944 C  CB  . GLU   A 1 247 ? -19.144 13.062  15.407 1.00 85.84  ? 543 GLU   A CB  1 
ATOM   1945 C  CG  . GLU   A 1 247 ? -18.276 11.817  15.204 1.00 85.65  ? 543 GLU   A CG  1 
ATOM   1946 C  CD  . GLU   A 1 247 ? -16.861 12.176  14.810 1.00 93.27  ? 543 GLU   A CD  1 
ATOM   1947 O  OE1 . GLU   A 1 247 ? -16.679 12.750  13.723 1.00 92.44  ? 543 GLU   A OE1 1 
ATOM   1948 O  OE2 . GLU   A 1 247 ? -15.931 11.905  15.604 1.00 92.48  ? 543 GLU   A OE2 1 
ATOM   1949 N  N   . VAL   A 1 248 ? -21.445 13.854  17.554 1.00 86.15  ? 544 VAL   A N   1 
ATOM   1950 C  CA  . VAL   A 1 248 ? -22.149 14.838  18.373 1.00 91.05  ? 544 VAL   A CA  1 
ATOM   1951 C  C   . VAL   A 1 248 ? -21.111 15.635  19.154 1.00 93.63  ? 544 VAL   A C   1 
ATOM   1952 O  O   . VAL   A 1 248 ? -20.369 15.051  19.954 1.00 87.54  ? 544 VAL   A O   1 
ATOM   1953 C  CB  . VAL   A 1 248 ? -23.148 14.180  19.342 1.00 86.44  ? 544 VAL   A CB  1 
ATOM   1954 C  CG1 . VAL   A 1 248 ? -23.948 15.267  20.049 1.00 90.91  ? 544 VAL   A CG1 1 
ATOM   1955 C  CG2 . VAL   A 1 248 ? -24.059 13.179  18.651 1.00 81.83  ? 544 VAL   A CG2 1 
ATOM   1956 N  N   . PRO   A 1 249 ? -20.997 16.946  18.944 1.00 94.68  ? 545 PRO   A N   1 
ATOM   1957 C  CA  . PRO   A 1 249 ? -20.183 17.773  19.842 1.00 98.38  ? 545 PRO   A CA  1 
ATOM   1958 C  C   . PRO   A 1 249 ? -20.920 18.004  21.152 1.00 99.29  ? 545 PRO   A C   1 
ATOM   1959 O  O   . PRO   A 1 249 ? -22.115 18.314  21.161 1.00 100.27 ? 545 PRO   A O   1 
ATOM   1960 C  CB  . PRO   A 1 249 ? -20.002 19.078  19.053 1.00 99.68  ? 545 PRO   A CB  1 
ATOM   1961 C  CG  . PRO   A 1 249 ? -21.177 19.126  18.142 1.00 100.54 ? 545 PRO   A CG  1 
ATOM   1962 C  CD  . PRO   A 1 249 ? -21.541 17.718  17.811 1.00 94.39  ? 545 PRO   A CD  1 
ATOM   1963 N  N   . ILE   A 1 250 ? -20.196 17.853  22.266 1.00 103.97 ? 546 ILE   A N   1 
ATOM   1964 C  CA  . ILE   A 1 250 ? -20.790 17.795  23.599 1.00 100.11 ? 546 ILE   A CA  1 
ATOM   1965 C  C   . ILE   A 1 250 ? -20.733 19.175  24.241 1.00 105.11 ? 546 ILE   A C   1 
ATOM   1966 O  O   . ILE   A 1 250 ? -19.661 19.654  24.632 1.00 107.61 ? 546 ILE   A O   1 
ATOM   1967 C  CB  . ILE   A 1 250 ? -20.083 16.765  24.488 1.00 104.27 ? 546 ILE   A CB  1 
ATOM   1968 C  CG1 . ILE   A 1 250 ? -19.977 15.420  23.768 1.00 100.33 ? 546 ILE   A CG1 1 
ATOM   1969 C  CG2 . ILE   A 1 250 ? -20.795 16.654  25.843 1.00 98.05  ? 546 ILE   A CG2 1 
ATOM   1970 C  CD1 . ILE   A 1 250 ? -21.303 14.853  23.324 1.00 95.99  ? 546 ILE   A CD1 1 
ATOM   1971 N  N   . ARG   A 1 251 ? -21.895 19.797  24.396 1.00 106.00 ? 547 ARG   A N   1 
ATOM   1972 C  CA  . ARG   A 1 251 ? -22.018 21.063  25.089 1.00 108.41 ? 547 ARG   A CA  1 
ATOM   1973 C  C   . ARG   A 1 251 ? -22.928 20.883  26.295 1.00 109.76 ? 547 ARG   A C   1 
ATOM   1974 O  O   . ARG   A 1 251 ? -23.746 19.959  26.352 1.00 106.92 ? 547 ARG   A O   1 
ATOM   1975 C  CB  . ARG   A 1 251 ? -22.568 22.168  24.168 1.00 111.92 ? 547 ARG   A CB  1 
ATOM   1976 C  CG  . ARG   A 1 251 ? -23.968 21.910  23.619 1.00 110.07 ? 547 ARG   A CG  1 
ATOM   1977 C  CD  . ARG   A 1 251 ? -23.917 21.165  22.267 1.00 108.80 ? 547 ARG   A CD  1 
ATOM   1978 N  NE  . ARG   A 1 251 ? -25.172 21.210  21.525 1.00 106.57 ? 547 ARG   A NE  1 
ATOM   1979 C  CZ  . ARG   A 1 251 ? -25.461 20.406  20.512 1.00 104.24 ? 547 ARG   A CZ  1 
ATOM   1980 N  NH1 . ARG   A 1 251 ? -24.667 19.395  20.188 1.00 101.21 ? 547 ARG   A NH1 1 
ATOM   1981 N  NH2 . ARG   A 1 251 ? -26.549 20.650  19.777 1.00 108.14 ? 547 ARG   A NH2 1 
ATOM   1982 N  N   . HIS   A 1 252 ? -22.771 21.749  27.234 1.00 109.70 ? 548 HIS   A N   1 
ATOM   1983 C  CA  . HIS   A 1 252 ? -23.663 21.740  28.372 1.00 117.62 ? 548 HIS   A CA  1 
ATOM   1984 C  C   . HIS   A 1 252 ? -24.720 22.829  28.226 1.00 121.00 ? 548 HIS   A C   1 
ATOM   1985 O  O   . HIS   A 1 252 ? -24.478 23.859  27.583 1.00 123.64 ? 548 HIS   A O   1 
ATOM   1986 C  CB  . HIS   A 1 252 ? -22.885 21.949  29.671 1.00 113.69 ? 548 HIS   A CB  1 
ATOM   1987 C  CG  . HIS   A 1 252 ? -23.655 21.575  30.895 1.00 118.48 ? 548 HIS   A CG  1 
ATOM   1988 N  ND1 . HIS   A 1 252 ? -24.404 22.484  31.610 1.00 120.58 ? 548 HIS   A ND1 1 
ATOM   1989 C  CD2 . HIS   A 1 252 ? -23.816 20.381  31.517 1.00 113.84 ? 548 HIS   A CD2 1 
ATOM   1990 C  CE1 . HIS   A 1 252 ? -24.982 21.868  32.626 1.00 119.34 ? 548 HIS   A CE1 1 
ATOM   1991 N  NE2 . HIS   A 1 252 ? -24.644 20.593  32.589 1.00 110.48 ? 548 HIS   A NE2 1 
ATOM   1992 N  N   . PRO   A 1 253 ? -25.917 22.608  28.773 1.00 119.89 ? 549 PRO   A N   1 
ATOM   1993 C  CA  . PRO   A 1 253 ? -26.958 23.638  28.729 1.00 120.54 ? 549 PRO   A CA  1 
ATOM   1994 C  C   . PRO   A 1 253 ? -26.797 24.734  29.766 1.00 128.77 ? 549 PRO   A C   1 
ATOM   1995 O  O   . PRO   A 1 253 ? -27.704 25.559  29.905 1.00 135.67 ? 549 PRO   A O   1 
ATOM   1996 C  CB  . PRO   A 1 253 ? -28.245 22.834  28.980 1.00 118.45 ? 549 PRO   A CB  1 
ATOM   1997 C  CG  . PRO   A 1 253 ? -27.807 21.659  29.761 1.00 116.10 ? 549 PRO   A CG  1 
ATOM   1998 C  CD  . PRO   A 1 253 ? -26.427 21.323  29.291 1.00 114.35 ? 549 PRO   A CD  1 
ATOM   1999 N  N   . LYS   A 1 254 ? -25.677 24.748  30.489 1.00 126.37 ? 550 LYS   A N   1 
ATOM   2000 C  CA  . LYS   A 1 254 ? -25.377 25.806  31.438 1.00 132.25 ? 550 LYS   A CA  1 
ATOM   2001 C  C   . LYS   A 1 254 ? -23.964 26.343  31.246 1.00 135.49 ? 550 LYS   A C   1 
ATOM   2002 O  O   . LYS   A 1 254 ? -23.771 27.556  31.133 1.00 142.92 ? 550 LYS   A O   1 
ATOM   2003 C  CB  . LYS   A 1 254 ? -25.545 25.301  32.870 1.00 131.26 ? 550 LYS   A CB  1 
ATOM   2004 C  CG  . LYS   A 1 254 ? -26.944 24.818  33.211 1.00 134.61 ? 550 LYS   A CG  1 
ATOM   2005 C  CD  . LYS   A 1 254 ? -27.770 25.920  33.858 1.00 145.06 ? 550 LYS   A CD  1 
ATOM   2006 C  CE  . LYS   A 1 254 ? -29.171 25.422  34.203 1.00 145.37 ? 550 LYS   A CE  1 
ATOM   2007 N  NZ  . LYS   A 1 254 ? -30.040 25.300  32.982 1.00 140.19 ? 550 LYS   A NZ  1 
ATOM   2008 N  N   . PHE   A 1 255 ? -22.968 25.462  31.226 1.00 130.63 ? 551 PHE   A N   1 
ATOM   2009 C  CA  . PHE   A 1 255 ? -21.572 25.879  31.310 1.00 135.98 ? 551 PHE   A CA  1 
ATOM   2010 C  C   . PHE   A 1 255 ? -21.033 26.078  29.904 1.00 141.68 ? 551 PHE   A C   1 
ATOM   2011 O  O   . PHE   A 1 255 ? -20.792 25.105  29.183 1.00 139.76 ? 551 PHE   A O   1 
ATOM   2012 C  CB  . PHE   A 1 255 ? -20.738 24.852  32.073 1.00 134.42 ? 551 PHE   A CB  1 
ATOM   2013 C  CG  . PHE   A 1 255 ? -21.280 24.513  33.443 1.00 132.54 ? 551 PHE   A CG  1 
ATOM   2014 C  CD1 . PHE   A 1 255 ? -20.984 25.300  34.539 1.00 132.03 ? 551 PHE   A CD1 1 
ATOM   2015 C  CD2 . PHE   A 1 255 ? -22.067 23.388  33.627 1.00 130.41 ? 551 PHE   A CD2 1 
ATOM   2016 C  CE1 . PHE   A 1 255 ? -21.482 24.984  35.788 1.00 135.79 ? 551 PHE   A CE1 1 
ATOM   2017 C  CE2 . PHE   A 1 255 ? -22.563 23.064  34.862 1.00 124.46 ? 551 PHE   A CE2 1 
ATOM   2018 C  CZ  . PHE   A 1 255 ? -22.272 23.861  35.950 1.00 130.97 ? 551 PHE   A CZ  1 
ATOM   2019 N  N   . ASP   A 1 256 ? -20.844 27.336  29.506 1.00 145.14 ? 552 ASP   A N   1 
ATOM   2020 C  CA  . ASP   A 1 256 ? -20.330 27.597  28.169 1.00 152.86 ? 552 ASP   A CA  1 
ATOM   2021 C  C   . ASP   A 1 256 ? -18.843 27.298  28.033 1.00 148.32 ? 552 ASP   A C   1 
ATOM   2022 O  O   . ASP   A 1 256 ? -18.356 27.195  26.902 1.00 152.17 ? 552 ASP   A O   1 
ATOM   2023 C  CB  . ASP   A 1 256 ? -20.616 29.049  27.761 1.00 164.28 ? 552 ASP   A CB  1 
ATOM   2024 C  CG  . ASP   A 1 256 ? -21.985 29.215  27.114 1.00 169.98 ? 552 ASP   A CG  1 
ATOM   2025 O  OD1 . ASP   A 1 256 ? -22.997 29.167  27.851 1.00 169.53 ? 552 ASP   A OD1 1 
ATOM   2026 O  OD2 . ASP   A 1 256 ? -22.046 29.381  25.870 1.00 171.30 ? 552 ASP   A OD2 1 
ATOM   2027 N  N   . TRP   A 1 257 ? -18.105 27.159  29.139 1.00 144.30 ? 553 TRP   A N   1 
ATOM   2028 C  CA  . TRP   A 1 257 ? -16.755 26.628  29.001 1.00 142.97 ? 553 TRP   A CA  1 
ATOM   2029 C  C   . TRP   A 1 257 ? -16.754 25.156  28.626 1.00 137.07 ? 553 TRP   A C   1 
ATOM   2030 O  O   . TRP   A 1 257 ? -15.693 24.626  28.281 1.00 134.68 ? 553 TRP   A O   1 
ATOM   2031 C  CB  . TRP   A 1 257 ? -15.963 26.811  30.287 1.00 145.55 ? 553 TRP   A CB  1 
ATOM   2032 C  CG  . TRP   A 1 257 ? -16.686 26.289  31.475 1.00 141.56 ? 553 TRP   A CG  1 
ATOM   2033 C  CD1 . TRP   A 1 257 ? -17.479 27.003  32.319 1.00 144.93 ? 553 TRP   A CD1 1 
ATOM   2034 C  CD2 . TRP   A 1 257 ? -16.712 24.936  31.945 1.00 133.80 ? 553 TRP   A CD2 1 
ATOM   2035 N  NE1 . TRP   A 1 257 ? -17.990 26.185  33.291 1.00 139.70 ? 553 TRP   A NE1 1 
ATOM   2036 C  CE2 . TRP   A 1 257 ? -17.531 24.911  33.090 1.00 137.14 ? 553 TRP   A CE2 1 
ATOM   2037 C  CE3 . TRP   A 1 257 ? -16.115 23.747  31.518 1.00 133.20 ? 553 TRP   A CE3 1 
ATOM   2038 C  CZ2 . TRP   A 1 257 ? -17.774 23.743  33.813 1.00 129.85 ? 553 TRP   A CZ2 1 
ATOM   2039 C  CZ3 . TRP   A 1 257 ? -16.357 22.586  32.236 1.00 130.13 ? 553 TRP   A CZ3 1 
ATOM   2040 C  CH2 . TRP   A 1 257 ? -17.179 22.594  33.370 1.00 128.82 ? 553 TRP   A CH2 1 
ATOM   2041 N  N   . PHE   A 1 258 ? -17.910 24.491  28.702 1.00 131.63 ? 554 PHE   A N   1 
ATOM   2042 C  CA  . PHE   A 1 258 ? -17.990 23.074  28.359 1.00 131.33 ? 554 PHE   A CA  1 
ATOM   2043 C  C   . PHE   A 1 258 ? -17.598 22.825  26.908 1.00 132.46 ? 554 PHE   A C   1 
ATOM   2044 O  O   . PHE   A 1 258 ? -17.011 21.784  26.590 1.00 130.66 ? 554 PHE   A O   1 
ATOM   2045 C  CB  . PHE   A 1 258 ? -19.402 22.556  28.612 1.00 123.10 ? 554 PHE   A CB  1 
ATOM   2046 C  CG  . PHE   A 1 258 ? -19.441 21.191  29.158 1.00 118.60 ? 554 PHE   A CG  1 
ATOM   2047 C  CD1 . PHE   A 1 258 ? -19.367 20.087  28.322 1.00 117.61 ? 554 PHE   A CD1 1 
ATOM   2048 C  CD2 . PHE   A 1 258 ? -19.543 20.999  30.521 1.00 119.18 ? 554 PHE   A CD2 1 
ATOM   2049 C  CE1 . PHE   A 1 258 ? -19.397 18.814  28.843 1.00 113.90 ? 554 PHE   A CE1 1 
ATOM   2050 C  CE2 . PHE   A 1 258 ? -19.574 19.737  31.055 1.00 109.96 ? 554 PHE   A CE2 1 
ATOM   2051 C  CZ  . PHE   A 1 258 ? -19.499 18.642  30.234 1.00 106.99 ? 554 PHE   A CZ  1 
ATOM   2052 N  N   . LYS   A 1 259 ? -17.923 23.762  26.010 1.00 129.99 ? 555 LYS   A N   1 
ATOM   2053 C  CA  . LYS   A 1 259 ? -17.552 23.590  24.606 1.00 139.93 ? 555 LYS   A CA  1 
ATOM   2054 C  C   . LYS   A 1 259 ? -16.039 23.565  24.434 1.00 139.19 ? 555 LYS   A C   1 
ATOM   2055 O  O   . LYS   A 1 259 ? -15.526 22.891  23.533 1.00 135.32 ? 555 LYS   A O   1 
ATOM   2056 C  CB  . LYS   A 1 259 ? -18.161 24.706  23.743 1.00 136.97 ? 555 LYS   A CB  1 
ATOM   2057 C  CG  . LYS   A 1 259 ? -17.634 26.112  24.063 1.00 145.70 ? 555 LYS   A CG  1 
ATOM   2058 C  CD  . LYS   A 1 259 ? -18.115 27.178  23.057 1.00 148.98 ? 555 LYS   A CD  1 
ATOM   2059 C  CE  . LYS   A 1 259 ? -19.407 27.866  23.508 1.00 155.79 ? 555 LYS   A CE  1 
ATOM   2060 N  NZ  . LYS   A 1 259 ? -20.487 26.882  23.832 1.00 161.28 ? 555 LYS   A NZ  1 
ATOM   2061 N  N   . ASP   A 1 260 ? -15.308 24.280  25.294 1.00 136.50 ? 556 ASP   A N   1 
ATOM   2062 C  CA  . ASP   A 1 260 ? -13.861 24.347  25.142 1.00 140.56 ? 556 ASP   A CA  1 
ATOM   2063 C  C   . ASP   A 1 260 ? -13.186 23.072  25.615 1.00 139.03 ? 556 ASP   A C   1 
ATOM   2064 O  O   . ASP   A 1 260 ? -12.032 22.824  25.249 1.00 141.94 ? 556 ASP   A O   1 
ATOM   2065 C  CB  . ASP   A 1 260 ? -13.310 25.568  25.881 1.00 143.06 ? 556 ASP   A CB  1 
ATOM   2066 C  CG  . ASP   A 1 260 ? -13.607 26.862  25.153 1.00 149.93 ? 556 ASP   A CG  1 
ATOM   2067 O  OD1 . ASP   A 1 260 ? -13.309 26.938  23.937 1.00 154.33 ? 556 ASP   A OD1 1 
ATOM   2068 O  OD2 . ASP   A 1 260 ? -14.161 27.789  25.783 1.00 154.41 ? 556 ASP   A OD2 1 
ATOM   2069 N  N   . LEU   A 1 261 ? -13.888 22.255  26.402 1.00 133.61 ? 557 LEU   A N   1 
ATOM   2070 C  CA  . LEU   A 1 261 ? -13.434 20.895  26.662 1.00 133.52 ? 557 LEU   A CA  1 
ATOM   2071 C  C   . LEU   A 1 261 ? -13.199 20.134  25.365 1.00 135.48 ? 557 LEU   A C   1 
ATOM   2072 O  O   . LEU   A 1 261 ? -12.390 19.202  25.329 1.00 135.31 ? 557 LEU   A O   1 
ATOM   2073 C  CB  . LEU   A 1 261 ? -14.457 20.168  27.537 1.00 129.08 ? 557 LEU   A CB  1 
ATOM   2074 C  CG  . LEU   A 1 261 ? -14.593 20.712  28.959 1.00 126.50 ? 557 LEU   A CG  1 
ATOM   2075 C  CD1 . LEU   A 1 261 ? -15.742 20.041  29.707 1.00 119.85 ? 557 LEU   A CD1 1 
ATOM   2076 C  CD2 . LEU   A 1 261 ? -13.287 20.476  29.681 1.00 133.31 ? 557 LEU   A CD2 1 
ATOM   2077 N  N   . GLY   A 1 262 ? -13.889 20.517  24.296 1.00 141.31 ? 558 GLY   A N   1 
ATOM   2078 C  CA  . GLY   A 1 262 ? -13.636 19.939  22.986 1.00 140.06 ? 558 GLY   A CA  1 
ATOM   2079 C  C   . GLY   A 1 262 ? -13.917 18.457  22.921 1.00 133.20 ? 558 GLY   A C   1 
ATOM   2080 O  O   . GLY   A 1 262 ? -13.203 17.720  22.228 1.00 134.33 ? 558 GLY   A O   1 
ATOM   2081 N  N   . LEU   A 1 263 ? -14.932 18.000  23.642 1.00 119.20 ? 559 LEU   A N   1 
ATOM   2082 C  CA  . LEU   A 1 263 ? -15.311 16.600  23.623 1.00 111.31 ? 559 LEU   A CA  1 
ATOM   2083 C  C   . LEU   A 1 263 ? -16.396 16.363  22.584 1.00 104.27 ? 559 LEU   A C   1 
ATOM   2084 O  O   . LEU   A 1 263 ? -17.150 17.269  22.222 1.00 103.07 ? 559 LEU   A O   1 
ATOM   2085 C  CB  . LEU   A 1 263 ? -15.786 16.150  25.005 1.00 107.89 ? 559 LEU   A CB  1 
ATOM   2086 C  CG  . LEU   A 1 263 ? -14.708 16.403  26.049 1.00 110.46 ? 559 LEU   A CG  1 
ATOM   2087 C  CD1 . LEU   A 1 263 ? -15.232 16.041  27.408 1.00 105.97 ? 559 LEU   A CD1 1 
ATOM   2088 C  CD2 . LEU   A 1 263 ? -13.434 15.623  25.731 1.00 108.35 ? 559 LEU   A CD2 1 
ATOM   2089 N  N   . LYS   A 1 264 ? -16.449 15.128  22.100 1.00 100.31 ? 560 LYS   A N   1 
ATOM   2090 C  CA  . LYS   A 1 264 ? -17.434 14.706  21.120 1.00 96.63  ? 560 LYS   A CA  1 
ATOM   2091 C  C   . LYS   A 1 264 ? -17.537 13.197  21.197 1.00 91.85  ? 560 LYS   A C   1 
ATOM   2092 O  O   . LYS   A 1 264 ? -16.667 12.525  21.758 1.00 89.06  ? 560 LYS   A O   1 
ATOM   2093 C  CB  . LYS   A 1 264 ? -17.074 15.123  19.687 1.00 96.74  ? 560 LYS   A CB  1 
ATOM   2094 C  CG  . LYS   A 1 264 ? -15.746 14.572  19.162 1.00 97.88  ? 560 LYS   A CG  1 
ATOM   2095 C  CD  . LYS   A 1 264 ? -15.581 14.896  17.674 1.00 100.99 ? 560 LYS   A CD  1 
ATOM   2096 C  CE  . LYS   A 1 264 ? -14.152 15.307  17.295 1.00 104.69 ? 560 LYS   A CE  1 
ATOM   2097 N  NZ  . LYS   A 1 264 ? -14.007 15.536  15.813 1.00 95.06  ? 560 LYS   A NZ  1 
ATOM   2098 N  N   . TRP   A 1 265 ? -18.610 12.667  20.622 1.00 87.96  ? 561 TRP   A N   1 
ATOM   2099 C  CA  . TRP   A 1 265 ? -18.756 11.222  20.557 1.00 84.40  ? 561 TRP   A CA  1 
ATOM   2100 C  C   . TRP   A 1 265 ? -19.527 10.893  19.290 1.00 82.16  ? 561 TRP   A C   1 
ATOM   2101 O  O   . TRP   A 1 265 ? -20.090 11.778  18.634 1.00 83.39  ? 561 TRP   A O   1 
ATOM   2102 C  CB  . TRP   A 1 265 ? -19.421 10.661  21.820 1.00 75.87  ? 561 TRP   A CB  1 
ATOM   2103 C  CG  . TRP   A 1 265 ? -19.044 9.211   22.042 1.00 76.07  ? 561 TRP   A CG  1 
ATOM   2104 C  CD1 . TRP   A 1 265 ? -19.831 8.122   21.826 1.00 75.38  ? 561 TRP   A CD1 1 
ATOM   2105 C  CD2 . TRP   A 1 265 ? -17.767 8.701   22.464 1.00 79.78  ? 561 TRP   A CD2 1 
ATOM   2106 N  NE1 . TRP   A 1 265 ? -19.141 6.970   22.103 1.00 73.26  ? 561 TRP   A NE1 1 
ATOM   2107 C  CE2 . TRP   A 1 265 ? -17.871 7.299   22.497 1.00 75.39  ? 561 TRP   A CE2 1 
ATOM   2108 C  CE3 . TRP   A 1 265 ? -16.550 9.296   22.829 1.00 82.06  ? 561 TRP   A CE3 1 
ATOM   2109 C  CZ2 . TRP   A 1 265 ? -16.812 6.476   22.879 1.00 75.70  ? 561 TRP   A CZ2 1 
ATOM   2110 C  CZ3 . TRP   A 1 265 ? -15.494 8.470   23.209 1.00 79.76  ? 561 TRP   A CZ3 1 
ATOM   2111 C  CH2 . TRP   A 1 265 ? -15.639 7.075   23.235 1.00 75.89  ? 561 TRP   A CH2 1 
ATOM   2112 N  N   . TYR   A 1 266 ? -19.499 9.620   18.921 1.00 77.44  ? 562 TYR   A N   1 
ATOM   2113 C  CA  . TYR   A 1 266 ? -20.228 9.171   17.744 1.00 77.27  ? 562 TYR   A CA  1 
ATOM   2114 C  C   . TYR   A 1 266 ? -21.617 8.699   18.156 1.00 75.46  ? 562 TYR   A C   1 
ATOM   2115 O  O   . TYR   A 1 266 ? -21.824 8.233   19.276 1.00 72.80  ? 562 TYR   A O   1 
ATOM   2116 C  CB  . TYR   A 1 266 ? -19.474 8.051   17.029 1.00 75.44  ? 562 TYR   A CB  1 
ATOM   2117 C  CG  . TYR   A 1 266 ? -18.948 6.980   17.964 1.00 72.99  ? 562 TYR   A CG  1 
ATOM   2118 C  CD1 . TYR   A 1 266 ? -19.702 5.851   18.248 1.00 72.90  ? 562 TYR   A CD1 1 
ATOM   2119 C  CD2 . TYR   A 1 266 ? -17.694 7.094   18.559 1.00 76.36  ? 562 TYR   A CD2 1 
ATOM   2120 C  CE1 . TYR   A 1 266 ? -19.223 4.864   19.107 1.00 72.50  ? 562 TYR   A CE1 1 
ATOM   2121 C  CE2 . TYR   A 1 266 ? -17.213 6.113   19.412 1.00 73.93  ? 562 TYR   A CE2 1 
ATOM   2122 C  CZ  . TYR   A 1 266 ? -17.979 5.005   19.677 1.00 71.27  ? 562 TYR   A CZ  1 
ATOM   2123 O  OH  . TYR   A 1 266 ? -17.514 4.019   20.522 1.00 73.86  ? 562 TYR   A OH  1 
ATOM   2124 N  N   . GLY   A 1 267 ? -22.581 8.836   17.244 1.00 74.16  ? 563 GLY   A N   1 
ATOM   2125 C  CA  . GLY   A 1 267 ? -23.950 8.524   17.620 1.00 72.93  ? 563 GLY   A CA  1 
ATOM   2126 C  C   . GLY   A 1 267 ? -24.210 7.039   17.736 1.00 67.92  ? 563 GLY   A C   1 
ATOM   2127 O  O   . GLY   A 1 267 ? -25.038 6.612   18.547 1.00 70.70  ? 563 GLY   A O   1 
ATOM   2128 N  N   . LEU   A 1 268 ? -23.470 6.228   16.972 1.00 64.28  ? 564 LEU   A N   1 
ATOM   2129 C  CA  . LEU   A 1 268 ? -23.850 4.849   16.703 1.00 64.68  ? 564 LEU   A CA  1 
ATOM   2130 C  C   . LEU   A 1 268 ? -23.035 3.870   17.535 1.00 63.79  ? 564 LEU   A C   1 
ATOM   2131 O  O   . LEU   A 1 268 ? -21.829 3.708   17.279 1.00 64.58  ? 564 LEU   A O   1 
ATOM   2132 C  CB  . LEU   A 1 268 ? -23.675 4.544   15.212 1.00 62.03  ? 564 LEU   A CB  1 
ATOM   2133 C  CG  . LEU   A 1 268 ? -24.251 3.207   14.763 1.00 63.23  ? 564 LEU   A CG  1 
ATOM   2134 C  CD1 . LEU   A 1 268 ? -25.753 3.327   14.565 1.00 65.93  ? 564 LEU   A CD1 1 
ATOM   2135 C  CD2 . LEU   A 1 268 ? -23.575 2.724   13.486 1.00 58.18  ? 564 LEU   A CD2 1 
ATOM   2136 N  N   . PRO   A 1 269 ? -23.637 3.175   18.513 1.00 62.31  ? 565 PRO   A N   1 
ATOM   2137 C  CA  . PRO   A 1 269 ? -22.900 2.129   19.230 1.00 60.90  ? 565 PRO   A CA  1 
ATOM   2138 C  C   . PRO   A 1 269 ? -23.049 0.824   18.474 1.00 57.44  ? 565 PRO   A C   1 
ATOM   2139 O  O   . PRO   A 1 269 ? -24.185 0.382   18.252 1.00 56.21  ? 565 PRO   A O   1 
ATOM   2140 C  CB  . PRO   A 1 269 ? -23.590 2.090   20.598 1.00 59.03  ? 565 PRO   A CB  1 
ATOM   2141 C  CG  . PRO   A 1 269 ? -25.023 2.457   20.301 1.00 60.49  ? 565 PRO   A CG  1 
ATOM   2142 C  CD  . PRO   A 1 269 ? -25.008 3.349   19.036 1.00 61.86  ? 565 PRO   A CD  1 
ATOM   2143 N  N   . ALA   A 1 270 ? -21.942 0.203   18.062 1.00 53.72  ? 566 ALA   A N   1 
ATOM   2144 C  CA  . ALA   A 1 270 ? -22.078 -0.887  17.083 1.00 56.92  ? 566 ALA   A CA  1 
ATOM   2145 C  C   . ALA   A 1 270 ? -21.014 -1.935  17.402 1.00 57.79  ? 566 ALA   A C   1 
ATOM   2146 O  O   . ALA   A 1 270 ? -19.855 -1.808  17.007 1.00 59.25  ? 566 ALA   A O   1 
ATOM   2147 C  CB  . ALA   A 1 270 ? -21.969 -0.367  15.653 1.00 57.00  ? 566 ALA   A CB  1 
ATOM   2148 N  N   . VAL   A 1 271 ? -21.425 -2.950  18.137 1.00 57.44  ? 567 VAL   A N   1 
ATOM   2149 C  CA  . VAL   A 1 271 ? -20.508 -3.989  18.576 1.00 59.27  ? 567 VAL   A CA  1 
ATOM   2150 C  C   . VAL   A 1 271 ? -20.202 -4.915  17.415 1.00 59.97  ? 567 VAL   A C   1 
ATOM   2151 O  O   . VAL   A 1 271 ? -21.118 -5.451  16.783 1.00 60.87  ? 567 VAL   A O   1 
ATOM   2152 C  CB  . VAL   A 1 271 ? -21.103 -4.767  19.749 1.00 59.34  ? 567 VAL   A CB  1 
ATOM   2153 C  CG1 . VAL   A 1 271 ? -20.381 -6.094  19.895 1.00 58.23  ? 567 VAL   A CG1 1 
ATOM   2154 C  CG2 . VAL   A 1 271 ? -20.996 -3.914  21.031 1.00 59.21  ? 567 VAL   A CG2 1 
ATOM   2155 N  N   . SER   A 1 272 ? -18.915 -5.143  17.159 1.00 61.41  ? 568 SER   A N   1 
ATOM   2156 C  CA  . SER   A 1 272 ? -18.504 -5.953  16.022 1.00 61.75  ? 568 SER   A CA  1 
ATOM   2157 C  C   . SER   A 1 272 ? -17.708 -7.199  16.384 1.00 62.25  ? 568 SER   A C   1 
ATOM   2158 O  O   . SER   A 1 272 ? -17.470 -8.031  15.503 1.00 64.19  ? 568 SER   A O   1 
ATOM   2159 C  CB  . SER   A 1 272 ? -17.682 -5.098  15.049 1.00 62.67  ? 568 SER   A CB  1 
ATOM   2160 O  OG  . SER   A 1 272 ? -16.593 -4.469  15.700 1.00 64.98  ? 568 SER   A OG  1 
ATOM   2161 N  N   . ASN   A 1 273 ? -17.296 -7.366  17.641 1.00 62.49  ? 569 ASN   A N   1 
ATOM   2162 C  CA  . ASN   A 1 273 ? -16.359 -8.423  17.998 1.00 64.35  ? 569 ASN   A CA  1 
ATOM   2163 C  C   . ASN   A 1 273 ? -17.021 -9.616  18.661 1.00 63.48  ? 569 ASN   A C   1 
ATOM   2164 O  O   . ASN   A 1 273 ? -16.314 -10.488 19.166 1.00 66.08  ? 569 ASN   A O   1 
ATOM   2165 C  CB  . ASN   A 1 273 ? -15.264 -7.889  18.922 1.00 65.11  ? 569 ASN   A CB  1 
ATOM   2166 C  CG  . ASN   A 1 273 ? -15.821 -7.296  20.199 1.00 61.84  ? 569 ASN   A CG  1 
ATOM   2167 O  OD1 . ASN   A 1 273 ? -17.036 -7.284  20.417 1.00 58.62  ? 569 ASN   A OD1 1 
ATOM   2168 N  ND2 . ASN   A 1 273 ? -14.933 -6.808  21.056 1.00 65.83  ? 569 ASN   A ND2 1 
ATOM   2169 N  N   . MET   A 1 274 ? -18.345 -9.681  18.685 1.00 61.84  ? 570 MET   A N   1 
ATOM   2170 C  CA  . MET   A 1 274 ? -19.013 -10.796 19.333 1.00 60.18  ? 570 MET   A CA  1 
ATOM   2171 C  C   . MET   A 1 274 ? -19.431 -11.839 18.307 1.00 64.12  ? 570 MET   A C   1 
ATOM   2172 O  O   . MET   A 1 274 ? -19.349 -11.633 17.100 1.00 62.06  ? 570 MET   A O   1 
ATOM   2173 C  CB  . MET   A 1 274 ? -20.208 -10.304 20.148 1.00 61.08  ? 570 MET   A CB  1 
ATOM   2174 C  CG  . MET   A 1 274 ? -19.774 -9.451  21.363 1.00 63.06  ? 570 MET   A CG  1 
ATOM   2175 S  SD  . MET   A 1 274 ? -21.195 -9.007  22.349 1.00 56.75  ? 570 MET   A SD  1 
ATOM   2176 C  CE  . MET   A 1 274 ? -21.423 -10.538 23.256 1.00 61.07  ? 570 MET   A CE  1 
ATOM   2177 N  N   . LEU   A 1 275 ? -19.857 -12.990 18.811 1.00 63.57  ? 571 LEU   A N   1 
ATOM   2178 C  CA  . LEU   A 1 275 ? -20.215 -14.117 17.976 1.00 65.30  ? 571 LEU   A CA  1 
ATOM   2179 C  C   . LEU   A 1 275 ? -21.697 -14.393 18.163 1.00 64.69  ? 571 LEU   A C   1 
ATOM   2180 O  O   . LEU   A 1 275 ? -22.167 -14.492 19.297 1.00 62.39  ? 571 LEU   A O   1 
ATOM   2181 C  CB  . LEU   A 1 275 ? -19.379 -15.336 18.332 1.00 65.81  ? 571 LEU   A CB  1 
ATOM   2182 C  CG  . LEU   A 1 275 ? -19.628 -16.558 17.456 1.00 69.09  ? 571 LEU   A CG  1 
ATOM   2183 C  CD1 . LEU   A 1 275 ? -18.300 -17.207 17.114 1.00 75.01  ? 571 LEU   A CD1 1 
ATOM   2184 C  CD2 . LEU   A 1 275 ? -20.569 -17.546 18.121 1.00 73.48  ? 571 LEU   A CD2 1 
ATOM   2185 N  N   . LEU   A 1 276 ? -22.429 -14.493 17.054 1.00 62.11  ? 572 LEU   A N   1 
ATOM   2186 C  CA  . LEU   A 1 276 ? -23.851 -14.815 17.086 1.00 63.05  ? 572 LEU   A CA  1 
ATOM   2187 C  C   . LEU   A 1 276 ? -24.040 -16.314 16.891 1.00 67.03  ? 572 LEU   A C   1 
ATOM   2188 O  O   . LEU   A 1 276 ? -23.526 -16.890 15.922 1.00 68.59  ? 572 LEU   A O   1 
ATOM   2189 C  CB  . LEU   A 1 276 ? -24.597 -14.037 16.000 1.00 62.59  ? 572 LEU   A CB  1 
ATOM   2190 C  CG  . LEU   A 1 276 ? -26.015 -14.458 15.615 1.00 62.76  ? 572 LEU   A CG  1 
ATOM   2191 C  CD1 . LEU   A 1 276 ? -26.927 -14.428 16.813 1.00 61.59  ? 572 LEU   A CD1 1 
ATOM   2192 C  CD2 . LEU   A 1 276 ? -26.560 -13.568 14.520 1.00 60.54  ? 572 LEU   A CD2 1 
ATOM   2193 N  N   . GLU   A 1 277 ? -24.790 -16.938 17.798 1.00 66.12  ? 573 GLU   A N   1 
ATOM   2194 C  CA  . GLU   A 1 277 ? -25.057 -18.372 17.768 1.00 69.99  ? 573 GLU   A CA  1 
ATOM   2195 C  C   . GLU   A 1 277 ? -26.527 -18.602 17.461 1.00 70.97  ? 573 GLU   A C   1 
ATOM   2196 O  O   . GLU   A 1 277 ? -27.394 -18.099 18.182 1.00 67.74  ? 573 GLU   A O   1 
ATOM   2197 C  CB  . GLU   A 1 277 ? -24.704 -19.029 19.097 1.00 73.54  ? 573 GLU   A CB  1 
ATOM   2198 C  CG  . GLU   A 1 277 ? -23.593 -20.037 18.990 1.00 84.20  ? 573 GLU   A CG  1 
ATOM   2199 C  CD  . GLU   A 1 277 ? -23.783 -21.191 19.924 1.00 90.67  ? 573 GLU   A CD  1 
ATOM   2200 O  OE1 . GLU   A 1 277 ? -24.737 -21.974 19.700 1.00 87.15  ? 573 GLU   A OE1 1 
ATOM   2201 O  OE2 . GLU   A 1 277 ? -22.988 -21.299 20.882 1.00 99.11  ? 573 GLU   A OE2 1 
ATOM   2202 N  N   . ILE   A 1 278 ? -26.800 -19.367 16.402 1.00 72.92  ? 574 ILE   A N   1 
ATOM   2203 C  CA  . ILE   A 1 278 ? -28.160 -19.701 15.982 1.00 73.20  ? 574 ILE   A CA  1 
ATOM   2204 C  C   . ILE   A 1 278 ? -28.185 -21.178 15.630 1.00 75.81  ? 574 ILE   A C   1 
ATOM   2205 O  O   . ILE   A 1 278 ? -27.415 -21.620 14.771 1.00 78.91  ? 574 ILE   A O   1 
ATOM   2206 C  CB  . ILE   A 1 278 ? -28.646 -18.869 14.782 1.00 69.94  ? 574 ILE   A CB  1 
ATOM   2207 C  CG1 . ILE   A 1 278 ? -28.561 -17.374 15.097 1.00 69.46  ? 574 ILE   A CG1 1 
ATOM   2208 C  CG2 . ILE   A 1 278 ? -30.076 -19.236 14.473 1.00 70.32  ? 574 ILE   A CG2 1 
ATOM   2209 C  CD1 . ILE   A 1 278 ? -28.856 -16.481 13.939 1.00 66.80  ? 574 ILE   A CD1 1 
ATOM   2210 N  N   . GLY   A 1 279 ? -29.078 -21.934 16.278 1.00 73.81  ? 575 GLY   A N   1 
ATOM   2211 C  CA  . GLY   A 1 279 ? -29.174 -23.371 16.134 1.00 79.30  ? 575 GLY   A CA  1 
ATOM   2212 C  C   . GLY   A 1 279 ? -27.834 -24.038 15.923 1.00 81.21  ? 575 GLY   A C   1 
ATOM   2213 O  O   . GLY   A 1 279 ? -27.648 -24.775 14.951 1.00 82.75  ? 575 GLY   A O   1 
ATOM   2214 N  N   . GLY   A 1 280 ? -26.871 -23.744 16.790 1.00 78.19  ? 576 GLY   A N   1 
ATOM   2215 C  CA  . GLY   A 1 280 ? -25.559 -24.343 16.677 1.00 81.65  ? 576 GLY   A CA  1 
ATOM   2216 C  C   . GLY   A 1 280 ? -24.655 -23.750 15.616 1.00 81.24  ? 576 GLY   A C   1 
ATOM   2217 O  O   . GLY   A 1 280 ? -23.465 -24.086 15.583 1.00 81.42  ? 576 GLY   A O   1 
ATOM   2218 N  N   . LEU   A 1 281 ? -25.166 -22.883 14.748 1.00 77.70  ? 577 LEU   A N   1 
ATOM   2219 C  CA  . LEU   A 1 281 ? -24.337 -22.241 13.736 1.00 75.69  ? 577 LEU   A CA  1 
ATOM   2220 C  C   . LEU   A 1 281 ? -23.653 -21.012 14.320 1.00 74.42  ? 577 LEU   A C   1 
ATOM   2221 O  O   . LEU   A 1 281 ? -24.270 -20.229 15.046 1.00 71.13  ? 577 LEU   A O   1 
ATOM   2222 C  CB  . LEU   A 1 281 ? -25.186 -21.847 12.532 1.00 77.83  ? 577 LEU   A CB  1 
ATOM   2223 C  CG  . LEU   A 1 281 ? -25.817 -22.987 11.738 1.00 78.65  ? 577 LEU   A CG  1 
ATOM   2224 C  CD1 . LEU   A 1 281 ? -26.496 -22.427 10.487 1.00 79.13  ? 577 LEU   A CD1 1 
ATOM   2225 C  CD2 . LEU   A 1 281 ? -24.776 -24.031 11.380 1.00 80.75  ? 577 LEU   A CD2 1 
ATOM   2226 N  N   . GLU   A 1 282 ? -22.375 -20.838 14.000 1.00 73.48  ? 578 GLU   A N   1 
ATOM   2227 C  CA  . GLU   A 1 282 ? -21.563 -19.793 14.608 1.00 69.89  ? 578 GLU   A CA  1 
ATOM   2228 C  C   . GLU   A 1 282 ? -21.262 -18.701 13.594 1.00 68.56  ? 578 GLU   A C   1 
ATOM   2229 O  O   . GLU   A 1 282 ? -20.668 -18.965 12.542 1.00 70.33  ? 578 GLU   A O   1 
ATOM   2230 C  CB  . GLU   A 1 282 ? -20.267 -20.376 15.175 1.00 73.54  ? 578 GLU   A CB  1 
ATOM   2231 C  CG  . GLU   A 1 282 ? -20.506 -21.337 16.319 1.00 77.93  ? 578 GLU   A CG  1 
ATOM   2232 C  CD  . GLU   A 1 282 ? -19.230 -21.759 17.015 1.00 82.33  ? 578 GLU   A CD  1 
ATOM   2233 O  OE1 . GLU   A 1 282 ? -18.256 -22.105 16.306 1.00 81.02  ? 578 GLU   A OE1 1 
ATOM   2234 O  OE2 . GLU   A 1 282 ? -19.209 -21.752 18.271 1.00 89.18  ? 578 GLU   A OE2 1 
ATOM   2235 N  N   . PHE   A 1 283 ? -21.670 -17.479 13.915 1.00 65.53  ? 579 PHE   A N   1 
ATOM   2236 C  CA  . PHE   A 1 283 ? -21.491 -16.306 13.057 1.00 66.65  ? 579 PHE   A CA  1 
ATOM   2237 C  C   . PHE   A 1 283 ? -20.443 -15.388 13.684 1.00 62.53  ? 579 PHE   A C   1 
ATOM   2238 O  O   . PHE   A 1 283 ? -20.762 -14.530 14.503 1.00 65.96  ? 579 PHE   A O   1 
ATOM   2239 C  CB  . PHE   A 1 283 ? -22.834 -15.614 12.850 1.00 64.46  ? 579 PHE   A CB  1 
ATOM   2240 C  CG  . PHE   A 1 283 ? -23.791 -16.425 12.018 1.00 66.06  ? 579 PHE   A CG  1 
ATOM   2241 C  CD1 . PHE   A 1 283 ? -23.635 -16.490 10.647 1.00 65.95  ? 579 PHE   A CD1 1 
ATOM   2242 C  CD2 . PHE   A 1 283 ? -24.814 -17.150 12.604 1.00 65.74  ? 579 PHE   A CD2 1 
ATOM   2243 C  CE1 . PHE   A 1 283 ? -24.507 -17.237 9.852  1.00 68.28  ? 579 PHE   A CE1 1 
ATOM   2244 C  CE2 . PHE   A 1 283 ? -25.687 -17.918 11.828 1.00 66.99  ? 579 PHE   A CE2 1 
ATOM   2245 C  CZ  . PHE   A 1 283 ? -25.527 -17.959 10.446 1.00 70.97  ? 579 PHE   A CZ  1 
ATOM   2246 N  N   . SER   A 1 284 ? -19.181 -15.579 13.289 1.00 65.24  ? 580 SER   A N   1 
ATOM   2247 C  CA  . SER   A 1 284 ? -18.048 -14.897 13.910 1.00 66.62  ? 580 SER   A CA  1 
ATOM   2248 C  C   . SER   A 1 284 ? -17.997 -13.412 13.596 1.00 65.73  ? 580 SER   A C   1 
ATOM   2249 O  O   . SER   A 1 284 ? -17.249 -12.673 14.241 1.00 67.56  ? 580 SER   A O   1 
ATOM   2250 C  CB  . SER   A 1 284 ? -16.755 -15.546 13.446 1.00 71.69  ? 580 SER   A CB  1 
ATOM   2251 O  OG  . SER   A 1 284 ? -16.781 -15.696 12.034 1.00 70.61  ? 580 SER   A OG  1 
ATOM   2252 N  N   . ALA   A 1 285 ? -18.736 -12.962 12.595 1.00 65.10  ? 581 ALA   A N   1 
ATOM   2253 C  CA  . ALA   A 1 285 ? -18.783 -11.551 12.258 1.00 61.32  ? 581 ALA   A CA  1 
ATOM   2254 C  C   . ALA   A 1 285 ? -20.248 -11.185 12.178 1.00 59.74  ? 581 ALA   A C   1 
ATOM   2255 O  O   . ALA   A 1 285 ? -20.955 -11.654 11.285 1.00 60.91  ? 581 ALA   A O   1 
ATOM   2256 C  CB  . ALA   A 1 285 ? -18.045 -11.263 10.956 1.00 64.47  ? 581 ALA   A CB  1 
ATOM   2257 N  N   . CYS   A 1 286 ? -20.711 -10.380 13.124 1.00 58.12  ? 582 CYS   A N   1 
ATOM   2258 C  CA  . CYS   A 1 286 ? -22.130 -10.080 13.132 1.00 56.45  ? 582 CYS   A CA  1 
ATOM   2259 C  C   . CYS   A 1 286 ? -22.393 -8.691  13.703 1.00 57.42  ? 582 CYS   A C   1 
ATOM   2260 O  O   . CYS   A 1 286 ? -23.244 -8.553  14.588 1.00 59.20  ? 582 CYS   A O   1 
ATOM   2261 C  CB  . CYS   A 1 286 ? -22.870 -11.146 13.931 1.00 59.95  ? 582 CYS   A CB  1 
ATOM   2262 S  SG  . CYS   A 1 286 ? -22.254 -11.281 15.638 1.00 58.05  ? 582 CYS   A SG  1 
ATOM   2263 N  N   . PRO   A 1 287 ? -21.747 -7.637  13.193 1.00 56.96  ? 583 PRO   A N   1 
ATOM   2264 C  CA  . PRO   A 1 287 ? -21.865 -6.320  13.839 1.00 56.22  ? 583 PRO   A CA  1 
ATOM   2265 C  C   . PRO   A 1 287 ? -23.318 -5.914  14.032 1.00 57.10  ? 583 PRO   A C   1 
ATOM   2266 O  O   . PRO   A 1 287 ? -24.139 -6.027  13.122 1.00 56.62  ? 583 PRO   A O   1 
ATOM   2267 C  CB  . PRO   A 1 287 ? -21.136 -5.381  12.869 1.00 56.79  ? 583 PRO   A CB  1 
ATOM   2268 C  CG  . PRO   A 1 287 ? -21.161 -6.078  11.560 1.00 59.53  ? 583 PRO   A CG  1 
ATOM   2269 C  CD  . PRO   A 1 287 ? -21.048 -7.544  11.899 1.00 59.92  ? 583 PRO   A CD  1 
ATOM   2270 N  N   . PHE   A 1 288 ? -23.641 -5.446  15.237 1.00 54.62  ? 584 PHE   A N   1 
ATOM   2271 C  CA  . PHE   A 1 288 ? -24.998 -5.040  15.568 1.00 55.27  ? 584 PHE   A CA  1 
ATOM   2272 C  C   . PHE   A 1 288 ? -24.977 -3.698  16.295 1.00 57.79  ? 584 PHE   A C   1 
ATOM   2273 O  O   . PHE   A 1 288 ? -24.045 -3.392  17.050 1.00 56.20  ? 584 PHE   A O   1 
ATOM   2274 C  CB  . PHE   A 1 288 ? -25.721 -6.111  16.422 1.00 57.31  ? 584 PHE   A CB  1 
ATOM   2275 C  CG  . PHE   A 1 288 ? -25.024 -6.439  17.723 1.00 59.56  ? 584 PHE   A CG  1 
ATOM   2276 C  CD1 . PHE   A 1 288 ? -25.178 -5.629  18.836 1.00 57.43  ? 584 PHE   A CD1 1 
ATOM   2277 C  CD2 . PHE   A 1 288 ? -24.244 -7.581  17.835 1.00 59.74  ? 584 PHE   A CD2 1 
ATOM   2278 C  CE1 . PHE   A 1 288 ? -24.553 -5.933  20.024 1.00 57.92  ? 584 PHE   A CE1 1 
ATOM   2279 C  CE2 . PHE   A 1 288 ? -23.616 -7.887  19.017 1.00 54.83  ? 584 PHE   A CE2 1 
ATOM   2280 C  CZ  . PHE   A 1 288 ? -23.779 -7.061  20.117 1.00 57.74  ? 584 PHE   A CZ  1 
ATOM   2281 N  N   . SER   A 1 289 ? -26.013 -2.890  16.052 1.00 54.67  ? 585 SER   A N   1 
ATOM   2282 C  CA  . SER   A 1 289 ? -26.033 -1.527  16.557 1.00 57.57  ? 585 SER   A CA  1 
ATOM   2283 C  C   . SER   A 1 289 ? -27.416 -1.149  17.069 1.00 57.74  ? 585 SER   A C   1 
ATOM   2284 O  O   . SER   A 1 289 ? -28.439 -1.636  16.576 1.00 54.07  ? 585 SER   A O   1 
ATOM   2285 C  CB  . SER   A 1 289 ? -25.563 -0.515  15.482 1.00 55.07  ? 585 SER   A CB  1 
ATOM   2286 O  OG  . SER   A 1 289 ? -26.336 -0.554  14.282 1.00 60.52  ? 585 SER   A OG  1 
ATOM   2287 N  N   . GLY   A 1 290 ? -27.431 -0.264  18.075 1.00 55.58  ? 586 GLY   A N   1 
ATOM   2288 C  CA  . GLY   A 1 290 ? -28.675 0.362   18.471 1.00 57.59  ? 586 GLY   A CA  1 
ATOM   2289 C  C   . GLY   A 1 290 ? -28.523 1.863   18.618 1.00 61.97  ? 586 GLY   A C   1 
ATOM   2290 O  O   . GLY   A 1 290 ? -28.105 2.554   17.684 1.00 58.28  ? 586 GLY   A O   1 
ATOM   2291 N  N   . TRP   A 1 291 ? -28.865 2.384   19.790 1.00 59.96  ? 587 TRP   A N   1 
ATOM   2292 C  CA  . TRP   A 1 291 ? -28.528 3.756   20.137 1.00 64.02  ? 587 TRP   A CA  1 
ATOM   2293 C  C   . TRP   A 1 291 ? -27.990 3.750   21.559 1.00 61.81  ? 587 TRP   A C   1 
ATOM   2294 O  O   . TRP   A 1 291 ? -28.082 2.749   22.264 1.00 56.45  ? 587 TRP   A O   1 
ATOM   2295 C  CB  . TRP   A 1 291 ? -29.720 4.699   20.010 1.00 68.48  ? 587 TRP   A CB  1 
ATOM   2296 C  CG  . TRP   A 1 291 ? -30.943 4.194   20.673 1.00 67.87  ? 587 TRP   A CG  1 
ATOM   2297 C  CD1 . TRP   A 1 291 ? -31.247 4.265   22.006 1.00 68.70  ? 587 TRP   A CD1 1 
ATOM   2298 C  CD2 . TRP   A 1 291 ? -32.049 3.546   20.040 1.00 69.17  ? 587 TRP   A CD2 1 
ATOM   2299 N  NE1 . TRP   A 1 291 ? -32.481 3.703   22.239 1.00 69.32  ? 587 TRP   A NE1 1 
ATOM   2300 C  CE2 . TRP   A 1 291 ? -32.995 3.258   21.046 1.00 72.46  ? 587 TRP   A CE2 1 
ATOM   2301 C  CE3 . TRP   A 1 291 ? -32.339 3.190   18.717 1.00 68.80  ? 587 TRP   A CE3 1 
ATOM   2302 C  CZ2 . TRP   A 1 291 ? -34.205 2.612   20.767 1.00 75.87  ? 587 TRP   A CZ2 1 
ATOM   2303 C  CZ3 . TRP   A 1 291 ? -33.544 2.564   18.443 1.00 70.49  ? 587 TRP   A CZ3 1 
ATOM   2304 C  CH2 . TRP   A 1 291 ? -34.459 2.281   19.459 1.00 75.53  ? 587 TRP   A CH2 1 
ATOM   2305 N  N   . TYR   A 1 292 ? -27.398 4.865   21.955 1.00 60.76  ? 588 TYR   A N   1 
ATOM   2306 C  CA  . TYR   A 1 292 ? -26.668 4.917   23.214 1.00 64.41  ? 588 TYR   A CA  1 
ATOM   2307 C  C   . TYR   A 1 292 ? -27.597 5.233   24.376 1.00 64.95  ? 588 TYR   A C   1 
ATOM   2308 O  O   . TYR   A 1 292 ? -28.506 6.063   24.260 1.00 64.66  ? 588 TYR   A O   1 
ATOM   2309 C  CB  . TYR   A 1 292 ? -25.564 5.974   23.133 1.00 62.98  ? 588 TYR   A CB  1 
ATOM   2310 C  CG  . TYR   A 1 292 ? -24.150 5.475   22.836 1.00 65.55  ? 588 TYR   A CG  1 
ATOM   2311 C  CD1 . TYR   A 1 292 ? -23.503 4.566   23.689 1.00 64.71  ? 588 TYR   A CD1 1 
ATOM   2312 C  CD2 . TYR   A 1 292 ? -23.439 5.966   21.738 1.00 65.69  ? 588 TYR   A CD2 1 
ATOM   2313 C  CE1 . TYR   A 1 292 ? -22.191 4.147   23.427 1.00 66.39  ? 588 TYR   A CE1 1 
ATOM   2314 C  CE2 . TYR   A 1 292 ? -22.138 5.566   21.483 1.00 65.92  ? 588 TYR   A CE2 1 
ATOM   2315 C  CZ  . TYR   A 1 292 ? -21.521 4.653   22.314 1.00 65.85  ? 588 TYR   A CZ  1 
ATOM   2316 O  OH  . TYR   A 1 292 ? -20.229 4.265   22.034 1.00 68.27  ? 588 TYR   A OH  1 
ATOM   2317 N  N   . MET   A 1 293 ? -27.363 4.558   25.497 1.00 63.58  ? 589 MET   A N   1 
ATOM   2318 C  CA  . MET   A 1 293 ? -27.745 5.094   26.793 1.00 66.05  ? 589 MET   A CA  1 
ATOM   2319 C  C   . MET   A 1 293 ? -26.660 6.058   27.251 1.00 62.80  ? 589 MET   A C   1 
ATOM   2320 O  O   . MET   A 1 293 ? -25.467 5.747   27.166 1.00 63.29  ? 589 MET   A O   1 
ATOM   2321 C  CB  . MET   A 1 293 ? -27.931 3.971   27.825 1.00 61.15  ? 589 MET   A CB  1 
ATOM   2322 C  CG  . MET   A 1 293 ? -28.490 4.458   29.153 1.00 63.91  ? 589 MET   A CG  1 
ATOM   2323 S  SD  . MET   A 1 293 ? -28.932 3.065   30.189 1.00 59.85  ? 589 MET   A SD  1 
ATOM   2324 C  CE  . MET   A 1 293 ? -27.334 2.519   30.808 1.00 59.81  ? 589 MET   A CE  1 
ATOM   2325 N  N   . GLY   A 1 294 ? -27.087 7.227   27.737 1.00 62.92  ? 590 GLY   A N   1 
ATOM   2326 C  CA  . GLY   A 1 294 ? -26.159 8.318   28.014 1.00 63.19  ? 590 GLY   A CA  1 
ATOM   2327 C  C   . GLY   A 1 294 ? -24.954 7.917   28.839 1.00 67.25  ? 590 GLY   A C   1 
ATOM   2328 O  O   . GLY   A 1 294 ? -23.836 8.373   28.581 1.00 67.87  ? 590 GLY   A O   1 
ATOM   2329 N  N   . THR   A 1 295 ? -25.165 7.071   29.852 1.00 63.96  ? 591 THR   A N   1 
ATOM   2330 C  CA  . THR   A 1 295 ? -24.088 6.766   30.791 1.00 68.68  ? 591 THR   A CA  1 
ATOM   2331 C  C   . THR   A 1 295 ? -22.930 6.037   30.121 1.00 67.29  ? 591 THR   A C   1 
ATOM   2332 O  O   . THR   A 1 295 ? -21.779 6.178   30.556 1.00 64.34  ? 591 THR   A O   1 
ATOM   2333 C  CB  . THR   A 1 295 ? -24.619 5.935   31.950 1.00 59.44  ? 591 THR   A CB  1 
ATOM   2334 O  OG1 . THR   A 1 295 ? -25.220 4.737   31.445 1.00 61.32  ? 591 THR   A OG1 1 
ATOM   2335 C  CG2 . THR   A 1 295 ? -25.656 6.733   32.697 1.00 64.31  ? 591 THR   A CG2 1 
ATOM   2336 N  N   . GLU   A 1 296 ? -23.205 5.254   29.073 1.00 60.92  ? 592 GLU   A N   1 
ATOM   2337 C  CA  . GLU   A 1 296 ? -22.116 4.560   28.392 1.00 62.79  ? 592 GLU   A CA  1 
ATOM   2338 C  C   . GLU   A 1 296 ? -21.027 5.542   27.983 1.00 63.69  ? 592 GLU   A C   1 
ATOM   2339 O  O   . GLU   A 1 296 ? -19.835 5.256   28.124 1.00 65.31  ? 592 GLU   A O   1 
ATOM   2340 C  CB  . GLU   A 1 296 ? -22.638 3.804   27.175 1.00 61.62  ? 592 GLU   A CB  1 
ATOM   2341 C  CG  . GLU   A 1 296 ? -23.632 2.695   27.465 1.00 61.86  ? 592 GLU   A CG  1 
ATOM   2342 C  CD  . GLU   A 1 296 ? -24.148 2.044   26.192 1.00 61.95  ? 592 GLU   A CD  1 
ATOM   2343 O  OE1 . GLU   A 1 296 ? -23.428 1.171   25.634 1.00 58.61  ? 592 GLU   A OE1 1 
ATOM   2344 O  OE2 . GLU   A 1 296 ? -25.258 2.420   25.733 1.00 63.18  ? 592 GLU   A OE2 1 
ATOM   2345 N  N   . ILE   A 1 297 ? -21.416 6.717   27.501 1.00 64.41  ? 593 ILE   A N   1 
ATOM   2346 C  CA  . ILE   A 1 297 ? -20.449 7.728   27.093 1.00 68.37  ? 593 ILE   A CA  1 
ATOM   2347 C  C   . ILE   A 1 297 ? -20.032 8.600   28.266 1.00 70.35  ? 593 ILE   A C   1 
ATOM   2348 O  O   . ILE   A 1 297 ? -18.843 8.873   28.469 1.00 73.36  ? 593 ILE   A O   1 
ATOM   2349 C  CB  . ILE   A 1 297 ? -21.034 8.605   25.967 1.00 69.54  ? 593 ILE   A CB  1 
ATOM   2350 C  CG1 . ILE   A 1 297 ? -21.576 7.778   24.808 1.00 69.73  ? 593 ILE   A CG1 1 
ATOM   2351 C  CG2 . ILE   A 1 297 ? -19.984 9.550   25.476 1.00 71.71  ? 593 ILE   A CG2 1 
ATOM   2352 C  CD1 . ILE   A 1 297 ? -22.402 8.614   23.833 1.00 70.64  ? 593 ILE   A CD1 1 
ATOM   2353 N  N   . GLY   A 1 298 ? -21.016 9.042   29.056 1.00 73.35  ? 594 GLY   A N   1 
ATOM   2354 C  CA  . GLY   A 1 298 ? -20.758 10.071  30.046 1.00 75.44  ? 594 GLY   A CA  1 
ATOM   2355 C  C   . GLY   A 1 298 ? -20.143 9.563   31.329 1.00 73.86  ? 594 GLY   A C   1 
ATOM   2356 O  O   . GLY   A 1 298 ? -19.492 10.329  32.037 1.00 71.73  ? 594 GLY   A O   1 
ATOM   2357 N  N   . VAL   A 1 299 ? -20.328 8.281   31.643 1.00 72.85  ? 595 VAL   A N   1 
ATOM   2358 C  CA  . VAL   A 1 299 ? -19.795 7.708   32.876 1.00 70.89  ? 595 VAL   A CA  1 
ATOM   2359 C  C   . VAL   A 1 299 ? -18.605 6.827   32.523 1.00 71.83  ? 595 VAL   A C   1 
ATOM   2360 O  O   . VAL   A 1 299 ? -17.478 7.076   32.957 1.00 72.96  ? 595 VAL   A O   1 
ATOM   2361 C  CB  . VAL   A 1 299 ? -20.875 6.919   33.643 1.00 70.45  ? 595 VAL   A CB  1 
ATOM   2362 C  CG1 . VAL   A 1 299 ? -20.335 6.425   35.020 1.00 64.87  ? 595 VAL   A CG1 1 
ATOM   2363 C  CG2 . VAL   A 1 299 ? -22.124 7.759   33.855 1.00 66.32  ? 595 VAL   A CG2 1 
ATOM   2364 N  N   . ARG   A 1 300 ? -18.839 5.805   31.712 1.00 67.65  ? 596 ARG   A N   1 
ATOM   2365 C  CA  . ARG   A 1 300 ? -17.778 4.857   31.393 1.00 69.27  ? 596 ARG   A CA  1 
ATOM   2366 C  C   . ARG   A 1 300 ? -16.757 5.453   30.418 1.00 72.63  ? 596 ARG   A C   1 
ATOM   2367 O  O   . ARG   A 1 300 ? -15.555 5.519   30.715 1.00 72.82  ? 596 ARG   A O   1 
ATOM   2368 C  CB  . ARG   A 1 300 ? -18.406 3.577   30.831 1.00 66.67  ? 596 ARG   A CB  1 
ATOM   2369 C  CG  . ARG   A 1 300 ? -19.459 3.009   31.764 1.00 63.92  ? 596 ARG   A CG  1 
ATOM   2370 C  CD  . ARG   A 1 300 ? -18.857 2.785   33.178 1.00 65.28  ? 596 ARG   A CD  1 
ATOM   2371 N  NE  . ARG   A 1 300 ? -17.593 2.052   33.127 1.00 63.92  ? 596 ARG   A NE  1 
ATOM   2372 C  CZ  . ARG   A 1 300 ? -17.497 0.775   32.776 1.00 62.02  ? 596 ARG   A CZ  1 
ATOM   2373 N  NH1 . ARG   A 1 300 ? -18.571 0.054   32.504 1.00 59.95  ? 596 ARG   A NH1 1 
ATOM   2374 N  NH2 . ARG   A 1 300 ? -16.293 0.220   32.664 1.00 62.66  ? 596 ARG   A NH2 1 
ATOM   2375 N  N   . ASP   A 1 301 ? -17.220 5.876   29.237 1.00 73.00  ? 597 ASP   A N   1 
ATOM   2376 C  CA  . ASP   A 1 301 ? -16.300 6.336   28.193 1.00 73.68  ? 597 ASP   A CA  1 
ATOM   2377 C  C   . ASP   A 1 301 ? -15.520 7.569   28.644 1.00 75.84  ? 597 ASP   A C   1 
ATOM   2378 O  O   . ASP   A 1 301 ? -14.293 7.642   28.502 1.00 79.26  ? 597 ASP   A O   1 
ATOM   2379 C  CB  . ASP   A 1 301 ? -17.075 6.629   26.897 1.00 70.85  ? 597 ASP   A CB  1 
ATOM   2380 C  CG  . ASP   A 1 301 ? -17.463 5.365   26.136 1.00 72.28  ? 597 ASP   A CG  1 
ATOM   2381 O  OD1 . ASP   A 1 301 ? -16.689 4.381   26.143 1.00 73.50  ? 597 ASP   A OD1 1 
ATOM   2382 O  OD2 . ASP   A 1 301 ? -18.541 5.351   25.507 1.00 70.21  ? 597 ASP   A OD2 1 
ATOM   2383 N  N   . TYR   A 1 302 ? -16.210 8.532   29.234 1.00 74.41  ? 598 TYR   A N   1 
ATOM   2384 C  CA  . TYR   A 1 302 ? -15.558 9.776   29.631 1.00 75.70  ? 598 TYR   A CA  1 
ATOM   2385 C  C   . TYR   A 1 302 ? -14.854 9.707   30.994 1.00 82.24  ? 598 TYR   A C   1 
ATOM   2386 O  O   . TYR   A 1 302 ? -13.907 10.469  31.243 1.00 84.33  ? 598 TYR   A O   1 
ATOM   2387 C  CB  . TYR   A 1 302 ? -16.603 10.888  29.640 1.00 80.22  ? 598 TYR   A CB  1 
ATOM   2388 C  CG  . TYR   A 1 302 ? -16.925 11.427  28.269 1.00 82.23  ? 598 TYR   A CG  1 
ATOM   2389 C  CD1 . TYR   A 1 302 ? -16.131 11.113  27.171 1.00 84.64  ? 598 TYR   A CD1 1 
ATOM   2390 C  CD2 . TYR   A 1 302 ? -18.001 12.289  28.077 1.00 85.69  ? 598 TYR   A CD2 1 
ATOM   2391 C  CE1 . TYR   A 1 302 ? -16.412 11.643  25.901 1.00 87.08  ? 598 TYR   A CE1 1 
ATOM   2392 C  CE2 . TYR   A 1 302 ? -18.285 12.820  26.802 1.00 86.66  ? 598 TYR   A CE2 1 
ATOM   2393 C  CZ  . TYR   A 1 302 ? -17.490 12.492  25.735 1.00 88.72  ? 598 TYR   A CZ  1 
ATOM   2394 O  OH  . TYR   A 1 302 ? -17.776 13.019  24.499 1.00 89.07  ? 598 TYR   A OH  1 
ATOM   2395 N  N   . CYS   A 1 303 ? -15.280 8.823   31.888 1.00 76.35  ? 599 CYS   A N   1 
ATOM   2396 C  CA  . CYS   A 1 303 ? -14.863 8.944   33.274 1.00 81.98  ? 599 CYS   A CA  1 
ATOM   2397 C  C   . CYS   A 1 303 ? -14.183 7.716   33.871 1.00 80.23  ? 599 CYS   A C   1 
ATOM   2398 O  O   . CYS   A 1 303 ? -13.588 7.846   34.949 1.00 83.91  ? 599 CYS   A O   1 
ATOM   2399 C  CB  . CYS   A 1 303 ? -16.065 9.346   34.142 1.00 78.77  ? 599 CYS   A CB  1 
ATOM   2400 S  SG  . CYS   A 1 303 ? -16.636 11.048  33.845 1.00 84.24  ? 599 CYS   A SG  1 
ATOM   2401 N  N   . ASP   A 1 304 ? -14.213 6.552   33.217 1.00 76.20  ? 600 ASP   A N   1 
ATOM   2402 C  CA  . ASP   A 1 304 ? -13.354 5.456   33.661 1.00 81.00  ? 600 ASP   A CA  1 
ATOM   2403 C  C   . ASP   A 1 304 ? -11.917 5.951   33.757 1.00 84.22  ? 600 ASP   A C   1 
ATOM   2404 O  O   . ASP   A 1 304 ? -11.469 6.756   32.940 1.00 87.97  ? 600 ASP   A O   1 
ATOM   2405 C  CB  . ASP   A 1 304 ? -13.413 4.257   32.704 1.00 79.27  ? 600 ASP   A CB  1 
ATOM   2406 C  CG  . ASP   A 1 304 ? -14.574 3.310   32.990 1.00 75.45  ? 600 ASP   A CG  1 
ATOM   2407 O  OD1 . ASP   A 1 304 ? -15.456 3.656   33.799 1.00 71.93  ? 600 ASP   A OD1 1 
ATOM   2408 O  OD2 . ASP   A 1 304 ? -14.612 2.213   32.383 1.00 72.08  ? 600 ASP   A OD2 1 
ATOM   2409 N  N   . ASN   A 1 305 ? -11.201 5.489   34.780 1.00 89.17  ? 601 ASN   A N   1 
ATOM   2410 C  CA  . ASN   A 1 305 ? -9.805  5.884   34.926 1.00 91.08  ? 601 ASN   A CA  1 
ATOM   2411 C  C   . ASN   A 1 305 ? -8.966  5.394   33.759 1.00 88.53  ? 601 ASN   A C   1 
ATOM   2412 O  O   . ASN   A 1 305 ? -7.934  5.997   33.445 1.00 88.66  ? 601 ASN   A O   1 
ATOM   2413 C  CB  . ASN   A 1 305 ? -9.239  5.348   36.241 1.00 89.27  ? 601 ASN   A CB  1 
ATOM   2414 C  CG  . ASN   A 1 305 ? -9.607  6.209   37.417 1.00 95.75  ? 601 ASN   A CG  1 
ATOM   2415 O  OD1 . ASN   A 1 305 ? -9.692  7.433   37.297 1.00 97.88  ? 601 ASN   A OD1 1 
ATOM   2416 N  ND2 . ASN   A 1 305 ? -9.808  5.583   38.577 1.00 96.25  ? 601 ASN   A ND2 1 
ATOM   2417 N  N   . SER   A 1 306 ? -9.389  4.298   33.127 1.00 87.56  ? 602 SER   A N   1 
ATOM   2418 C  CA  . SER   A 1 306 ? -8.697  3.653   32.024 1.00 83.54  ? 602 SER   A CA  1 
ATOM   2419 C  C   . SER   A 1 306 ? -9.203  4.122   30.674 1.00 86.74  ? 602 SER   A C   1 
ATOM   2420 O  O   . SER   A 1 306 ? -8.821  3.547   29.652 1.00 86.46  ? 602 SER   A O   1 
ATOM   2421 C  CB  . SER   A 1 306 ? -8.850  2.131   32.129 1.00 86.13  ? 602 SER   A CB  1 
ATOM   2422 O  OG  . SER   A 1 306 ? -8.438  1.665   33.410 1.00 92.95  ? 602 SER   A OG  1 
ATOM   2423 N  N   . ARG   A 1 307 ? -10.065 5.138   30.656 1.00 90.95  ? 603 ARG   A N   1 
ATOM   2424 C  CA  . ARG   A 1 307 ? -10.605 5.693   29.425 1.00 87.98  ? 603 ARG   A CA  1 
ATOM   2425 C  C   . ARG   A 1 307 ? -10.223 7.166   29.339 1.00 89.43  ? 603 ARG   A C   1 
ATOM   2426 O  O   . ARG   A 1 307 ? -9.109  7.531   29.727 1.00 90.90  ? 603 ARG   A O   1 
ATOM   2427 C  CB  . ARG   A 1 307 ? -12.117 5.482   29.365 1.00 83.69  ? 603 ARG   A CB  1 
ATOM   2428 C  CG  . ARG   A 1 307 ? -12.522 4.018   29.442 1.00 81.17  ? 603 ARG   A CG  1 
ATOM   2429 C  CD  . ARG   A 1 307 ? -12.022 3.183   28.277 1.00 81.87  ? 603 ARG   A CD  1 
ATOM   2430 N  NE  . ARG   A 1 307 ? -12.531 3.698   27.014 1.00 78.03  ? 603 ARG   A NE  1 
ATOM   2431 C  CZ  . ARG   A 1 307 ? -13.782 3.560   26.605 1.00 77.08  ? 603 ARG   A CZ  1 
ATOM   2432 N  NH1 . ARG   A 1 307 ? -14.662 2.859   27.297 1.00 68.04  ? 603 ARG   A NH1 1 
ATOM   2433 N  NH2 . ARG   A 1 307 ? -14.161 4.140   25.467 1.00 78.40  ? 603 ARG   A NH2 1 
ATOM   2434 N  N   . TYR   A 1 308 ? -11.124 8.025   28.848 1.00 84.51  ? 604 TYR   A N   1 
ATOM   2435 C  CA  . TYR   A 1 308 ? -10.759 9.433   28.666 1.00 85.74  ? 604 TYR   A CA  1 
ATOM   2436 C  C   . TYR   A 1 308 ? -10.422 10.121  29.981 1.00 92.17  ? 604 TYR   A C   1 
ATOM   2437 O  O   . TYR   A 1 308 ? -9.558  11.011  30.008 1.00 91.04  ? 604 TYR   A O   1 
ATOM   2438 C  CB  . TYR   A 1 308 ? -11.872 10.177  27.941 1.00 87.21  ? 604 TYR   A CB  1 
ATOM   2439 C  CG  . TYR   A 1 308 ? -11.756 9.980   26.452 1.00 90.85  ? 604 TYR   A CG  1 
ATOM   2440 C  CD1 . TYR   A 1 308 ? -12.212 8.820   25.854 1.00 89.35  ? 604 TYR   A CD1 1 
ATOM   2441 C  CD2 . TYR   A 1 308 ? -11.153 10.940  25.645 1.00 98.02  ? 604 TYR   A CD2 1 
ATOM   2442 C  CE1 . TYR   A 1 308 ? -12.091 8.629   24.480 1.00 86.94  ? 604 TYR   A CE1 1 
ATOM   2443 C  CE2 . TYR   A 1 308 ? -11.031 10.749  24.264 1.00 96.05  ? 604 TYR   A CE2 1 
ATOM   2444 C  CZ  . TYR   A 1 308 ? -11.496 9.591   23.704 1.00 90.36  ? 604 TYR   A CZ  1 
ATOM   2445 O  OH  . TYR   A 1 308 ? -11.390 9.383   22.337 1.00 95.86  ? 604 TYR   A OH  1 
ATOM   2446 N  N   . ASN   A 1 309 ? -11.092 9.746   31.069 1.00 85.89  ? 605 ASN   A N   1 
ATOM   2447 C  CA  . ASN   A 1 309 ? -10.658 10.143  32.403 1.00 89.84  ? 605 ASN   A CA  1 
ATOM   2448 C  C   . ASN   A 1 309 ? -10.730 11.662  32.563 1.00 93.42  ? 605 ASN   A C   1 
ATOM   2449 O  O   . ASN   A 1 309 ? -9.748  12.326  32.911 1.00 98.93  ? 605 ASN   A O   1 
ATOM   2450 C  CB  . ASN   A 1 309 ? -9.244  9.611   32.662 1.00 90.82  ? 605 ASN   A CB  1 
ATOM   2451 C  CG  . ASN   A 1 309 ? -8.842  9.661   34.107 1.00 96.85  ? 605 ASN   A CG  1 
ATOM   2452 O  OD1 . ASN   A 1 309 ? -9.305  10.503  34.877 1.00 100.87 ? 605 ASN   A OD1 1 
ATOM   2453 N  ND2 . ASN   A 1 309 ? -7.963  8.747   34.489 1.00 96.94  ? 605 ASN   A ND2 1 
ATOM   2454 N  N   . ILE   A 1 310 ? -11.916 12.220  32.284 1.00 94.82  ? 606 ILE   A N   1 
ATOM   2455 C  CA  . ILE   A 1 310 ? -12.078 13.671  32.251 1.00 97.51  ? 606 ILE   A CA  1 
ATOM   2456 C  C   . ILE   A 1 310 ? -12.587 14.256  33.567 1.00 103.77 ? 606 ILE   A C   1 
ATOM   2457 O  O   . ILE   A 1 310 ? -12.800 15.473  33.642 1.00 110.11 ? 606 ILE   A O   1 
ATOM   2458 C  CB  . ILE   A 1 310 ? -13.028 14.096  31.114 1.00 99.78  ? 606 ILE   A CB  1 
ATOM   2459 C  CG1 . ILE   A 1 310 ? -14.463 13.663  31.423 1.00 98.68  ? 606 ILE   A CG1 1 
ATOM   2460 C  CG2 . ILE   A 1 310 ? -12.583 13.501  29.778 1.00 89.56  ? 606 ILE   A CG2 1 
ATOM   2461 C  CD1 . ILE   A 1 310 ? -15.456 14.110  30.342 1.00 91.38  ? 606 ILE   A CD1 1 
ATOM   2462 N  N   . LEU   A 1 311 ? -12.796 13.433  34.605 1.00 104.38 ? 607 LEU   A N   1 
ATOM   2463 C  CA  . LEU   A 1 311 ? -13.185 13.973  35.910 1.00 103.04 ? 607 LEU   A CA  1 
ATOM   2464 C  C   . LEU   A 1 311 ? -12.186 15.008  36.390 1.00 112.26 ? 607 LEU   A C   1 
ATOM   2465 O  O   . LEU   A 1 311 ? -12.575 16.047  36.939 1.00 117.80 ? 607 LEU   A O   1 
ATOM   2466 C  CB  . LEU   A 1 311 ? -13.317 12.860  36.949 1.00 85.55  ? 607 LEU   A CB  1 
ATOM   2467 C  CG  . LEU   A 1 311 ? -14.611 12.041  36.895 1.00 86.22  ? 607 LEU   A CG  1 
ATOM   2468 C  CD1 . LEU   A 1 311 ? -14.699 11.035  38.055 1.00 87.02  ? 607 LEU   A CD1 1 
ATOM   2469 C  CD2 . LEU   A 1 311 ? -15.800 12.971  36.913 1.00 83.60  ? 607 LEU   A CD2 1 
ATOM   2470 N  N   . GLU   A 1 312 ? -10.895 14.736  36.195 1.00 112.06 ? 608 GLU   A N   1 
ATOM   2471 C  CA  . GLU   A 1 312 ? -9.828  15.676  36.532 1.00 125.30 ? 608 GLU   A CA  1 
ATOM   2472 C  C   . GLU   A 1 312 ? -10.112 17.085  36.016 1.00 130.75 ? 608 GLU   A C   1 
ATOM   2473 O  O   . GLU   A 1 312 ? -10.307 18.017  36.808 1.00 132.16 ? 608 GLU   A O   1 
ATOM   2474 C  CB  . GLU   A 1 312 ? -8.496  15.179  35.962 1.00 130.97 ? 608 GLU   A CB  1 
ATOM   2475 C  CG  . GLU   A 1 312 ? -7.775  14.133  36.795 1.00 129.51 ? 608 GLU   A CG  1 
ATOM   2476 C  CD  . GLU   A 1 312 ? -6.868  14.762  37.838 1.00 136.94 ? 608 GLU   A CD  1 
ATOM   2477 O  OE1 . GLU   A 1 312 ? -7.376  15.534  38.679 1.00 135.88 ? 608 GLU   A OE1 1 
ATOM   2478 O  OE2 . GLU   A 1 312 ? -5.645  14.501  37.810 1.00 138.87 ? 608 GLU   A OE2 1 
ATOM   2479 N  N   . GLU   A 1 313 ? -10.152 17.240  34.689 1.00 142.42 ? 609 GLU   A N   1 
ATOM   2480 C  CA  . GLU   A 1 313 ? -10.244 18.566  34.092 1.00 150.86 ? 609 GLU   A CA  1 
ATOM   2481 C  C   . GLU   A 1 313 ? -11.657 19.133  34.086 1.00 149.08 ? 609 GLU   A C   1 
ATOM   2482 O  O   . GLU   A 1 313 ? -11.815 20.354  33.987 1.00 157.24 ? 609 GLU   A O   1 
ATOM   2483 C  CB  . GLU   A 1 313 ? -9.700  18.553  32.661 1.00 161.01 ? 609 GLU   A CB  1 
ATOM   2484 C  CG  . GLU   A 1 313 ? -8.176  18.690  32.559 1.00 170.28 ? 609 GLU   A CG  1 
ATOM   2485 C  CD  . GLU   A 1 313 ? -7.654  20.101  32.866 1.00 179.10 ? 609 GLU   A CD  1 
ATOM   2486 O  OE1 . GLU   A 1 313 ? -8.429  20.965  33.334 1.00 178.52 ? 609 GLU   A OE1 1 
ATOM   2487 O  OE2 . GLU   A 1 313 ? -6.450  20.346  32.634 1.00 183.92 ? 609 GLU   A OE2 1 
ATOM   2488 N  N   . VAL   A 1 314 ? -12.688 18.297  34.181 1.00 130.72 ? 610 VAL   A N   1 
ATOM   2489 C  CA  . VAL   A 1 314 ? -14.028 18.855  34.319 1.00 127.35 ? 610 VAL   A CA  1 
ATOM   2490 C  C   . VAL   A 1 314 ? -14.206 19.492  35.692 1.00 127.72 ? 610 VAL   A C   1 
ATOM   2491 O  O   . VAL   A 1 314 ? -14.753 20.595  35.810 1.00 128.42 ? 610 VAL   A O   1 
ATOM   2492 C  CB  . VAL   A 1 314 ? -15.087 17.777  34.052 1.00 117.93 ? 610 VAL   A CB  1 
ATOM   2493 C  CG1 . VAL   A 1 314 ? -16.448 18.237  34.555 1.00 116.37 ? 610 VAL   A CG1 1 
ATOM   2494 C  CG2 . VAL   A 1 314 ? -15.140 17.474  32.576 1.00 113.57 ? 610 VAL   A CG2 1 
ATOM   2495 N  N   . ALA   A 1 315 ? -13.743 18.815  36.745 1.00 124.12 ? 611 ALA   A N   1 
ATOM   2496 C  CA  . ALA   A 1 315 ? -13.865 19.370  38.087 1.00 127.47 ? 611 ALA   A CA  1 
ATOM   2497 C  C   . ALA   A 1 315 ? -13.107 20.681  38.207 1.00 132.95 ? 611 ALA   A C   1 
ATOM   2498 O  O   . ALA   A 1 315 ? -13.582 21.621  38.855 1.00 135.12 ? 611 ALA   A O   1 
ATOM   2499 C  CB  . ALA   A 1 315 ? -13.367 18.367  39.125 1.00 120.47 ? 611 ALA   A CB  1 
ATOM   2500 N  N   . LYS   A 1 316 ? -11.923 20.759  37.596 1.00 133.38 ? 612 LYS   A N   1 
ATOM   2501 C  CA  . LYS   A 1 316 ? -11.155 21.999  37.590 1.00 136.07 ? 612 LYS   A CA  1 
ATOM   2502 C  C   . LYS   A 1 316 ? -12.018 23.169  37.139 1.00 138.41 ? 612 LYS   A C   1 
ATOM   2503 O  O   . LYS   A 1 316 ? -12.226 24.135  37.882 1.00 140.21 ? 612 LYS   A O   1 
ATOM   2504 C  CB  . LYS   A 1 316 ? -9.935  21.861  36.673 1.00 141.47 ? 612 LYS   A CB  1 
ATOM   2505 C  CG  . LYS   A 1 316 ? -8.674  21.347  37.349 1.00 143.16 ? 612 LYS   A CG  1 
ATOM   2506 C  CD  . LYS   A 1 316 ? -7.430  21.789  36.577 1.00 150.88 ? 612 LYS   A CD  1 
ATOM   2507 C  CE  . LYS   A 1 316 ? -7.307  23.316  36.551 1.00 151.22 ? 612 LYS   A CE  1 
ATOM   2508 N  NZ  . LYS   A 1 316 ? -6.121  23.826  35.790 1.00 154.76 ? 612 LYS   A NZ  1 
ATOM   2509 N  N   . LYS   A 1 317 ? -12.558 23.068  35.921 1.00 134.22 ? 613 LYS   A N   1 
ATOM   2510 C  CA  . LYS   A 1 317 ? -13.326 24.152  35.316 1.00 136.68 ? 613 LYS   A CA  1 
ATOM   2511 C  C   . LYS   A 1 317 ? -14.640 24.419  36.033 1.00 135.89 ? 613 LYS   A C   1 
ATOM   2512 O  O   . LYS   A 1 317 ? -15.262 25.457  35.787 1.00 140.57 ? 613 LYS   A O   1 
ATOM   2513 C  CB  . LYS   A 1 317 ? -13.618 23.842  33.845 1.00 133.78 ? 613 LYS   A CB  1 
ATOM   2514 C  CG  . LYS   A 1 317 ? -12.606 24.382  32.876 1.00 138.64 ? 613 LYS   A CG  1 
ATOM   2515 C  CD  . LYS   A 1 317 ? -11.516 23.378  32.589 1.00 142.52 ? 613 LYS   A CD  1 
ATOM   2516 C  CE  . LYS   A 1 317 ? -10.708 23.840  31.380 1.00 142.55 ? 613 LYS   A CE  1 
ATOM   2517 N  NZ  . LYS   A 1 317 ? -9.778  22.797  30.864 1.00 149.44 ? 613 LYS   A NZ  1 
ATOM   2518 N  N   . MET   A 1 318 ? -15.099 23.495  36.875 1.00 131.21 ? 614 MET   A N   1 
ATOM   2519 C  CA  . MET   A 1 318 ? -16.235 23.774  37.742 1.00 134.12 ? 614 MET   A CA  1 
ATOM   2520 C  C   . MET   A 1 318 ? -15.828 24.515  39.004 1.00 137.54 ? 614 MET   A C   1 
ATOM   2521 O  O   . MET   A 1 318 ? -16.709 24.987  39.731 1.00 142.39 ? 614 MET   A O   1 
ATOM   2522 C  CB  . MET   A 1 318 ? -16.954 22.475  38.118 1.00 127.60 ? 614 MET   A CB  1 
ATOM   2523 C  CG  . MET   A 1 318 ? -17.648 21.809  36.941 1.00 129.15 ? 614 MET   A CG  1 
ATOM   2524 S  SD  . MET   A 1 318 ? -18.621 20.365  37.411 1.00 121.43 ? 614 MET   A SD  1 
ATOM   2525 C  CE  . MET   A 1 318 ? -19.717 21.089  38.640 1.00 112.49 ? 614 MET   A CE  1 
ATOM   2526 N  N   . ASP   A 1 319 ? -14.522 24.639  39.259 1.00 143.05 ? 615 ASP   A N   1 
ATOM   2527 C  CA  . ASP   A 1 319 ? -13.961 25.171  40.500 1.00 152.34 ? 615 ASP   A CA  1 
ATOM   2528 C  C   . ASP   A 1 319 ? -14.502 24.406  41.705 1.00 148.46 ? 615 ASP   A C   1 
ATOM   2529 O  O   . ASP   A 1 319 ? -15.368 24.903  42.433 1.00 150.12 ? 615 ASP   A O   1 
ATOM   2530 C  CB  . ASP   A 1 319 ? -14.237 26.673  40.628 1.00 163.65 ? 615 ASP   A CB  1 
ATOM   2531 C  CG  . ASP   A 1 319 ? -13.150 27.401  41.407 1.00 172.38 ? 615 ASP   A CG  1 
ATOM   2532 O  OD1 . ASP   A 1 319 ? -11.967 27.310  41.012 1.00 174.11 ? 615 ASP   A OD1 1 
ATOM   2533 O  OD2 . ASP   A 1 319 ? -13.481 28.078  42.402 1.00 178.02 ? 615 ASP   A OD2 1 
ATOM   2534 N  N   . LEU   A 1 320 ? -13.982 23.198  41.922 1.00 144.13 ? 616 LEU   A N   1 
ATOM   2535 C  CA  . LEU   A 1 320 ? -14.493 22.272  42.921 1.00 137.24 ? 616 LEU   A CA  1 
ATOM   2536 C  C   . LEU   A 1 320 ? -13.480 22.053  44.030 1.00 136.24 ? 616 LEU   A C   1 
ATOM   2537 O  O   . LEU   A 1 320 ? -12.271 22.204  43.830 1.00 139.65 ? 616 LEU   A O   1 
ATOM   2538 C  CB  . LEU   A 1 320 ? -14.832 20.915  42.307 1.00 129.13 ? 616 LEU   A CB  1 
ATOM   2539 C  CG  . LEU   A 1 320 ? -16.061 20.886  41.416 1.00 128.49 ? 616 LEU   A CG  1 
ATOM   2540 C  CD1 . LEU   A 1 320 ? -16.360 19.452  41.006 1.00 120.30 ? 616 LEU   A CD1 1 
ATOM   2541 C  CD2 . LEU   A 1 320 ? -17.236 21.498  42.146 1.00 126.07 ? 616 LEU   A CD2 1 
ATOM   2542 N  N   . ASP   A 1 321 ? -13.996 21.671  45.198 1.00 134.12 ? 617 ASP   A N   1 
ATOM   2543 C  CA  . ASP   A 1 321 ? -13.156 21.260  46.313 1.00 137.09 ? 617 ASP   A CA  1 
ATOM   2544 C  C   . ASP   A 1 321 ? -12.491 19.940  45.949 1.00 131.32 ? 617 ASP   A C   1 
ATOM   2545 O  O   . ASP   A 1 321 ? -13.049 18.869  46.197 1.00 126.06 ? 617 ASP   A O   1 
ATOM   2546 C  CB  . ASP   A 1 321 ? -13.988 21.141  47.595 1.00 134.63 ? 617 ASP   A CB  1 
ATOM   2547 C  CG  . ASP   A 1 321 ? -13.132 21.042  48.840 1.00 141.88 ? 617 ASP   A CG  1 
ATOM   2548 O  OD1 . ASP   A 1 321 ? -11.890 21.066  48.713 1.00 149.68 ? 617 ASP   A OD1 1 
ATOM   2549 O  OD2 . ASP   A 1 321 ? -13.700 20.947  49.951 1.00 138.88 ? 617 ASP   A OD2 1 
ATOM   2550 N  N   . MET   A 1 322 ? -11.304 20.010  45.347 1.00 133.38 ? 618 MET   A N   1 
ATOM   2551 C  CA  . MET   A 1 322 ? -10.648 18.842  44.776 1.00 132.93 ? 618 MET   A CA  1 
ATOM   2552 C  C   . MET   A 1 322 ? -9.634  18.197  45.717 1.00 140.90 ? 618 MET   A C   1 
ATOM   2553 O  O   . MET   A 1 322 ? -9.167  17.089  45.435 1.00 141.65 ? 618 MET   A O   1 
ATOM   2554 C  CB  . MET   A 1 322 ? -9.969  19.232  43.451 1.00 133.84 ? 618 MET   A CB  1 
ATOM   2555 C  CG  . MET   A 1 322 ? -9.926  18.144  42.382 1.00 127.31 ? 618 MET   A CG  1 
ATOM   2556 S  SD  . MET   A 1 322 ? -10.226 18.781  40.712 1.00 132.81 ? 618 MET   A SD  1 
ATOM   2557 C  CE  . MET   A 1 322 ? -8.821  18.110  39.822 1.00 132.42 ? 618 MET   A CE  1 
ATOM   2558 N  N   . ARG   A 1 323 ? -9.294  18.848  46.830 1.00 152.62 ? 619 ARG   A N   1 
ATOM   2559 C  CA  . ARG   A 1 323 ? -8.329  18.270  47.760 1.00 155.12 ? 619 ARG   A CA  1 
ATOM   2560 C  C   . ARG   A 1 323 ? -8.925  17.099  48.532 1.00 152.21 ? 619 ARG   A C   1 
ATOM   2561 O  O   . ARG   A 1 323 ? -8.252  16.085  48.749 1.00 152.50 ? 619 ARG   A O   1 
ATOM   2562 C  CB  . ARG   A 1 323 ? -7.831  19.345  48.730 1.00 160.85 ? 619 ARG   A CB  1 
ATOM   2563 C  CG  . ARG   A 1 323 ? -7.178  20.533  48.051 1.00 169.54 ? 619 ARG   A CG  1 
ATOM   2564 C  CD  . ARG   A 1 323 ? -7.430  21.807  48.830 1.00 177.94 ? 619 ARG   A CD  1 
ATOM   2565 N  NE  . ARG   A 1 323 ? -8.856  22.040  49.027 1.00 177.33 ? 619 ARG   A NE  1 
ATOM   2566 C  CZ  . ARG   A 1 323 ? -9.364  23.093  49.654 1.00 183.97 ? 619 ARG   A CZ  1 
ATOM   2567 N  NH1 . ARG   A 1 323 ? -8.588  24.040  50.157 1.00 189.96 ? 619 ARG   A NH1 1 
ATOM   2568 N  NH2 . ARG   A 1 323 ? -10.685 23.200  49.777 1.00 180.98 ? 619 ARG   A NH2 1 
ATOM   2569 N  N   . LYS   A 1 324 ? -10.178 17.215  48.955 1.00 141.71 ? 620 LYS   A N   1 
ATOM   2570 C  CA  . LYS   A 1 324 ? -10.809 16.224  49.813 1.00 131.03 ? 620 LYS   A CA  1 
ATOM   2571 C  C   . LYS   A 1 324 ? -11.606 15.240  48.969 1.00 119.84 ? 620 LYS   A C   1 
ATOM   2572 O  O   . LYS   A 1 324 ? -12.301 15.634  48.024 1.00 118.90 ? 620 LYS   A O   1 
ATOM   2573 C  CB  . LYS   A 1 324 ? -11.722 16.897  50.846 1.00 132.91 ? 620 LYS   A CB  1 
ATOM   2574 C  CG  . LYS   A 1 324 ? -11.006 17.517  52.035 1.00 144.83 ? 620 LYS   A CG  1 
ATOM   2575 C  CD  . LYS   A 1 324 ? -10.308 18.831  51.705 1.00 153.60 ? 620 LYS   A CD  1 
ATOM   2576 C  CE  . LYS   A 1 324 ? -9.561  19.370  52.926 1.00 153.72 ? 620 LYS   A CE  1 
ATOM   2577 N  NZ  . LYS   A 1 324 ? -8.910  20.684  52.663 1.00 160.88 ? 620 LYS   A NZ  1 
ATOM   2578 N  N   . THR   A 1 325 ? -11.480 13.950  49.294 1.00 114.86 ? 621 THR   A N   1 
ATOM   2579 C  CA  . THR   A 1 325 ? -12.245 12.936  48.574 1.00 103.52 ? 621 THR   A CA  1 
ATOM   2580 C  C   . THR   A 1 325 ? -13.737 13.048  48.873 1.00 103.17 ? 621 THR   A C   1 
ATOM   2581 O  O   . THR   A 1 325 ? -14.575 12.744  48.017 1.00 91.54  ? 621 THR   A O   1 
ATOM   2582 C  CB  . THR   A 1 325 ? -11.729 11.532  48.927 1.00 98.47  ? 621 THR   A CB  1 
ATOM   2583 O  OG1 . THR   A 1 325 ? -12.623 10.539  48.410 1.00 100.58 ? 621 THR   A OG1 1 
ATOM   2584 C  CG2 . THR   A 1 325 ? -11.598 11.340  50.441 1.00 108.10 ? 621 THR   A CG2 1 
ATOM   2585 N  N   . SER   A 1 326 ? -14.076 13.514  50.073 1.00 103.78 ? 622 SER   A N   1 
ATOM   2586 C  CA  . SER   A 1 326 ? -15.430 13.533  50.608 1.00 99.56  ? 622 SER   A CA  1 
ATOM   2587 C  C   . SER   A 1 326 ? -16.227 14.751  50.170 1.00 98.63  ? 622 SER   A C   1 
ATOM   2588 O  O   . SER   A 1 326 ? -17.423 14.825  50.466 1.00 97.17  ? 622 SER   A O   1 
ATOM   2589 C  CB  . SER   A 1 326 ? -15.355 13.485  52.136 1.00 98.10  ? 622 SER   A CB  1 
ATOM   2590 O  OG  . SER   A 1 326 ? -14.007 13.649  52.517 1.00 100.35 ? 622 SER   A OG  1 
ATOM   2591 N  N   . SER   A 1 327 ? -15.598 15.715  49.497 1.00 102.30 ? 623 SER   A N   1 
ATOM   2592 C  CA  . SER   A 1 327 ? -16.363 16.772  48.849 1.00 104.91 ? 623 SER   A CA  1 
ATOM   2593 C  C   . SER   A 1 327 ? -17.252 16.242  47.731 1.00 100.24 ? 623 SER   A C   1 
ATOM   2594 O  O   . SER   A 1 327 ? -18.098 16.989  47.228 1.00 101.89 ? 623 SER   A O   1 
ATOM   2595 C  CB  . SER   A 1 327 ? -15.418 17.840  48.290 1.00 110.50 ? 623 SER   A CB  1 
ATOM   2596 O  OG  . SER   A 1 327 ? -14.796 17.389  47.094 1.00 111.03 ? 623 SER   A OG  1 
ATOM   2597 N  N   . LEU   A 1 328 ? -17.074 14.986  47.321 1.00 98.95  ? 624 LEU   A N   1 
ATOM   2598 C  CA  . LEU   A 1 328 ? -17.838 14.395  46.221 1.00 95.26  ? 624 LEU   A CA  1 
ATOM   2599 C  C   . LEU   A 1 328 ? -17.698 15.233  44.952 1.00 96.29  ? 624 LEU   A C   1 
ATOM   2600 O  O   . LEU   A 1 328 ? -18.638 15.378  44.169 1.00 97.68  ? 624 LEU   A O   1 
ATOM   2601 C  CB  . LEU   A 1 328 ? -19.312 14.204  46.601 1.00 92.64  ? 624 LEU   A CB  1 
ATOM   2602 C  CG  . LEU   A 1 328 ? -19.584 13.391  47.882 1.00 92.53  ? 624 LEU   A CG  1 
ATOM   2603 C  CD1 . LEU   A 1 328 ? -21.007 12.817  47.882 1.00 86.67  ? 624 LEU   A CD1 1 
ATOM   2604 C  CD2 . LEU   A 1 328 ? -18.581 12.272  47.978 1.00 91.65  ? 624 LEU   A CD2 1 
ATOM   2605 N  N   . TRP   A 1 329 ? -16.504 15.797  44.752 1.00 97.74  ? 625 TRP   A N   1 
ATOM   2606 C  CA  . TRP   A 1 329 ? -16.261 16.563  43.541 1.00 102.09 ? 625 TRP   A CA  1 
ATOM   2607 C  C   . TRP   A 1 329 ? -16.322 15.673  42.314 1.00 100.08 ? 625 TRP   A C   1 
ATOM   2608 O  O   . TRP   A 1 329 ? -16.775 16.121  41.259 1.00 100.82 ? 625 TRP   A O   1 
ATOM   2609 C  CB  . TRP   A 1 329 ? -14.915 17.283  43.610 1.00 104.51 ? 625 TRP   A CB  1 
ATOM   2610 C  CG  . TRP   A 1 329 ? -13.730 16.377  43.697 1.00 107.90 ? 625 TRP   A CG  1 
ATOM   2611 C  CD1 . TRP   A 1 329 ? -13.103 15.966  44.834 1.00 111.10 ? 625 TRP   A CD1 1 
ATOM   2612 C  CD2 . TRP   A 1 329 ? -13.025 15.763  42.608 1.00 107.18 ? 625 TRP   A CD2 1 
ATOM   2613 N  NE1 . TRP   A 1 329 ? -12.049 15.145  44.527 1.00 108.99 ? 625 TRP   A NE1 1 
ATOM   2614 C  CE2 . TRP   A 1 329 ? -11.982 14.998  43.166 1.00 107.83 ? 625 TRP   A CE2 1 
ATOM   2615 C  CE3 . TRP   A 1 329 ? -13.175 15.783  41.216 1.00 104.71 ? 625 TRP   A CE3 1 
ATOM   2616 C  CZ2 . TRP   A 1 329 ? -11.092 14.260  42.384 1.00 103.05 ? 625 TRP   A CZ2 1 
ATOM   2617 C  CZ3 . TRP   A 1 329 ? -12.286 15.051  40.438 1.00 103.06 ? 625 TRP   A CZ3 1 
ATOM   2618 C  CH2 . TRP   A 1 329 ? -11.257 14.304  41.023 1.00 105.59 ? 625 TRP   A CH2 1 
ATOM   2619 N  N   . LYS   A 1 330 ? -15.878 14.414  42.432 1.00 95.58  ? 626 LYS   A N   1 
ATOM   2620 C  CA  . LYS   A 1 330 ? -16.015 13.470  41.324 1.00 93.43  ? 626 LYS   A CA  1 
ATOM   2621 C  C   . LYS   A 1 330 ? -17.477 13.259  40.955 1.00 91.54  ? 626 LYS   A C   1 
ATOM   2622 O  O   . LYS   A 1 330 ? -17.835 13.258  39.769 1.00 91.21  ? 626 LYS   A O   1 
ATOM   2623 C  CB  . LYS   A 1 330 ? -15.363 12.129  41.678 1.00 93.22  ? 626 LYS   A CB  1 
ATOM   2624 C  CG  . LYS   A 1 330 ? -13.839 12.119  41.721 1.00 92.89  ? 626 LYS   A CG  1 
ATOM   2625 C  CD  . LYS   A 1 330 ? -13.279 10.699  41.530 1.00 89.02  ? 626 LYS   A CD  1 
ATOM   2626 C  CE  . LYS   A 1 330 ? -11.757 10.684  41.616 1.00 91.90  ? 626 LYS   A CE  1 
ATOM   2627 N  NZ  . LYS   A 1 330 ? -11.196 9.328   41.868 1.00 88.90  ? 626 LYS   A NZ  1 
ATOM   2628 N  N   . ASP   A 1 331 ? -18.324 13.049  41.960 1.00 91.29  ? 627 ASP   A N   1 
ATOM   2629 C  CA  . ASP   A 1 331 ? -19.744 12.801  41.741 1.00 89.30  ? 627 ASP   A CA  1 
ATOM   2630 C  C   . ASP   A 1 331 ? -20.411 13.981  41.063 1.00 92.27  ? 627 ASP   A C   1 
ATOM   2631 O  O   . ASP   A 1 331 ? -21.092 13.826  40.038 1.00 93.54  ? 627 ASP   A O   1 
ATOM   2632 C  CB  . ASP   A 1 331 ? -20.419 12.526  43.081 1.00 89.54  ? 627 ASP   A CB  1 
ATOM   2633 C  CG  . ASP   A 1 331 ? -19.790 11.369  43.809 1.00 86.10  ? 627 ASP   A CG  1 
ATOM   2634 O  OD1 . ASP   A 1 331 ? -18.703 11.534  44.394 1.00 81.45  ? 627 ASP   A OD1 1 
ATOM   2635 O  OD2 . ASP   A 1 331 ? -20.374 10.280  43.743 1.00 82.18  ? 627 ASP   A OD2 1 
ATOM   2636 N  N   . GLN   A 1 332 ? -20.242 15.166  41.645 1.00 91.42  ? 628 GLN   A N   1 
ATOM   2637 C  CA  . GLN   A 1 332 ? -20.837 16.381  41.106 1.00 97.45  ? 628 GLN   A CA  1 
ATOM   2638 C  C   . GLN   A 1 332 ? -20.412 16.614  39.662 1.00 96.79  ? 628 GLN   A C   1 
ATOM   2639 O  O   . GLN   A 1 332 ? -21.248 16.908  38.796 1.00 95.24  ? 628 GLN   A O   1 
ATOM   2640 C  CB  . GLN   A 1 332 ? -20.441 17.558  41.990 1.00 101.90 ? 628 GLN   A CB  1 
ATOM   2641 C  CG  . GLN   A 1 332 ? -21.481 18.629  42.088 1.00 106.66 ? 628 GLN   A CG  1 
ATOM   2642 C  CD  . GLN   A 1 332 ? -21.403 19.362  43.417 1.00 110.99 ? 628 GLN   A CD  1 
ATOM   2643 O  OE1 . GLN   A 1 332 ? -20.364 19.372  44.087 1.00 111.61 ? 628 GLN   A OE1 1 
ATOM   2644 N  NE2 . GLN   A 1 332 ? -22.508 19.974  43.806 1.00 109.42 ? 628 GLN   A NE2 1 
ATOM   2645 N  N   . ALA   A 1 333 ? -19.112 16.481  39.378 1.00 98.03  ? 629 ALA   A N   1 
ATOM   2646 C  CA  . ALA   A 1 333 ? -18.644 16.644  38.003 1.00 95.65  ? 629 ALA   A CA  1 
ATOM   2647 C  C   . ALA   A 1 333 ? -19.208 15.568  37.087 1.00 96.10  ? 629 ALA   A C   1 
ATOM   2648 O  O   . ALA   A 1 333 ? -19.386 15.803  35.877 1.00 87.91  ? 629 ALA   A O   1 
ATOM   2649 C  CB  . ALA   A 1 333 ? -17.116 16.625  37.950 1.00 99.28  ? 629 ALA   A CB  1 
ATOM   2650 N  N   . LEU   A 1 334 ? -19.501 14.385  37.632 1.00 91.55  ? 630 LEU   A N   1 
ATOM   2651 C  CA  . LEU   A 1 334 ? -19.970 13.300  36.772 1.00 87.36  ? 630 LEU   A CA  1 
ATOM   2652 C  C   . LEU   A 1 334 ? -21.418 13.490  36.348 1.00 91.86  ? 630 LEU   A C   1 
ATOM   2653 O  O   . LEU   A 1 334 ? -21.801 13.061  35.250 1.00 87.79  ? 630 LEU   A O   1 
ATOM   2654 C  CB  . LEU   A 1 334 ? -19.821 11.958  37.484 1.00 86.77  ? 630 LEU   A CB  1 
ATOM   2655 C  CG  . LEU   A 1 334 ? -20.378 10.719  36.814 1.00 82.16  ? 630 LEU   A CG  1 
ATOM   2656 C  CD1 . LEU   A 1 334 ? -19.244 10.041  36.095 1.00 80.34  ? 630 LEU   A CD1 1 
ATOM   2657 C  CD2 . LEU   A 1 334 ? -20.996 9.799   37.867 1.00 82.36  ? 630 LEU   A CD2 1 
ATOM   2658 N  N   . VAL   A 1 335 ? -22.235 14.118  37.197 1.00 85.67  ? 631 VAL   A N   1 
ATOM   2659 C  CA  . VAL   A 1 335 ? -23.611 14.426  36.816 1.00 90.49  ? 631 VAL   A CA  1 
ATOM   2660 C  C   . VAL   A 1 335 ? -23.632 15.435  35.670 1.00 94.31  ? 631 VAL   A C   1 
ATOM   2661 O  O   . VAL   A 1 335 ? -24.290 15.220  34.642 1.00 90.38  ? 631 VAL   A O   1 
ATOM   2662 C  CB  . VAL   A 1 335 ? -24.412 14.934  38.026 1.00 93.47  ? 631 VAL   A CB  1 
ATOM   2663 C  CG1 . VAL   A 1 335 ? -25.699 15.572  37.547 1.00 95.73  ? 631 VAL   A CG1 1 
ATOM   2664 C  CG2 . VAL   A 1 335 ? -24.700 13.774  38.997 1.00 95.44  ? 631 VAL   A CG2 1 
ATOM   2665 N  N   . GLU   A 1 336 ? -22.886 16.535  35.817 1.00 92.65  ? 632 GLU   A N   1 
ATOM   2666 C  CA  . GLU   A 1 336 ? -22.814 17.541  34.748 1.00 97.98  ? 632 GLU   A CA  1 
ATOM   2667 C  C   . GLU   A 1 336 ? -22.393 16.930  33.421 1.00 95.53  ? 632 GLU   A C   1 
ATOM   2668 O  O   . GLU   A 1 336 ? -22.917 17.305  32.363 1.00 92.85  ? 632 GLU   A O   1 
ATOM   2669 C  CB  . GLU   A 1 336 ? -21.833 18.651  35.118 1.00 104.22 ? 632 GLU   A CB  1 
ATOM   2670 C  CG  . GLU   A 1 336 ? -22.086 19.231  36.454 1.00 106.37 ? 632 GLU   A CG  1 
ATOM   2671 C  CD  . GLU   A 1 336 ? -23.371 20.015  36.499 1.00 115.21 ? 632 GLU   A CD  1 
ATOM   2672 O  OE1 . GLU   A 1 336 ? -23.848 20.448  35.416 1.00 112.28 ? 632 GLU   A OE1 1 
ATOM   2673 O  OE2 . GLU   A 1 336 ? -23.893 20.198  37.624 1.00 114.91 ? 632 GLU   A OE2 1 
ATOM   2674 N  N   . ILE   A 1 337 ? -21.439 15.995  33.457 1.00 93.63  ? 633 ILE   A N   1 
ATOM   2675 C  CA  . ILE   A 1 337 ? -20.944 15.385  32.222 1.00 91.98  ? 633 ILE   A CA  1 
ATOM   2676 C  C   . ILE   A 1 337 ? -22.061 14.645  31.501 1.00 90.21  ? 633 ILE   A C   1 
ATOM   2677 O  O   . ILE   A 1 337 ? -22.165 14.702  30.271 1.00 91.96  ? 633 ILE   A O   1 
ATOM   2678 C  CB  . ILE   A 1 337 ? -19.738 14.468  32.513 1.00 88.76  ? 633 ILE   A CB  1 
ATOM   2679 C  CG1 . ILE   A 1 337 ? -18.528 15.333  32.883 1.00 92.74  ? 633 ILE   A CG1 1 
ATOM   2680 C  CG2 . ILE   A 1 337 ? -19.414 13.605  31.305 1.00 87.09  ? 633 ILE   A CG2 1 
ATOM   2681 C  CD1 . ILE   A 1 337 ? -17.329 14.557  33.362 1.00 93.58  ? 633 ILE   A CD1 1 
ATOM   2682 N  N   . ASN   A 1 338 ? -22.924 13.951  32.245 1.00 89.38  ? 634 ASN   A N   1 
ATOM   2683 C  CA  . ASN   A 1 338 ? -23.981 13.185  31.591 1.00 88.74  ? 634 ASN   A CA  1 
ATOM   2684 C  C   . ASN   A 1 338 ? -25.209 14.029  31.263 1.00 92.01  ? 634 ASN   A C   1 
ATOM   2685 O  O   . ASN   A 1 338 ? -25.979 13.652  30.370 1.00 88.57  ? 634 ASN   A O   1 
ATOM   2686 C  CB  . ASN   A 1 338 ? -24.370 11.973  32.446 1.00 84.87  ? 634 ASN   A CB  1 
ATOM   2687 C  CG  . ASN   A 1 338 ? -23.229 10.980  32.587 1.00 80.56  ? 634 ASN   A CG  1 
ATOM   2688 O  OD1 . ASN   A 1 338 ? -23.235 9.912   31.987 1.00 73.94  ? 634 ASN   A OD1 1 
ATOM   2689 N  ND2 . ASN   A 1 338 ? -22.237 11.340  33.391 1.00 82.05  ? 634 ASN   A ND2 1 
ATOM   2690 N  N   . ILE   A 1 339 ? -25.403 15.169  31.938 1.00 91.89  ? 635 ILE   A N   1 
ATOM   2691 C  CA  . ILE   A 1 339 ? -26.387 16.139  31.460 1.00 93.33  ? 635 ILE   A CA  1 
ATOM   2692 C  C   . ILE   A 1 339 ? -25.956 16.698  30.110 1.00 96.05  ? 635 ILE   A C   1 
ATOM   2693 O  O   . ILE   A 1 339 ? -26.778 16.872  29.198 1.00 91.41  ? 635 ILE   A O   1 
ATOM   2694 C  CB  . ILE   A 1 339 ? -26.600 17.259  32.499 1.00 94.82  ? 635 ILE   A CB  1 
ATOM   2695 C  CG1 . ILE   A 1 339 ? -27.212 16.687  33.779 1.00 96.24  ? 635 ILE   A CG1 1 
ATOM   2696 C  CG2 . ILE   A 1 339 ? -27.495 18.361  31.927 1.00 96.85  ? 635 ILE   A CG2 1 
ATOM   2697 C  CD1 . ILE   A 1 339 ? -27.390 17.719  34.885 1.00 97.22  ? 635 ILE   A CD1 1 
ATOM   2698 N  N   . ALA   A 1 340 ? -24.651 16.944  29.950 1.00 96.44  ? 636 ALA   A N   1 
ATOM   2699 C  CA  . ALA   A 1 340 ? -24.124 17.488  28.703 1.00 96.90  ? 636 ALA   A CA  1 
ATOM   2700 C  C   . ALA   A 1 340 ? -24.233 16.494  27.551 1.00 96.96  ? 636 ALA   A C   1 
ATOM   2701 O  O   . ALA   A 1 340 ? -24.628 16.866  26.437 1.00 93.11  ? 636 ALA   A O   1 
ATOM   2702 C  CB  . ALA   A 1 340 ? -22.672 17.912  28.898 1.00 99.70  ? 636 ALA   A CB  1 
ATOM   2703 N  N   . VAL   A 1 341 ? -23.848 15.238  27.788 1.00 91.89  ? 637 VAL   A N   1 
ATOM   2704 C  CA  . VAL   A 1 341 ? -23.962 14.215  26.754 1.00 88.20  ? 637 VAL   A CA  1 
ATOM   2705 C  C   . VAL   A 1 341 ? -25.397 14.139  26.262 1.00 92.56  ? 637 VAL   A C   1 
ATOM   2706 O  O   . VAL   A 1 341 ? -25.673 14.278  25.062 1.00 93.04  ? 637 VAL   A O   1 
ATOM   2707 C  CB  . VAL   A 1 341 ? -23.479 12.853  27.282 1.00 88.90  ? 637 VAL   A CB  1 
ATOM   2708 C  CG1 . VAL   A 1 341 ? -23.749 11.758  26.265 1.00 81.85  ? 637 VAL   A CG1 1 
ATOM   2709 C  CG2 . VAL   A 1 341 ? -21.996 12.895  27.603 1.00 90.10  ? 637 VAL   A CG2 1 
ATOM   2710 N  N   . LEU   A 1 342 ? -26.335 13.956  27.192 1.00 89.56  ? 638 LEU   A N   1 
ATOM   2711 C  CA  . LEU   A 1 342 ? -27.746 13.888  26.837 1.00 90.79  ? 638 LEU   A CA  1 
ATOM   2712 C  C   . LEU   A 1 342 ? -28.183 15.117  26.049 1.00 97.02  ? 638 LEU   A C   1 
ATOM   2713 O  O   . LEU   A 1 342 ? -28.644 15.008  24.907 1.00 94.06  ? 638 LEU   A O   1 
ATOM   2714 C  CB  . LEU   A 1 342 ? -28.577 13.733  28.107 1.00 94.08  ? 638 LEU   A CB  1 
ATOM   2715 C  CG  . LEU   A 1 342 ? -28.422 12.395  28.821 1.00 86.83  ? 638 LEU   A CG  1 
ATOM   2716 C  CD1 . LEU   A 1 342 ? -29.398 12.322  29.953 1.00 86.69  ? 638 LEU   A CD1 1 
ATOM   2717 C  CD2 . LEU   A 1 342 ? -28.679 11.299  27.813 1.00 79.39  ? 638 LEU   A CD2 1 
ATOM   2718 N  N   . TYR   A 1 343 ? -28.024 16.303  26.654 1.00 93.58  ? 639 TYR   A N   1 
ATOM   2719 C  CA  . TYR   A 1 343 ? -28.493 17.535  26.033 1.00 102.22 ? 639 TYR   A CA  1 
ATOM   2720 C  C   . TYR   A 1 343 ? -27.940 17.683  24.624 1.00 100.82 ? 639 TYR   A C   1 
ATOM   2721 O  O   . TYR   A 1 343 ? -28.661 18.094  23.710 1.00 103.69 ? 639 TYR   A O   1 
ATOM   2722 C  CB  . TYR   A 1 343 ? -28.105 18.745  26.894 1.00 107.30 ? 639 TYR   A CB  1 
ATOM   2723 C  CG  . TYR   A 1 343 ? -28.325 20.101  26.211 1.00 110.79 ? 639 TYR   A CG  1 
ATOM   2724 C  CD1 . TYR   A 1 343 ? -29.558 20.737  26.272 1.00 111.98 ? 639 TYR   A CD1 1 
ATOM   2725 C  CD2 . TYR   A 1 343 ? -27.293 20.746  25.541 1.00 109.25 ? 639 TYR   A CD2 1 
ATOM   2726 C  CE1 . TYR   A 1 343 ? -29.767 21.954  25.680 1.00 114.16 ? 639 TYR   A CE1 1 
ATOM   2727 C  CE2 . TYR   A 1 343 ? -27.492 21.989  24.932 1.00 112.81 ? 639 TYR   A CE2 1 
ATOM   2728 C  CZ  . TYR   A 1 343 ? -28.736 22.583  25.006 1.00 114.29 ? 639 TYR   A CZ  1 
ATOM   2729 O  OH  . TYR   A 1 343 ? -28.965 23.809  24.422 1.00 122.88 ? 639 TYR   A OH  1 
ATOM   2730 N  N   . SER   A 1 344 ? -26.668 17.323  24.423 1.00 100.29 ? 640 SER   A N   1 
ATOM   2731 C  CA  . SER   A 1 344 ? -26.050 17.518  23.115 1.00 98.83  ? 640 SER   A CA  1 
ATOM   2732 C  C   . SER   A 1 344 ? -26.671 16.599  22.075 1.00 100.32 ? 640 SER   A C   1 
ATOM   2733 O  O   . SER   A 1 344 ? -27.051 17.055  20.993 1.00 95.58  ? 640 SER   A O   1 
ATOM   2734 C  CB  . SER   A 1 344 ? -24.540 17.292  23.204 1.00 100.35 ? 640 SER   A CB  1 
ATOM   2735 O  OG  . SER   A 1 344 ? -23.972 18.039  24.281 1.00 101.75 ? 640 SER   A OG  1 
ATOM   2736 N  N   . PHE   A 1 345 ? -26.799 15.307  22.396 1.00 93.40  ? 641 PHE   A N   1 
ATOM   2737 C  CA  . PHE   A 1 345 ? -27.428 14.361  21.475 1.00 90.54  ? 641 PHE   A CA  1 
ATOM   2738 C  C   . PHE   A 1 345 ? -28.850 14.795  21.117 1.00 96.84  ? 641 PHE   A C   1 
ATOM   2739 O  O   . PHE   A 1 345 ? -29.223 14.809  19.938 1.00 99.17  ? 641 PHE   A O   1 
ATOM   2740 C  CB  . PHE   A 1 345 ? -27.435 12.956  22.083 1.00 85.65  ? 641 PHE   A CB  1 
ATOM   2741 C  CG  . PHE   A 1 345 ? -26.209 12.115  21.762 1.00 80.33  ? 641 PHE   A CG  1 
ATOM   2742 C  CD1 . PHE   A 1 345 ? -24.942 12.500  22.182 1.00 80.11  ? 641 PHE   A CD1 1 
ATOM   2743 C  CD2 . PHE   A 1 345 ? -26.344 10.905  21.081 1.00 75.42  ? 641 PHE   A CD2 1 
ATOM   2744 C  CE1 . PHE   A 1 345 ? -23.829 11.716  21.904 1.00 76.66  ? 641 PHE   A CE1 1 
ATOM   2745 C  CE2 . PHE   A 1 345 ? -25.236 10.111  20.809 1.00 72.63  ? 641 PHE   A CE2 1 
ATOM   2746 C  CZ  . PHE   A 1 345 ? -23.975 10.525  21.214 1.00 71.16  ? 641 PHE   A CZ  1 
ATOM   2747 N  N   . GLN   A 1 346 ? -29.662 15.160  22.118 1.00 94.80  ? 642 GLN   A N   1 
ATOM   2748 C  CA  . GLN   A 1 346 ? -31.045 15.559  21.842 1.00 99.92  ? 642 GLN   A CA  1 
ATOM   2749 C  C   . GLN   A 1 346 ? -31.112 16.844  21.032 1.00 100.43 ? 642 GLN   A C   1 
ATOM   2750 O  O   . GLN   A 1 346 ? -31.926 16.954  20.108 1.00 104.95 ? 642 GLN   A O   1 
ATOM   2751 C  CB  . GLN   A 1 346 ? -31.832 15.757  23.131 1.00 99.43  ? 642 GLN   A CB  1 
ATOM   2752 C  CG  . GLN   A 1 346 ? -31.974 14.534  23.987 1.00 103.38 ? 642 GLN   A CG  1 
ATOM   2753 C  CD  . GLN   A 1 346 ? -32.181 14.917  25.426 1.00 105.12 ? 642 GLN   A CD  1 
ATOM   2754 O  OE1 . GLN   A 1 346 ? -31.262 15.410  26.078 1.00 103.19 ? 642 GLN   A OE1 1 
ATOM   2755 N  NE2 . GLN   A 1 346 ? -33.399 14.740  25.921 1.00 112.22 ? 642 GLN   A NE2 1 
ATOM   2756 N  N   . SER   A 1 347 ? -30.297 17.841  21.385 1.00 100.17 ? 643 SER   A N   1 
ATOM   2757 C  CA  . SER   A 1 347 ? -30.282 19.094  20.635 1.00 102.18 ? 643 SER   A CA  1 
ATOM   2758 C  C   . SER   A 1 347 ? -29.890 18.895  19.174 1.00 103.91 ? 643 SER   A C   1 
ATOM   2759 O  O   . SER   A 1 347 ? -30.020 19.833  18.374 1.00 106.33 ? 643 SER   A O   1 
ATOM   2760 C  CB  . SER   A 1 347 ? -29.336 20.098  21.311 1.00 103.50 ? 643 SER   A CB  1 
ATOM   2761 O  OG  . SER   A 1 347 ? -29.794 20.488  22.625 1.00 104.43 ? 643 SER   A OG  1 
ATOM   2762 N  N   . ASP   A 1 348 ? -29.433 17.698  18.797 1.00 103.06 ? 644 ASP   A N   1 
ATOM   2763 C  CA  . ASP   A 1 348 ? -29.084 17.396  17.412 1.00 105.16 ? 644 ASP   A CA  1 
ATOM   2764 C  C   . ASP   A 1 348 ? -30.023 16.375  16.770 1.00 103.71 ? 644 ASP   A C   1 
ATOM   2765 O  O   . ASP   A 1 348 ? -29.751 15.918  15.656 1.00 103.64 ? 644 ASP   A O   1 
ATOM   2766 C  CB  . ASP   A 1 348 ? -27.639 16.898  17.327 1.00 103.20 ? 644 ASP   A CB  1 
ATOM   2767 C  CG  . ASP   A 1 348 ? -26.621 17.989  17.615 1.00 100.66 ? 644 ASP   A CG  1 
ATOM   2768 O  OD1 . ASP   A 1 348 ? -27.005 19.184  17.673 1.00 102.08 ? 644 ASP   A OD1 1 
ATOM   2769 O  OD2 . ASP   A 1 348 ? -25.430 17.650  17.787 1.00 93.67  ? 644 ASP   A OD2 1 
ATOM   2770 N  N   . LYS   A 1 349 ? -31.114 16.005  17.453 1.00 110.99 ? 645 LYS   A N   1 
ATOM   2771 C  CA  . LYS   A 1 349 ? -32.038 14.955  17.003 1.00 109.00 ? 645 LYS   A CA  1 
ATOM   2772 C  C   . LYS   A 1 349 ? -31.315 13.619  16.828 1.00 101.73 ? 645 LYS   A C   1 
ATOM   2773 O  O   . LYS   A 1 349 ? -31.700 12.785  16.005 1.00 103.50 ? 645 LYS   A O   1 
ATOM   2774 C  CB  . LYS   A 1 349 ? -32.769 15.354  15.706 1.00 118.40 ? 645 LYS   A CB  1 
ATOM   2775 C  CG  . LYS   A 1 349 ? -34.072 14.570  15.379 1.00 123.95 ? 645 LYS   A CG  1 
ATOM   2776 C  CD  . LYS   A 1 349 ? -33.886 13.571  14.209 1.00 118.00 ? 645 LYS   A CD  1 
ATOM   2777 C  CE  . LYS   A 1 349 ? -35.184 12.879  13.797 1.00 120.59 ? 645 LYS   A CE  1 
ATOM   2778 N  NZ  . LYS   A 1 349 ? -35.961 13.658  12.781 1.00 128.49 ? 645 LYS   A NZ  1 
ATOM   2779 N  N   . VAL   A 1 350 ? -30.256 13.384  17.596 1.00 96.31  ? 646 VAL   A N   1 
ATOM   2780 C  CA  . VAL   A 1 350 ? -29.571 12.096  17.566 1.00 93.14  ? 646 VAL   A CA  1 
ATOM   2781 C  C   . VAL   A 1 350 ? -30.105 11.243  18.705 1.00 87.69  ? 646 VAL   A C   1 
ATOM   2782 O  O   . VAL   A 1 350 ? -30.069 11.653  19.880 1.00 88.78  ? 646 VAL   A O   1 
ATOM   2783 C  CB  . VAL   A 1 350 ? -28.047 12.260  17.674 1.00 90.61  ? 646 VAL   A CB  1 
ATOM   2784 C  CG1 . VAL   A 1 350 ? -27.367 10.881  17.592 1.00 78.95  ? 646 VAL   A CG1 1 
ATOM   2785 C  CG2 . VAL   A 1 350 ? -27.525 13.196  16.607 1.00 89.78  ? 646 VAL   A CG2 1 
ATOM   2786 N  N   . THR   A 1 351 ? -30.580 10.049  18.359 1.00 80.36  ? 647 THR   A N   1 
ATOM   2787 C  CA  . THR   A 1 351 ? -31.235 9.180   19.327 1.00 77.26  ? 647 THR   A CA  1 
ATOM   2788 C  C   . THR   A 1 351 ? -30.294 8.814   20.468 1.00 77.55  ? 647 THR   A C   1 
ATOM   2789 O  O   . THR   A 1 351 ? -29.181 8.315   20.256 1.00 75.88  ? 647 THR   A O   1 
ATOM   2790 C  CB  . THR   A 1 351 ? -31.746 7.911   18.641 1.00 75.57  ? 647 THR   A CB  1 
ATOM   2791 O  OG1 . THR   A 1 351 ? -32.561 8.278   17.527 1.00 82.35  ? 647 THR   A OG1 1 
ATOM   2792 C  CG2 . THR   A 1 351 ? -32.581 7.072   19.610 1.00 73.47  ? 647 THR   A CG2 1 
ATOM   2793 N  N   . ILE   A 1 352 ? -30.765 9.050   21.693 1.00 79.26  ? 648 ILE   A N   1 
ATOM   2794 C  CA  . ILE   A 1 352 ? -30.052 8.663   22.899 1.00 72.46  ? 648 ILE   A CA  1 
ATOM   2795 C  C   . ILE   A 1 352 ? -31.111 8.492   23.978 1.00 74.68  ? 648 ILE   A C   1 
ATOM   2796 O  O   . ILE   A 1 352 ? -32.225 9.009   23.865 1.00 73.58  ? 648 ILE   A O   1 
ATOM   2797 C  CB  . ILE   A 1 352 ? -28.989 9.720   23.286 1.00 73.07  ? 648 ILE   A CB  1 
ATOM   2798 C  CG1 . ILE   A 1 352 ? -27.963 9.142   24.274 1.00 72.15  ? 648 ILE   A CG1 1 
ATOM   2799 C  CG2 . ILE   A 1 352 ? -29.665 10.957  23.846 1.00 79.94  ? 648 ILE   A CG2 1 
ATOM   2800 C  CD1 . ILE   A 1 352 ? -26.805 10.083  24.585 1.00 75.81  ? 648 ILE   A CD1 1 
ATOM   2801 N  N   . VAL   A 1 353 ? -30.776 7.743   25.027 1.00 70.34  ? 649 VAL   A N   1 
ATOM   2802 C  CA  . VAL   A 1 353 ? -31.735 7.462   26.085 1.00 69.92  ? 649 VAL   A CA  1 
ATOM   2803 C  C   . VAL   A 1 353 ? -31.034 7.654   27.426 1.00 71.62  ? 649 VAL   A C   1 
ATOM   2804 O  O   . VAL   A 1 353 ? -29.863 7.290   27.588 1.00 70.16  ? 649 VAL   A O   1 
ATOM   2805 C  CB  . VAL   A 1 353 ? -32.338 6.045   25.911 1.00 70.74  ? 649 VAL   A CB  1 
ATOM   2806 C  CG1 . VAL   A 1 353 ? -31.248 4.966   25.895 1.00 67.93  ? 649 VAL   A CG1 1 
ATOM   2807 C  CG2 . VAL   A 1 353 ? -33.441 5.763   26.945 1.00 70.53  ? 649 VAL   A CG2 1 
ATOM   2808 N  N   . ASP   A 1 354 ? -31.729 8.285   28.367 1.00 73.71  ? 650 ASP   A N   1 
ATOM   2809 C  CA  . ASP   A 1 354 ? -31.126 8.556   29.650 1.00 75.99  ? 650 ASP   A CA  1 
ATOM   2810 C  C   . ASP   A 1 354 ? -31.226 7.293   30.492 1.00 72.96  ? 650 ASP   A C   1 
ATOM   2811 O  O   . ASP   A 1 354 ? -32.012 6.387   30.197 1.00 70.51  ? 650 ASP   A O   1 
ATOM   2812 C  CB  . ASP   A 1 354 ? -31.797 9.759   30.315 1.00 79.23  ? 650 ASP   A CB  1 
ATOM   2813 C  CG  . ASP   A 1 354 ? -33.199 9.462   30.799 1.00 81.76  ? 650 ASP   A CG  1 
ATOM   2814 O  OD1 . ASP   A 1 354 ? -33.327 8.607   31.685 1.00 80.20  ? 650 ASP   A OD1 1 
ATOM   2815 O  OD2 . ASP   A 1 354 ? -34.170 10.106  30.343 1.00 84.83  ? 650 ASP   A OD2 1 
ATOM   2816 N  N   . HIS   A 1 355 ? -30.390 7.204   31.522 1.00 74.21  ? 651 HIS   A N   1 
ATOM   2817 C  CA  . HIS   A 1 355 ? -30.374 5.955   32.271 1.00 67.63  ? 651 HIS   A CA  1 
ATOM   2818 C  C   . HIS   A 1 355 ? -31.676 5.721   33.033 1.00 73.46  ? 651 HIS   A C   1 
ATOM   2819 O  O   . HIS   A 1 355 ? -31.967 4.573   33.390 1.00 72.40  ? 651 HIS   A O   1 
ATOM   2820 C  CB  . HIS   A 1 355 ? -29.162 5.915   33.207 1.00 73.01  ? 651 HIS   A CB  1 
ATOM   2821 C  CG  . HIS   A 1 355 ? -28.951 7.165   34.009 1.00 70.08  ? 651 HIS   A CG  1 
ATOM   2822 N  ND1 . HIS   A 1 355 ? -28.426 8.318   33.464 1.00 70.25  ? 651 HIS   A ND1 1 
ATOM   2823 C  CD2 . HIS   A 1 355 ? -29.148 7.428   35.325 1.00 74.13  ? 651 HIS   A CD2 1 
ATOM   2824 C  CE1 . HIS   A 1 355 ? -28.319 9.241   34.407 1.00 76.08  ? 651 HIS   A CE1 1 
ATOM   2825 N  NE2 . HIS   A 1 355 ? -28.766 8.732   35.542 1.00 73.68  ? 651 HIS   A NE2 1 
ATOM   2826 N  N   . HIS   A 1 356 ? -32.461 6.776   33.289 1.00 73.93  ? 652 HIS   A N   1 
ATOM   2827 C  CA  . HIS   A 1 356 ? -33.753 6.630   33.956 1.00 73.15  ? 652 HIS   A CA  1 
ATOM   2828 C  C   . HIS   A 1 356 ? -34.808 6.090   33.008 1.00 75.00  ? 652 HIS   A C   1 
ATOM   2829 O  O   . HIS   A 1 356 ? -35.541 5.149   33.342 1.00 71.29  ? 652 HIS   A O   1 
ATOM   2830 C  CB  . HIS   A 1 356 ? -34.203 7.966   34.525 1.00 77.82  ? 652 HIS   A CB  1 
ATOM   2831 C  CG  . HIS   A 1 356 ? -33.196 8.585   35.432 1.00 80.24  ? 652 HIS   A CG  1 
ATOM   2832 N  ND1 . HIS   A 1 356 ? -32.958 8.109   36.701 1.00 76.95  ? 652 HIS   A ND1 1 
ATOM   2833 C  CD2 . HIS   A 1 356 ? -32.349 9.625   35.250 1.00 80.05  ? 652 HIS   A CD2 1 
ATOM   2834 C  CE1 . HIS   A 1 356 ? -32.011 8.833   37.265 1.00 79.66  ? 652 HIS   A CE1 1 
ATOM   2835 N  NE2 . HIS   A 1 356 ? -31.619 9.755   36.405 1.00 79.27  ? 652 HIS   A NE2 1 
ATOM   2836 N  N   . SER   A 1 357 ? -34.885 6.652   31.802 1.00 75.23  ? 653 SER   A N   1 
ATOM   2837 C  CA  . SER   A 1 357 ? -35.875 6.152   30.862 1.00 74.64  ? 653 SER   A CA  1 
ATOM   2838 C  C   . SER   A 1 357 ? -35.570 4.723   30.449 1.00 68.77  ? 653 SER   A C   1 
ATOM   2839 O  O   . SER   A 1 357 ? -36.483 3.899   30.347 1.00 70.84  ? 653 SER   A O   1 
ATOM   2840 C  CB  . SER   A 1 357 ? -35.973 7.047   29.636 1.00 75.52  ? 653 SER   A CB  1 
ATOM   2841 O  OG  . SER   A 1 357 ? -37.180 6.718   28.983 1.00 77.97  ? 653 SER   A OG  1 
ATOM   2842 N  N   . ALA   A 1 358 ? -34.295 4.402   30.216 1.00 69.19  ? 654 ALA   A N   1 
ATOM   2843 C  CA  . ALA   A 1 358 ? -33.952 3.058   29.758 1.00 68.05  ? 654 ALA   A CA  1 
ATOM   2844 C  C   . ALA   A 1 358 ? -34.249 2.018   30.832 1.00 68.65  ? 654 ALA   A C   1 
ATOM   2845 O  O   . ALA   A 1 358 ? -34.820 0.958   30.542 1.00 61.30  ? 654 ALA   A O   1 
ATOM   2846 C  CB  . ALA   A 1 358 ? -32.480 2.993   29.350 1.00 64.22  ? 654 ALA   A CB  1 
ATOM   2847 N  N   . THR   A 1 359 ? -33.867 2.296   32.082 1.00 65.66  ? 655 THR   A N   1 
ATOM   2848 C  CA  . THR   A 1 359 ? -34.109 1.294   33.111 1.00 64.34  ? 655 THR   A CA  1 
ATOM   2849 C  C   . THR   A 1 359 ? -35.596 1.131   33.380 1.00 66.26  ? 655 THR   A C   1 
ATOM   2850 O  O   . THR   A 1 359 ? -36.047 0.017   33.677 1.00 65.07  ? 655 THR   A O   1 
ATOM   2851 C  CB  . THR   A 1 359 ? -33.349 1.642   34.394 1.00 66.36  ? 655 THR   A CB  1 
ATOM   2852 O  OG1 . THR   A 1 359 ? -33.685 2.964   34.820 1.00 64.46  ? 655 THR   A OG1 1 
ATOM   2853 C  CG2 . THR   A 1 359 ? -31.863 1.562   34.135 1.00 64.51  ? 655 THR   A CG2 1 
ATOM   2854 N  N   . GLU   A 1 360 ? -36.380 2.208   33.260 1.00 68.04  ? 656 GLU   A N   1 
ATOM   2855 C  CA  . GLU   A 1 360 ? -37.822 2.041   33.416 1.00 71.86  ? 656 GLU   A CA  1 
ATOM   2856 C  C   . GLU   A 1 360 ? -38.387 1.161   32.310 1.00 71.61  ? 656 GLU   A C   1 
ATOM   2857 O  O   . GLU   A 1 360 ? -39.236 0.301   32.565 1.00 72.98  ? 656 GLU   A O   1 
ATOM   2858 C  CB  . GLU   A 1 360 ? -38.539 3.387   33.433 1.00 77.25  ? 656 GLU   A CB  1 
ATOM   2859 C  CG  . GLU   A 1 360 ? -40.000 3.252   33.870 1.00 86.53  ? 656 GLU   A CG  1 
ATOM   2860 C  CD  . GLU   A 1 360 ? -40.902 4.351   33.330 1.00 99.12  ? 656 GLU   A CD  1 
ATOM   2861 O  OE1 . GLU   A 1 360 ? -40.375 5.398   32.881 1.00 99.76  ? 656 GLU   A OE1 1 
ATOM   2862 O  OE2 . GLU   A 1 360 ? -42.143 4.160   33.349 1.00 104.83 ? 656 GLU   A OE2 1 
ATOM   2863 N  N   . SER   A 1 361 ? -37.920 1.351   31.075 1.00 70.59  ? 657 SER   A N   1 
ATOM   2864 C  CA  A SER   A 1 361 ? -38.415 0.527   29.980 0.47 70.34  ? 657 SER   A CA  1 
ATOM   2865 C  CA  B SER   A 1 361 ? -38.397 0.527   29.967 0.53 72.63  ? 657 SER   A CA  1 
ATOM   2866 C  C   . SER   A 1 361 ? -38.019 -0.930  30.169 1.00 71.61  ? 657 SER   A C   1 
ATOM   2867 O  O   . SER   A 1 361 ? -38.760 -1.834  29.756 1.00 71.87  ? 657 SER   A O   1 
ATOM   2868 C  CB  A SER   A 1 361 ? -37.899 1.062   28.641 0.47 72.02  ? 657 SER   A CB  1 
ATOM   2869 C  CB  B SER   A 1 361 ? -37.828 1.034   28.638 0.53 67.55  ? 657 SER   A CB  1 
ATOM   2870 O  OG  A SER   A 1 361 ? -38.262 2.419   28.464 0.47 68.32  ? 657 SER   A OG  1 
ATOM   2871 O  OG  B SER   A 1 361 ? -36.543 0.484   28.398 0.53 69.17  ? 657 SER   A OG  1 
ATOM   2872 N  N   . PHE   A 1 362 ? -36.866 -1.175  30.794 1.00 69.17  ? 658 PHE   A N   1 
ATOM   2873 C  CA  . PHE   A 1 362 ? -36.453 -2.547  31.038 1.00 68.12  ? 658 PHE   A CA  1 
ATOM   2874 C  C   . PHE   A 1 362 ? -37.353 -3.235  32.058 1.00 69.92  ? 658 PHE   A C   1 
ATOM   2875 O  O   . PHE   A 1 362 ? -37.683 -4.414  31.893 1.00 69.99  ? 658 PHE   A O   1 
ATOM   2876 C  CB  . PHE   A 1 362 ? -35.005 -2.605  31.500 1.00 64.55  ? 658 PHE   A CB  1 
ATOM   2877 C  CG  . PHE   A 1 362 ? -34.492 -3.994  31.613 1.00 61.94  ? 658 PHE   A CG  1 
ATOM   2878 C  CD1 . PHE   A 1 362 ? -34.276 -4.754  30.471 1.00 61.77  ? 658 PHE   A CD1 1 
ATOM   2879 C  CD2 . PHE   A 1 362 ? -34.274 -4.564  32.855 1.00 63.97  ? 658 PHE   A CD2 1 
ATOM   2880 C  CE1 . PHE   A 1 362 ? -33.815 -6.045  30.567 1.00 60.50  ? 658 PHE   A CE1 1 
ATOM   2881 C  CE2 . PHE   A 1 362 ? -33.814 -5.866  32.963 1.00 63.00  ? 658 PHE   A CE2 1 
ATOM   2882 C  CZ  . PHE   A 1 362 ? -33.584 -6.602  31.824 1.00 61.43  ? 658 PHE   A CZ  1 
ATOM   2883 N  N   . ILE   A 1 363 ? -37.747 -2.536  33.133 1.00 70.94  ? 659 ILE   A N   1 
ATOM   2884 C  CA  . ILE   A 1 363 ? -38.735 -3.120  34.038 1.00 70.30  ? 659 ILE   A CA  1 
ATOM   2885 C  C   . ILE   A 1 363 ? -40.019 -3.415  33.272 1.00 75.09  ? 659 ILE   A C   1 
ATOM   2886 O  O   . ILE   A 1 363 ? -40.623 -4.484  33.423 1.00 76.97  ? 659 ILE   A O   1 
ATOM   2887 C  CB  . ILE   A 1 363 ? -38.992 -2.203  35.257 1.00 75.10  ? 659 ILE   A CB  1 
ATOM   2888 C  CG1 . ILE   A 1 363 ? -37.709 -1.952  36.059 1.00 67.57  ? 659 ILE   A CG1 1 
ATOM   2889 C  CG2 . ILE   A 1 363 ? -40.045 -2.809  36.180 1.00 76.47  ? 659 ILE   A CG2 1 
ATOM   2890 C  CD1 . ILE   A 1 363 ? -37.348 -3.052  37.034 1.00 68.34  ? 659 ILE   A CD1 1 
ATOM   2891 N  N   . LYS   A 1 364 ? -40.432 -2.491  32.401 1.00 76.27  ? 660 LYS   A N   1 
ATOM   2892 C  CA  . LYS   A 1 364 ? -41.594 -2.748  31.551 1.00 77.29  ? 660 LYS   A CA  1 
ATOM   2893 C  C   . LYS   A 1 364 ? -41.350 -3.940  30.641 1.00 76.25  ? 660 LYS   A C   1 
ATOM   2894 O  O   . LYS   A 1 364 ? -42.239 -4.785  30.465 1.00 79.45  ? 660 LYS   A O   1 
ATOM   2895 C  CB  . LYS   A 1 364 ? -41.940 -1.508  30.731 1.00 76.75  ? 660 LYS   A CB  1 
ATOM   2896 C  CG  . LYS   A 1 364 ? -43.417 -1.389  30.374 1.00 85.02  ? 660 LYS   A CG  1 
ATOM   2897 C  CD  . LYS   A 1 364 ? -43.972 -0.042  30.829 1.00 96.51  ? 660 LYS   A CD  1 
ATOM   2898 C  CE  . LYS   A 1 364 ? -44.984 0.537   29.843 1.00 99.38  ? 660 LYS   A CE  1 
ATOM   2899 N  NZ  . LYS   A 1 364 ? -44.376 0.908   28.525 1.00 100.43 ? 660 LYS   A NZ  1 
ATOM   2900 N  N   . HIS   A 1 365 ? -40.144 -4.032  30.063 1.00 77.35  ? 661 HIS   A N   1 
ATOM   2901 C  CA  . HIS   A 1 365 ? -39.783 -5.202  29.267 1.00 73.52  ? 661 HIS   A CA  1 
ATOM   2902 C  C   . HIS   A 1 365 ? -39.838 -6.482  30.091 1.00 77.29  ? 661 HIS   A C   1 
ATOM   2903 O  O   . HIS   A 1 365 ? -40.358 -7.508  29.629 1.00 74.75  ? 661 HIS   A O   1 
ATOM   2904 C  CB  . HIS   A 1 365 ? -38.386 -5.048  28.674 1.00 72.35  ? 661 HIS   A CB  1 
ATOM   2905 C  CG  . HIS   A 1 365 ? -37.955 -6.233  27.855 1.00 70.86  ? 661 HIS   A CG  1 
ATOM   2906 N  ND1 . HIS   A 1 365 ? -36.726 -6.841  28.004 1.00 69.47  ? 661 HIS   A ND1 1 
ATOM   2907 C  CD2 . HIS   A 1 365 ? -38.601 -6.932  26.893 1.00 69.94  ? 661 HIS   A CD2 1 
ATOM   2908 C  CE1 . HIS   A 1 365 ? -36.628 -7.856  27.163 1.00 67.50  ? 661 HIS   A CE1 1 
ATOM   2909 N  NE2 . HIS   A 1 365 ? -37.754 -7.934  26.480 1.00 71.73  ? 661 HIS   A NE2 1 
ATOM   2910 N  N   . MET   A 1 366 ? -39.275 -6.451  31.306 1.00 74.56  ? 662 MET   A N   1 
ATOM   2911 C  CA  . MET   A 1 366 ? -39.312 -7.631  32.166 1.00 75.33  ? 662 MET   A CA  1 
ATOM   2912 C  C   . MET   A 1 366 ? -40.744 -8.087  32.404 1.00 77.80  ? 662 MET   A C   1 
ATOM   2913 O  O   . MET   A 1 366 ? -41.034 -9.286  32.345 1.00 77.88  ? 662 MET   A O   1 
ATOM   2914 C  CB  . MET   A 1 366 ? -38.600 -7.354  33.496 1.00 70.88  ? 662 MET   A CB  1 
ATOM   2915 C  CG  . MET   A 1 366 ? -37.089 -7.605  33.496 1.00 65.64  ? 662 MET   A CG  1 
ATOM   2916 S  SD  . MET   A 1 366 ? -36.401 -7.238  35.149 1.00 65.73  ? 662 MET   A SD  1 
ATOM   2917 C  CE  . MET   A 1 366 ? -36.267 -8.879  35.886 1.00 64.25  ? 662 MET   A CE  1 
ATOM   2918 N  N   . GLU   A 1 367 ? -41.655 -7.146  32.655 1.00 73.35  ? 663 GLU   A N   1 
ATOM   2919 C  CA  . GLU   A 1 367 ? -43.054 -7.511  32.864 1.00 81.94  ? 663 GLU   A CA  1 
ATOM   2920 C  C   . GLU   A 1 367 ? -43.608 -8.261  31.661 1.00 83.07  ? 663 GLU   A C   1 
ATOM   2921 O  O   . GLU   A 1 367 ? -44.305 -9.272  31.803 1.00 87.93  ? 663 GLU   A O   1 
ATOM   2922 C  CB  . GLU   A 1 367 ? -43.897 -6.263  33.131 1.00 84.09  ? 663 GLU   A CB  1 
ATOM   2923 C  CG  . GLU   A 1 367 ? -43.609 -5.554  34.436 1.00 87.44  ? 663 GLU   A CG  1 
ATOM   2924 C  CD  . GLU   A 1 367 ? -44.443 -4.295  34.585 1.00 91.34  ? 663 GLU   A CD  1 
ATOM   2925 O  OE1 . GLU   A 1 367 ? -45.321 -4.041  33.721 1.00 93.82  ? 663 GLU   A OE1 1 
ATOM   2926 O  OE2 . GLU   A 1 367 ? -44.209 -3.556  35.563 1.00 89.82  ? 663 GLU   A OE2 1 
ATOM   2927 N  N   . ASN   A 1 368 ? -43.304 -7.776  30.461 1.00 83.07  ? 664 ASN   A N   1 
ATOM   2928 C  CA  . ASN   A 1 368 ? -43.812 -8.430  29.263 1.00 87.59  ? 664 ASN   A CA  1 
ATOM   2929 C  C   . ASN   A 1 368 ? -43.187 -9.809  29.080 1.00 89.04  ? 664 ASN   A C   1 
ATOM   2930 O  O   . ASN   A 1 368 ? -43.880 -10.773 28.736 1.00 93.87  ? 664 ASN   A O   1 
ATOM   2931 C  CB  . ASN   A 1 368 ? -43.559 -7.535  28.053 1.00 86.69  ? 664 ASN   A CB  1 
ATOM   2932 C  CG  . ASN   A 1 368 ? -44.221 -6.175  28.198 1.00 88.43  ? 664 ASN   A CG  1 
ATOM   2933 O  OD1 . ASN   A 1 368 ? -45.294 -6.058  28.800 1.00 94.54  ? 664 ASN   A OD1 1 
ATOM   2934 N  ND2 . ASN   A 1 368 ? -43.583 -5.139  27.662 1.00 81.65  ? 664 ASN   A ND2 1 
ATOM   2935 N  N   . GLU   A 1 369 ? -41.884 -9.932  29.337 1.00 85.31  ? 665 GLU   A N   1 
ATOM   2936 C  CA  . GLU   A 1 369 ? -41.234 -11.231 29.212 1.00 84.26  ? 665 GLU   A CA  1 
ATOM   2937 C  C   . GLU   A 1 369 ? -41.759 -12.228 30.241 1.00 87.82  ? 665 GLU   A C   1 
ATOM   2938 O  O   . GLU   A 1 369 ? -41.953 -13.404 29.922 1.00 88.67  ? 665 GLU   A O   1 
ATOM   2939 C  CB  . GLU   A 1 369 ? -39.723 -11.071 29.333 1.00 78.11  ? 665 GLU   A CB  1 
ATOM   2940 C  CG  . GLU   A 1 369 ? -39.102 -10.211 28.256 1.00 76.36  ? 665 GLU   A CG  1 
ATOM   2941 C  CD  . GLU   A 1 369 ? -38.634 -11.005 27.038 1.00 76.62  ? 665 GLU   A CD  1 
ATOM   2942 O  OE1 . GLU   A 1 369 ? -37.441 -11.408 27.014 1.00 77.78  ? 665 GLU   A OE1 1 
ATOM   2943 O  OE2 . GLU   A 1 369 ? -39.453 -11.220 26.118 1.00 69.39  ? 665 GLU   A OE2 1 
ATOM   2944 N  N   . TYR   A 1 370 ? -41.999 -11.789 31.481 1.00 85.67  ? 666 TYR   A N   1 
ATOM   2945 C  CA  . TYR   A 1 370 ? -42.522 -12.718 32.477 1.00 87.41  ? 666 TYR   A CA  1 
ATOM   2946 C  C   . TYR   A 1 370 ? -43.976 -13.092 32.221 1.00 92.16  ? 666 TYR   A C   1 
ATOM   2947 O  O   . TYR   A 1 370 ? -44.449 -14.101 32.759 1.00 95.35  ? 666 TYR   A O   1 
ATOM   2948 C  CB  . TYR   A 1 370 ? -42.357 -12.138 33.884 1.00 85.69  ? 666 TYR   A CB  1 
ATOM   2949 C  CG  . TYR   A 1 370 ? -40.973 -12.384 34.424 1.00 82.41  ? 666 TYR   A CG  1 
ATOM   2950 C  CD1 . TYR   A 1 370 ? -39.923 -11.548 34.091 1.00 78.97  ? 666 TYR   A CD1 1 
ATOM   2951 C  CD2 . TYR   A 1 370 ? -40.710 -13.472 35.248 1.00 85.75  ? 666 TYR   A CD2 1 
ATOM   2952 C  CE1 . TYR   A 1 370 ? -38.654 -11.776 34.560 1.00 78.28  ? 666 TYR   A CE1 1 
ATOM   2953 C  CE2 . TYR   A 1 370 ? -39.437 -13.705 35.730 1.00 83.41  ? 666 TYR   A CE2 1 
ATOM   2954 C  CZ  . TYR   A 1 370 ? -38.411 -12.856 35.374 1.00 79.55  ? 666 TYR   A CZ  1 
ATOM   2955 O  OH  . TYR   A 1 370 ? -37.134 -13.076 35.848 1.00 80.01  ? 666 TYR   A OH  1 
ATOM   2956 N  N   . ARG   A 1 371 ? -44.686 -12.324 31.396 1.00 94.67  ? 667 ARG   A N   1 
ATOM   2957 C  CA  . ARG   A 1 371 ? -46.088 -12.611 31.113 1.00 101.24 ? 667 ARG   A CA  1 
ATOM   2958 C  C   . ARG   A 1 371 ? -46.226 -13.519 29.896 1.00 104.26 ? 667 ARG   A C   1 
ATOM   2959 O  O   . ARG   A 1 371 ? -46.780 -14.618 29.996 1.00 103.94 ? 667 ARG   A O   1 
ATOM   2960 C  CB  . ARG   A 1 371 ? -46.863 -11.303 30.915 1.00 105.03 ? 667 ARG   A CB  1 
ATOM   2961 C  CG  . ARG   A 1 371 ? -48.357 -11.478 30.675 1.00 112.67 ? 667 ARG   A CG  1 
ATOM   2962 C  CD  . ARG   A 1 371 ? -49.016 -10.139 30.359 1.00 118.60 ? 667 ARG   A CD  1 
ATOM   2963 N  NE  . ARG   A 1 371 ? -48.149 -9.297  29.539 1.00 118.15 ? 667 ARG   A NE  1 
ATOM   2964 C  CZ  . ARG   A 1 371 ? -48.017 -9.399  28.220 1.00 123.41 ? 667 ARG   A CZ  1 
ATOM   2965 N  NH1 . ARG   A 1 371 ? -48.694 -10.300 27.520 1.00 127.96 ? 667 ARG   A NH1 1 
ATOM   2966 N  NH2 . ARG   A 1 371 ? -47.183 -8.578  27.585 1.00 121.57 ? 667 ARG   A NH2 1 
ATOM   2967 N  N   . CYS   A 1 372 ? -45.703 -13.078 28.750 1.00 102.04 ? 668 CYS   A N   1 
ATOM   2968 C  CA  . CYS   A 1 372 ? -45.848 -13.791 27.490 1.00 103.45 ? 668 CYS   A CA  1 
ATOM   2969 C  C   . CYS   A 1 372 ? -44.669 -14.709 27.182 1.00 101.03 ? 668 CYS   A C   1 
ATOM   2970 O  O   . CYS   A 1 372 ? -44.596 -15.245 26.071 1.00 102.34 ? 668 CYS   A O   1 
ATOM   2971 C  CB  . CYS   A 1 372 ? -46.046 -12.794 26.339 1.00 108.70 ? 668 CYS   A CB  1 
ATOM   2972 S  SG  . CYS   A 1 372 ? -44.568 -11.851 25.832 1.00 118.14 ? 668 CYS   A SG  1 
ATOM   2973 N  N   . ARG   A 1 373 ? -43.747 -14.906 28.128 1.00 95.88  ? 669 ARG   A N   1 
ATOM   2974 C  CA  . ARG   A 1 373 ? -42.590 -15.761 27.874 1.00 91.44  ? 669 ARG   A CA  1 
ATOM   2975 C  C   . ARG   A 1 373 ? -42.163 -16.558 29.101 1.00 89.97  ? 669 ARG   A C   1 
ATOM   2976 O  O   . ARG   A 1 373 ? -41.397 -17.522 28.980 1.00 88.01  ? 669 ARG   A O   1 
ATOM   2977 C  CB  . ARG   A 1 373 ? -41.404 -14.932 27.373 1.00 86.32  ? 669 ARG   A CB  1 
ATOM   2978 C  CG  . ARG   A 1 373 ? -40.371 -15.756 26.625 1.00 81.04  ? 669 ARG   A CG  1 
ATOM   2979 C  CD  . ARG   A 1 373 ? -39.086 -14.990 26.395 1.00 78.12  ? 669 ARG   A CD  1 
ATOM   2980 N  NE  . ARG   A 1 373 ? -38.254 -15.688 25.422 1.00 74.89  ? 669 ARG   A NE  1 
ATOM   2981 C  CZ  . ARG   A 1 373 ? -36.960 -15.463 25.247 1.00 72.22  ? 669 ARG   A CZ  1 
ATOM   2982 N  NH1 . ARG   A 1 373 ? -36.313 -14.563 25.972 1.00 68.75  ? 669 ARG   A NH1 1 
ATOM   2983 N  NH2 . ARG   A 1 373 ? -36.301 -16.160 24.323 1.00 71.73  ? 669 ARG   A NH2 1 
ATOM   2984 N  N   . GLY   A 1 374 ? -42.632 -16.158 30.285 1.00 90.66  ? 670 GLY   A N   1 
ATOM   2985 C  CA  . GLY   A 1 374 ? -42.334 -16.874 31.506 1.00 88.92  ? 670 GLY   A CA  1 
ATOM   2986 C  C   . GLY   A 1 374 ? -41.057 -16.465 32.212 1.00 89.41  ? 670 GLY   A C   1 
ATOM   2987 O  O   . GLY   A 1 374 ? -40.697 -17.094 33.219 1.00 88.89  ? 670 GLY   A O   1 
ATOM   2988 N  N   . GLY   A 1 375 ? -40.366 -15.442 31.724 1.00 86.46  ? 671 GLY   A N   1 
ATOM   2989 C  CA  . GLY   A 1 375 ? -39.110 -15.037 32.319 1.00 83.59  ? 671 GLY   A CA  1 
ATOM   2990 C  C   . GLY   A 1 375 ? -38.356 -14.094 31.411 1.00 81.18  ? 671 GLY   A C   1 
ATOM   2991 O  O   . GLY   A 1 375 ? -38.764 -13.808 30.282 1.00 79.76  ? 671 GLY   A O   1 
ATOM   2992 N  N   . CYS   A 1 376 ? -37.232 -13.620 31.937 1.00 74.19  ? 672 CYS   A N   1 
ATOM   2993 C  CA  . CYS   A 1 376 ? -36.346 -12.706 31.237 1.00 71.75  ? 672 CYS   A CA  1 
ATOM   2994 C  C   . CYS   A 1 376 ? -34.959 -12.828 31.847 1.00 66.54  ? 672 CYS   A C   1 
ATOM   2995 O  O   . CYS   A 1 376 ? -34.741 -12.359 32.966 1.00 67.12  ? 672 CYS   A O   1 
ATOM   2996 C  CB  . CYS   A 1 376 ? -36.853 -11.262 31.329 1.00 71.48  ? 672 CYS   A CB  1 
ATOM   2997 S  SG  . CYS   A 1 376 ? -35.858 -10.049 30.411 1.00 65.43  ? 672 CYS   A SG  1 
ATOM   2998 N  N   . PRO   A 1 377 ? -34.006 -13.463 31.171 1.00 68.14  ? 673 PRO   A N   1 
ATOM   2999 C  CA  . PRO   A 1 377 ? -32.634 -13.477 31.698 1.00 62.85  ? 673 PRO   A CA  1 
ATOM   3000 C  C   . PRO   A 1 377 ? -32.120 -12.059 31.848 1.00 63.36  ? 673 PRO   A C   1 
ATOM   3001 O  O   . PRO   A 1 377 ? -32.228 -11.239 30.927 1.00 54.11  ? 673 PRO   A O   1 
ATOM   3002 C  CB  . PRO   A 1 377 ? -31.844 -14.248 30.637 1.00 65.61  ? 673 PRO   A CB  1 
ATOM   3003 C  CG  . PRO   A 1 377 ? -32.715 -14.227 29.395 1.00 61.14  ? 673 PRO   A CG  1 
ATOM   3004 C  CD  . PRO   A 1 377 ? -34.123 -14.118 29.847 1.00 64.63  ? 673 PRO   A CD  1 
ATOM   3005 N  N   . ALA   A 1 378 ? -31.569 -11.759 33.024 1.00 54.26  ? 674 ALA   A N   1 
ATOM   3006 C  CA  . ALA   A 1 378 ? -31.100 -10.400 33.260 1.00 54.22  ? 674 ALA   A CA  1 
ATOM   3007 C  C   . ALA   A 1 378 ? -29.908 -10.419 34.206 1.00 55.26  ? 674 ALA   A C   1 
ATOM   3008 O  O   . ALA   A 1 378 ? -29.904 -11.157 35.188 1.00 55.13  ? 674 ALA   A O   1 
ATOM   3009 C  CB  . ALA   A 1 378 ? -32.236 -9.526  33.798 1.00 57.43  ? 674 ALA   A CB  1 
ATOM   3010 N  N   . ASP   A 1 379 ? -28.893 -9.626  33.881 1.00 51.99  ? 675 ASP   A N   1 
ATOM   3011 C  CA  . ASP   A 1 379 ? -27.629 -9.597  34.595 1.00 52.27  ? 675 ASP   A CA  1 
ATOM   3012 C  C   . ASP   A 1 379 ? -27.617 -8.278  35.349 1.00 55.40  ? 675 ASP   A C   1 
ATOM   3013 O  O   . ASP   A 1 379 ? -27.300 -7.219  34.794 1.00 50.51  ? 675 ASP   A O   1 
ATOM   3014 C  CB  . ASP   A 1 379 ? -26.427 -9.725  33.672 1.00 53.84  ? 675 ASP   A CB  1 
ATOM   3015 C  CG  . ASP   A 1 379 ? -25.130 -9.864  34.439 1.00 55.22  ? 675 ASP   A CG  1 
ATOM   3016 O  OD1 . ASP   A 1 379 ? -25.095 -9.472  35.637 1.00 54.65  ? 675 ASP   A OD1 1 
ATOM   3017 O  OD2 . ASP   A 1 379 ? -24.145 -10.371 33.863 1.00 56.09  ? 675 ASP   A OD2 1 
ATOM   3018 N  N   . TRP   A 1 380 ? -27.976 -8.359  36.626 1.00 50.51  ? 676 TRP   A N   1 
ATOM   3019 C  CA  . TRP   A 1 380 ? -28.041 -7.171  37.462 1.00 49.46  ? 676 TRP   A CA  1 
ATOM   3020 C  C   . TRP   A 1 380 ? -26.739 -6.381  37.435 1.00 47.16  ? 676 TRP   A C   1 
ATOM   3021 O  O   . TRP   A 1 380 ? -26.761 -5.148  37.364 1.00 45.28  ? 676 TRP   A O   1 
ATOM   3022 C  CB  . TRP   A 1 380 ? -28.375 -7.599  38.884 1.00 50.96  ? 676 TRP   A CB  1 
ATOM   3023 C  CG  . TRP   A 1 380 ? -28.872 -6.506  39.776 1.00 50.01  ? 676 TRP   A CG  1 
ATOM   3024 C  CD1 . TRP   A 1 380 ? -30.169 -6.274  40.116 1.00 51.08  ? 676 TRP   A CD1 1 
ATOM   3025 C  CD2 . TRP   A 1 380 ? -28.080 -5.547  40.517 1.00 50.07  ? 676 TRP   A CD2 1 
ATOM   3026 N  NE1 . TRP   A 1 380 ? -30.240 -5.234  41.029 1.00 56.11  ? 676 TRP   A NE1 1 
ATOM   3027 C  CE2 . TRP   A 1 380 ? -28.976 -4.777  41.296 1.00 51.86  ? 676 TRP   A CE2 1 
ATOM   3028 C  CE3 . TRP   A 1 380 ? -26.709 -5.271  40.604 1.00 46.00  ? 676 TRP   A CE3 1 
ATOM   3029 C  CZ2 . TRP   A 1 380 ? -28.552 -3.709  42.105 1.00 52.38  ? 676 TRP   A CZ2 1 
ATOM   3030 C  CZ3 . TRP   A 1 380 ? -26.286 -4.211  41.449 1.00 51.43  ? 676 TRP   A CZ3 1 
ATOM   3031 C  CH2 . TRP   A 1 380 ? -27.205 -3.452  42.165 1.00 46.78  ? 676 TRP   A CH2 1 
ATOM   3032 N  N   . VAL   A 1 381 ? -25.590 -7.063  37.528 1.00 48.20  ? 677 VAL   A N   1 
ATOM   3033 C  CA  . VAL   A 1 381 ? -24.296 -6.367  37.517 1.00 47.16  ? 677 VAL   A CA  1 
ATOM   3034 C  C   . VAL   A 1 381 ? -24.198 -5.424  36.329 1.00 51.98  ? 677 VAL   A C   1 
ATOM   3035 O  O   . VAL   A 1 381 ? -23.642 -4.322  36.440 1.00 46.66  ? 677 VAL   A O   1 
ATOM   3036 C  CB  . VAL   A 1 381 ? -23.126 -7.372  37.520 1.00 51.09  ? 677 VAL   A CB  1 
ATOM   3037 C  CG1 . VAL   A 1 381 ? -21.811 -6.632  37.481 1.00 51.62  ? 677 VAL   A CG1 1 
ATOM   3038 C  CG2 . VAL   A 1 381 ? -23.160 -8.256  38.770 1.00 53.93  ? 677 VAL   A CG2 1 
ATOM   3039 N  N   . TRP   A 1 382 ? -24.722 -5.851  35.161 1.00 53.64  ? 678 TRP   A N   1 
ATOM   3040 C  CA  . TRP   A 1 382 ? -24.664 -5.064  33.930 1.00 53.41  ? 678 TRP   A CA  1 
ATOM   3041 C  C   . TRP   A 1 382 ? -25.898 -4.208  33.691 1.00 52.63  ? 678 TRP   A C   1 
ATOM   3042 O  O   . TRP   A 1 382 ? -25.798 -3.165  33.025 1.00 53.51  ? 678 TRP   A O   1 
ATOM   3043 C  CB  . TRP   A 1 382 ? -24.460 -5.983  32.710 1.00 54.25  ? 678 TRP   A CB  1 
ATOM   3044 C  CG  . TRP   A 1 382 ? -23.011 -6.305  32.472 1.00 56.89  ? 678 TRP   A CG  1 
ATOM   3045 C  CD1 . TRP   A 1 382 ? -22.166 -6.970  33.315 1.00 58.24  ? 678 TRP   A CD1 1 
ATOM   3046 C  CD2 . TRP   A 1 382 ? -22.234 -5.961  31.313 1.00 60.76  ? 678 TRP   A CD2 1 
ATOM   3047 N  NE1 . TRP   A 1 382 ? -20.908 -7.057  32.751 1.00 58.80  ? 678 TRP   A NE1 1 
ATOM   3048 C  CE2 . TRP   A 1 382 ? -20.926 -6.443  31.524 1.00 60.54  ? 678 TRP   A CE2 1 
ATOM   3049 C  CE3 . TRP   A 1 382 ? -22.518 -5.287  30.127 1.00 59.05  ? 678 TRP   A CE3 1 
ATOM   3050 C  CZ2 . TRP   A 1 382 ? -19.908 -6.271  30.595 1.00 62.39  ? 678 TRP   A CZ2 1 
ATOM   3051 C  CZ3 . TRP   A 1 382 ? -21.502 -5.125  29.193 1.00 62.88  ? 678 TRP   A CZ3 1 
ATOM   3052 C  CH2 . TRP   A 1 382 ? -20.216 -5.617  29.432 1.00 64.13  ? 678 TRP   A CH2 1 
ATOM   3053 N  N   . ILE   A 1 383 ? -27.063 -4.604  34.205 1.00 50.51  ? 679 ILE   A N   1 
ATOM   3054 C  CA  . ILE   A 1 383 ? -28.274 -3.828  33.916 1.00 52.58  ? 679 ILE   A CA  1 
ATOM   3055 C  C   . ILE   A 1 383 ? -28.293 -2.531  34.725 1.00 55.91  ? 679 ILE   A C   1 
ATOM   3056 O  O   . ILE   A 1 383 ? -28.762 -1.494  34.237 1.00 53.38  ? 679 ILE   A O   1 
ATOM   3057 C  CB  . ILE   A 1 383 ? -29.533 -4.680  34.180 1.00 53.41  ? 679 ILE   A CB  1 
ATOM   3058 C  CG1 . ILE   A 1 383 ? -29.599 -5.866  33.210 1.00 49.07  ? 679 ILE   A CG1 1 
ATOM   3059 C  CG2 . ILE   A 1 383 ? -30.807 -3.835  34.085 1.00 51.20  ? 679 ILE   A CG2 1 
ATOM   3060 C  CD1 . ILE   A 1 383 ? -30.007 -5.472  31.729 1.00 55.13  ? 679 ILE   A CD1 1 
ATOM   3061 N  N   . VAL   A 1 384 ? -27.781 -2.545  35.949 1.00 51.08  ? 680 VAL   A N   1 
ATOM   3062 C  CA  . VAL   A 1 384 ? -27.835 -1.318  36.758 1.00 52.22  ? 680 VAL   A CA  1 
ATOM   3063 C  C   . VAL   A 1 384 ? -26.869 -0.284  36.191 1.00 52.42  ? 680 VAL   A C   1 
ATOM   3064 O  O   . VAL   A 1 384 ? -25.683 -0.592  35.982 1.00 49.43  ? 680 VAL   A O   1 
ATOM   3065 C  CB  . VAL   A 1 384 ? -27.512 -1.623  38.207 1.00 52.23  ? 680 VAL   A CB  1 
ATOM   3066 C  CG1 . VAL   A 1 384 ? -27.332 -0.312  39.009 1.00 51.40  ? 680 VAL   A CG1 1 
ATOM   3067 C  CG2 . VAL   A 1 384 ? -28.618 -2.470  38.788 1.00 53.18  ? 680 VAL   A CG2 1 
ATOM   3068 N  N   . PRO   A 1 385 ? -27.314 0.940   35.941 1.00 55.86  ? 681 PRO   A N   1 
ATOM   3069 C  CA  . PRO   A 1 385 ? -26.434 1.951   35.337 1.00 56.28  ? 681 PRO   A CA  1 
ATOM   3070 C  C   . PRO   A 1 385 ? -25.233 2.247   36.216 1.00 61.34  ? 681 PRO   A C   1 
ATOM   3071 O  O   . PRO   A 1 385 ? -25.285 2.074   37.448 1.00 62.74  ? 681 PRO   A O   1 
ATOM   3072 C  CB  . PRO   A 1 385 ? -27.346 3.177   35.203 1.00 56.91  ? 681 PRO   A CB  1 
ATOM   3073 C  CG  . PRO   A 1 385 ? -28.706 2.613   35.123 1.00 58.52  ? 681 PRO   A CG  1 
ATOM   3074 C  CD  . PRO   A 1 385 ? -28.713 1.394   36.026 1.00 56.61  ? 681 PRO   A CD  1 
ATOM   3075 N  N   . PRO   A 1 386 ? -24.136 2.721   35.625 1.00 60.79  ? 682 PRO   A N   1 
ATOM   3076 C  CA  . PRO   A 1 386 ? -22.904 2.946   36.388 1.00 62.36  ? 682 PRO   A CA  1 
ATOM   3077 C  C   . PRO   A 1 386 ? -22.888 4.222   37.222 1.00 64.58  ? 682 PRO   A C   1 
ATOM   3078 O  O   . PRO   A 1 386 ? -21.833 4.580   37.760 1.00 66.13  ? 682 PRO   A O   1 
ATOM   3079 C  CB  . PRO   A 1 386 ? -21.844 2.998   35.272 1.00 62.33  ? 682 PRO   A CB  1 
ATOM   3080 C  CG  . PRO   A 1 386 ? -22.561 3.556   34.128 1.00 63.52  ? 682 PRO   A CG  1 
ATOM   3081 C  CD  . PRO   A 1 386 ? -23.954 3.009   34.189 1.00 59.87  ? 682 PRO   A CD  1 
ATOM   3082 N  N   . MET   A 1 387 ? -24.012 4.928   37.336 1.00 64.91  ? 683 MET   A N   1 
ATOM   3083 C  CA  . MET   A 1 387 ? -24.150 6.044   38.262 1.00 66.09  ? 683 MET   A CA  1 
ATOM   3084 C  C   . MET   A 1 387 ? -25.593 6.038   38.734 1.00 67.68  ? 683 MET   A C   1 
ATOM   3085 O  O   . MET   A 1 387 ? -26.469 5.459   38.089 1.00 64.41  ? 683 MET   A O   1 
ATOM   3086 C  CB  . MET   A 1 387 ? -23.812 7.405   37.619 1.00 70.38  ? 683 MET   A CB  1 
ATOM   3087 C  CG  . MET   A 1 387 ? -24.873 7.866   36.624 1.00 66.89  ? 683 MET   A CG  1 
ATOM   3088 S  SD  . MET   A 1 387 ? -24.545 9.431   35.767 1.00 83.25  ? 683 MET   A SD  1 
ATOM   3089 C  CE  . MET   A 1 387 ? -24.774 10.647  37.047 1.00 73.81  ? 683 MET   A CE  1 
ATOM   3090 N  N   . SER   A 1 388 ? -25.833 6.680   39.872 1.00 69.92  ? 684 SER   A N   1 
ATOM   3091 C  CA  . SER   A 1 388 ? -27.185 6.840   40.418 1.00 70.87  ? 684 SER   A CA  1 
ATOM   3092 C  C   . SER   A 1 388 ? -27.927 5.513   40.531 1.00 68.92  ? 684 SER   A C   1 
ATOM   3093 O  O   . SER   A 1 388 ? -29.156 5.475   40.439 1.00 70.17  ? 684 SER   A O   1 
ATOM   3094 C  CB  . SER   A 1 388 ? -28.011 7.812   39.575 1.00 70.96  ? 684 SER   A CB  1 
ATOM   3095 O  OG  . SER   A 1 388 ? -27.365 9.059   39.424 1.00 74.87  ? 684 SER   A OG  1 
ATOM   3096 N  N   . GLY   A 1 389 ? -27.193 4.421   40.714 1.00 63.36  ? 685 GLY   A N   1 
ATOM   3097 C  CA  . GLY   A 1 389 ? -27.789 3.101   40.698 1.00 63.04  ? 685 GLY   A CA  1 
ATOM   3098 C  C   . GLY   A 1 389 ? -29.170 2.978   41.319 1.00 64.82  ? 685 GLY   A C   1 
ATOM   3099 O  O   . GLY   A 1 389 ? -30.133 2.652   40.626 1.00 63.17  ? 685 GLY   A O   1 
ATOM   3100 N  N   . SER   A 1 390 ? -29.296 3.285   42.608 1.00 65.45  ? 686 SER   A N   1 
ATOM   3101 C  CA  . SER   A 1 390 ? -30.520 2.978   43.343 1.00 66.86  ? 686 SER   A CA  1 
ATOM   3102 C  C   . SER   A 1 390 ? -31.651 3.967   43.125 1.00 67.42  ? 686 SER   A C   1 
ATOM   3103 O  O   . SER   A 1 390 ? -32.762 3.696   43.595 1.00 71.55  ? 686 SER   A O   1 
ATOM   3104 C  CB  . SER   A 1 390 ? -30.252 2.876   44.846 1.00 63.49  ? 686 SER   A CB  1 
ATOM   3105 O  OG  . SER   A 1 390 ? -29.626 4.038   45.280 1.00 63.45  ? 686 SER   A OG  1 
ATOM   3106 N  N   . ILE   A 1 391 ? -31.418 5.108   42.463 1.00 69.43  ? 687 ILE   A N   1 
ATOM   3107 C  CA  . ILE   A 1 391 ? -32.546 5.951   42.077 1.00 68.32  ? 687 ILE   A CA  1 
ATOM   3108 C  C   . ILE   A 1 391 ? -33.096 5.577   40.704 1.00 70.63  ? 687 ILE   A C   1 
ATOM   3109 O  O   . ILE   A 1 391 ? -33.984 6.275   40.196 1.00 74.78  ? 687 ILE   A O   1 
ATOM   3110 C  CB  . ILE   A 1 391 ? -32.226 7.463   42.098 1.00 72.61  ? 687 ILE   A CB  1 
ATOM   3111 C  CG1 . ILE   A 1 391 ? -31.224 7.850   41.006 1.00 78.99  ? 687 ILE   A CG1 1 
ATOM   3112 C  CG2 . ILE   A 1 391 ? -31.849 7.950   43.544 1.00 75.31  ? 687 ILE   A CG2 1 
ATOM   3113 C  CD1 . ILE   A 1 391 ? -31.046 9.364   40.859 1.00 81.86  ? 687 ILE   A CD1 1 
ATOM   3114 N  N   . THR   A 1 392 ? -32.587 4.473   40.077 1.00 69.92  ? 688 THR   A N   1 
ATOM   3115 C  CA  . THR   A 1 392 ? -33.219 3.809   38.945 1.00 69.68  ? 688 THR   A CA  1 
ATOM   3116 C  C   . THR   A 1 392 ? -33.948 2.557   39.422 1.00 68.74  ? 688 THR   A C   1 
ATOM   3117 O  O   . THR   A 1 392 ? -33.537 1.927   40.406 1.00 69.07  ? 688 THR   A O   1 
ATOM   3118 C  CB  . THR   A 1 392 ? -32.196 3.428   37.867 1.00 69.90  ? 688 THR   A CB  1 
ATOM   3119 O  OG1 . THR   A 1 392 ? -31.398 2.323   38.309 1.00 61.41  ? 688 THR   A OG1 1 
ATOM   3120 C  CG2 . THR   A 1 392 ? -31.302 4.630   37.506 1.00 69.34  ? 688 THR   A CG2 1 
ATOM   3121 N  N   . PRO   A 1 393 ? -35.054 2.192   38.767 1.00 68.22  ? 689 PRO   A N   1 
ATOM   3122 C  CA  . PRO   A 1 393 ? -35.879 1.087   39.278 1.00 68.35  ? 689 PRO   A CA  1 
ATOM   3123 C  C   . PRO   A 1 393 ? -35.245 -0.284  39.129 1.00 66.86  ? 689 PRO   A C   1 
ATOM   3124 O  O   . PRO   A 1 393 ? -35.709 -1.225  39.790 1.00 68.97  ? 689 PRO   A O   1 
ATOM   3125 C  CB  . PRO   A 1 393 ? -37.148 1.194   38.426 1.00 72.51  ? 689 PRO   A CB  1 
ATOM   3126 C  CG  . PRO   A 1 393 ? -36.591 1.589   37.094 1.00 71.61  ? 689 PRO   A CG  1 
ATOM   3127 C  CD  . PRO   A 1 393 ? -35.540 2.641   37.450 1.00 70.23  ? 689 PRO   A CD  1 
ATOM   3128 N  N   . VAL   A 1 394 ? -34.225 -0.445  38.283 1.00 64.29  ? 690 VAL   A N   1 
ATOM   3129 C  CA  . VAL   A 1 394 ? -33.602 -1.760  38.136 1.00 61.36  ? 690 VAL   A CA  1 
ATOM   3130 C  C   . VAL   A 1 394 ? -32.734 -2.124  39.337 1.00 63.42  ? 690 VAL   A C   1 
ATOM   3131 O  O   . VAL   A 1 394 ? -32.486 -3.317  39.577 1.00 57.33  ? 690 VAL   A O   1 
ATOM   3132 C  CB  . VAL   A 1 394 ? -32.749 -1.857  36.859 1.00 62.93  ? 690 VAL   A CB  1 
ATOM   3133 C  CG1 . VAL   A 1 394 ? -33.644 -1.875  35.596 1.00 59.70  ? 690 VAL   A CG1 1 
ATOM   3134 C  CG2 . VAL   A 1 394 ? -31.749 -0.736  36.801 1.00 60.57  ? 690 VAL   A CG2 1 
ATOM   3135 N  N   . PHE   A 1 395 ? -32.266 -1.128  40.105 1.00 64.39  ? 691 PHE   A N   1 
ATOM   3136 C  CA  . PHE   A 1 395 ? -31.480 -1.416  41.306 1.00 61.20  ? 691 PHE   A CA  1 
ATOM   3137 C  C   . PHE   A 1 395 ? -32.261 -2.288  42.264 1.00 62.93  ? 691 PHE   A C   1 
ATOM   3138 O  O   . PHE   A 1 395 ? -31.690 -3.161  42.933 1.00 61.95  ? 691 PHE   A O   1 
ATOM   3139 C  CB  . PHE   A 1 395 ? -31.071 -0.117  42.005 1.00 62.37  ? 691 PHE   A CB  1 
ATOM   3140 C  CG  . PHE   A 1 395 ? -30.221 -0.313  43.235 1.00 62.55  ? 691 PHE   A CG  1 
ATOM   3141 C  CD1 . PHE   A 1 395 ? -30.808 -0.585  44.469 1.00 63.35  ? 691 PHE   A CD1 1 
ATOM   3142 C  CD2 . PHE   A 1 395 ? -28.844 -0.184  43.172 1.00 57.25  ? 691 PHE   A CD2 1 
ATOM   3143 C  CE1 . PHE   A 1 395 ? -30.026 -0.746  45.621 1.00 62.85  ? 691 PHE   A CE1 1 
ATOM   3144 C  CE2 . PHE   A 1 395 ? -28.060 -0.349  44.333 1.00 65.29  ? 691 PHE   A CE2 1 
ATOM   3145 C  CZ  . PHE   A 1 395 ? -28.651 -0.625  45.538 1.00 60.14  ? 691 PHE   A CZ  1 
ATOM   3146 N  N   . HIS   A 1 396 ? -33.569 -2.060  42.349 1.00 64.81  ? 692 HIS   A N   1 
ATOM   3147 C  CA  . HIS   A 1 396 ? -34.419 -2.703  43.340 1.00 67.14  ? 692 HIS   A CA  1 
ATOM   3148 C  C   . HIS   A 1 396 ? -35.114 -3.934  42.789 1.00 68.75  ? 692 HIS   A C   1 
ATOM   3149 O  O   . HIS   A 1 396 ? -36.009 -4.480  43.438 1.00 70.00  ? 692 HIS   A O   1 
ATOM   3150 C  CB  . HIS   A 1 396 ? -35.437 -1.692  43.859 1.00 73.85  ? 692 HIS   A CB  1 
ATOM   3151 C  CG  . HIS   A 1 396 ? -34.818 -0.387  44.255 1.00 71.25  ? 692 HIS   A CG  1 
ATOM   3152 N  ND1 . HIS   A 1 396 ? -34.095 -0.233  45.417 1.00 69.62  ? 692 HIS   A ND1 1 
ATOM   3153 C  CD2 . HIS   A 1 396 ? -34.783 0.813   43.630 1.00 71.49  ? 692 HIS   A CD2 1 
ATOM   3154 C  CE1 . HIS   A 1 396 ? -33.663 1.014   45.505 1.00 71.04  ? 692 HIS   A CE1 1 
ATOM   3155 N  NE2 . HIS   A 1 396 ? -34.068 1.670   44.435 1.00 71.53  ? 692 HIS   A NE2 1 
ATOM   3156 N  N   . GLN   A 1 397 ? -34.707 -4.384  41.614 1.00 66.49  ? 693 GLN   A N   1 
ATOM   3157 C  CA  . GLN   A 1 397 ? -35.357 -5.466  40.891 1.00 65.88  ? 693 GLN   A CA  1 
ATOM   3158 C  C   . GLN   A 1 397 ? -34.475 -6.700  40.943 1.00 62.17  ? 693 GLN   A C   1 
ATOM   3159 O  O   . GLN   A 1 397 ? -33.351 -6.674  40.440 1.00 58.21  ? 693 GLN   A O   1 
ATOM   3160 C  CB  . GLN   A 1 397 ? -35.603 -5.058  39.441 1.00 65.99  ? 693 GLN   A CB  1 
ATOM   3161 C  CG  . GLN   A 1 397 ? -36.215 -6.154  38.608 1.00 65.81  ? 693 GLN   A CG  1 
ATOM   3162 C  CD  . GLN   A 1 397 ? -37.608 -6.479  39.081 1.00 69.43  ? 693 GLN   A CD  1 
ATOM   3163 O  OE1 . GLN   A 1 397 ? -38.457 -5.594  39.185 1.00 70.03  ? 693 GLN   A OE1 1 
ATOM   3164 N  NE2 . GLN   A 1 397 ? -37.847 -7.749  39.406 1.00 70.59  ? 693 GLN   A NE2 1 
ATOM   3165 N  N   . GLU   A 1 398 ? -34.966 -7.762  41.579 1.00 67.81  ? 694 GLU   A N   1 
ATOM   3166 C  CA  . GLU   A 1 398 ? -34.259 -9.033  41.542 1.00 65.48  ? 694 GLU   A CA  1 
ATOM   3167 C  C   . GLU   A 1 398 ? -34.329 -9.594  40.132 1.00 66.69  ? 694 GLU   A C   1 
ATOM   3168 O  O   . GLU   A 1 398 ? -35.385 -9.552  39.493 1.00 66.70  ? 694 GLU   A O   1 
ATOM   3169 C  CB  . GLU   A 1 398 ? -34.855 -10.014 42.550 1.00 66.19  ? 694 GLU   A CB  1 
ATOM   3170 C  CG  . GLU   A 1 398 ? -34.591 -9.603  44.023 1.00 67.73  ? 694 GLU   A CG  1 
ATOM   3171 C  CD  . GLU   A 1 398 ? -35.327 -10.475 44.998 1.00 70.35  ? 694 GLU   A CD  1 
ATOM   3172 O  OE1 . GLU   A 1 398 ? -36.044 -11.381 44.519 1.00 75.48  ? 694 GLU   A OE1 1 
ATOM   3173 O  OE2 . GLU   A 1 398 ? -35.184 -10.265 46.234 1.00 74.05  ? 694 GLU   A OE2 1 
ATOM   3174 N  N   . MET   A 1 399 ? -33.197 -10.088 39.633 1.00 61.41  ? 695 MET   A N   1 
ATOM   3175 C  CA  . MET   A 1 399 ? -33.107 -10.589 38.270 1.00 63.28  ? 695 MET   A CA  1 
ATOM   3176 C  C   . MET   A 1 399 ? -32.395 -11.923 38.284 1.00 64.09  ? 695 MET   A C   1 
ATOM   3177 O  O   . MET   A 1 399 ? -31.301 -12.039 38.848 1.00 65.42  ? 695 MET   A O   1 
ATOM   3178 C  CB  . MET   A 1 399 ? -32.350 -9.625  37.346 1.00 59.53  ? 695 MET   A CB  1 
ATOM   3179 C  CG  . MET   A 1 399 ? -32.846 -8.205  37.348 1.00 61.47  ? 695 MET   A CG  1 
ATOM   3180 S  SD  . MET   A 1 399 ? -31.700 -7.139  36.473 1.00 55.94  ? 695 MET   A SD  1 
ATOM   3181 C  CE  . MET   A 1 399 ? -32.342 -5.532  36.921 1.00 57.11  ? 695 MET   A CE  1 
ATOM   3182 N  N   . LEU   A 1 400 ? -33.023 -12.919 37.671 1.00 63.57  ? 696 LEU   A N   1 
ATOM   3183 C  CA  . LEU   A 1 400 ? -32.411 -14.222 37.464 1.00 62.92  ? 696 LEU   A CA  1 
ATOM   3184 C  C   . LEU   A 1 400 ? -31.604 -14.171 36.177 1.00 63.90  ? 696 LEU   A C   1 
ATOM   3185 O  O   . LEU   A 1 400 ? -32.148 -13.849 35.115 1.00 62.22  ? 696 LEU   A O   1 
ATOM   3186 C  CB  . LEU   A 1 400 ? -33.473 -15.313 37.377 1.00 66.49  ? 696 LEU   A CB  1 
ATOM   3187 C  CG  . LEU   A 1 400 ? -34.249 -15.607 38.659 1.00 69.33  ? 696 LEU   A CG  1 
ATOM   3188 C  CD1 . LEU   A 1 400 ? -35.375 -16.574 38.374 1.00 76.10  ? 696 LEU   A CD1 1 
ATOM   3189 C  CD2 . LEU   A 1 400 ? -33.322 -16.169 39.712 1.00 70.73  ? 696 LEU   A CD2 1 
ATOM   3190 N  N   . ASN   A 1 401 ? -30.312 -14.460 36.273 1.00 63.31  ? 697 ASN   A N   1 
ATOM   3191 C  CA  . ASN   A 1 401 ? -29.463 -14.601 35.102 1.00 62.65  ? 697 ASN   A CA  1 
ATOM   3192 C  C   . ASN   A 1 401 ? -29.387 -16.072 34.718 1.00 66.84  ? 697 ASN   A C   1 
ATOM   3193 O  O   . ASN   A 1 401 ? -29.228 -16.938 35.586 1.00 67.89  ? 697 ASN   A O   1 
ATOM   3194 C  CB  . ASN   A 1 401 ? -28.060 -14.051 35.359 1.00 61.69  ? 697 ASN   A CB  1 
ATOM   3195 C  CG  . ASN   A 1 401 ? -27.329 -13.767 34.083 1.00 55.78  ? 697 ASN   A CG  1 
ATOM   3196 O  OD1 . ASN   A 1 401 ? -27.959 -13.627 33.057 1.00 60.42  ? 697 ASN   A OD1 1 
ATOM   3197 N  ND2 . ASN   A 1 401 ? -26.006 -13.699 34.127 1.00 54.29  ? 697 ASN   A ND2 1 
ATOM   3198 N  N   . TYR   A 1 402 ? -29.531 -16.347 33.420 1.00 67.06  ? 698 TYR   A N   1 
ATOM   3199 C  CA  . TYR   A 1 402 ? -29.361 -17.681 32.879 1.00 66.72  ? 698 TYR   A CA  1 
ATOM   3200 C  C   . TYR   A 1 402 ? -29.209 -17.567 31.356 1.00 71.20  ? 698 TYR   A C   1 
ATOM   3201 O  O   . TYR   A 1 402 ? -29.655 -16.590 30.742 1.00 68.12  ? 698 TYR   A O   1 
ATOM   3202 C  CB  . TYR   A 1 402 ? -30.529 -18.589 33.295 1.00 70.44  ? 698 TYR   A CB  1 
ATOM   3203 C  CG  . TYR   A 1 402 ? -31.908 -18.002 33.060 1.00 71.31  ? 698 TYR   A CG  1 
ATOM   3204 C  CD1 . TYR   A 1 402 ? -32.526 -18.112 31.807 1.00 68.56  ? 698 TYR   A CD1 1 
ATOM   3205 C  CD2 . TYR   A 1 402 ? -32.599 -17.338 34.084 1.00 66.31  ? 698 TYR   A CD2 1 
ATOM   3206 C  CE1 . TYR   A 1 402 ? -33.783 -17.590 31.577 1.00 68.88  ? 698 TYR   A CE1 1 
ATOM   3207 C  CE2 . TYR   A 1 402 ? -33.866 -16.805 33.865 1.00 68.81  ? 698 TYR   A CE2 1 
ATOM   3208 C  CZ  . TYR   A 1 402 ? -34.452 -16.935 32.601 1.00 72.77  ? 698 TYR   A CZ  1 
ATOM   3209 O  OH  . TYR   A 1 402 ? -35.707 -16.408 32.369 1.00 74.49  ? 698 TYR   A OH  1 
ATOM   3210 N  N   . ARG   A 1 403 ? -28.531 -18.551 30.763 1.00 72.26  ? 699 ARG   A N   1 
ATOM   3211 C  CA  . ARG   A 1 403 ? -28.088 -18.484 29.375 1.00 77.28  ? 699 ARG   A CA  1 
ATOM   3212 C  C   . ARG   A 1 403 ? -29.113 -19.187 28.501 1.00 75.62  ? 699 ARG   A C   1 
ATOM   3213 O  O   . ARG   A 1 403 ? -29.344 -20.389 28.652 1.00 80.17  ? 699 ARG   A O   1 
ATOM   3214 C  CB  . ARG   A 1 403 ? -26.715 -19.126 29.206 1.00 84.19  ? 699 ARG   A CB  1 
ATOM   3215 C  CG  . ARG   A 1 403 ? -25.654 -18.608 30.142 1.00 85.81  ? 699 ARG   A CG  1 
ATOM   3216 C  CD  . ARG   A 1 403 ? -24.445 -18.111 29.387 1.00 91.25  ? 699 ARG   A CD  1 
ATOM   3217 N  NE  . ARG   A 1 403 ? -24.805 -17.068 28.431 1.00 96.75  ? 699 ARG   A NE  1 
ATOM   3218 C  CZ  . ARG   A 1 403 ? -23.984 -16.595 27.502 1.00 99.44  ? 699 ARG   A CZ  1 
ATOM   3219 N  NH1 . ARG   A 1 403 ? -22.736 -17.023 27.406 1.00 105.92 ? 699 ARG   A NH1 1 
ATOM   3220 N  NH2 . ARG   A 1 403 ? -24.427 -15.673 26.645 1.00 92.55  ? 699 ARG   A NH2 1 
ATOM   3221 N  N   . LEU   A 1 404 ? -29.736 -18.439 27.605 1.00 70.38  ? 700 LEU   A N   1 
ATOM   3222 C  CA  . LEU   A 1 404 ? -30.618 -19.008 26.603 1.00 69.44  ? 700 LEU   A CA  1 
ATOM   3223 C  C   . LEU   A 1 404 ? -29.989 -18.864 25.224 1.00 70.65  ? 700 LEU   A C   1 
ATOM   3224 O  O   . LEU   A 1 404 ? -29.038 -18.107 25.024 1.00 71.13  ? 700 LEU   A O   1 
ATOM   3225 C  CB  . LEU   A 1 404 ? -31.991 -18.333 26.610 1.00 67.59  ? 700 LEU   A CB  1 
ATOM   3226 C  CG  . LEU   A 1 404 ? -32.876 -18.353 27.851 1.00 68.80  ? 700 LEU   A CG  1 
ATOM   3227 C  CD1 . LEU   A 1 404 ? -34.205 -17.702 27.501 1.00 67.67  ? 700 LEU   A CD1 1 
ATOM   3228 C  CD2 . LEU   A 1 404 ? -33.097 -19.752 28.387 1.00 72.79  ? 700 LEU   A CD2 1 
ATOM   3229 N  N   . THR   A 1 405 ? -30.534 -19.607 24.270 1.00 68.41  ? 701 THR   A N   1 
ATOM   3230 C  CA  . THR   A 1 405 ? -30.059 -19.551 22.905 1.00 67.72  ? 701 THR   A CA  1 
ATOM   3231 C  C   . THR   A 1 405 ? -31.253 -19.328 21.978 1.00 66.75  ? 701 THR   A C   1 
ATOM   3232 O  O   . THR   A 1 405 ? -32.375 -19.712 22.325 1.00 69.46  ? 701 THR   A O   1 
ATOM   3233 C  CB  . THR   A 1 405 ? -29.312 -20.853 22.567 1.00 71.14  ? 701 THR   A CB  1 
ATOM   3234 O  OG1 . THR   A 1 405 ? -28.397 -20.630 21.496 1.00 69.03  ? 701 THR   A OG1 1 
ATOM   3235 C  CG2 . THR   A 1 405 ? -30.265 -21.957 22.213 1.00 68.73  ? 701 THR   A CG2 1 
ATOM   3236 N  N   . PRO   A 1 406 ? -31.081 -18.657 20.822 1.00 68.28  ? 702 PRO   A N   1 
ATOM   3237 C  CA  . PRO   A 1 406 ? -29.875 -18.034 20.245 1.00 66.27  ? 702 PRO   A CA  1 
ATOM   3238 C  C   . PRO   A 1 406 ? -29.240 -16.967 21.131 1.00 66.10  ? 702 PRO   A C   1 
ATOM   3239 O  O   . PRO   A 1 406 ? -29.915 -16.351 21.956 1.00 66.50  ? 702 PRO   A O   1 
ATOM   3240 C  CB  . PRO   A 1 406 ? -30.401 -17.413 18.939 1.00 66.25  ? 702 PRO   A CB  1 
ATOM   3241 C  CG  . PRO   A 1 406 ? -31.598 -18.225 18.569 1.00 66.89  ? 702 PRO   A CG  1 
ATOM   3242 C  CD  . PRO   A 1 406 ? -32.223 -18.598 19.887 1.00 67.48  ? 702 PRO   A CD  1 
ATOM   3243 N  N   . SER   A 1 407 ? -27.942 -16.708 20.981 1.00 65.60  ? 703 SER   A N   1 
ATOM   3244 C  CA  . SER   A 1 407 ? -27.267 -15.812 21.904 1.00 65.93  ? 703 SER   A CA  1 
ATOM   3245 C  C   . SER   A 1 407 ? -26.081 -15.148 21.218 1.00 65.30  ? 703 SER   A C   1 
ATOM   3246 O  O   . SER   A 1 407 ? -25.514 -15.674 20.250 1.00 63.58  ? 703 SER   A O   1 
ATOM   3247 C  CB  . SER   A 1 407 ? -26.801 -16.567 23.156 1.00 69.06  ? 703 SER   A CB  1 
ATOM   3248 O  OG  . SER   A 1 407 ? -25.703 -17.413 22.851 1.00 70.51  ? 703 SER   A OG  1 
ATOM   3249 N  N   . PHE   A 1 408 ? -25.722 -13.971 21.728 1.00 66.17  ? 704 PHE   A N   1 
ATOM   3250 C  CA  . PHE   A 1 408 ? -24.455 -13.332 21.404 1.00 63.98  ? 704 PHE   A CA  1 
ATOM   3251 C  C   . PHE   A 1 408 ? -23.442 -13.778 22.446 1.00 69.74  ? 704 PHE   A C   1 
ATOM   3252 O  O   . PHE   A 1 408 ? -23.745 -13.796 23.640 1.00 71.11  ? 704 PHE   A O   1 
ATOM   3253 C  CB  . PHE   A 1 408 ? -24.573 -11.803 21.386 1.00 57.73  ? 704 PHE   A CB  1 
ATOM   3254 C  CG  . PHE   A 1 408 ? -25.459 -11.281 20.304 1.00 61.25  ? 704 PHE   A CG  1 
ATOM   3255 C  CD1 . PHE   A 1 408 ? -25.001 -11.219 18.969 1.00 59.64  ? 704 PHE   A CD1 1 
ATOM   3256 C  CD2 . PHE   A 1 408 ? -26.751 -10.860 20.595 1.00 60.50  ? 704 PHE   A CD2 1 
ATOM   3257 C  CE1 . PHE   A 1 408 ? -25.820 -10.738 17.951 1.00 56.33  ? 704 PHE   A CE1 1 
ATOM   3258 C  CE2 . PHE   A 1 408 ? -27.577 -10.375 19.584 1.00 59.41  ? 704 PHE   A CE2 1 
ATOM   3259 C  CZ  . PHE   A 1 408 ? -27.107 -10.321 18.249 1.00 57.44  ? 704 PHE   A CZ  1 
ATOM   3260 N  N   . GLU   A 1 409 ? -22.259 -14.161 21.993 1.00 72.51  ? 705 GLU   A N   1 
ATOM   3261 C  CA  . GLU   A 1 409 ? -21.209 -14.661 22.854 1.00 75.99  ? 705 GLU   A CA  1 
ATOM   3262 C  C   . GLU   A 1 409 ? -19.942 -13.866 22.594 1.00 74.65  ? 705 GLU   A C   1 
ATOM   3263 O  O   . GLU   A 1 409 ? -19.752 -13.291 21.513 1.00 70.47  ? 705 GLU   A O   1 
ATOM   3264 C  CB  . GLU   A 1 409 ? -20.943 -16.150 22.610 1.00 87.75  ? 705 GLU   A CB  1 
ATOM   3265 C  CG  . GLU   A 1 409 ? -22.154 -17.054 22.780 1.00 87.95  ? 705 GLU   A CG  1 
ATOM   3266 C  CD  . GLU   A 1 409 ? -22.597 -17.186 24.228 1.00 94.37  ? 705 GLU   A CD  1 
ATOM   3267 O  OE1 . GLU   A 1 409 ? -21.855 -16.737 25.129 1.00 99.97  ? 705 GLU   A OE1 1 
ATOM   3268 O  OE2 . GLU   A 1 409 ? -23.690 -17.740 24.462 1.00 90.60  ? 705 GLU   A OE2 1 
ATOM   3269 N  N   . TYR   A 1 410 ? -19.080 -13.820 23.601 1.00 84.56  ? 706 TYR   A N   1 
ATOM   3270 C  CA  . TYR   A 1 410 ? -17.755 -13.286 23.380 1.00 80.97  ? 706 TYR   A CA  1 
ATOM   3271 C  C   . TYR   A 1 410 ? -16.931 -14.280 22.590 1.00 84.44  ? 706 TYR   A C   1 
ATOM   3272 O  O   . TYR   A 1 410 ? -17.281 -15.454 22.446 1.00 92.74  ? 706 TYR   A O   1 
ATOM   3273 C  CB  . TYR   A 1 410 ? -17.034 -12.990 24.695 1.00 87.59  ? 706 TYR   A CB  1 
ATOM   3274 C  CG  . TYR   A 1 410 ? -17.722 -11.987 25.567 1.00 84.05  ? 706 TYR   A CG  1 
ATOM   3275 C  CD1 . TYR   A 1 410 ? -17.899 -10.679 25.145 1.00 78.40  ? 706 TYR   A CD1 1 
ATOM   3276 C  CD2 . TYR   A 1 410 ? -18.173 -12.339 26.831 1.00 94.40  ? 706 TYR   A CD2 1 
ATOM   3277 C  CE1 . TYR   A 1 410 ? -18.530 -9.756  25.944 1.00 79.39  ? 706 TYR   A CE1 1 
ATOM   3278 C  CE2 . TYR   A 1 410 ? -18.797 -11.424 27.646 1.00 87.36  ? 706 TYR   A CE2 1 
ATOM   3279 C  CZ  . TYR   A 1 410 ? -18.972 -10.140 27.202 1.00 84.11  ? 706 TYR   A CZ  1 
ATOM   3280 O  OH  . TYR   A 1 410 ? -19.597 -9.244  28.017 1.00 79.59  ? 706 TYR   A OH  1 
ATOM   3281 N  N   . GLN   A 1 411 ? -15.797 -13.799 22.106 1.00 77.27  ? 707 GLN   A N   1 
ATOM   3282 C  CA  . GLN   A 1 411 ? -14.883 -14.631 21.348 1.00 79.27  ? 707 GLN   A CA  1 
ATOM   3283 C  C   . GLN   A 1 411 ? -13.522 -13.980 21.431 1.00 78.84  ? 707 GLN   A C   1 
ATOM   3284 O  O   . GLN   A 1 411 ? -13.442 -12.763 21.618 1.00 77.68  ? 707 GLN   A O   1 
ATOM   3285 C  CB  . GLN   A 1 411 ? -15.341 -14.762 19.884 1.00 76.47  ? 707 GLN   A CB  1 
ATOM   3286 C  CG  . GLN   A 1 411 ? -15.298 -13.467 19.126 1.00 72.88  ? 707 GLN   A CG  1 
ATOM   3287 C  CD  . GLN   A 1 411 ? -15.898 -13.588 17.732 1.00 71.45  ? 707 GLN   A CD  1 
ATOM   3288 O  OE1 . GLN   A 1 411 ? -15.870 -14.658 17.122 1.00 71.31  ? 707 GLN   A OE1 1 
ATOM   3289 N  NE2 . GLN   A 1 411 ? -16.454 -12.491 17.232 1.00 67.80  ? 707 GLN   A NE2 1 
ATOM   3290 N  N   . PRO   A 1 412 ? -12.443 -14.748 21.312 1.00 80.10  ? 708 PRO   A N   1 
ATOM   3291 C  CA  . PRO   A 1 412 ? -11.106 -14.154 21.401 1.00 82.55  ? 708 PRO   A CA  1 
ATOM   3292 C  C   . PRO   A 1 412 ? -10.914 -13.064 20.361 1.00 84.57  ? 708 PRO   A C   1 
ATOM   3293 O  O   . PRO   A 1 412 ? -11.527 -13.078 19.292 1.00 83.66  ? 708 PRO   A O   1 
ATOM   3294 C  CB  . PRO   A 1 412 ? -10.168 -15.339 21.136 1.00 88.08  ? 708 PRO   A CB  1 
ATOM   3295 C  CG  . PRO   A 1 412 ? -10.979 -16.557 21.411 1.00 88.75  ? 708 PRO   A CG  1 
ATOM   3296 C  CD  . PRO   A 1 412 ? -12.399 -16.203 21.085 1.00 85.36  ? 708 PRO   A CD  1 
ATOM   3297 N  N   . ASP   A 1 413 ? -10.056 -12.111 20.691 1.00 87.20  ? 709 ASP   A N   1 
ATOM   3298 C  CA  . ASP   A 1 413 ? -9.646  -11.136 19.701 1.00 87.70  ? 709 ASP   A CA  1 
ATOM   3299 C  C   . ASP   A 1 413 ? -8.915  -11.851 18.568 1.00 91.35  ? 709 ASP   A C   1 
ATOM   3300 O  O   . ASP   A 1 413 ? -8.071  -12.721 18.819 1.00 94.72  ? 709 ASP   A O   1 
ATOM   3301 C  CB  . ASP   A 1 413 ? -8.757  -10.066 20.326 1.00 90.99  ? 709 ASP   A CB  1 
ATOM   3302 C  CG  . ASP   A 1 413 ? -9.534  -9.114  21.223 1.00 92.97  ? 709 ASP   A CG  1 
ATOM   3303 O  OD1 . ASP   A 1 413 ? -10.708 -8.815  20.905 1.00 90.50  ? 709 ASP   A OD1 1 
ATOM   3304 O  OD2 . ASP   A 1 413 ? -8.974  -8.669  22.249 1.00 95.32  ? 709 ASP   A OD2 1 
ATOM   3305 N  N   . PRO   A 1 414 ? -9.221  -11.524 17.316 1.00 91.76  ? 710 PRO   A N   1 
ATOM   3306 C  CA  . PRO   A 1 414 ? -8.726  -12.355 16.205 1.00 94.33  ? 710 PRO   A CA  1 
ATOM   3307 C  C   . PRO   A 1 414 ? -7.213  -12.373 16.068 1.00 100.15 ? 710 PRO   A C   1 
ATOM   3308 O  O   . PRO   A 1 414 ? -6.667  -13.351 15.538 1.00 104.29 ? 710 PRO   A O   1 
ATOM   3309 C  CB  . PRO   A 1 414 ? -9.403  -11.736 14.971 1.00 87.21  ? 710 PRO   A CB  1 
ATOM   3310 C  CG  . PRO   A 1 414 ? -9.852  -10.383 15.396 1.00 86.04  ? 710 PRO   A CG  1 
ATOM   3311 C  CD  . PRO   A 1 414 ? -10.132 -10.457 16.868 1.00 88.82  ? 710 PRO   A CD  1 
ATOM   3312 N  N   . TRP   A 1 415 ? -6.513  -11.333 16.522 1.00 98.20  ? 711 TRP   A N   1 
ATOM   3313 C  CA  . TRP   A 1 415 ? -5.064  -11.313 16.362 1.00 101.88 ? 711 TRP   A CA  1 
ATOM   3314 C  C   . TRP   A 1 415 ? -4.345  -12.259 17.317 1.00 103.49 ? 711 TRP   A C   1 
ATOM   3315 O  O   . TRP   A 1 415 ? -3.161  -12.543 17.103 1.00 105.16 ? 711 TRP   A O   1 
ATOM   3316 C  CB  . TRP   A 1 415 ? -4.522  -9.887  16.529 1.00 100.46 ? 711 TRP   A CB  1 
ATOM   3317 C  CG  . TRP   A 1 415 ? -4.922  -9.199  17.797 1.00 95.79  ? 711 TRP   A CG  1 
ATOM   3318 C  CD1 . TRP   A 1 415 ? -4.239  -9.198  18.981 1.00 97.37  ? 711 TRP   A CD1 1 
ATOM   3319 C  CD2 . TRP   A 1 415 ? -6.092  -8.398  18.010 1.00 93.53  ? 711 TRP   A CD2 1 
ATOM   3320 N  NE1 . TRP   A 1 415 ? -4.915  -8.453  19.917 1.00 98.19  ? 711 TRP   A NE1 1 
ATOM   3321 C  CE2 . TRP   A 1 415 ? -6.055  -7.950  19.346 1.00 95.65  ? 711 TRP   A CE2 1 
ATOM   3322 C  CE3 . TRP   A 1 415 ? -7.169  -8.020  17.202 1.00 92.02  ? 711 TRP   A CE3 1 
ATOM   3323 C  CZ2 . TRP   A 1 415 ? -7.051  -7.141  19.890 1.00 94.20  ? 711 TRP   A CZ2 1 
ATOM   3324 C  CZ3 . TRP   A 1 415 ? -8.156  -7.221  17.741 1.00 90.31  ? 711 TRP   A CZ3 1 
ATOM   3325 C  CH2 . TRP   A 1 415 ? -8.092  -6.791  19.074 1.00 93.63  ? 711 TRP   A CH2 1 
ATOM   3326 N  N   . ASN   A 1 416 ? -5.022  -12.760 18.352 1.00 103.47 ? 712 ASN   A N   1 
ATOM   3327 C  CA  . ASN   A 1 416 ? -4.428  -13.784 19.203 1.00 106.57 ? 712 ASN   A CA  1 
ATOM   3328 C  C   . ASN   A 1 416 ? -4.551  -15.179 18.609 1.00 110.81 ? 712 ASN   A C   1 
ATOM   3329 O  O   . ASN   A 1 416 ? -3.862  -16.096 19.067 1.00 113.62 ? 712 ASN   A O   1 
ATOM   3330 C  CB  . ASN   A 1 416 ? -5.079  -13.775 20.592 1.00 105.21 ? 712 ASN   A CB  1 
ATOM   3331 C  CG  . ASN   A 1 416 ? -4.982  -12.426 21.277 1.00 102.91 ? 712 ASN   A CG  1 
ATOM   3332 O  OD1 . ASN   A 1 416 ? -4.029  -11.673 21.058 1.00 104.50 ? 712 ASN   A OD1 1 
ATOM   3333 N  ND2 . ASN   A 1 416 ? -5.967  -12.113 22.117 1.00 99.73  ? 712 ASN   A ND2 1 
ATOM   3334 N  N   . THR   A 1 417 ? -5.395  -15.351 17.591 1.00 115.12 ? 713 THR   A N   1 
ATOM   3335 C  CA  . THR   A 1 417 ? -5.817  -16.663 17.127 1.00 116.01 ? 713 THR   A CA  1 
ATOM   3336 C  C   . THR   A 1 417 ? -5.634  -16.893 15.631 1.00 119.12 ? 713 THR   A C   1 
ATOM   3337 O  O   . THR   A 1 417 ? -5.858  -18.017 15.167 1.00 124.38 ? 713 THR   A O   1 
ATOM   3338 C  CB  . THR   A 1 417 ? -7.296  -16.879 17.482 1.00 119.67 ? 713 THR   A CB  1 
ATOM   3339 O  OG1 . THR   A 1 417 ? -8.048  -15.723 17.092 1.00 115.92 ? 713 THR   A OG1 1 
ATOM   3340 C  CG2 . THR   A 1 417 ? -7.464  -17.092 18.983 1.00 115.83 ? 713 THR   A CG2 1 
ATOM   3341 N  N   . HIS   A 1 418 ? -5.222  -15.883 14.868 1.00 116.84 ? 714 HIS   A N   1 
ATOM   3342 C  CA  . HIS   A 1 418 ? -5.230  -15.943 13.408 1.00 117.81 ? 714 HIS   A CA  1 
ATOM   3343 C  C   . HIS   A 1 418 ? -3.878  -16.440 12.906 1.00 120.57 ? 714 HIS   A C   1 
ATOM   3344 O  O   . HIS   A 1 418 ? -2.888  -15.701 12.936 1.00 124.38 ? 714 HIS   A O   1 
ATOM   3345 C  CB  . HIS   A 1 418 ? -5.571  -14.567 12.836 1.00 114.51 ? 714 HIS   A CB  1 
ATOM   3346 C  CG  . HIS   A 1 418 ? -5.427  -14.465 11.349 1.00 115.74 ? 714 HIS   A CG  1 
ATOM   3347 N  ND1 . HIS   A 1 418 ? -5.768  -15.490 10.494 1.00 114.85 ? 714 HIS   A ND1 1 
ATOM   3348 C  CD2 . HIS   A 1 418 ? -4.989  -13.451 10.564 1.00 118.27 ? 714 HIS   A CD2 1 
ATOM   3349 C  CE1 . HIS   A 1 418 ? -5.539  -15.116 9.247  1.00 112.75 ? 714 HIS   A CE1 1 
ATOM   3350 N  NE2 . HIS   A 1 418 ? -5.066  -13.883 9.262  1.00 113.75 ? 714 HIS   A NE2 1 
ATOM   3351 N  N   . VAL   A 1 419 ? -3.836  -17.694 12.448 1.00 124.01 ? 715 VAL   A N   1 
ATOM   3352 C  CA  . VAL   A 1 419 ? -2.642  -18.234 11.803 1.00 126.25 ? 715 VAL   A CA  1 
ATOM   3353 C  C   . VAL   A 1 419 ? -2.321  -17.339 10.614 1.00 130.87 ? 715 VAL   A C   1 
ATOM   3354 O  O   . VAL   A 1 419 ? -3.014  -17.368 9.591  1.00 126.67 ? 715 VAL   A O   1 
ATOM   3355 C  CB  . VAL   A 1 419 ? -2.831  -19.702 11.378 1.00 123.95 ? 715 VAL   A CB  1 
ATOM   3356 C  CG1 . VAL   A 1 419 ? -1.672  -20.154 10.524 1.00 126.75 ? 715 VAL   A CG1 1 
ATOM   3357 C  CG2 . VAL   A 1 419 ? -2.967  -20.609 12.602 1.00 120.19 ? 715 VAL   A CG2 1 
ATOM   3358 N  N   . TRP   A 1 420 ? -1.274  -16.530 10.753 1.00 143.48 ? 716 TRP   A N   1 
ATOM   3359 C  CA  . TRP   A 1 420 ? -1.050  -15.382 9.891  1.00 147.42 ? 716 TRP   A CA  1 
ATOM   3360 C  C   . TRP   A 1 420 ? -0.183  -15.743 8.685  1.00 162.01 ? 716 TRP   A C   1 
ATOM   3361 O  O   . TRP   A 1 420 ? 0.219   -16.894 8.494  1.00 164.71 ? 716 TRP   A O   1 
ATOM   3362 C  CB  . TRP   A 1 420 ? -0.412  -14.253 10.695 1.00 146.53 ? 716 TRP   A CB  1 
ATOM   3363 C  CG  . TRP   A 1 420 ? -1.005  -12.913 10.423 1.00 143.57 ? 716 TRP   A CG  1 
ATOM   3364 C  CD1 . TRP   A 1 420 ? -1.266  -12.362 9.202  1.00 143.21 ? 716 TRP   A CD1 1 
ATOM   3365 C  CD2 . TRP   A 1 420 ? -1.398  -11.941 11.393 1.00 142.37 ? 716 TRP   A CD2 1 
ATOM   3366 N  NE1 . TRP   A 1 420 ? -1.806  -11.108 9.352  1.00 139.99 ? 716 TRP   A NE1 1 
ATOM   3367 C  CE2 . TRP   A 1 420 ? -1.896  -10.826 10.689 1.00 140.27 ? 716 TRP   A CE2 1 
ATOM   3368 C  CE3 . TRP   A 1 420 ? -1.382  -11.906 12.788 1.00 144.07 ? 716 TRP   A CE3 1 
ATOM   3369 C  CZ2 . TRP   A 1 420 ? -2.370  -9.691  11.333 1.00 139.98 ? 716 TRP   A CZ2 1 
ATOM   3370 C  CZ3 . TRP   A 1 420 ? -1.852  -10.778 13.427 1.00 144.32 ? 716 TRP   A CZ3 1 
ATOM   3371 C  CH2 . TRP   A 1 420 ? -2.338  -9.685  12.700 1.00 143.91 ? 716 TRP   A CH2 1 
ATOM   3372 N  N   . LYS   A 1 421 ? 0.106   -14.733 7.861  1.00 138.02 ? 717 LYS   A N   1 
ATOM   3373 C  CA  . LYS   A 1 421 ? 0.959   -14.862 6.676  1.00 128.86 ? 717 LYS   A CA  1 
ATOM   3374 C  C   . LYS   A 1 421 ? 1.636   -13.534 6.320  1.00 123.46 ? 717 LYS   A C   1 
ATOM   3375 O  O   . LYS   A 1 421 ? 1.648   -13.106 5.160  1.00 114.46 ? 717 LYS   A O   1 
ATOM   3376 C  CB  . LYS   A 1 421 ? 0.149   -15.364 5.485  1.00 123.35 ? 717 LYS   A CB  1 
ATOM   3377 C  CG  . LYS   A 1 421 ? -0.062  -16.864 5.472  1.00 121.49 ? 717 LYS   A CG  1 
ATOM   3378 C  CD  . LYS   A 1 421 ? -1.428  -17.223 4.915  1.00 120.12 ? 717 LYS   A CD  1 
ATOM   3379 C  CE  . LYS   A 1 421 ? -1.521  -18.707 4.569  1.00 114.82 ? 717 LYS   A CE  1 
ATOM   3380 N  NZ  . LYS   A 1 421 ? -0.959  -19.015 3.216  1.00 110.09 ? 717 LYS   A NZ  1 
HETATM 3381 C  CHA . HEM   B 2 .   ? -25.027 -4.382  26.034 1.00 59.47  ? 801 HEM   A CHA 1 
HETATM 3382 C  CHB . HEM   B 2 .   ? -28.171 -0.734  25.711 1.00 59.52  ? 801 HEM   A CHB 1 
HETATM 3383 C  CHC . HEM   B 2 .   ? -29.504 -2.331  21.316 1.00 55.78  ? 801 HEM   A CHC 1 
HETATM 3384 C  CHD . HEM   B 2 .   ? -27.107 -6.447  22.149 1.00 57.25  ? 801 HEM   A CHD 1 
HETATM 3385 C  C1A . HEM   B 2 .   ? -25.669 -3.192  26.253 1.00 56.96  ? 801 HEM   A C1A 1 
HETATM 3386 C  C2A . HEM   B 2 .   ? -25.332 -2.200  27.260 1.00 60.92  ? 801 HEM   A C2A 1 
HETATM 3387 C  C3A . HEM   B 2 .   ? -26.192 -1.196  27.175 1.00 60.29  ? 801 HEM   A C3A 1 
HETATM 3388 C  C4A . HEM   B 2 .   ? -27.120 -1.512  26.108 1.00 59.42  ? 801 HEM   A C4A 1 
HETATM 3389 C  CMA . HEM   B 2 .   ? -26.189 0.073   28.069 1.00 57.79  ? 801 HEM   A CMA 1 
HETATM 3390 C  CAA . HEM   B 2 .   ? -24.150 -2.268  28.235 1.00 58.70  ? 801 HEM   A CAA 1 
HETATM 3391 C  CBA . HEM   B 2 .   ? -22.961 -1.932  27.328 1.00 59.64  ? 801 HEM   A CBA 1 
HETATM 3392 C  CGA . HEM   B 2 .   ? -21.715 -1.822  28.159 1.00 61.57  ? 801 HEM   A CGA 1 
HETATM 3393 O  O1A . HEM   B 2 .   ? -21.831 -1.542  29.384 1.00 56.89  ? 801 HEM   A O1A 1 
HETATM 3394 O  O2A . HEM   B 2 .   ? -20.610 -2.019  27.602 1.00 63.07  ? 801 HEM   A O2A 1 
HETATM 3395 C  C1B . HEM   B 2 .   ? -28.763 -0.816  24.481 1.00 58.65  ? 801 HEM   A C1B 1 
HETATM 3396 C  C2B . HEM   B 2 .   ? -29.625 0.190   23.906 1.00 57.85  ? 801 HEM   A C2B 1 
HETATM 3397 C  C3B . HEM   B 2 .   ? -30.007 -0.264  22.707 1.00 61.77  ? 801 HEM   A C3B 1 
HETATM 3398 C  C4B . HEM   B 2 .   ? -29.380 -1.555  22.455 1.00 58.69  ? 801 HEM   A C4B 1 
HETATM 3399 C  CMB . HEM   B 2 .   ? -30.061 1.520   24.568 1.00 61.00  ? 801 HEM   A CMB 1 
HETATM 3400 C  CAB . HEM   B 2 .   ? -30.940 0.510   21.749 1.00 64.09  ? 801 HEM   A CAB 1 
HETATM 3401 C  CBB . HEM   B 2 .   ? -31.690 -0.136  20.857 1.00 66.31  ? 801 HEM   A CBB 1 
HETATM 3402 C  C1C . HEM   B 2 .   ? -28.956 -3.572  21.130 1.00 55.36  ? 801 HEM   A C1C 1 
HETATM 3403 C  C2C . HEM   B 2 .   ? -29.047 -4.395  19.929 1.00 59.19  ? 801 HEM   A C2C 1 
HETATM 3404 C  C3C . HEM   B 2 .   ? -28.365 -5.539  20.151 1.00 54.91  ? 801 HEM   A C3C 1 
HETATM 3405 C  C4C . HEM   B 2 .   ? -27.846 -5.476  21.516 1.00 58.59  ? 801 HEM   A C4C 1 
HETATM 3406 C  CMC . HEM   B 2 .   ? -29.794 -3.893  18.679 1.00 59.24  ? 801 HEM   A CMC 1 
HETATM 3407 C  CAC . HEM   B 2 .   ? -28.142 -6.790  19.286 1.00 57.69  ? 801 HEM   A CAC 1 
HETATM 3408 C  CBC . HEM   B 2 .   ? -28.972 -7.130  18.292 1.00 58.93  ? 801 HEM   A CBC 1 
HETATM 3409 C  C1D . HEM   B 2 .   ? -26.358 -6.258  23.291 1.00 60.86  ? 801 HEM   A C1D 1 
HETATM 3410 C  C2D . HEM   B 2 .   ? -25.504 -7.234  23.907 1.00 58.82  ? 801 HEM   A C2D 1 
HETATM 3411 C  C3D . HEM   B 2 .   ? -24.933 -6.652  24.970 1.00 58.07  ? 801 HEM   A C3D 1 
HETATM 3412 C  C4D . HEM   B 2 .   ? -25.391 -5.296  25.058 1.00 58.95  ? 801 HEM   A C4D 1 
HETATM 3413 C  CMD . HEM   B 2 .   ? -25.325 -8.672  23.408 1.00 59.72  ? 801 HEM   A CMD 1 
HETATM 3414 C  CAD . HEM   B 2 .   ? -23.984 -7.288  26.017 1.00 59.33  ? 801 HEM   A CAD 1 
HETATM 3415 C  CBD . HEM   B 2 .   ? -22.561 -7.320  25.504 1.00 66.56  ? 801 HEM   A CBD 1 
HETATM 3416 C  CGD . HEM   B 2 .   ? -21.772 -8.069  26.543 1.00 68.71  ? 801 HEM   A CGD 1 
HETATM 3417 O  O1D . HEM   B 2 .   ? -20.643 -7.582  26.799 1.00 74.00  ? 801 HEM   A O1D 1 
HETATM 3418 O  O2D . HEM   B 2 .   ? -22.238 -9.121  27.101 1.00 67.68  ? 801 HEM   A O2D 1 
HETATM 3419 N  NA  . HEM   B 2 .   ? -26.788 -2.743  25.582 1.00 60.73  ? 801 HEM   A NA  1 
HETATM 3420 N  NB  . HEM   B 2 .   ? -28.625 -1.870  23.579 1.00 60.84  ? 801 HEM   A NB  1 
HETATM 3421 N  NC  . HEM   B 2 .   ? -28.226 -4.273  22.068 1.00 59.07  ? 801 HEM   A NC  1 
HETATM 3422 N  ND  . HEM   B 2 .   ? -26.266 -5.084  24.033 1.00 54.92  ? 801 HEM   A ND  1 
HETATM 3423 FE FE  . HEM   B 2 .   ? -27.763 -3.723  24.041 1.00 53.05  ? 801 HEM   A FE  1 
HETATM 3424 N  N1  . H4B   C 3 .   ? -21.857 -3.230  33.705 1.00 59.21  ? 802 H4B   A N1  1 
HETATM 3425 C  C2  . H4B   C 3 .   ? -21.901 -2.729  32.430 1.00 56.25  ? 802 H4B   A C2  1 
HETATM 3426 N  N2  . H4B   C 3 .   ? -23.078 -2.328  31.893 1.00 51.83  ? 802 H4B   A N2  1 
HETATM 3427 N  N3  . H4B   C 3 .   ? -20.773 -2.598  31.714 1.00 56.68  ? 802 H4B   A N3  1 
HETATM 3428 C  C4  . H4B   C 3 .   ? -19.573 -2.979  32.179 1.00 58.00  ? 802 H4B   A C4  1 
HETATM 3429 O  O4  . H4B   C 3 .   ? -18.522 -2.863  31.500 1.00 55.64  ? 802 H4B   A O4  1 
HETATM 3430 C  C4A . H4B   C 3 .   ? -19.505 -3.515  33.453 1.00 58.76  ? 802 H4B   A C4A 1 
HETATM 3431 C  C8A . H4B   C 3 .   ? -20.664 -3.620  34.216 1.00 58.29  ? 802 H4B   A C8A 1 
HETATM 3432 N  N5  . H4B   C 3 .   ? -18.321 -3.911  33.954 1.00 57.01  ? 802 H4B   A N5  1 
HETATM 3433 N  N8  . H4B   C 3 .   ? -20.622 -4.139  35.461 1.00 54.60  ? 802 H4B   A N8  1 
HETATM 3434 C  C6  . H4B   C 3 .   ? -18.411 -4.926  35.002 1.00 60.51  ? 802 H4B   A C6  1 
HETATM 3435 C  C7  . H4B   C 3 .   ? -19.349 -4.429  36.084 1.00 57.61  ? 802 H4B   A C7  1 
HETATM 3436 C  C9  . H4B   C 3 .   ? -17.090 -5.244  35.682 1.00 57.56  ? 802 H4B   A C9  1 
HETATM 3437 O  O9  . H4B   C 3 .   ? -16.560 -3.981  36.073 1.00 60.19  ? 802 H4B   A O9  1 
HETATM 3438 C  C10 . H4B   C 3 .   ? -17.353 -6.151  36.900 1.00 58.89  ? 802 H4B   A C10 1 
HETATM 3439 C  C11 . H4B   C 3 .   ? -16.129 -6.353  37.800 1.00 61.05  ? 802 H4B   A C11 1 
HETATM 3440 O  O10 . H4B   C 3 .   ? -17.850 -7.448  36.520 1.00 58.56  ? 802 H4B   A O10 1 
HETATM 3441 ZN ZN  . ZN    D 4 .   ? -24.334 -16.579 40.816 0.41 54.78  ? 803 ZN    A ZN  1 
HETATM 3442 C  C11 . A1A0D E 5 .   ? -22.378 -1.528  23.513 1.00 64.32  ? 804 A1A0D A C11 1 
HETATM 3443 C  C12 . A1A0D E 5 .   ? -21.396 -0.568  23.471 1.00 64.82  ? 804 A1A0D A C12 1 
HETATM 3444 C  C13 . A1A0D E 5 .   ? -20.123 -0.852  23.904 1.00 68.27  ? 804 A1A0D A C13 1 
HETATM 3445 C  C15 . A1A0D E 5 .   ? -20.814 -3.091  24.447 1.00 67.10  ? 804 A1A0D A C15 1 
HETATM 3446 C  C16 . A1A0D E 5 .   ? -22.101 -2.804  23.997 1.00 62.53  ? 804 A1A0D A C16 1 
HETATM 3447 C  C17 . A1A0D E 5 .   ? -20.455 -4.451  24.994 1.00 73.06  ? 804 A1A0D A C17 1 
HETATM 3448 C  C19 . A1A0D E 5 .   ? -18.859 -6.179  24.446 1.00 86.60  ? 804 A1A0D A C19 1 
HETATM 3449 C  C20 . A1A0D E 5 .   ? -17.758 -6.069  25.485 1.00 88.10  ? 804 A1A0D A C20 1 
HETATM 3450 C  C21 . A1A0D E 5 .   ? -18.102 -4.610  25.706 1.00 84.86  ? 804 A1A0D A C21 1 
HETATM 3451 C  C02 . A1A0D E 5 .   ? -25.608 0.280   23.118 1.00 61.06  ? 804 A1A0D A C02 1 
HETATM 3452 C  C03 . A1A0D E 5 .   ? -26.222 -0.458  22.101 1.00 58.17  ? 804 A1A0D A C03 1 
HETATM 3453 C  C04 . A1A0D E 5 .   ? -25.552 -1.542  21.546 1.00 60.72  ? 804 A1A0D A C04 1 
HETATM 3454 C  C05 . A1A0D E 5 .   ? -24.302 -1.895  22.016 1.00 60.67  ? 804 A1A0D A C05 1 
HETATM 3455 C  C06 . A1A0D E 5 .   ? -23.726 -1.149  23.029 1.00 62.11  ? 804 A1A0D A C06 1 
HETATM 3456 C  C07 . A1A0D E 5 .   ? -26.157 -2.356  20.428 1.00 58.15  ? 804 A1A0D A C07 1 
HETATM 3457 C  C14 . A1A0D E 5 .   ? -19.831 -2.115  24.387 1.00 69.19  ? 804 A1A0D A C14 1 
HETATM 3458 F  F12 . A1A0D E 5 .   ? -21.674 0.651   22.986 1.00 65.95  ? 804 A1A0D A F12 1 
HETATM 3459 F  F13 . A1A0D E 5 .   ? -19.185 0.104   23.845 1.00 80.35  ? 804 A1A0D A F13 1 
HETATM 3460 F  F22 . A1A0D E 5 .   ? -17.961 -6.780  26.573 1.00 93.61  ? 804 A1A0D A F22 1 
HETATM 3461 F  F23 . A1A0D E 5 .   ? -16.568 -6.264  24.928 1.00 89.51  ? 804 A1A0D A F23 1 
HETATM 3462 N  N01 . A1A0D E 5 .   ? -24.375 -0.080  23.548 1.00 62.11  ? 804 A1A0D A N01 1 
HETATM 3463 N  N02 . A1A0D E 5 .   ? -26.231 1.342   23.684 1.00 58.46  ? 804 A1A0D A N02 1 
HETATM 3464 N  N18 . A1A0D E 5 .   ? -19.074 -4.728  24.596 1.00 79.46  ? 804 A1A0D A N18 1 
HETATM 3465 O  O   . HOH   F 6 .   ? -18.682 1.895   20.442 1.00 62.49  ? 901 HOH   A O   1 
HETATM 3466 O  O   . HOH   F 6 .   ? -28.543 0.861   15.335 1.00 58.86  ? 902 HOH   A O   1 
HETATM 3467 O  O   . HOH   F 6 .   ? -29.924 -13.129 40.320 1.00 62.13  ? 903 HOH   A O   1 
HETATM 3468 O  O   . HOH   F 6 .   ? -21.629 -14.839 -2.729 1.00 60.51  ? 904 HOH   A O   1 
HETATM 3469 O  O   . HOH   F 6 .   ? -38.538 -22.709 8.359  1.00 89.58  ? 905 HOH   A O   1 
HETATM 3470 O  O   . HOH   F 6 .   ? -14.181 13.469  14.497 1.00 100.80 ? 906 HOH   A O   1 
HETATM 3471 O  O   . HOH   F 6 .   ? -24.452 -10.939 37.558 1.00 54.41  ? 907 HOH   A O   1 
HETATM 3472 O  O   . HOH   F 6 .   ? -18.557 -1.813  28.972 1.00 62.99  ? 908 HOH   A O   1 
HETATM 3473 O  O   . HOH   F 6 .   ? -34.518 6.397   16.462 1.00 74.87  ? 909 HOH   A O   1 
HETATM 3474 O  O   . HOH   F 6 .   ? -19.669 -8.335  34.514 1.00 58.22  ? 910 HOH   A O   1 
HETATM 3475 O  O   . HOH   F 6 .   ? -11.035 -6.988  -0.943 1.00 93.35  ? 911 HOH   A O   1 
HETATM 3476 O  O   . HOH   F 6 .   ? -20.911 1.289   25.872 1.00 61.66  ? 912 HOH   A O   1 
HETATM 3477 O  O   . HOH   F 6 .   ? -14.569 -20.967 9.420  1.00 95.68  ? 913 HOH   A O   1 
HETATM 3478 O  O   . HOH   F 6 .   ? -35.092 -1.282  17.922 1.00 69.64  ? 914 HOH   A O   1 
HETATM 3479 O  O   . HOH   F 6 .   ? -11.892 10.333  35.231 1.00 89.75  ? 915 HOH   A O   1 
HETATM 3480 O  O   . HOH   F 6 .   ? -34.859 -11.784 35.790 1.00 64.22  ? 916 HOH   A O   1 
HETATM 3481 O  O   . HOH   F 6 .   ? -34.887 6.479   37.742 1.00 72.76  ? 917 HOH   A O   1 
HETATM 3482 O  O   . HOH   F 6 .   ? -18.947 3.095   24.003 1.00 68.23  ? 918 HOH   A O   1 
HETATM 3483 O  O   . HOH   F 6 .   ? -23.808 2.556   30.983 1.00 54.23  ? 919 HOH   A O   1 
HETATM 3484 O  O   . HOH   F 6 .   ? -27.897 -13.398 23.936 1.00 82.83  ? 920 HOH   A O   1 
HETATM 3485 O  O   . HOH   F 6 .   ? -25.319 -4.213  5.937  1.00 58.93  ? 921 HOH   A O   1 
HETATM 3486 O  O   . HOH   F 6 .   ? -29.661 -15.657 28.265 1.00 61.31  ? 922 HOH   A O   1 
HETATM 3487 O  O   . HOH   F 6 .   ? -23.489 -0.840  34.496 1.00 55.04  ? 923 HOH   A O   1 
HETATM 3488 O  O   . HOH   F 6 .   ? -28.363 -10.709 37.816 1.00 57.99  ? 924 HOH   A O   1 
HETATM 3489 O  O   . HOH   F 6 .   ? -27.285 -2.939  29.726 1.00 60.17  ? 925 HOH   A O   1 
HETATM 3490 O  O   . HOH   F 6 .   ? -15.528 3.436   22.243 1.00 79.05  ? 926 HOH   A O   1 
HETATM 3491 O  O   . HOH   F 6 .   ? -24.298 -12.535 32.260 1.00 62.65  ? 927 HOH   A O   1 
HETATM 3492 O  O   . HOH   F 6 .   ? -17.209 -16.658 9.530  1.00 78.37  ? 928 HOH   A O   1 
HETATM 3493 O  O   . HOH   F 6 .   ? -21.656 -10.144 35.139 1.00 56.62  ? 929 HOH   A O   1 
HETATM 3494 O  O   . HOH   F 6 .   ? -21.942 1.079   30.126 1.00 54.50  ? 930 HOH   A O   1 
HETATM 3495 O  O   . HOH   F 6 .   ? -22.949 6.947   12.008 1.00 60.76  ? 931 HOH   A O   1 
HETATM 3496 O  O   . HOH   F 6 .   ? -24.525 -12.831 29.353 1.00 80.70  ? 932 HOH   A O   1 
HETATM 3497 O  O   . HOH   F 6 .   ? -29.755 22.587  18.709 1.00 88.86  ? 933 HOH   A O   1 
HETATM 3498 O  O   . HOH   F 6 .   ? -41.209 -5.970  38.799 1.00 73.59  ? 934 HOH   A O   1 
HETATM 3499 O  O   . HOH   F 6 .   ? -27.271 -1.002  31.879 1.00 54.33  ? 935 HOH   A O   1 
HETATM 3500 O  O   . HOH   F 6 .   ? -26.356 -34.964 13.806 1.00 120.28 ? 936 HOH   A O   1 
HETATM 3501 O  O   . HOH   F 6 .   ? -20.414 -8.356  16.867 1.00 59.10  ? 937 HOH   A O   1 
HETATM 3502 O  O   . HOH   F 6 .   ? -21.569 0.504   32.769 1.00 56.36  ? 938 HOH   A O   1 
HETATM 3503 O  O   . HOH   F 6 .   ? -8.421  -17.036 11.148 1.00 101.38 ? 939 HOH   A O   1 
HETATM 3504 O  O   . HOH   F 6 .   ? -43.062 -14.560 23.138 1.00 85.21  ? 940 HOH   A O   1 
HETATM 3505 O  O   . HOH   F 6 .   ? -24.976 -10.556 27.298 1.00 60.87  ? 941 HOH   A O   1 
HETATM 3506 O  O   . HOH   F 6 .   ? -37.537 -7.985  10.665 1.00 70.85  ? 942 HOH   A O   1 
HETATM 3507 O  O   . HOH   F 6 .   ? -35.613 -7.370  9.219  1.00 69.20  ? 943 HOH   A O   1 
HETATM 3508 O  O   . HOH   F 6 .   ? -28.680 1.226   3.611  1.00 71.09  ? 944 HOH   A O   1 
HETATM 3509 O  O   . HOH   F 6 .   ? -25.196 0.297   32.393 1.00 58.04  ? 945 HOH   A O   1 
HETATM 3510 O  O   . HOH   F 6 .   ? -45.386 -13.444 36.140 1.00 94.31  ? 946 HOH   A O   1 
HETATM 3511 O  O   . HOH   F 6 .   ? -17.397 0.943   28.771 1.00 63.95  ? 947 HOH   A O   1 
HETATM 3512 O  O   . HOH   F 6 .   ? -28.555 -1.294  2.516  1.00 73.32  ? 948 HOH   A O   1 
HETATM 3513 O  O   . HOH   F 6 .   ? -34.703 1.896   25.331 1.00 75.78  ? 949 HOH   A O   1 
HETATM 3514 O  O   . HOH   F 6 .   ? -43.774 -12.614 21.719 1.00 83.78  ? 950 HOH   A O   1 
HETATM 3515 O  O   . HOH   F 6 .   ? -14.792 15.698  11.864 1.00 88.52  ? 951 HOH   A O   1 
HETATM 3516 O  O   . HOH   F 6 .   ? -31.492 -0.529  3.356  1.00 71.71  ? 952 HOH   A O   1 
# 
loop_
_atom_site_anisotrop.id 
_atom_site_anisotrop.type_symbol 
_atom_site_anisotrop.pdbx_label_atom_id 
_atom_site_anisotrop.pdbx_label_alt_id 
_atom_site_anisotrop.pdbx_label_comp_id 
_atom_site_anisotrop.pdbx_label_asym_id 
_atom_site_anisotrop.pdbx_label_seq_id 
_atom_site_anisotrop.pdbx_PDB_ins_code 
_atom_site_anisotrop.U[1][1] 
_atom_site_anisotrop.U[2][2] 
_atom_site_anisotrop.U[3][3] 
_atom_site_anisotrop.U[1][2] 
_atom_site_anisotrop.U[1][3] 
_atom_site_anisotrop.U[2][3] 
_atom_site_anisotrop.pdbx_auth_seq_id 
_atom_site_anisotrop.pdbx_auth_comp_id 
_atom_site_anisotrop.pdbx_auth_asym_id 
_atom_site_anisotrop.pdbx_auth_atom_id 
1    N N   . ARG A 3   ? 2.1350 1.9318 1.6384 -0.6437 0.0300  0.0623  299 ARG A N   
2    C CA  . ARG A 3   ? 2.1756 1.9466 1.6844 -0.6367 0.0198  0.0514  299 ARG A CA  
3    C C   . ARG A 3   ? 1.9946 1.9206 1.5878 -0.6421 0.0240  0.0408  299 ARG A C   
4    O O   . ARG A 3   ? 2.0290 1.9575 1.6243 -0.6482 0.0172  0.0320  299 ARG A O   
5    C CB  . ARG A 3   ? 2.3412 2.0023 1.7495 -0.6711 0.0129  0.0516  299 ARG A CB  
6    C CG  . ARG A 3   ? 2.4008 1.9438 1.7707 -0.6420 0.0005  0.0460  299 ARG A CG  
7    C CD  . ARG A 3   ? 2.4723 1.9210 1.8312 -0.5869 -0.0054 0.0516  299 ARG A CD  
8    N NE  . ARG A 3   ? 2.2909 1.7821 1.7281 -0.5352 -0.0105 0.0422  299 ARG A NE  
9    C CZ  . ARG A 3   ? 2.3284 1.7579 1.7514 -0.5087 -0.0199 0.0336  299 ARG A CZ  
10   N NH1 . ARG A 3   ? 2.4464 1.7626 1.7770 -0.5271 -0.0250 0.0330  299 ARG A NH1 
11   N NH2 . ARG A 3   ? 2.1701 1.6640 1.6747 -0.4511 -0.0238 0.0244  299 ARG A NH2 
12   N N   . PHE A 4   ? 1.6993 1.7549 1.3573 -0.6354 0.0353  0.0418  300 PHE A N   
13   C CA  . PHE A 4   ? 1.5104 1.7252 1.2506 -0.6251 0.0398  0.0324  300 PHE A CA  
14   C C   . PHE A 4   ? 1.3994 1.6886 1.2020 -0.5715 0.0472  0.0323  300 PHE A C   
15   O O   . PHE A 4   ? 1.3338 1.7273 1.1590 -0.5803 0.0602  0.0350  300 PHE A O   
16   C CB  . PHE A 4   ? 1.5297 1.8292 1.2529 -0.6698 0.0447  0.0318  300 PHE A CB  
17   C CG  . PHE A 4   ? 1.7017 1.8911 1.3250 -0.7229 0.0399  0.0370  300 PHE A CG  
18   C CD1 . PHE A 4   ? 1.7393 1.8760 1.3038 -0.7487 0.0449  0.0470  300 PHE A CD1 
19   C CD2 . PHE A 4   ? 1.7186 1.8538 1.3011 -0.7460 0.0302  0.0318  300 PHE A CD2 
20   C CE1 . PHE A 4   ? 1.8270 1.8568 1.2916 -0.7960 0.0394  0.0511  300 PHE A CE1 
21   C CE2 . PHE A 4   ? 1.8175 1.8460 1.2986 -0.7935 0.0257  0.0360  300 PHE A CE2 
22   C CZ  . PHE A 4   ? 1.8704 1.8451 1.2912 -0.8184 0.0298  0.0454  300 PHE A CZ  
23   N N   . LEU A 5   ? 1.3207 1.5514 1.1458 -0.5049 0.0372  0.0273  301 LEU A N   
24   C CA  . LEU A 5   ? 1.2244 1.4588 1.0745 -0.4477 0.0386  0.0279  301 LEU A CA  
25   C C   . LEU A 5   ? 1.1075 1.4745 1.0281 -0.4093 0.0449  0.0195  301 LEU A C   
26   O O   . LEU A 5   ? 1.0502 1.4919 1.0119 -0.4042 0.0432  0.0114  301 LEU A O   
27   C CB  . LEU A 5   ? 1.1971 1.3271 1.0425 -0.3973 0.0246  0.0259  301 LEU A CB  
28   C CG  . LEU A 5   ? 1.3350 1.3261 1.1042 -0.4176 0.0175  0.0341  301 LEU A CG  
29   C CD1 . LEU A 5   ? 1.2442 1.1638 1.0181 -0.3757 0.0038  0.0287  301 LEU A CD1 
30   C CD2 . LEU A 5   ? 1.3224 1.2635 1.0520 -0.4121 0.0202  0.0448  301 LEU A CD2 
31   N N   . LYS A 6   ? 1.0843 1.4726 1.0118 -0.3782 0.0513  0.0213  302 LYS A N   
32   C CA  . LYS A 6   ? 0.9996 1.4959 0.9767 -0.3344 0.0581  0.0136  302 LYS A CA  
33   C C   . LYS A 6   ? 0.9522 1.3957 0.9448 -0.2690 0.0482  0.0080  302 LYS A C   
34   O O   . LYS A 6   ? 0.9502 1.3039 0.9135 -0.2588 0.0426  0.0130  302 LYS A O   
35   C CB  . LYS A 6   ? 0.9740 1.5406 0.9394 -0.3494 0.0746  0.0187  302 LYS A CB  
36   C CG  . LYS A 6   ? 1.0365 1.6606 0.9797 -0.4233 0.0860  0.0263  302 LYS A CG  
37   C CD  . LYS A 6   ? 0.9637 1.7313 0.9550 -0.4313 0.0911  0.0192  302 LYS A CD  
38   C CE  . LYS A 6   ? 1.0068 1.8523 0.9764 -0.5018 0.1020  0.0258  302 LYS A CE  
39   N NZ  . LYS A 6   ? 0.9513 1.8427 0.9049 -0.5026 0.1166  0.0313  302 LYS A NZ  
40   N N   . VAL A 7   ? 0.8783 1.3784 0.9124 -0.2264 0.0455  -0.0018 303 VAL A N   
41   C CA  . VAL A 7   ? 0.8174 1.2801 0.8608 -0.1683 0.0377  -0.0076 303 VAL A CA  
42   C C   . VAL A 7   ? 0.8057 1.3558 0.8620 -0.1316 0.0480  -0.0138 303 VAL A C   
43   O O   . VAL A 7   ? 0.7989 1.4541 0.8785 -0.1348 0.0564  -0.0171 303 VAL A O   
44   C CB  . VAL A 7   ? 0.7943 1.2261 0.8603 -0.1462 0.0245  -0.0135 303 VAL A CB  
45   C CG1 . VAL A 7   ? 0.8277 1.1825 0.8774 -0.1792 0.0164  -0.0085 303 VAL A CG1 
46   C CG2 . VAL A 7   ? 0.7941 1.3218 0.8935 -0.1384 0.0274  -0.0202 303 VAL A CG2 
47   N N   . LYS A 8   ? 0.8093 1.3192 0.8464 -0.0966 0.0473  -0.0154 304 LYS A N   
48   C CA  . LYS A 8   ? 0.7652 1.3404 0.8019 -0.0539 0.0567  -0.0226 304 LYS A CA  
49   C C   . LYS A 8   ? 0.7487 1.2789 0.7826 0.0017  0.0457  -0.0316 304 LYS A C   
50   O O   . LYS A 8   ? 0.7422 1.1810 0.7677 0.0040  0.0317  -0.0307 304 LYS A O   
51   C CB  . LYS A 8   ? 0.8010 1.3651 0.8044 -0.0569 0.0663  -0.0187 304 LYS A CB  
52   C CG  . LYS A 8   ? 0.8038 1.4558 0.8035 -0.0173 0.0807  -0.0260 304 LYS A CG  
53   C CD  . LYS A 8   ? 0.8455 1.4979 0.8116 -0.0269 0.0927  -0.0216 304 LYS A CD  
54   C CE  . LYS A 8   ? 0.8799 1.6168 0.8378 0.0230  0.1072  -0.0308 304 LYS A CE  
55   N NZ  . LYS A 8   ? 0.9253 1.6359 0.8419 0.0275  0.1156  -0.0292 304 LYS A NZ  
56   N N   . ASN A 9   ? 0.7907 1.3871 0.8268 0.0465  0.0521  -0.0399 305 ASN A N   
57   C CA  . ASN A 9   ? 0.8155 1.3583 0.8255 0.1031  0.0443  -0.0485 305 ASN A CA  
58   C C   . ASN A 9   ? 0.8827 1.4224 0.8540 0.1297  0.0536  -0.0521 305 ASN A C   
59   O O   . ASN A 9   ? 0.8829 1.5182 0.8581 0.1377  0.0698  -0.0534 305 ASN A O   
60   C CB  . ASN A 9   ? 0.7972 1.3999 0.8211 0.1452  0.0437  -0.0560 305 ASN A CB  
61   C CG  . ASN A 9   ? 0.8489 1.3714 0.8315 0.2005  0.0336  -0.0640 305 ASN A CG  
62   O OD1 . ASN A 9   ? 0.9347 1.4319 0.8744 0.2363  0.0377  -0.0696 305 ASN A OD1 
63   N ND2 . ASN A 9   ? 0.8240 1.3004 0.8123 0.2059  0.0203  -0.0646 305 ASN A ND2 
64   N N   . TRP A 10  ? 0.8619 1.2974 0.7947 0.1415  0.0436  -0.0538 306 TRP A N   
65   C CA  . TRP A 10  ? 0.9331 1.3495 0.8212 0.1637  0.0505  -0.0577 306 TRP A CA  
66   C C   . TRP A 10  ? 0.9899 1.3833 0.8337 0.2289  0.0497  -0.0703 306 TRP A C   
67   O O   . TRP A 10  ? 1.0618 1.4289 0.8586 0.2537  0.0548  -0.0758 306 TRP A O   
68   C CB  . TRP A 10  ? 0.9468 1.2648 0.8109 0.1356  0.0392  -0.0522 306 TRP A CB  
69   C CG  . TRP A 10  ? 0.9082 1.2396 0.7979 0.0808  0.0415  -0.0399 306 TRP A CG  
70   C CD1 . TRP A 10  ? 0.8844 1.1878 0.8019 0.0469  0.0313  -0.0327 306 TRP A CD1 
71   C CD2 . TRP A 10  ? 0.9057 1.2746 0.7863 0.0547  0.0550  -0.0331 306 TRP A CD2 
72   N NE1 . TRP A 10  ? 0.8568 1.1676 0.7771 0.0036  0.0366  -0.0221 306 TRP A NE1 
73   C CE2 . TRP A 10  ? 0.8973 1.2470 0.7948 0.0046  0.0510  -0.0214 306 TRP A CE2 
74   C CE3 . TRP A 10  ? 0.9059 1.3192 0.7601 0.0697  0.0706  -0.0357 306 TRP A CE3 
75   C CZ2 . TRP A 10  ? 0.8944 1.2596 0.7786 -0.0338 0.0611  -0.0113 306 TRP A CZ2 
76   C CZ3 . TRP A 10  ? 0.9067 1.3467 0.7546 0.0291  0.0817  -0.0253 306 TRP A CZ3 
77   C CH2 . TRP A 10  ? 0.9011 1.3128 0.7617 -0.0237 0.0765  -0.0128 306 TRP A CH2 
78   N N   . GLU A 11  ? 0.9752 1.3680 0.8244 0.2585  0.0428  -0.0752 307 GLU A N   
79   C CA  . GLU A 11  ? 1.0424 1.4258 0.8439 0.3274  0.0444  -0.0868 307 GLU A CA  
80   C C   . GLU A 11  ? 1.0187 1.5420 0.8458 0.3607  0.0613  -0.0901 307 GLU A C   
81   O O   . GLU A 11  ? 1.0469 1.5893 0.8308 0.4216  0.0696  -0.0997 307 GLU A O   
82   C CB  . GLU A 11  ? 1.0531 1.3516 0.8340 0.3459  0.0270  -0.0896 307 GLU A CB  
83   C CG  . GLU A 11  ? 1.1045 1.3408 0.8084 0.4169  0.0239  -0.1014 307 GLU A CG  
84   C CD  . GLU A 11  ? 1.2012 1.3966 0.8948 0.4397  0.0111  -0.1024 307 GLU A CD  
85   O OE1 . GLU A 11  ? 1.1201 1.2983 0.8543 0.3951  0.0010  -0.0947 307 GLU A OE1 
86   O OE2 . GLU A 11  ? 1.2742 1.4534 0.9139 0.5059  0.0115  -0.1110 307 GLU A OE2 
87   N N   . THR A 12  ? 0.9808 1.6054 0.8735 0.3221  0.0665  -0.0827 308 THR A N   
88   C CA  . THR A 12  ? 0.9537 1.7279 0.8775 0.3471  0.0805  -0.0850 308 THR A CA  
89   C C   . THR A 12  ? 0.9361 1.8282 0.9018 0.2955  0.0972  -0.0773 308 THR A C   
90   O O   . THR A 12  ? 0.8915 1.9263 0.8842 0.3109  0.1103  -0.0788 308 THR A O   
91   C CB  . THR A 12  ? 0.9085 1.7171 0.8678 0.3510  0.0707  -0.0843 308 THR A CB  
92   O OG1 . THR A 12  ? 0.8894 1.6987 0.8969 0.2772  0.0654  -0.0744 308 THR A OG1 
93   C CG2 . THR A 12  ? 0.9934 1.6778 0.9058 0.3947  0.0538  -0.0899 308 THR A CG2 
94   N N   . ASP A 13  ? 1.0021 1.8416 0.9702 0.2345  0.0969  -0.0686 309 ASP A N   
95   C CA  . ASP A 13  ? 0.9515 1.8800 0.9470 0.1758  0.1116  -0.0593 309 ASP A CA  
96   C C   . ASP A 13  ? 0.9035 1.9232 0.9519 0.1315  0.1116  -0.0536 309 ASP A C   
97   O O   . ASP A 13  ? 0.9285 2.0484 0.9979 0.0847  0.1250  -0.0469 309 ASP A O   
98   C CB  . ASP A 13  ? 0.9990 2.0318 0.9796 0.2052  0.1328  -0.0632 309 ASP A CB  
99   C CG  . ASP A 13  ? 1.1184 2.0595 1.0425 0.2278  0.1349  -0.0665 309 ASP A CG  
100  O OD1 . ASP A 13  ? 1.1901 2.0437 1.1018 0.1798  0.1290  -0.0584 309 ASP A OD1 
101  O OD2 . ASP A 13  ? 1.1776 2.1327 1.0649 0.2953  0.1419  -0.0775 309 ASP A OD2 
102  N N   . VAL A 14  ? 0.8471 1.8342 0.9132 0.1414  0.0966  -0.0559 310 VAL A N   
103  C CA  . VAL A 14  ? 0.7771 1.8414 0.8881 0.0987  0.0946  -0.0516 310 VAL A CA  
104  C C   . VAL A 14  ? 0.7735 1.7575 0.8868 0.0245  0.0880  -0.0416 310 VAL A C   
105  O O   . VAL A 14  ? 0.7939 1.6485 0.8881 0.0241  0.0753  -0.0404 310 VAL A O   
106  C CB  . VAL A 14  ? 0.7708 1.8298 0.8947 0.1415  0.0812  -0.0581 310 VAL A CB  
107  C CG1 . VAL A 14  ? 0.7558 1.8605 0.9195 0.0886  0.0753  -0.0533 310 VAL A CG1 
108  C CG2 . VAL A 14  ? 0.7674 1.9285 0.8880 0.2141  0.0886  -0.0668 310 VAL A CG2 
109  N N   . VAL A 15  ? 0.7452 1.8059 0.8768 -0.0382 0.0963  -0.0344 311 VAL A N   
110  C CA  . VAL A 15  ? 0.7660 1.7492 0.8890 -0.1079 0.0903  -0.0251 311 VAL A CA  
111  C C   . VAL A 15  ? 0.7841 1.8081 0.9357 -0.1405 0.0828  -0.0252 311 VAL A C   
112  O O   . VAL A 15  ? 0.7841 1.9404 0.9651 -0.1377 0.0883  -0.0285 311 VAL A O   
113  C CB  . VAL A 15  ? 0.7592 1.7682 0.8604 -0.1639 0.1047  -0.0154 311 VAL A CB  
114  C CG1 . VAL A 15  ? 0.8152 1.7170 0.8906 -0.2282 0.0968  -0.0056 311 VAL A CG1 
115  C CG2 . VAL A 15  ? 0.7670 1.7474 0.8398 -0.1272 0.1126  -0.0163 311 VAL A CG2 
116  N N   . LEU A 16  ? 0.7769 1.6909 0.9183 -0.1684 0.0697  -0.0222 312 LEU A N   
117  C CA  . LEU A 16  ? 0.7710 1.6993 0.9281 -0.2064 0.0617  -0.0223 312 LEU A CA  
118  C C   . LEU A 16  ? 0.8222 1.6598 0.9444 -0.2733 0.0594  -0.0135 312 LEU A C   
119  O O   . LEU A 16  ? 0.8420 1.5731 0.9326 -0.2716 0.0573  -0.0087 312 LEU A O   
120  C CB  . LEU A 16  ? 0.7739 1.6485 0.9460 -0.1624 0.0468  -0.0291 312 LEU A CB  
121  C CG  . LEU A 16  ? 0.7629 1.7068 0.9554 -0.0924 0.0471  -0.0373 312 LEU A CG  
122  C CD1 . LEU A 16  ? 0.7408 1.6020 0.9338 -0.0519 0.0322  -0.0419 312 LEU A CD1 
123  C CD2 . LEU A 16  ? 0.7695 1.8696 0.9932 -0.0996 0.0530  -0.0398 312 LEU A CD2 
124  N N   . THR A 17  ? 0.8200 1.6986 0.9413 -0.3322 0.0592  -0.0114 313 THR A N   
125  C CA  . THR A 17  ? 0.8679 1.6517 0.9416 -0.3979 0.0566  -0.0036 313 THR A CA  
126  C C   . THR A 17  ? 0.8860 1.5857 0.9548 -0.3997 0.0414  -0.0077 313 THR A C   
127  O O   . THR A 17  ? 0.8462 1.6122 0.9437 -0.4016 0.0365  -0.0140 313 THR A O   
128  C CB  . THR A 17  ? 0.8901 1.7397 0.9396 -0.4626 0.0636  0.0012  313 THR A CB  
129  O OG1 . THR A 17  ? 0.8927 1.8178 0.9428 -0.4564 0.0772  0.0046  313 THR A OG1 
130  C CG2 . THR A 17  ? 0.9875 1.7097 0.9687 -0.5243 0.0589  0.0089  313 THR A CG2 
131  N N   . ASP A 18  ? 0.9525 1.5121 0.9835 -0.3968 0.0340  -0.0042 314 ASP A N   
132  C CA  . ASP A 18  ? 0.9770 1.4500 0.9986 -0.3912 0.0208  -0.0083 314 ASP A CA  
133  C C   . ASP A 18  ? 1.0280 1.4269 0.9895 -0.4580 0.0189  -0.0034 314 ASP A C   
134  O O   . ASP A 18  ? 1.1280 1.4347 1.0360 -0.4771 0.0204  0.0048  314 ASP A O   
135  C CB  . ASP A 18  ? 0.9792 1.3537 0.9975 -0.3383 0.0132  -0.0082 314 ASP A CB  
136  C CG  . ASP A 18  ? 0.9573 1.2650 0.9755 -0.3228 0.0011  -0.0134 314 ASP A CG  
137  O OD1 . ASP A 18  ? 0.9661 1.1986 0.9399 -0.3580 -0.0028 -0.0117 314 ASP A OD1 
138  O OD2 . ASP A 18  ? 0.8750 1.2016 0.9311 -0.2759 -0.0041 -0.0192 314 ASP A OD2 
139  N N   . THR A 19  ? 0.9514 1.3846 0.9142 -0.4935 0.0147  -0.0085 315 THR A N   
140  C CA  . THR A 19  ? 1.0210 1.3558 0.9143 -0.5460 0.0095  -0.0064 315 THR A CA  
141  C C   . THR A 19  ? 1.0098 1.2672 0.8972 -0.5282 -0.0028 -0.0142 315 THR A C   
142  O O   . THR A 19  ? 1.0625 1.2038 0.8807 -0.5537 -0.0079 -0.0130 315 THR A O   
143  C CB  . THR A 19  ? 1.0090 1.4126 0.8816 -0.5869 0.0127  -0.0063 315 THR A CB  
144  O OG1 . THR A 19  ? 0.9665 1.4688 0.8926 -0.5645 0.0088  -0.0148 315 THR A OG1 
145  C CG2 . THR A 19  ? 1.0594 1.5450 0.9342 -0.6031 0.0245  0.0002  315 THR A CG2 
146  N N   . LEU A 20  ? 0.9576 1.2657 0.9061 -0.4716 -0.0073 -0.0215 316 LEU A N   
147  C CA  . LEU A 20  ? 1.0013 1.2448 0.9469 -0.4463 -0.0177 -0.0287 316 LEU A CA  
148  C C   . LEU A 20  ? 1.0483 1.1507 0.9459 -0.4239 -0.0217 -0.0256 316 LEU A C   
149  O O   . LEU A 20  ? 1.0899 1.1122 0.9523 -0.4248 -0.0287 -0.0302 316 LEU A O   
150  C CB  . LEU A 20  ? 0.9194 1.2380 0.9344 -0.3873 -0.0205 -0.0347 316 LEU A CB  
151  C CG  . LEU A 20  ? 0.9023 1.1771 0.9238 -0.3589 -0.0299 -0.0419 316 LEU A CG  
152  C CD1 . LEU A 20  ? 0.8798 1.1619 0.8781 -0.4054 -0.0350 -0.0479 316 LEU A CD1 
153  C CD2 . LEU A 20  ? 0.8192 1.1597 0.8997 -0.3025 -0.0318 -0.0452 316 LEU A CD2 
154  N N   . HIS A 21  ? 1.0501 1.1241 0.9436 -0.4006 -0.0178 -0.0181 317 HIS A N   
155  C CA  . HIS A 21  ? 1.0952 1.0506 0.9478 -0.3718 -0.0227 -0.0145 317 HIS A CA  
156  C C   . HIS A 21  ? 1.2195 1.0599 0.9838 -0.4122 -0.0255 -0.0122 317 HIS A C   
157  O O   . HIS A 21  ? 1.2611 0.9990 0.9844 -0.3829 -0.0313 -0.0114 317 HIS A O   
158  C CB  . HIS A 21  ? 1.0923 1.0450 0.9498 -0.3490 -0.0185 -0.0061 317 HIS A CB  
159  C CG  . HIS A 21  ? 1.1723 1.1130 0.9831 -0.3981 -0.0110 0.0027  317 HIS A CG  
160  N ND1 . HIS A 21  ? 1.1497 1.1931 0.9830 -0.4361 -0.0017 0.0034  317 HIS A ND1 
161  C CD2 . HIS A 21  ? 1.3088 1.1482 1.0471 -0.4160 -0.0111 0.0118  317 HIS A CD2 
162  C CE1 . HIS A 21  ? 1.2877 1.2962 1.0661 -0.4805 0.0045  0.0129  317 HIS A CE1 
163  N NE2 . HIS A 21  ? 1.4117 1.2899 1.1288 -0.4694 -0.0014 0.0184  317 HIS A NE2 
164  N N   . LEU A 22  ? 1.2216 1.0762 0.9502 -0.4787 -0.0219 -0.0109 318 LEU A N   
165  C CA  . LEU A 22  ? 1.3211 1.0532 0.9517 -0.5240 -0.0258 -0.0098 318 LEU A CA  
166  C C   . LEU A 22  ? 1.3410 1.0214 0.9554 -0.5101 -0.0344 -0.0208 318 LEU A C   
167  O O   . LEU A 22  ? 1.4461 0.9917 0.9777 -0.5089 -0.0397 -0.0214 318 LEU A O   
168  C CB  . LEU A 22  ? 1.3269 1.1071 0.9285 -0.5858 -0.0193 -0.0055 318 LEU A CB  
169  C CG  . LEU A 22  ? 1.3580 1.1958 0.9643 -0.6089 -0.0091 0.0048  318 LEU A CG  
170  C CD1 . LEU A 22  ? 1.3393 1.2269 0.9115 -0.6639 -0.0048 0.0066  318 LEU A CD1 
171  C CD2 . LEU A 22  ? 1.6162 1.3343 1.1586 -0.6004 -0.0090 0.0152  318 LEU A CD2 
172  N N   . LYS A 23  ? 1.2625 1.0443 0.9473 -0.4985 -0.0360 -0.0295 319 LYS A N   
173  C CA  . LYS A 23  ? 1.3095 1.0455 0.9794 -0.4835 -0.0436 -0.0400 319 LYS A CA  
174  C C   . LYS A 23  ? 1.3313 1.0106 1.0123 -0.4099 -0.0467 -0.0414 319 LYS A C   
175  O O   . LYS A 23  ? 1.3817 1.0143 1.0442 -0.3908 -0.0518 -0.0497 319 LYS A O   
176  C CB  . LYS A 23  ? 1.2542 1.1138 0.9925 -0.4905 -0.0453 -0.0483 319 LYS A CB  
177  C CG  . LYS A 23  ? 1.2406 1.2025 0.9905 -0.5404 -0.0403 -0.0451 319 LYS A CG  
178  C CD  . LYS A 23  ? 1.3752 1.2674 1.0379 -0.5878 -0.0401 -0.0424 319 LYS A CD  
179  C CE  . LYS A 23  ? 1.5185 1.4188 1.1730 -0.5975 -0.0464 -0.0513 319 LYS A CE  
180  N NZ  . LYS A 23  ? 1.4760 1.5270 1.1922 -0.6102 -0.0448 -0.0525 319 LYS A NZ  
181  N N   . SER A 24  ? 1.3319 1.0189 1.0405 -0.3705 -0.0439 -0.0337 320 SER A N   
182  C CA  . SER A 24  ? 1.3756 1.0242 1.0969 -0.3052 -0.0473 -0.0340 320 SER A CA  
183  C C   . SER A 24  ? 1.5485 1.0600 1.1797 -0.2941 -0.0518 -0.0350 320 SER A C   
184  O O   . SER A 24  ? 1.5919 1.0137 1.1396 -0.3312 -0.0521 -0.0311 320 SER A O   
185  C CB  . SER A 24  ? 1.2867 0.9635 1.0422 -0.2740 -0.0450 -0.0249 320 SER A CB  
186  O OG  . SER A 24  ? 1.3306 0.9472 1.0708 -0.2220 -0.0496 -0.0233 320 SER A OG  
187  N N   . THR A 25  ? 1.7435 1.2379 1.3872 -0.2405 -0.0552 -0.0400 321 THR A N   
188  C CA  . THR A 25  ? 1.8390 1.2119 1.3994 -0.2161 -0.0592 -0.0432 321 THR A CA  
189  C C   . THR A 25  ? 1.8363 1.2017 1.4124 -0.1482 -0.0611 -0.0385 321 THR A C   
190  O O   . THR A 25  ? 1.8461 1.1243 1.3569 -0.1294 -0.0636 -0.0320 321 THR A O   
191  C CB  . THR A 25  ? 1.8692 1.2319 1.4186 -0.2186 -0.0610 -0.0561 321 THR A CB  
192  O OG1 . THR A 25  ? 1.9620 1.2338 1.4538 -0.1687 -0.0636 -0.0605 321 THR A OG1 
193  C CG2 . THR A 25  ? 1.7573 1.2493 1.4096 -0.2063 -0.0594 -0.0605 321 THR A CG2 
194  N N   . LEU A 26  ? 1.6582 1.1175 1.3181 -0.1136 -0.0605 -0.0409 322 LEU A N   
195  C CA  . LEU A 26  ? 1.6160 1.0889 1.2982 -0.0541 -0.0628 -0.0371 322 LEU A CA  
196  C C   . LEU A 26  ? 1.6074 1.0876 1.2965 -0.0491 -0.0642 -0.0254 322 LEU A C   
197  O O   . LEU A 26  ? 1.5110 1.0032 1.2023 -0.0897 -0.0617 -0.0206 322 LEU A O   
198  C CB  . LEU A 26  ? 1.5089 1.0853 1.2771 -0.0328 -0.0616 -0.0410 322 LEU A CB  
199  C CG  . LEU A 26  ? 1.5739 1.1435 1.3353 -0.0101 -0.0609 -0.0508 322 LEU A CG  
200  C CD1 . LEU A 26  ? 1.4557 1.1140 1.2856 -0.0273 -0.0587 -0.0555 322 LEU A CD1 
201  C CD2 . LEU A 26  ? 1.6179 1.1937 1.3827 0.0493  -0.0624 -0.0487 322 LEU A CD2 
202  N N   . GLU A 27  ? 1.5876 1.0673 1.2796 0.0022  -0.0683 -0.0210 323 GLU A N   
203  C CA  . GLU A 27  ? 1.5448 1.0299 1.2393 0.0137  -0.0716 -0.0101 323 GLU A CA  
204  C C   . GLU A 27  ? 1.4573 1.0542 1.2420 0.0252  -0.0725 -0.0081 323 GLU A C   
205  O O   . GLU A 27  ? 1.4033 1.0637 1.2401 0.0365  -0.0716 -0.0138 323 GLU A O   
206  C CB  . GLU A 27  ? 1.6408 1.0494 1.2693 0.0634  -0.0777 -0.0055 323 GLU A CB  
207  C CG  . GLU A 27  ? 1.7463 1.0191 1.2650 0.0524  -0.0779 -0.0066 323 GLU A CG  
208  C CD  . GLU A 27  ? 1.9179 1.1045 1.3594 0.1049  -0.0849 0.0002  323 GLU A CD  
209  O OE1 . GLU A 27  ? 1.8975 1.1450 1.3799 0.1469  -0.0899 0.0063  323 GLU A OE1 
210  O OE2 . GLU A 27  ? 2.0334 1.0891 1.3681 0.1044  -0.0864 -0.0005 323 GLU A OE2 
211  N N   . THR A 28  ? 1.4137 1.0267 1.2081 0.0196  -0.0745 0.0004  324 THR A N   
212  C CA  . THR A 28  ? 1.3045 1.0072 1.1694 0.0203  -0.0758 0.0023  324 THR A CA  
213  C C   . THR A 28  ? 1.3280 1.0578 1.2065 0.0605  -0.0841 0.0081  324 THR A C   
214  O O   . THR A 28  ? 1.2407 1.0445 1.1750 0.0633  -0.0866 0.0079  324 THR A O   
215  C CB  . THR A 28  ? 1.2658 0.9780 1.1338 -0.0149 -0.0720 0.0065  324 THR A CB  
216  O OG1 . THR A 28  ? 1.2428 0.8927 1.0550 -0.0110 -0.0750 0.0155  324 THR A OG1 
217  C CG2 . THR A 28  ? 1.2227 0.9316 1.0844 -0.0572 -0.0640 0.0013  324 THR A CG2 
218  N N   . GLY A 29  ? 1.2822 0.9533 1.1060 0.0906  -0.0894 0.0136  325 GLY A N   
219  C CA  . GLY A 29  ? 1.2260 0.9287 1.0583 0.1277  -0.0988 0.0205  325 GLY A CA  
220  C C   . GLY A 29  ? 1.1804 0.8556 0.9855 0.1194  -0.1030 0.0300  325 GLY A C   
221  O O   . GLY A 29  ? 1.2225 0.8870 1.0019 0.1549  -0.1121 0.0373  325 GLY A O   
222  N N   . CYS A 30  ? 1.1642 0.8317 0.9721 0.0758  -0.0965 0.0303  326 CYS A N   
223  C CA  . CYS A 30  ? 1.1707 0.8087 0.9465 0.0665  -0.0989 0.0394  326 CYS A CA  
224  C C   . CYS A 30  ? 1.2812 0.8093 0.9669 0.0696  -0.0989 0.0457  326 CYS A C   
225  O O   . CYS A 30  ? 1.3505 0.8195 0.9967 0.0635  -0.0946 0.0413  326 CYS A O   
226  C CB  . CYS A 30  ? 1.1081 0.7778 0.9112 0.0220  -0.0904 0.0377  326 CYS A CB  
227  S SG  . CYS A 30  ? 0.9657 0.7380 0.8537 0.0161  -0.0899 0.0298  326 CYS A SG  
228  N N   . THR A 31  ? 1.3437 0.8367 0.9890 0.0779  -0.1044 0.0560  327 THR A N   
229  C CA  . THR A 31  ? 1.4530 0.8302 1.0015 0.0723  -0.1041 0.0641  327 THR A CA  
230  C C   . THR A 31  ? 1.4874 0.8569 1.0207 0.0307  -0.0988 0.0715  327 THR A C   
231  O O   . THR A 31  ? 1.4371 0.8889 1.0333 0.0131  -0.0956 0.0692  327 THR A O   
232  C CB  . THR A 31  ? 1.4757 0.7999 0.9680 0.1320  -0.1169 0.0716  327 THR A CB  
233  O OG1 . THR A 31  ? 1.4521 0.8276 0.9684 0.1499  -0.1258 0.0793  327 THR A OG1 
234  C CG2 . THR A 31  ? 1.4167 0.7750 0.9351 0.1791  -0.1212 0.0639  327 THR A CG2 
235  N N   . GLU A 32  ? 1.6075 0.8720 1.0492 0.0148  -0.0975 0.0805  328 GLU A N   
236  C CA  . GLU A 32  ? 1.6232 0.8794 1.0425 -0.0215 -0.0924 0.0895  328 GLU A CA  
237  C C   . GLU A 32  ? 1.5666 0.8767 1.0174 0.0093  -0.1016 0.0950  328 GLU A C   
238  O O   . GLU A 32  ? 1.5928 0.9370 1.0580 -0.0187 -0.0961 0.0982  328 GLU A O   
239  C CB  . GLU A 32  ? 1.8137 0.9346 1.1148 -0.0414 -0.0914 0.1007  328 GLU A CB  
240  C CG  . GLU A 32  ? 1.8590 0.9300 1.1206 -0.0995 -0.0800 0.0968  328 GLU A CG  
241  C CD  . GLU A 32  ? 1.9966 0.9907 1.2124 -0.0773 -0.0847 0.0902  328 GLU A CD  
242  O OE1 . GLU A 32  ? 1.9387 0.9838 1.2092 -0.0279 -0.0908 0.0818  328 GLU A OE1 
243  O OE2 . GLU A 32  ? 2.1430 1.0232 1.2624 -0.1116 -0.0820 0.0934  328 GLU A OE2 
244  N N   . HIS A 33  ? 1.5074 0.8339 0.9701 0.0656  -0.1155 0.0956  329 HIS A N   
245  C CA  . HIS A 33  ? 1.5042 0.8749 0.9838 0.0933  -0.1271 0.1020  329 HIS A CA  
246  C C   . HIS A 33  ? 1.3777 0.8636 0.9484 0.1147  -0.1341 0.0938  329 HIS A C   
247  O O   . HIS A 33  ? 1.3133 0.8423 0.8986 0.1341  -0.1456 0.0984  329 HIS A O   
248  C CB  . HIS A 33  ? 1.6209 0.9117 1.0196 0.1421  -0.1406 0.1137  329 HIS A CB  
249  C CG  . HIS A 33  ? 1.7712 0.9257 1.0611 0.1237  -0.1355 0.1227  329 HIS A CG  
250  N ND1 . HIS A 33  ? 1.8371 0.9077 1.0733 0.1244  -0.1316 0.1192  329 HIS A ND1 
251  C CD2 . HIS A 33  ? 1.8688 0.9502 1.0861 0.1002  -0.1339 0.1352  329 HIS A CD2 
252  C CE1 . HIS A 33  ? 1.9691 0.9156 1.1002 0.0994  -0.1284 0.1294  329 HIS A CE1 
253  N NE2 . HIS A 33  ? 1.9606 0.9133 1.0795 0.0838  -0.1293 0.1398  329 HIS A NE2 
254  N N   . ILE A 34  ? 1.2948 0.8303 0.9220 0.1083  -0.1285 0.0824  330 ILE A N   
255  C CA  . ILE A 34  ? 1.1625 0.8013 0.8687 0.1199  -0.1345 0.0755  330 ILE A CA  
256  C C   . ILE A 34  ? 1.1309 0.8112 0.8913 0.0890  -0.1228 0.0639  330 ILE A C   
257  O O   . ILE A 34  ? 1.1333 0.7790 0.8811 0.0819  -0.1149 0.0593  330 ILE A O   
258  C CB  . ILE A 34  ? 1.1589 0.8249 0.8701 0.1724  -0.1471 0.0769  330 ILE A CB  
259  C CG1 . ILE A 34  ? 1.0664 0.8442 0.8543 0.1738  -0.1540 0.0718  330 ILE A CG1 
260  C CG2 . ILE A 34  ? 1.2862 0.9115 0.9785 0.1886  -0.1411 0.0714  330 ILE A CG2 
261  C CD1 . ILE A 34  ? 1.0871 0.9145 0.8765 0.2196  -0.1708 0.0781  330 ILE A CD1 
262  N N   . CYS A 35  ? 1.0518 0.8008 0.8660 0.0712  -0.1224 0.0589  331 CYS A N   
263  C CA  . CYS A 35  ? 0.9865 0.7745 0.8478 0.0470  -0.1128 0.0486  331 CYS A CA  
264  C C   . CYS A 35  ? 0.9487 0.8022 0.8604 0.0632  -0.1201 0.0436  331 CYS A C   
265  O O   . CYS A 35  ? 0.8754 0.7732 0.8058 0.0696  -0.1305 0.0455  331 CYS A O   
266  C CB  . CYS A 35  ? 0.9333 0.7421 0.8084 0.0171  -0.1057 0.0457  331 CYS A CB  
267  S SG  . CYS A 35  ? 0.7886 0.6448 0.7154 -0.0019 -0.0960 0.0336  331 CYS A SG  
268  N N   . MET A 36  ? 0.9047 0.7639 0.8338 0.0660  -0.1148 0.0376  332 MET A N   
269  C CA  . MET A 36  ? 0.8917 0.8122 0.8657 0.0771  -0.1189 0.0331  332 MET A CA  
270  C C   . MET A 36  ? 0.8293 0.7829 0.8421 0.0497  -0.1124 0.0252  332 MET A C   
271  O O   . MET A 36  ? 0.7566 0.7493 0.8004 0.0524  -0.1129 0.0212  332 MET A O   
272  C CB  . MET A 36  ? 0.9338 0.8376 0.8962 0.1030  -0.1171 0.0314  332 MET A CB  
273  C CG  . MET A 36  ? 1.0351 0.8879 0.9442 0.1374  -0.1228 0.0384  332 MET A CG  
274  S SD  . MET A 36  ? 1.1626 1.0809 1.0862 0.1881  -0.1357 0.0425  332 MET A SD  
275  C CE  . MET A 36  ? 1.1844 1.0267 1.0326 0.2218  -0.1440 0.0533  332 MET A CE  
276  N N   . GLY A 37  ? 0.7993 0.7385 0.8070 0.0260  -0.1061 0.0233  333 GLY A N   
277  C CA  . GLY A 37  ? 0.7763 0.7391 0.8113 0.0077  -0.0996 0.0158  333 GLY A CA  
278  C C   . GLY A 37  ? 0.7493 0.7535 0.8112 0.0050  -0.1067 0.0134  333 GLY A C   
279  O O   . GLY A 37  ? 0.7333 0.7475 0.8098 -0.0057 -0.1021 0.0076  333 GLY A O   
280  N N   . SER A 38  ? 0.7524 0.7803 0.8165 0.0121  -0.1183 0.0179  334 SER A N   
281  C CA  . SER A 38  ? 0.6833 0.7496 0.7668 0.0008  -0.1257 0.0162  334 SER A CA  
282  C C   . SER A 38  ? 0.6874 0.8015 0.7923 0.0125  -0.1318 0.0193  334 SER A C   
283  O O   . SER A 38  ? 0.6673 0.8227 0.7853 -0.0016 -0.1397 0.0202  334 SER A O   
284  C CB  . SER A 38  ? 0.7138 0.7800 0.7807 -0.0114 -0.1353 0.0179  334 SER A CB  
285  O OG  . SER A 38  ? 0.7363 0.8251 0.7984 0.0007  -0.1463 0.0250  334 SER A OG  
286  N N   . ILE A 39  ? 0.6971 0.8064 0.8001 0.0373  -0.1283 0.0210  335 ILE A N   
287  C CA  . ILE A 39  ? 0.7329 0.8916 0.8556 0.0553  -0.1309 0.0224  335 ILE A CA  
288  C C   . ILE A 39  ? 0.7553 0.9228 0.8980 0.0432  -0.1223 0.0164  335 ILE A C   
289  O O   . ILE A 39  ? 0.7835 0.9081 0.9179 0.0412  -0.1127 0.0116  335 ILE A O   
290  C CB  . ILE A 39  ? 0.7671 0.9024 0.8670 0.0929  -0.1300 0.0252  335 ILE A CB  
291  C CG1 . ILE A 39  ? 0.8095 0.9238 0.8803 0.1061  -0.1387 0.0323  335 ILE A CG1 
292  C CG2 . ILE A 39  ? 0.7964 0.9915 0.9149 0.1193  -0.1320 0.0259  335 ILE A CG2 
293  C CD1 . ILE A 39  ? 0.7658 0.9479 0.8537 0.1031  -0.1529 0.0374  335 ILE A CD1 
294  N N   . MET A 40  ? 0.7434 0.9693 0.9100 0.0324  -0.1261 0.0173  336 MET A N   
295  C CA  . MET A 40  ? 0.7609 0.9908 0.9410 0.0150  -0.1191 0.0128  336 MET A CA  
296  C C   . MET A 40  ? 0.8513 1.0752 1.0351 0.0373  -0.1095 0.0089  336 MET A C   
297  O O   . MET A 40  ? 0.8442 1.0284 1.0222 0.0315  -0.1016 0.0035  336 MET A O   
298  C CB  . MET A 40  ? 0.7686 1.0597 0.9652 -0.0080 -0.1255 0.0161  336 MET A CB  
299  C CG  . MET A 40  ? 0.8064 1.1039 1.0123 -0.0223 -0.1182 0.0133  336 MET A CG  
300  S SD  . MET A 40  ? 0.8715 1.1292 1.0556 -0.0635 -0.1217 0.0124  336 MET A SD  
301  C CE  . MET A 40  ? 0.7085 1.0212 0.8908 -0.0927 -0.1358 0.0194  336 MET A CE  
302  N N   . LEU A 41  ? 0.8037 1.0706 0.9947 0.0642  -0.1106 0.0111  337 LEU A N   
303  C CA  . LEU A 41  ? 0.9244 1.1806 1.1097 0.0903  -0.1020 0.0065  337 LEU A CA  
304  C C   . LEU A 41  ? 1.0442 1.2586 1.1969 0.1271  -0.1031 0.0073  337 LEU A C   
305  O O   . LEU A 41  ? 1.0956 1.3477 1.2458 0.1628  -0.1057 0.0097  337 LEU A O   
306  C CB  . LEU A 41  ? 0.9087 1.2449 1.1189 0.0994  -0.1004 0.0076  337 LEU A CB  
307  C CG  . LEU A 41  ? 0.8571 1.2533 1.0937 0.0607  -0.1037 0.0113  337 LEU A CG  
308  C CD1 . LEU A 41  ? 0.8457 1.3416 1.1055 0.0734  -0.1044 0.0152  337 LEU A CD1 
309  C CD2 . LEU A 41  ? 0.8306 1.1928 1.0665 0.0347  -0.0964 0.0068  337 LEU A CD2 
310  N N   . PRO A 42  ? 1.1292 1.2678 1.2521 0.1205  -0.1013 0.0060  338 PRO A N   
311  C CA  . PRO A 42  ? 1.2674 1.3525 1.3465 0.1515  -0.1034 0.0084  338 PRO A CA  
312  C C   . PRO A 42  ? 1.4733 1.5354 1.5271 0.1853  -0.0979 0.0034  338 PRO A C   
313  O O   . PRO A 42  ? 1.4709 1.5368 1.5358 0.1759  -0.0904 -0.0033 338 PRO A O   
314  C CB  . PRO A 42  ? 1.2827 1.2953 1.3357 0.1246  -0.1000 0.0075  338 PRO A CB  
315  C CG  . PRO A 42  ? 1.2402 1.2627 1.3192 0.0929  -0.0929 0.0011  338 PRO A CG  
316  C CD  . PRO A 42  ? 1.1090 1.2068 1.2312 0.0870  -0.0958 0.0018  338 PRO A CD  
317  N N   . SER A 43  ? 1.6391 1.6743 1.6530 0.2285  -0.1022 0.0066  339 SER A N   
318  C CA  . SER A 43  ? 1.7217 1.7308 1.7004 0.2716  -0.0979 0.0016  339 SER A CA  
319  C C   . SER A 43  ? 1.7844 1.7130 1.7304 0.2526  -0.0888 -0.0074 339 SER A C   
320  O O   . SER A 43  ? 1.7770 1.6926 1.7021 0.2790  -0.0836 -0.0143 339 SER A O   
321  C CB  . SER A 43  ? 1.7941 1.7543 1.7142 0.3216  -0.1049 0.0068  339 SER A CB  
322  O OG  . SER A 43  ? 1.8998 1.8259 1.7748 0.3711  -0.1010 0.0011  339 SER A OG  
323  N N   . GLN A 44  ? 1.7095 1.5910 1.6504 0.2071  -0.0870 -0.0077 340 GLN A N   
324  C CA  . GLN A 44  ? 1.7418 1.5574 1.6534 0.1813  -0.0799 -0.0157 340 GLN A CA  
325  C C   . GLN A 44  ? 1.7264 1.5999 1.6903 0.1546  -0.0744 -0.0218 340 GLN A C   
326  O O   . GLN A 44  ? 1.7244 1.5697 1.6696 0.1526  -0.0691 -0.0299 340 GLN A O   
327  C CB  . GLN A 44  ? 1.6579 1.4111 1.5404 0.1437  -0.0801 -0.0127 340 GLN A CB  
328  C CG  . GLN A 44  ? 1.6731 1.3228 1.4721 0.1603  -0.0830 -0.0091 340 GLN A CG  
329  C CD  . GLN A 44  ? 1.7016 1.3606 1.4905 0.1972  -0.0913 0.0006  340 GLN A CD  
330  O OE1 . GLN A 44  ? 1.6981 1.4481 1.5438 0.2120  -0.0956 0.0040  340 GLN A OE1 
331  N NE2 . GLN A 44  ? 1.6951 1.2567 1.4052 0.2101  -0.0947 0.0055  340 GLN A NE2 
332  N N   . HIS A 45  ? 1.6970 1.6432 1.7184 0.1337  -0.0762 -0.0179 341 HIS A N   
333  C CA  . HIS A 45  ? 1.6244 1.6144 1.6870 0.1065  -0.0722 -0.0219 341 HIS A CA  
334  C C   . HIS A 45  ? 1.5846 1.6212 1.6650 0.1252  -0.0685 -0.0256 341 HIS A C   
335  O O   . HIS A 45  ? 1.5172 1.5892 1.6275 0.1044  -0.0656 -0.0276 341 HIS A O   
336  C CB  . HIS A 45  ? 1.5233 1.5603 1.6250 0.0833  -0.0764 -0.0162 341 HIS A CB  
337  C CG  . HIS A 45  ? 1.4756 1.5233 1.5986 0.0526  -0.0732 -0.0197 341 HIS A CG  
338  N ND1 . HIS A 45  ? 1.4186 1.4621 1.5416 0.0468  -0.0680 -0.0263 341 HIS A ND1 
339  C CD2 . HIS A 45  ? 1.3774 1.4384 1.5172 0.0307  -0.0752 -0.0175 341 HIS A CD2 
340  C CE1 . HIS A 45  ? 1.3426 1.4003 1.4835 0.0242  -0.0675 -0.0273 341 HIS A CE1 
341  N NE2 . HIS A 45  ? 1.3330 1.3992 1.4824 0.0160  -0.0714 -0.0223 341 HIS A NE2 
342  N N   . THR A 46  ? 1.7879 1.8251 1.8464 0.1661  -0.0679 -0.0264 342 THR A N   
343  C CA  . THR A 46  ? 1.7560 1.8488 1.8310 0.1876  -0.0629 -0.0296 342 THR A CA  
344  C C   . THR A 46  ? 1.8205 1.8491 1.8425 0.2161  -0.0574 -0.0389 342 THR A C   
345  O O   . THR A 46  ? 1.9088 1.8610 1.8755 0.2376  -0.0597 -0.0401 342 THR A O   
346  C CB  . THR A 46  ? 1.7365 1.9114 1.8358 0.2170  -0.0668 -0.0226 342 THR A CB  
347  O OG1 . THR A 46  ? 1.6706 1.8956 1.8102 0.1846  -0.0732 -0.0147 342 THR A OG1 
348  C CG2 . THR A 46  ? 1.6987 1.9459 1.8175 0.2367  -0.0598 -0.0253 342 THR A CG2 
349  N N   . ARG A 47  ? 1.6078 1.6591 1.6389 0.2146  -0.0504 -0.0454 343 ARG A N   
350  C CA  . ARG A 47  ? 1.7168 1.7124 1.6952 0.2439  -0.0447 -0.0556 343 ARG A CA  
351  C C   . ARG A 47  ? 1.6941 1.7483 1.6723 0.2979  -0.0405 -0.0561 343 ARG A C   
352  O O   . ARG A 47  ? 1.6057 1.7415 1.6228 0.2972  -0.0345 -0.0562 343 ARG A O   
353  C CB  . ARG A 47  ? 1.5935 1.5790 1.5761 0.2131  -0.0397 -0.0634 343 ARG A CB  
354  C CG  . ARG A 47  ? 1.6062 1.5213 1.5675 0.1708  -0.0432 -0.0664 343 ARG A CG  
355  C CD  . ARG A 47  ? 1.7658 1.5965 1.6723 0.1779  -0.0479 -0.0652 343 ARG A CD  
356  N NE  . ARG A 47  ? 1.7506 1.5259 1.6368 0.1319  -0.0503 -0.0672 343 ARG A NE  
357  C CZ  . ARG A 47  ? 1.8058 1.5190 1.6546 0.1188  -0.0543 -0.0636 343 ARG A CZ  
358  N NH1 . ARG A 47  ? 1.8631 1.5523 1.6878 0.1505  -0.0574 -0.0574 343 ARG A NH1 
359  N NH2 . ARG A 47  ? 1.8339 1.5136 1.6680 0.0723  -0.0553 -0.0656 343 ARG A NH2 
360  N N   . VAL A 52  ? 2.0157 1.6845 1.5748 0.5645  -0.0115 -0.1207 348 VAL A N   
361  C CA  . VAL A 52  ? 2.1262 1.6907 1.6139 0.5508  -0.0081 -0.1359 348 VAL A CA  
362  C C   . VAL A 52  ? 2.2150 1.6185 1.6184 0.5138  -0.0180 -0.1385 348 VAL A C   
363  O O   . VAL A 52  ? 2.2138 1.5591 1.5789 0.5302  -0.0253 -0.1314 348 VAL A O   
364  C CB  . VAL A 52  ? 2.1187 1.6761 1.5474 0.6134  -0.0007 -0.1424 348 VAL A CB  
365  C CG1 . VAL A 52  ? 2.1663 1.6361 1.5069 0.6518  -0.0088 -0.1354 348 VAL A CG1 
366  C CG2 . VAL A 52  ? 2.1158 1.6040 1.4944 0.5953  0.0046  -0.1583 348 VAL A CG2 
367  N N   . ALA A 53  ? 2.2575 1.5957 1.6324 0.4596  -0.0188 -0.1478 349 ALA A N   
368  C CA  . ALA A 53  ? 2.2810 1.4781 1.5772 0.4102  -0.0277 -0.1507 349 ALA A CA  
369  C C   . ALA A 53  ? 2.3071 1.3807 1.4933 0.4147  -0.0268 -0.1662 349 ALA A C   
370  O O   . ALA A 53  ? 2.3167 1.4253 1.5136 0.4220  -0.0199 -0.1775 349 ALA A O   
371  C CB  . ALA A 53  ? 2.2002 1.4507 1.5719 0.3243  -0.0321 -0.1443 349 ALA A CB  
372  N N   . THR A 54  ? 2.3514 1.3000 1.4418 0.3990  -0.0347 -0.1605 350 THR A N   
373  C CA  . THR A 54  ? 2.4137 1.2563 1.3998 0.4000  -0.0361 -0.1657 350 THR A CA  
374  C C   . THR A 54  ? 2.4233 1.1917 1.3723 0.3157  -0.0419 -0.1723 350 THR A C   
375  O O   . THR A 54  ? 2.3634 1.1587 1.3618 0.2551  -0.0456 -0.1720 350 THR A O   
376  C CB  . THR A 54  ? 2.4672 1.2145 1.3561 0.4374  -0.0418 -0.1544 350 THR A CB  
377  O OG1 . THR A 54  ? 2.5540 1.1916 1.3765 0.3738  -0.0506 -0.1486 350 THR A OG1 
378  C CG2 . THR A 54  ? 2.3983 1.2267 1.3391 0.4928  -0.0410 -0.1434 350 THR A CG2 
379  N N   . LYS A 55  ? 2.5236 1.2011 1.3811 0.3120  -0.0434 -0.1774 351 LYS A N   
380  C CA  . LYS A 55  ? 2.5530 1.1757 1.3759 0.2333  -0.0489 -0.1838 351 LYS A CA  
381  C C   . LYS A 55  ? 2.5718 1.1174 1.3461 0.1691  -0.0578 -0.1723 351 LYS A C   
382  O O   . LYS A 55  ? 2.4836 1.0414 1.2782 0.0915  -0.0622 -0.1741 351 LYS A O   
383  C CB  . LYS A 55  ? 2.6358 1.1822 1.3702 0.2512  -0.0482 -0.1914 351 LYS A CB  
384  C CG  . LYS A 55  ? 2.7515 1.2206 1.3960 0.3238  -0.0478 -0.1842 351 LYS A CG  
385  C CD  . LYS A 55  ? 2.8967 1.2912 1.4526 0.3461  -0.0469 -0.1923 351 LYS A CD  
386  C CE  . LYS A 55  ? 3.0325 1.3443 1.4882 0.4201  -0.0482 -0.1843 351 LYS A CE  
387  N NZ  . LYS A 55  ? 3.1031 1.2986 1.4389 0.4289  -0.0507 -0.1894 351 LYS A NZ  
388  N N   . ASP A 56  ? 2.6798 1.1537 1.3889 0.1997  -0.0606 -0.1599 352 ASP A N   
389  C CA  . ASP A 56  ? 2.7509 1.1503 1.4057 0.1399  -0.0677 -0.1479 352 ASP A CA  
390  C C   . ASP A 56  ? 2.6067 1.0959 1.3616 0.0925  -0.0681 -0.1435 352 ASP A C   
391  O O   . ASP A 56  ? 2.6215 1.1027 1.3733 0.0137  -0.0722 -0.1396 352 ASP A O   
392  C CB  . ASP A 56  ? 2.9122 1.2203 1.4746 0.1914  -0.0706 -0.1362 352 ASP A CB  
393  C CG  . ASP A 56  ? 3.0402 1.3008 1.5331 0.2695  -0.0685 -0.1410 352 ASP A CG  
394  O OD1 . ASP A 56  ? 3.0092 1.3626 1.5709 0.3353  -0.0621 -0.1459 352 ASP A OD1 
395  O OD2 . ASP A 56  ? 3.1849 1.3196 1.5531 0.2640  -0.0731 -0.1394 352 ASP A OD2 
396  N N   . GLN A 57  ? 2.4627 1.0447 1.3069 0.1395  -0.0639 -0.1435 353 GLN A N   
397  C CA  . GLN A 57  ? 2.3590 1.0232 1.2952 0.1004  -0.0646 -0.1396 353 GLN A CA  
398  C C   . GLN A 57  ? 2.2454 0.9834 1.2495 0.0404  -0.0649 -0.1502 353 GLN A C   
399  O O   . GLN A 57  ? 2.1186 0.9115 1.1807 -0.0113 -0.0675 -0.1459 353 GLN A O   
400  C CB  . GLN A 57  ? 2.2970 1.0423 1.3072 0.1688  -0.0605 -0.1371 353 GLN A CB  
401  C CG  . GLN A 57  ? 2.3837 1.0857 1.3353 0.2469  -0.0598 -0.1302 353 GLN A CG  
402  C CD  . GLN A 57  ? 2.3496 1.1609 1.3780 0.3223  -0.0534 -0.1324 353 GLN A CD  
403  O OE1 . GLN A 57  ? 2.3313 1.2198 1.4206 0.3296  -0.0473 -0.1434 353 GLN A OE1 
404  N NE2 . GLN A 57  ? 2.3254 1.1520 1.3511 0.3766  -0.0549 -0.1213 353 GLN A NE2 
405  N N   . LEU A 58  ? 2.2507 0.9946 1.2463 0.0464  -0.0629 -0.1633 354 LEU A N   
406  C CA  . LEU A 58  ? 2.1448 0.9769 1.2140 0.0045  -0.0637 -0.1745 354 LEU A CA  
407  C C   . LEU A 58  ? 2.1263 0.9542 1.1829 -0.0867 -0.0708 -0.1715 354 LEU A C   
408  O O   . LEU A 58  ? 1.9862 0.9057 1.1187 -0.1332 -0.0738 -0.1728 354 LEU A O   
409  C CB  . LEU A 58  ? 2.1435 0.9904 1.2081 0.0439  -0.0588 -0.1891 354 LEU A CB  
410  C CG  . LEU A 58  ? 1.9922 0.9956 1.1813 0.0773  -0.0513 -0.1860 354 LEU A CG  
411  C CD1 . LEU A 58  ? 1.9608 1.0160 1.1970 0.1421  -0.0451 -0.1747 354 LEU A CD1 
412  C CD2 . LEU A 58  ? 1.9675 0.9757 1.1378 0.1041  -0.0463 -0.2001 354 LEU A CD2 
413  N N   . PHE A 59  ? 2.2129 0.9430 1.1736 -0.1129 -0.0736 -0.1662 355 PHE A N   
414  C CA  . PHE A 59  ? 2.2158 0.9605 1.1687 -0.1986 -0.0792 -0.1633 355 PHE A CA  
415  C C   . PHE A 59  ? 2.1803 0.9737 1.1739 -0.2511 -0.0808 -0.1500 355 PHE A C   
416  O O   . PHE A 59  ? 2.1284 1.0131 1.1803 -0.3095 -0.0836 -0.1497 355 PHE A O   
417  C CB  . PHE A 59  ? 2.4314 1.0578 1.2644 -0.2196 -0.0819 -0.1606 355 PHE A CB  
418  C CG  . PHE A 59  ? 2.5281 1.1858 1.3580 -0.3019 -0.0871 -0.1603 355 PHE A CG  
419  C CD1 . PHE A 59  ? 2.4531 1.1900 1.3375 -0.3163 -0.0893 -0.1728 355 PHE A CD1 
420  C CD2 . PHE A 59  ? 2.5697 1.1879 1.3440 -0.3646 -0.0898 -0.1471 355 PHE A CD2 
421  C CE1 . PHE A 59  ? 2.4319 1.2126 1.3193 -0.3886 -0.0947 -0.1716 355 PHE A CE1 
422  C CE2 . PHE A 59  ? 2.5958 1.2583 1.3710 -0.4392 -0.0938 -0.1459 355 PHE A CE2 
423  C CZ  . PHE A 59  ? 2.5275 1.2741 1.3617 -0.4495 -0.0966 -0.1580 355 PHE A CZ  
424  N N   . PRO A 60  ? 2.1852 0.9284 1.1498 -0.2320 -0.0791 -0.1381 356 PRO A N   
425  C CA  . PRO A 60  ? 2.0863 0.8929 1.1029 -0.2772 -0.0792 -0.1264 356 PRO A CA  
426  C C   . PRO A 60  ? 1.9245 0.8663 1.0642 -0.2806 -0.0788 -0.1313 356 PRO A C   
427  O O   . PRO A 60  ? 1.8179 0.8477 1.0117 -0.3370 -0.0800 -0.1260 356 PRO A O   
428  C CB  . PRO A 60  ? 2.1338 0.8629 1.1024 -0.2343 -0.0774 -0.1156 356 PRO A CB  
429  C CG  . PRO A 60  ? 2.2442 0.8971 1.1585 -0.1561 -0.0763 -0.1225 356 PRO A CG  
430  C CD  . PRO A 60  ? 2.2687 0.8960 1.1434 -0.1737 -0.0777 -0.1331 356 PRO A CD  
431  N N   . LEU A 61  ? 1.9080 0.8723 1.0896 -0.2193 -0.0771 -0.1410 357 LEU A N   
432  C CA  . LEU A 61  ? 1.7162 0.8380 1.0294 -0.2107 -0.0743 -0.1371 357 LEU A CA  
433  C C   . LEU A 61  ? 1.7083 0.9077 1.0606 -0.2522 -0.0778 -0.1452 357 LEU A C   
434  O O   . LEU A 61  ? 1.6043 0.9279 1.0475 -0.2756 -0.0780 -0.1390 357 LEU A O   
435  C CB  . LEU A 61  ? 1.6465 0.8081 1.0088 -0.1294 -0.0680 -0.1358 357 LEU A CB  
436  C CG  . LEU A 61  ? 1.7686 0.8573 1.0872 -0.0801 -0.0661 -0.1288 357 LEU A CG  
437  C CD1 . LEU A 61  ? 1.7252 0.8553 1.0804 -0.0011 -0.0604 -0.1295 357 LEU A CD1 
438  C CD2 . LEU A 61  ? 1.7237 0.8606 1.0907 -0.1019 -0.0664 -0.1140 357 LEU A CD2 
439  N N   . ALA A 62  ? 1.7630 0.8902 1.0440 -0.2579 -0.0811 -0.1593 358 ALA A N   
440  C CA  . ALA A 62  ? 1.7004 0.8975 1.0103 -0.2991 -0.0863 -0.1672 358 ALA A CA  
441  C C   . ALA A 62  ? 1.6902 0.9236 0.9983 -0.3751 -0.0908 -0.1593 358 ALA A C   
442  O O   . ALA A 62  ? 1.5917 0.9466 0.9749 -0.4070 -0.0942 -0.1580 358 ALA A O   
443  C CB  . ALA A 62  ? 1.8131 0.9265 1.0458 -0.2830 -0.0877 -0.1822 358 ALA A CB  
444  N N   . LYS A 63  ? 1.7632 0.9055 0.9895 -0.3976 -0.0891 -0.1502 359 LYS A N   
445  C CA  . LYS A 63  ? 1.7762 0.9559 0.9938 -0.4666 -0.0902 -0.1390 359 LYS A CA  
446  C C   . LYS A 63  ? 1.7219 1.0133 1.0244 -0.4854 -0.0878 -0.1290 359 LYS A C   
447  O O   . LYS A 63  ? 1.6798 1.0856 1.0373 -0.5261 -0.0891 -0.1253 359 LYS A O   
448  C CB  . LYS A 63  ? 1.9045 0.9500 1.0052 -0.4831 -0.0886 -0.1304 359 LYS A CB  
449  C CG  . LYS A 63  ? 1.9174 0.9944 0.9994 -0.5540 -0.0879 -0.1172 359 LYS A CG  
450  C CD  . LYS A 63  ? 2.0657 0.9982 1.0183 -0.5715 -0.0872 -0.1085 359 LYS A CD  
451  C CE  . LYS A 63  ? 2.0646 1.0124 0.9703 -0.6502 -0.0887 -0.1015 359 LYS A CE  
452  N NZ  . LYS A 63  ? 2.0723 1.1769 1.0726 -0.6909 -0.0859 -0.0951 359 LYS A NZ  
453  N N   . GLU A 64  ? 1.6632 0.9249 0.9749 -0.4523 -0.0842 -0.1240 360 GLU A N   
454  C CA  . GLU A 64  ? 1.6206 0.9858 1.0147 -0.4618 -0.0817 -0.1156 360 GLU A CA  
455  C C   . GLU A 64  ? 1.5114 1.0172 1.0083 -0.4587 -0.0848 -0.1217 360 GLU A C   
456  O O   . GLU A 64  ? 1.4696 1.0903 1.0231 -0.4907 -0.0839 -0.1150 360 GLU A O   
457  C CB  . GLU A 64  ? 1.6365 0.9408 1.0247 -0.4154 -0.0788 -0.1122 360 GLU A CB  
458  C CG  . GLU A 64  ? 1.5964 0.9911 1.0602 -0.4199 -0.0757 -0.1028 360 GLU A CG  
459  C CD  . GLU A 64  ? 1.6365 1.0025 1.1172 -0.3520 -0.0710 -0.0952 360 GLU A CD  
460  O OE1 . GLU A 64  ? 1.7870 1.0242 1.1818 -0.3294 -0.0718 -0.0959 360 GLU A OE1 
461  O OE2 . GLU A 64  ? 1.5189 0.9895 1.0934 -0.3205 -0.0673 -0.0889 360 GLU A OE2 
462  N N   . PHE A 65  ? 1.4810 0.9906 1.0052 -0.4094 -0.0860 -0.1307 361 PHE A N   
463  C CA  . PHE A 65  ? 1.3658 1.0127 0.9892 -0.3909 -0.0863 -0.1301 361 PHE A CA  
464  C C   . PHE A 65  ? 1.4048 1.1110 1.0265 -0.4458 -0.0948 -0.1375 361 PHE A C   
465  O O   . PHE A 65  ? 1.3298 1.1620 1.0214 -0.4611 -0.0966 -0.1330 361 PHE A O   
466  C CB  . PHE A 65  ? 1.3133 0.9544 0.9616 -0.3246 -0.0830 -0.1337 361 PHE A CB  
467  C CG  . PHE A 65  ? 1.1934 0.9530 0.9231 -0.3093 -0.0847 -0.1335 361 PHE A CG  
468  C CD1 . PHE A 65  ? 1.1132 0.9695 0.9253 -0.2879 -0.0817 -0.1232 361 PHE A CD1 
469  C CD2 . PHE A 65  ? 1.1914 0.9577 0.9066 -0.3159 -0.0899 -0.1437 361 PHE A CD2 
470  C CE1 . PHE A 65  ? 1.0462 0.9961 0.9195 -0.2709 -0.0841 -0.1224 361 PHE A CE1 
471  C CE2 . PHE A 65  ? 1.1138 0.9821 0.8962 -0.2998 -0.0922 -0.1424 361 PHE A CE2 
472  C CZ  . PHE A 65  ? 1.0447 1.0014 0.9038 -0.2764 -0.0894 -0.1314 361 PHE A CZ  
473  N N   . LEU A 66  ? 1.4609 1.0870 1.0077 -0.4632 -0.0980 -0.1453 362 LEU A N   
474  C CA  . LEU A 66  ? 1.4377 1.1300 0.9903 -0.4999 -0.1025 -0.1458 362 LEU A CA  
475  C C   . LEU A 66  ? 1.4727 1.2373 1.0399 -0.5470 -0.0993 -0.1324 362 LEU A C   
476  O O   . LEU A 66  ? 1.4272 1.3083 1.0436 -0.5653 -0.1018 -0.1298 362 LEU A O   
477  C CB  . LEU A 66  ? 1.5491 1.1288 1.0084 -0.5098 -0.1048 -0.1541 362 LEU A CB  
478  C CG  . LEU A 66  ? 1.5447 1.0720 0.9874 -0.4641 -0.1074 -0.1696 362 LEU A CG  
479  C CD1 . LEU A 66  ? 1.6229 1.0522 0.9746 -0.4765 -0.1093 -0.1767 362 LEU A CD1 
480  C CD2 . LEU A 66  ? 1.4062 1.0565 0.9345 -0.4486 -0.1126 -0.1747 362 LEU A CD2 
481  N N   . ASP A 67  ? 1.4983 1.1977 1.0202 -0.5639 -0.0933 -0.1234 363 ASP A N   
482  C CA  . ASP A 67  ? 1.5185 1.2831 1.0444 -0.6107 -0.0888 -0.1109 363 ASP A CA  
483  C C   . ASP A 67  ? 1.4253 1.3396 1.0537 -0.5971 -0.0862 -0.1055 363 ASP A C   
484  O O   . ASP A 67  ? 1.4256 1.4442 1.0808 -0.6267 -0.0842 -0.0993 363 ASP A O   
485  C CB  . ASP A 67  ? 1.6171 1.2732 1.0681 -0.6270 -0.0832 -0.1023 363 ASP A CB  
486  C CG  . ASP A 67  ? 1.7858 1.3267 1.1246 -0.6646 -0.0847 -0.1016 363 ASP A CG  
487  O OD1 . ASP A 67  ? 1.8706 1.4588 1.1895 -0.7179 -0.0848 -0.0969 363 ASP A OD1 
488  O OD2 . ASP A 67  ? 1.8403 1.2429 1.1059 -0.6393 -0.0857 -0.1056 363 ASP A OD2 
489  N N   . GLN A 68  ? 1.3549 1.2819 1.0363 -0.5508 -0.0858 -0.1075 364 GLN A N   
490  C CA  . GLN A 68  ? 1.2876 1.3491 1.0587 -0.5331 -0.0832 -0.1018 364 GLN A CA  
491  C C   . GLN A 68  ? 1.2332 1.3960 1.0637 -0.5113 -0.0895 -0.1072 364 GLN A C   
492  O O   . GLN A 68  ? 1.2174 1.5023 1.1033 -0.5070 -0.0878 -0.1017 364 GLN A O   
493  C CB  . GLN A 68  ? 1.2250 1.2625 1.0256 -0.4961 -0.0803 -0.1001 364 GLN A CB  
494  C CG  . GLN A 68  ? 1.2122 1.2082 1.0279 -0.4467 -0.0844 -0.1084 364 GLN A CG  
495  C CD  . GLN A 68  ? 1.1921 1.1340 1.0162 -0.3980 -0.0767 -0.1007 364 GLN A CD  
496  O OE1 . GLN A 68  ? 1.0611 1.0476 0.9444 -0.3455 -0.0739 -0.0970 364 GLN A OE1 
497  N NE2 . GLN A 68  ? 1.2480 1.0898 1.0065 -0.4167 -0.0742 -0.0979 364 GLN A NE2 
498  N N   . TYR A 69  ? 1.2379 1.3494 1.0504 -0.4954 -0.0966 -0.1179 365 TYR A N   
499  C CA  . TYR A 69  ? 1.2037 1.4031 1.0620 -0.4771 -0.1035 -0.1224 365 TYR A CA  
500  C C   . TYR A 69  ? 1.2464 1.5167 1.0980 -0.5139 -0.1046 -0.1188 365 TYR A C   
501  O O   . TYR A 69  ? 1.2155 1.6053 1.1226 -0.4998 -0.1058 -0.1148 365 TYR A O   
502  C CB  . TYR A 69  ? 1.1970 1.3201 1.0250 -0.4583 -0.1101 -0.1353 365 TYR A CB  
503  C CG  . TYR A 69  ? 1.1504 1.3541 1.0105 -0.4472 -0.1179 -0.1392 365 TYR A CG  
504  C CD1 . TYR A 69  ? 1.0592 1.3761 0.9936 -0.4128 -0.1199 -0.1339 365 TYR A CD1 
505  C CD2 . TYR A 69  ? 1.2117 1.3746 1.0220 -0.4685 -0.1234 -0.1472 365 TYR A CD2 
506  C CE1 . TYR A 69  ? 1.0250 1.4102 0.9820 -0.3984 -0.1276 -0.1359 365 TYR A CE1 
507  C CE2 . TYR A 69  ? 1.1454 1.3826 0.9830 -0.4580 -0.1313 -0.1500 365 TYR A CE2 
508  C CZ  . TYR A 69  ? 1.0514 1.3993 0.9621 -0.4224 -0.1334 -0.1439 365 TYR A CZ  
509  O OH  . TYR A 69  ? 1.0191 1.4351 0.9508 -0.4076 -0.1416 -0.1453 365 TYR A OH  
510  N N   . TYR A 70  ? 1.3145 1.5097 1.0923 -0.5596 -0.1042 -0.1199 366 TYR A N   
511  C CA  . TYR A 70  ? 1.3633 1.6280 1.1298 -0.6014 -0.1052 -0.1162 366 TYR A CA  
512  C C   . TYR A 70  ? 1.3755 1.7317 1.1683 -0.6211 -0.0969 -0.1046 366 TYR A C   
513  O O   . TYR A 70  ? 1.4087 1.8749 1.2249 -0.6373 -0.0969 -0.1009 366 TYR A O   
514  C CB  . TYR A 70  ? 1.4790 1.6330 1.1510 -0.6478 -0.1071 -0.1198 366 TYR A CB  
515  C CG  . TYR A 70  ? 1.4851 1.5876 1.1340 -0.6331 -0.1159 -0.1322 366 TYR A CG  
516  C CD1 . TYR A 70  ? 1.4898 1.6695 1.1540 -0.6455 -0.1228 -0.1349 366 TYR A CD1 
517  C CD2 . TYR A 70  ? 1.4999 1.4798 1.1098 -0.6040 -0.1170 -0.1414 366 TYR A CD2 
518  C CE1 . TYR A 70  ? 1.4943 1.6274 1.1350 -0.6320 -0.1309 -0.1465 366 TYR A CE1 
519  C CE2 . TYR A 70  ? 1.5120 1.4465 1.0964 -0.5884 -0.1239 -0.1538 366 TYR A CE2 
520  C CZ  . TYR A 70  ? 1.5282 1.5387 1.1285 -0.6037 -0.1311 -0.1562 366 TYR A CZ  
521  O OH  . TYR A 70  ? 1.4790 1.4455 1.0517 -0.5885 -0.1381 -0.1687 366 TYR A OH  
522  N N   . SER A 71  ? 1.3547 1.6697 1.1415 -0.6189 -0.0896 -0.0990 367 SER A N   
523  C CA  . SER A 71  ? 1.3632 1.7741 1.1828 -0.6278 -0.0813 -0.0891 367 SER A CA  
524  C C   . SER A 71  ? 1.2721 1.8153 1.1780 -0.5793 -0.0818 -0.0885 367 SER A C   
525  O O   . SER A 71  ? 1.3059 1.9624 1.2376 -0.5868 -0.0774 -0.0830 367 SER A O   
526  C CB  . SER A 71  ? 1.3906 1.7290 1.1912 -0.6266 -0.0742 -0.0839 367 SER A CB  
527  O OG  . SER A 71  ? 1.3892 1.7816 1.1789 -0.6618 -0.0659 -0.0745 367 SER A OG  
528  N N   . SER A 72  ? 1.2257 1.7545 1.1696 -0.5283 -0.0874 -0.0941 368 SER A N   
529  C CA  . SER A 72  ? 1.1492 1.7845 1.1640 -0.4763 -0.0883 -0.0925 368 SER A CA  
530  C C   . SER A 72  ? 1.1935 1.9188 1.2254 -0.4713 -0.0943 -0.0943 368 SER A C   
531  O O   . SER A 72  ? 1.1759 2.0072 1.2520 -0.4386 -0.0926 -0.0904 368 SER A O   
532  C CB  . SER A 72  ? 1.0751 1.6606 1.1160 -0.4275 -0.0925 -0.0969 368 SER A CB  
533  O OG  . SER A 72  ? 1.0616 1.6775 1.1241 -0.3969 -0.1016 -0.1019 368 SER A OG  
534  N N   . ILE A 73  ? 1.2140 1.8972 1.2076 -0.5000 -0.1014 -0.1002 369 ILE A N   
535  C CA  . ILE A 73  ? 1.2283 1.9982 1.2347 -0.4996 -0.1075 -0.1015 369 ILE A CA  
536  C C   . ILE A 73  ? 1.3090 2.1321 1.2852 -0.5567 -0.1028 -0.0969 369 ILE A C   
537  O O   . ILE A 73  ? 1.3230 2.1992 1.2903 -0.5764 -0.1080 -0.0984 369 ILE A O   
538  C CB  . ILE A 73  ? 1.2349 1.9422 1.2183 -0.4971 -0.1185 -0.1108 369 ILE A CB  
539  C CG1 . ILE A 73  ? 1.3115 1.8916 1.2220 -0.5453 -0.1188 -0.1161 369 ILE A CG1 
540  C CG2 . ILE A 73  ? 1.1461 1.8287 1.1635 -0.4385 -0.1234 -0.1144 369 ILE A CG2 
541  C CD1 . ILE A 73  ? 1.2736 1.7850 1.1537 -0.5408 -0.1286 -0.1270 369 ILE A CD1 
542  N N   . LYS A 74  ? 1.3775 2.1894 1.3354 -0.5852 -0.0932 -0.0908 370 LYS A N   
543  C CA  . LYS A 74  ? 1.4200 2.2928 1.3483 -0.6408 -0.0873 -0.0847 370 LYS A CA  
544  C C   . LYS A 74  ? 1.5348 2.3565 1.3984 -0.7000 -0.0926 -0.0876 370 LYS A C   
545  O O   . LYS A 74  ? 1.6241 2.5242 1.4701 -0.7429 -0.0913 -0.0839 370 LYS A O   
546  C CB  . LYS A 74  ? 1.3729 2.4077 1.3521 -0.6169 -0.0844 -0.0807 370 LYS A CB  
547  C CG  . LYS A 74  ? 1.3407 2.4195 1.3832 -0.5410 -0.0832 -0.0805 370 LYS A CG  
548  C CD  . LYS A 74  ? 1.3045 2.4642 1.3693 -0.5290 -0.0724 -0.0740 370 LYS A CD  
549  C CE  . LYS A 74  ? 1.3076 2.4636 1.4195 -0.4570 -0.0715 -0.0743 370 LYS A CE  
550  N NZ  . LYS A 74  ? 1.2266 2.4867 1.3662 -0.4266 -0.0629 -0.0698 370 LYS A NZ  
551  N N   . ARG A 75  ? 1.5000 2.1903 1.3238 -0.7021 -0.0987 -0.0945 371 ARG A N   
552  C CA  . ARG A 75  ? 1.5496 2.1578 1.2956 -0.7578 -0.1031 -0.0976 371 ARG A CA  
553  C C   . ARG A 75  ? 1.5949 2.0429 1.2713 -0.7761 -0.1002 -0.0981 371 ARG A C   
554  O O   . ARG A 75  ? 1.6322 1.9633 1.2593 -0.7760 -0.1059 -0.1059 371 ARG A O   
555  C CB  . ARG A 75  ? 1.5312 2.1289 1.2820 -0.7392 -0.1143 -0.1072 371 ARG A CB  
556  C CG  . ARG A 75  ? 1.4863 2.2350 1.2975 -0.7186 -0.1183 -0.1061 371 ARG A CG  
557  C CD  . ARG A 75  ? 1.4766 2.2297 1.3365 -0.6536 -0.1264 -0.1130 371 ARG A CD  
558  N NE  . ARG A 75  ? 1.4925 2.3055 1.3583 -0.6543 -0.1360 -0.1170 371 ARG A NE  
559  C CZ  . ARG A 75  ? 1.5925 2.3307 1.4067 -0.6820 -0.1440 -0.1247 371 ARG A CZ  
560  N NH1 . ARG A 75  ? 1.6681 2.2646 1.4162 -0.7088 -0.1430 -0.1296 371 ARG A NH1 
561  N NH2 . ARG A 75  ? 1.5755 2.3793 1.4002 -0.6800 -0.1532 -0.1278 371 ARG A NH2 
562  N N   . PHE A 76  ? 1.6032 2.0448 1.2721 -0.7879 -0.0912 -0.0901 372 PHE A N   
563  C CA  . PHE A 76  ? 1.6474 1.9390 1.2462 -0.8022 -0.0881 -0.0888 372 PHE A CA  
564  C C   . PHE A 76  ? 1.7575 1.9561 1.2521 -0.8659 -0.0901 -0.0877 372 PHE A C   
565  O O   . PHE A 76  ? 1.7424 2.0059 1.2121 -0.9199 -0.0880 -0.0814 372 PHE A O   
566  C CB  . PHE A 76  ? 1.5865 1.9037 1.1988 -0.8046 -0.0784 -0.0794 372 PHE A CB  
567  C CG  . PHE A 76  ? 1.6207 1.7856 1.1642 -0.8107 -0.0755 -0.0772 372 PHE A CG  
568  C CD1 . PHE A 76  ? 1.6975 1.7579 1.1357 -0.8663 -0.0751 -0.0731 372 PHE A CD1 
569  C CD2 . PHE A 76  ? 1.6177 1.7423 1.1962 -0.7600 -0.0736 -0.0785 372 PHE A CD2 
570  C CE1 . PHE A 76  ? 1.8161 1.7314 1.1838 -0.8652 -0.0730 -0.0704 372 PHE A CE1 
571  C CE2 . PHE A 76  ? 1.7370 1.7239 1.2501 -0.7612 -0.0712 -0.0760 372 PHE A CE2 
572  C CZ  . PHE A 76  ? 1.8286 1.7094 1.2353 -0.8110 -0.0710 -0.0719 372 PHE A CZ  
573  N N   . GLY A 77  ? 1.9181 1.9619 1.3454 -0.8588 -0.0938 -0.0937 373 GLY A N   
574  C CA  . GLY A 77  ? 2.1185 2.0436 1.4301 -0.9137 -0.0952 -0.0917 373 GLY A CA  
575  C C   . GLY A 77  ? 2.1480 2.1158 1.4347 -0.9570 -0.1013 -0.0943 373 GLY A C   
576  O O   . GLY A 77  ? 2.3170 2.2069 1.5052 -1.0146 -0.1022 -0.0906 373 GLY A O   
577  N N   . SER A 78  ? 1.8892 1.9774 1.2588 -0.9303 -0.1060 -0.1000 374 SER A N   
578  C CA  . SER A 78  ? 1.8428 1.9748 1.1938 -0.9657 -0.1130 -0.1033 374 SER A CA  
579  C C   . SER A 78  ? 1.9306 1.9105 1.2013 -0.9659 -0.1200 -0.1131 374 SER A C   
580  O O   . SER A 78  ? 1.9676 1.8108 1.1939 -0.9373 -0.1188 -0.1170 374 SER A O   
581  C CB  . SER A 78  ? 1.7271 2.0170 1.1838 -0.9270 -0.1171 -0.1071 374 SER A CB  
582  O OG  . SER A 78  ? 1.7026 1.9640 1.2090 -0.8581 -0.1210 -0.1163 374 SER A OG  
583  N N   . LYS A 79  ? 1.8733 1.8792 1.1217 -0.9967 -0.1274 -0.1173 375 LYS A N   
584  C CA  . LYS A 79  ? 1.9459 1.8207 1.1234 -0.9918 -0.1347 -0.1283 375 LYS A CA  
585  C C   . LYS A 79  ? 1.8628 1.7276 1.1000 -0.9156 -0.1387 -0.1408 375 LYS A C   
586  O O   . LYS A 79  ? 1.9207 1.6469 1.1016 -0.8876 -0.1398 -0.1495 375 LYS A O   
587  C CB  . LYS A 79  ? 1.9750 1.8938 1.1209 -1.0440 -0.1422 -0.1298 375 LYS A CB  
588  C CG  . LYS A 79  ? 2.1204 1.8915 1.1706 -1.0523 -0.1492 -0.1400 375 LYS A CG  
589  C CD  . LYS A 79  ? 2.2554 1.8811 1.1723 -1.1101 -0.1462 -0.1327 375 LYS A CD  
590  C CE  . LYS A 79  ? 2.3554 1.8429 1.1713 -1.1214 -0.1536 -0.1424 375 LYS A CE  
591  N NZ  . LYS A 79  ? 2.3133 1.7249 1.1458 -1.0433 -0.1557 -0.1571 375 LYS A NZ  
592  N N   . ALA A 80  ? 1.7837 1.7932 1.1286 -0.8795 -0.1407 -0.1416 376 ALA A N   
593  C CA  . ALA A 80  ? 1.7473 1.7519 1.1451 -0.8107 -0.1446 -0.1523 376 ALA A CA  
594  C C   . ALA A 80  ? 1.7766 1.6905 1.1699 -0.7707 -0.1377 -0.1529 376 ALA A C   
595  O O   . ALA A 80  ? 1.7823 1.6236 1.1689 -0.7245 -0.1398 -0.1636 376 ALA A O   
596  C CB  . ALA A 80  ? 1.6135 1.7871 1.1193 -0.7798 -0.1478 -0.1501 376 ALA A CB  
597  N N   . HIS A 81  ? 1.7714 1.6883 1.1632 -0.7885 -0.1294 -0.1416 377 HIS A N   
598  C CA  . HIS A 81  ? 1.8010 1.6264 1.1798 -0.7553 -0.1231 -0.1409 377 HIS A CA  
599  C C   . HIS A 81  ? 1.9278 1.5724 1.1915 -0.7627 -0.1225 -0.1453 377 HIS A C   
600  O O   . HIS A 81  ? 1.9193 1.4739 1.1661 -0.7135 -0.1221 -0.1539 377 HIS A O   
601  C CB  . HIS A 81  ? 1.7824 1.6651 1.1871 -0.7750 -0.1147 -0.1271 377 HIS A CB  
602  C CG  . HIS A 81  ? 1.7947 1.5894 1.1856 -0.7446 -0.1086 -0.1248 377 HIS A CG  
603  N ND1 . HIS A 81  ? 1.7728 1.5878 1.1679 -0.7624 -0.1009 -0.1131 377 HIS A ND1 
604  C CD2 . HIS A 81  ? 1.7810 1.4715 1.1526 -0.6966 -0.1088 -0.1328 377 HIS A CD2 
605  C CE1 . HIS A 81  ? 1.7473 1.4717 1.1269 -0.7273 -0.0975 -0.1134 377 HIS A CE1 
606  N NE2 . HIS A 81  ? 1.7661 1.4156 1.1315 -0.6863 -0.1020 -0.1252 377 HIS A NE2 
607  N N   . MET A 82  ? 2.0980 1.6867 1.2756 -0.8222 -0.1222 -0.1389 378 MET A N   
608  C CA  . MET A 82  ? 2.2022 1.6102 1.2571 -0.8285 -0.1216 -0.1406 378 MET A CA  
609  C C   . MET A 82  ? 2.2103 1.5389 1.2293 -0.7940 -0.1274 -0.1559 378 MET A C   
610  O O   . MET A 82  ? 2.2984 1.4805 1.2373 -0.7644 -0.1255 -0.1603 378 MET A O   
611  C CB  . MET A 82  ? 2.3349 1.7050 1.2990 -0.9057 -0.1214 -0.1302 378 MET A CB  
612  C CG  . MET A 82  ? 2.4430 1.8159 1.3912 -0.9348 -0.1139 -0.1155 378 MET A CG  
613  S SD  . MET A 82  ? 2.5340 1.7464 1.4240 -0.8828 -0.1088 -0.1141 378 MET A SD  
614  C CE  . MET A 82  ? 2.6871 1.7018 1.4261 -0.8863 -0.1138 -0.1200 378 MET A CE  
615  N N   . ASP A 83  ? 2.0538 1.4760 1.1259 -0.7940 -0.1341 -0.1639 379 ASP A N   
616  C CA  . ASP A 83  ? 2.0739 1.4264 1.1138 -0.7586 -0.1390 -0.1793 379 ASP A CA  
617  C C   . ASP A 83  ? 1.9866 1.3353 1.0796 -0.6837 -0.1361 -0.1885 379 ASP A C   
618  O O   . ASP A 83  ? 1.9963 1.2339 1.0326 -0.6423 -0.1346 -0.1991 379 ASP A O   
619  C CB  . ASP A 83  ? 2.0269 1.4774 1.0996 -0.7837 -0.1479 -0.1846 379 ASP A CB  
620  C CG  . ASP A 83  ? 2.1033 1.5019 1.0847 -0.8510 -0.1516 -0.1808 379 ASP A CG  
621  O OD1 . ASP A 83  ? 2.2628 1.5058 1.1351 -0.8528 -0.1511 -0.1848 379 ASP A OD1 
622  O OD2 . ASP A 83  ? 2.1018 1.6134 1.1152 -0.9016 -0.1546 -0.1731 379 ASP A OD2 
623  N N   . ARG A 84  ? 1.9191 1.3887 1.1163 -0.6645 -0.1346 -0.1841 380 ARG A N   
624  C CA  . ARG A 84  ? 1.8151 1.2822 1.0595 -0.6001 -0.1312 -0.1906 380 ARG A CA  
625  C C   . ARG A 84  ? 1.8743 1.2188 1.0623 -0.5753 -0.1231 -0.1876 380 ARG A C   
626  O O   . ARG A 84  ? 1.8803 1.1672 1.0612 -0.5186 -0.1196 -0.1963 380 ARG A O   
627  C CB  . ARG A 84  ? 1.6777 1.2981 1.0377 -0.5909 -0.1319 -0.1840 380 ARG A CB  
628  C CG  . ARG A 84  ? 1.5757 1.2032 0.9849 -0.5317 -0.1291 -0.1897 380 ARG A CG  
629  C CD  . ARG A 84  ? 1.5377 1.2067 0.9740 -0.5024 -0.1350 -0.2014 380 ARG A CD  
630  N NE  . ARG A 84  ? 1.4682 1.1342 0.9378 -0.4490 -0.1311 -0.2071 380 ARG A NE  
631  C CZ  . ARG A 84  ? 1.5004 1.0710 0.9179 -0.4090 -0.1267 -0.2195 380 ARG A CZ  
632  N NH1 . ARG A 84  ? 1.5394 1.0094 0.8722 -0.4110 -0.1259 -0.2277 380 ARG A NH1 
633  N NH2 . ARG A 84  ? 1.3744 0.9731 0.8491 -0.3463 -0.1158 -0.2123 380 ARG A NH2 
634  N N   . LEU A 85  ? 1.9363 1.2442 1.0823 -0.6150 -0.1198 -0.1747 381 LEU A N   
635  C CA  . LEU A 85  ? 2.0287 1.2047 1.1023 -0.5924 -0.1136 -0.1706 381 LEU A CA  
636  C C   . LEU A 85  ? 2.1238 1.1509 1.0868 -0.5721 -0.1141 -0.1790 381 LEU A C   
637  O O   . LEU A 85  ? 2.1516 1.0901 1.0803 -0.5131 -0.1096 -0.1839 381 LEU A O   
638  C CB  . LEU A 85  ? 2.0761 1.2456 1.1185 -0.6454 -0.1107 -0.1541 381 LEU A CB  
639  C CG  . LEU A 85  ? 2.0498 1.1758 1.0890 -0.6213 -0.1042 -0.1452 381 LEU A CG  
640  C CD1 . LEU A 85  ? 1.9150 1.1741 1.0759 -0.6011 -0.1021 -0.1434 381 LEU A CD1 
641  C CD2 . LEU A 85  ? 2.1359 1.2090 1.0991 -0.6770 -0.1019 -0.1305 381 LEU A CD2 
642  N N   . GLU A 86  ? 2.1659 1.1669 1.0702 -0.6177 -0.1193 -0.1803 382 GLU A N   
643  C CA  . GLU A 86  ? 2.2433 1.1077 1.0420 -0.5978 -0.1204 -0.1891 382 GLU A CA  
644  C C   . GLU A 86  ? 2.1762 1.0530 1.0106 -0.5322 -0.1195 -0.2058 382 GLU A C   
645  O O   . GLU A 86  ? 2.2798 1.0491 1.0515 -0.4766 -0.1149 -0.2123 382 GLU A O   
646  C CB  . GLU A 86  ? 2.3353 1.1871 1.0744 -0.6647 -0.1271 -0.1878 382 GLU A CB  
647  C CG  . GLU A 86  ? 2.4659 1.1649 1.0812 -0.6515 -0.1286 -0.1951 382 GLU A CG  
648  C CD  . GLU A 86  ? 2.6398 1.1936 1.1274 -0.6777 -0.1271 -0.1826 382 GLU A CD  
649  O OE1 . GLU A 86  ? 2.6489 1.2187 1.1487 -0.6972 -0.1238 -0.1693 382 GLU A OE1 
650  O OE2 . GLU A 86  ? 2.7698 1.1914 1.1399 -0.6790 -0.1295 -0.1856 382 GLU A OE2 
651  N N   . GLU A 87  ? 2.0491 1.0603 0.9804 -0.5358 -0.1236 -0.2121 383 GLU A N   
652  C CA  . GLU A 87  ? 1.9946 1.0271 0.9580 -0.4795 -0.1227 -0.2275 383 GLU A CA  
653  C C   . GLU A 87  ? 2.0590 1.0537 1.0343 -0.4088 -0.1134 -0.2303 383 GLU A C   
654  O O   . GLU A 87  ? 2.0249 0.9548 0.9599 -0.3527 -0.1080 -0.2412 383 GLU A O   
655  C CB  . GLU A 87  ? 1.8305 1.0216 0.8990 -0.4963 -0.1294 -0.2296 383 GLU A CB  
656  C CG  . GLU A 87  ? 1.8321 1.0524 0.9271 -0.4484 -0.1294 -0.2445 383 GLU A CG  
657  C CD  . GLU A 87  ? 1.7679 1.1347 0.9481 -0.4703 -0.1386 -0.2443 383 GLU A CD  
658  O OE1 . GLU A 87  ? 1.6450 1.1167 0.9037 -0.4882 -0.1409 -0.2334 383 GLU A OE1 
659  O OE2 . GLU A 87  ? 1.7502 1.1278 0.9164 -0.4663 -0.1435 -0.2544 383 GLU A OE2 
660  N N   . VAL A 88  ? 2.0267 1.0645 1.0555 -0.4084 -0.1106 -0.2201 384 VAL A N   
661  C CA  . VAL A 88  ? 2.0125 1.0304 1.0619 -0.3422 -0.1024 -0.2223 384 VAL A CA  
662  C C   . VAL A 88  ? 2.1577 1.0329 1.1093 -0.3063 -0.0963 -0.2187 384 VAL A C   
663  O O   . VAL A 88  ? 2.1476 0.9806 1.0826 -0.2363 -0.0889 -0.2252 384 VAL A O   
664  C CB  . VAL A 88  ? 1.8730 0.9879 1.0136 -0.3533 -0.1024 -0.2127 384 VAL A CB  
665  C CG1 . VAL A 88  ? 1.8680 0.9508 1.0187 -0.2880 -0.0942 -0.2136 384 VAL A CG1 
666  C CG2 . VAL A 88  ? 1.7021 0.9594 0.9376 -0.3721 -0.1085 -0.2160 384 VAL A CG2 
667  N N   . ASN A 89  ? 2.2781 1.0825 1.1616 -0.3510 -0.0991 -0.2071 385 ASN A N   
668  C CA  . ASN A 89  ? 2.3801 1.0365 1.1501 -0.3210 -0.0958 -0.2027 385 ASN A CA  
669  C C   . ASN A 89  ? 2.4166 1.0016 1.1229 -0.2746 -0.0938 -0.2157 385 ASN A C   
670  O O   . ASN A 89  ? 2.5167 1.0430 1.1894 -0.2014 -0.0870 -0.2184 385 ASN A O   
671  C CB  . ASN A 89  ? 2.5018 1.0936 1.1945 -0.3908 -0.1007 -0.1894 385 ASN A CB  
672  C CG  . ASN A 89  ? 2.6762 1.1229 1.2576 -0.3634 -0.0983 -0.1795 385 ASN A CG  
673  O OD1 . ASN A 89  ? 2.8094 1.1355 1.2762 -0.3630 -0.1004 -0.1797 385 ASN A OD1 
674  N ND2 . ASN A 89  ? 2.6616 1.1174 1.2713 -0.3402 -0.0947 -0.1703 385 ASN A ND2 
675  N N   . LYS A 90  ? 2.3916 0.9908 1.0838 -0.3140 -0.0993 -0.2234 386 LYS A N   
676  C CA  . LYS A 90  ? 2.4776 1.0090 1.1054 -0.2740 -0.0974 -0.2359 386 LYS A CA  
677  C C   . LYS A 90  ? 2.4207 1.0113 1.1103 -0.1977 -0.0887 -0.2479 386 LYS A C   
678  O O   . LYS A 90  ? 2.4743 0.9967 1.1081 -0.1327 -0.0818 -0.2536 386 LYS A O   
679  C CB  . LYS A 90  ? 2.5049 1.0583 1.1187 -0.3349 -0.1058 -0.2420 386 LYS A CB  
680  C CG  . LYS A 90  ? 2.6295 1.1003 1.1522 -0.4053 -0.1127 -0.2307 386 LYS A CG  
681  C CD  . LYS A 90  ? 2.6235 1.1258 1.1351 -0.4662 -0.1214 -0.2363 386 LYS A CD  
682  C CE  . LYS A 90  ? 2.7256 1.1340 1.1316 -0.5354 -0.1269 -0.2242 386 LYS A CE  
683  N NZ  . LYS A 90  ? 2.7688 1.2375 1.1810 -0.6085 -0.1359 -0.2260 386 LYS A NZ  
684  N N   . GLU A 91  ? 2.2915 1.0113 1.0924 -0.2028 -0.0885 -0.2507 387 GLU A N   
685  C CA  . GLU A 91  ? 2.2183 0.9957 1.0722 -0.1339 -0.0791 -0.2605 387 GLU A CA  
686  C C   . GLU A 91  ? 2.2663 1.0106 1.1157 -0.0658 -0.0694 -0.2543 387 GLU A C   
687  O O   . GLU A 91  ? 2.2823 1.0264 1.1264 0.0062  -0.0590 -0.2606 387 GLU A O   
688  C CB  . GLU A 91  ? 2.0657 0.9811 1.0278 -0.1591 -0.0827 -0.2633 387 GLU A CB  
689  C CG  . GLU A 91  ? 1.9855 0.9611 0.9912 -0.0976 -0.0731 -0.2735 387 GLU A CG  
690  C CD  . GLU A 91  ? 1.8515 0.9715 0.9708 -0.1196 -0.0763 -0.2673 387 GLU A CD  
691  O OE1 . GLU A 91  ? 1.7765 0.9445 0.9337 -0.1805 -0.0872 -0.2601 387 GLU A OE1 
692  O OE2 . GLU A 91  ? 1.7867 0.9919 0.9721 -0.0728 -0.0660 -0.2628 387 GLU A OE2 
693  N N   . ILE A 92  ? 2.2818 1.0076 1.1351 -0.0856 -0.0721 -0.2410 388 ILE A N   
694  C CA  . ILE A 92  ? 2.3244 1.0085 1.1601 -0.0213 -0.0648 -0.2334 388 ILE A CA  
695  C C   . ILE A 92  ? 2.4579 1.0121 1.1760 0.0162  -0.0634 -0.2309 388 ILE A C   
696  O O   . ILE A 92  ? 2.5077 1.0356 1.2050 0.0882  -0.0568 -0.2270 388 ILE A O   
697  C CB  . ILE A 92  ? 2.2600 0.9573 1.1273 -0.0538 -0.0686 -0.2194 388 ILE A CB  
698  C CG1 . ILE A 92  ? 2.1175 0.9435 1.0987 -0.0829 -0.0703 -0.2215 388 ILE A CG1 
699  C CG2 . ILE A 92  ? 2.3072 0.9663 1.1565 0.0141  -0.0626 -0.2108 388 ILE A CG2 
700  C CD1 . ILE A 92  ? 2.0803 0.9279 1.0941 -0.1275 -0.0748 -0.2079 388 ILE A CD1 
701  N N   . GLU A 93  ? 2.5047 0.9788 1.1415 -0.0289 -0.0701 -0.2321 389 GLU A N   
702  C CA  . GLU A 93  ? 2.6376 0.9890 1.1584 0.0154  -0.0686 -0.2322 389 GLU A CA  
703  C C   . GLU A 93  ? 2.6000 0.9938 1.1414 0.0833  -0.0593 -0.2457 389 GLU A C   
704  O O   . GLU A 93  ? 2.6072 1.0038 1.1457 0.1633  -0.0509 -0.2440 389 GLU A O   
705  C CB  . GLU A 93  ? 2.7220 0.9753 1.1454 -0.0512 -0.0779 -0.2307 389 GLU A CB  
706  C CG  . GLU A 93  ? 2.7863 1.0041 1.1834 -0.1229 -0.0854 -0.2158 389 GLU A CG  
707  C CD  . GLU A 93  ? 2.9622 1.0605 1.2617 -0.0903 -0.0856 -0.2021 389 GLU A CD  
708  O OE1 . GLU A 93  ? 3.0339 1.0468 1.2531 -0.0225 -0.0828 -0.2041 389 GLU A OE1 
709  O OE2 . GLU A 93  ? 2.9744 1.0672 1.2749 -0.1313 -0.0887 -0.1890 389 GLU A OE2 
710  N N   . SER A 94  ? 2.6131 1.0535 1.1805 0.0503  -0.0607 -0.2582 390 SER A N   
711  C CA  . SER A 94  ? 2.5311 1.0152 1.1141 0.1006  -0.0519 -0.2718 390 SER A CA  
712  C C   . SER A 94  ? 2.4991 1.0809 1.1613 0.1754  -0.0387 -0.2724 390 SER A C   
713  O O   . SER A 94  ? 2.5356 1.1006 1.1651 0.2500  -0.0295 -0.2731 390 SER A O   
714  C CB  . SER A 94  ? 2.5067 1.0610 1.1365 0.0409  -0.0573 -0.2827 390 SER A CB  
715  O OG  . SER A 94  ? 2.5717 1.2035 1.2458 0.0869  -0.0473 -0.2945 390 SER A OG  
716  N N   . THR A 95  ? 2.4148 1.1043 1.1795 0.1556  -0.0379 -0.2713 391 THR A N   
717  C CA  . THR A 95  ? 2.3385 1.1365 1.1859 0.2160  -0.0253 -0.2717 391 THR A CA  
718  C C   . THR A 95  ? 2.3268 1.1395 1.2067 0.2427  -0.0240 -0.2585 391 THR A C   
719  O O   . THR A 95  ? 2.2338 1.1427 1.1848 0.2915  -0.0139 -0.2565 391 THR A O   
720  C CB  . THR A 95  ? 2.2107 1.1224 1.1463 0.1822  -0.0251 -0.2794 391 THR A CB  
721  O OG1 . THR A 95  ? 2.1563 1.0912 1.1369 0.1218  -0.0358 -0.2733 391 THR A OG1 
722  C CG2 . THR A 95  ? 2.1904 1.0918 1.0954 0.1469  -0.0294 -0.2913 391 THR A CG2 
723  N N   . SER A 96  ? 2.4655 1.1913 1.2953 0.2098  -0.0336 -0.2485 392 SER A N   
724  C CA  . SER A 96  ? 2.4708 1.2038 1.3259 0.2273  -0.0342 -0.2353 392 SER A CA  
725  C C   . SER A 96  ? 2.3506 1.1978 1.3167 0.2066  -0.0331 -0.2351 392 SER A C   
726  O O   . SER A 96  ? 2.3716 1.2543 1.3789 0.2352  -0.0308 -0.2258 392 SER A O   
727  C CB  . SER A 96  ? 2.5428 1.2716 1.3748 0.3178  -0.0260 -0.2289 392 SER A CB  
728  O OG  . SER A 96  ? 2.4727 1.3195 1.3782 0.3702  -0.0136 -0.2345 392 SER A OG  
729  N N   . THR A 97  ? 2.1645 1.0688 1.1750 0.1582  -0.0360 -0.2448 393 THR A N   
730  C CA  . THR A 97  ? 1.9991 1.0317 1.1291 0.1223  -0.0380 -0.2338 393 THR A CA  
731  C C   . THR A 97  ? 1.9334 0.9889 1.0761 0.0473  -0.0478 -0.2384 393 THR A C   
732  O O   . THR A 97  ? 2.0217 0.9725 1.0664 0.0159  -0.0549 -0.2529 393 THR A O   
733  C CB  . THR A 97  ? 1.8589 1.0314 1.0917 0.1737  -0.0258 -0.2251 393 THR A CB  
734  O OG1 . THR A 97  ? 1.7246 1.0222 1.0726 0.1320  -0.0288 -0.2110 393 THR A OG1 
735  C CG2 . THR A 97  ? 1.9117 1.0971 1.1220 0.2050  -0.0175 -0.2377 393 THR A CG2 
736  N N   . TYR A 98  ? 1.7324 0.9223 0.9896 0.0183  -0.0492 -0.2264 394 TYR A N   
737  C CA  . TYR A 98  ? 1.6627 0.8926 0.9388 -0.0452 -0.0592 -0.2297 394 TYR A CA  
738  C C   . TYR A 98  ? 1.5284 0.9110 0.9289 -0.0456 -0.0569 -0.2167 394 TYR A C   
739  O O   . TYR A 98  ? 1.4677 0.9170 0.9343 -0.0052 -0.0481 -0.2054 394 TYR A O   
740  C CB  . TYR A 98  ? 1.7026 0.8786 0.9391 -0.1144 -0.0717 -0.2291 394 TYR A CB  
741  C CG  . TYR A 98  ? 1.5957 0.8407 0.9091 -0.1318 -0.0727 -0.2120 394 TYR A CG  
742  C CD1 . TYR A 98  ? 1.6720 0.8644 0.9659 -0.1034 -0.0682 -0.2048 394 TYR A CD1 
743  C CD2 . TYR A 98  ? 1.5230 0.8841 0.9230 -0.1732 -0.0784 -0.2034 394 TYR A CD2 
744  C CE1 . TYR A 98  ? 1.5840 0.8360 0.9430 -0.1196 -0.0690 -0.1899 394 TYR A CE1 
745  C CE2 . TYR A 98  ? 1.4266 0.8486 0.8915 -0.1855 -0.0784 -0.1888 394 TYR A CE2 
746  C CZ  . TYR A 98  ? 1.4793 0.8451 0.9232 -0.1608 -0.0735 -0.1824 394 TYR A CZ  
747  O OH  . TYR A 98  ? 1.3938 0.8171 0.8978 -0.1731 -0.0734 -0.1686 394 TYR A OH  
748  N N   . GLN A 99  ? 1.4585 0.8931 0.8837 -0.0926 -0.0661 -0.2183 395 GLN A N   
749  C CA  . GLN A 99  ? 1.3379 0.8991 0.8594 -0.0924 -0.0658 -0.2080 395 GLN A CA  
750  C C   . GLN A 99  ? 1.2798 0.8977 0.8407 -0.1486 -0.0783 -0.2020 395 GLN A C   
751  O O   . GLN A 99  ? 1.2925 0.8725 0.8019 -0.1972 -0.0889 -0.2110 395 GLN A O   
752  C CB  . GLN A 99  ? 1.3219 0.8997 0.8285 -0.0811 -0.0643 -0.2171 395 GLN A CB  
753  C CG  . GLN A 99  ? 1.3186 0.8603 0.7906 -0.0223 -0.0501 -0.2235 395 GLN A CG  
754  C CD  . GLN A 99  ? 1.2605 0.8819 0.8087 0.0214  -0.0379 -0.2089 395 GLN A CD  
755  O OE1 . GLN A 99  ? 1.2585 0.9708 0.8866 0.0095  -0.0396 -0.1951 395 GLN A OE1 
756  N NE2 . GLN A 99  ? 1.2548 0.8411 0.7733 0.0726  -0.0262 -0.2118 395 GLN A NE2 
757  N N   . LEU A 100 ? 1.2104 0.9217 0.8584 -0.1420 -0.0771 -0.1872 396 LEU A N   
758  C CA  . LEU A 100 ? 1.1353 0.9138 0.8259 -0.1846 -0.0872 -0.1806 396 LEU A CA  
759  C C   . LEU A 100 ? 1.1026 0.9491 0.8130 -0.2021 -0.0961 -0.1832 396 LEU A C   
760  O O   . LEU A 100 ? 1.0766 0.9505 0.8046 -0.1718 -0.0922 -0.1822 396 LEU A O   
761  C CB  . LEU A 100 ? 1.0462 0.8913 0.8135 -0.1646 -0.0827 -0.1647 396 LEU A CB  
762  C CG  . LEU A 100 ? 1.0916 0.8849 0.8487 -0.1472 -0.0754 -0.1599 396 LEU A CG  
763  C CD1 . LEU A 100 ? 1.0225 0.8835 0.8541 -0.1191 -0.0702 -0.1454 396 LEU A CD1 
764  C CD2 . LEU A 100 ? 1.1364 0.8900 0.8575 -0.1928 -0.0816 -0.1615 396 LEU A CD2 
765  N N   . LYS A 101 ? 1.1201 0.9985 0.8259 -0.2521 -0.1085 -0.1857 397 LYS A N   
766  C CA  . LYS A 101 ? 1.0893 1.0617 0.8328 -0.2649 -0.1188 -0.1839 397 LYS A CA  
767  C C   . LYS A 101 ? 1.0169 1.0732 0.8401 -0.2288 -0.1152 -0.1687 397 LYS A C   
768  O O   . LYS A 101 ? 0.9827 1.0401 0.8376 -0.2118 -0.1078 -0.1595 397 LYS A O   
769  C CB  . LYS A 101 ? 1.0961 1.1087 0.8303 -0.3246 -0.1322 -0.1872 397 LYS A CB  
770  C CG  . LYS A 101 ? 1.1653 1.0915 0.8102 -0.3721 -0.1385 -0.2024 397 LYS A CG  
771  C CD  . LYS A 101 ? 1.2359 1.1668 0.8508 -0.3767 -0.1468 -0.2129 397 LYS A CD  
772  C CE  . LYS A 101 ? 1.3321 1.1314 0.8442 -0.3908 -0.1459 -0.2293 397 LYS A CE  
773  N NZ  . LYS A 101 ? 1.2700 1.0620 0.7632 -0.3630 -0.1459 -0.2373 397 LYS A NZ  
774  N N   . ASP A 102 ? 0.9870 1.1074 0.8352 -0.2174 -0.1214 -0.1659 398 ASP A N   
775  C CA  . ASP A 102 ? 0.9083 1.0990 0.8183 -0.1864 -0.1205 -0.1516 398 ASP A CA  
776  C C   . ASP A 102 ? 0.9127 1.1574 0.8596 -0.2012 -0.1242 -0.1449 398 ASP A C   
777  O O   . ASP A 102 ? 0.8159 1.0706 0.7985 -0.1765 -0.1175 -0.1346 398 ASP A O   
778  C CB  . ASP A 102 ? 0.9682 1.2156 0.8867 -0.1760 -0.1298 -0.1498 398 ASP A CB  
779  C CG  . ASP A 102 ? 0.9956 1.1988 0.8855 -0.1539 -0.1234 -0.1529 398 ASP A CG  
780  O OD1 . ASP A 102 ? 1.0259 1.1601 0.8887 -0.1459 -0.1117 -0.1581 398 ASP A OD1 
781  O OD2 . ASP A 102 ? 1.0207 1.2610 0.9131 -0.1420 -0.1297 -0.1497 398 ASP A OD2 
782  N N   . THR A 103 ? 0.9005 1.1826 0.8364 -0.2443 -0.1346 -0.1509 399 THR A N   
783  C CA  . THR A 103 ? 0.8599 1.2036 0.8292 -0.2613 -0.1367 -0.1450 399 THR A CA  
784  C C   . THR A 103 ? 0.8823 1.1629 0.8462 -0.2629 -0.1254 -0.1420 399 THR A C   
785  O O   . THR A 103 ? 0.8485 1.1641 0.8522 -0.2462 -0.1209 -0.1325 399 THR A O   
786  C CB  . THR A 103 ? 0.9020 1.2968 0.8527 -0.3169 -0.1491 -0.1528 399 THR A CB  
787  O OG1 . THR A 103 ? 0.9632 1.2646 0.8457 -0.3553 -0.1494 -0.1650 399 THR A OG1 
788  C CG2 . THR A 103 ? 0.8068 1.2892 0.7740 -0.3095 -0.1623 -0.1534 399 THR A CG2 
789  N N   . GLU A 104 ? 0.9637 1.1467 0.8723 -0.2796 -0.1210 -0.1503 400 GLU A N   
790  C CA  . GLU A 104 ? 0.9531 1.0681 0.8474 -0.2768 -0.1113 -0.1473 400 GLU A CA  
791  C C   . GLU A 104 ? 0.9072 1.0186 0.8410 -0.2240 -0.1014 -0.1375 400 GLU A C   
792  O O   . GLU A 104 ? 0.8849 0.9912 0.8379 -0.2162 -0.0958 -0.1301 400 GLU A O   
793  C CB  . GLU A 104 ? 1.0364 1.0379 0.8520 -0.2941 -0.1095 -0.1587 400 GLU A CB  
794  C CG  . GLU A 104 ? 1.0982 1.0839 0.8612 -0.3578 -0.1193 -0.1677 400 GLU A CG  
795  C CD  . GLU A 104 ? 1.2073 1.0725 0.8794 -0.3697 -0.1198 -0.1812 400 GLU A CD  
796  O OE1 . GLU A 104 ? 1.2127 1.0171 0.8698 -0.3216 -0.1111 -0.1831 400 GLU A OE1 
797  O OE2 . GLU A 104 ? 1.2763 1.1083 0.8883 -0.4269 -0.1288 -0.1901 400 GLU A OE2 
798  N N   . LEU A 105 ? 0.8922 1.0080 0.8356 -0.1911 -0.0996 -0.1370 401 LEU A N   
799  C CA  . LEU A 105 ? 0.8787 0.9936 0.8541 -0.1485 -0.0908 -0.1275 401 LEU A CA  
800  C C   . LEU A 105 ? 0.8205 1.0037 0.8477 -0.1368 -0.0930 -0.1162 401 LEU A C   
801  O O   . LEU A 105 ? 0.7547 0.9301 0.8023 -0.1218 -0.0871 -0.1087 401 LEU A O   
802  C CB  . LEU A 105 ? 0.8503 0.9585 0.8176 -0.1242 -0.0883 -0.1292 401 LEU A CB  
803  C CG  . LEU A 105 ? 0.8268 0.9273 0.8147 -0.0881 -0.0781 -0.1205 401 LEU A CG  
804  C CD1 . LEU A 105 ? 0.8425 0.8822 0.8055 -0.0763 -0.0688 -0.1241 401 LEU A CD1 
805  C CD2 . LEU A 105 ? 0.7914 0.9074 0.7756 -0.0725 -0.0771 -0.1199 401 LEU A CD2 
806  N N   . ILE A 106 ? 0.7973 1.0471 0.8410 -0.1420 -0.1022 -0.1154 402 ILE A N   
807  C CA  . ILE A 106 ? 0.7560 1.0675 0.8392 -0.1235 -0.1048 -0.1058 402 ILE A CA  
808  C C   . ILE A 106 ? 0.7373 1.0652 0.8342 -0.1404 -0.1026 -0.1039 402 ILE A C   
809  O O   . ILE A 106 ? 0.7003 1.0397 0.8215 -0.1192 -0.0988 -0.0958 402 ILE A O   
810  C CB  . ILE A 106 ? 0.7141 1.0967 0.8047 -0.1208 -0.1162 -0.1063 402 ILE A CB  
811  C CG1 . ILE A 106 ? 0.6877 1.0472 0.7611 -0.1021 -0.1175 -0.1064 402 ILE A CG1 
812  C CG2 . ILE A 106 ? 0.6570 1.1004 0.7787 -0.0943 -0.1194 -0.0974 402 ILE A CG2 
813  C CD1 . ILE A 106 ? 0.6716 1.0901 0.7402 -0.1031 -0.1304 -0.1088 402 ILE A CD1 
814  N N   . TYR A 107 ? 0.7337 1.0582 0.8090 -0.1817 -0.1049 -0.1111 403 TYR A N   
815  C CA  . TYR A 107 ? 0.7499 1.0852 0.8306 -0.2045 -0.1018 -0.1088 403 TYR A CA  
816  C C   . TYR A 107 ? 0.7995 1.0619 0.8735 -0.1891 -0.0920 -0.1044 403 TYR A C   
817  O O   . TYR A 107 ? 0.7169 0.9978 0.8169 -0.1738 -0.0880 -0.0969 403 TYR A O   
818  C CB  . TYR A 107 ? 0.7972 1.1292 0.8424 -0.2603 -0.1065 -0.1171 403 TYR A CB  
819  C CG  . TYR A 107 ? 0.8472 1.1731 0.8850 -0.2913 -0.1019 -0.1141 403 TYR A CG  
820  C CD1 . TYR A 107 ? 0.8944 1.1214 0.8954 -0.2959 -0.0949 -0.1138 403 TYR A CD1 
821  C CD2 . TYR A 107 ? 0.8497 1.2723 0.9143 -0.3142 -0.1044 -0.1111 403 TYR A CD2 
822  C CE1 . TYR A 107 ? 0.9404 1.1551 0.9283 -0.3247 -0.0908 -0.1098 403 TYR A CE1 
823  C CE2 . TYR A 107 ? 0.8867 1.3063 0.9421 -0.3458 -0.0989 -0.1075 403 TYR A CE2 
824  C CZ  . TYR A 107 ? 0.9360 1.2464 0.9512 -0.3521 -0.0923 -0.1065 403 TYR A CZ  
825  O OH  . TYR A 107 ? 0.9668 1.2672 0.9663 -0.3840 -0.0871 -0.1019 403 TYR A OH  
826  N N   . GLY A 108 ? 0.8195 1.0001 0.8552 -0.1903 -0.0886 -0.1096 404 GLY A N   
827  C CA  . GLY A 108 ? 0.8137 0.9323 0.8417 -0.1703 -0.0805 -0.1054 404 GLY A CA  
828  C C   . GLY A 108 ? 0.7664 0.9119 0.8363 -0.1325 -0.0770 -0.0960 404 GLY A C   
829  O O   . GLY A 108 ? 0.7340 0.8734 0.8168 -0.1248 -0.0733 -0.0896 404 GLY A O   
830  N N   . ALA A 109 ? 0.7516 0.9232 0.8372 -0.1115 -0.0789 -0.0946 405 ALA A N   
831  C CA  . ALA A 109 ? 0.7078 0.8930 0.8207 -0.0816 -0.0765 -0.0855 405 ALA A CA  
832  C C   . ALA A 109 ? 0.7111 0.9389 0.8489 -0.0783 -0.0786 -0.0795 405 ALA A C   
833  O O   . ALA A 109 ? 0.6491 0.8647 0.7978 -0.0655 -0.0751 -0.0732 405 ALA A O   
834  C CB  . ALA A 109 ? 0.7134 0.9133 0.8271 -0.0660 -0.0788 -0.0846 405 ALA A CB  
835  N N   . LYS A 110 ? 0.6923 0.9752 0.8375 -0.0883 -0.0844 -0.0818 406 LYS A N   
836  C CA  . LYS A 110 ? 0.6698 1.0014 0.8362 -0.0778 -0.0855 -0.0769 406 LYS A CA  
837  C C   . LYS A 110 ? 0.6625 0.9807 0.8303 -0.0930 -0.0799 -0.0755 406 LYS A C   
838  O O   . LYS A 110 ? 0.6324 0.9599 0.8130 -0.0758 -0.0775 -0.0700 406 LYS A O   
839  C CB  . LYS A 110 ? 0.6324 1.0414 0.8072 -0.0852 -0.0928 -0.0803 406 LYS A CB  
840  C CG  . LYS A 110 ? 0.6363 1.0659 0.8097 -0.0588 -0.0997 -0.0791 406 LYS A CG  
841  C CD  . LYS A 110 ? 0.6035 1.1232 0.7876 -0.0592 -0.1082 -0.0815 406 LYS A CD  
842  C CE  . LYS A 110 ? 0.6100 1.1420 0.7854 -0.0293 -0.1163 -0.0795 406 LYS A CE  
843  N NZ  . LYS A 110 ? 0.6005 1.2318 0.7876 -0.0196 -0.1258 -0.0808 406 LYS A NZ  
844  N N   . HIS A 111 ? 0.6507 0.9378 0.7974 -0.1250 -0.0781 -0.0802 407 HIS A N   
845  C CA  . HIS A 111 ? 0.6940 0.9615 0.8329 -0.1429 -0.0732 -0.0780 407 HIS A CA  
846  C C   . HIS A 111 ? 0.7058 0.9075 0.8367 -0.1251 -0.0684 -0.0737 407 HIS A C   
847  O O   . HIS A 111 ? 0.6737 0.8660 0.8050 -0.1278 -0.0649 -0.0693 407 HIS A O   
848  C CB  . HIS A 111 ? 0.7211 0.9748 0.8283 -0.1884 -0.0744 -0.0840 407 HIS A CB  
849  C CG  . HIS A 111 ? 0.7212 1.0623 0.8426 -0.2145 -0.0781 -0.0858 407 HIS A CG  
850  N ND1 . HIS A 111 ? 0.7068 1.1065 0.8404 -0.2128 -0.0853 -0.0899 407 HIS A ND1 
851  C CD2 . HIS A 111 ? 0.7181 1.1096 0.8456 -0.2408 -0.0755 -0.0833 407 HIS A CD2 
852  C CE1 . HIS A 111 ? 0.6942 1.1822 0.8424 -0.2363 -0.0878 -0.0903 407 HIS A CE1 
853  N NE2 . HIS A 111 ? 0.6919 1.1788 0.8373 -0.2550 -0.0811 -0.0864 407 HIS A NE2 
854  N N   . ALA A 112 ? 0.7158 0.8805 0.8403 -0.1063 -0.0681 -0.0745 408 ALA A N   
855  C CA  . ALA A 112 ? 0.7087 0.8370 0.8353 -0.0843 -0.0646 -0.0692 408 ALA A CA  
856  C C   . ALA A 112 ? 0.6948 0.8528 0.8479 -0.0663 -0.0651 -0.0621 408 ALA A C   
857  O O   . ALA A 112 ? 0.7144 0.8579 0.8698 -0.0616 -0.0632 -0.0573 408 ALA A O   
858  C CB  . ALA A 112 ? 0.6860 0.7902 0.8046 -0.0680 -0.0636 -0.0713 408 ALA A CB  
859  N N   . TRP A 113 ? 0.6565 0.8501 0.8225 -0.0551 -0.0685 -0.0615 409 TRP A N   
860  C CA  . TRP A 113 ? 0.6397 0.8506 0.8167 -0.0373 -0.0697 -0.0559 409 TRP A CA  
861  C C   . TRP A 113 ? 0.6392 0.8766 0.8215 -0.0450 -0.0678 -0.0559 409 TRP A C   
862  O O   . TRP A 113 ? 0.6106 0.8347 0.7933 -0.0377 -0.0659 -0.0518 409 TRP A O   
863  C CB  . TRP A 113 ? 0.6164 0.8526 0.7937 -0.0208 -0.0746 -0.0555 409 TRP A CB  
864  C CG  . TRP A 113 ? 0.6155 0.8516 0.7881 0.0026  -0.0768 -0.0505 409 TRP A CG  
865  C CD1 . TRP A 113 ? 0.6505 0.8631 0.8194 0.0082  -0.0750 -0.0466 409 TRP A CD1 
866  C CD2 . TRP A 113 ? 0.6412 0.8932 0.8026 0.0260  -0.0821 -0.0492 409 TRP A CD2 
867  N NE1 . TRP A 113 ? 0.6368 0.8432 0.7885 0.0325  -0.0786 -0.0438 409 TRP A NE1 
868  C CE2 . TRP A 113 ? 0.6468 0.8751 0.7919 0.0461  -0.0829 -0.0451 409 TRP A CE2 
869  C CE3 . TRP A 113 ? 0.6541 0.9343 0.8118 0.0339  -0.0871 -0.0512 409 TRP A CE3 
870  C CZ2 . TRP A 113 ? 0.6730 0.8960 0.7922 0.0767  -0.0883 -0.0429 409 TRP A CZ2 
871  C CZ3 . TRP A 113 ? 0.6796 0.9630 0.8170 0.0652  -0.0927 -0.0482 409 TRP A CZ3 
872  C CH2 . TRP A 113 ? 0.6833 0.9339 0.7987 0.0878  -0.0932 -0.0441 409 TRP A CH2 
873  N N   . ARG A 114 ? 0.6081 0.8876 0.7928 -0.0628 -0.0683 -0.0603 410 ARG A N   
874  C CA  . ARG A 114 ? 0.6235 0.9438 0.8141 -0.0741 -0.0652 -0.0599 410 ARG A CA  
875  C C   . ARG A 114 ? 0.6398 0.9173 0.8193 -0.0877 -0.0601 -0.0567 410 ARG A C   
876  O O   . ARG A 114 ? 0.5954 0.8917 0.7791 -0.0839 -0.0566 -0.0537 410 ARG A O   
877  C CB  . ARG A 114 ? 0.6241 0.9967 0.8153 -0.1035 -0.0667 -0.0650 410 ARG A CB  
878  C CG  . ARG A 114 ? 0.6540 1.0969 0.8559 -0.1159 -0.0633 -0.0644 410 ARG A CG  
879  C CD  . ARG A 114 ? 0.6490 1.1461 0.8484 -0.1566 -0.0657 -0.0692 410 ARG A CD  
880  N NE  . ARG A 114 ? 0.6293 1.2152 0.8437 -0.1682 -0.0616 -0.0679 410 ARG A NE  
881  C CZ  . ARG A 114 ? 0.6086 1.2752 0.8279 -0.2037 -0.0634 -0.0708 410 ARG A CZ  
882  N NH1 . ARG A 114 ? 0.6441 1.3066 0.8503 -0.2338 -0.0704 -0.0760 410 ARG A NH1 
883  N NH2 . ARG A 114 ? 0.6179 1.3770 0.8543 -0.2101 -0.0581 -0.0688 410 ARG A NH2 
884  N N   . ASN A 115 ? 0.6283 0.8469 0.7896 -0.0986 -0.0598 -0.0572 411 ASN A N   
885  C CA  . ASN A 115 ? 0.6924 0.8640 0.8353 -0.1080 -0.0565 -0.0537 411 ASN A CA  
886  C C   . ASN A 115 ? 0.6729 0.8138 0.8209 -0.0818 -0.0570 -0.0485 411 ASN A C   
887  O O   . ASN A 115 ? 0.6462 0.7494 0.7787 -0.0839 -0.0557 -0.0449 411 ASN A O   
888  C CB  . ASN A 115 ? 0.7102 0.8284 0.8194 -0.1288 -0.0566 -0.0573 411 ASN A CB  
889  C CG  . ASN A 115 ? 0.7576 0.8985 0.8515 -0.1669 -0.0568 -0.0620 411 ASN A CG  
890  O OD1 . ASN A 115 ? 0.7269 0.9243 0.8338 -0.1830 -0.0548 -0.0605 411 ASN A OD1 
891  N ND2 . ASN A 115 ? 0.7465 0.8473 0.8096 -0.1828 -0.0593 -0.0680 411 ASN A ND2 
892  N N   . ALA A 116 ? 0.6477 0.8030 0.8121 -0.0595 -0.0598 -0.0474 412 ALA A N   
893  C CA  . ALA A 116 ? 0.6245 0.7546 0.7908 -0.0425 -0.0617 -0.0427 412 ALA A CA  
894  C C   . ALA A 116 ? 0.6129 0.7456 0.7791 -0.0377 -0.0613 -0.0387 412 ALA A C   
895  O O   . ALA A 116 ? 0.5492 0.7006 0.7184 -0.0259 -0.0625 -0.0386 412 ALA A O   
896  C CB  . ALA A 116 ? 0.6480 0.7864 0.8215 -0.0291 -0.0649 -0.0424 412 ALA A CB  
897  N N   . SER A 117 ? 0.6362 0.7445 0.7920 -0.0438 -0.0600 -0.0357 413 SER A N   
898  C CA  . SER A 117 ? 0.5754 0.6893 0.7271 -0.0435 -0.0584 -0.0329 413 SER A CA  
899  C C   . SER A 117 ? 0.5954 0.7023 0.7477 -0.0271 -0.0628 -0.0302 413 SER A C   
900  O O   . SER A 117 ? 0.5950 0.7088 0.7406 -0.0214 -0.0617 -0.0299 413 SER A O   
901  C CB  . SER A 117 ? 0.6401 0.7242 0.7734 -0.0559 -0.0563 -0.0295 413 SER A CB  
902  O OG  . SER A 117 ? 0.6610 0.7142 0.7885 -0.0444 -0.0609 -0.0255 413 SER A OG  
903  N N   . ARG A 118 ? 0.6077 0.7021 0.7633 -0.0213 -0.0676 -0.0285 414 ARG A N   
904  C CA  . ARG A 118 ? 0.6018 0.6846 0.7498 -0.0149 -0.0730 -0.0257 414 ARG A CA  
905  C C   . ARG A 118 ? 0.6419 0.7251 0.7813 -0.0062 -0.0748 -0.0277 414 ARG A C   
906  O O   . ARG A 118 ? 0.5667 0.6266 0.6868 -0.0040 -0.0799 -0.0255 414 ARG A O   
907  C CB  . ARG A 118 ? 0.6342 0.7121 0.7874 -0.0182 -0.0774 -0.0217 414 ARG A CB  
908  C CG  . ARG A 118 ? 0.6703 0.7424 0.8228 -0.0182 -0.0780 -0.0186 414 ARG A CG  
909  C CD  . ARG A 118 ? 0.7243 0.8076 0.8840 -0.0153 -0.0825 -0.0146 414 ARG A CD  
910  N NE  . ARG A 118 ? 0.7088 0.7855 0.8617 -0.0094 -0.0852 -0.0108 414 ARG A NE  
911  C CZ  . ARG A 118 ? 0.7530 0.8486 0.9109 -0.0014 -0.0902 -0.0065 414 ARG A CZ  
912  N NH1 . ARG A 118 ? 0.7130 0.8412 0.8854 -0.0015 -0.0916 -0.0056 414 ARG A NH1 
913  N NH2 . ARG A 118 ? 0.7178 0.8047 0.8643 0.0075  -0.0940 -0.0025 414 ARG A NH2 
914  N N   . CYS A 119 ? 0.5901 0.6952 0.7363 -0.0015 -0.0717 -0.0316 415 CYS A N   
915  C CA  . CYS A 119 ? 0.6385 0.7419 0.7716 0.0123  -0.0744 -0.0328 415 CYS A CA  
916  C C   . CYS A 119 ? 0.6251 0.7422 0.7451 0.0317  -0.0728 -0.0358 415 CYS A C   
917  O O   . CYS A 119 ? 0.6183 0.7790 0.7540 0.0319  -0.0679 -0.0391 415 CYS A O   
918  C CB  . CYS A 119 ? 0.6272 0.7526 0.7735 0.0102  -0.0735 -0.0351 415 CYS A CB  
919  S SG  . CYS A 119 ? 0.5526 0.6773 0.6769 0.0332  -0.0778 -0.0359 415 CYS A SG  
920  N N   . VAL A 120 ? 0.6709 0.7517 0.7570 0.0481  -0.0770 -0.0351 416 VAL A N   
921  C CA  . VAL A 120 ? 0.6201 0.7123 0.6866 0.0760  -0.0750 -0.0388 416 VAL A CA  
922  C C   . VAL A 120 ? 0.6565 0.7735 0.7165 0.1013  -0.0762 -0.0413 416 VAL A C   
923  O O   . VAL A 120 ? 0.6329 0.7799 0.6823 0.1305  -0.0737 -0.0449 416 VAL A O   
924  C CB  . VAL A 120 ? 0.6601 0.6902 0.6795 0.0868  -0.0796 -0.0382 416 VAL A CB  
925  C CG1 . VAL A 120 ? 0.6920 0.6628 0.6682 0.0935  -0.0876 -0.0358 416 VAL A CG1 
926  C CG2 . VAL A 120 ? 0.6988 0.7439 0.6987 0.1167  -0.0749 -0.0431 416 VAL A CG2 
927  N N   . GLY A 121 ? 0.6842 0.7970 0.7501 0.0936  -0.0798 -0.0394 417 GLY A N   
928  C CA  . GLY A 121 ? 0.6465 0.7778 0.6997 0.1204  -0.0829 -0.0408 417 GLY A CA  
929  C C   . GLY A 121 ? 0.7035 0.9136 0.7967 0.1147  -0.0799 -0.0442 417 GLY A C   
930  O O   . GLY A 121 ? 0.6891 0.9226 0.7772 0.1327  -0.0839 -0.0450 417 GLY A O   
931  N N   . ARG A 122 ? 0.6675 0.9159 0.7946 0.0881  -0.0738 -0.0460 418 ARG A N   
932  C CA  . ARG A 122 ? 0.6422 0.9510 0.7998 0.0685  -0.0720 -0.0491 418 ARG A CA  
933  C C   . ARG A 122 ? 0.6427 1.0303 0.8075 0.0897  -0.0723 -0.0526 418 ARG A C   
934  O O   . ARG A 122 ? 0.6342 1.0769 0.8203 0.0711  -0.0729 -0.0553 418 ARG A O   
935  C CB  . ARG A 122 ? 0.6065 0.9228 0.7834 0.0334  -0.0659 -0.0495 418 ARG A CB  
936  C CG  . ARG A 122 ? 0.5836 0.8447 0.7603 0.0119  -0.0666 -0.0472 418 ARG A CG  
937  C CD  . ARG A 122 ? 0.6011 0.8567 0.7837 -0.0143 -0.0616 -0.0469 418 ARG A CD  
938  N NE  . ARG A 122 ? 0.5811 0.8214 0.7559 -0.0074 -0.0591 -0.0440 418 ARG A NE  
939  C CZ  . ARG A 122 ? 0.5980 0.8357 0.7716 -0.0258 -0.0544 -0.0426 418 ARG A CZ  
940  N NH1 . ARG A 122 ? 0.5291 0.7725 0.7036 -0.0535 -0.0519 -0.0437 418 ARG A NH1 
941  N NH2 . ARG A 122 ? 0.5908 0.8125 0.7547 -0.0176 -0.0528 -0.0398 418 ARG A NH2 
942  N N   . ILE A 123 ? 0.6530 1.0504 0.7970 0.1294  -0.0724 -0.0530 419 ILE A N   
943  C CA  . ILE A 123 ? 0.6230 1.1078 0.7735 0.1586  -0.0731 -0.0562 419 ILE A CA  
944  C C   . ILE A 123 ? 0.6618 1.1654 0.8143 0.1636  -0.0815 -0.0563 419 ILE A C   
945  O O   . ILE A 123 ? 0.6123 1.2075 0.7845 0.1692  -0.0834 -0.0590 419 ILE A O   
946  C CB  . ILE A 123 ? 0.6770 1.1494 0.7903 0.2132  -0.0731 -0.0569 419 ILE A CB  
947  C CG1 . ILE A 123 ? 0.6506 1.2376 0.7773 0.2462  -0.0715 -0.0606 419 ILE A CG1 
948  C CG2 . ILE A 123 ? 0.6664 1.0398 0.7270 0.2430  -0.0818 -0.0538 419 ILE A CG2 
949  C CD1 . ILE A 123 ? 0.7046 1.2762 0.7832 0.3157  -0.0742 -0.0620 419 ILE A CD1 
950  N N   . GLN A 124 ? 0.6966 1.1197 0.8289 0.1586  -0.0865 -0.0530 420 GLN A N   
951  C CA  . GLN A 124 ? 0.7110 1.1345 0.8362 0.1646  -0.0943 -0.0520 420 GLN A CA  
952  C C   . GLN A 124 ? 0.6826 1.1223 0.8373 0.1187  -0.0937 -0.0541 420 GLN A C   
953  O O   . GLN A 124 ? 0.6887 1.1185 0.8358 0.1184  -0.0994 -0.0535 420 GLN A O   
954  C CB  . GLN A 124 ? 0.8038 1.1279 0.8822 0.1823  -0.0992 -0.0465 420 GLN A CB  
955  C CG  . GLN A 124 ? 0.9085 1.2007 0.9373 0.2344  -0.1030 -0.0450 420 GLN A CG  
956  C CD  . GLN A 124 ? 0.9786 1.2955 0.9828 0.2755  -0.1119 -0.0440 420 GLN A CD  
957  O OE1 . GLN A 124 ? 0.9422 1.3055 0.9704 0.2615  -0.1155 -0.0445 420 GLN A OE1 
958  N NE2 . GLN A 124 ? 1.0711 1.3515 1.0203 0.3291  -0.1162 -0.0428 420 GLN A NE2 
959  N N   . TRP A 125 ? 0.6567 1.1152 0.8373 0.0814  -0.0870 -0.0567 421 TRP A N   
960  C CA  . TRP A 125 ? 0.6339 1.0707 0.8252 0.0409  -0.0859 -0.0587 421 TRP A CA  
961  C C   . TRP A 125 ? 0.6380 1.1240 0.8361 0.0303  -0.0919 -0.0627 421 TRP A C   
962  O O   . TRP A 125 ? 0.6294 1.0806 0.8227 0.0099  -0.0929 -0.0644 421 TRP A O   
963  C CB  . TRP A 125 ? 0.6245 1.0640 0.8291 0.0054  -0.0787 -0.0604 421 TRP A CB  
964  C CG  . TRP A 125 ? 0.6075 1.1328 0.8284 -0.0114 -0.0776 -0.0639 421 TRP A CG  
965  C CD1 . TRP A 125 ? 0.5928 1.1781 0.8224 0.0029  -0.0739 -0.0633 421 TRP A CD1 
966  C CD2 . TRP A 125 ? 0.6229 1.1904 0.8501 -0.0483 -0.0802 -0.0686 421 TRP A CD2 
967  N NE1 . TRP A 125 ? 0.5706 1.2435 0.8165 -0.0252 -0.0734 -0.0665 421 TRP A NE1 
968  C CE2 . TRP A 125 ? 0.5738 1.2339 0.8166 -0.0600 -0.0781 -0.0698 421 TRP A CE2 
969  C CE3 . TRP A 125 ? 0.6091 1.1451 0.8262 -0.0740 -0.0840 -0.0724 421 TRP A CE3 
970  C CZ2 . TRP A 125 ? 0.5438 1.2663 0.7920 -0.1029 -0.0807 -0.0740 421 TRP A CZ2 
971  C CZ3 . TRP A 125 ? 0.5907 1.1767 0.8080 -0.1134 -0.0870 -0.0776 421 TRP A CZ3 
972  C CH2 . TRP A 125 ? 0.6026 1.2817 0.8354 -0.1304 -0.0859 -0.0781 421 TRP A CH2 
973  N N   . SER A 126 ? 0.5961 1.1682 0.8043 0.0439  -0.0960 -0.0648 422 SER A N   
974  C CA  . SER A 126 ? 0.6283 1.2529 0.8419 0.0311  -0.1036 -0.0687 422 SER A CA  
975  C C   . SER A 126 ? 0.6450 1.2519 0.8381 0.0679  -0.1121 -0.0659 422 SER A C   
976  O O   . SER A 126 ? 0.6026 1.2417 0.7959 0.0584  -0.1193 -0.0688 422 SER A O   
977  C CB  . SER A 126 ? 0.6210 1.3641 0.8569 0.0235  -0.1055 -0.0721 422 SER A CB  
978  O OG  . SER A 126 ? 0.6412 1.4322 0.8780 0.0725  -0.1054 -0.0693 422 SER A OG  
979  N N   . LYS A 127 ? 0.6911 1.2433 0.8597 0.1076  -0.1123 -0.0600 423 LYS A N   
980  C CA  . LYS A 127 ? 0.6730 1.1866 0.8087 0.1399  -0.1201 -0.0555 423 LYS A CA  
981  C C   . LYS A 127 ? 0.7034 1.1236 0.8232 0.1188  -0.1163 -0.0521 423 LYS A C   
982  O O   . LYS A 127 ? 0.7305 1.0798 0.8247 0.1311  -0.1140 -0.0464 423 LYS A O   
983  C CB  . LYS A 127 ? 0.7748 1.2737 0.8784 0.1945  -0.1233 -0.0509 423 LYS A CB  
984  C CG  . LYS A 127 ? 0.7943 1.3607 0.8858 0.2386  -0.1335 -0.0507 423 LYS A CG  
985  C CD  . LYS A 127 ? 0.8662 1.3516 0.8948 0.2894  -0.1402 -0.0435 423 LYS A CD  
986  C CE  . LYS A 127 ? 0.9410 1.4927 0.9511 0.3437  -0.1514 -0.0429 423 LYS A CE  
987  N NZ  . LYS A 127 ? 1.0194 1.6297 1.0496 0.3245  -0.1593 -0.0444 423 LYS A NZ  
988  N N   . LEU A 128 ? 0.6996 1.1231 0.8323 0.0849  -0.1155 -0.0562 424 LEU A N   
989  C CA  . LEU A 128 ? 0.6891 1.0424 0.8116 0.0656  -0.1103 -0.0541 424 LEU A CA  
990  C C   . LEU A 128 ? 0.6722 1.0286 0.7837 0.0586  -0.1148 -0.0559 424 LEU A C   
991  O O   . LEU A 128 ? 0.6559 1.0613 0.7804 0.0412  -0.1182 -0.0631 424 LEU A O   
992  C CB  . LEU A 128 ? 0.6434 0.9832 0.7871 0.0326  -0.1016 -0.0583 424 LEU A CB  
993  C CG  . LEU A 128 ? 0.6537 0.9355 0.7900 0.0177  -0.0954 -0.0568 424 LEU A CG  
994  C CD1 . LEU A 128 ? 0.6610 0.8940 0.7794 0.0324  -0.0940 -0.0479 424 LEU A CD1 
995  C CD2 . LEU A 128 ? 0.6510 0.9210 0.8014 -0.0072 -0.0884 -0.0616 424 LEU A CD2 
996  N N   . GLN A 129 ? 0.6710 0.9749 0.7544 0.0688  -0.1150 -0.0493 425 GLN A N   
997  C CA  . GLN A 129 ? 0.6837 0.9841 0.7532 0.0611  -0.1175 -0.0505 425 GLN A CA  
998  C C   . GLN A 129 ? 0.6967 0.9680 0.7753 0.0320  -0.1075 -0.0543 425 GLN A C   
999  O O   . GLN A 129 ? 0.6993 0.9332 0.7794 0.0271  -0.1000 -0.0501 425 GLN A O   
1000 C CB  . GLN A 129 ? 0.7233 0.9813 0.7509 0.0845  -0.1221 -0.0404 425 GLN A CB  
1001 C CG  . GLN A 129 ? 0.7164 0.9689 0.7261 0.0764  -0.1237 -0.0406 425 GLN A CG  
1002 C CD  . GLN A 129 ? 0.7606 1.0771 0.7787 0.0792  -0.1335 -0.0481 425 GLN A CD  
1003 O OE1 . GLN A 129 ? 0.7971 1.1693 0.8315 0.0923  -0.1404 -0.0511 425 GLN A OE1 
1004 N NE2 . GLN A 129 ? 0.7699 1.0847 0.7755 0.0661  -0.1342 -0.0511 425 GLN A NE2 
1005 N N   . VAL A 130 ? 0.6918 0.9827 0.7739 0.0139  -0.1080 -0.0630 426 VAL A N   
1006 C CA  . VAL A 130 ? 0.6999 0.9621 0.7828 -0.0064 -0.0988 -0.0686 426 VAL A CA  
1007 C C   . VAL A 130 ? 0.7004 0.9491 0.7596 -0.0054 -0.0982 -0.0686 426 VAL A C   
1008 O O   . VAL A 130 ? 0.6771 0.9509 0.7247 -0.0051 -0.1065 -0.0723 426 VAL A O   
1009 C CB  . VAL A 130 ? 0.7016 0.9796 0.7936 -0.0301 -0.0989 -0.0798 426 VAL A CB  
1010 C CG1 . VAL A 130 ? 0.6772 0.9115 0.7575 -0.0420 -0.0895 -0.0858 426 VAL A CG1 
1011 C CG2 . VAL A 130 ? 0.6538 0.9517 0.7674 -0.0325 -0.0991 -0.0783 426 VAL A CG2 
1012 N N   . PHE A 131 ? 0.6817 0.8981 0.7331 -0.0050 -0.0888 -0.0639 427 PHE A N   
1013 C CA  . PHE A 131 ? 0.6782 0.8844 0.7062 -0.0054 -0.0853 -0.0634 427 PHE A CA  
1014 C C   . PHE A 131 ? 0.6991 0.8950 0.7266 -0.0151 -0.0759 -0.0739 427 PHE A C   
1015 O O   . PHE A 131 ? 0.6793 0.8632 0.7175 -0.0145 -0.0664 -0.0726 427 PHE A O   
1016 C CB  . PHE A 131 ? 0.6736 0.8579 0.6867 -0.0003 -0.0808 -0.0500 427 PHE A CB  
1017 C CG  . PHE A 131 ? 0.7051 0.8803 0.6984 0.0137  -0.0911 -0.0401 427 PHE A CG  
1018 C CD1 . PHE A 131 ? 0.7300 0.9170 0.7019 0.0247  -0.1010 -0.0405 427 PHE A CD1 
1019 C CD2 . PHE A 131 ? 0.6927 0.8440 0.6826 0.0189  -0.0919 -0.0311 427 PHE A CD2 
1020 C CE1 . PHE A 131 ? 0.7554 0.9294 0.7012 0.0461  -0.1113 -0.0312 427 PHE A CE1 
1021 C CE2 . PHE A 131 ? 0.7262 0.8560 0.6853 0.0378  -0.1016 -0.0228 427 PHE A CE2 
1022 C CZ  . PHE A 131 ? 0.7592 0.8997 0.6957 0.0541  -0.1112 -0.0225 427 PHE A CZ  
1023 N N   . ASP A 132 ? 0.7242 0.9237 0.7345 -0.0221 -0.0795 -0.0846 428 ASP A N   
1024 C CA  . ASP A 132 ? 0.6911 0.8673 0.6847 -0.0274 -0.0718 -0.0965 428 ASP A CA  
1025 C C   . ASP A 132 ? 0.7209 0.8914 0.6994 -0.0168 -0.0609 -0.0932 428 ASP A C   
1026 O O   . ASP A 132 ? 0.7667 0.9432 0.7240 -0.0163 -0.0629 -0.0929 428 ASP A O   
1027 C CB  . ASP A 132 ? 0.7465 0.9228 0.7179 -0.0433 -0.0810 -0.1093 428 ASP A CB  
1028 C CG  . ASP A 132 ? 0.7977 0.9308 0.7370 -0.0485 -0.0743 -0.1232 428 ASP A CG  
1029 O OD1 . ASP A 132 ? 0.8158 0.9267 0.7523 -0.0324 -0.0618 -0.1227 428 ASP A OD1 
1030 O OD2 . ASP A 132 ? 0.8289 0.9502 0.7410 -0.0681 -0.0822 -0.1348 428 ASP A OD2 
1031 N N   . ALA A 133 ? 0.7195 0.8856 0.7090 -0.0085 -0.0492 -0.0900 429 ALA A N   
1032 C CA  . ALA A 133 ? 0.7187 0.8941 0.6978 0.0008  -0.0363 -0.0873 429 ALA A CA  
1033 C C   . ALA A 133 ? 0.7264 0.8847 0.6861 0.0141  -0.0268 -0.1006 429 ALA A C   
1034 O O   . ALA A 133 ? 0.7265 0.9032 0.6861 0.0285  -0.0137 -0.0987 429 ALA A O   
1035 C CB  . ALA A 133 ? 0.7391 0.9353 0.7425 0.0006  -0.0301 -0.0731 429 ALA A CB  
1036 N N   . ARG A 134 ? 0.7589 0.8819 0.6970 0.0099  -0.0332 -0.1140 430 ARG A N   
1037 C CA  . ARG A 134 ? 0.8141 0.9012 0.7192 0.0263  -0.0250 -0.1273 430 ARG A CA  
1038 C C   . ARG A 134 ? 0.8492 0.9321 0.7165 0.0390  -0.0169 -0.1356 430 ARG A C   
1039 O O   . ARG A 134 ? 0.8858 0.9359 0.7180 0.0605  -0.0087 -0.1472 430 ARG A O   
1040 C CB  . ARG A 134 ? 0.8354 0.8721 0.7156 0.0114  -0.0347 -0.1387 430 ARG A CB  
1041 C CG  . ARG A 134 ? 0.8540 0.8855 0.7611 0.0071  -0.0376 -0.1329 430 ARG A CG  
1042 C CD  . ARG A 134 ? 0.8896 0.8747 0.7682 -0.0169 -0.0474 -0.1425 430 ARG A CD  
1043 N NE  . ARG A 134 ? 0.8880 0.8964 0.7684 -0.0456 -0.0596 -0.1442 430 ARG A NE  
1044 C CZ  . ARG A 134 ? 0.9486 0.9280 0.7952 -0.0748 -0.0690 -0.1545 430 ARG A CZ  
1045 N NH1 . ARG A 134 ? 1.0067 0.9177 0.8081 -0.0820 -0.0678 -0.1636 430 ARG A NH1 
1046 N NH2 . ARG A 134 ? 0.8715 0.8899 0.7238 -0.0980 -0.0806 -0.1555 430 ARG A NH2 
1047 N N   . ASP A 135 ? 0.8168 0.9276 0.6840 0.0298  -0.0187 -0.1301 431 ASP A N   
1048 C CA  . ASP A 135 ? 0.8443 0.9582 0.6768 0.0426  -0.0089 -0.1362 431 ASP A CA  
1049 C C   . ASP A 135 ? 0.8281 0.9933 0.6806 0.0568  0.0071  -0.1246 431 ASP A C   
1050 O O   . ASP A 135 ? 0.8486 1.0289 0.6762 0.0680  0.0180  -0.1277 431 ASP A O   
1051 C CB  . ASP A 135 ? 0.8547 0.9700 0.6676 0.0244  -0.0196 -0.1368 431 ASP A CB  
1052 C CG  . ASP A 135 ? 0.8484 0.9988 0.6939 0.0103  -0.0277 -0.1187 431 ASP A CG  
1053 O OD1 . ASP A 135 ? 0.7953 0.9643 0.6763 0.0102  -0.0252 -0.1063 431 ASP A OD1 
1054 O OD2 . ASP A 135 ? 0.8118 0.9664 0.6410 0.0006  -0.0377 -0.1171 431 ASP A OD2 
1055 N N   . CYS A 136 ? 0.7928 0.9880 0.6871 0.0537  0.0087  -0.1114 432 CYS A N   
1056 C CA  . CYS A 136 ? 0.7938 1.0462 0.7086 0.0565  0.0220  -0.0985 432 CYS A CA  
1057 C C   . CYS A 136 ? 0.8103 1.0864 0.7152 0.0891  0.0386  -0.1070 432 CYS A C   
1058 O O   . CYS A 136 ? 0.8706 1.1125 0.7628 0.1118  0.0382  -0.1190 432 CYS A O   
1059 C CB  . CYS A 136 ? 0.7238 0.9945 0.6800 0.0410  0.0167  -0.0838 432 CYS A CB  
1060 S SG  . CYS A 136 ? 0.6925 1.0319 0.6689 0.0269  0.0290  -0.0651 432 CYS A SG  
1061 N N   . THR A 137 ? 0.8360 1.1707 0.7410 0.0932  0.0535  -0.1005 433 THR A N   
1062 C CA  . THR A 137 ? 0.7995 1.1730 0.6944 0.1307  0.0708  -0.1085 433 THR A CA  
1063 C C   . THR A 137 ? 0.7779 1.2476 0.7086 0.1280  0.0844  -0.0939 433 THR A C   
1064 O O   . THR A 137 ? 0.7735 1.2904 0.7066 0.1642  0.0974  -0.0993 433 THR A O   
1065 C CB  . THR A 137 ? 0.8966 1.2569 0.7421 0.1482  0.0799  -0.1213 433 THR A CB  
1066 O OG1 . THR A 137 ? 0.8892 1.2868 0.7349 0.1201  0.0839  -0.1090 433 THR A OG1 
1067 C CG2 . THR A 137 ? 0.9279 1.1951 0.7300 0.1488  0.0663  -0.1379 433 THR A CG2 
1068 N N   . THR A 138 ? 0.8133 1.3133 0.7664 0.0870  0.0815  -0.0758 434 THR A N   
1069 C CA  . THR A 138 ? 0.7863 1.3800 0.7638 0.0719  0.0945  -0.0610 434 THR A CA  
1070 C C   . THR A 138 ? 0.7258 1.3223 0.7343 0.0341  0.0834  -0.0448 434 THR A C   
1071 O O   . THR A 138 ? 0.7631 1.2894 0.7704 0.0200  0.0668  -0.0438 434 THR A O   
1072 C CB  . THR A 138 ? 0.7782 1.4036 0.7303 0.0514  0.1056  -0.0539 434 THR A CB  
1073 O OG1 . THR A 138 ? 0.8316 1.3799 0.7562 0.0286  0.0918  -0.0520 434 THR A OG1 
1074 C CG2 . THR A 138 ? 0.8107 1.4688 0.7376 0.0927  0.1229  -0.0684 434 THR A CG2 
1075 N N   . ALA A 139 ? 0.7405 1.4234 0.7744 0.0180  0.0927  -0.0324 435 ALA A N   
1076 C CA  . ALA A 139 ? 0.7045 1.3875 0.7586 -0.0229 0.0822  -0.0169 435 ALA A CA  
1077 C C   . ALA A 139 ? 0.7205 1.3512 0.7434 -0.0673 0.0747  -0.0040 435 ALA A C   
1078 O O   . ALA A 139 ? 0.7347 1.3064 0.7546 -0.0891 0.0596  0.0027  435 ALA A O   
1079 C CB  . ALA A 139 ? 0.7332 1.5281 0.8173 -0.0357 0.0932  -0.0067 435 ALA A CB  
1080 N N   . HIS A 140 ? 0.7997 1.4471 0.7932 -0.0774 0.0852  -0.0007 436 HIS A N   
1081 C CA  . HIS A 140 ? 0.8048 1.3882 0.7566 -0.1108 0.0771  0.0103  436 HIS A CA  
1082 C C   . HIS A 140 ? 0.7762 1.2657 0.7136 -0.0909 0.0600  0.0005  436 HIS A C   
1083 O O   . HIS A 140 ? 0.8111 1.2372 0.7250 -0.1113 0.0462  0.0097  436 HIS A O   
1084 C CB  . HIS A 140 ? 0.8657 1.4845 0.7859 -0.1192 0.0922  0.0139  436 HIS A CB  
1085 C CG  . HIS A 140 ? 0.8896 1.5808 0.8040 -0.1650 0.1048  0.0322  436 HIS A CG  
1086 N ND1 . HIS A 140 ? 0.8652 1.6666 0.8181 -0.1657 0.1186  0.0337  436 HIS A ND1 
1087 C CD2 . HIS A 140 ? 0.9096 1.5815 0.7790 -0.2136 0.1059  0.0502  436 HIS A CD2 
1088 C CE1 . HIS A 140 ? 0.8689 1.7239 0.8048 -0.2181 0.1278  0.0518  436 HIS A CE1 
1089 N NE2 . HIS A 140 ? 0.8987 1.6693 0.7803 -0.2496 0.1205  0.0624  436 HIS A NE2 
1090 N N   . GLY A 141 ? 0.7720 1.2517 0.7169 -0.0511 0.0606  -0.0181 437 GLY A N   
1091 C CA  . GLY A 141 ? 0.7763 1.1813 0.7124 -0.0377 0.0440  -0.0276 437 GLY A CA  
1092 C C   . GLY A 141 ? 0.7764 1.1506 0.7358 -0.0455 0.0301  -0.0234 437 GLY A C   
1093 O O   . GLY A 141 ? 0.7855 1.1067 0.7306 -0.0543 0.0156  -0.0193 437 GLY A O   
1094 N N   . MET A 142 ? 0.7662 1.1773 0.7596 -0.0398 0.0344  -0.0239 438 MET A N   
1095 C CA  . MET A 142 ? 0.7151 1.1003 0.7297 -0.0474 0.0223  -0.0200 438 MET A CA  
1096 C C   . MET A 142 ? 0.7105 1.0717 0.7063 -0.0834 0.0152  -0.0027 438 MET A C   
1097 O O   . MET A 142 ? 0.7304 1.0354 0.7169 -0.0860 0.0011  -0.0006 438 MET A O   
1098 C CB  . MET A 142 ? 0.7043 1.1414 0.7541 -0.0357 0.0290  -0.0220 438 MET A CB  
1099 C CG  . MET A 142 ? 0.6872 1.1302 0.7433 0.0051  0.0347  -0.0389 438 MET A CG  
1100 S SD  . MET A 142 ? 0.7198 1.2342 0.8108 0.0254  0.0429  -0.0387 438 MET A SD  
1101 C CE  . MET A 142 ? 0.6535 1.1288 0.7657 0.0067  0.0265  -0.0321 438 MET A CE  
1102 N N   . PHE A 143 ? 0.6880 1.0910 0.6730 -0.1117 0.0249  0.0100  439 PHE A N   
1103 C CA  . PHE A 143 ? 0.7312 1.0958 0.6800 -0.1510 0.0183  0.0272  439 PHE A CA  
1104 C C   . PHE A 143 ? 0.8058 1.0894 0.7135 -0.1444 0.0056  0.0282  439 PHE A C   
1105 O O   . PHE A 143 ? 0.7645 0.9874 0.6532 -0.1493 -0.0080 0.0335  439 PHE A O   
1106 C CB  . PHE A 143 ? 0.7996 1.2185 0.7298 -0.1857 0.0323  0.0398  439 PHE A CB  
1107 C CG  . PHE A 143 ? 0.8819 1.2477 0.7592 -0.2321 0.0256  0.0584  439 PHE A CG  
1108 C CD1 . PHE A 143 ? 0.8895 1.2166 0.7604 -0.2532 0.0143  0.0652  439 PHE A CD1 
1109 C CD2 . PHE A 143 ? 0.8834 1.2274 0.7084 -0.2546 0.0300  0.0690  439 PHE A CD2 
1110 C CE1 . PHE A 143 ? 0.9612 1.2224 0.7691 -0.2958 0.0074  0.0817  439 PHE A CE1 
1111 C CE2 . PHE A 143 ? 0.9693 1.2472 0.7315 -0.2981 0.0229  0.0868  439 PHE A CE2 
1112 C CZ  . PHE A 143 ? 1.0027 1.2349 0.7537 -0.3184 0.0113  0.0927  439 PHE A CZ  
1113 N N   . ASN A 144 ? 0.7507 1.0347 0.6416 -0.1297 0.0095  0.0225  440 ASN A N   
1114 C CA  . ASN A 144 ? 0.7728 0.9918 0.6260 -0.1194 -0.0038 0.0231  440 ASN A CA  
1115 C C   . ASN A 144 ? 0.7611 0.9474 0.6353 -0.0946 -0.0185 0.0136  440 ASN A C   
1116 O O   . ASN A 144 ? 0.8586 0.9910 0.7055 -0.0929 -0.0320 0.0202  440 ASN A O   
1117 C CB  . ASN A 144 ? 0.8087 1.0424 0.6471 -0.1048 0.0020  0.0153  440 ASN A CB  
1118 C CG  . ASN A 144 ? 0.8114 0.9873 0.5999 -0.1017 -0.0108 0.0214  440 ASN A CG  
1119 O OD1 . ASN A 144 ? 0.8108 0.9481 0.5523 -0.1238 -0.0134 0.0380  440 ASN A OD1 
1120 N ND2 . ASN A 144 ? 0.7990 0.9660 0.5926 -0.0751 -0.0201 0.0084  440 ASN A ND2 
1121 N N   . TYR A 145 ? 0.6937 0.9102 0.6104 -0.0739 -0.0159 -0.0017 441 TYR A N   
1122 C CA  . TYR A 145 ? 0.7887 0.9805 0.7238 -0.0561 -0.0288 -0.0100 441 TYR A CA  
1123 C C   . TYR A 145 ? 0.7511 0.9181 0.6895 -0.0657 -0.0358 -0.0009 441 TYR A C   
1124 O O   . TYR A 145 ? 0.7969 0.9277 0.7246 -0.0552 -0.0486 -0.0001 441 TYR A O   
1125 C CB  . TYR A 145 ? 0.7576 0.9763 0.7282 -0.0390 -0.0240 -0.0262 441 TYR A CB  
1126 C CG  . TYR A 145 ? 0.7119 0.9255 0.6709 -0.0248 -0.0267 -0.0397 441 TYR A CG  
1127 C CD1 . TYR A 145 ? 0.7326 0.9247 0.6864 -0.0189 -0.0412 -0.0442 441 TYR A CD1 
1128 C CD2 . TYR A 145 ? 0.7428 0.9766 0.6939 -0.0172 -0.0150 -0.0486 441 TYR A CD2 
1129 C CE1 . TYR A 145 ? 0.7051 0.8963 0.6462 -0.0125 -0.0454 -0.0566 441 TYR A CE1 
1130 C CE2 . TYR A 145 ? 0.6997 0.9204 0.6316 -0.0075 -0.0186 -0.0621 441 TYR A CE2 
1131 C CZ  . TYR A 145 ? 0.7173 0.9168 0.6447 -0.0087 -0.0345 -0.0659 441 TYR A CZ  
1132 O OH  . TYR A 145 ? 0.7866 0.9769 0.6926 -0.0057 -0.0395 -0.0793 441 TYR A OH  
1133 N N   . ILE A 146 ? 0.7285 0.9187 0.6792 -0.0849 -0.0278 0.0059  442 ILE A N   
1134 C CA  . ILE A 146 ? 0.7288 0.8945 0.6809 -0.0961 -0.0346 0.0129  442 ILE A CA  
1135 C C   . ILE A 146 ? 0.7980 0.8990 0.6927 -0.1102 -0.0438 0.0263  442 ILE A C   
1136 O O   . ILE A 146 ? 0.8192 0.8739 0.6995 -0.1021 -0.0549 0.0280  442 ILE A O   
1137 C CB  . ILE A 146 ? 0.7269 0.9428 0.7046 -0.1160 -0.0247 0.0167  442 ILE A CB  
1138 C CG1 . ILE A 146 ? 0.7105 0.9711 0.7373 -0.0916 -0.0195 0.0033  442 ILE A CG1 
1139 C CG2 . ILE A 146 ? 0.7332 0.9180 0.6956 -0.1397 -0.0320 0.0270  442 ILE A CG2 
1140 C CD1 . ILE A 146 ? 0.6322 0.9586 0.6852 -0.1019 -0.0092 0.0063  442 ILE A CD1 
1141 N N   . CYS A 147 ? 0.8043 0.8962 0.6584 -0.1291 -0.0392 0.0361  443 CYS A N   
1142 C CA  . CYS A 147 ? 0.8405 0.8557 0.6242 -0.1400 -0.0486 0.0496  443 CYS A CA  
1143 C C   . CYS A 147 ? 0.8733 0.8458 0.6392 -0.1018 -0.0625 0.0445  443 CYS A C   
1144 O O   . CYS A 147 ? 0.9168 0.8219 0.6371 -0.0939 -0.0740 0.0512  443 CYS A O   
1145 C CB  . CYS A 147 ? 0.9149 0.9308 0.6564 -0.1656 -0.0403 0.0604  443 CYS A CB  
1146 S SG  . CYS A 147 ? 1.0049 1.0602 0.7390 -0.2226 -0.0264 0.0736  443 CYS A SG  
1147 N N   . ASN A 148 ? 0.8366 0.8472 0.6303 -0.0780 -0.0620 0.0331  444 ASN A N   
1148 C CA  . ASN A 148 ? 0.8589 0.8511 0.6446 -0.0434 -0.0758 0.0274  444 ASN A CA  
1149 C C   . ASN A 148 ? 0.8502 0.8413 0.6650 -0.0268 -0.0827 0.0212  444 ASN A C   
1150 O O   . ASN A 148 ? 0.8445 0.8044 0.6350 -0.0012 -0.0950 0.0225  444 ASN A O   
1151 C CB  . ASN A 148 ? 0.8727 0.9143 0.6873 -0.0294 -0.0741 0.0144  444 ASN A CB  
1152 C CG  . ASN A 148 ? 0.8847 0.9220 0.6614 -0.0379 -0.0699 0.0200  444 ASN A CG  
1153 O OD1 . ASN A 148 ? 0.9337 0.9278 0.6584 -0.0541 -0.0691 0.0350  444 ASN A OD1 
1154 N ND2 . ASN A 148 ? 0.8365 0.9122 0.6314 -0.0291 -0.0677 0.0081  444 ASN A ND2 
1155 N N   . HIS A 149 ? 0.8070 0.8361 0.6724 -0.0372 -0.0747 0.0142  445 HIS A N   
1156 C CA  . HIS A 149 ? 0.7839 0.8121 0.6753 -0.0253 -0.0797 0.0091  445 HIS A CA  
1157 C C   . HIS A 149 ? 0.8176 0.7821 0.6625 -0.0289 -0.0864 0.0204  445 HIS A C   
1158 O O   . HIS A 149 ? 0.8592 0.7948 0.6845 -0.0026 -0.0967 0.0198  445 HIS A O   
1159 C CB  . HIS A 149 ? 0.7487 0.8221 0.6932 -0.0370 -0.0698 0.0015  445 HIS A CB  
1160 C CG  . HIS A 149 ? 0.7398 0.8133 0.7104 -0.0284 -0.0737 -0.0030 445 HIS A CG  
1161 N ND1 . HIS A 149 ? 0.7005 0.8104 0.7156 -0.0222 -0.0705 -0.0144 445 HIS A ND1 
1162 C CD2 . HIS A 149 ? 0.6896 0.7256 0.6411 -0.0257 -0.0802 0.0023  445 HIS A CD2 
1163 C CE1 . HIS A 149 ? 0.6702 0.7713 0.6968 -0.0170 -0.0745 -0.0151 445 HIS A CE1 
1164 N NE2 . HIS A 149 ? 0.7361 0.7947 0.7262 -0.0175 -0.0802 -0.0057 445 HIS A NE2 
1165 N N   . VAL A 150 ? 0.8392 0.7817 0.6603 -0.0619 -0.0808 0.0306  446 VAL A N   
1166 C CA  . VAL A 150 ? 0.9131 0.7805 0.6753 -0.0735 -0.0877 0.0414  446 VAL A CA  
1167 C C   . VAL A 150 ? 1.0071 0.8044 0.7018 -0.0449 -0.0997 0.0468  446 VAL A C   
1168 O O   . VAL A 150 ? 1.0897 0.8435 0.7587 -0.0183 -0.1091 0.0457  446 VAL A O   
1169 C CB  . VAL A 150 ? 0.9388 0.7955 0.6726 -0.1222 -0.0804 0.0534  446 VAL A CB  
1170 C CG1 . VAL A 150 ? 1.0580 0.8160 0.7088 -0.1398 -0.0895 0.0655  446 VAL A CG1 
1171 C CG2 . VAL A 150 ? 0.8565 0.7879 0.6544 -0.1435 -0.0703 0.0487  446 VAL A CG2 
1172 N N   . LYS A 151 ? 1.0067 0.7940 0.6690 -0.0458 -0.0996 0.0525  447 LYS A N   
1173 C CA  . LYS A 151 ? 1.1056 0.8208 0.6932 -0.0163 -0.1121 0.0596  447 LYS A CA  
1174 C C   . LYS A 151 ? 1.1022 0.8427 0.7136 0.0364  -0.1219 0.0491  447 LYS A C   
1175 O O   . LYS A 151 ? 1.1666 0.8461 0.7232 0.0694  -0.1330 0.0526  447 LYS A O   
1176 C CB  . LYS A 151 ? 1.1150 0.8285 0.6719 -0.0244 -0.1100 0.0664  447 LYS A CB  
1177 C CG  . LYS A 151 ? 1.2059 0.8284 0.6681 0.0014  -0.1231 0.0776  447 LYS A CG  
1178 C CD  . LYS A 151 ? 1.2610 0.8801 0.6896 -0.0112 -0.1204 0.0856  447 LYS A CD  
1179 C CE  . LYS A 151 ? 1.3213 0.8219 0.6321 -0.0066 -0.1306 0.1026  447 LYS A CE  
1180 N NZ  . LYS A 151 ? 1.2984 0.7928 0.5714 -0.0268 -0.1262 0.1124  447 LYS A NZ  
1181 N N   . TYR A 152 ? 1.0038 0.8342 0.6912 0.0451  -0.1181 0.0362  448 TYR A N   
1182 C CA  . TYR A 152 ? 0.9922 0.8628 0.7073 0.0863  -0.1267 0.0264  448 TYR A CA  
1183 C C   . TYR A 152 ? 0.9866 0.8433 0.7106 0.0976  -0.1282 0.0234  448 TYR A C   
1184 O O   . TYR A 152 ? 0.9981 0.8296 0.6886 0.1370  -0.1378 0.0239  448 TYR A O   
1185 C CB  . TYR A 152 ? 0.9330 0.8945 0.7207 0.0809  -0.1220 0.0133  448 TYR A CB  
1186 C CG  . TYR A 152 ? 0.9068 0.9216 0.7277 0.1119  -0.1297 0.0035  448 TYR A CG  
1187 C CD1 . TYR A 152 ? 0.9323 0.9726 0.7366 0.1441  -0.1413 0.0025  448 TYR A CD1 
1188 C CD2 . TYR A 152 ? 0.8721 0.9174 0.7391 0.1081  -0.1256 -0.0041 448 TYR A CD2 
1189 C CE1 . TYR A 152 ? 0.8808 0.9860 0.7172 0.1696  -0.1481 -0.0058 448 TYR A CE1 
1190 C CE2 . TYR A 152 ? 0.8467 0.9484 0.7425 0.1316  -0.1314 -0.0121 448 TYR A CE2 
1191 C CZ  . TYR A 152 ? 0.8915 1.0279 0.7736 0.1612  -0.1424 -0.0130 448 TYR A CZ  
1192 O OH  . TYR A 152 ? 0.9223 1.1313 0.8359 0.1815  -0.1479 -0.0205 448 TYR A OH  
1193 N N   . ALA A 153 ? 0.9366 0.8140 0.7048 0.0674  -0.1186 0.0196  449 ALA A N   
1194 C CA  . ALA A 153 ? 0.9496 0.8225 0.7320 0.0770  -0.1195 0.0155  449 ALA A CA  
1195 C C   . ALA A 153 ? 1.0463 0.8234 0.7492 0.0883  -0.1267 0.0246  449 ALA A C   
1196 O O   . ALA A 153 ? 1.0767 0.8395 0.7710 0.1144  -0.1308 0.0208  449 ALA A O   
1197 C CB  . ALA A 153 ? 0.8725 0.7787 0.7083 0.0419  -0.1090 0.0116  449 ALA A CB  
1198 N N   . THR A 154 ? 1.0214 0.7276 0.6592 0.0670  -0.1279 0.0364  450 THR A N   
1199 C CA  . THR A 154 ? 1.1584 0.7539 0.7043 0.0705  -0.1353 0.0454  450 THR A CA  
1200 C C   . THR A 154 ? 1.2557 0.8016 0.7364 0.1277  -0.1475 0.0474  450 THR A C   
1201 O O   . THR A 154 ? 1.2528 0.7445 0.6876 0.1614  -0.1542 0.0460  450 THR A O   
1202 C CB  . THR A 154 ? 1.1955 0.7313 0.6887 0.0183  -0.1320 0.0584  450 THR A CB  
1203 O OG1 . THR A 154 ? 1.1221 0.7243 0.6835 -0.0275 -0.1208 0.0557  450 THR A OG1 
1204 C CG2 . THR A 154 ? 1.2736 0.6804 0.6596 0.0133  -0.1406 0.0676  450 THR A CG2 
1205 N N   . ASN A 155 ? 1.2281 0.7934 0.7009 0.1432  -0.1508 0.0504  451 ASN A N   
1206 C CA  . ASN A 155 ? 1.2420 0.7913 0.6698 0.2055  -0.1631 0.0508  451 ASN A CA  
1207 C C   . ASN A 155 ? 1.4091 0.8229 0.7196 0.2319  -0.1727 0.0595  451 ASN A C   
1208 O O   . ASN A 155 ? 1.4454 0.8447 0.7277 0.2893  -0.1805 0.0551  451 ASN A O   
1209 C CB  . ASN A 155 ? 1.1639 0.8211 0.6693 0.2437  -0.1640 0.0369  451 ASN A CB  
1210 C CG  . ASN A 155 ? 1.2494 0.9250 0.7239 0.3086  -0.1766 0.0365  451 ASN A CG  
1211 O OD1 . ASN A 155 ? 1.2875 0.9165 0.7004 0.3239  -0.1844 0.0455  451 ASN A OD1 
1212 N ND2 . ASN A 155 ? 1.1813 0.9312 0.6974 0.3480  -0.1787 0.0266  451 ASN A ND2 
1213 N N   . LYS A 156 ? 1.4729 0.7857 0.7101 0.1872  -0.1716 0.0718  452 LYS A N   
1214 C CA  . LYS A 156 ? 1.5695 0.7274 0.6724 0.2009  -0.1815 0.0822  452 LYS A CA  
1215 C C   . LYS A 156 ? 1.6644 0.7819 0.7487 0.2210  -0.1836 0.0748  452 LYS A C   
1216 O O   . LYS A 156 ? 1.7744 0.7808 0.7537 0.2660  -0.1940 0.0776  452 LYS A O   
1217 C CB  . LYS A 156 ? 1.6814 0.7865 0.7043 0.2647  -0.1946 0.0881  452 LYS A CB  
1218 C CG  . LYS A 156 ? 1.7562 0.9079 0.7967 0.2532  -0.1941 0.0946  452 LYS A CG  
1219 C CD  . LYS A 156 ? 1.9395 0.9694 0.8493 0.2850  -0.2067 0.1086  452 LYS A CD  
1220 C CE  . LYS A 156 ? 2.0786 1.0940 0.9621 0.3620  -0.2108 0.0935  452 LYS A CE  
1221 N NZ  . LYS A 156 ? 2.0214 1.1803 1.0039 0.4124  -0.2131 0.0819  452 LYS A NZ  
1222 N N   . GLY A 157 ? 1.5668 0.7708 0.7473 0.1919  -0.1738 0.0650  453 GLY A N   
1223 C CA  . GLY A 157 ? 1.6088 0.7889 0.7836 0.2050  -0.1742 0.0572  453 GLY A CA  
1224 C C   . GLY A 157 ? 1.5623 0.8395 0.8049 0.2649  -0.1738 0.0439  453 GLY A C   
1225 O O   . GLY A 157 ? 1.5103 0.8048 0.7804 0.2672  -0.1702 0.0358  453 GLY A O   
1226 N N   . ASN A 158 ? 1.5302 0.8768 0.7999 0.3104  -0.1774 0.0418  454 ASN A N   
1227 C CA  . ASN A 158 ? 1.4767 0.9416 0.8236 0.3558  -0.1759 0.0295  454 ASN A CA  
1228 C C   . ASN A 158 ? 1.3391 0.9296 0.8098 0.3074  -0.1647 0.0228  454 ASN A C   
1229 O O   . ASN A 158 ? 1.2667 0.9491 0.7954 0.3106  -0.1643 0.0198  454 ASN A O   
1230 C CB  . ASN A 158 ? 1.4687 0.9634 0.7899 0.4235  -0.1860 0.0301  454 ASN A CB  
1231 C CG  . ASN A 158 ? 1.4468 1.0778 0.8470 0.4661  -0.1844 0.0179  454 ASN A CG  
1232 O OD1 . ASN A 158 ? 1.4116 1.0913 0.8676 0.4523  -0.1760 0.0096  454 ASN A OD1 
1233 N ND2 . ASN A 158 ? 1.4641 1.1623 0.8683 0.5156  -0.1927 0.0174  454 ASN A ND2 
1234 N N   . LEU A 159 ? 1.2932 0.8807 0.7969 0.2631  -0.1564 0.0201  455 LEU A N   
1235 C CA  . LEU A 159 ? 1.1592 0.8303 0.7562 0.2108  -0.1460 0.0165  455 LEU A CA  
1236 C C   . LEU A 159 ? 1.0499 0.8467 0.7348 0.2275  -0.1428 0.0061  455 LEU A C   
1237 O O   . LEU A 159 ? 1.0565 0.8935 0.7483 0.2714  -0.1459 0.0002  455 LEU A O   
1238 C CB  . LEU A 159 ? 1.1849 0.8349 0.7972 0.1719  -0.1397 0.0152  455 LEU A CB  
1239 C CG  . LEU A 159 ? 1.2106 0.7849 0.7792 0.1184  -0.1385 0.0248  455 LEU A CG  
1240 C CD1 . LEU A 159 ? 1.3110 0.7831 0.7793 0.1232  -0.1465 0.0360  455 LEU A CD1 
1241 C CD2 . LEU A 159 ? 1.1986 0.7260 0.7464 0.1007  -0.1385 0.0234  455 LEU A CD2 
1242 N N   . ARG A 160 ? 0.9649 0.8239 0.7127 0.1904  -0.1363 0.0039  456 ARG A N   
1243 C CA  . ARG A 160 ? 0.9132 0.8792 0.7328 0.1947  -0.1342 -0.0053 456 ARG A CA  
1244 C C   . ARG A 160 ? 0.7921 0.7959 0.6743 0.1485  -0.1238 -0.0099 456 ARG A C   
1245 O O   . ARG A 160 ? 0.8538 0.8235 0.7300 0.1152  -0.1190 -0.0050 456 ARG A O   
1246 C CB  . ARG A 160 ? 0.8879 0.8834 0.7015 0.2059  -0.1402 -0.0039 456 ARG A CB  
1247 C CG  . ARG A 160 ? 0.9611 0.9349 0.7156 0.2613  -0.1522 0.0001  456 ARG A CG  
1248 C CD  . ARG A 160 ? 0.9441 0.9588 0.6967 0.2732  -0.1597 0.0012  456 ARG A CD  
1249 N NE  . ARG A 160 ? 0.9522 0.9022 0.6674 0.2449  -0.1583 0.0100  456 ARG A NE  
1250 C CZ  . ARG A 160 ? 1.0303 0.9769 0.7137 0.2581  -0.1658 0.0148  456 ARG A CZ  
1251 N NH1 . ARG A 160 ? 0.9646 0.9715 0.6498 0.3006  -0.1768 0.0118  456 ARG A NH1 
1252 N NH2 . ARG A 160 ? 1.0018 0.8884 0.6491 0.2280  -0.1625 0.0235  456 ARG A NH2 
1253 N N   . SER A 161 ? 0.7321 0.8076 0.6701 0.1470  -0.1202 -0.0188 457 SER A N   
1254 C CA  . SER A 161 ? 0.7896 0.8884 0.7763 0.1095  -0.1111 -0.0231 457 SER A CA  
1255 C C   . SER A 161 ? 0.7087 0.8412 0.7195 0.0894  -0.1088 -0.0263 457 SER A C   
1256 O O   . SER A 161 ? 0.7627 0.9331 0.7745 0.1026  -0.1144 -0.0293 457 SER A O   
1257 C CB  . SER A 161 ? 0.7116 0.8600 0.7374 0.1115  -0.1078 -0.0303 457 SER A CB  
1258 O OG  . SER A 161 ? 0.7604 0.8768 0.7577 0.1354  -0.1098 -0.0280 457 SER A OG  
1259 N N   . ALA A 162 ? 0.6630 0.7836 0.6897 0.0598  -0.1011 -0.0261 458 ALA A N   
1260 C CA  . ALA A 162 ? 0.7121 0.8549 0.7518 0.0445  -0.0980 -0.0298 458 ALA A CA  
1261 C C   . ALA A 162 ? 0.6929 0.8368 0.7580 0.0204  -0.0883 -0.0325 458 ALA A C   
1262 O O   . ALA A 162 ? 0.6222 0.7465 0.6901 0.0130  -0.0848 -0.0285 458 ALA A O   
1263 C CB  . ALA A 162 ? 0.7086 0.8207 0.7081 0.0479  -0.1009 -0.0223 458 ALA A CB  
1264 N N   . ILE A 163 ? 0.6056 0.7716 0.6839 0.0106  -0.0846 -0.0396 459 ILE A N   
1265 C CA  . ILE A 163 ? 0.6419 0.8075 0.7356 -0.0032 -0.0754 -0.0429 459 ILE A CA  
1266 C C   . ILE A 163 ? 0.6427 0.8144 0.7257 -0.0069 -0.0719 -0.0469 459 ILE A C   
1267 O O   . ILE A 163 ? 0.6692 0.8523 0.7422 -0.0038 -0.0775 -0.0513 459 ILE A O   
1268 C CB  . ILE A 163 ? 0.6151 0.7913 0.7314 -0.0080 -0.0738 -0.0509 459 ILE A CB  
1269 C CG1 . ILE A 163 ? 0.5950 0.7629 0.7181 -0.0133 -0.0652 -0.0537 459 ILE A CG1 
1270 C CG2 . ILE A 163 ? 0.6330 0.8310 0.7494 -0.0119 -0.0785 -0.0599 459 ILE A CG2 
1271 C CD1 . ILE A 163 ? 0.6139 0.7757 0.7477 -0.0174 -0.0641 -0.0593 459 ILE A CD1 
1272 N N   . THR A 164 ? 0.6447 0.8146 0.7283 -0.0123 -0.0628 -0.0453 460 THR A N   
1273 C CA  . THR A 164 ? 0.6504 0.8272 0.7211 -0.0130 -0.0570 -0.0495 460 THR A CA  
1274 C C   . THR A 164 ? 0.6578 0.8382 0.7383 -0.0097 -0.0485 -0.0580 460 THR A C   
1275 O O   . THR A 164 ? 0.6757 0.8638 0.7698 -0.0081 -0.0429 -0.0539 460 THR A O   
1276 C CB  . THR A 164 ? 0.6434 0.8206 0.6971 -0.0190 -0.0524 -0.0386 460 THR A CB  
1277 O OG1 . THR A 164 ? 0.6309 0.7883 0.6612 -0.0181 -0.0615 -0.0307 460 THR A OG1 
1278 C CG2 . THR A 164 ? 0.6901 0.8801 0.7295 -0.0178 -0.0447 -0.0437 460 THR A CG2 
1279 N N   . ILE A 165 ? 0.6618 0.8337 0.7293 -0.0076 -0.0485 -0.0700 461 ILE A N   
1280 C CA  . ILE A 165 ? 0.6666 0.8219 0.7288 -0.0008 -0.0429 -0.0796 461 ILE A CA  
1281 C C   . ILE A 165 ? 0.7068 0.8622 0.7466 0.0107  -0.0337 -0.0857 461 ILE A C   
1282 O O   . ILE A 165 ? 0.7220 0.8654 0.7369 0.0075  -0.0360 -0.0939 461 ILE A O   
1283 C CB  . ILE A 165 ? 0.6825 0.8143 0.7341 -0.0113 -0.0504 -0.0893 461 ILE A CB  
1284 C CG1 . ILE A 165 ? 0.6559 0.7961 0.7314 -0.0193 -0.0568 -0.0833 461 ILE A CG1 
1285 C CG2 . ILE A 165 ? 0.7414 0.8357 0.7687 -0.0042 -0.0452 -0.0992 461 ILE A CG2 
1286 C CD1 . ILE A 165 ? 0.6897 0.8325 0.7598 -0.0365 -0.0656 -0.0896 461 ILE A CD1 
1287 N N   . PHE A 166 ? 0.6809 0.8557 0.7284 0.0247  -0.0235 -0.0821 462 PHE A N   
1288 C CA  . PHE A 166 ? 0.7057 0.8922 0.7336 0.0419  -0.0123 -0.0876 462 PHE A CA  
1289 C C   . PHE A 166 ? 0.7708 0.9141 0.7672 0.0613  -0.0100 -0.1022 462 PHE A C   
1290 O O   . PHE A 166 ? 0.7953 0.9007 0.7865 0.0559  -0.0171 -0.1061 462 PHE A O   
1291 C CB  . PHE A 166 ? 0.6564 0.8964 0.7072 0.0477  -0.0028 -0.0767 462 PHE A CB  
1292 C CG  . PHE A 166 ? 0.6937 0.9594 0.7540 0.0242  -0.0043 -0.0633 462 PHE A CG  
1293 C CD1 . PHE A 166 ? 0.6823 0.9549 0.7211 0.0189  -0.0006 -0.0628 462 PHE A CD1 
1294 C CD2 . PHE A 166 ? 0.6516 0.9227 0.7324 0.0068  -0.0106 -0.0513 462 PHE A CD2 
1295 C CE1 . PHE A 166 ? 0.7080 0.9901 0.7432 -0.0033 -0.0028 -0.0493 462 PHE A CE1 
1296 C CE2 . PHE A 166 ? 0.6512 0.9269 0.7247 -0.0152 -0.0130 -0.0390 462 PHE A CE2 
1297 C CZ  . PHE A 166 ? 0.7179 0.9969 0.7674 -0.0205 -0.0093 -0.0373 462 PHE A CZ  
1298 N N   . PRO A 167 ? 0.7839 0.9241 0.7496 0.0829  -0.0004 -0.1110 463 PRO A N   
1299 C CA  . PRO A 167 ? 0.8504 0.9277 0.7668 0.1021  0.0005  -0.1267 463 PRO A CA  
1300 C C   . PRO A 167 ? 0.8931 0.9451 0.8094 0.1183  -0.0004 -0.1263 463 PRO A C   
1301 O O   . PRO A 167 ? 0.8479 0.9474 0.7998 0.1307  0.0038  -0.1162 463 PRO A O   
1302 C CB  . PRO A 167 ? 0.8484 0.9431 0.7377 0.1326  0.0141  -0.1334 463 PRO A CB  
1303 C CG  . PRO A 167 ? 0.8124 0.9598 0.7243 0.1130  0.0162  -0.1248 463 PRO A CG  
1304 C CD  . PRO A 167 ? 0.7519 0.9358 0.7154 0.0876  0.0093  -0.1082 463 PRO A CD  
1305 N N   . GLN A 168 ? 0.9953 0.9700 0.8667 0.1143  -0.0068 -0.1368 464 GLN A N   
1306 C CA  . GLN A 168 ? 0.9623 0.8975 0.8208 0.1284  -0.0086 -0.1364 464 GLN A CA  
1307 C C   . GLN A 168 ? 1.0359 0.9700 0.8684 0.1808  0.0022  -0.1403 464 GLN A C   
1308 O O   . GLN A 168 ? 1.0049 0.9386 0.8062 0.2057  0.0107  -0.1491 464 GLN A O   
1309 C CB  . GLN A 168 ? 1.0140 0.8581 0.8174 0.1061  -0.0178 -0.1465 464 GLN A CB  
1310 C CG  . GLN A 168 ? 1.0643 0.8382 0.7915 0.1175  -0.0155 -0.1632 464 GLN A CG  
1311 C CD  . GLN A 168 ? 1.1765 0.8872 0.8613 0.0718  -0.0271 -0.1718 464 GLN A CD  
1312 O OE1 . GLN A 168 ? 1.0932 0.8487 0.8178 0.0330  -0.0349 -0.1669 464 GLN A OE1 
1313 N NE2 . GLN A 168 ? 1.2579 0.8633 0.8556 0.0761  -0.0290 -0.1847 464 GLN A NE2 
1314 N N   . ARG A 169 ? 1.0036 0.9425 0.8483 0.2009  0.0019  -0.1338 465 ARG A N   
1315 C CA  . ARG A 169 ? 1.0875 1.0223 0.9007 0.2576  0.0103  -0.1379 465 ARG A CA  
1316 C C   . ARG A 169 ? 1.2020 1.0281 0.9222 0.2797  0.0109  -0.1550 465 ARG A C   
1317 O O   . ARG A 169 ? 1.2410 0.9800 0.9181 0.2469  0.0018  -0.1614 465 ARG A O   
1318 C CB  . ARG A 169 ? 1.1155 1.0536 0.9439 0.2731  0.0061  -0.1289 465 ARG A CB  
1319 C CG  . ARG A 169 ? 1.2031 1.1222 0.9851 0.3384  0.0122  -0.1341 465 ARG A CG  
1320 C CD  . ARG A 169 ? 1.2102 1.1436 1.0098 0.3562  0.0071  -0.1240 465 ARG A CD  
1321 N NE  . ARG A 169 ? 1.1659 1.2255 1.0501 0.3456  0.0087  -0.1100 465 ARG A NE  
1322 C CZ  . ARG A 169 ? 1.0691 1.1530 1.0004 0.3099  0.0004  -0.0985 465 ARG A CZ  
1323 N NH1 . ARG A 169 ? 1.0989 1.1019 1.0086 0.2828  -0.0088 -0.0985 465 ARG A NH1 
1324 N NH2 . ARG A 169 ? 1.0162 1.2079 1.0129 0.2991  0.0017  -0.0868 465 ARG A NH2 
1325 N N   . THR A 170 ? 1.2882 1.1213 0.9732 0.3336  0.0220  -0.1629 466 THR A N   
1326 C CA  . THR A 170 ? 1.3951 1.1124 0.9774 0.3631  0.0230  -0.1804 466 THR A CA  
1327 C C   . THR A 170 ? 1.5019 1.1884 1.0379 0.4319  0.0272  -0.1824 466 THR A C   
1328 O O   . THR A 170 ? 1.5187 1.1231 1.0144 0.4340  0.0186  -0.1811 466 THR A O   
1329 C CB  . THR A 170 ? 1.4031 1.1368 0.9629 0.3750  0.0327  -0.1915 466 THR A CB  
1330 O OG1 . THR A 170 ? 1.3725 1.2382 0.9970 0.4015  0.0455  -0.1830 466 THR A OG1 
1331 C CG2 . THR A 170 ? 1.3663 1.0875 0.9376 0.3103  0.0248  -0.1935 466 THR A CG2 
1332 N N   . ASP A 171 ? 1.5010 1.2589 1.0414 0.4899  0.0406  -0.1849 467 ASP A N   
1333 C CA  . ASP A 171 ? 1.5705 1.3212 1.0719 0.5658  0.0450  -0.1863 467 ASP A CA  
1334 C C   . ASP A 171 ? 1.5578 1.4064 1.1381 0.5678  0.0416  -0.1685 467 ASP A C   
1335 O O   . ASP A 171 ? 1.6711 1.4859 1.2164 0.6135  0.0378  -0.1663 467 ASP A O   
1336 C CB  . ASP A 171 ? 1.6555 1.4720 1.1446 0.6206  0.0592  -0.1909 467 ASP A CB  
1337 C CG  . ASP A 171 ? 1.6304 1.6191 1.2198 0.6108  0.0716  -0.1831 467 ASP A CG  
1338 O OD1 . ASP A 171 ? 1.6102 1.6388 1.2667 0.5404  0.0657  -0.1727 467 ASP A OD1 
1339 O OD2 . ASP A 171 ? 1.6437 1.7274 1.2513 0.6463  0.0794  -0.1756 467 ASP A OD2 
1340 N N   . GLY A 172 ? 1.4802 1.4441 1.1598 0.5179  0.0415  -0.1551 468 GLY A N   
1341 C CA  . GLY A 172 ? 1.3849 1.4542 1.1402 0.5161  0.0389  -0.1388 468 GLY A CA  
1342 C C   . GLY A 172 ? 1.3449 1.5717 1.1608 0.5391  0.0513  -0.1321 468 GLY A C   
1343 O O   . GLY A 172 ? 1.2534 1.5828 1.1435 0.5139  0.0487  -0.1175 468 GLY A O   
1344 N N   . LYS A 173 ? 1.3799 1.6295 1.1624 0.5838  0.0648  -0.1426 469 LYS A N   
1345 C CA  . LYS A 173 ? 1.3180 1.7216 1.1558 0.5919  0.0766  -0.1343 469 LYS A CA  
1346 C C   . LYS A 173 ? 1.2961 1.7457 1.1695 0.5416  0.0849  -0.1343 469 LYS A C   
1347 O O   . LYS A 173 ? 1.2044 1.7871 1.1281 0.5359  0.0961  -0.1264 469 LYS A O   
1348 C CB  . LYS A 173 ? 1.3625 1.7652 1.1440 0.6488  0.0802  -0.1364 469 LYS A CB  
1349 C CG  . LYS A 173 ? 1.4026 1.7896 1.1545 0.6927  0.0698  -0.1292 469 LYS A CG  
1350 C CD  . LYS A 173 ? 1.3319 1.8808 1.1509 0.6936  0.0703  -0.1130 469 LYS A CD  
1351 C CE  . LYS A 173 ? 1.3622 2.0078 1.1826 0.7154  0.0815  -0.1123 469 LYS A CE  
1352 N NZ  . LYS A 173 ? 1.2867 2.0980 1.1746 0.7005  0.0824  -0.0969 469 LYS A NZ  
1353 N N   . HIS A 174 ? 1.3009 1.6426 1.1457 0.4980  0.0776  -0.1405 470 HIS A N   
1354 C CA  . HIS A 174 ? 1.2724 1.6388 1.1443 0.4431  0.0803  -0.1376 470 HIS A CA  
1355 C C   . HIS A 174 ? 1.2523 1.5828 1.1611 0.3773  0.0648  -0.1276 470 HIS A C   
1356 O O   . HIS A 174 ? 1.3117 1.5448 1.1896 0.3486  0.0557  -0.1342 470 HIS A O   
1357 C CB  . HIS A 174 ? 1.3198 1.6013 1.1221 0.4555  0.0849  -0.1547 470 HIS A CB  
1358 C CG  . HIS A 174 ? 1.3704 1.6781 1.1268 0.5270  0.1007  -0.1663 470 HIS A CG  
1359 N ND1 . HIS A 174 ? 1.4755 1.6775 1.1453 0.5851  0.1002  -0.1823 470 HIS A ND1 
1360 C CD2 . HIS A 174 ? 1.3448 1.7739 1.1255 0.5522  0.1180  -0.1640 470 HIS A CD2 
1361 C CE1 . HIS A 174 ? 1.5447 1.7933 1.1936 0.6300  0.1094  -0.1821 470 HIS A CE1 
1362 N NE2 . HIS A 174 ? 1.4855 1.8757 1.2027 0.6115  0.1207  -0.1718 470 HIS A NE2 
1363 N N   . ASP A 175 ? 1.1629 1.5771 1.1356 0.3540  0.0617  -0.1118 471 ASP A N   
1364 C CA  . ASP A 175 ? 1.0615 1.4487 1.0678 0.3005  0.0478  -0.1019 471 ASP A CA  
1365 C C   . ASP A 175 ? 0.9908 1.4398 1.0409 0.2486  0.0489  -0.0902 471 ASP A C   
1366 O O   . ASP A 175 ? 0.9827 1.5342 1.0648 0.2459  0.0578  -0.0812 471 ASP A O   
1367 C CB  . ASP A 175 ? 1.0463 1.4634 1.0810 0.3104  0.0411  -0.0929 471 ASP A CB  
1368 C CG  . ASP A 175 ? 1.0852 1.3995 1.0727 0.3373  0.0331  -0.1010 471 ASP A CG  
1369 O OD1 . ASP A 175 ? 1.1737 1.3928 1.1026 0.3469  0.0330  -0.1141 471 ASP A OD1 
1370 O OD2 . ASP A 175 ? 1.0830 1.4077 1.0864 0.3456  0.0263  -0.0940 471 ASP A OD2 
1371 N N   . PHE A 176 ? 0.9257 1.3132 0.9727 0.2073  0.0395  -0.0897 472 PHE A N   
1372 C CA  . PHE A 176 ? 0.8177 1.2420 0.8975 0.1590  0.0368  -0.0770 472 PHE A CA  
1373 C C   . PHE A 176 ? 0.7685 1.2113 0.8849 0.1359  0.0274  -0.0649 472 PHE A C   
1374 O O   . PHE A 176 ? 0.7284 1.1132 0.8408 0.1358  0.0175  -0.0675 472 PHE A O   
1375 C CB  . PHE A 176 ? 0.8005 1.1559 0.8589 0.1323  0.0294  -0.0816 472 PHE A CB  
1376 C CG  . PHE A 176 ? 0.8161 1.1652 0.8410 0.1433  0.0379  -0.0907 472 PHE A CG  
1377 C CD1 . PHE A 176 ? 0.8578 1.1630 0.8387 0.1809  0.0426  -0.1066 472 PHE A CD1 
1378 C CD2 . PHE A 176 ? 0.8035 1.1826 0.8326 0.1167  0.0410  -0.0835 472 PHE A CD2 
1379 C CE1 . PHE A 176 ? 0.8798 1.1749 0.8241 0.1915  0.0504  -0.1163 472 PHE A CE1 
1380 C CE2 . PHE A 176 ? 0.7901 1.1642 0.7861 0.1270  0.0490  -0.0919 472 PHE A CE2 
1381 C CZ  . PHE A 176 ? 0.8118 1.1460 0.7670 0.1645  0.0538  -0.1088 472 PHE A CZ  
1382 N N   . ARG A 177 ? 0.7180 1.2389 0.8651 0.1128  0.0306  -0.0518 473 ARG A N   
1383 C CA  . ARG A 177 ? 0.7013 1.2388 0.8769 0.0879  0.0213  -0.0407 473 ARG A CA  
1384 C C   . ARG A 177 ? 0.6727 1.2398 0.8582 0.0390  0.0201  -0.0272 473 ARG A C   
1385 O O   . ARG A 177 ? 0.6691 1.3002 0.8559 0.0287  0.0304  -0.0220 473 ARG A O   
1386 C CB  . ARG A 177 ? 0.6726 1.2827 0.8694 0.1151  0.0243  -0.0382 473 ARG A CB  
1387 C CG  . ARG A 177 ? 0.7146 1.2779 0.8926 0.1632  0.0221  -0.0490 473 ARG A CG  
1388 C CD  . ARG A 177 ? 0.6966 1.1712 0.8674 0.1472  0.0089  -0.0500 473 ARG A CD  
1389 N NE  . ARG A 177 ? 0.6854 1.1851 0.8861 0.1170  -0.0001 -0.0384 473 ARG A NE  
1390 C CZ  . ARG A 177 ? 0.7165 1.2502 0.9322 0.1326  -0.0043 -0.0343 473 ARG A CZ  
1391 N NH1 . ARG A 177 ? 0.7160 1.2676 0.9201 0.1823  -0.0001 -0.0398 473 ARG A NH1 
1392 N NH2 . ARG A 177 ? 0.6824 1.2278 0.9189 0.1003  -0.0135 -0.0247 473 ARG A NH2 
1393 N N   . VAL A 178 ? 0.6659 1.1821 0.8512 0.0095  0.0082  -0.0215 474 VAL A N   
1394 C CA  . VAL A 178 ? 0.6604 1.1971 0.8479 -0.0356 0.0044  -0.0073 474 VAL A CA  
1395 C C   . VAL A 178 ? 0.6676 1.2630 0.8811 -0.0408 0.0016  -0.0011 474 VAL A C   
1396 O O   . VAL A 178 ? 0.6801 1.2461 0.9025 -0.0279 -0.0068 -0.0041 474 VAL A O   
1397 C CB  . VAL A 178 ? 0.6523 1.1052 0.8196 -0.0578 -0.0076 -0.0047 474 VAL A CB  
1398 C CG1 . VAL A 178 ? 0.6730 1.1274 0.8221 -0.1033 -0.0106 0.0094  474 VAL A CG1 
1399 C CG2 . VAL A 178 ? 0.6929 1.0933 0.8391 -0.0439 -0.0074 -0.0131 474 VAL A CG2 
1400 N N   . TRP A 179 ? 0.6530 1.3379 0.8782 -0.0608 0.0086  0.0077  475 TRP A N   
1401 C CA  . TRP A 179 ? 0.6662 1.4229 0.9176 -0.0686 0.0048  0.0141  475 TRP A CA  
1402 C C   . TRP A 179 ? 0.6706 1.3876 0.9116 -0.1160 -0.0086 0.0236  475 TRP A C   
1403 O O   . TRP A 179 ? 0.6686 1.4154 0.9273 -0.1179 -0.0161 0.0261  475 TRP A O   
1404 C CB  . TRP A 179 ? 0.6444 1.5274 0.9135 -0.0772 0.0167  0.0206  475 TRP A CB  
1405 C CG  . TRP A 179 ? 0.6671 1.6035 0.9485 -0.0169 0.0289  0.0101  475 TRP A CG  
1406 C CD1 . TRP A 179 ? 0.6707 1.5383 0.9330 0.0276  0.0329  -0.0034 475 TRP A CD1 
1407 C CD2 . TRP A 179 ? 0.6550 1.7220 0.9636 0.0082  0.0379  0.0116  475 TRP A CD2 
1408 N NE1 . TRP A 179 ? 0.6789 1.6121 0.9470 0.0807  0.0441  -0.0109 475 TRP A NE1 
1409 C CE2 . TRP A 179 ? 0.6837 1.7444 0.9825 0.0740  0.0478  -0.0019 475 TRP A CE2 
1410 C CE3 . TRP A 179 ? 0.6589 1.8104 0.9760 -0.0181 0.0358  0.0223  475 TRP A CE3 
1411 C CZ2 . TRP A 179 ? 0.7298 1.8737 1.0311 0.1186  0.0560  -0.0045 475 TRP A CZ2 
1412 C CZ3 . TRP A 179 ? 0.6984 1.9261 1.0158 0.0236  0.0426  0.0198  475 TRP A CZ3 
1413 C CH2 . TRP A 179 ? 0.7859 2.0087 1.0952 0.0925  0.0522  0.0069  475 TRP A CH2 
1414 N N   . ASN A 180 ? 0.6758 1.3225 0.8826 -0.1508 -0.0123 0.0286  476 ASN A N   
1415 C CA  . ASN A 180 ? 0.6636 1.2472 0.8461 -0.1872 -0.0256 0.0352  476 ASN A CA  
1416 C C   . ASN A 180 ? 0.6627 1.1858 0.8534 -0.1561 -0.0345 0.0267  476 ASN A C   
1417 O O   . ASN A 180 ? 0.6311 1.1189 0.8271 -0.1180 -0.0320 0.0165  476 ASN A O   
1418 C CB  . ASN A 180 ? 0.7253 1.2283 0.8587 -0.2160 -0.0280 0.0406  476 ASN A CB  
1419 C CG  . ASN A 180 ? 0.7693 1.3197 0.8870 -0.2459 -0.0177 0.0491  476 ASN A CG  
1420 O OD1 . ASN A 180 ? 0.7216 1.3247 0.8586 -0.2204 -0.0055 0.0442  476 ASN A OD1 
1421 N ND2 . ASN A 180 ? 0.8172 1.3416 0.8915 -0.3015 -0.0224 0.0619  476 ASN A ND2 
1422 N N   . SER A 181 ? 0.6372 1.1483 0.8249 -0.1762 -0.0451 0.0309  477 SER A N   
1423 C CA  . SER A 181 ? 0.6301 1.0809 0.8200 -0.1519 -0.0532 0.0240  477 SER A CA  
1424 C C   . SER A 181 ? 0.6503 1.0045 0.8063 -0.1513 -0.0574 0.0213  477 SER A C   
1425 O O   . SER A 181 ? 0.6068 0.9201 0.7684 -0.1217 -0.0591 0.0131  477 SER A O   
1426 C CB  . SER A 181 ? 0.6248 1.0881 0.8156 -0.1740 -0.0636 0.0291  477 SER A CB  
1427 O OG  . SER A 181 ? 0.6490 1.1108 0.8081 -0.2277 -0.0682 0.0394  477 SER A OG  
1428 N N   . GLN A 182 ? 0.6795 0.9986 0.7961 -0.1837 -0.0592 0.0288  478 GLN A N   
1429 C CA  . GLN A 182 ? 0.7022 0.9337 0.7789 -0.1793 -0.0637 0.0277  478 GLN A CA  
1430 C C   . GLN A 182 ? 0.7249 0.9490 0.7679 -0.2040 -0.0595 0.0355  478 GLN A C   
1431 O O   . GLN A 182 ? 0.7595 1.0228 0.7931 -0.2423 -0.0572 0.0447  478 GLN A O   
1432 C CB  . GLN A 182 ? 0.7522 0.9140 0.7923 -0.1923 -0.0754 0.0300  478 GLN A CB  
1433 C CG  . GLN A 182 ? 0.7343 0.8934 0.8021 -0.1652 -0.0793 0.0221  478 GLN A CG  
1434 C CD  . GLN A 182 ? 0.8304 0.9690 0.8781 -0.1888 -0.0887 0.0259  478 GLN A CD  
1435 O OE1 . GLN A 182 ? 0.8857 0.9571 0.8781 -0.2112 -0.0959 0.0305  478 GLN A OE1 
1436 N NE2 . GLN A 182 ? 0.7980 0.9884 0.8836 -0.1824 -0.0894 0.0238  478 GLN A NE2 
1437 N N   . LEU A 183 ? 0.7461 0.9264 0.7706 -0.1838 -0.0586 0.0322  479 LEU A N   
1438 C CA  . LEU A 183 ? 0.7495 0.9224 0.7416 -0.2013 -0.0539 0.0391  479 LEU A CA  
1439 C C   . LEU A 183 ? 0.8090 0.9418 0.7434 -0.2504 -0.0587 0.0527  479 LEU A C   
1440 O O   . LEU A 183 ? 0.8634 1.0287 0.7826 -0.2834 -0.0520 0.0616  479 LEU A O   
1441 C CB  . LEU A 183 ? 0.7797 0.8971 0.7503 -0.1717 -0.0569 0.0343  479 LEU A CB  
1442 C CG  . LEU A 183 ? 0.7568 0.9050 0.7709 -0.1320 -0.0527 0.0211  479 LEU A CG  
1443 C CD1 . LEU A 183 ? 0.6985 0.8053 0.6847 -0.1138 -0.0563 0.0191  479 LEU A CD1 
1444 C CD2 . LEU A 183 ? 0.7219 0.9469 0.7726 -0.1305 -0.0405 0.0179  479 LEU A CD2 
1445 N N   . ILE A 184 ? 0.8442 0.9012 0.7381 -0.2573 -0.0702 0.0546  480 ILE A N   
1446 C CA  . ILE A 184 ? 0.8936 0.8874 0.7153 -0.3054 -0.0771 0.0667  480 ILE A CA  
1447 C C   . ILE A 184 ? 0.9828 0.9864 0.8112 -0.3279 -0.0838 0.0667  480 ILE A C   
1448 O O   . ILE A 184 ? 0.9659 0.9346 0.8006 -0.2995 -0.0905 0.0590  480 ILE A O   
1449 C CB  . ILE A 184 ? 0.9728 0.8454 0.7171 -0.2907 -0.0862 0.0690  480 ILE A CB  
1450 C CG1 . ILE A 184 ? 0.9778 0.8482 0.7131 -0.2723 -0.0806 0.0704  480 ILE A CG1 
1451 C CG2 . ILE A 184 ? 1.0901 0.8760 0.7435 -0.3417 -0.0946 0.0811  480 ILE A CG2 
1452 C CD1 . ILE A 184 ? 1.0381 0.8008 0.7023 -0.2455 -0.0904 0.0720  480 ILE A CD1 
1453 N N   . ARG A 185 ? 0.9690 1.0311 0.7993 -0.3792 -0.0817 0.0752  481 ARG A N   
1454 C CA  . ARG A 185 ? 0.9867 1.0650 0.8166 -0.4112 -0.0896 0.0770  481 ARG A CA  
1455 C C   . ARG A 185 ? 1.0925 1.1775 0.8716 -0.4858 -0.0913 0.0911  481 ARG A C   
1456 O O   . ARG A 185 ? 1.0449 1.1765 0.8242 -0.5080 -0.0817 0.0984  481 ARG A O   
1457 C CB  . ARG A 185 ? 0.9140 1.1117 0.8323 -0.3890 -0.0847 0.0703  481 ARG A CB  
1458 C CG  . ARG A 185 ? 0.8833 1.0826 0.8509 -0.3232 -0.0818 0.0574  481 ARG A CG  
1459 C CD  . ARG A 185 ? 0.8284 1.0958 0.8500 -0.3088 -0.0839 0.0524  481 ARG A CD  
1460 N NE  . ARG A 185 ? 0.9046 1.1283 0.8919 -0.3374 -0.0965 0.0549  481 ARG A NE  
1461 C CZ  . ARG A 185 ? 0.8725 1.1376 0.8923 -0.3297 -0.1016 0.0517  481 ARG A CZ  
1462 N NH1 . ARG A 185 ? 0.7553 1.1005 0.8391 -0.2919 -0.0954 0.0463  481 ARG A NH1 
1463 N NH2 . ARG A 185 ? 0.9404 1.1596 0.9203 -0.3603 -0.1137 0.0539  481 ARG A NH2 
1464 N N   . TYR A 186 ? 1.1017 1.1419 0.8345 -0.5278 -0.1034 0.0947  482 TYR A N   
1465 C CA  . TYR A 186 ? 1.2209 1.2679 0.8996 -0.5947 -0.1052 0.1066  482 TYR A CA  
1466 C C   . TYR A 186 ? 1.1639 1.3668 0.9132 -0.6011 -0.0977 0.1072  482 TYR A C   
1467 O O   . TYR A 186 ? 1.0869 1.3651 0.9098 -0.5672 -0.0971 0.0994  482 TYR A O   
1468 C CB  . TYR A 186 ? 1.3063 1.2282 0.8916 -0.6163 -0.1197 0.1074  482 TYR A CB  
1469 C CG  . TYR A 186 ? 1.4091 1.1704 0.9120 -0.5996 -0.1268 0.1067  482 TYR A CG  
1470 C CD1 . TYR A 186 ? 1.4597 1.1656 0.9097 -0.6094 -0.1226 0.1147  482 TYR A CD1 
1471 C CD2 . TYR A 186 ? 1.4286 1.0953 0.9050 -0.5672 -0.1372 0.0980  482 TYR A CD2 
1472 C CE1 . TYR A 186 ? 1.5249 1.0812 0.8934 -0.5836 -0.1294 0.1151  482 TYR A CE1 
1473 C CE2 . TYR A 186 ? 1.4900 1.0188 0.8900 -0.5321 -0.1421 0.0962  482 TYR A CE2 
1474 C CZ  . TYR A 186 ? 1.5260 1.0003 0.8723 -0.5376 -0.1387 0.1047  482 TYR A CZ  
1475 O OH  . TYR A 186 ? 1.5706 0.9129 0.8394 -0.4926 -0.1445 0.1027  482 TYR A OH  
1476 N N   . ALA A 187 ? 1.1880 1.4368 0.9086 -0.6425 -0.0927 0.1165  483 ALA A N   
1477 C CA  . ALA A 187 ? 1.1680 1.5663 0.9451 -0.6483 -0.0854 0.1182  483 ALA A CA  
1478 C C   . ALA A 187 ? 1.1968 1.6084 0.9654 -0.6642 -0.0955 0.1180  483 ALA A C   
1479 O O   . ALA A 187 ? 1.2264 1.5306 0.9184 -0.6942 -0.1076 0.1204  483 ALA A O   
1480 C CB  . ALA A 187 ? 1.2003 1.6405 0.9397 -0.6932 -0.0792 0.1279  483 ALA A CB  
1481 N N   . GLY A 188 ? 1.1244 1.6670 0.9667 -0.6414 -0.0903 0.1154  484 GLY A N   
1482 C CA  . GLY A 188 ? 1.1430 1.7235 0.9812 -0.6599 -0.0982 0.1172  484 GLY A CA  
1483 C C   . GLY A 188 ? 1.1810 1.8795 1.0190 -0.6950 -0.0936 0.1256  484 GLY A C   
1484 O O   . GLY A 188 ? 1.1190 1.9400 1.0199 -0.6660 -0.0824 0.1242  484 GLY A O   
1485 N N   . TYR A 189 ? 1.3182 1.9801 1.0801 -0.7568 -0.1027 0.1340  485 TYR A N   
1486 C CA  . TYR A 189 ? 1.3362 2.1084 1.0865 -0.8007 -0.1007 0.1428  485 TYR A CA  
1487 C C   . TYR A 189 ? 1.4102 2.2127 1.1513 -0.8221 -0.1103 0.1453  485 TYR A C   
1488 O O   . TYR A 189 ? 1.4919 2.1843 1.1611 -0.8573 -0.1223 0.1475  485 TYR A O   
1489 C CB  . TYR A 189 ? 1.3949 2.1054 1.0527 -0.8660 -0.1038 0.1518  485 TYR A CB  
1490 C CG  . TYR A 189 ? 1.3896 2.0416 1.0372 -0.8530 -0.0968 0.1503  485 TYR A CG  
1491 C CD1 . TYR A 189 ? 1.3536 2.1139 1.0544 -0.8342 -0.0831 0.1503  485 TYR A CD1 
1492 C CD2 . TYR A 189 ? 1.4483 1.9350 1.0269 -0.8585 -0.1041 0.1491  485 TYR A CD2 
1493 C CE1 . TYR A 189 ? 1.3983 2.1054 1.0880 -0.8243 -0.0764 0.1496  485 TYR A CE1 
1494 C CE2 . TYR A 189 ? 1.5023 1.9346 1.0677 -0.8471 -0.0980 0.1487  485 TYR A CE2 
1495 C CZ  . TYR A 189 ? 1.4417 1.9854 1.0640 -0.8325 -0.0840 0.1493  485 TYR A CZ  
1496 O OH  . TYR A 189 ? 1.4367 1.9259 1.0443 -0.8226 -0.0776 0.1495  485 TYR A OH  
1497 N N   . LYS A 190 ? 1.3847 2.3331 1.1932 -0.7987 -0.1051 0.1449  486 LYS A N   
1498 C CA  . LYS A 190 ? 1.4765 2.4810 1.2727 -0.8291 -0.1132 0.1498  486 LYS A CA  
1499 C C   . LYS A 190 ? 1.5585 2.5988 1.2846 -0.9072 -0.1160 0.1619  486 LYS A C   
1500 O O   . LYS A 190 ? 1.5581 2.6493 1.2791 -0.9225 -0.1084 0.1656  486 LYS A O   
1501 C CB  . LYS A 190 ? 1.4170 2.5680 1.3028 -0.7752 -0.1070 0.1457  486 LYS A CB  
1502 C CG  . LYS A 190 ? 1.3928 2.6509 1.3322 -0.7375 -0.0924 0.1439  486 LYS A CG  
1503 C CD  . LYS A 190 ? 1.3452 2.7573 1.3506 -0.6936 -0.0874 0.1421  486 LYS A CD  
1504 C CE  . LYS A 190 ? 1.3171 2.7166 1.3878 -0.6119 -0.0851 0.1304  486 LYS A CE  
1505 N NZ  . LYS A 190 ? 1.2499 2.7876 1.3791 -0.5538 -0.0747 0.1272  486 LYS A NZ  
1506 N N   . GLN A 191 ? 1.5986 2.6103 1.2664 -0.9590 -0.1276 0.1680  487 GLN A N   
1507 C CA  . GLN A 191 ? 1.6613 2.6819 1.2441 -1.0426 -0.1331 0.1797  487 GLN A CA  
1508 C C   . GLN A 191 ? 1.6484 2.8468 1.2633 -1.0635 -0.1311 0.1864  487 GLN A C   
1509 O O   . GLN A 191 ? 1.5934 2.8783 1.2785 -1.0196 -0.1295 0.1825  487 GLN A O   
1510 C CB  . GLN A 191 ? 1.7563 2.6214 1.2362 -1.0934 -0.1480 0.1830  487 GLN A CB  
1511 C CG  . GLN A 191 ? 1.7764 2.4583 1.1976 -1.0837 -0.1515 0.1781  487 GLN A CG  
1512 C CD  . GLN A 191 ? 1.8819 2.5267 1.2405 -1.1230 -0.1495 0.1832  487 GLN A CD  
1513 O OE1 . GLN A 191 ? 1.7965 2.5252 1.2119 -1.0987 -0.1381 0.1819  487 GLN A OE1 
1514 N NE2 . GLN A 191 ? 2.0430 2.5563 1.2782 -1.1835 -0.1612 0.1886  487 GLN A NE2 
1515 N N   . PRO A 192 ? 1.6731 2.9314 1.2339 -1.1310 -0.1320 0.1966  488 PRO A N   
1516 C CA  . PRO A 192 ? 1.6357 3.0704 1.2197 -1.1566 -0.1310 0.2039  488 PRO A CA  
1517 C C   . PRO A 192 ? 1.6511 3.0856 1.2163 -1.1811 -0.1414 0.2073  488 PRO A C   
1518 O O   . PRO A 192 ? 1.6256 3.2140 1.2270 -1.1860 -0.1401 0.2118  488 PRO A O   
1519 C CB  . PRO A 192 ? 1.7052 3.1661 1.2115 -1.2377 -0.1330 0.2143  488 PRO A CB  
1520 C CG  . PRO A 192 ? 1.7765 3.0410 1.1950 -1.2669 -0.1397 0.2134  488 PRO A CG  
1521 C CD  . PRO A 192 ? 1.7564 2.9351 1.2353 -1.1839 -0.1338 0.2014  488 PRO A CD  
1522 N N   . ASP A 193 ? 1.7116 2.9811 1.2199 -1.1947 -0.1518 0.2053  489 ASP A N   
1523 C CA  . ASP A 193 ? 1.6800 2.9357 1.1732 -1.2109 -0.1620 0.2070  489 ASP A CA  
1524 C C   . ASP A 193 ? 1.6330 2.8525 1.2009 -1.1305 -0.1616 0.1949  489 ASP A C   
1525 O O   . ASP A 193 ? 1.6505 2.8063 1.1949 -1.1390 -0.1717 0.1938  489 ASP A O   
1526 C CB  . ASP A 193 ? 1.7992 2.8943 1.1646 -1.2854 -0.1755 0.2132  489 ASP A CB  
1527 C CG  . ASP A 193 ? 1.8571 2.7585 1.1810 -1.2591 -0.1782 0.2054  489 ASP A CG  
1528 O OD1 . ASP A 193 ? 1.8644 2.7319 1.1782 -1.2525 -0.1723 0.2040  489 ASP A OD1 
1529 O OD2 . ASP A 193 ? 1.8294 2.6169 1.1315 -1.2427 -0.1862 0.2003  489 ASP A OD2 
1530 N N   . GLY A 194 ? 1.5667 2.8201 1.2183 -1.0548 -0.1509 0.1856  490 GLY A N   
1531 C CA  . GLY A 194 ? 1.5330 2.7727 1.2587 -0.9781 -0.1505 0.1742  490 GLY A CA  
1532 C C   . GLY A 194 ? 1.5598 2.6277 1.2679 -0.9482 -0.1538 0.1651  490 GLY A C   
1533 O O   . GLY A 194 ? 1.5353 2.6014 1.3134 -0.8772 -0.1495 0.1547  490 GLY A O   
1534 N N   . SER A 195 ? 1.6449 2.5676 1.2563 -0.9992 -0.1618 0.1686  491 SER A N   
1535 C CA  . SER A 195 ? 1.6519 2.4103 1.2378 -0.9700 -0.1656 0.1600  491 SER A CA  
1536 C C   . SER A 195 ? 1.6105 2.3561 1.2307 -0.9305 -0.1546 0.1551  491 SER A C   
1537 O O   . SER A 195 ? 1.5480 2.4142 1.2219 -0.9162 -0.1437 0.1568  491 SER A O   
1538 C CB  . SER A 195 ? 1.6995 2.3048 1.1611 -1.0316 -0.1776 0.1652  491 SER A CB  
1539 O OG  . SER A 195 ? 1.7929 2.4105 1.1827 -1.0996 -0.1776 0.1764  491 SER A OG  
1540 N N   . THR A 196 ? 1.6080 2.2072 1.1950 -0.9106 -0.1573 0.1488  492 THR A N   
1541 C CA  . THR A 196 ? 1.5425 2.1264 1.1711 -0.8649 -0.1475 0.1427  492 THR A CA  
1542 C C   . THR A 196 ? 1.5860 2.0065 1.1250 -0.8847 -0.1519 0.1430  492 THR A C   
1543 O O   . THR A 196 ? 1.6659 1.9560 1.1434 -0.8883 -0.1621 0.1400  492 THR A O   
1544 C CB  . THR A 196 ? 1.4522 2.0520 1.1683 -0.7900 -0.1449 0.1307  492 THR A CB  
1545 O OG1 . THR A 196 ? 1.3777 2.1222 1.1683 -0.7670 -0.1419 0.1302  492 THR A OG1 
1546 C CG2 . THR A 196 ? 1.3401 1.9313 1.0988 -0.7456 -0.1345 0.1249  492 THR A CG2 
1547 N N   . LEU A 197 ? 1.5712 1.9980 1.1002 -0.8935 -0.1442 0.1463  493 LEU A N   
1548 C CA  . LEU A 197 ? 1.5889 1.8678 1.0367 -0.9047 -0.1474 0.1463  493 LEU A CA  
1549 C C   . LEU A 197 ? 1.4986 1.7554 1.0078 -0.8408 -0.1395 0.1373  493 LEU A C   
1550 O O   . LEU A 197 ? 1.4145 1.7893 1.0197 -0.8026 -0.1283 0.1340  493 LEU A O   
1551 C CB  . LEU A 197 ? 1.6007 1.8924 0.9867 -0.9616 -0.1457 0.1560  493 LEU A CB  
1552 C CG  . LEU A 197 ? 1.6769 1.8052 0.9518 -0.9858 -0.1523 0.1577  493 LEU A CG  
1553 C CD1 . LEU A 197 ? 1.7688 1.7441 0.9374 -1.0076 -0.1673 0.1574  493 LEU A CD1 
1554 C CD2 . LEU A 197 ? 1.7834 1.9464 1.0060 -1.0442 -0.1508 0.1666  493 LEU A CD2 
1555 N N   . GLY A 198 ? 1.5165 1.6206 0.9651 -0.8271 -0.1456 0.1332  494 GLY A N   
1556 C CA  . GLY A 198 ? 1.4530 1.5289 0.9518 -0.7700 -0.1397 0.1250  494 GLY A CA  
1557 C C   . GLY A 198 ? 1.3276 1.4399 0.9073 -0.7178 -0.1401 0.1147  494 GLY A C   
1558 O O   . GLY A 198 ? 1.3983 1.4726 0.9563 -0.7206 -0.1496 0.1119  494 GLY A O   
1559 N N   . ASP A 199 ? 1.2592 1.4462 0.9288 -0.6711 -0.1304 0.1088  495 ASP A N   
1560 C CA  . ASP A 199 ? 1.2042 1.4131 0.9427 -0.6199 -0.1322 0.0980  495 ASP A CA  
1561 C C   . ASP A 199 ? 1.1330 1.4943 0.9558 -0.6037 -0.1267 0.0974  495 ASP A C   
1562 O O   . ASP A 199 ? 1.0820 1.5426 0.9634 -0.5838 -0.1151 0.0978  495 ASP A O   
1563 C CB  . ASP A 199 ? 1.1823 1.3634 0.9564 -0.5759 -0.1273 0.0909  495 ASP A CB  
1564 C CG  . ASP A 199 ? 1.1594 1.3121 0.9692 -0.5315 -0.1341 0.0792  495 ASP A CG  
1565 O OD1 . ASP A 199 ? 1.0754 1.2760 0.9157 -0.5235 -0.1386 0.0762  495 ASP A OD1 
1566 O OD2 . ASP A 199 ? 1.1473 1.2296 0.9509 -0.5053 -0.1357 0.0732  495 ASP A OD2 
1567 N N   . PRO A 200 ? 1.1201 1.5020 0.9485 -0.6067 -0.1347 0.0961  496 PRO A N   
1568 C CA  . PRO A 200 ? 1.0494 1.5728 0.9529 -0.5848 -0.1303 0.0957  496 PRO A CA  
1569 C C   . PRO A 200 ? 0.9782 1.5581 0.9648 -0.5198 -0.1237 0.0866  496 PRO A C   
1570 O O   . PRO A 200 ? 0.9291 1.6263 0.9724 -0.4941 -0.1171 0.0868  496 PRO A O   
1571 C CB  . PRO A 200 ? 1.0653 1.5677 0.9468 -0.5989 -0.1426 0.0951  496 PRO A CB  
1572 C CG  . PRO A 200 ? 1.1542 1.5225 0.9345 -0.6464 -0.1513 0.0990  496 PRO A CG  
1573 C CD  . PRO A 200 ? 1.1509 1.4260 0.9087 -0.6304 -0.1479 0.0955  496 PRO A CD  
1574 N N   . ALA A 201 ? 0.9643 1.4634 0.9537 -0.4913 -0.1256 0.0789  497 ALA A N   
1575 C CA  . ALA A 201 ? 0.9492 1.4972 1.0095 -0.4329 -0.1198 0.0709  497 ALA A CA  
1576 C C   . ALA A 201 ? 0.9239 1.5583 1.0199 -0.4191 -0.1049 0.0734  497 ALA A C   
1577 O O   . ALA A 201 ? 0.9112 1.6283 1.0649 -0.3728 -0.0982 0.0691  497 ALA A O   
1578 C CB  . ALA A 201 ? 0.9405 1.3865 0.9885 -0.4135 -0.1250 0.0633  497 ALA A CB  
1579 N N   . ASN A 202 ? 0.9506 1.5613 1.0056 -0.4570 -0.0997 0.0802  498 ASN A N   
1580 C CA  . ASN A 202 ? 0.9492 1.6248 1.0296 -0.4456 -0.0855 0.0819  498 ASN A CA  
1581 C C   . ASN A 202 ? 0.9596 1.7378 1.0389 -0.4710 -0.0785 0.0901  498 ASN A C   
1582 O O   . ASN A 202 ? 0.9601 1.7823 1.0408 -0.4764 -0.0674 0.0934  498 ASN A O   
1583 C CB  . ASN A 202 ? 0.9675 1.5506 1.0015 -0.4688 -0.0842 0.0843  498 ASN A CB  
1584 C CG  . ASN A 202 ? 0.9275 1.4034 0.9498 -0.4500 -0.0937 0.0769  498 ASN A CG  
1585 O OD1 . ASN A 202 ? 0.8803 1.3716 0.9508 -0.3991 -0.0936 0.0676  498 ASN A OD1 
1586 N ND2 . ASN A 202 ? 0.9621 1.3177 0.9095 -0.4833 -0.1015 0.0805  498 ASN A ND2 
1587 N N   . VAL A 203 ? 1.0007 1.8221 1.0761 -0.4872 -0.0851 0.0933  499 VAL A N   
1588 C CA  . VAL A 203 ? 1.0183 1.9392 1.0846 -0.5190 -0.0806 0.1020  499 VAL A CA  
1589 C C   . VAL A 203 ? 1.0078 2.0499 1.1316 -0.4727 -0.0669 0.0991  499 VAL A C   
1590 O O   . VAL A 203 ? 1.0485 2.1568 1.1625 -0.4936 -0.0585 0.1049  499 VAL A O   
1591 C CB  . VAL A 203 ? 0.9850 1.9333 1.0386 -0.5424 -0.0911 0.1056  499 VAL A CB  
1592 C CG1 . VAL A 203 ? 1.0498 2.1342 1.1138 -0.5587 -0.0855 0.1127  499 VAL A CG1 
1593 C CG2 . VAL A 203 ? 1.0578 1.8898 1.0327 -0.6012 -0.1029 0.1107  499 VAL A CG2 
1594 N N   . GLN A 204 ? 0.8848 1.9535 1.0623 -0.4080 -0.0650 0.0899  500 GLN A N   
1595 C CA  . GLN A 204 ? 0.8898 2.0554 1.1101 -0.3565 -0.0520 0.0859  500 GLN A CA  
1596 C C   . GLN A 204 ? 0.8747 2.0142 1.0925 -0.3508 -0.0410 0.0839  500 GLN A C   
1597 O O   . GLN A 204 ? 0.9047 2.1193 1.1234 -0.3530 -0.0303 0.0868  500 GLN A O   
1598 C CB  . GLN A 204 ? 0.8810 2.0596 1.1449 -0.2868 -0.0535 0.0764  500 GLN A CB  
1599 C CG  . GLN A 204 ? 0.8421 2.0837 1.1371 -0.2249 -0.0400 0.0699  500 GLN A CG  
1600 C CD  . GLN A 204 ? 0.8273 2.1180 1.1500 -0.1609 -0.0413 0.0642  500 GLN A CD  
1601 O OE1 . GLN A 204 ? 0.8374 2.0922 1.1647 -0.1519 -0.0525 0.0627  500 GLN A OE1 
1602 N NE2 . GLN A 204 ? 0.8014 2.1711 1.1365 -0.1144 -0.0302 0.0611  500 GLN A NE2 
1603 N N   . PHE A 205 ? 0.8974 1.9345 1.1104 -0.3440 -0.0439 0.0789  501 PHE A N   
1604 C CA  . PHE A 205 ? 0.8789 1.8899 1.0895 -0.3378 -0.0338 0.0769  501 PHE A CA  
1605 C C   . PHE A 205 ? 0.9254 1.9385 1.0903 -0.3976 -0.0300 0.0874  501 PHE A C   
1606 O O   . PHE A 205 ? 0.8971 1.9547 1.0665 -0.3909 -0.0177 0.0879  501 PHE A O   
1607 C CB  . PHE A 205 ? 0.8357 1.7360 1.0417 -0.3292 -0.0403 0.0711  501 PHE A CB  
1608 C CG  . PHE A 205 ? 0.8396 1.7140 1.0425 -0.3232 -0.0307 0.0692  501 PHE A CG  
1609 C CD1 . PHE A 205 ? 0.7697 1.6860 1.0120 -0.2658 -0.0200 0.0598  501 PHE A CD1 
1610 C CD2 . PHE A 205 ? 0.8568 1.6596 1.0093 -0.3740 -0.0324 0.0770  501 PHE A CD2 
1611 C CE1 . PHE A 205 ? 0.7383 1.6181 0.9679 -0.2559 -0.0105 0.0568  501 PHE A CE1 
1612 C CE2 . PHE A 205 ? 0.8354 1.6078 0.9784 -0.3651 -0.0233 0.0756  501 PHE A CE2 
1613 C CZ  . PHE A 205 ? 0.7778 1.5839 0.9576 -0.3032 -0.0121 0.0647  501 PHE A CZ  
1614 N N   . THR A 206 ? 0.9554 1.9154 1.0695 -0.4563 -0.0409 0.0957  502 THR A N   
1615 C CA  . THR A 206 ? 1.0116 1.9650 1.0703 -0.5166 -0.0393 0.1063  502 THR A CA  
1616 C C   . THR A 206 ? 1.0364 2.1266 1.1135 -0.5178 -0.0297 0.1098  502 THR A C   
1617 O O   . THR A 206 ? 1.0722 2.1859 1.1289 -0.5403 -0.0218 0.1145  502 THR A O   
1618 C CB  . THR A 206 ? 1.0503 1.9237 1.0430 -0.5759 -0.0539 0.1136  502 THR A CB  
1619 O OG1 . THR A 206 ? 1.0548 1.7934 1.0204 -0.5728 -0.0626 0.1101  502 THR A OG1 
1620 C CG2 . THR A 206 ? 1.0980 1.9642 1.0234 -0.6411 -0.0540 0.1247  502 THR A CG2 
1621 N N   . GLU A 207 ? 1.0857 2.2693 1.1997 -0.4913 -0.0306 0.1076  503 GLU A N   
1622 C CA  . GLU A 207 ? 1.0932 2.4139 1.2224 -0.4887 -0.0225 0.1109  503 GLU A CA  
1623 C C   . GLU A 207 ? 1.0685 2.4448 1.2389 -0.4282 -0.0077 0.1031  503 GLU A C   
1624 O O   . GLU A 207 ? 1.1397 2.5940 1.3051 -0.4374 0.0011  0.1064  503 GLU A O   
1625 C CB  . GLU A 207 ? 1.1229 2.5258 1.2728 -0.4772 -0.0286 0.1115  503 GLU A CB  
1626 C CG  . GLU A 207 ? 1.2475 2.6531 1.3466 -0.5523 -0.0394 0.1225  503 GLU A CG  
1627 C CD  . GLU A 207 ? 1.3444 2.7068 1.4421 -0.5549 -0.0520 0.1217  503 GLU A CD  
1628 O OE1 . GLU A 207 ? 1.3097 2.6800 1.4547 -0.4943 -0.0520 0.1133  503 GLU A OE1 
1629 O OE2 . GLU A 207 ? 1.4337 2.7501 1.4777 -0.6177 -0.0625 0.1293  503 GLU A OE2 
1630 N N   . ILE A 208 ? 0.9637 2.2976 1.1698 -0.3673 -0.0053 0.0924  504 ILE A N   
1631 C CA  . ILE A 208 ? 0.9090 2.2770 1.1444 -0.3081 0.0084  0.0837  504 ILE A CA  
1632 C C   . ILE A 208 ? 0.9615 2.3048 1.1716 -0.3382 0.0172  0.0872  504 ILE A C   
1633 O O   . ILE A 208 ? 0.9429 2.3587 1.1611 -0.3172 0.0293  0.0855  504 ILE A O   
1634 C CB  . ILE A 208 ? 0.8207 2.1219 1.0850 -0.2490 0.0071  0.0720  504 ILE A CB  
1635 C CG1 . ILE A 208 ? 0.7814 2.1224 1.0699 -0.2084 0.0005  0.0681  504 ILE A CG1 
1636 C CG2 . ILE A 208 ? 0.7461 2.0544 1.0262 -0.1962 0.0208  0.0626  504 ILE A CG2 
1637 C CD1 . ILE A 208 ? 0.7731 2.0390 1.0817 -0.1587 -0.0043 0.0579  504 ILE A CD1 
1638 N N   . CYS A 209 ? 0.9544 2.1921 1.1284 -0.3866 0.0109  0.0925  505 CYS A N   
1639 C CA  . CYS A 209 ? 0.9709 2.1738 1.1124 -0.4184 0.0182  0.0973  505 CYS A CA  
1640 C C   . CYS A 209 ? 1.0537 2.3346 1.1663 -0.4656 0.0208  0.1069  505 CYS A C   
1641 O O   . CYS A 209 ? 1.0325 2.3446 1.1380 -0.4677 0.0319  0.1081  505 CYS A O   
1642 C CB  . CYS A 209 ? 0.9618 2.0270 1.0588 -0.4598 0.0084  0.1020  505 CYS A CB  
1643 S SG  . CYS A 209 ? 0.8732 1.8543 1.0033 -0.4090 0.0038  0.0907  505 CYS A SG  
1644 N N   . ILE A 210 ? 1.0170 2.3337 1.1111 -0.5052 0.0105  0.1138  506 ILE A N   
1645 C CA  . ILE A 210 ? 1.0500 2.4508 1.1156 -0.5540 0.0115  0.1228  506 ILE A CA  
1646 C C   . ILE A 210 ? 0.9961 2.5423 1.1073 -0.5052 0.0230  0.1180  506 ILE A C   
1647 O O   . ILE A 210 ? 1.0021 2.6195 1.1003 -0.5267 0.0296  0.1224  506 ILE A O   
1648 C CB  . ILE A 210 ? 1.0827 2.4824 1.1100 -0.6127 -0.0032 0.1312  506 ILE A CB  
1649 C CG1 . ILE A 210 ? 1.1001 2.3428 1.0786 -0.6477 -0.0153 0.1337  506 ILE A CG1 
1650 C CG2 . ILE A 210 ? 1.1311 2.6000 1.1154 -0.6767 -0.0042 0.1413  506 ILE A CG2 
1651 C CD1 . ILE A 210 ? 1.1747 2.3962 1.1009 -0.7093 -0.0299 0.1417  506 ILE A CD1 
1652 N N   . GLN A 211 ? 0.9795 2.5675 1.1394 -0.4371 0.0251  0.1089  507 GLN A N   
1653 C CA  . GLN A 211 ? 0.9540 2.6656 1.1487 -0.3800 0.0355  0.1032  507 GLN A CA  
1654 C C   . GLN A 211 ? 0.9378 2.6383 1.1408 -0.3432 0.0499  0.0965  507 GLN A C   
1655 O O   . GLN A 211 ? 0.8966 2.6971 1.1087 -0.3191 0.0593  0.0950  507 GLN A O   
1656 C CB  . GLN A 211 ? 0.9753 2.7113 1.2076 -0.3135 0.0328  0.0948  507 GLN A CB  
1657 C CG  . GLN A 211 ? 1.0271 2.7725 1.2530 -0.3457 0.0192  0.1009  507 GLN A CG  
1658 C CD  . GLN A 211 ? 1.1156 2.9949 1.3312 -0.3787 0.0171  0.1097  507 GLN A CD  
1659 O OE1 . GLN A 211 ? 1.1457 3.1378 1.3774 -0.3426 0.0253  0.1077  507 GLN A OE1 
1660 N NE2 . GLN A 211 ? 1.1398 3.0078 1.3242 -0.4475 0.0056  0.1193  507 GLN A NE2 
1661 N N   . GLN A 212 ? 0.9486 2.5324 1.1466 -0.3376 0.0519  0.0923  508 GLN A N   
1662 C CA  . GLN A 212 ? 0.9474 2.5095 1.1438 -0.3152 0.0656  0.0873  508 GLN A CA  
1663 C C   . GLN A 212 ? 0.9489 2.4798 1.1011 -0.3855 0.0670  0.0982  508 GLN A C   
1664 O O   . GLN A 212 ? 0.9214 2.4355 1.0662 -0.3749 0.0789  0.0959  508 GLN A O   
1665 C CB  . GLN A 212 ? 0.9327 2.3926 1.1434 -0.2724 0.0676  0.0772  508 GLN A CB  
1666 C CG  . GLN A 212 ? 0.9459 2.4122 1.1912 -0.2073 0.0637  0.0665  508 GLN A CG  
1667 C CD  . GLN A 212 ? 0.9984 2.5411 1.2623 -0.1332 0.0744  0.0561  508 GLN A CD  
1668 O OE1 . GLN A 212 ? 1.0261 2.5237 1.2986 -0.0747 0.0802  0.0437  508 GLN A OE1 
1669 N NE2 . GLN A 212 ? 0.9651 2.6211 1.2295 -0.1345 0.0761  0.0607  508 GLN A NE2 
1670 N N   . GLY A 213 ? 0.9934 2.5092 1.1092 -0.4568 0.0548  0.1098  509 GLY A N   
1671 C CA  . GLY A 213 ? 1.0246 2.5266 1.0899 -0.5246 0.0549  0.1205  509 GLY A CA  
1672 C C   . GLY A 213 ? 1.1060 2.4722 1.1116 -0.5887 0.0429  0.1292  509 GLY A C   
1673 O O   . GLY A 213 ? 1.1377 2.4706 1.0904 -0.6442 0.0420  0.1379  509 GLY A O   
1674 N N   . TRP A 214 ? 1.0927 2.3742 1.0995 -0.5812 0.0328  0.1269  510 TRP A N   
1675 C CA  . TRP A 214 ? 1.1787 2.3173 1.1213 -0.6330 0.0211  0.1341  510 TRP A CA  
1676 C C   . TRP A 214 ? 1.2400 2.3780 1.1197 -0.7093 0.0091  0.1447  510 TRP A C   
1677 O O   . TRP A 214 ? 1.2310 2.4684 1.1250 -0.7214 0.0052  0.1461  510 TRP A O   
1678 C CB  . TRP A 214 ? 1.1641 2.2196 1.1204 -0.6085 0.0117  0.1289  510 TRP A CB  
1679 C CG  . TRP A 214 ? 1.2095 2.1065 1.0973 -0.6464 0.0013  0.1348  510 TRP A CG  
1680 C CD1 . TRP A 214 ? 1.2413 2.0547 1.0875 -0.6579 0.0058  0.1390  510 TRP A CD1 
1681 C CD2 . TRP A 214 ? 1.2596 2.0573 1.1046 -0.6734 -0.0154 0.1370  510 TRP A CD2 
1682 N NE1 . TRP A 214 ? 1.2830 1.9481 1.0603 -0.6871 -0.0079 0.1439  510 TRP A NE1 
1683 C CE2 . TRP A 214 ? 1.3002 1.9520 1.0751 -0.6966 -0.0210 0.1420  510 TRP A CE2 
1684 C CE3 . TRP A 214 ? 1.2414 2.0563 1.0958 -0.6777 -0.0261 0.1354  510 TRP A CE3 
1685 C CZ2 . TRP A 214 ? 1.3295 1.8499 1.0412 -0.7197 -0.0373 0.1441  510 TRP A CZ2 
1686 C CZ3 . TRP A 214 ? 1.2764 1.9642 1.0716 -0.7050 -0.0414 0.1377  510 TRP A CZ3 
1687 C CH2 . TRP A 214 ? 1.3459 1.8870 1.0693 -0.7238 -0.0470 0.1413  510 TRP A CH2 
1688 N N   . LYS A 215 ? 1.3267 2.3493 1.1305 -0.7604 0.0028  0.1522  511 LYS A N   
1689 C CA  . LYS A 215 ? 1.3804 2.3724 1.1058 -0.8378 -0.0102 0.1616  511 LYS A CA  
1690 C C   . LYS A 215 ? 1.3972 2.2436 1.0665 -0.8576 -0.0264 0.1627  511 LYS A C   
1691 O O   . LYS A 215 ? 1.4692 2.1748 1.0881 -0.8598 -0.0303 0.1639  511 LYS A O   
1692 C CB  . LYS A 215 ? 1.4433 2.4026 1.1130 -0.8782 -0.0063 0.1682  511 LYS A CB  
1693 C CG  . LYS A 215 ? 1.4307 2.5096 1.1613 -0.8400 0.0127  0.1650  511 LYS A CG  
1694 C CD  . LYS A 215 ? 1.4510 2.6819 1.1923 -0.8707 0.0150  0.1684  511 LYS A CD  
1695 C CE  . LYS A 215 ? 1.3871 2.7498 1.1957 -0.8344 0.0153  0.1631  511 LYS A CE  
1696 N NZ  . LYS A 215 ? 1.4549 2.9452 1.2508 -0.8823 0.0114  0.1692  511 LYS A NZ  
1697 N N   . ALA A 216 ? 1.4214 2.3015 1.0969 -0.8682 -0.0357 0.1623  512 ALA A N   
1698 C CA  . ALA A 216 ? 1.4107 2.1644 1.0450 -0.8744 -0.0497 0.1614  512 ALA A CA  
1699 C C   . ALA A 216 ? 1.4729 2.1062 0.9890 -0.9464 -0.0645 0.1689  512 ALA A C   
1700 O O   . ALA A 216 ? 1.4450 2.1366 0.9230 -1.0027 -0.0688 0.1751  512 ALA A O   
1701 C CB  . ALA A 216 ? 1.3879 2.2216 1.0708 -0.8577 -0.0535 0.1582  512 ALA A CB  
1702 N N   . PRO A 217 ? 1.5142 1.9772 0.9641 -0.9453 -0.0733 0.1683  513 PRO A N   
1703 C CA  . PRO A 217 ? 1.6221 1.9491 0.9474 -1.0054 -0.0899 0.1731  513 PRO A CA  
1704 C C   . PRO A 217 ? 1.7281 2.0171 1.0252 -1.0188 -0.1030 0.1720  513 PRO A C   
1705 O O   . PRO A 217 ? 1.8246 1.9574 1.0349 -1.0287 -0.1160 0.1711  513 PRO A O   
1706 C CB  . PRO A 217 ? 1.6564 1.8232 0.9287 -0.9817 -0.0920 0.1716  513 PRO A CB  
1707 C CG  . PRO A 217 ? 1.6057 1.8017 0.9733 -0.9087 -0.0819 0.1651  513 PRO A CG  
1708 C CD  . PRO A 217 ? 1.5127 1.9002 0.9925 -0.8870 -0.0678 0.1629  513 PRO A CD  
1709 N N   . ARG A 218 ? 1.7585 2.1901 1.1247 -1.0166 -0.0996 0.1721  514 ARG A N   
1710 C CA  . ARG A 218 ? 1.7164 2.1498 1.0869 -1.0169 -0.1081 0.1707  514 ARG A CA  
1711 C C   . ARG A 218 ? 1.8022 2.0589 1.0656 -1.0414 -0.1245 0.1708  514 ARG A C   
1712 O O   . ARG A 218 ? 1.9068 2.1381 1.0916 -1.1005 -0.1356 0.1763  514 ARG A O   
1713 C CB  . ARG A 218 ? 1.7421 2.3186 1.1243 -1.0612 -0.1086 0.1769  514 ARG A CB  
1714 C CG  . ARG A 218 ? 1.6424 2.4034 1.1366 -1.0219 -0.0933 0.1749  514 ARG A CG  
1715 C CD  . ARG A 218 ? 1.6737 2.5800 1.1903 -1.0493 -0.0947 0.1797  514 ARG A CD  
1716 N NE  . ARG A 218 ? 1.5835 2.6116 1.2101 -0.9817 -0.0850 0.1733  514 ARG A NE  
1717 C CZ  . ARG A 218 ? 1.5174 2.6493 1.2223 -0.9303 -0.0707 0.1687  514 ARG A CZ  
1718 N NH1 . ARG A 218 ? 1.5425 2.6827 1.2366 -0.9391 -0.0632 0.1701  514 ARG A NH1 
1719 N NH2 . ARG A 218 ? 1.4649 2.6885 1.2557 -0.8670 -0.0641 0.1620  514 ARG A NH2 
1720 N N   . GLY A 219 ? 1.7803 1.9158 1.0365 -0.9950 -0.1262 0.1645  515 GLY A N   
1721 C CA  . GLY A 219 ? 1.8429 1.8160 1.0077 -1.0002 -0.1408 0.1622  515 GLY A CA  
1722 C C   . GLY A 219 ? 1.8091 1.7662 1.0384 -0.9384 -0.1402 0.1538  515 GLY A C   
1723 O O   . GLY A 219 ? 1.7024 1.7885 1.0430 -0.9041 -0.1309 0.1505  515 GLY A O   
1724 N N   . ARG A 220 ? 1.8747 1.6726 1.0309 -0.9208 -0.1506 0.1493  516 ARG A N   
1725 C CA  . ARG A 220 ? 1.8086 1.5794 1.0168 -0.8626 -0.1513 0.1404  516 ARG A CA  
1726 C C   . ARG A 220 ? 1.7947 1.5779 1.0744 -0.8058 -0.1412 0.1351  516 ARG A C   
1727 O O   . ARG A 220 ? 1.6593 1.5726 1.0514 -0.7773 -0.1302 0.1323  516 ARG A O   
1728 C CB  . ARG A 220 ? 1.9162 1.5116 1.0142 -0.8590 -0.1656 0.1367  516 ARG A CB  
1729 C CG  . ARG A 220 ? 1.8291 1.4241 0.9596 -0.8323 -0.1703 0.1302  516 ARG A CG  
1730 C CD  . ARG A 220 ? 1.9120 1.5130 0.9864 -0.8870 -0.1789 0.1359  516 ARG A CD  
1731 N NE  . ARG A 220 ? 2.0243 1.4751 1.0020 -0.8798 -0.1915 0.1316  516 ARG A NE  
1732 C CZ  . ARG A 220 ? 2.0218 1.4705 1.0320 -0.8506 -0.1948 0.1251  516 ARG A CZ  
1733 N NH1 . ARG A 220 ? 1.9056 1.4910 1.0382 -0.8293 -0.1878 0.1221  516 ARG A NH1 
1734 N NH2 . ARG A 220 ? 2.0894 1.3937 1.0024 -0.8402 -0.2055 0.1209  516 ARG A NH2 
1735 N N   . PHE A 221 ? 1.7962 1.4406 1.0034 -0.7882 -0.1454 0.1337  517 PHE A N   
1736 C CA  . PHE A 221 ? 1.6815 1.3033 0.9362 -0.7310 -0.1392 0.1287  517 PHE A CA  
1737 C C   . PHE A 221 ? 1.6600 1.3350 0.9399 -0.7368 -0.1274 0.1347  517 PHE A C   
1738 O O   . PHE A 221 ? 1.7096 1.2915 0.9399 -0.7198 -0.1275 0.1366  517 PHE A O   
1739 C CB  . PHE A 221 ? 1.7364 1.1813 0.8973 -0.6990 -0.1504 0.1237  517 PHE A CB  
1740 C CG  . PHE A 221 ? 1.7841 1.1709 0.9095 -0.6933 -0.1615 0.1174  517 PHE A CG  
1741 C CD1 . PHE A 221 ? 1.6469 1.0854 0.8550 -0.6559 -0.1603 0.1092  517 PHE A CD1 
1742 C CD2 . PHE A 221 ? 1.8884 1.1664 0.8926 -0.7262 -0.1734 0.1193  517 PHE A CD2 
1743 C CE1 . PHE A 221 ? 1.7172 1.1018 0.8905 -0.6503 -0.1698 0.1036  517 PHE A CE1 
1744 C CE2 . PHE A 221 ? 1.9340 1.1574 0.9013 -0.7207 -0.1826 0.1141  517 PHE A CE2 
1745 C CZ  . PHE A 221 ? 1.8285 1.1071 0.8826 -0.6821 -0.1803 0.1066  517 PHE A CZ  
1746 N N   . ASP A 222 ? 1.6037 1.4353 0.9607 -0.7574 -0.1169 0.1378  518 ASP A N   
1747 C CA  . ASP A 222 ? 1.5167 1.4290 0.9158 -0.7582 -0.1031 0.1423  518 ASP A CA  
1748 C C   . ASP A 222 ? 1.3997 1.3715 0.8983 -0.7009 -0.0925 0.1362  518 ASP A C   
1749 O O   . ASP A 222 ? 1.2860 1.3661 0.8746 -0.6774 -0.0883 0.1298  518 ASP A O   
1750 C CB  . ASP A 222 ? 1.5149 1.5733 0.9503 -0.7973 -0.0966 0.1467  518 ASP A CB  
1751 C CG  . ASP A 222 ? 1.6586 1.6691 0.9973 -0.8605 -0.1088 0.1524  518 ASP A CG  
1752 O OD1 . ASP A 222 ? 1.7529 1.6091 0.9901 -0.8728 -0.1220 0.1522  518 ASP A OD1 
1753 O OD2 . ASP A 222 ? 1.6533 1.7816 1.0134 -0.8966 -0.1056 0.1566  518 ASP A OD2 
1754 N N   . VAL A 223 ? 1.4304 1.3282 0.9074 -0.6771 -0.0890 0.1383  519 VAL A N   
1755 C CA  . VAL A 223 ? 1.3303 1.2805 0.8931 -0.6233 -0.0798 0.1319  519 VAL A CA  
1756 C C   . VAL A 223 ? 1.2106 1.3328 0.8671 -0.6229 -0.0634 0.1312  519 VAL A C   
1757 O O   . VAL A 223 ? 1.2177 1.3845 0.8573 -0.6519 -0.0547 0.1388  519 VAL A O   
1758 C CB  . VAL A 223 ? 1.3534 1.1984 0.8663 -0.5810 -0.0801 0.1315  519 VAL A CB  
1759 C CG1 . VAL A 223 ? 1.2188 1.1270 0.8200 -0.5035 -0.0725 0.1171  519 VAL A CG1 
1760 C CG2 . VAL A 223 ? 1.4589 1.1339 0.8717 -0.5726 -0.0964 0.1319  519 VAL A CG2 
1761 N N   . LEU A 224 ? 1.1263 1.3411 0.8755 -0.5748 -0.0601 0.1187  520 LEU A N   
1762 C CA  . LEU A 224 ? 1.0564 1.4297 0.8881 -0.5643 -0.0451 0.1167  520 LEU A CA  
1763 C C   . LEU A 224 ? 1.0300 1.4130 0.8770 -0.5233 -0.0323 0.1129  520 LEU A C   
1764 O O   . LEU A 224 ? 1.0826 1.3701 0.9069 -0.4821 -0.0364 0.1068  520 LEU A O   
1765 C CB  . LEU A 224 ? 0.9790 1.4298 0.8922 -0.5175 -0.0462 0.1043  520 LEU A CB  
1766 C CG  . LEU A 224 ? 0.9821 1.4754 0.8995 -0.5424 -0.0545 0.1059  520 LEU A CG  
1767 C CD1 . LEU A 224 ? 0.9316 1.4118 0.8913 -0.5033 -0.0631 0.0953  520 LEU A CD1 
1768 C CD2 . LEU A 224 ? 0.9727 1.6111 0.9336 -0.5403 -0.0437 0.1072  520 LEU A CD2 
1769 N N   . PRO A 225 ? 1.0094 1.5139 0.8954 -0.5314 -0.0168 0.1158  521 PRO A N   
1770 C CA  . PRO A 225 ? 0.9664 1.4894 0.8726 -0.4864 -0.0041 0.1095  521 PRO A CA  
1771 C C   . PRO A 225 ? 0.9093 1.4677 0.8856 -0.4119 -0.0022 0.0919  521 PRO A C   
1772 O O   . PRO A 225 ? 0.8362 1.4289 0.8523 -0.3971 -0.0078 0.0862  521 PRO A O   
1773 C CB  . PRO A 225 ? 0.9792 1.6309 0.9015 -0.5230 0.0123  0.1185  521 PRO A CB  
1774 C CG  . PRO A 225 ? 0.9840 1.7164 0.9355 -0.5364 0.0062  0.1176  521 PRO A CG  
1775 C CD  . PRO A 225 ? 1.0475 1.6707 0.9541 -0.5634 -0.0123 0.1204  521 PRO A CD  
1776 N N   . LEU A 226 ? 0.8875 1.4329 0.8721 -0.3679 0.0053  0.0835  522 LEU A N   
1777 C CA  . LEU A 226 ? 0.8218 1.3895 0.8593 -0.3020 0.0079  0.0668  522 LEU A CA  
1778 C C   . LEU A 226 ? 0.7731 1.4715 0.8602 -0.2819 0.0236  0.0626  522 LEU A C   
1779 O O   . LEU A 226 ? 0.7763 1.5352 0.8548 -0.3011 0.0365  0.0688  522 LEU A O   
1780 C CB  . LEU A 226 ? 0.8582 1.3479 0.8749 -0.2668 0.0069  0.0589  522 LEU A CB  
1781 C CG  . LEU A 226 ? 0.8678 1.2348 0.8388 -0.2681 -0.0084 0.0605  522 LEU A CG  
1782 C CD1 . LEU A 226 ? 0.8421 1.1587 0.7924 -0.2380 -0.0082 0.0547  522 LEU A CD1 
1783 C CD2 . LEU A 226 ? 0.8351 1.1762 0.8330 -0.2440 -0.0190 0.0522  522 LEU A CD2 
1784 N N   . LEU A 227 ? 0.7019 1.4419 0.8361 -0.2399 0.0227  0.0521  523 LEU A N   
1785 C CA  . LEU A 227 ? 0.6823 1.5326 0.8576 -0.2017 0.0365  0.0450  523 LEU A CA  
1786 C C   . LEU A 227 ? 0.6812 1.4785 0.8629 -0.1387 0.0375  0.0281  523 LEU A C   
1787 O O   . LEU A 227 ? 0.6439 1.4039 0.8408 -0.1096 0.0288  0.0202  523 LEU A O   
1788 C CB  . LEU A 227 ? 0.6383 1.5812 0.8529 -0.2020 0.0340  0.0476  523 LEU A CB  
1789 C CG  . LEU A 227 ? 0.6430 1.7335 0.8795 -0.2187 0.0467  0.0552  523 LEU A CG  
1790 C CD1 . LEU A 227 ? 0.6548 1.8035 0.9197 -0.1771 0.0422  0.0497  523 LEU A CD1 
1791 C CD2 . LEU A 227 ? 0.6639 1.8012 0.8955 -0.1964 0.0652  0.0514  523 LEU A CD2 
1792 N N   . LEU A 228 ? 0.7002 1.4919 0.8654 -0.1213 0.0480  0.0227  524 LEU A N   
1793 C CA  . LEU A 228 ? 0.6932 1.4201 0.8511 -0.0727 0.0474  0.0069  524 LEU A CA  
1794 C C   . LEU A 228 ? 0.7239 1.5210 0.8947 -0.0245 0.0621  -0.0038 524 LEU A C   
1795 O O   . LEU A 228 ? 0.7232 1.5964 0.8916 -0.0298 0.0765  -0.0002 524 LEU A O   
1796 C CB  . LEU A 228 ? 0.7230 1.3732 0.8424 -0.0871 0.0451  0.0072  524 LEU A CB  
1797 C CG  . LEU A 228 ? 0.7680 1.3572 0.8635 -0.1336 0.0324  0.0203  524 LEU A CG  
1798 C CD1 . LEU A 228 ? 0.7538 1.2718 0.8078 -0.1409 0.0292  0.0216  524 LEU A CD1 
1799 C CD2 . LEU A 228 ? 0.7370 1.2736 0.8456 -0.1269 0.0176  0.0175  524 LEU A CD2 
1800 N N   . GLN A 229 ? 0.6866 1.4540 0.8642 0.0230  0.0587  -0.0169 525 GLN A N   
1801 C CA  . GLN A 229 ? 0.7196 1.5276 0.8957 0.0797  0.0704  -0.0293 525 GLN A CA  
1802 C C   . GLN A 229 ? 0.7445 1.4544 0.8836 0.1078  0.0690  -0.0448 525 GLN A C   
1803 O O   . GLN A 229 ? 0.7420 1.3644 0.8721 0.1096  0.0563  -0.0504 525 GLN A O   
1804 C CB  . GLN A 229 ? 0.7224 1.5626 0.9217 0.1126  0.0662  -0.0313 525 GLN A CB  
1805 C CG  . GLN A 229 ? 0.7688 1.6067 0.9498 0.1823  0.0736  -0.0465 525 GLN A CG  
1806 C CD  . GLN A 229 ? 0.7843 1.6166 0.9754 0.2157  0.0650  -0.0485 525 GLN A CD  
1807 O OE1 . GLN A 229 ? 0.7382 1.5963 0.9594 0.1870  0.0553  -0.0377 525 GLN A OE1 
1808 N NE2 . GLN A 229 ? 0.8350 1.6248 0.9930 0.2765  0.0680  -0.0622 525 GLN A NE2 
1809 N N   . ALA A 230 ? 0.7699 1.4978 0.8855 0.1262  0.0819  -0.0517 526 ALA A N   
1810 C CA  . ALA A 230 ? 0.7840 1.4234 0.8579 0.1469  0.0806  -0.0667 526 ALA A CA  
1811 C C   . ALA A 230 ? 0.8221 1.4626 0.8705 0.2094  0.0901  -0.0826 526 ALA A C   
1812 O O   . ALA A 230 ? 0.8147 1.5468 0.8702 0.2370  0.1050  -0.0821 526 ALA A O   
1813 C CB  . ALA A 230 ? 0.7252 1.3663 0.7784 0.1212  0.0867  -0.0638 526 ALA A CB  
1814 N N   . ASN A 231 ? 0.8582 1.3972 0.8725 0.2314  0.0812  -0.0962 527 ASN A N   
1815 C CA  . ASN A 231 ? 0.9481 1.4502 0.9149 0.2904  0.0880  -0.1134 527 ASN A CA  
1816 C C   . ASN A 231 ? 1.0068 1.5945 0.9896 0.3383  0.0978  -0.1116 527 ASN A C   
1817 O O   . ASN A 231 ? 1.0191 1.6310 0.9699 0.3915  0.1110  -0.1219 527 ASN A O   
1818 C CB  . ASN A 231 ? 0.9688 1.4557 0.8924 0.3015  0.0984  -0.1243 527 ASN A CB  
1819 C CG  . ASN A 231 ? 1.0829 1.4739 0.9358 0.3486  0.0988  -0.1451 527 ASN A CG  
1820 O OD1 . ASN A 231 ? 1.1684 1.4714 0.9979 0.3529  0.0865  -0.1509 527 ASN A OD1 
1821 N ND2 . ASN A 231 ? 1.0867 1.4885 0.8980 0.3824  0.1129  -0.1563 527 ASN A ND2 
1822 N N   . GLY A 232 ? 0.9900 1.6276 1.0204 0.3222  0.0910  -0.0985 528 GLY A N   
1823 C CA  . GLY A 232 ? 0.9950 1.7257 1.0465 0.3646  0.0974  -0.0951 528 GLY A CA  
1824 C C   . GLY A 232 ? 0.9312 1.8129 1.0197 0.3602  0.1127  -0.0854 528 GLY A C   
1825 O O   . GLY A 232 ? 0.9680 1.9383 1.0770 0.3882  0.1148  -0.0799 528 GLY A O   
1826 N N   . ASN A 233 ? 0.8565 1.7625 0.9487 0.3190  0.1200  -0.0808 529 ASN A N   
1827 C CA  . ASN A 233 ? 0.8419 1.8933 0.9641 0.3073  0.1358  -0.0705 529 ASN A CA  
1828 C C   . ASN A 233 ? 0.8105 1.9374 0.9850 0.2483  0.1280  -0.0505 529 ASN A C   
1829 O O   . ASN A 233 ? 0.8165 1.8739 1.0005 0.2050  0.1127  -0.0442 529 ASN A O   
1830 C CB  . ASN A 233 ? 0.7614 1.8032 0.8598 0.2808  0.1461  -0.0714 529 ASN A CB  
1831 C CG  . ASN A 233 ? 0.8232 1.8102 0.8658 0.3395  0.1558  -0.0913 529 ASN A CG  
1832 O OD1 . ASN A 233 ? 0.8863 1.9341 0.9161 0.3732  0.1658  -0.0929 529 ASN A OD1 
1833 N ND2 . ASN A 233 ? 0.8565 1.7012 0.8573 0.3409  0.1439  -0.1031 529 ASN A ND2 
1834 N N   . ASP A 234 ? 0.7506 1.9775 0.9391 0.2380  0.1288  -0.0389 530 ASP A N   
1835 C CA  . ASP A 234 ? 0.8004 2.0910 1.0232 0.1788  0.1194  -0.0208 530 ASP A CA  
1836 C C   . ASP A 234 ? 0.7632 2.0206 0.9938 0.1069  0.1186  -0.0112 530 ASP A C   
1837 O O   . ASP A 234 ? 0.7749 2.0242 0.9870 0.0883  0.1299  -0.0113 530 ASP A O   
1838 C CB  . ASP A 234 ? 0.8422 2.2488 1.0684 0.1706  0.1235  -0.0114 530 ASP A CB  
1839 C CG  . ASP A 234 ? 0.9319 2.3768 1.1437 0.2461  0.1248  -0.0201 530 ASP A CG  
1840 O OD1 . ASP A 234 ? 0.9568 2.3400 1.1574 0.2971  0.1186  -0.0297 530 ASP A OD1 
1841 O OD2 . ASP A 234 ? 0.9351 2.4711 1.1424 0.2542  0.1313  -0.0166 530 ASP A OD2 
1842 N N   . PRO A 235 ? 0.7228 1.9548 0.9735 0.0666  0.1050  -0.0025 531 PRO A N   
1843 C CA  . PRO A 235 ? 0.6915 1.8440 0.9293 0.0066  0.0978  0.0053  531 PRO A CA  
1844 C C   . PRO A 235 ? 0.6832 1.8998 0.9156 -0.0595 0.1053  0.0217  531 PRO A C   
1845 O O   . PRO A 235 ? 0.7167 2.0163 0.9504 -0.0689 0.1071  0.0283  531 PRO A O   
1846 C CB  . PRO A 235 ? 0.6707 1.7748 0.9237 -0.0101 0.0790  0.0092  531 PRO A CB  
1847 C CG  . PRO A 235 ? 0.6784 1.8853 0.9587 0.0073  0.0788  0.0124  531 PRO A CG  
1848 C CD  . PRO A 235 ? 0.7413 1.9868 1.0115 0.0746  0.0908  0.0008  531 PRO A CD  
1849 N N   . GLU A 236 ? 0.6997 1.8158 0.8973 -0.1027 0.0982  0.0275  532 GLU A N   
1850 C CA  . GLU A 236 ? 0.6876 1.8303 0.8597 -0.1631 0.1056  0.0423  532 GLU A CA  
1851 C C   . GLU A 236 ? 0.7165 1.7619 0.8579 -0.2239 0.0889  0.0550  532 GLU A C   
1852 O O   . GLU A 236 ? 0.7470 1.6784 0.8762 -0.2103 0.0741  0.0491  532 GLU A O   
1853 C CB  . GLU A 236 ? 0.7216 1.8314 0.8613 -0.1439 0.1172  0.0358  532 GLU A CB  
1854 C CG  . GLU A 236 ? 0.6983 1.8802 0.8536 -0.0767 0.1335  0.0206  532 GLU A CG  
1855 C CD  . GLU A 236 ? 0.7804 1.8846 0.8978 -0.0470 0.1383  0.0085  532 GLU A CD  
1856 O OE1 . GLU A 236 ? 0.7666 1.8322 0.8501 -0.0870 0.1394  0.0171  532 GLU A OE1 
1857 O OE2 . GLU A 236 ? 0.8225 1.8983 0.9379 0.0152  0.1398  -0.0096 532 GLU A OE2 
1858 N N   . LEU A 237 ? 0.7109 1.8004 0.8336 -0.2915 0.0917  0.0724  533 LEU A N   
1859 C CA  . LEU A 237 ? 0.7506 1.7484 0.8330 -0.3517 0.0758  0.0853  533 LEU A CA  
1860 C C   . LEU A 237 ? 0.7940 1.6718 0.8135 -0.3696 0.0725  0.0901  533 LEU A C   
1861 O O   . LEU A 237 ? 0.8476 1.7523 0.8459 -0.3775 0.0858  0.0938  533 LEU A O   
1862 C CB  . LEU A 237 ? 0.7601 1.8179 0.8273 -0.4102 0.0716  0.0984  533 LEU A CB  
1863 C CG  . LEU A 237 ? 0.7762 1.9002 0.8830 -0.3910 0.0625  0.0934  533 LEU A CG  
1864 C CD1 . LEU A 237 ? 0.9069 2.0915 0.9902 -0.4415 0.0564  0.1035  533 LEU A CD1 
1865 C CD2 . LEU A 237 ? 0.7584 1.7986 0.8698 -0.3915 0.0479  0.0917  533 LEU A CD2 
1866 N N   . PHE A 238 ? 0.8360 1.5842 0.8231 -0.3738 0.0545  0.0904  534 PHE A N   
1867 C CA  . PHE A 238 ? 0.9233 1.5521 0.8446 -0.3873 0.0480  0.0961  534 PHE A CA  
1868 C C   . PHE A 238 ? 0.9759 1.4967 0.8475 -0.4242 0.0299  0.1055  534 PHE A C   
1869 O O   . PHE A 238 ? 0.9551 1.4478 0.8499 -0.4049 0.0184  0.0985  534 PHE A O   
1870 C CB  . PHE A 238 ? 0.8840 1.4529 0.8132 -0.3244 0.0450  0.0803  534 PHE A CB  
1871 C CG  . PHE A 238 ? 0.8626 1.5163 0.8335 -0.2796 0.0605  0.0673  534 PHE A CG  
1872 C CD1 . PHE A 238 ? 0.8096 1.5129 0.8354 -0.2342 0.0619  0.0531  534 PHE A CD1 
1873 C CD2 . PHE A 238 ? 0.8603 1.5343 0.8067 -0.2804 0.0733  0.0689  534 PHE A CD2 
1874 C CE1 . PHE A 238 ? 0.7801 1.5460 0.8306 -0.1885 0.0757  0.0402  534 PHE A CE1 
1875 C CE2 . PHE A 238 ? 0.8241 1.5678 0.7999 -0.2356 0.0878  0.0553  534 PHE A CE2 
1876 C CZ  . PHE A 238 ? 0.7775 1.5633 0.8028 -0.1883 0.0888  0.0406  534 PHE A CZ  
1877 N N   . GLN A 239 ? 1.1131 1.5645 0.9084 -0.4743 0.0273  0.1212  535 GLN A N   
1878 C CA  . GLN A 239 ? 1.1766 1.5037 0.9024 -0.5078 0.0101  0.1306  535 GLN A CA  
1879 C C   . GLN A 239 ? 1.2073 1.4081 0.8934 -0.4626 -0.0018 0.1251  535 GLN A C   
1880 O O   . GLN A 239 ? 1.2424 1.4066 0.8896 -0.4558 0.0015  0.1289  535 GLN A O   
1881 C CB  . GLN A 239 ? 1.2634 1.5666 0.9113 -0.5878 0.0124  0.1514  535 GLN A CB  
1882 C CG  . GLN A 239 ? 1.3845 1.5248 0.9341 -0.6154 -0.0059 0.1610  535 GLN A CG  
1883 C CD  . GLN A 239 ? 1.5458 1.6206 0.9942 -0.6818 -0.0043 0.1810  535 GLN A CD  
1884 O OE1 . GLN A 239 ? 1.6609 1.5882 1.0171 -0.6798 -0.0157 0.1880  535 GLN A OE1 
1885 N NE2 . GLN A 239 ? 1.6151 1.7964 1.0865 -0.7172 0.0026  0.1799  535 GLN A NE2 
1886 N N   . ILE A 240 ? 1.1898 1.3311 0.8848 -0.4323 -0.0156 0.1166  536 ILE A N   
1887 C CA  . ILE A 240 ? 1.1882 1.2157 0.8433 -0.3908 -0.0289 0.1122  536 ILE A CA  
1888 C C   . ILE A 240 ? 1.3091 1.2204 0.8550 -0.4269 -0.0365 0.1288  536 ILE A C   
1889 O O   . ILE A 240 ? 1.3306 1.1965 0.8226 -0.4796 -0.0416 0.1401  536 ILE A O   
1890 C CB  . ILE A 240 ? 1.1804 1.1740 0.8591 -0.3627 -0.0412 0.1024  536 ILE A CB  
1891 C CG1 . ILE A 240 ? 1.1079 1.2112 0.8840 -0.3365 -0.0338 0.0888  536 ILE A CG1 
1892 C CG2 . ILE A 240 ? 1.1544 1.0571 0.8042 -0.3123 -0.0533 0.0962  536 ILE A CG2 
1893 C CD1 . ILE A 240 ? 1.0308 1.1557 0.8282 -0.3579 -0.0388 0.0888  536 ILE A CD1 
1894 N N   . PRO A 241 ? 1.3010 1.1575 0.8032 -0.4040 -0.0382 0.1314  537 PRO A N   
1895 C CA  . PRO A 241 ? 1.3752 1.1075 0.7603 -0.4351 -0.0463 0.1485  537 PRO A CA  
1896 C C   . PRO A 241 ? 1.4180 1.0364 0.7411 -0.4388 -0.0628 0.1511  537 PRO A C   
1897 O O   . PRO A 241 ? 1.3638 0.9554 0.7107 -0.3842 -0.0725 0.1389  537 PRO A O   
1898 C CB  . PRO A 241 ? 1.3800 1.0725 0.7443 -0.3834 -0.0502 0.1454  537 PRO A CB  
1899 C CG  . PRO A 241 ? 1.2927 1.1111 0.7598 -0.3507 -0.0380 0.1301  537 PRO A CG  
1900 C CD  . PRO A 241 ? 1.1983 1.0905 0.7468 -0.3462 -0.0354 0.1186  537 PRO A CD  
1901 N N   . PRO A 242 ? 1.4787 1.0333 0.7216 -0.5048 -0.0657 0.1661  538 PRO A N   
1902 C CA  . PRO A 242 ? 1.5317 0.9747 0.7104 -0.5111 -0.0812 0.1670  538 PRO A CA  
1903 C C   . PRO A 242 ? 1.5827 0.8979 0.6965 -0.4467 -0.0963 0.1635  538 PRO A C   
1904 O O   . PRO A 242 ? 1.6045 0.8787 0.7207 -0.4137 -0.1063 0.1541  538 PRO A O   
1905 C CB  . PRO A 242 ? 1.5986 0.9778 0.6775 -0.6002 -0.0816 0.1864  538 PRO A CB  
1906 C CG  . PRO A 242 ? 1.5865 1.1141 0.7338 -0.6416 -0.0634 0.1896  538 PRO A CG  
1907 C CD  . PRO A 242 ? 1.5201 1.1062 0.7259 -0.5810 -0.0546 0.1825  538 PRO A CD  
1908 N N   . GLU A 243 ? 1.6028 0.8669 0.6650 -0.4219 -0.0978 0.1699  539 GLU A N   
1909 C CA  . GLU A 243 ? 1.6080 0.7667 0.6117 -0.3531 -0.1127 0.1666  539 GLU A CA  
1910 C C   . GLU A 243 ? 1.5703 0.8105 0.6784 -0.2818 -0.1142 0.1466  539 GLU A C   
1911 O O   . GLU A 243 ? 1.5716 0.7427 0.6438 -0.2234 -0.1269 0.1415  539 GLU A O   
1912 C CB  . GLU A 243 ? 1.7371 0.8423 0.6716 -0.3405 -0.1141 0.1778  539 GLU A CB  
1913 C CG  . GLU A 243 ? 1.5989 0.8346 0.6253 -0.3247 -0.1012 0.1720  539 GLU A CG  
1914 C CD  . GLU A 243 ? 1.5770 0.8915 0.6240 -0.3958 -0.0836 0.1814  539 GLU A CD  
1915 O OE1 . GLU A 243 ? 1.6288 0.9709 0.6855 -0.4536 -0.0778 0.1852  539 GLU A OE1 
1916 O OE2 . GLU A 243 ? 1.5627 0.9206 0.6182 -0.3931 -0.0753 0.1845  539 GLU A OE2 
1917 N N   . LEU A 244 ? 1.4772 0.8614 0.7077 -0.2854 -0.1016 0.1355  540 LEU A N   
1918 C CA  . LEU A 244 ? 1.3978 0.8594 0.7248 -0.2302 -0.1021 0.1172  540 LEU A CA  
1919 C C   . LEU A 244 ? 1.3593 0.8291 0.7188 -0.2347 -0.1047 0.1097  540 LEU A C   
1920 O O   . LEU A 244 ? 1.2238 0.7321 0.6426 -0.1880 -0.1074 0.0960  540 LEU A O   
1921 C CB  . LEU A 244 ? 1.3157 0.9131 0.7461 -0.2279 -0.0880 0.1082  540 LEU A CB  
1922 C CG  . LEU A 244 ? 1.3061 0.9222 0.7298 -0.2114 -0.0845 0.1101  540 LEU A CG  
1923 C CD1 . LEU A 244 ? 1.1656 0.9026 0.6942 -0.1901 -0.0744 0.0946  540 LEU A CD1 
1924 C CD2 . LEU A 244 ? 1.3292 0.8609 0.6896 -0.1617 -0.0995 0.1115  540 LEU A CD2 
1925 N N   . VAL A 245 ? 1.3916 0.8306 0.7132 -0.2924 -0.1043 0.1182  541 VAL A N   
1926 C CA  . VAL A 245 ? 1.3918 0.8386 0.7401 -0.3003 -0.1076 0.1114  541 VAL A CA  
1927 C C   . VAL A 245 ? 1.4714 0.7695 0.7100 -0.2895 -0.1226 0.1151  541 VAL A C   
1928 O O   . VAL A 245 ? 1.5609 0.7622 0.6997 -0.3388 -0.1276 0.1280  541 VAL A O   
1929 C CB  . VAL A 245 ? 1.3510 0.8679 0.7293 -0.3689 -0.0994 0.1169  541 VAL A CB  
1930 C CG1 . VAL A 245 ? 1.3867 0.8986 0.7792 -0.3782 -0.1058 0.1108  541 VAL A CG1 
1931 C CG2 . VAL A 245 ? 1.2418 0.9066 0.7280 -0.3642 -0.0843 0.1108  541 VAL A CG2 
1932 N N   . LEU A 246 ? 1.4879 0.7679 0.7412 -0.2268 -0.1295 0.1035  542 LEU A N   
1933 C CA  . LEU A 246 ? 1.5576 0.6979 0.7049 -0.2007 -0.1433 0.1048  542 LEU A CA  
1934 C C   . LEU A 246 ? 1.5979 0.7128 0.7349 -0.2311 -0.1467 0.1014  542 LEU A C   
1935 O O   . LEU A 246 ? 1.4995 0.7048 0.7290 -0.2174 -0.1424 0.0899  542 LEU A O   
1936 C CB  . LEU A 246 ? 1.5659 0.7125 0.7335 -0.1162 -0.1483 0.0939  542 LEU A CB  
1937 C CG  . LEU A 246 ? 1.6861 0.7101 0.7578 -0.0670 -0.1612 0.0917  542 LEU A CG  
1938 C CD1 . LEU A 246 ? 1.8145 0.6938 0.7466 -0.0668 -0.1706 0.1055  542 LEU A CD1 
1939 C CD2 . LEU A 246 ? 1.6368 0.7284 0.7708 0.0116  -0.1623 0.0784  542 LEU A CD2 
1940 N N   . GLU A 247 ? 1.6694 0.6544 0.6866 -0.2732 -0.1553 0.1114  543 GLU A N   
1941 C CA  . GLU A 247 ? 1.7481 0.6972 0.7395 -0.3115 -0.1604 0.1091  543 GLU A CA  
1942 C C   . GLU A 247 ? 1.8519 0.6432 0.7206 -0.2761 -0.1738 0.1048  543 GLU A C   
1943 O O   . GLU A 247 ? 1.9365 0.6395 0.7180 -0.2502 -0.1789 0.1034  543 GLU A O   
1944 C CB  . GLU A 247 ? 1.7793 0.7375 0.7447 -0.4077 -0.1579 0.1216  543 GLU A CB  
1945 C CG  . GLU A 247 ? 1.6697 0.8114 0.7731 -0.4359 -0.1438 0.1200  543 GLU A CG  
1946 C CD  . GLU A 247 ? 1.7632 0.9364 0.8441 -0.5245 -0.1399 0.1325  543 GLU A CD  
1947 O OE1 . GLU A 247 ? 1.7828 0.9216 0.8078 -0.5426 -0.1384 0.1396  543 GLU A OE1 
1948 O OE2 . GLU A 247 ? 1.7086 0.9663 0.8391 -0.5626 -0.1389 0.1286  543 GLU A OE2 
1949 N N   . VAL A 248 ? 1.8690 0.6559 0.7483 -0.2678 -0.1775 0.0944  544 VAL A N   
1950 C CA  . VAL A 248 ? 1.9957 0.6780 0.7856 -0.2241 -0.1867 0.0809  544 VAL A CA  
1951 C C   . VAL A 248 ? 2.0617 0.7048 0.7911 -0.2885 -0.1922 0.0782  544 VAL A C   
1952 O O   . VAL A 248 ? 1.9375 0.6562 0.7323 -0.3283 -0.1898 0.0788  544 VAL A O   
1953 C CB  . VAL A 248 ? 1.9095 0.6210 0.7538 -0.1569 -0.1865 0.0712  544 VAL A CB  
1954 C CG1 . VAL A 248 ? 2.0335 0.6423 0.7785 -0.1054 -0.1938 0.0573  544 VAL A CG1 
1955 C CG2 . VAL A 248 ? 1.7873 0.5968 0.7252 -0.0981 -0.1797 0.0702  544 VAL A CG2 
1956 N N   . PRO A 249 ? 2.1547 0.6847 0.7581 -0.3017 -0.2003 0.0756  545 PRO A N   
1957 C CA  . PRO A 249 ? 2.2432 0.7226 0.7723 -0.3532 -0.2081 0.0732  545 PRO A CA  
1958 C C   . PRO A 249 ? 2.2810 0.7111 0.7804 -0.3023 -0.2128 0.0614  545 PRO A C   
1959 O O   . PRO A 249 ? 2.3278 0.6962 0.7860 -0.2266 -0.2143 0.0522  545 PRO A O   
1960 C CB  . PRO A 249 ? 2.3446 0.7054 0.7376 -0.3755 -0.2159 0.0739  545 PRO A CB  
1961 C CG  . PRO A 249 ? 2.3745 0.6932 0.7524 -0.3031 -0.2141 0.0702  545 PRO A CG  
1962 C CD  . PRO A 249 ? 2.2075 0.6515 0.7273 -0.2744 -0.2033 0.0757  545 PRO A CD  
1963 N N   . ILE A 250 ? 2.3208 0.7870 0.8424 -0.3425 -0.2145 0.0619  546 ILE A N   
1964 C CA  . ILE A 250 ? 2.2779 0.7264 0.7992 -0.2997 -0.2166 0.0521  546 ILE A CA  
1965 C C   . ILE A 250 ? 2.4349 0.7509 0.8078 -0.3070 -0.2275 0.0484  546 ILE A C   
1966 O O   . ILE A 250 ? 2.4861 0.7884 0.8143 -0.3765 -0.2331 0.0551  546 ILE A O   
1967 C CB  . ILE A 250 ? 2.2541 0.8197 0.8879 -0.3347 -0.2122 0.0543  546 ILE A CB  
1968 C CG1 . ILE A 250 ? 2.1166 0.8093 0.8861 -0.3376 -0.2021 0.0588  546 ILE A CG1 
1969 C CG2 . ILE A 250 ? 2.1809 0.7279 0.8166 -0.2856 -0.2137 0.0432  546 ILE A CG2 
1970 C CD1 . ILE A 250 ? 2.0478 0.7428 0.8567 -0.2586 -0.1974 0.0529  546 ILE A CD1 
1971 N N   . ARG A 251 ? 2.5029 0.7266 0.7980 -0.2333 -0.2305 0.0379  547 ARG A N   
1972 C CA  . ARG A 251 ? 2.6267 0.7177 0.7748 -0.2269 -0.2405 0.0332  547 ARG A CA  
1973 C C   . ARG A 251 ? 2.6405 0.7300 0.7999 -0.1602 -0.2387 0.0232  547 ARG A C   
1974 O O   . ARG A 251 ? 2.5434 0.7152 0.8040 -0.1035 -0.2302 0.0173  547 ARG A O   
1975 C CB  . ARG A 251 ? 2.7560 0.7229 0.7736 -0.1968 -0.2463 0.0290  547 ARG A CB  
1976 C CG  . ARG A 251 ? 2.7204 0.6969 0.7648 -0.1013 -0.2404 0.0195  547 ARG A CG  
1977 C CD  . ARG A 251 ? 2.6473 0.7037 0.7830 -0.1088 -0.2334 0.0257  547 ARG A CD  
1978 N NE  . ARG A 251 ? 2.6250 0.6696 0.7545 -0.0248 -0.2303 0.0185  547 ARG A NE  
1979 C CZ  . ARG A 251 ? 2.5373 0.6639 0.7594 -0.0081 -0.2234 0.0234  547 ARG A CZ  
1980 N NH1 . ARG A 251 ? 2.4274 0.6568 0.7613 -0.0627 -0.2176 0.0348  547 ARG A NH1 
1981 N NH2 . ARG A 251 ? 2.6024 0.7078 0.7986 0.0646  -0.2224 0.0177  547 ARG A NH2 
1982 N N   . HIS A 252 ? 2.7050 0.7038 0.7595 -0.1694 -0.2466 0.0220  548 HIS A N   
1983 C CA  . HIS A 252 ? 2.8132 0.7971 0.8587 -0.1039 -0.2451 0.0127  548 HIS A CA  
1984 C C   . HIS A 252 ? 2.9420 0.8033 0.8520 -0.0321 -0.2495 0.0041  548 HIS A C   
1985 O O   . HIS A 252 ? 3.0537 0.8049 0.8391 -0.0521 -0.2577 0.0062  548 HIS A O   
1986 C CB  . HIS A 252 ? 2.7790 0.7440 0.7967 -0.1526 -0.2505 0.0172  548 HIS A CB  
1987 C CG  . HIS A 252 ? 2.8206 0.8093 0.8718 -0.0948 -0.2463 0.0087  548 HIS A CG  
1988 N ND1 . HIS A 252 ? 2.9218 0.8045 0.8551 -0.0413 -0.2508 0.0029  548 HIS A ND1 
1989 C CD2 . HIS A 252 ? 2.6777 0.7841 0.8636 -0.0806 -0.2379 0.0045  548 HIS A CD2 
1990 C CE1 . HIS A 252 ? 2.8651 0.8053 0.8638 0.0023  -0.2446 -0.0039 548 HIS A CE1 
1991 N NE2 . HIS A 252 ? 2.6579 0.7313 0.8083 -0.0214 -0.2369 -0.0037 548 HIS A NE2 
1992 N N   . PRO A 253 ? 2.9139 0.7968 0.8447 0.0536  -0.2439 -0.0060 549 PRO A N   
1993 C CA  . PRO A 253 ? 3.0006 0.7776 0.8018 0.1288  -0.2476 -0.0142 549 PRO A CA  
1994 C C   . PRO A 253 ? 3.1860 0.8443 0.8625 0.1234  -0.2549 -0.0134 549 PRO A C   
1995 O O   . PRO A 253 ? 3.3280 0.9105 0.9164 0.1914  -0.2554 -0.0200 549 PRO A O   
1996 C CB  . PRO A 253 ? 2.9066 0.7880 0.8061 0.2178  -0.2363 -0.0238 549 PRO A CB  
1997 C CG  . PRO A 253 ? 2.7924 0.7894 0.8295 0.1857  -0.2298 -0.0215 549 PRO A CG  
1998 C CD  . PRO A 253 ? 2.7482 0.7673 0.8294 0.0886  -0.2329 -0.0106 549 PRO A CD  
1999 N N   . LYS A 254 ? 3.1610 0.8078 0.8328 0.0455  -0.2600 -0.0049 550 LYS A N   
2000 C CA  . LYS A 254 ? 3.3138 0.8444 0.8667 0.0283  -0.2676 -0.0026 550 LYS A CA  
2001 C C   . LYS A 254 ? 3.3917 0.8679 0.8882 -0.0758 -0.2765 0.0088  550 LYS A C   
2002 O O   . LYS A 254 ? 3.5750 0.9198 0.9354 -0.0915 -0.2845 0.0105  550 LYS A O   
2003 C CB  . LYS A 254 ? 3.2712 0.8464 0.8697 0.0457  -0.2648 -0.0045 550 LYS A CB  
2004 C CG  . LYS A 254 ? 3.2779 0.9111 0.9257 0.1472  -0.2557 -0.0154 550 LYS A CG  
2005 C CD  . LYS A 254 ? 3.4877 1.0114 1.0124 0.2124  -0.2580 -0.0210 550 LYS A CD  
2006 C CE  . LYS A 254 ? 3.4476 1.0486 1.0271 0.3132  -0.2480 -0.0310 550 LYS A CE  
2007 N NZ  . LYS A 254 ? 3.3592 1.0031 0.9642 0.3702  -0.2428 -0.0366 550 LYS A NZ  
2008 N N   . PHE A 255 ? 3.2631 0.8412 0.8590 -0.1474 -0.2755 0.0170  551 PHE A N   
2009 C CA  . PHE A 255 ? 3.3532 0.9058 0.9077 -0.2490 -0.2831 0.0290  551 PHE A CA  
2010 C C   . PHE A 255 ? 3.4303 0.9806 0.9724 -0.2945 -0.2846 0.0340  551 PHE A C   
2011 O O   . PHE A 255 ? 3.3313 0.9948 0.9842 -0.3113 -0.2790 0.0366  551 PHE A O   
2012 C CB  . PHE A 255 ? 3.2568 0.9287 0.9217 -0.3022 -0.2813 0.0361  551 PHE A CB  
2013 C CG  . PHE A 255 ? 3.2210 0.9054 0.9096 -0.2573 -0.2792 0.0308  551 PHE A CG  
2014 C CD1 . PHE A 255 ? 3.2745 0.8713 0.8706 -0.2767 -0.2860 0.0330  551 PHE A CD1 
2015 C CD2 . PHE A 255 ? 3.1138 0.9072 0.9340 -0.1975 -0.2684 0.0219  551 PHE A CD2 
2016 C CE1 . PHE A 255 ? 3.3119 0.9194 0.9281 -0.2355 -0.2840 0.0281  551 PHE A CE1 
2017 C CE2 . PHE A 255 ? 3.0230 0.8344 0.8716 -0.1575 -0.2653 0.0156  551 PHE A CE2 
2018 C CZ  . PHE A 255 ? 3.1730 0.8887 0.9145 -0.1757 -0.2736 0.0194  551 PHE A CZ  
2019 N N   . ASP A 256 ? 3.5646 0.9826 0.9673 -0.3148 -0.2923 0.0354  552 ASP A N   
2020 C CA  . ASP A 256 ? 3.6738 1.0805 1.0538 -0.3598 -0.2941 0.0400  552 ASP A CA  
2021 C C   . ASP A 256 ? 3.5768 1.0591 0.9995 -0.4679 -0.2963 0.0533  552 ASP A C   
2022 O O   . ASP A 256 ? 3.6087 1.1238 1.0492 -0.5080 -0.2954 0.0578  552 ASP A O   
2023 C CB  . ASP A 256 ? 3.9329 1.1673 1.1416 -0.3471 -0.3023 0.0370  552 ASP A CB  
2024 C CG  . ASP A 256 ? 4.0273 1.2186 1.2127 -0.2468 -0.2984 0.0253  552 ASP A CG  
2025 O OD1 . ASP A 256 ? 4.0245 1.2061 1.2110 -0.1662 -0.2953 0.0169  552 ASP A OD1 
2026 O OD2 . ASP A 256 ? 4.0562 1.2293 1.2233 -0.2485 -0.2984 0.0248  552 ASP A OD2 
2027 N N   . TRP A 257 ? 3.5094 1.0251 0.9481 -0.5154 -0.2989 0.0599  553 TRP A N   
2028 C CA  . TRP A 257 ? 3.4320 1.0593 0.9409 -0.6085 -0.2987 0.0724  553 TRP A CA  
2029 C C   . TRP A 257 ? 3.2463 1.0399 0.9219 -0.5977 -0.2888 0.0733  553 TRP A C   
2030 O O   . TRP A 257 ? 3.1573 1.0590 0.9008 -0.6671 -0.2870 0.0835  553 TRP A O   
2031 C CB  . TRP A 257 ? 3.4713 1.1008 0.9582 -0.6608 -0.3040 0.0796  553 TRP A CB  
2032 C CG  . TRP A 257 ? 3.3990 1.0466 0.9332 -0.6001 -0.3011 0.0730  553 TRP A CG  
2033 C CD1 . TRP A 257 ? 3.5120 1.0411 0.9538 -0.5461 -0.3048 0.0654  553 TRP A CD1 
2034 C CD2 . TRP A 257 ? 3.2038 0.9948 0.8851 -0.5851 -0.2937 0.0731  553 TRP A CD2 
2035 N NE1 . TRP A 257 ? 3.3969 0.9899 0.9211 -0.4998 -0.2999 0.0606  553 TRP A NE1 
2036 C CE2 . TRP A 257 ? 3.2636 1.0138 0.9333 -0.5239 -0.2935 0.0651  553 TRP A CE2 
2037 C CE3 . TRP A 257 ? 3.0879 1.0464 0.9268 -0.6143 -0.2850 0.0772  553 TRP A CE3 
2038 C CZ2 . TRP A 257 ? 3.0855 0.9533 0.8948 -0.4942 -0.2853 0.0602  553 TRP A CZ2 
2039 C CZ3 . TRP A 257 ? 2.9632 1.0374 0.9439 -0.5822 -0.2766 0.0717  553 TRP A CZ3 
2040 C CH2 . TRP A 257 ? 2.9678 0.9947 0.9321 -0.5244 -0.2771 0.0628  553 TRP A CH2 
2041 N N   . PHE A 258 ? 3.1479 0.9664 0.8869 -0.5125 -0.2825 0.0630  554 PHE A N   
2042 C CA  . PHE A 258 ? 3.0289 1.0098 0.9514 -0.4954 -0.2698 0.0618  554 PHE A CA  
2043 C C   . PHE A 258 ? 3.0119 1.0456 0.9754 -0.5255 -0.2657 0.0666  554 PHE A C   
2044 O O   . PHE A 258 ? 2.8963 1.0731 0.9951 -0.5546 -0.2572 0.0721  554 PHE A O   
2045 C CB  . PHE A 258 ? 2.9057 0.8922 0.8794 -0.3956 -0.2631 0.0488  554 PHE A CB  
2046 C CG  . PHE A 258 ? 2.7466 0.8762 0.8833 -0.3815 -0.2535 0.0466  554 PHE A CG  
2047 C CD1 . PHE A 258 ? 2.6489 0.9009 0.9190 -0.3825 -0.2440 0.0480  554 PHE A CD1 
2048 C CD2 . PHE A 258 ? 2.7463 0.8840 0.8981 -0.3683 -0.2542 0.0430  554 PHE A CD2 
2049 C CE1 . PHE A 258 ? 2.5133 0.8897 0.9246 -0.3703 -0.2360 0.0451  554 PHE A CE1 
2050 C CE2 . PHE A 258 ? 2.5397 0.8035 0.8349 -0.3564 -0.2461 0.0393  554 PHE A CE2 
2051 C CZ  . PHE A 258 ? 2.4204 0.8018 0.8431 -0.3576 -0.2374 0.0399  554 PHE A CZ  
2052 N N   . LYS A 259 ? 3.0582 0.9770 0.9036 -0.5168 -0.2714 0.0642  555 LYS A N   
2053 C CA  . LYS A 259 ? 3.1603 1.1207 1.0358 -0.5468 -0.2678 0.0687  555 LYS A CA  
2054 C C   . LYS A 259 ? 3.1206 1.1543 1.0136 -0.6484 -0.2691 0.0821  555 LYS A C   
2055 O O   . LYS A 259 ? 3.0046 1.1466 0.9904 -0.6777 -0.2614 0.0880  555 LYS A O   
2056 C CB  . LYS A 259 ? 3.2217 1.0312 0.9515 -0.5201 -0.2751 0.0625  555 LYS A CB  
2057 C CG  . LYS A 259 ? 3.4305 1.1031 1.0023 -0.5664 -0.2861 0.0656  555 LYS A CG  
2058 C CD  . LYS A 259 ? 3.5597 1.0948 1.0061 -0.5453 -0.2909 0.0606  555 LYS A CD  
2059 C CE  . LYS A 259 ? 3.7161 1.1282 1.0750 -0.4525 -0.2933 0.0487  555 LYS A CE  
2060 N NZ  . LYS A 259 ? 3.7228 1.2156 1.1893 -0.3658 -0.2848 0.0400  555 LYS A NZ  
2061 N N   . ASP A 260 ? 3.1333 1.1153 0.9377 -0.7021 -0.2783 0.0876  556 ASP A N   
2062 C CA  . ASP A 260 ? 3.1589 1.2128 0.9691 -0.7996 -0.2801 0.1006  556 ASP A CA  
2063 C C   . ASP A 260 ? 3.0200 1.2617 1.0009 -0.8194 -0.2697 0.1064  556 ASP A C   
2064 O O   . ASP A 260 ? 3.0068 1.3534 1.0329 -0.8882 -0.2670 0.1166  556 ASP A O   
2065 C CB  . ASP A 260 ? 3.2763 1.2157 0.9438 -0.8498 -0.2917 0.1048  556 ASP A CB  
2066 C CG  . ASP A 260 ? 3.4673 1.2443 0.9852 -0.8505 -0.2991 0.1010  556 ASP A CG  
2067 O OD1 . ASP A 260 ? 3.5199 1.3111 1.0330 -0.8788 -0.2977 0.1035  556 ASP A OD1 
2068 O OD2 . ASP A 260 ? 3.6099 1.2438 1.0131 -0.8202 -0.3061 0.0954  556 ASP A OD2 
2069 N N   . LEU A 261 ? 2.9046 1.1930 0.9790 -0.7584 -0.2638 0.0994  557 LEU A N   
2070 C CA  . LEU A 261 ? 2.7870 1.2535 1.0326 -0.7627 -0.2529 0.1020  557 LEU A CA  
2071 C C   . LEU A 261 ? 2.7435 1.3180 1.0861 -0.7696 -0.2427 0.1054  557 LEU A C   
2072 O O   . LEU A 261 ? 2.6505 1.3791 1.1117 -0.7986 -0.2346 0.1111  557 LEU A O   
2073 C CB  . LEU A 261 ? 2.7027 1.1813 1.0204 -0.6873 -0.2488 0.0912  557 LEU A CB  
2074 C CG  . LEU A 261 ? 2.7199 1.1205 0.9662 -0.6811 -0.2568 0.0883  557 LEU A CG  
2075 C CD1 . LEU A 261 ? 2.6132 1.0184 0.9223 -0.6003 -0.2523 0.0758  557 LEU A CD1 
2076 C CD2 . LEU A 261 ? 2.7605 1.2569 1.0478 -0.7518 -0.2581 0.0979  557 LEU A CD2 
2077 N N   . GLY A 262 ? 2.8603 1.3571 1.1517 -0.7407 -0.2428 0.1018  558 GLY A N   
2078 C CA  . GLY A 262 ? 2.7913 1.3746 1.1557 -0.7526 -0.2338 0.1062  558 GLY A CA  
2079 C C   . GLY A 262 ? 2.6026 1.3259 1.1324 -0.7136 -0.2208 0.1044  558 GLY A C   
2080 O O   . GLY A 262 ? 2.5440 1.3950 1.1648 -0.7435 -0.2117 0.1113  558 GLY A O   
2081 N N   . LEU A 263 ? 2.4196 1.1229 0.9863 -0.6474 -0.2197 0.0950  559 LEU A N   
2082 C CA  . LEU A 263 ? 2.2323 1.0530 0.9442 -0.6086 -0.2088 0.0918  559 LEU A CA  
2083 C C   . LEU A 263 ? 2.1516 0.9366 0.8733 -0.5524 -0.2041 0.0881  559 LEU A C   
2084 O O   . LEU A 263 ? 2.2139 0.8712 0.8310 -0.5210 -0.2101 0.0841  559 LEU A O   
2085 C CB  . LEU A 263 ? 2.1732 1.0019 0.9243 -0.5714 -0.2104 0.0830  559 LEU A CB  
2086 C CG  . LEU A 263 ? 2.1988 1.0611 0.9370 -0.6265 -0.2155 0.0877  559 LEU A CG  
2087 C CD1 . LEU A 263 ? 2.1346 0.9914 0.9002 -0.5885 -0.2177 0.0783  559 LEU A CD1 
2088 C CD2 . LEU A 263 ? 2.0850 1.1083 0.9233 -0.6802 -0.2083 0.0967  559 LEU A CD2 
2089 N N   . LYS A 264 ? 2.0214 0.9227 0.8671 -0.5391 -0.1934 0.0896  560 LYS A N   
2090 C CA  . LYS A 264 ? 1.9712 0.8585 0.8420 -0.4878 -0.1880 0.0885  560 LYS A CA  
2091 C C   . LYS A 264 ? 1.8204 0.8367 0.8327 -0.4701 -0.1784 0.0871  560 LYS A C   
2092 O O   . LYS A 264 ? 1.7221 0.8489 0.8127 -0.5045 -0.1751 0.0875  560 LYS A O   
2093 C CB  . LYS A 264 ? 1.9898 0.8641 0.8220 -0.5174 -0.1853 0.0978  560 LYS A CB  
2094 C CG  . LYS A 264 ? 1.9349 0.9441 0.8400 -0.5835 -0.1768 0.1077  560 LYS A CG  
2095 C CD  . LYS A 264 ? 1.9902 0.9856 0.8612 -0.6031 -0.1728 0.1158  560 LYS A CD  
2096 C CE  . LYS A 264 ? 2.0238 1.0782 0.8758 -0.6820 -0.1719 0.1238  560 LYS A CE  
2097 N NZ  . LYS A 264 ? 1.9124 0.9612 0.7385 -0.7002 -0.1669 0.1309  560 LYS A NZ  
2098 N N   . TRP A 265 ? 1.7659 0.7690 0.8070 -0.4140 -0.1747 0.0852  561 TRP A N   
2099 C CA  . TRP A 265 ? 1.6265 0.7734 0.8069 -0.3862 -0.1641 0.0799  561 TRP A CA  
2100 C C   . TRP A 265 ? 1.5833 0.7505 0.7880 -0.3396 -0.1569 0.0812  561 TRP A C   
2101 O O   . TRP A 265 ? 1.6685 0.7224 0.7774 -0.3231 -0.1622 0.0867  561 TRP A O   
2102 C CB  . TRP A 265 ? 1.4922 0.6671 0.7235 -0.3368 -0.1652 0.0657  561 TRP A CB  
2103 C CG  . TRP A 265 ? 1.3931 0.7325 0.7646 -0.3312 -0.1550 0.0604  561 TRP A CG  
2104 C CD1 . TRP A 265 ? 1.3269 0.7492 0.7882 -0.2746 -0.1461 0.0523  561 TRP A CD1 
2105 C CD2 . TRP A 265 ? 1.3886 0.8254 0.8174 -0.3845 -0.1534 0.0635  561 TRP A CD2 
2106 N NE1 . TRP A 265 ? 1.2242 0.7731 0.7864 -0.2869 -0.1391 0.0500  561 TRP A NE1 
2107 C CE2 . TRP A 265 ? 1.2508 0.8158 0.7979 -0.3497 -0.1434 0.0567  561 TRP A CE2 
2108 C CE3 . TRP A 265 ? 1.4334 0.8634 0.8211 -0.4589 -0.1603 0.0715  561 TRP A CE3 
2109 C CZ2 . TRP A 265 ? 1.1903 0.8725 0.8135 -0.3774 -0.1399 0.0576  561 TRP A CZ2 
2110 C CZ3 . TRP A 265 ? 1.3309 0.8954 0.8043 -0.4894 -0.1569 0.0724  561 TRP A CZ3 
2111 C CH2 . TRP A 265 ? 1.2026 0.8893 0.7915 -0.4439 -0.1468 0.0654  561 TRP A CH2 
2112 N N   . TYR A 266 ? 1.4362 0.7441 0.7622 -0.3202 -0.1455 0.0766  562 TYR A N   
2113 C CA  . TYR A 266 ? 1.4131 0.7527 0.7703 -0.2778 -0.1389 0.0763  562 TYR A CA  
2114 C C   . TYR A 266 ? 1.3759 0.7235 0.7678 -0.2018 -0.1396 0.0636  562 TYR A C   
2115 O O   . TYR A 266 ? 1.3169 0.6973 0.7518 -0.1849 -0.1398 0.0544  562 TYR A O   
2116 C CB  . TYR A 266 ? 1.3100 0.7887 0.7677 -0.2978 -0.1262 0.0774  562 TYR A CB  
2117 C CG  . TYR A 266 ? 1.2101 0.7986 0.7646 -0.3013 -0.1213 0.0695  562 TYR A CG  
2118 C CD1 . TYR A 266 ? 1.1592 0.8154 0.7954 -0.2490 -0.1164 0.0576  562 TYR A CD1 
2119 C CD2 . TYR A 266 ? 1.2390 0.8639 0.7983 -0.3585 -0.1224 0.0746  562 TYR A CD2 
2120 C CE1 . TYR A 266 ? 1.0989 0.8431 0.8126 -0.2501 -0.1126 0.0514  562 TYR A CE1 
2121 C CE2 . TYR A 266 ? 1.1471 0.8717 0.7903 -0.3559 -0.1192 0.0680  562 TYR A CE2 
2122 C CZ  . TYR A 266 ? 1.0712 0.8486 0.7881 -0.3000 -0.1142 0.0567  562 TYR A CZ  
2123 O OH  . TYR A 266 ? 1.0508 0.9149 0.8407 -0.2950 -0.1116 0.0511  562 TYR A OH  
2124 N N   . GLY A 267 ? 1.3751 0.6969 0.7457 -0.1571 -0.1403 0.0638  563 GLY A N   
2125 C CA  . GLY A 267 ? 1.3480 0.6808 0.7422 -0.0873 -0.1419 0.0528  563 GLY A CA  
2126 C C   . GLY A 267 ? 1.1983 0.6664 0.7161 -0.0691 -0.1325 0.0429  563 GLY A C   
2127 O O   . GLY A 267 ? 1.2123 0.7091 0.7648 -0.0305 -0.1324 0.0330  563 GLY A O   
2128 N N   . LEU A 268 ? 1.1043 0.6541 0.6841 -0.0985 -0.1240 0.0454  564 LEU A N   
2129 C CA  . LEU A 268 ? 1.0411 0.6990 0.7176 -0.0764 -0.1158 0.0366  564 LEU A CA  
2130 C C   . LEU A 268 ? 0.9801 0.7143 0.7295 -0.0996 -0.1093 0.0321  564 LEU A C   
2131 O O   . LEU A 268 ? 0.9737 0.7418 0.7381 -0.1407 -0.1047 0.0378  564 LEU A O   
2132 C CB  . LEU A 268 ? 0.9924 0.6835 0.6807 -0.0834 -0.1107 0.0409  564 LEU A CB  
2133 C CG  . LEU A 268 ? 0.9506 0.7328 0.7190 -0.0575 -0.1042 0.0310  564 LEU A CG  
2134 C CD1 . LEU A 268 ? 0.9930 0.7631 0.7489 -0.0078 -0.1107 0.0256  564 LEU A CD1 
2135 C CD2 . LEU A 268 ? 0.8652 0.6918 0.6536 -0.0785 -0.0964 0.0344  564 LEU A CD2 
2136 N N   . PRO A 269 ? 0.9347 0.7033 0.7295 -0.0736 -0.1086 0.0226  565 PRO A N   
2137 C CA  . PRO A 269 ? 0.8710 0.7107 0.7324 -0.0900 -0.1029 0.0188  565 PRO A CA  
2138 C C   . PRO A 269 ? 0.7799 0.6965 0.7061 -0.0773 -0.0946 0.0132  565 PRO A C   
2139 O O   . PRO A 269 ? 0.7548 0.6839 0.6970 -0.0457 -0.0944 0.0065  565 PRO A O   
2140 C CB  . PRO A 269 ? 0.8512 0.6760 0.7156 -0.0675 -0.1064 0.0120  565 PRO A CB  
2141 C CG  . PRO A 269 ? 0.8880 0.6837 0.7266 -0.0247 -0.1095 0.0080  565 PRO A CG  
2142 C CD  . PRO A 269 ? 0.9410 0.6863 0.7229 -0.0275 -0.1130 0.0156  565 PRO A CD  
2143 N N   . ALA A 270 ? 0.7041 0.6738 0.6635 -0.1008 -0.0879 0.0155  566 ALA A N   
2144 C CA  . ALA A 270 ? 0.7129 0.7364 0.7135 -0.0874 -0.0803 0.0102  566 ALA A CA  
2145 C C   . ALA A 270 ? 0.6865 0.7741 0.7351 -0.0968 -0.0733 0.0082  566 ALA A C   
2146 O O   . ALA A 270 ? 0.6942 0.8131 0.7441 -0.1205 -0.0690 0.0143  566 ALA A O   
2147 C CB  . ALA A 270 ? 0.7283 0.7389 0.6984 -0.0958 -0.0785 0.0159  566 ALA A CB  
2148 N N   . VAL A 271 ? 0.6638 0.7718 0.7471 -0.0773 -0.0722 0.0002  567 VAL A N   
2149 C CA  . VAL A 271 ? 0.6577 0.8160 0.7781 -0.0770 -0.0671 -0.0020 567 VAL A CA  
2150 C C   . VAL A 271 ? 0.6484 0.8439 0.7862 -0.0669 -0.0586 -0.0062 567 VAL A C   
2151 O O   . VAL A 271 ? 0.6637 0.8475 0.8016 -0.0510 -0.0573 -0.0132 567 VAL A O   
2152 C CB  . VAL A 271 ? 0.6539 0.8073 0.7934 -0.0599 -0.0692 -0.0083 567 VAL A CB  
2153 C CG1 . VAL A 271 ? 0.6162 0.8107 0.7854 -0.0486 -0.0637 -0.0120 567 VAL A CG1 
2154 C CG2 . VAL A 271 ? 0.6662 0.7936 0.7897 -0.0716 -0.0765 -0.0038 567 VAL A CG2 
2155 N N   . SER A 272 ? 0.6457 0.8908 0.7967 -0.0755 -0.0528 -0.0026 568 SER A N   
2156 C CA  . SER A 272 ? 0.6345 0.9160 0.7956 -0.0628 -0.0433 -0.0069 568 SER A CA  
2157 C C   . SER A 272 ? 0.6176 0.9436 0.8041 -0.0405 -0.0378 -0.0118 568 SER A C   
2158 O O   . SER A 272 ? 0.6349 0.9809 0.8230 -0.0216 -0.0298 -0.0179 568 SER A O   
2159 C CB  . SER A 272 ? 0.6422 0.9507 0.7884 -0.0875 -0.0386 0.0019  568 SER A CB  
2160 O OG  . SER A 272 ? 0.6585 1.0025 0.8080 -0.1141 -0.0401 0.0112  568 SER A OG  
2161 N N   . ASN A 273 ? 0.6120 0.9500 0.8125 -0.0387 -0.0422 -0.0098 569 ASN A N   
2162 C CA  . ASN A 273 ? 0.6136 0.9988 0.8327 -0.0142 -0.0381 -0.0123 569 ASN A CA  
2163 C C   . ASN A 273 ? 0.6175 0.9609 0.8334 0.0140  -0.0401 -0.0207 569 ASN A C   
2164 O O   . ASN A 273 ? 0.6405 1.0077 0.8626 0.0387  -0.0388 -0.0221 569 ASN A O   
2165 C CB  . ASN A 273 ? 0.6005 1.0386 0.8348 -0.0305 -0.0424 -0.0032 569 ASN A CB  
2166 C CG  . ASN A 273 ? 0.5757 0.9700 0.8038 -0.0467 -0.0533 -0.0003 569 ASN A CG  
2167 O OD1 . ASN A 273 ? 0.5606 0.8909 0.7756 -0.0431 -0.0564 -0.0048 569 ASN A OD1 
2168 N ND2 . ASN A 273 ? 0.6102 1.0445 0.8466 -0.0648 -0.0590 0.0069  569 ASN A ND2 
2169 N N   . MET A 274 ? 0.6210 0.9049 0.8236 0.0108  -0.0434 -0.0257 570 MET A N   
2170 C CA  . MET A 274 ? 0.6168 0.8594 0.8105 0.0283  -0.0451 -0.0326 570 MET A CA  
2171 C C   . MET A 274 ? 0.6820 0.8986 0.8556 0.0443  -0.0396 -0.0426 570 MET A C   
2172 O O   . MET A 274 ? 0.6528 0.8831 0.8222 0.0428  -0.0349 -0.0448 570 MET A O   
2173 C CB  . MET A 274 ? 0.6419 0.8460 0.8329 0.0122  -0.0519 -0.0318 570 MET A CB  
2174 C CG  . MET A 274 ? 0.6595 0.8760 0.8604 0.0000  -0.0580 -0.0236 570 MET A CG  
2175 S SD  . MET A 274 ? 0.5968 0.7697 0.7896 -0.0098 -0.0639 -0.0245 570 MET A SD  
2176 C CE  . MET A 274 ? 0.6606 0.8113 0.8484 0.0059  -0.0630 -0.0289 570 MET A CE  
2177 N N   . LEU A 275 ? 0.6960 0.8693 0.8502 0.0579  -0.0406 -0.0487 571 LEU A N   
2178 C CA  . LEU A 275 ? 0.7419 0.8754 0.8638 0.0711  -0.0368 -0.0591 571 LEU A CA  
2179 C C   . LEU A 275 ? 0.7554 0.8407 0.8618 0.0496  -0.0416 -0.0638 571 LEU A C   
2180 O O   . LEU A 275 ? 0.7320 0.7989 0.8395 0.0410  -0.0459 -0.0609 571 LEU A O   
2181 C CB  . LEU A 275 ? 0.7631 0.8777 0.8598 0.1055  -0.0341 -0.0624 571 LEU A CB  
2182 C CG  . LEU A 275 ? 0.8400 0.8977 0.8875 0.1223  -0.0302 -0.0743 571 LEU A CG  
2183 C CD1 . LEU A 275 ? 0.9137 0.9912 0.9452 0.1674  -0.0234 -0.0768 571 LEU A CD1 
2184 C CD2 . LEU A 275 ? 0.9364 0.9130 0.9426 0.1130  -0.0352 -0.0789 571 LEU A CD2 
2185 N N   . LEU A 276 ? 0.7316 0.8044 0.8240 0.0393  -0.0410 -0.0707 572 LEU A N   
2186 C CA  . LEU A 276 ? 0.7586 0.8006 0.8364 0.0158  -0.0458 -0.0758 572 LEU A CA  
2187 C C   . LEU A 276 ? 0.8466 0.8260 0.8741 0.0188  -0.0449 -0.0856 572 LEU A C   
2188 O O   . LEU A 276 ? 0.8818 0.8426 0.8818 0.0352  -0.0408 -0.0928 572 LEU A O   
2189 C CB  . LEU A 276 ? 0.7410 0.8086 0.8285 0.0013  -0.0479 -0.0774 572 LEU A CB  
2190 C CG  . LEU A 276 ? 0.7537 0.8066 0.8243 -0.0219 -0.0531 -0.0846 572 LEU A CG  
2191 C CD1 . LEU A 276 ? 0.7348 0.7900 0.8152 -0.0389 -0.0573 -0.0814 572 LEU A CD1 
2192 C CD2 . LEU A 276 ? 0.7104 0.7977 0.7921 -0.0278 -0.0561 -0.0846 572 LEU A CD2 
2193 N N   . GLU A 277 ? 0.8539 0.7958 0.8624 0.0017  -0.0486 -0.0860 573 GLU A N   
2194 C CA  . GLU A 277 ? 0.9490 0.8141 0.8960 -0.0032 -0.0491 -0.0941 573 GLU A CA  
2195 C C   . GLU A 277 ? 0.9696 0.8253 0.9015 -0.0455 -0.0541 -0.0994 573 GLU A C   
2196 O O   . GLU A 277 ? 0.9081 0.7979 0.8677 -0.0692 -0.0571 -0.0942 573 GLU A O   
2197 C CB  . GLU A 277 ? 1.0155 0.8380 0.9405 0.0060  -0.0497 -0.0891 573 GLU A CB  
2198 C CG  . GLU A 277 ? 1.1855 0.9520 1.0615 0.0452  -0.0465 -0.0928 573 GLU A CG  
2199 C CD  . GLU A 277 ? 1.3167 0.9969 1.1315 0.0423  -0.0493 -0.0925 573 GLU A CD  
2200 O OE1 . GLU A 277 ? 1.3110 0.9270 1.0734 0.0091  -0.0519 -0.0988 573 GLU A OE1 
2201 O OE2 . GLU A 277 ? 1.4243 1.1013 1.2400 0.0701  -0.0495 -0.0852 573 GLU A OE2 
2202 N N   . ILE A 278 ? 1.0235 0.8375 0.9095 -0.0547 -0.0550 -0.1102 574 ILE A N   
2203 C CA  . ILE A 278 ? 1.0356 0.8447 0.9010 -0.0994 -0.0610 -0.1164 574 ILE A CA  
2204 C C   . ILE A 278 ? 1.1312 0.8390 0.9102 -0.1109 -0.0622 -0.1270 574 ILE A C   
2205 O O   . ILE A 278 ? 1.1963 0.8627 0.9394 -0.0833 -0.0591 -0.1347 574 ILE A O   
2206 C CB  . ILE A 278 ? 0.9631 0.8346 0.8598 -0.1059 -0.0638 -0.1194 574 ILE A CB  
2207 C CG1 . ILE A 278 ? 0.9063 0.8596 0.8732 -0.0910 -0.0630 -0.1088 574 ILE A CG1 
2208 C CG2 . ILE A 278 ? 0.9709 0.8515 0.8495 -0.1534 -0.0715 -0.1251 574 ILE A CG2 
2209 C CD1 . ILE A 278 ? 0.8476 0.8524 0.8381 -0.0888 -0.0657 -0.1097 574 ILE A CD1 
2210 N N   . GLY A 279 ? 1.1332 0.7985 0.8727 -0.1526 -0.0665 -0.1274 575 GLY A N   
2211 C CA  . GLY A 279 ? 1.2738 0.8235 0.9156 -0.1712 -0.0689 -0.1362 575 GLY A CA  
2212 C C   . GLY A 279 ? 1.3425 0.8109 0.9322 -0.1175 -0.0639 -0.1406 575 GLY A C   
2213 O O   . GLY A 279 ? 1.4067 0.8066 0.9308 -0.1113 -0.0644 -0.1526 575 GLY A O   
2214 N N   . GLY A 280 ? 1.2898 0.7725 0.9087 -0.0750 -0.0591 -0.1315 576 GLY A N   
2215 C CA  . GLY A 280 ? 1.3679 0.7915 0.9429 -0.0170 -0.0543 -0.1345 576 GLY A CA  
2216 C C   . GLY A 280 ? 1.3312 0.8130 0.9425 0.0255  -0.0482 -0.1386 576 GLY A C   
2217 O O   . GLY A 280 ? 1.3471 0.8092 0.9373 0.0801  -0.0428 -0.1397 576 GLY A O   
2218 N N   . LEU A 281 ? 1.2445 0.8010 0.9069 0.0039  -0.0486 -0.1403 577 LEU A N   
2219 C CA  . LEU A 281 ? 1.1880 0.8033 0.8845 0.0384  -0.0421 -0.1425 577 LEU A CA  
2220 C C   . LEU A 281 ? 1.1106 0.8246 0.8926 0.0575  -0.0384 -0.1291 577 LEU A C   
2221 O O   . LEU A 281 ? 1.0364 0.7977 0.8686 0.0307  -0.0425 -0.1201 577 LEU A O   
2222 C CB  . LEU A 281 ? 1.2024 0.8471 0.9077 0.0065  -0.0454 -0.1494 577 LEU A CB  
2223 C CG  . LEU A 281 ? 1.2725 0.8255 0.8905 -0.0167 -0.0499 -0.1643 577 LEU A CG  
2224 C CD1 . LEU A 281 ? 1.2556 0.8580 0.8930 -0.0415 -0.0534 -0.1699 577 LEU A CD1 
2225 C CD2 . LEU A 281 ? 1.3544 0.8192 0.8944 0.0308  -0.0437 -0.1740 577 LEU A CD2 
2226 N N   . GLU A 282 ? 1.0837 0.8302 0.8780 0.1031  -0.0307 -0.1280 578 GLU A N   
2227 C CA  . GLU A 282 ? 0.9862 0.8194 0.8498 0.1189  -0.0277 -0.1154 578 GLU A CA  
2228 C C   . GLU A 282 ? 0.9276 0.8400 0.8373 0.1170  -0.0230 -0.1131 578 GLU A C   
2229 O O   . GLU A 282 ? 0.9559 0.8720 0.8442 0.1405  -0.0160 -0.1201 578 GLU A O   
2230 C CB  . GLU A 282 ? 1.0406 0.8671 0.8865 0.1691  -0.0232 -0.1134 578 GLU A CB  
2231 C CG  . GLU A 282 ? 1.1388 0.8848 0.9375 0.1723  -0.0287 -0.1126 578 GLU A CG  
2232 C CD  . GLU A 282 ? 1.1958 0.9481 0.9841 0.2257  -0.0262 -0.1082 578 GLU A CD  
2233 O OE1 . GLU A 282 ? 1.1810 0.9475 0.9499 0.2720  -0.0192 -0.1136 578 GLU A OE1 
2234 O OE2 . GLU A 282 ? 1.2809 1.0286 1.0790 0.2234  -0.0314 -0.0993 578 GLU A OE2 
2235 N N   . PHE A 283 ? 0.8514 0.8213 0.8171 0.0904  -0.0266 -0.1033 579 PHE A N   
2236 C CA  . PHE A 283 ? 0.8315 0.8663 0.8344 0.0826  -0.0238 -0.0986 579 PHE A CA  
2237 C C   . PHE A 283 ? 0.7426 0.8428 0.7904 0.0919  -0.0208 -0.0862 579 PHE A C   
2238 O O   . PHE A 283 ? 0.7689 0.8892 0.8482 0.0723  -0.0263 -0.0773 579 PHE A O   
2239 C CB  . PHE A 283 ? 0.7977 0.8366 0.8149 0.0465  -0.0317 -0.0974 579 PHE A CB  
2240 C CG  . PHE A 283 ? 0.8475 0.8399 0.8225 0.0320  -0.0352 -0.1095 579 PHE A CG  
2241 C CD1 . PHE A 283 ? 0.8521 0.8468 0.8069 0.0380  -0.0316 -0.1165 579 PHE A CD1 
2242 C CD2 . PHE A 283 ? 0.8664 0.8139 0.8176 0.0092  -0.0421 -0.1140 579 PHE A CD2 
2243 C CE1 . PHE A 283 ? 0.9108 0.8617 0.8218 0.0214  -0.0362 -0.1284 579 PHE A CE1 
2244 C CE2 . PHE A 283 ? 0.9106 0.8169 0.8177 -0.0118 -0.0465 -0.1254 579 PHE A CE2 
2245 C CZ  . PHE A 283 ? 0.9678 0.8745 0.8543 -0.0052 -0.0443 -0.1331 579 PHE A CZ  
2246 N N   . SER A 284 ? 0.7652 0.9015 0.8122 0.1216  -0.0121 -0.0862 580 SER A N   
2247 C CA  . SER A 284 ? 0.7467 0.9528 0.8317 0.1293  -0.0095 -0.0751 580 SER A CA  
2248 C C   . SER A 284 ? 0.7061 0.9655 0.8259 0.0982  -0.0099 -0.0648 580 SER A C   
2249 O O   . SER A 284 ? 0.7025 1.0130 0.8512 0.0905  -0.0106 -0.0544 580 SER A O   
2250 C CB  . SER A 284 ? 0.8023 1.0461 0.8755 0.1709  0.0007  -0.0786 580 SER A CB  
2251 O OG  . SER A 284 ? 0.7962 1.0392 0.8475 0.1766  0.0084  -0.0864 580 SER A OG  
2252 N N   . ALA A 285 ? 0.7056 0.9513 0.8167 0.0797  -0.0103 -0.0670 581 ALA A N   
2253 C CA  . ALA A 285 ? 0.6411 0.9183 0.7706 0.0515  -0.0118 -0.0567 581 ALA A CA  
2254 C C   . ALA A 285 ? 0.6389 0.8709 0.7600 0.0323  -0.0211 -0.0585 581 ALA A C   
2255 O O   . ALA A 285 ? 0.6696 0.8759 0.7690 0.0337  -0.0214 -0.0671 581 ALA A O   
2256 C CB  . ALA A 285 ? 0.6691 0.9882 0.7924 0.0534  -0.0018 -0.0556 581 ALA A CB  
2257 N N   . CYS A 286 ? 0.6157 0.8412 0.7515 0.0162  -0.0288 -0.0512 582 CYS A N   
2258 C CA  . CYS A 286 ? 0.6072 0.8015 0.7363 0.0048  -0.0373 -0.0533 582 CYS A CA  
2259 C C   . CYS A 286 ? 0.6167 0.8119 0.7531 -0.0098 -0.0437 -0.0428 582 CYS A C   
2260 O O   . CYS A 286 ? 0.6435 0.8215 0.7843 -0.0120 -0.0502 -0.0429 582 CYS A O   
2261 C CB  . CYS A 286 ? 0.6629 0.8267 0.7883 0.0090  -0.0408 -0.0611 582 CYS A CB  
2262 S SG  . CYS A 286 ? 0.6325 0.7977 0.7754 0.0138  -0.0419 -0.0555 582 CYS A SG  
2263 N N   . PRO A 287 ? 0.6082 0.8177 0.7383 -0.0207 -0.0420 -0.0337 583 PRO A N   
2264 C CA  . PRO A 287 ? 0.6065 0.8002 0.7293 -0.0349 -0.0486 -0.0237 583 PRO A CA  
2265 C C   . PRO A 287 ? 0.6318 0.7942 0.7436 -0.0292 -0.0574 -0.0258 583 PRO A C   
2266 O O   . PRO A 287 ? 0.6305 0.7891 0.7318 -0.0229 -0.0595 -0.0301 583 PRO A O   
2267 C CB  . PRO A 287 ? 0.6177 0.8198 0.7201 -0.0512 -0.0452 -0.0147 583 PRO A CB  
2268 C CG  . PRO A 287 ? 0.6486 0.8662 0.7472 -0.0416 -0.0388 -0.0212 583 PRO A CG  
2269 C CD  . PRO A 287 ? 0.6420 0.8738 0.7611 -0.0228 -0.0344 -0.0323 583 PRO A CD  
2270 N N   . PHE A 288 ? 0.6053 0.7512 0.7188 -0.0296 -0.0628 -0.0231 584 PHE A N   
2271 C CA  . PHE A 288 ? 0.6227 0.7503 0.7271 -0.0188 -0.0703 -0.0251 584 PHE A CA  
2272 C C   . PHE A 288 ? 0.6746 0.7680 0.7532 -0.0210 -0.0760 -0.0170 584 PHE A C   
2273 O O   . PHE A 288 ? 0.6570 0.7435 0.7349 -0.0347 -0.0752 -0.0120 584 PHE A O   
2274 C CB  . PHE A 288 ? 0.6364 0.7769 0.7643 -0.0124 -0.0702 -0.0334 584 PHE A CB  
2275 C CG  . PHE A 288 ? 0.6605 0.7996 0.8027 -0.0167 -0.0682 -0.0318 584 PHE A CG  
2276 C CD1 . PHE A 288 ? 0.6415 0.7638 0.7767 -0.0164 -0.0724 -0.0274 584 PHE A CD1 
2277 C CD2 . PHE A 288 ? 0.6539 0.8053 0.8106 -0.0172 -0.0626 -0.0352 584 PHE A CD2 
2278 C CE1 . PHE A 288 ? 0.6438 0.7664 0.7903 -0.0207 -0.0717 -0.0260 584 PHE A CE1 
2279 C CE2 . PHE A 288 ? 0.5881 0.7402 0.7552 -0.0175 -0.0621 -0.0331 584 PHE A CE2 
2280 C CZ  . PHE A 288 ? 0.6300 0.7699 0.7940 -0.0213 -0.0669 -0.0283 584 PHE A CZ  
2281 N N   . SER A 289 ? 0.6515 0.7222 0.7035 -0.0060 -0.0826 -0.0160 585 SER A N   
2282 C CA  . SER A 289 ? 0.7194 0.7395 0.7286 -0.0034 -0.0887 -0.0087 585 SER A CA  
2283 C C   . SER A 289 ? 0.7282 0.7405 0.7253 0.0264  -0.0949 -0.0124 585 SER A C   
2284 O O   . SER A 289 ? 0.6642 0.7125 0.6775 0.0432  -0.0961 -0.0181 585 SER A O   
2285 C CB  . SER A 289 ? 0.7162 0.6977 0.6783 -0.0132 -0.0909 0.0004  585 SER A CB  
2286 O OG  . SER A 289 ? 0.7855 0.7757 0.7384 0.0033  -0.0930 -0.0012 585 SER A OG  
2287 N N   . GLY A 290 ? 0.7258 0.6944 0.6916 0.0325  -0.0988 -0.0094 586 GLY A N   
2288 C CA  . GLY A 290 ? 0.7642 0.7194 0.7046 0.0679  -0.1044 -0.0119 586 GLY A CA  
2289 C C   . GLY A 290 ? 0.8735 0.7429 0.7383 0.0776  -0.1114 -0.0050 586 GLY A C   
2290 O O   . GLY A 290 ? 0.8560 0.6808 0.6775 0.0695  -0.1146 0.0023  586 GLY A O   
2291 N N   . TRP A 291 ? 0.8664 0.7050 0.7068 0.0944  -0.1138 -0.0071 587 TRP A N   
2292 C CA  . TRP A 291 ? 0.9785 0.7179 0.7363 0.0969  -0.1206 -0.0014 587 TRP A CA  
2293 C C   . TRP A 291 ? 0.9553 0.6781 0.7152 0.0799  -0.1194 -0.0036 587 TRP A C   
2294 O O   . TRP A 291 ? 0.8452 0.6327 0.6670 0.0760  -0.1136 -0.0093 587 TRP A O   
2295 C CB  . TRP A 291 ? 1.0690 0.7663 0.7665 0.1503  -0.1275 -0.0025 587 TRP A CB  
2296 C CG  . TRP A 291 ? 1.0252 0.7917 0.7619 0.1895  -0.1248 -0.0116 587 TRP A CG  
2297 C CD1 . TRP A 291 ? 1.0370 0.8019 0.7716 0.2039  -0.1227 -0.0170 587 TRP A CD1 
2298 C CD2 . TRP A 291 ? 0.9972 0.8518 0.7792 0.2162  -0.1237 -0.0161 587 TRP A CD2 
2299 N NE1 . TRP A 291 ? 1.0019 0.8528 0.7790 0.2378  -0.1191 -0.0241 587 TRP A NE1 
2300 C CE2 . TRP A 291 ? 1.0124 0.9214 0.8194 0.2440  -0.1203 -0.0236 587 TRP A CE2 
2301 C CE3 . TRP A 291 ? 0.9723 0.8679 0.7737 0.2170  -0.1257 -0.0145 587 TRP A CE3 
2302 C CZ2 . TRP A 291 ? 1.0065 1.0166 0.8597 0.2678  -0.1189 -0.0290 587 TRP A CZ2 
2303 C CZ3 . TRP A 291 ? 0.9481 0.9376 0.7927 0.2422  -0.1256 -0.0206 587 TRP A CZ3 
2304 C CH2 . TRP A 291 ? 0.9833 1.0323 0.8542 0.2652  -0.1223 -0.0275 587 TRP A CH2 
2305 N N   . TYR A 292 ? 0.9978 0.6279 0.6831 0.0666  -0.1256 0.0013  588 TYR A N   
2306 C CA  . TYR A 292 ? 1.0518 0.6622 0.7332 0.0406  -0.1262 0.0002  588 TYR A CA  
2307 C C   . TYR A 292 ? 1.0740 0.6625 0.7312 0.0804  -0.1274 -0.0075 588 TYR A C   
2308 O O   . TYR A 292 ? 1.1076 0.6444 0.7047 0.1242  -0.1316 -0.0093 588 TYR A O   
2309 C CB  . TYR A 292 ? 1.0888 0.6093 0.6950 -0.0010 -0.1333 0.0087  588 TYR A CB  
2310 C CG  . TYR A 292 ? 1.0925 0.6587 0.7393 -0.0587 -0.1304 0.0152  588 TYR A CG  
2311 C CD1 . TYR A 292 ? 1.0369 0.6725 0.7491 -0.0791 -0.1266 0.0123  588 TYR A CD1 
2312 C CD2 . TYR A 292 ? 1.1142 0.6543 0.7276 -0.0914 -0.1316 0.0248  588 TYR A CD2 
2313 C CE1 . TYR A 292 ? 1.0298 0.7161 0.7765 -0.1251 -0.1244 0.0182  588 TYR A CE1 
2314 C CE2 . TYR A 292 ? 1.0876 0.6809 0.7364 -0.1421 -0.1281 0.0307  588 TYR A CE2 
2315 C CZ  . TYR A 292 ? 1.0382 0.7085 0.7552 -0.1561 -0.1245 0.0271  588 TYR A CZ  
2316 O OH  . TYR A 292 ? 1.0361 0.7700 0.7879 -0.1997 -0.1212 0.0331  588 TYR A OH  
2317 N N   . MET A 293 ? 1.0284 0.6580 0.7295 0.0685  -0.1236 -0.0119 589 MET A N   
2318 C CA  . MET A 293 ? 1.0888 0.6734 0.7474 0.0890  -0.1258 -0.0174 589 MET A CA  
2319 C C   . MET A 293 ? 1.1038 0.5930 0.6893 0.0516  -0.1345 -0.0130 589 MET A C   
2320 O O   . MET A 293 ? 1.0952 0.6037 0.7059 0.0010  -0.1356 -0.0074 589 MET A O   
2321 C CB  . MET A 293 ? 0.9762 0.6408 0.7063 0.0884  -0.1184 -0.0230 589 MET A CB  
2322 C CG  . MET A 293 ? 1.0366 0.6657 0.7260 0.1154  -0.1187 -0.0296 589 MET A CG  
2323 S SD  . MET A 293 ? 0.9238 0.6538 0.6963 0.1174  -0.1084 -0.0347 589 MET A SD  
2324 C CE  . MET A 293 ? 0.9143 0.6453 0.7130 0.0606  -0.1119 -0.0297 589 MET A CE  
2325 N N   . GLY A 294 ? 1.1709 0.5586 0.6613 0.0774  -0.1409 -0.0159 590 GLY A N   
2326 C CA  . GLY A 294 ? 1.2432 0.5174 0.6404 0.0394  -0.1513 -0.0115 590 GLY A CA  
2327 C C   . GLY A 294 ? 1.2751 0.5767 0.7034 -0.0176 -0.1533 -0.0098 590 GLY A C   
2328 O O   . GLY A 294 ? 1.3070 0.5706 0.7010 -0.0725 -0.1600 -0.0023 590 GLY A O   
2329 N N   . THR A 295 ? 1.1896 0.5606 0.6801 -0.0064 -0.1479 -0.0161 591 THR A N   
2330 C CA  . THR A 295 ? 1.2362 0.6274 0.7460 -0.0528 -0.1518 -0.0150 591 THR A CA  
2331 C C   . THR A 295 ? 1.1701 0.6397 0.7471 -0.1009 -0.1507 -0.0065 591 THR A C   
2332 O O   . THR A 295 ? 1.1355 0.6056 0.7038 -0.1501 -0.1577 -0.0024 591 THR A O   
2333 C CB  . THR A 295 ? 1.0821 0.5326 0.6438 -0.0270 -0.1455 -0.0224 591 THR A CB  
2334 O OG1 . THR A 295 ? 1.0419 0.5937 0.6943 -0.0039 -0.1345 -0.0229 591 THR A OG1 
2335 C CG2 . THR A 295 ? 1.1924 0.5692 0.6818 0.0197  -0.1460 -0.0310 591 THR A CG2 
2336 N N   . GLU A 296 ? 1.0440 0.5845 0.6859 -0.0870 -0.1424 -0.0044 592 GLU A N   
2337 C CA  . GLU A 296 ? 1.0235 0.6383 0.7240 -0.1255 -0.1401 0.0026  592 GLU A CA  
2338 C C   . GLU A 296 ? 1.0724 0.6353 0.7121 -0.1783 -0.1485 0.0111  592 GLU A C   
2339 O O   . GLU A 296 ? 1.0659 0.6817 0.7340 -0.2223 -0.1508 0.0163  592 GLU A O   
2340 C CB  . GLU A 296 ? 0.9710 0.6442 0.7262 -0.1021 -0.1310 0.0030  592 GLU A CB  
2341 C CG  . GLU A 296 ? 0.9323 0.6676 0.7505 -0.0621 -0.1227 -0.0044 592 GLU A CG  
2342 C CD  . GLU A 296 ? 0.9037 0.6868 0.7634 -0.0450 -0.1157 -0.0045 592 GLU A CD  
2343 O OE1 . GLU A 296 ? 0.8240 0.6677 0.7352 -0.0633 -0.1114 -0.0019 592 GLU A OE1 
2344 O OE2 . GLU A 296 ? 0.9342 0.6951 0.7713 -0.0115 -0.1151 -0.0075 592 GLU A OE2 
2345 N N   . ILE A 297 ? 1.1457 0.6054 0.6962 -0.1752 -0.1536 0.0131  593 ILE A N   
2346 C CA  . ILE A 297 ? 1.2423 0.6366 0.7187 -0.2316 -0.1619 0.0222  593 ILE A CA  
2347 C C   . ILE A 297 ? 1.3218 0.6322 0.7189 -0.2617 -0.1737 0.0204  593 ILE A C   
2348 O O   . ILE A 297 ? 1.3625 0.6814 0.7435 -0.3249 -0.1805 0.0267  593 ILE A O   
2349 C CB  . ILE A 297 ? 1.3113 0.6175 0.7135 -0.2161 -0.1630 0.0265  593 ILE A CB  
2350 C CG1 . ILE A 297 ? 1.2636 0.6478 0.7380 -0.1830 -0.1525 0.0270  593 ILE A CG1 
2351 C CG2 . ILE A 297 ? 1.3855 0.6281 0.7113 -0.2826 -0.1704 0.0376  593 ILE A CG2 
2352 C CD1 . ILE A 297 ? 1.3289 0.6260 0.7291 -0.1525 -0.1548 0.0299  593 ILE A CD1 
2353 N N   . GLY A 298 ? 1.4029 0.6362 0.7479 -0.2168 -0.1762 0.0114  594 GLY A N   
2354 C CA  . GLY A 298 ? 1.5006 0.6225 0.7433 -0.2404 -0.1882 0.0085  594 GLY A CA  
2355 C C   . GLY A 298 ? 1.4485 0.6261 0.7318 -0.2642 -0.1918 0.0046  594 GLY A C   
2356 O O   . GLY A 298 ? 1.4703 0.5771 0.6781 -0.3087 -0.2037 0.0047  594 GLY A O   
2357 N N   . VAL A 299 ? 1.3582 0.6569 0.7529 -0.2375 -0.1825 0.0014  595 VAL A N   
2358 C CA  . VAL A 299 ? 1.3014 0.6560 0.7362 -0.2533 -0.1859 -0.0016 595 VAL A CA  
2359 C C   . VAL A 299 ? 1.2435 0.7208 0.7648 -0.2941 -0.1849 0.0066  595 VAL A C   
2360 O O   . VAL A 299 ? 1.2572 0.7507 0.7642 -0.3490 -0.1949 0.0111  595 VAL A O   
2361 C CB  . VAL A 299 ? 1.2674 0.6587 0.7507 -0.1925 -0.1768 -0.0108 595 VAL A CB  
2362 C CG1 . VAL A 299 ? 1.1745 0.6069 0.6834 -0.2086 -0.1817 -0.0135 595 VAL A CG1 
2363 C CG2 . VAL A 299 ? 1.2759 0.5645 0.6796 -0.1425 -0.1756 -0.0191 595 VAL A CG2 
2364 N N   . ARG A 300 ? 1.1325 0.6985 0.7395 -0.2672 -0.1731 0.0084  596 ARG A N   
2365 C CA  . ARG A 300 ? 1.0859 0.7712 0.7748 -0.2925 -0.1706 0.0148  596 ARG A CA  
2366 C C   . ARG A 300 ? 1.1335 0.8269 0.7990 -0.3469 -0.1741 0.0246  596 ARG A C   
2367 O O   . ARG A 300 ? 1.1167 0.8616 0.7886 -0.3970 -0.1815 0.0303  596 ARG A O   
2368 C CB  . ARG A 300 ? 0.9992 0.7608 0.7732 -0.2450 -0.1570 0.0123  596 ARG A CB  
2369 C CG  . ARG A 300 ? 0.9606 0.7156 0.7525 -0.1985 -0.1528 0.0038  596 ARG A CG  
2370 C CD  . ARG A 300 ? 0.9702 0.7444 0.7659 -0.2137 -0.1606 0.0028  596 ARG A CD  
2371 N NE  . ARG A 300 ? 0.9029 0.7718 0.7540 -0.2402 -0.1631 0.0094  596 ARG A NE  
2372 C CZ  . ARG A 300 ? 0.8272 0.7780 0.7513 -0.2167 -0.1548 0.0105  596 ARG A CZ  
2373 N NH1 . ARG A 300 ? 0.7922 0.7419 0.7438 -0.1749 -0.1441 0.0056  596 ARG A NH1 
2374 N NH2 . ARG A 300 ? 0.7932 0.8289 0.7586 -0.2359 -0.1575 0.0164  596 ARG A NH2 
2375 N N   . ASP A 301 ? 1.1615 0.8120 0.8001 -0.3389 -0.1688 0.0273  597 ASP A N   
2376 C CA  . ASP A 301 ? 1.1709 0.8370 0.7916 -0.3898 -0.1694 0.0377  597 ASP A CA  
2377 C C   . ASP A 301 ? 1.2541 0.8457 0.7818 -0.4561 -0.1833 0.0429  597 ASP A C   
2378 O O   . ASP A 301 ? 1.2672 0.9335 0.8108 -0.5002 -0.1816 0.0526  597 ASP A O   
2379 C CB  . ASP A 301 ? 1.1593 0.7766 0.7560 -0.3648 -0.1621 0.0394  597 ASP A CB  
2380 C CG  . ASP A 301 ? 1.1138 0.8271 0.8054 -0.3211 -0.1487 0.0369  597 ASP A CG  
2381 O OD1 . ASP A 301 ? 1.0665 0.8912 0.8351 -0.3284 -0.1439 0.0382  597 ASP A OD1 
2382 O OD2 . ASP A 301 ? 1.1022 0.7787 0.7868 -0.2785 -0.1436 0.0334  597 ASP A OD2 
2383 N N   . TYR A 302 ? 1.3116 0.7703 0.7451 -0.4458 -0.1908 0.0380  598 TYR A N   
2384 C CA  . TYR A 302 ? 1.3814 0.7727 0.7222 -0.4847 -0.1956 0.0460  598 TYR A CA  
2385 C C   . TYR A 302 ? 1.4479 0.8784 0.7984 -0.5054 -0.2014 0.0453  598 TYR A C   
2386 O O   . TYR A 302 ? 1.4933 0.9173 0.7937 -0.5526 -0.2049 0.0548  598 TYR A O   
2387 C CB  . TYR A 302 ? 1.5301 0.7609 0.7571 -0.4547 -0.1997 0.0421  598 TYR A CB  
2388 C CG  . TYR A 302 ? 1.5899 0.7642 0.7703 -0.4515 -0.1962 0.0482  598 TYR A CG  
2389 C CD1 . TYR A 302 ? 1.5777 0.8347 0.8036 -0.4881 -0.1901 0.0583  598 TYR A CD1 
2390 C CD2 . TYR A 302 ? 1.7099 0.7503 0.7958 -0.4087 -0.1990 0.0442  598 TYR A CD2 
2391 C CE1 . TYR A 302 ? 1.6437 0.8445 0.8203 -0.4874 -0.1874 0.0645  598 TYR A CE1 
2392 C CE2 . TYR A 302 ? 1.7567 0.7426 0.7932 -0.4036 -0.1970 0.0504  598 TYR A CE2 
2393 C CZ  . TYR A 302 ? 1.7422 0.8050 0.8236 -0.4456 -0.1916 0.0606  598 TYR A CZ  
2394 O OH  . TYR A 302 ? 1.7831 0.7891 0.8121 -0.4411 -0.1900 0.0666  598 TYR A OH  
2395 N N   . CYS A 303 ? 1.3409 0.8107 0.7495 -0.4735 -0.2034 0.0348  599 CYS A N   
2396 C CA  . CYS A 303 ? 1.4160 0.8885 0.8104 -0.4858 -0.2104 0.0328  599 CYS A CA  
2397 C C   . CYS A 303 ? 1.3131 0.9249 0.8103 -0.4872 -0.2109 0.0321  599 CYS A C   
2398 O O   . CYS A 303 ? 1.3578 0.9859 0.8444 -0.5059 -0.2170 0.0332  599 CYS A O   
2399 C CB  . CYS A 303 ? 1.4355 0.7912 0.7664 -0.4430 -0.2148 0.0203  599 CYS A CB  
2400 S SG  . CYS A 303 ? 1.6126 0.7937 0.7945 -0.4392 -0.2169 0.0232  599 CYS A SG  
2401 N N   . ASP A 304 ? 1.1979 0.9090 0.7884 -0.4669 -0.2050 0.0311  600 ASP A N   
2402 C CA  . ASP A 304 ? 1.1833 1.0317 0.8627 -0.4673 -0.2049 0.0337  600 ASP A CA  
2403 C C   . ASP A 304 ? 1.2083 1.1149 0.8767 -0.5154 -0.2049 0.0455  600 ASP A C   
2404 O O   . ASP A 304 ? 1.2774 1.1623 0.9028 -0.5491 -0.2010 0.0540  600 ASP A O   
2405 C CB  . ASP A 304 ? 1.0986 1.0450 0.8683 -0.4411 -0.1968 0.0341  600 ASP A CB  
2406 C CG  . ASP A 304 ? 1.0385 0.9773 0.8509 -0.3701 -0.1865 0.0261  600 ASP A CG  
2407 O OD1 . ASP A 304 ? 1.0358 0.8915 0.8057 -0.3484 -0.1887 0.0188  600 ASP A OD1 
2408 O OD2 . ASP A 304 ? 0.9461 0.9620 0.8304 -0.3372 -0.1756 0.0269  600 ASP A OD2 
2409 N N   . ASN A 305 ? 1.2360 1.2148 0.9373 -0.5197 -0.2100 0.0463  601 ASN A N   
2410 C CA  . ASN A 305 ? 1.2398 1.2866 0.9341 -0.5645 -0.2106 0.0572  601 ASN A CA  
2411 C C   . ASN A 305 ? 1.1508 1.3105 0.9024 -0.5706 -0.1998 0.0653  601 ASN A C   
2412 O O   . ASN A 305 ? 1.1485 1.3453 0.8749 -0.6148 -0.1978 0.0756  601 ASN A O   
2413 C CB  . ASN A 305 ? 1.1852 1.2964 0.9104 -0.5604 -0.2187 0.0559  601 ASN A CB  
2414 C CG  . ASN A 305 ? 1.3290 1.3336 0.9754 -0.5764 -0.2293 0.0518  601 ASN A CG  
2415 O OD1 . ASN A 305 ? 1.4188 1.3234 0.9770 -0.6093 -0.2309 0.0551  601 ASN A OD1 
2416 N ND2 . ASN A 305 ? 1.3216 1.3431 0.9924 -0.5520 -0.2369 0.0450  601 ASN A ND2 
2417 N N   . SER A 306 ? 1.0960 1.3111 0.9199 -0.5269 -0.1927 0.0609  602 SER A N   
2418 C CA  . SER A 306 ? 0.9893 1.3127 0.8721 -0.5199 -0.1811 0.0664  602 SER A CA  
2419 C C   . SER A 306 ? 1.0557 1.3271 0.9130 -0.5279 -0.1732 0.0682  602 SER A C   
2420 O O   . SER A 306 ? 1.0099 1.3608 0.9143 -0.5168 -0.1626 0.0712  602 SER A O   
2421 C CB  . SER A 306 ? 0.9647 1.3737 0.9341 -0.4635 -0.1781 0.0608  602 SER A CB  
2422 O OG  . SER A 306 ? 1.0311 1.4814 1.0192 -0.4523 -0.1868 0.0594  602 SER A OG  
2423 N N   . ARG A 307 ? 1.1799 1.3166 0.9593 -0.5427 -0.1782 0.0661  603 ARG A N   
2424 C CA  . ARG A 307 ? 1.1767 1.2477 0.9184 -0.5498 -0.1726 0.0682  603 ARG A CA  
2425 C C   . ARG A 307 ? 1.2580 1.2426 0.8973 -0.6018 -0.1767 0.0767  603 ARG A C   
2426 O O   . ARG A 307 ? 1.2652 1.2993 0.8891 -0.6412 -0.1787 0.0846  603 ARG A O   
2427 C CB  . ARG A 307 ? 1.1544 1.1356 0.8898 -0.5089 -0.1752 0.0574  603 ARG A CB  
2428 C CG  . ARG A 307 ? 1.0643 1.1271 0.8929 -0.4615 -0.1725 0.0501  603 ARG A CG  
2429 C CD  . ARG A 307 ? 1.0145 1.1849 0.9114 -0.4506 -0.1603 0.0543  603 ARG A CD  
2430 N NE  . ARG A 307 ? 0.9954 1.1096 0.8596 -0.4578 -0.1545 0.0566  603 ARG A NE  
2431 C CZ  . ARG A 307 ? 1.0098 1.0527 0.8664 -0.4095 -0.1478 0.0503  603 ARG A CZ  
2432 N NH1 . ARG A 307 ? 0.8907 0.9192 0.7755 -0.3575 -0.1460 0.0413  603 ARG A NH1 
2433 N NH2 . ARG A 307 ? 1.0571 1.0466 0.8753 -0.4153 -0.1429 0.0538  603 ARG A NH2 
2434 N N   . TYR A 308 ? 1.2650 1.1187 0.8273 -0.6017 -0.1788 0.0755  604 TYR A N   
2435 C CA  . TYR A 308 ? 1.3470 1.1102 0.8003 -0.6493 -0.1832 0.0844  604 TYR A CA  
2436 C C   . TYR A 308 ? 1.4650 1.1790 0.8581 -0.6737 -0.1937 0.0850  604 TYR A C   
2437 O O   . TYR A 308 ? 1.4773 1.1774 0.8044 -0.7265 -0.1972 0.0950  604 TYR A O   
2438 C CB  . TYR A 308 ? 1.4379 1.0617 0.8141 -0.6326 -0.1844 0.0822  604 TYR A CB  
2439 C CG  . TYR A 308 ? 1.4626 1.1269 0.8624 -0.6379 -0.1749 0.0879  604 TYR A CG  
2440 C CD1 . TYR A 308 ? 1.3881 1.1260 0.8809 -0.5993 -0.1667 0.0826  604 TYR A CD1 
2441 C CD2 . TYR A 308 ? 1.5892 1.2201 0.9149 -0.6840 -0.1747 0.0987  604 TYR A CD2 
2442 C CE1 . TYR A 308 ? 1.3379 1.1144 0.8510 -0.6045 -0.1574 0.0882  604 TYR A CE1 
2443 C CE2 . TYR A 308 ? 1.5443 1.2147 0.8906 -0.6896 -0.1657 0.1039  604 TYR A CE2 
2444 C CZ  . TYR A 308 ? 1.4159 1.1599 0.8573 -0.6490 -0.1566 0.0988  604 TYR A CZ  
2445 O OH  . TYR A 308 ? 1.4662 1.2492 0.9269 -0.6536 -0.1470 0.1040  604 TYR A OH  
2446 N N   . ASN A 309 ? 1.3897 1.0750 0.7987 -0.6389 -0.1991 0.0746  605 ASN A N   
2447 C CA  . ASN A 309 ? 1.4578 1.1251 0.8305 -0.6596 -0.2082 0.0747  605 ASN A CA  
2448 C C   . ASN A 309 ? 1.5960 1.1207 0.8327 -0.6933 -0.2156 0.0799  605 ASN A C   
2449 O O   . ASN A 309 ? 1.6795 1.2120 0.8673 -0.7462 -0.2203 0.0893  605 ASN A O   
2450 C CB  . ASN A 309 ? 1.3995 1.2154 0.8361 -0.6918 -0.2066 0.0826  605 ASN A CB  
2451 C CG  . ASN A 309 ? 1.4760 1.3007 0.9032 -0.7034 -0.2157 0.0810  605 ASN A CG  
2452 O OD1 . ASN A 309 ? 1.5945 1.3012 0.9371 -0.7102 -0.2240 0.0782  605 ASN A OD1 
2453 N ND2 . ASN A 309 ? 1.4024 1.3674 0.9135 -0.7025 -0.2144 0.0828  605 ASN A ND2 
2454 N N   . ILE A 310 ? 1.6804 1.0724 0.8498 -0.6602 -0.2169 0.0737  606 ILE A N   
2455 C CA  . ILE A 310 ? 1.8101 1.0555 0.8396 -0.6827 -0.2237 0.0784  606 ILE A CA  
2456 C C   . ILE A 310 ? 1.9487 1.0898 0.9043 -0.6672 -0.2324 0.0719  606 ILE A C   
2457 O O   . ILE A 310 ? 2.1155 1.1235 0.9449 -0.6789 -0.2388 0.0750  606 ILE A O   
2458 C CB  . ILE A 310 ? 1.8862 1.0384 0.8664 -0.6521 -0.2206 0.0765  606 ILE A CB  
2459 C CG1 . ILE A 310 ? 1.8844 0.9822 0.8828 -0.5783 -0.2192 0.0620  606 ILE A CG1 
2460 C CG2 . ILE A 310 ? 1.6998 0.9514 0.7517 -0.6658 -0.2114 0.0826  606 ILE A CG2 
2461 C CD1 . ILE A 310 ? 1.8405 0.8456 0.7860 -0.5412 -0.2167 0.0599  606 ILE A CD1 
2462 N N   . LEU A 311 ? 1.9159 1.1100 0.9400 -0.6398 -0.2332 0.0628  607 LEU A N   
2463 C CA  . LEU A 311 ? 1.9525 1.0555 0.9069 -0.6282 -0.2410 0.0569  607 LEU A CA  
2464 C C   . LEU A 311 ? 2.1130 1.1756 0.9770 -0.6923 -0.2491 0.0685  607 LEU A C   
2465 O O   . LEU A 311 ? 2.2670 1.1948 1.0141 -0.6912 -0.2559 0.0680  607 LEU A O   
2466 C CB  . LEU A 311 ? 1.6722 0.8589 0.7193 -0.6006 -0.2412 0.0467  607 LEU A CB  
2467 C CG  . LEU A 311 ? 1.6650 0.8465 0.7646 -0.5310 -0.2360 0.0320  607 LEU A CG  
2468 C CD1 . LEU A 311 ? 1.6276 0.8796 0.7992 -0.5096 -0.2384 0.0222  607 LEU A CD1 
2469 C CD2 . LEU A 311 ? 1.7175 0.7462 0.7127 -0.4890 -0.2365 0.0254  607 LEU A CD2 
2470 N N   . GLU A 312 ? 2.0551 1.2348 0.9679 -0.7471 -0.2485 0.0792  608 GLU A N   
2471 C CA  . GLU A 312 ? 2.2574 1.4158 1.0876 -0.8169 -0.2558 0.0917  608 GLU A CA  
2472 C C   . GLU A 312 ? 2.4290 1.4292 1.1099 -0.8372 -0.2607 0.0977  608 GLU A C   
2473 O O   . GLU A 312 ? 2.5248 1.4027 1.0941 -0.8465 -0.2694 0.0980  608 GLU A O   
2474 C CB  . GLU A 312 ? 2.2518 1.5673 1.1569 -0.8662 -0.2513 0.1027  608 GLU A CB  
2475 C CG  . GLU A 312 ? 2.1476 1.6117 1.1614 -0.8670 -0.2511 0.1011  608 GLU A CG  
2476 C CD  . GLU A 312 ? 2.2624 1.7232 1.2177 -0.9225 -0.2607 0.1086  608 GLU A CD  
2477 O OE1 . GLU A 312 ? 2.3233 1.6542 1.1854 -0.9219 -0.2689 0.1053  608 GLU A OE1 
2478 O OE2 . GLU A 312 ? 2.2298 1.8182 1.2285 -0.9661 -0.2599 0.1179  608 GLU A OE2 
2479 N N   . GLU A 313 ? 2.5803 1.5779 1.2531 -0.8419 -0.2557 0.1020  609 GLU A N   
2480 C CA  . GLU A 313 ? 2.7823 1.6400 1.3095 -0.8687 -0.2616 0.1086  609 GLU A CA  
2481 C C   . GLU A 313 ? 2.8403 1.5402 1.2837 -0.8048 -0.2640 0.0986  609 GLU A C   
2482 O O   . GLU A 313 ? 3.0397 1.5967 1.3380 -0.8199 -0.2720 0.1023  609 GLU A O   
2483 C CB  . GLU A 313 ? 2.8860 1.8015 1.4299 -0.9008 -0.2561 0.1168  609 GLU A CB  
2484 C CG  . GLU A 313 ? 2.9684 1.9852 1.5162 -0.9829 -0.2573 0.1306  609 GLU A CG  
2485 C CD  . GLU A 313 ? 3.1737 2.0713 1.5601 -1.0476 -0.2693 0.1402  609 GLU A CD  
2486 O OE1 . GLU A 313 ? 3.2599 1.9934 1.5295 -1.0269 -0.2774 0.1360  609 GLU A OE1 
2487 O OE2 . GLU A 313 ? 3.2156 2.1853 1.5874 -1.1195 -0.2707 0.1521  609 GLU A OE2 
2488 N N   . VAL A 314 ? 2.5736 1.2953 1.0977 -0.7329 -0.2576 0.0859  610 VAL A N   
2489 C CA  . VAL A 314 ? 2.6053 1.1860 1.0473 -0.6674 -0.2597 0.0760  610 VAL A CA  
2490 C C   . VAL A 314 ? 2.6694 1.1570 1.0263 -0.6625 -0.2678 0.0733  610 VAL A C   
2491 O O   . VAL A 314 ? 2.7742 1.1112 0.9939 -0.6454 -0.2742 0.0728  610 VAL A O   
2492 C CB  . VAL A 314 ? 2.4317 1.0678 0.9813 -0.5939 -0.2503 0.0633  610 VAL A CB  
2493 C CG1 . VAL A 314 ? 2.4767 0.9911 0.9539 -0.5207 -0.2518 0.0517  610 VAL A CG1 
2494 C CG2 . VAL A 314 ? 2.3484 1.0267 0.9400 -0.5920 -0.2438 0.0663  610 VAL A CG2 
2495 N N   . ALA A 315 ? 2.5701 1.1438 1.0022 -0.6758 -0.2680 0.0713  611 ALA A N   
2496 C CA  . ALA A 315 ? 2.6656 1.1565 1.0213 -0.6737 -0.2755 0.0688  611 ALA A CA  
2497 C C   . ALA A 315 ? 2.8170 1.2059 1.0285 -0.7386 -0.2859 0.0818  611 ALA A C   
2498 O O   . ALA A 315 ? 2.9336 1.1809 1.0196 -0.7234 -0.2929 0.0804  611 ALA A O   
2499 C CB  . ALA A 315 ? 2.4994 1.1126 0.9653 -0.6836 -0.2748 0.0648  611 ALA A CB  
2500 N N   . LYS A 316 ? 2.7951 1.2547 1.0180 -0.8114 -0.2869 0.0946  612 LYS A N   
2501 C CA  . LYS A 316 ? 2.9076 1.2742 0.9882 -0.8813 -0.2969 0.1076  612 LYS A CA  
2502 C C   . LYS A 316 ? 3.0513 1.2321 0.9758 -0.8519 -0.3023 0.1060  612 LYS A C   
2503 O O   . LYS A 316 ? 3.1651 1.2069 0.9552 -0.8544 -0.3114 0.1072  612 LYS A O   
2504 C CB  . LYS A 316 ? 2.9261 1.4029 1.0460 -0.9535 -0.2948 0.1201  612 LYS A CB  
2505 C CG  . LYS A 316 ? 2.8756 1.4930 1.0708 -1.0133 -0.2955 0.1278  612 LYS A CG  
2506 C CD  . LYS A 316 ? 2.9670 1.6379 1.1277 -1.0978 -0.2971 0.1430  612 LYS A CD  
2507 C CE  . LYS A 316 ? 3.0940 1.5917 1.0599 -1.1469 -0.3089 0.1516  612 LYS A CE  
2508 N NZ  . LYS A 316 ? 3.1414 1.6814 1.0575 -1.2347 -0.3115 0.1660  612 LYS A NZ  
2509 N N   . LYS A 317 ? 2.9947 1.1710 0.9341 -0.8194 -0.2969 0.1027  613 LYS A N   
2510 C CA  . LYS A 317 ? 3.1299 1.1403 0.9229 -0.7904 -0.3023 0.1006  613 LYS A CA  
2511 C C   . LYS A 317 ? 3.1749 1.0751 0.9132 -0.7052 -0.3032 0.0887  613 LYS A C   
2512 O O   . LYS A 317 ? 3.3303 1.0802 0.9306 -0.6771 -0.3089 0.0860  613 LYS A O   
2513 C CB  . LYS A 317 ? 3.0647 1.1138 0.9046 -0.7712 -0.2956 0.0984  613 LYS A CB  
2514 C CG  . LYS A 317 ? 3.1432 1.1962 0.9282 -0.8494 -0.2995 0.1102  613 LYS A CG  
2515 C CD  . LYS A 317 ? 3.0800 1.3241 1.0112 -0.9012 -0.2918 0.1175  613 LYS A CD  
2516 C CE  . LYS A 317 ? 3.0918 1.3471 0.9773 -0.9654 -0.2934 0.1271  613 LYS A CE  
2517 N NZ  . LYS A 317 ? 3.0644 1.5148 1.0988 -1.0011 -0.2835 0.1331  613 LYS A NZ  
2518 N N   . MET A 318 ? 3.0534 1.0306 0.9014 -0.6594 -0.2968 0.0796  614 MET A N   
2519 C CA  . MET A 318 ? 3.1406 1.0221 0.9331 -0.5847 -0.2975 0.0690  614 MET A CA  
2520 C C   . MET A 318 ? 3.2474 1.0417 0.9370 -0.6170 -0.3071 0.0739  614 MET A C   
2521 O O   . MET A 318 ? 3.3695 1.0599 0.9808 -0.5595 -0.3092 0.0670  614 MET A O   
2522 C CB  . MET A 318 ? 2.9683 0.9654 0.9146 -0.5219 -0.2866 0.0560  614 MET A CB  
2523 C CG  . MET A 318 ? 2.9393 0.9978 0.9699 -0.4742 -0.2772 0.0495  614 MET A CG  
2524 S SD  . MET A 318 ? 2.7508 0.9248 0.9380 -0.3986 -0.2652 0.0335  614 MET A SD  
2525 C CE  . MET A 318 ? 2.7153 0.7637 0.7951 -0.3287 -0.2678 0.0243  614 MET A CE  
2526 N N   . ASP A 319 ? 3.3044 1.1410 0.9900 -0.7066 -0.3128 0.0860  615 ASP A N   
2527 C CA  . ASP A 319 ? 3.4656 1.2469 1.0757 -0.7490 -0.3216 0.0915  615 ASP A CA  
2528 C C   . ASP A 319 ? 3.3719 1.2023 1.0666 -0.6981 -0.3173 0.0797  615 ASP A C   
2529 O O   . ASP A 319 ? 3.4580 1.1759 1.0698 -0.6437 -0.3195 0.0729  615 ASP A O   
2530 C CB  . ASP A 319 ? 3.7435 1.3237 1.1507 -0.7507 -0.3322 0.0950  615 ASP A CB  
2531 C CG  . ASP A 319 ? 3.8996 1.4326 1.2173 -0.8360 -0.3429 0.1061  615 ASP A CG  
2532 O OD1 . ASP A 319 ? 3.8862 1.5001 1.2291 -0.9203 -0.3451 0.1182  615 ASP A OD1 
2533 O OD2 . ASP A 319 ? 4.0428 1.4592 1.2617 -0.8190 -0.3491 0.1027  615 ASP A OD2 
2534 N N   . LEU A 320 ? 3.2075 1.2062 1.0627 -0.7145 -0.3113 0.0769  616 LEU A N   
2535 C CA  . LEU A 320 ? 3.0647 1.1312 1.0187 -0.6658 -0.3064 0.0637  616 LEU A CA  
2536 C C   . LEU A 320 ? 3.0222 1.1503 1.0041 -0.7245 -0.3126 0.0676  616 LEU A C   
2537 O O   . LEU A 320 ? 3.0473 1.2292 1.0294 -0.8034 -0.3173 0.0804  616 LEU A O   
2538 C CB  . LEU A 320 ? 2.8576 1.0710 0.9778 -0.6274 -0.2950 0.0547  616 LEU A CB  
2539 C CG  . LEU A 320 ? 2.8646 1.0354 0.9820 -0.5528 -0.2875 0.0465  616 LEU A CG  
2540 C CD1 . LEU A 320 ? 2.6565 0.9748 0.9394 -0.5199 -0.2769 0.0373  616 LEU A CD1 
2541 C CD2 . LEU A 320 ? 2.9081 0.9515 0.9305 -0.4825 -0.2881 0.0373  616 LEU A CD2 
2542 N N   . ASP A 321 ? 2.9873 1.1142 0.9945 -0.6838 -0.3122 0.0561  617 ASP A N   
2543 C CA  . ASP A 321 ? 2.9845 1.1863 1.0381 -0.7276 -0.3176 0.0564  617 ASP A CA  
2544 C C   . ASP A 321 ? 2.7906 1.1862 1.0126 -0.7461 -0.3124 0.0555  617 ASP A C   
2545 O O   . ASP A 321 ? 2.6608 1.1383 0.9906 -0.6951 -0.3060 0.0426  617 ASP A O   
2546 C CB  . ASP A 321 ? 2.9756 1.1260 1.0136 -0.6717 -0.3177 0.0423  617 ASP A CB  
2547 C CG  . ASP A 321 ? 3.0532 1.2406 1.0971 -0.7210 -0.3264 0.0435  617 ASP A CG  
2548 O OD1 . ASP A 321 ? 3.1223 1.3806 1.1841 -0.7978 -0.3323 0.0557  617 ASP A OD1 
2549 O OD2 . ASP A 321 ? 3.0327 1.1821 1.0619 -0.6823 -0.3272 0.0321  617 ASP A OD2 
2550 N N   . MET A 322 ? 2.7860 1.2559 1.0259 -0.8178 -0.3149 0.0695  618 MET A N   
2551 C CA  . MET A 322 ? 2.6697 1.3213 1.0596 -0.8319 -0.3091 0.0708  618 MET A CA  
2552 C C   . MET A 322 ? 2.7039 1.4808 1.1688 -0.8713 -0.3145 0.0722  618 MET A C   
2553 O O   . MET A 322 ? 2.6176 1.5513 1.2130 -0.8696 -0.3101 0.0712  618 MET A O   
2554 C CB  . MET A 322 ? 2.6793 1.3543 1.0519 -0.8798 -0.3068 0.0849  618 MET A CB  
2555 C CG  . MET A 322 ? 2.5055 1.3188 1.0130 -0.8591 -0.2965 0.0830  618 MET A CG  
2556 S SD  . MET A 322 ? 2.6164 1.3640 1.0659 -0.8601 -0.2911 0.0901  618 MET A SD  
2557 C CE  . MET A 322 ? 2.5144 1.4483 1.0685 -0.9199 -0.2861 0.1023  618 MET A CE  
2558 N N   . ARG A 323 ? 2.9012 1.6130 1.2849 -0.9037 -0.3243 0.0744  619 ARG A N   
2559 C CA  . ARG A 323 ? 2.8710 1.7017 1.3212 -0.9403 -0.3308 0.0754  619 ARG A CA  
2560 C C   . ARG A 323 ? 2.7762 1.6775 1.3294 -0.8789 -0.3288 0.0590  619 ARG A C   
2561 O O   . ARG A 323 ? 2.6914 1.7460 1.3570 -0.8863 -0.3298 0.0584  619 ARG A O   
2562 C CB  . ARG A 323 ? 3.0181 1.7499 1.3434 -0.9944 -0.3426 0.0823  619 ARG A CB  
2563 C CG  . ARG A 323 ? 3.1925 1.8488 1.4006 -1.0637 -0.3462 0.0997  619 ARG A CG  
2564 C CD  . ARG A 323 ? 3.4159 1.8882 1.4567 -1.0831 -0.3558 0.1024  619 ARG A CD  
2565 N NE  . ARG A 323 ? 3.4714 1.8076 1.4587 -1.0029 -0.3524 0.0894  619 ARG A NE  
2566 C CZ  . ARG A 323 ? 3.6629 1.8241 1.5030 -0.9955 -0.3588 0.0890  619 ARG A CZ  
2567 N NH1 . ARG A 323 ? 3.8021 1.8895 1.5259 -1.0670 -0.3699 0.1009  619 ARG A NH1 
2568 N NH2 . ARG A 323 ? 3.6708 1.7297 1.4759 -0.9134 -0.3539 0.0767  619 ARG A NH2 
2569 N N   . LYS A 324 ? 2.6929 1.4865 1.2050 -0.8163 -0.3262 0.0458  620 LYS A N   
2570 C CA  . LYS A 324 ? 2.5168 1.3583 1.1035 -0.7610 -0.3249 0.0299  620 LYS A CA  
2571 C C   . LYS A 324 ? 2.3226 1.2255 1.0052 -0.7019 -0.3137 0.0215  620 LYS A C   
2572 O O   . LYS A 324 ? 2.3453 1.1788 0.9936 -0.6761 -0.3064 0.0218  620 LYS A O   
2573 C CB  . LYS A 324 ? 2.6234 1.3191 1.1076 -0.7256 -0.3273 0.0198  620 LYS A CB  
2574 C CG  . LYS A 324 ? 2.8115 1.4677 1.2237 -0.7747 -0.3395 0.0236  620 LYS A CG  
2575 C CD  . LYS A 324 ? 2.9935 1.5569 1.2856 -0.8414 -0.3460 0.0400  620 LYS A CD  
2576 C CE  . LYS A 324 ? 3.0278 1.5604 1.2526 -0.8943 -0.3588 0.0436  620 LYS A CE  
2577 N NZ  . LYS A 324 ? 3.1968 1.6271 1.2890 -0.9633 -0.3658 0.0601  620 LYS A NZ  
2578 N N   . THR A 325 ? 2.1771 1.2106 0.9764 -0.6816 -0.3133 0.0148  621 THR A N   
2579 C CA  . THR A 325 ? 1.9846 1.0762 0.8724 -0.6274 -0.3037 0.0067  621 THR A CA  
2580 C C   . THR A 325 ? 2.0306 1.0163 0.8733 -0.5601 -0.2971 -0.0079 621 THR A C   
2581 O O   . THR A 325 ? 1.8770 0.8553 0.7458 -0.5177 -0.2877 -0.0129 621 THR A O   
2582 C CB  . THR A 325 ? 1.8274 1.0765 0.8375 -0.6215 -0.3065 0.0045  621 THR A CB  
2583 O OG1 . THR A 325 ? 1.8178 1.1047 0.8991 -0.5659 -0.2982 -0.0045 621 THR A OG1 
2584 C CG2 . THR A 325 ? 1.9524 1.2049 0.9500 -0.6207 -0.3159 -0.0019 621 THR A CG2 
2585 N N   . SER A 326 ? 2.0886 0.9939 0.8606 -0.5489 -0.3014 -0.0148 622 SER A N   
2586 C CA  . SER A 326 ? 2.0753 0.8987 0.8087 -0.4814 -0.2943 -0.0297 622 SER A CA  
2587 C C   . SER A 326 ? 2.1505 0.8258 0.7713 -0.4556 -0.2892 -0.0291 622 SER A C   
2588 O O   . SER A 326 ? 2.1641 0.7760 0.7520 -0.3915 -0.2811 -0.0409 622 SER A O   
2589 C CB  . SER A 326 ? 2.0703 0.8803 0.7769 -0.4813 -0.3011 -0.0368 622 SER A CB  
2590 O OG  . SER A 326 ? 2.0806 0.9410 0.7913 -0.5495 -0.3134 -0.0258 622 SER A OG  
2591 N N   . SER A 327 ? 2.2369 0.8576 0.7926 -0.5018 -0.2936 -0.0151 623 SER A N   
2592 C CA  . SER A 327 ? 2.3483 0.8366 0.8012 -0.4728 -0.2894 -0.0127 623 SER A CA  
2593 C C   . SER A 327 ? 2.2599 0.7785 0.7701 -0.4199 -0.2780 -0.0182 623 SER A C   
2594 O O   . SER A 327 ? 2.3401 0.7580 0.7733 -0.3787 -0.2736 -0.0187 623 SER A O   
2595 C CB  . SER A 327 ? 2.4661 0.8964 0.8358 -0.5401 -0.2974 0.0049  623 SER A CB  
2596 O OG  . SER A 327 ? 2.4157 0.9417 0.8613 -0.5722 -0.2948 0.0135  623 SER A OG  
2597 N N   . LEU A 328 ? 2.1559 0.8095 0.7943 -0.4191 -0.2740 -0.0216 624 LEU A N   
2598 C CA  . LEU A 328 ? 2.0764 0.7676 0.7753 -0.3756 -0.2638 -0.0264 624 LEU A CA  
2599 C C   . LEU A 328 ? 2.1263 0.7606 0.7718 -0.3931 -0.2634 -0.0149 624 LEU A C   
2600 O O   . LEU A 328 ? 2.1627 0.7561 0.7927 -0.3442 -0.2560 -0.0188 624 LEU A O   
2601 C CB  . LEU A 328 ? 2.0617 0.7105 0.7478 -0.2934 -0.2539 -0.0422 624 LEU A CB  
2602 C CG  . LEU A 328 ? 2.0301 0.7277 0.7579 -0.2712 -0.2528 -0.0547 624 LEU A CG  
2603 C CD1 . LEU A 328 ? 1.9443 0.6509 0.6981 -0.1919 -0.2391 -0.0698 624 LEU A CD1 
2604 C CD2 . LEU A 328 ? 1.9392 0.7699 0.7731 -0.3170 -0.2591 -0.0514 624 LEU A CD2 
2605 N N   . TRP A 329 ? 2.1549 0.7901 0.7687 -0.4641 -0.2714 -0.0002 625 TRP A N   
2606 C CA  . TRP A 329 ? 2.2440 0.8310 0.8039 -0.4884 -0.2715 0.0116  625 TRP A CA  
2607 C C   . TRP A 329 ? 2.1504 0.8375 0.8147 -0.4785 -0.2637 0.0114  625 TRP A C   
2608 O O   . TRP A 329 ? 2.1894 0.8247 0.8166 -0.4611 -0.2600 0.0143  625 TRP A O   
2609 C CB  . TRP A 329 ? 2.2949 0.8751 0.8011 -0.5715 -0.2808 0.0275  625 TRP A CB  
2610 C CG  . TRP A 329 ? 2.2489 0.9850 0.8659 -0.6225 -0.2825 0.0327  625 TRP A CG  
2611 C CD1 . TRP A 329 ? 2.2569 1.0552 0.9093 -0.6464 -0.2886 0.0312  625 TRP A CD1 
2612 C CD2 . TRP A 329 ? 2.1708 1.0254 0.8761 -0.6512 -0.2782 0.0405  625 TRP A CD2 
2613 N NE1 . TRP A 329 ? 2.1450 1.0951 0.9011 -0.6852 -0.2886 0.0378  625 TRP A NE1 
2614 C CE2 . TRP A 329 ? 2.1060 1.0943 0.8970 -0.6879 -0.2816 0.0436  625 TRP A CE2 
2615 C CE3 . TRP A 329 ? 2.1324 0.9948 0.8512 -0.6468 -0.2717 0.0450  625 TRP A CE3 
2616 C CZ2 . TRP A 329 ? 1.9654 1.0962 0.8537 -0.7162 -0.2779 0.0512  625 TRP A CZ2 
2617 C CZ3 . TRP A 329 ? 2.0331 1.0338 0.8488 -0.6793 -0.2678 0.0524  625 TRP A CZ3 
2618 C CH2 . TRP A 329 ? 1.9931 1.1271 0.8919 -0.7118 -0.2704 0.0556  625 TRP A CH2 
2619 N N   . LYS A 330 ? 2.0044 0.8323 0.7947 -0.4875 -0.2618 0.0083  626 LYS A N   
2620 C CA  . LYS A 330 ? 1.9123 0.8344 0.8031 -0.4726 -0.2543 0.0072  626 LYS A CA  
2621 C C   . LYS A 330 ? 1.9048 0.7783 0.7949 -0.3986 -0.2461 -0.0055 626 LYS A C   
2622 O O   . LYS A 330 ? 1.8984 0.7684 0.7989 -0.3837 -0.2407 -0.0035 626 LYS A O   
2623 C CB  . LYS A 330 ? 1.8174 0.8914 0.8331 -0.4866 -0.2550 0.0054  626 LYS A CB  
2624 C CG  . LYS A 330 ? 1.7741 0.9372 0.8181 -0.5545 -0.2605 0.0191  626 LYS A CG  
2625 C CD  . LYS A 330 ? 1.6260 0.9525 0.8039 -0.5545 -0.2585 0.0193  626 LYS A CD  
2626 C CE  . LYS A 330 ? 1.6194 1.0463 0.8261 -0.6138 -0.2628 0.0326  626 LYS A CE  
2627 N NZ  . LYS A 330 ? 1.4917 1.0710 0.8151 -0.6042 -0.2633 0.0318  626 LYS A NZ  
2628 N N   . ASP A 331 ? 1.9152 0.7586 0.7948 -0.3511 -0.2445 -0.0185 627 ASP A N   
2629 C CA  . ASP A 331 ? 1.8998 0.7117 0.7814 -0.2762 -0.2352 -0.0315 627 ASP A CA  
2630 C C   . ASP A 331 ? 2.0107 0.7051 0.7899 -0.2467 -0.2331 -0.0281 627 ASP A C   
2631 O O   . ASP A 331 ? 2.0194 0.7171 0.8176 -0.2112 -0.2264 -0.0301 627 ASP A O   
2632 C CB  . ASP A 331 ? 1.9100 0.7091 0.7831 -0.2356 -0.2333 -0.0448 627 ASP A CB  
2633 C CG  . ASP A 331 ? 1.7994 0.7089 0.7632 -0.2617 -0.2373 -0.0480 627 ASP A CG  
2634 O OD1 . ASP A 331 ? 1.7349 0.6659 0.6938 -0.3154 -0.2466 -0.0398 627 ASP A OD1 
2635 O OD2 . ASP A 331 ? 1.7021 0.6799 0.7403 -0.2285 -0.2316 -0.0578 627 ASP A OD2 
2636 N N   . GLN A 332 ? 2.0737 0.6612 0.7386 -0.2592 -0.2396 -0.0226 628 GLN A N   
2637 C CA  . GLN A 332 ? 2.2300 0.6942 0.7785 -0.2304 -0.2402 -0.0184 628 GLN A CA  
2638 C C   . GLN A 332 ? 2.2202 0.6890 0.7685 -0.2607 -0.2409 -0.0078 628 GLN A C   
2639 O O   . GLN A 332 ? 2.2238 0.6516 0.7433 -0.2142 -0.2366 -0.0097 628 GLN A O   
2640 C CB  . GLN A 332 ? 2.3653 0.7176 0.7889 -0.2560 -0.2497 -0.0120 628 GLN A CB  
2641 C CG  . GLN A 332 ? 2.5107 0.7316 0.8104 -0.1947 -0.2494 -0.0145 628 GLN A CG  
2642 C CD  . GLN A 332 ? 2.6267 0.7590 0.8314 -0.1977 -0.2559 -0.0145 628 GLN A CD  
2643 O OE1 . GLN A 332 ? 2.6299 0.7760 0.8350 -0.2623 -0.2634 -0.0088 628 GLN A OE1 
2644 N NE2 . GLN A 332 ? 2.6627 0.7088 0.7859 -0.1259 -0.2530 -0.0206 628 GLN A NE2 
2645 N N   . ALA A 333 ? 2.2057 0.7319 0.7870 -0.3372 -0.2460 0.0035  629 ALA A N   
2646 C CA  . ALA A 333 ? 2.1687 0.7108 0.7548 -0.3694 -0.2455 0.0137  629 ALA A CA  
2647 C C   . ALA A 333 ? 2.1084 0.7392 0.8039 -0.3333 -0.2360 0.0072  629 ALA A C   
2648 O O   . ALA A 333 ? 2.0149 0.6284 0.6969 -0.3283 -0.2336 0.0117  629 ALA A O   
2649 C CB  . ALA A 333 ? 2.1846 0.7932 0.7942 -0.4562 -0.2509 0.0270  629 ALA A CB  
2650 N N   . LEU A 334 ? 1.9858 0.7081 0.7846 -0.3089 -0.2313 -0.0033 630 LEU A N   
2651 C CA  . LEU A 334 ? 1.8704 0.6776 0.7711 -0.2810 -0.2233 -0.0088 630 LEU A CA  
2652 C C   . LEU A 334 ? 1.9578 0.7055 0.8268 -0.2030 -0.2165 -0.0180 630 LEU A C   
2653 O O   . LEU A 334 ? 1.8805 0.6609 0.7942 -0.1841 -0.2111 -0.0179 630 LEU A O   
2654 C CB  . LEU A 334 ? 1.7887 0.7086 0.7998 -0.2810 -0.2218 -0.0172 630 LEU A CB  
2655 C CG  . LEU A 334 ? 1.6684 0.6726 0.7807 -0.2502 -0.2149 -0.0247 630 LEU A CG  
2656 C CD1 . LEU A 334 ? 1.5822 0.6939 0.7765 -0.3051 -0.2164 -0.0142 630 LEU A CD1 
2657 C CD2 . LEU A 334 ? 1.6347 0.6921 0.8026 -0.2102 -0.2105 -0.0367 630 LEU A CD2 
2658 N N   . VAL A 335 ? 1.9310 0.5993 0.7249 -0.1548 -0.2162 -0.0252 631 VAL A N   
2659 C CA  . VAL A 335 ? 2.0197 0.6414 0.7769 -0.0751 -0.2093 -0.0325 631 VAL A CA  
2660 C C   . VAL A 335 ? 2.1216 0.6651 0.7965 -0.0770 -0.2128 -0.0229 631 VAL A C   
2661 O O   . VAL A 335 ? 2.0572 0.6195 0.7575 -0.0399 -0.2075 -0.0242 631 VAL A O   
2662 C CB  . VAL A 335 ? 2.0993 0.6619 0.7902 -0.0230 -0.2079 -0.0410 631 VAL A CB  
2663 C CG1 . VAL A 335 ? 2.1660 0.6754 0.7958 0.0556  -0.2027 -0.0446 631 VAL A CG1 
2664 C CG2 . VAL A 335 ? 2.0649 0.7157 0.8458 -0.0048 -0.2012 -0.0537 631 VAL A CG2 
2665 N N   . GLU A 336 ? 2.1643 0.6196 0.7364 -0.1226 -0.2224 -0.0131 632 GLU A N   
2666 C CA  . GLU A 336 ? 2.2904 0.6624 0.7700 -0.1316 -0.2271 -0.0045 632 GLU A CA  
2667 C C   . GLU A 336 ? 2.2094 0.6541 0.7660 -0.1612 -0.2237 0.0013  632 GLU A C   
2668 O O   . GLU A 336 ? 2.1994 0.6075 0.7209 -0.1327 -0.2225 0.0023  632 GLU A O   
2669 C CB  . GLU A 336 ? 2.4373 0.7182 0.8042 -0.1944 -0.2383 0.0062  632 GLU A CB  
2670 C CG  . GLU A 336 ? 2.5148 0.7223 0.8045 -0.1752 -0.2425 0.0025  632 GLU A CG  
2671 C CD  . GLU A 336 ? 2.6915 0.8020 0.8839 -0.0926 -0.2416 -0.0044 632 GLU A CD  
2672 O OE1 . GLU A 336 ? 2.6816 0.7533 0.8311 -0.0648 -0.2414 -0.0039 632 GLU A OE1 
2673 O OE2 . GLU A 336 ? 2.7103 0.7875 0.8683 -0.0543 -0.2412 -0.0105 632 GLU A OE2 
2674 N N   . ILE A 337 ? 2.1159 0.6662 0.7753 -0.2170 -0.2223 0.0054  633 ILE A N   
2675 C CA  . ILE A 337 ? 2.0450 0.6711 0.7786 -0.2487 -0.2187 0.0122  633 ILE A CA  
2676 C C   . ILE A 337 ? 1.9888 0.6525 0.7862 -0.1836 -0.2103 0.0044  633 ILE A C   
2677 O O   . ILE A 337 ? 2.0113 0.6733 0.8094 -0.1816 -0.2083 0.0097  633 ILE A O   
2678 C CB  . ILE A 337 ? 1.9305 0.6767 0.7653 -0.3130 -0.2185 0.0173  633 ILE A CB  
2679 C CG1 . ILE A 337 ? 2.0147 0.7297 0.7793 -0.3837 -0.2265 0.0289  633 ILE A CG1 
2680 C CG2 . ILE A 337 ? 1.8464 0.6881 0.7746 -0.3309 -0.2124 0.0222  633 ILE A CG2 
2681 C CD1 . ILE A 337 ? 1.9545 0.7922 0.8088 -0.4405 -0.2269 0.0339  633 ILE A CD1 
2682 N N   . ASN A 338 ? 1.9497 0.6486 0.7980 -0.1294 -0.2052 -0.0080 634 ASN A N   
2683 C CA  . ASN A 338 ? 1.9042 0.6506 0.8170 -0.0684 -0.1969 -0.0148 634 ASN A CA  
2684 C C   . ASN A 338 ? 1.9969 0.6695 0.8294 0.0058  -0.1951 -0.0185 634 ASN A C   
2685 O O   . ASN A 338 ? 1.9296 0.6362 0.7993 0.0502  -0.1897 -0.0194 634 ASN A O   
2686 C CB  . ASN A 338 ? 1.7934 0.6284 0.8027 -0.0438 -0.1909 -0.0265 634 ASN A CB  
2687 C CG  . ASN A 338 ? 1.6639 0.6188 0.7783 -0.1067 -0.1898 -0.0204 634 ASN A CG  
2688 O OD1 . ASN A 338 ? 1.5019 0.5801 0.7275 -0.1028 -0.1804 -0.0165 634 ASN A OD1 
2689 N ND2 . ASN A 338 ? 1.7092 0.6260 0.7821 -0.1636 -0.2004 -0.0198 634 ASN A ND2 
2690 N N   . ILE A 339 ? 2.0643 0.6412 0.7857 0.0210  -0.2001 -0.0200 635 ILE A N   
2691 C CA  . ILE A 339 ? 2.1391 0.6397 0.7673 0.0828  -0.2007 -0.0222 635 ILE A CA  
2692 C C   . ILE A 339 ? 2.2041 0.6593 0.7862 0.0526  -0.2054 -0.0127 635 ILE A C   
2693 O O   . ILE A 339 ? 2.1518 0.6011 0.7203 0.1027  -0.2029 -0.0145 635 ILE A O   
2694 C CB  . ILE A 339 ? 2.2323 0.6306 0.7399 0.1017  -0.2064 -0.0251 635 ILE A CB  
2695 C CG1 . ILE A 339 ? 2.2177 0.6668 0.7721 0.1427  -0.1999 -0.0353 635 ILE A CG1 
2696 C CG2 . ILE A 339 ? 2.3247 0.6349 0.7202 0.1607  -0.2090 -0.0271 635 ILE A CG2 
2697 C CD1 . ILE A 339 ? 2.3012 0.6523 0.7403 0.1607  -0.2053 -0.0369 635 ILE A CD1 
2698 N N   . ALA A 340 ? 2.2223 0.6570 0.7851 -0.0307 -0.2117 -0.0025 636 ALA A N   
2699 C CA  . ALA A 340 ? 2.2572 0.6515 0.7729 -0.0684 -0.2156 0.0069  636 ALA A CA  
2700 C C   . ALA A 340 ? 2.1924 0.6780 0.8135 -0.0648 -0.2085 0.0104  636 ALA A C   
2701 O O   . ALA A 340 ? 2.1662 0.6196 0.7520 -0.0432 -0.2085 0.0126  636 ALA A O   
2702 C CB  . ALA A 340 ? 2.3117 0.6854 0.7911 -0.1610 -0.2227 0.0176  636 ALA A CB  
2703 N N   . VAL A 341 ? 2.0503 0.6461 0.7951 -0.0878 -0.2030 0.0112  637 VAL A N   
2704 C CA  . VAL A 341 ? 1.9427 0.6232 0.7854 -0.0835 -0.1965 0.0154  637 VAL A CA  
2705 C C   . VAL A 341 ? 1.9977 0.6768 0.8423 0.0044  -0.1925 0.0094  637 VAL A C   
2706 O O   . VAL A 341 ? 2.0101 0.6814 0.8437 0.0187  -0.1919 0.0153  637 VAL A O   
2707 C CB  . VAL A 341 ? 1.8729 0.6655 0.8394 -0.1112 -0.1922 0.0134  637 VAL A CB  
2708 C CG1 . VAL A 341 ? 1.7012 0.6235 0.7851 -0.0937 -0.1815 0.0165  637 VAL A CG1 
2709 C CG2 . VAL A 341 ? 1.8747 0.6979 0.8509 -0.1980 -0.1959 0.0207  637 VAL A CG2 
2710 N N   . LEU A 342 ? 1.9504 0.6453 0.8073 0.0650  -0.1893 -0.0022 638 LEU A N   
2711 C CA  . LEU A 342 ? 1.9543 0.6752 0.8201 0.1515  -0.1845 -0.0085 638 LEU A CA  
2712 C C   . LEU A 342 ? 2.0995 0.7313 0.8555 0.1794  -0.1890 -0.0079 638 LEU A C   
2713 O O   . LEU A 342 ? 2.0492 0.7042 0.8206 0.2052  -0.1877 -0.0040 638 LEU A O   
2714 C CB  . LEU A 342 ? 1.9830 0.7311 0.8603 0.2044  -0.1799 -0.0213 638 LEU A CB  
2715 C CG  . LEU A 342 ? 1.8168 0.6706 0.8118 0.1917  -0.1736 -0.0252 638 LEU A CG  
2716 C CD1 . LEU A 342 ? 1.8073 0.6836 0.8030 0.2523  -0.1680 -0.0378 638 LEU A CD1 
2717 C CD2 . LEU A 342 ? 1.6345 0.6305 0.7516 0.1930  -0.1649 -0.0207 638 LEU A CD2 
2718 N N   . TYR A 343 ? 2.1305 0.6559 0.7691 0.1738  -0.1952 -0.0115 639 TYR A N   
2719 C CA  . TYR A 343 ? 2.3133 0.7395 0.8310 0.2057  -0.2003 -0.0135 639 TYR A CA  
2720 C C   . TYR A 343 ? 2.3066 0.7115 0.8128 0.1668  -0.2031 -0.0038 639 TYR A C   
2721 O O   . TYR A 343 ? 2.3630 0.7455 0.8313 0.2123  -0.2034 -0.0058 639 TYR A O   
2722 C CB  . TYR A 343 ? 2.4630 0.7662 0.8479 0.1868  -0.2087 -0.0157 639 TYR A CB  
2723 C CG  . TYR A 343 ? 2.5980 0.7745 0.8369 0.2039  -0.2164 -0.0170 639 TYR A CG  
2724 C CD1 . TYR A 343 ? 2.6491 0.7880 0.8177 0.2894  -0.2158 -0.0269 639 TYR A CD1 
2725 C CD2 . TYR A 343 ? 2.6287 0.7259 0.7962 0.1340  -0.2241 -0.0087 639 TYR A CD2 
2726 C CE1 . TYR A 343 ? 2.7638 0.7812 0.7927 0.3082  -0.2232 -0.0292 639 TYR A CE1 
2727 C CE2 . TYR A 343 ? 2.7632 0.7349 0.7882 0.1487  -0.2316 -0.0112 639 TYR A CE2 
2728 C CZ  . TYR A 343 ? 2.8203 0.7478 0.7745 0.2377  -0.2314 -0.0219 639 TYR A CZ  
2729 O OH  . TYR A 343 ? 3.0221 0.8192 0.8276 0.2574  -0.2392 -0.0254 639 TYR A OH  
2730 N N   . SER A 344 ? 2.2826 0.7035 0.8244 0.0830  -0.2047 0.0069  640 SER A N   
2731 C CA  . SER A 344 ? 2.2764 0.6777 0.8010 0.0390  -0.2066 0.0172  640 SER A CA  
2732 C C   . SER A 344 ? 2.2350 0.7244 0.8525 0.0759  -0.2002 0.0214  640 SER A C   
2733 O O   . SER A 344 ? 2.2012 0.6556 0.7749 0.0982  -0.2016 0.0233  640 SER A O   
2734 C CB  . SER A 344 ? 2.2800 0.7029 0.8300 -0.0594 -0.2082 0.0280  640 SER A CB  
2735 O OG  . SER A 344 ? 2.3449 0.7026 0.8185 -0.0935 -0.2148 0.0255  640 SER A OG  
2736 N N   . PHE A 345 ? 2.0689 0.6702 0.8096 0.0839  -0.1940 0.0230  641 PHE A N   
2737 C CA  . PHE A 345 ? 1.9737 0.6648 0.8014 0.1207  -0.1895 0.0285  641 PHE A CA  
2738 C C   . PHE A 345 ? 2.0651 0.7534 0.8608 0.2090  -0.1893 0.0193  641 PHE A C   
2739 O O   . PHE A 345 ? 2.0904 0.7915 0.8861 0.2294  -0.1899 0.0245  641 PHE A O   
2740 C CB  . PHE A 345 ? 1.8241 0.6451 0.7852 0.1190  -0.1825 0.0265  641 PHE A CB  
2741 C CG  . PHE A 345 ? 1.6954 0.6092 0.7475 0.0403  -0.1759 0.0326  641 PHE A CG  
2742 C CD1 . PHE A 345 ? 1.7227 0.5851 0.7359 -0.0339 -0.1797 0.0383  641 PHE A CD1 
2743 C CD2 . PHE A 345 ? 1.5438 0.6022 0.7195 0.0430  -0.1662 0.0317  641 PHE A CD2 
2744 C CE1 . PHE A 345 ? 1.6169 0.5798 0.7162 -0.0985 -0.1732 0.0436  641 PHE A CE1 
2745 C CE2 . PHE A 345 ? 1.4539 0.5976 0.7083 -0.0190 -0.1596 0.0362  641 PHE A CE2 
2746 C CZ  . PHE A 345 ? 1.4614 0.5625 0.6797 -0.0871 -0.1628 0.0424  641 PHE A CZ  
2747 N N   . GLN A 346 ? 2.0518 0.7306 0.8194 0.2620  -0.1881 0.0056  642 GLN A N   
2748 C CA  . GLN A 346 ? 2.1200 0.8150 0.8615 0.3465  -0.1865 -0.0041 642 GLN A CA  
2749 C C   . GLN A 346 ? 2.2063 0.7863 0.8233 0.3558  -0.1924 -0.0051 642 GLN A C   
2750 O O   . GLN A 346 ? 2.2562 0.8608 0.8705 0.4040  -0.1920 -0.0063 642 GLN A O   
2751 C CB  . GLN A 346 ? 2.1144 0.8222 0.8414 0.3969  -0.1829 -0.0176 642 GLN A CB  
2752 C CG  . GLN A 346 ? 2.0868 0.9102 0.9310 0.3990  -0.1761 -0.0196 642 GLN A CG  
2753 C CD  . GLN A 346 ? 2.1317 0.9262 0.9363 0.4161  -0.1742 -0.0297 642 GLN A CD  
2754 O OE1 . GLN A 346 ? 2.1562 0.8626 0.9020 0.3674  -0.1790 -0.0282 642 GLN A OE1 
2755 N NE2 . GLN A 346 ? 2.1866 1.0590 1.0184 0.4837  -0.1673 -0.0393 642 GLN A NE2 
2756 N N   . SER A 347 ? 2.2808 0.7357 0.7895 0.3107  -0.1986 -0.0052 643 SER A N   
2757 C CA  . SER A 347 ? 2.3907 0.7231 0.7686 0.3141  -0.2054 -0.0066 643 SER A CA  
2758 C C   . SER A 347 ? 2.4026 0.7438 0.8017 0.2840  -0.2061 0.0047  643 SER A C   
2759 O O   . SER A 347 ? 2.4965 0.7470 0.7965 0.2948  -0.2110 0.0034  643 SER A O   
2760 C CB  . SER A 347 ? 2.4889 0.6933 0.7503 0.2578  -0.2132 -0.0071 643 SER A CB  
2761 O OG  . SER A 347 ? 2.5258 0.7013 0.7408 0.2937  -0.2139 -0.0170 643 SER A OG  
2762 N N   . ASP A 348 ? 2.3168 0.7622 0.8368 0.2488  -0.2015 0.0162  644 ASP A N   
2763 C CA  . ASP A 348 ? 2.3275 0.7941 0.8742 0.2219  -0.2014 0.0291  644 ASP A CA  
2764 C C   . ASP A 348 ? 2.2325 0.8244 0.8835 0.2766  -0.1973 0.0319  644 ASP A C   
2765 O O   . ASP A 348 ? 2.2073 0.8356 0.8948 0.2553  -0.1971 0.0443  644 ASP A O   
2766 C CB  . ASP A 348 ? 2.2837 0.7666 0.8707 0.1268  -0.2000 0.0431  644 ASP A CB  
2767 C CG  . ASP A 348 ? 2.3261 0.6944 0.8042 0.0613  -0.2056 0.0424  644 ASP A CG  
2768 O OD1 . ASP A 348 ? 2.4218 0.6783 0.7786 0.0882  -0.2118 0.0328  644 ASP A OD1 
2769 O OD2 . ASP A 348 ? 2.2177 0.6125 0.7286 -0.0177 -0.2041 0.0513  644 ASP A OD2 
2770 N N   . LYS A 349 ? 2.2846 0.9501 0.9826 0.3435  -0.1943 0.0207  645 LYS A N   
2771 C CA  . LYS A 349 ? 2.1766 0.9826 0.9821 0.3909  -0.1912 0.0214  645 LYS A CA  
2772 C C   . LYS A 349 ? 2.0183 0.9146 0.9322 0.3416  -0.1899 0.0348  645 LYS A C   
2773 O O   . LYS A 349 ? 1.9846 0.9774 0.9704 0.3565  -0.1906 0.0405  645 LYS A O   
2774 C CB  . LYS A 349 ? 2.3060 1.1123 1.0803 0.4326  -0.1939 0.0220  645 LYS A CB  
2775 C CG  . LYS A 349 ? 2.2973 1.2506 1.1616 0.4968  -0.1914 0.0166  645 LYS A CG  
2776 C CD  . LYS A 349 ? 2.1655 1.2074 1.1107 0.4742  -0.1939 0.0296  645 LYS A CD  
2777 C CE  . LYS A 349 ? 2.1227 1.3108 1.1484 0.5301  -0.1929 0.0226  645 LYS A CE  
2778 N NZ  . LYS A 349 ? 2.2507 1.4146 1.2166 0.5759  -0.1959 0.0198  645 LYS A NZ  
2779 N N   . VAL A 350 ? 1.9555 0.8248 0.8791 0.2817  -0.1889 0.0396  646 VAL A N   
2780 C CA  . VAL A 350 ? 1.8332 0.8243 0.8814 0.2284  -0.1805 0.0417  646 VAL A CA  
2781 C C   . VAL A 350 ? 1.6978 0.7949 0.8392 0.2513  -0.1734 0.0280  646 VAL A C   
2782 O O   . VAL A 350 ? 1.7426 0.7855 0.8450 0.2577  -0.1747 0.0224  646 VAL A O   
2783 C CB  . VAL A 350 ? 1.8241 0.7658 0.8530 0.1401  -0.1786 0.0498  646 VAL A CB  
2784 C CG1 . VAL A 350 ? 1.5797 0.6713 0.7488 0.0919  -0.1666 0.0472  646 VAL A CG1 
2785 C CG2 . VAL A 350 ? 1.8871 0.7143 0.8098 0.1119  -0.1852 0.0647  646 VAL A CG2 
2786 N N   . THR A 351 ? 1.5172 0.7603 0.7756 0.2595  -0.1660 0.0226  647 THR A N   
2787 C CA  . THR A 351 ? 1.4140 0.7632 0.7585 0.2819  -0.1590 0.0107  647 THR A CA  
2788 C C   . THR A 351 ? 1.4065 0.7572 0.7827 0.2316  -0.1535 0.0078  647 THR A C   
2789 O O   . THR A 351 ? 1.3647 0.7371 0.7814 0.1704  -0.1495 0.0123  647 THR A O   
2790 C CB  . THR A 351 ? 1.3071 0.8013 0.7627 0.2831  -0.1528 0.0069  647 THR A CB  
2791 O OG1 . THR A 351 ? 1.4030 0.8988 0.8271 0.3265  -0.1597 0.0103  647 THR A OG1 
2792 C CG2 . THR A 351 ? 1.2202 0.8193 0.7520 0.3070  -0.1462 -0.0044 647 THR A CG2 
2793 N N   . ILE A 352 ? 1.4399 0.7742 0.7976 0.2613  -0.1532 -0.0001 648 ILE A N   
2794 C CA  . ILE A 352 ? 1.3398 0.6844 0.7291 0.2227  -0.1487 -0.0041 648 ILE A CA  
2795 C C   . ILE A 352 ? 1.3478 0.7355 0.7541 0.2743  -0.1448 -0.0149 648 ILE A C   
2796 O O   . ILE A 352 ? 1.3505 0.7291 0.7161 0.3390  -0.1474 -0.0184 648 ILE A O   
2797 C CB  . ILE A 352 ? 1.4260 0.6344 0.7161 0.1826  -0.1564 0.0017  648 ILE A CB  
2798 C CG1 . ILE A 352 ? 1.3865 0.6283 0.7266 0.1263  -0.1527 0.0000  648 ILE A CG1 
2799 C CG2 . ILE A 352 ? 1.5933 0.6800 0.7641 0.2352  -0.1641 -0.0021 648 ILE A CG2 
2800 C CD1 . ILE A 352 ? 1.5009 0.6274 0.7523 0.0727  -0.1610 0.0063  648 ILE A CD1 
2801 N N   . VAL A 353 ? 1.2548 0.6964 0.7213 0.2480  -0.1383 -0.0198 649 VAL A N   
2802 C CA  . VAL A 353 ? 1.2239 0.7189 0.7139 0.2897  -0.1325 -0.0294 649 VAL A CA  
2803 C C   . VAL A 353 ? 1.2714 0.7142 0.7357 0.2634  -0.1326 -0.0324 649 VAL A C   
2804 O O   . VAL A 353 ? 1.2458 0.6844 0.7355 0.2041  -0.1333 -0.0281 649 VAL A O   
2805 C CB  . VAL A 353 ? 1.1457 0.7905 0.7517 0.2875  -0.1228 -0.0327 649 VAL A CB  
2806 C CG1 . VAL A 353 ? 1.0704 0.7604 0.7502 0.2226  -0.1186 -0.0293 649 VAL A CG1 
2807 C CG2 . VAL A 353 ? 1.1130 0.8247 0.7420 0.3289  -0.1157 -0.0416 649 VAL A CG2 
2808 N N   . ASP A 354 ? 1.3304 0.7322 0.7380 0.3101  -0.1326 -0.0399 650 ASP A N   
2809 C CA  . ASP A 354 ? 1.3907 0.7343 0.7624 0.2884  -0.1338 -0.0436 650 ASP A CA  
2810 C C   . ASP A 354 ? 1.2795 0.7404 0.7524 0.2721  -0.1234 -0.0475 650 ASP A C   
2811 O O   . ASP A 354 ? 1.1844 0.7585 0.7360 0.2889  -0.1149 -0.0490 650 ASP A O   
2812 C CB  . ASP A 354 ? 1.5035 0.7446 0.7625 0.3469  -0.1378 -0.0508 650 ASP A CB  
2813 C CG  . ASP A 354 ? 1.4955 0.8255 0.7855 0.4149  -0.1280 -0.0597 650 ASP A CG  
2814 O OD1 . ASP A 354 ? 1.4235 0.8401 0.7835 0.4029  -0.1188 -0.0639 650 ASP A OD1 
2815 O OD2 . ASP A 354 ? 1.5563 0.8707 0.7961 0.4815  -0.1296 -0.0622 650 ASP A OD2 
2816 N N   . HIS A 355 ? 1.3065 0.7390 0.7740 0.2344  -0.1248 -0.0484 651 HIS A N   
2817 C CA  . HIS A 355 ? 1.1587 0.6940 0.7170 0.2151  -0.1158 -0.0502 651 HIS A CA  
2818 C C   . HIS A 355 ? 1.2077 0.8032 0.7805 0.2665  -0.1058 -0.0584 651 HIS A C   
2819 O O   . HIS A 355 ? 1.1341 0.8299 0.7868 0.2554  -0.0966 -0.0588 651 HIS A O   
2820 C CB  . HIS A 355 ? 1.2433 0.7394 0.7913 0.1653  -0.1210 -0.0486 651 HIS A CB  
2821 C CG  . HIS A 355 ? 1.2830 0.6575 0.7223 0.1731  -0.1294 -0.0531 651 HIS A CG  
2822 N ND1 . HIS A 355 ? 1.3545 0.6130 0.7017 0.1604  -0.1407 -0.0499 651 HIS A ND1 
2823 C CD2 . HIS A 355 ? 1.3576 0.7008 0.7581 0.1880  -0.1286 -0.0606 651 HIS A CD2 
2824 C CE1 . HIS A 355 ? 1.4945 0.6495 0.7467 0.1667  -0.1472 -0.0558 651 HIS A CE1 
2825 N NE2 . HIS A 355 ? 1.4366 0.6425 0.7203 0.1861  -0.1399 -0.0629 651 HIS A NE2 
2826 N N   . HIS A 356 ? 1.2603 0.7963 0.7524 0.3229  -0.1071 -0.0647 652 HIS A N   
2827 C CA  . HIS A 356 ? 1.2232 0.8293 0.7269 0.3778  -0.0964 -0.0727 652 HIS A CA  
2828 C C   . HIS A 356 ? 1.1891 0.9067 0.7538 0.4067  -0.0903 -0.0717 652 HIS A C   
2829 O O   . HIS A 356 ? 1.0785 0.9149 0.7153 0.4092  -0.0793 -0.0737 652 HIS A O   
2830 C CB  . HIS A 356 ? 1.3549 0.8578 0.7439 0.4353  -0.0999 -0.0805 652 HIS A CB  
2831 C CG  . HIS A 356 ? 1.4501 0.8331 0.7658 0.4043  -0.1078 -0.0824 652 HIS A CG  
2832 N ND1 . HIS A 356 ? 1.3929 0.8003 0.7305 0.3839  -0.1025 -0.0862 652 HIS A ND1 
2833 C CD2 . HIS A 356 ? 1.5284 0.7669 0.7464 0.3848  -0.1213 -0.0805 652 HIS A CD2 
2834 C CE1 . HIS A 356 ? 1.4932 0.7809 0.7524 0.3547  -0.1133 -0.0873 652 HIS A CE1 
2835 N NE2 . HIS A 356 ? 1.5476 0.7314 0.7328 0.3516  -0.1247 -0.0839 652 HIS A NE2 
2836 N N   . SER A 357 ? 1.2140 0.8958 0.7484 0.4238  -0.0981 -0.0680 653 SER A N   
2837 C CA  . SER A 357 ? 1.1513 0.9426 0.7421 0.4494  -0.0943 -0.0671 653 SER A CA  
2838 C C   . SER A 357 ? 1.0088 0.8990 0.7051 0.3917  -0.0893 -0.0625 653 SER A C   
2839 O O   . SER A 357 ? 0.9733 0.9838 0.7344 0.3990  -0.0815 -0.0644 653 SER A O   
2840 C CB  . SER A 357 ? 1.2038 0.9304 0.7353 0.4795  -0.1048 -0.0633 653 SER A CB  
2841 O OG  . SER A 357 ? 1.1825 1.0230 0.7570 0.5208  -0.1014 -0.0647 653 SER A OG  
2842 N N   . ALA A 358 ? 1.0255 0.8679 0.7357 0.3337  -0.0938 -0.0566 654 ALA A N   
2843 C CA  . ALA A 358 ? 0.9550 0.8774 0.7532 0.2851  -0.0896 -0.0528 654 ALA A CA  
2844 C C   . ALA A 358 ? 0.9192 0.9173 0.7719 0.2687  -0.0793 -0.0557 654 ALA A C   
2845 O O   . ALA A 358 ? 0.7731 0.8664 0.6895 0.2554  -0.0730 -0.0558 654 ALA A O   
2846 C CB  . ALA A 358 ? 0.9283 0.7873 0.7244 0.2337  -0.0960 -0.0462 654 ALA A CB  
2847 N N   . THR A 359 ? 0.9066 0.8590 0.7291 0.2661  -0.0780 -0.0580 655 THR A N   
2848 C CA  . THR A 359 ? 0.8524 0.8709 0.7213 0.2483  -0.0683 -0.0594 655 THR A CA  
2849 C C   . THR A 359 ? 0.8397 0.9521 0.7259 0.2862  -0.0582 -0.0645 655 THR A C   
2850 O O   . THR A 359 ? 0.7774 0.9759 0.7193 0.2631  -0.0494 -0.0637 655 THR A O   
2851 C CB  . THR A 359 ? 0.9137 0.8636 0.7439 0.2369  -0.0701 -0.0605 655 THR A CB  
2852 O OG1 . THR A 359 ? 0.9395 0.8198 0.6898 0.2817  -0.0732 -0.0662 655 THR A OG1 
2853 C CG2 . THR A 359 ? 0.9109 0.8000 0.7403 0.1908  -0.0794 -0.0544 655 THR A CG2 
2854 N N   . GLU A 360 ? 0.8833 0.9831 0.7189 0.3441  -0.0595 -0.0693 656 GLU A N   
2855 C CA  . GLU A 360 ? 0.8869 1.0985 0.7451 0.3831  -0.0498 -0.0738 656 GLU A CA  
2856 C C   . GLU A 360 ? 0.8277 1.1410 0.7521 0.3643  -0.0489 -0.0708 656 GLU A C   
2857 O O   . GLU A 360 ? 0.7904 1.2170 0.7653 0.3529  -0.0393 -0.0716 656 GLU A O   
2858 C CB  . GLU A 360 ? 0.9903 1.1691 0.7757 0.4587  -0.0522 -0.0798 656 GLU A CB  
2859 C CG  . GLU A 360 ? 1.0576 1.3653 0.8647 0.5042  -0.0402 -0.0853 656 GLU A CG  
2860 C CD  . GLU A 360 ? 1.2337 1.5456 0.9869 0.5825  -0.0442 -0.0894 656 GLU A CD  
2861 O OE1 . GLU A 360 ? 1.3099 1.4939 0.9866 0.6041  -0.0558 -0.0885 656 GLU A OE1 
2862 O OE2 . GLU A 360 ? 1.2590 1.6886 1.0355 0.5972  -0.0370 -0.0894 656 GLU A OE2 
2863 N N   . SER A 361 ? 0.8293 1.1026 0.7501 0.3564  -0.0590 -0.0671 657 SER A N   
2864 C CA  A SER A 361 ? 0.7778 1.1398 0.7551 0.3369  -0.0595 -0.0650 657 SER A CA  
2865 C CA  B SER A 361 ? 0.8072 1.1678 0.7844 0.3364  -0.0596 -0.0650 657 SER A CA  
2866 C C   . SER A 361 ? 0.7608 1.1620 0.7981 0.2718  -0.0539 -0.0622 657 SER A C   
2867 O O   . SER A 361 ? 0.7160 1.2142 0.8004 0.2516  -0.0501 -0.0624 657 SER A O   
2868 C CB  A SER A 361 ? 0.8274 1.1277 0.7815 0.3413  -0.0712 -0.0615 657 SER A CB  
2869 C CB  B SER A 361 ? 0.7718 1.0683 0.7265 0.3383  -0.0714 -0.0612 657 SER A CB  
2870 O OG  A SER A 361 ? 0.8210 1.0688 0.7060 0.4029  -0.0774 -0.0632 657 SER A OG  
2871 O OG  B SER A 361 ? 0.8069 1.0439 0.7772 0.2841  -0.0741 -0.0566 657 SER A OG  
2872 N N   . PHE A 362 ? 0.7575 1.0830 0.7876 0.2386  -0.0543 -0.0595 658 PHE A N   
2873 C CA  . PHE A 362 ? 0.7213 1.0708 0.7962 0.1843  -0.0496 -0.0565 658 PHE A CA  
2874 C C   . PHE A 362 ? 0.7101 1.1395 0.8070 0.1762  -0.0381 -0.0581 658 PHE A C   
2875 O O   . PHE A 362 ? 0.6794 1.1664 0.8137 0.1376  -0.0336 -0.0564 658 PHE A O   
2876 C CB  . PHE A 362 ? 0.7114 0.9698 0.7715 0.1576  -0.0536 -0.0528 658 PHE A CB  
2877 C CG  . PHE A 362 ? 0.6618 0.9329 0.7586 0.1102  -0.0506 -0.0493 658 PHE A CG  
2878 C CD1 . PHE A 362 ? 0.6464 0.9307 0.7697 0.0860  -0.0533 -0.0479 658 PHE A CD1 
2879 C CD2 . PHE A 362 ? 0.6889 0.9549 0.7867 0.0926  -0.0452 -0.0477 658 PHE A CD2 
2880 C CE1 . PHE A 362 ? 0.6236 0.9070 0.7681 0.0478  -0.0508 -0.0453 658 PHE A CE1 
2881 C CE2 . PHE A 362 ? 0.6689 0.9355 0.7892 0.0533  -0.0432 -0.0439 658 PHE A CE2 
2882 C CZ  . PHE A 362 ? 0.6403 0.9122 0.7813 0.0325  -0.0460 -0.0430 658 PHE A CZ  
2883 N N   . ILE A 363 ? 0.7328 1.1621 0.8006 0.2095  -0.0328 -0.0612 659 ILE A N   
2884 C CA  . ILE A 363 ? 0.6875 1.2082 0.7756 0.2044  -0.0201 -0.0625 659 ILE A CA  
2885 C C   . ILE A 363 ? 0.6965 1.3384 0.8183 0.2111  -0.0169 -0.0642 659 ILE A C   
2886 O O   . ILE A 363 ? 0.6810 1.4052 0.8382 0.1716  -0.0093 -0.0623 659 ILE A O   
2887 C CB  . ILE A 363 ? 0.7683 1.2713 0.8140 0.2475  -0.0144 -0.0668 659 ILE A CB  
2888 C CG1 . ILE A 363 ? 0.7229 1.1104 0.7340 0.2338  -0.0192 -0.0652 659 ILE A CG1 
2889 C CG2 . ILE A 363 ? 0.7428 1.3523 0.8105 0.2414  0.0006  -0.0676 659 ILE A CG2 
2890 C CD1 . ILE A 363 ? 0.7238 1.1177 0.7551 0.1875  -0.0126 -0.0607 659 ILE A CD1 
2891 N N   . LYS A 364 ? 0.7129 1.3652 0.8197 0.2580  -0.0237 -0.0672 660 LYS A N   
2892 C CA  . LYS A 364 ? 0.6745 1.4477 0.8146 0.2652  -0.0234 -0.0686 660 LYS A CA  
2893 C C   . LYS A 364 ? 0.6427 1.4324 0.8222 0.2035  -0.0274 -0.0651 660 LYS A C   
2894 O O   . LYS A 364 ? 0.6353 1.5329 0.8505 0.1731  -0.0229 -0.0651 660 LYS A O   
2895 C CB  . LYS A 364 ? 0.6814 1.4452 0.7893 0.3309  -0.0324 -0.0715 660 LYS A CB  
2896 C CG  . LYS A 364 ? 0.7440 1.6270 0.8594 0.3555  -0.0290 -0.0732 660 LYS A CG  
2897 C CD  . LYS A 364 ? 0.9195 1.7762 0.9713 0.4273  -0.0280 -0.0765 660 LYS A CD  
2898 C CE  . LYS A 364 ? 0.9490 1.8497 0.9772 0.4610  -0.0334 -0.0766 660 LYS A CE  
2899 N NZ  . LYS A 364 ? 0.9901 1.8206 1.0053 0.4669  -0.0462 -0.0748 660 LYS A NZ  
2900 N N   . HIS A 365 ? 0.6950 1.3794 0.8644 0.1826  -0.0358 -0.0625 661 HIS A N   
2901 C CA  . HIS A 365 ? 0.6376 1.3208 0.8350 0.1272  -0.0389 -0.0602 661 HIS A CA  
2902 C C   . HIS A 365 ? 0.6723 1.3775 0.8870 0.0734  -0.0300 -0.0579 661 HIS A C   
2903 O O   . HIS A 365 ? 0.6139 1.3757 0.8505 0.0307  -0.0290 -0.0577 661 HIS A O   
2904 C CB  . HIS A 365 ? 0.6665 1.2353 0.8470 0.1190  -0.0472 -0.0577 661 HIS A CB  
2905 C CG  . HIS A 365 ? 0.6438 1.2033 0.8452 0.0699  -0.0497 -0.0565 661 HIS A CG  
2906 N ND1 . HIS A 365 ? 0.6549 1.1337 0.8510 0.0411  -0.0503 -0.0536 661 HIS A ND1 
2907 C CD2 . HIS A 365 ? 0.6050 1.2252 0.8273 0.0464  -0.0521 -0.0585 661 HIS A CD2 
2908 C CE1 . HIS A 365 ? 0.6245 1.1072 0.8330 0.0064  -0.0523 -0.0543 661 HIS A CE1 
2909 N NE2 . HIS A 365 ? 0.6461 1.2102 0.8693 0.0057  -0.0536 -0.0574 661 HIS A NE2 
2910 N N   . MET A 366 ? 0.6609 1.3133 0.8586 0.0719  -0.0244 -0.0558 662 MET A N   
2911 C CA  . MET A 366 ? 0.6651 1.3278 0.8694 0.0235  -0.0162 -0.0523 662 MET A CA  
2912 C C   . MET A 366 ? 0.6475 1.4365 0.8720 0.0069  -0.0071 -0.0531 662 MET A C   
2913 O O   . MET A 366 ? 0.6365 1.4526 0.8698 -0.0486 -0.0040 -0.0504 662 MET A O   
2914 C CB  . MET A 366 ? 0.6389 1.2354 0.8188 0.0330  -0.0122 -0.0500 662 MET A CB  
2915 C CG  . MET A 366 ? 0.6146 1.0991 0.7803 0.0183  -0.0196 -0.0465 662 MET A CG  
2916 S SD  . MET A 366 ? 0.6453 1.0702 0.7818 0.0291  -0.0162 -0.0441 662 MET A SD  
2917 C CE  . MET A 366 ? 0.6287 1.0465 0.7660 -0.0261 -0.0099 -0.0372 662 MET A CE  
2918 N N   . GLU A 367 ? 0.5638 1.4322 0.7909 0.0542  -0.0029 -0.0567 663 GLU A N   
2919 C CA  . GLU A 367 ? 0.6170 1.6288 0.8677 0.0413  0.0063  -0.0574 663 GLU A CA  
2920 C C   . GLU A 367 ? 0.6062 1.6730 0.8771 0.0018  0.0003  -0.0572 663 GLU A C   
2921 O O   . GLU A 367 ? 0.6542 1.7641 0.9227 -0.0519 0.0058  -0.0539 663 GLU A O   
2922 C CB  . GLU A 367 ? 0.6221 1.7062 0.8666 0.1124  0.0100  -0.0621 663 GLU A CB  
2923 C CG  . GLU A 367 ? 0.6886 1.7297 0.9039 0.1505  0.0181  -0.0635 663 GLU A CG  
2924 C CD  . GLU A 367 ? 0.7308 1.8181 0.9218 0.2258  0.0198  -0.0688 663 GLU A CD  
2925 O OE1 . GLU A 367 ? 0.7471 1.8842 0.9335 0.2404  0.0138  -0.0689 663 GLU A OE1 
2926 O OE2 . GLU A 367 ? 0.7330 1.7848 0.8950 0.2686  0.0258  -0.0723 663 GLU A OE2 
2927 N N   . ASN A 368 ? 0.6157 1.6526 0.8881 0.0262  -0.0117 -0.0599 664 ASN A N   
2928 C CA  . ASN A 368 ? 0.6641 1.7248 0.9392 -0.0082 -0.0177 -0.0597 664 ASN A CA  
2929 C C   . ASN A 368 ? 0.6994 1.7081 0.9757 -0.0791 -0.0193 -0.0576 664 ASN A C   
2930 O O   . ASN A 368 ? 0.7538 1.7919 1.0211 -0.1282 -0.0177 -0.0561 664 ASN A O   
2931 C CB  . ASN A 368 ? 0.6622 1.6969 0.9346 0.0369  -0.0296 -0.0626 664 ASN A CB  
2932 C CG  . ASN A 368 ? 0.6789 1.7477 0.9335 0.1089  -0.0287 -0.0645 664 ASN A CG  
2933 O OD1 . ASN A 368 ? 0.7329 1.8787 0.9807 0.1192  -0.0203 -0.0644 664 ASN A OD1 
2934 N ND2 . ASN A 368 ? 0.6190 1.6252 0.8580 0.1590  -0.0378 -0.0659 664 ASN A ND2 
2935 N N   . GLU A 369 ? 0.6901 1.5934 0.9578 -0.0827 -0.0220 -0.0566 665 GLU A N   
2936 C CA  . GLU A 369 ? 0.7080 1.5349 0.9587 -0.1411 -0.0232 -0.0542 665 GLU A CA  
2937 C C   . GLU A 369 ? 0.7468 1.6030 0.9871 -0.1933 -0.0129 -0.0500 665 GLU A C   
2938 O O   . GLU A 369 ? 0.7655 1.6131 0.9905 -0.2530 -0.0139 -0.0490 665 GLU A O   
2939 C CB  . GLU A 369 ? 0.6811 1.3749 0.9117 -0.1229 -0.0269 -0.0524 665 GLU A CB  
2940 C CG  . GLU A 369 ? 0.6705 1.3262 0.9046 -0.0836 -0.0365 -0.0553 665 GLU A CG  
2941 C CD  . GLU A 369 ? 0.6900 1.3030 0.9184 -0.1126 -0.0437 -0.0574 665 GLU A CD  
2942 O OE1 . GLU A 369 ? 0.7422 1.2599 0.9534 -0.1186 -0.0454 -0.0558 665 GLU A OE1 
2943 O OE2 . GLU A 369 ? 0.5730 1.2512 0.8122 -0.1273 -0.0479 -0.0609 665 GLU A OE2 
2944 N N   . TYR A 370 ? 0.7100 1.5944 0.9506 -0.1742 -0.0030 -0.0473 666 TYR A N   
2945 C CA  . TYR A 370 ? 0.7264 1.6411 0.9535 -0.2261 0.0077  -0.0420 666 TYR A CA  
2946 C C   . TYR A 370 ? 0.7557 1.7676 0.9783 -0.2516 0.0117  -0.0414 666 TYR A C   
2947 O O   . TYR A 370 ? 0.8049 1.8185 0.9995 -0.3058 0.0179  -0.0363 666 TYR A O   
2948 C CB  . TYR A 370 ? 0.7101 1.6158 0.9297 -0.1949 0.0176  -0.0391 666 TYR A CB  
2949 C CG  . TYR A 370 ? 0.7260 1.4897 0.9155 -0.1927 0.0144  -0.0353 666 TYR A CG  
2950 C CD1 . TYR A 370 ? 0.7084 1.3943 0.8978 -0.1450 0.0056  -0.0380 666 TYR A CD1 
2951 C CD2 . TYR A 370 ? 0.7969 1.5065 0.9546 -0.2402 0.0195  -0.0282 666 TYR A CD2 
2952 C CE1 . TYR A 370 ? 0.7450 1.3185 0.9108 -0.1438 0.0018  -0.0344 666 TYR A CE1 
2953 C CE2 . TYR A 370 ? 0.8169 1.4050 0.9471 -0.2328 0.0152  -0.0244 666 TYR A CE2 
2954 C CZ  . TYR A 370 ? 0.7856 1.3134 0.9237 -0.1844 0.0063  -0.0278 666 TYR A CZ  
2955 O OH  . TYR A 370 ? 0.8339 1.2576 0.9485 -0.1773 0.0013  -0.0239 666 TYR A OH  
2956 N N   . ARG A 371 ? 0.7598 1.8390 0.9983 -0.2130 0.0071  -0.0458 667 ARG A N   
2957 C CA  . ARG A 371 ? 0.8149 1.9875 1.0442 -0.2322 0.0093  -0.0453 667 ARG A CA  
2958 C C   . ARG A 371 ? 0.8664 2.0147 1.0802 -0.2781 0.0012  -0.0461 667 ARG A C   
2959 O O   . ARG A 371 ? 0.8698 2.0249 1.0546 -0.3385 0.0038  -0.0428 667 ARG A O   
2960 C CB  . ARG A 371 ? 0.8280 2.0884 1.0742 -0.1640 0.0088  -0.0492 667 ARG A CB  
2961 C CG  . ARG A 371 ? 0.8895 2.2639 1.1278 -0.1774 0.0104  -0.0489 667 ARG A CG  
2962 C CD  . ARG A 371 ? 0.9375 2.3839 1.1847 -0.1026 0.0080  -0.0530 667 ARG A CD  
2963 N NE  . ARG A 371 ? 0.9522 2.3289 1.2081 -0.0540 -0.0007 -0.0566 667 ARG A NE  
2964 C CZ  . ARG A 371 ? 1.0246 2.3810 1.2834 -0.0598 -0.0104 -0.0583 667 ARG A CZ  
2965 N NH1 . ARG A 371 ? 1.0701 2.4685 1.3234 -0.1107 -0.0124 -0.0575 667 ARG A NH1 
2966 N NH2 . ARG A 371 ? 1.0219 2.3123 1.2850 -0.0148 -0.0184 -0.0609 667 ARG A NH2 
2967 N N   . CYS A 372 ? 0.8451 1.9596 1.0722 -0.2509 -0.0089 -0.0505 668 CYS A N   
2968 C CA  . CYS A 372 ? 0.8738 1.9699 1.0868 -0.2855 -0.0170 -0.0525 668 CYS A CA  
2969 C C   . CYS A 372 ? 0.8910 1.8646 1.0829 -0.3224 -0.0222 -0.0529 668 CYS A C   
2970 O O   . CYS A 372 ? 0.9230 1.8651 1.1002 -0.3448 -0.0298 -0.0558 668 CYS A O   
2971 C CB  . CYS A 372 ? 0.9207 2.0548 1.1548 -0.2344 -0.0253 -0.0570 668 CYS A CB  
2972 S SG  . CYS A 372 ? 1.0632 2.1092 1.3164 -0.1808 -0.0347 -0.0606 668 CYS A SG  
2973 N N   . ARG A 373 ? 0.8511 1.7546 1.0372 -0.3276 -0.0186 -0.0503 669 ARG A N   
2974 C CA  . ARG A 373 ? 0.8442 1.6271 1.0032 -0.3570 -0.0241 -0.0510 669 ARG A CA  
2975 C C   . ARG A 373 ? 0.8577 1.5761 0.9846 -0.3919 -0.0170 -0.0450 669 ARG A C   
2976 O O   . ARG A 373 ? 0.8825 1.4934 0.9682 -0.4236 -0.0206 -0.0445 669 ARG A O   
2977 C CB  . ARG A 373 ? 0.7855 1.5233 0.9712 -0.3110 -0.0327 -0.0558 669 ARG A CB  
2978 C CG  . ARG A 373 ? 0.7657 1.3926 0.9209 -0.3340 -0.0406 -0.0592 669 ARG A CG  
2979 C CD  . ARG A 373 ? 0.7524 1.3014 0.9146 -0.2764 -0.0438 -0.0595 669 ARG A CD  
2980 N NE  . ARG A 373 ? 0.7511 1.2101 0.8843 -0.2869 -0.0502 -0.0634 669 ARG A NE  
2981 C CZ  . ARG A 373 ? 0.7473 1.1228 0.8738 -0.2526 -0.0520 -0.0630 669 ARG A CZ  
2982 N NH1 . ARG A 373 ? 0.7012 1.0652 0.8459 -0.2111 -0.0493 -0.0587 669 ARG A NH1 
2983 N NH2 . ARG A 373 ? 0.7740 1.0792 0.8721 -0.2611 -0.0566 -0.0673 669 ARG A NH2 
2984 N N   . GLY A 374 ? 0.8428 1.6197 0.9820 -0.3829 -0.0071 -0.0405 670 GLY A N   
2985 C CA  . GLY A 374 ? 0.8499 1.5726 0.9561 -0.4163 0.0004  -0.0336 670 GLY A CA  
2986 C C   . GLY A 374 ? 0.8806 1.5253 0.9913 -0.3841 0.0003  -0.0319 670 GLY A C   
2987 O O   . GLY A 374 ? 0.9083 1.4871 0.9821 -0.4055 0.0056  -0.0249 670 GLY A O   
2988 N N   . GLY A 375 ? 0.8403 1.4662 0.9786 -0.3226 -0.0059 -0.0364 671 GLY A N   
2989 C CA  . GLY A 375 ? 0.8386 1.3700 0.9675 -0.2818 -0.0072 -0.0339 671 GLY A CA  
2990 C C   . GLY A 375 ? 0.8089 1.3154 0.9603 -0.2308 -0.0161 -0.0391 671 GLY A C   
2991 O O   . GLY A 375 ? 0.7694 1.3209 0.9402 -0.2254 -0.0214 -0.0444 671 GLY A O   
2992 N N   . CYS A 376 ? 0.7462 1.1810 0.8916 -0.1966 -0.0180 -0.0368 672 CYS A N   
2993 C CA  . CYS A 376 ? 0.7221 1.1227 0.8814 -0.1534 -0.0258 -0.0399 672 CYS A CA  
2994 C C   . CYS A 376 ? 0.6931 1.0016 0.8335 -0.1410 -0.0285 -0.0357 672 CYS A C   
2995 O O   . CYS A 376 ? 0.7044 1.0052 0.8405 -0.1254 -0.0255 -0.0325 672 CYS A O   
2996 C CB  . CYS A 376 ? 0.6904 1.1526 0.8728 -0.1094 -0.0250 -0.0427 672 CYS A CB  
2997 S SG  . CYS A 376 ? 0.6279 1.0425 0.8155 -0.0635 -0.0349 -0.0453 672 CYS A SG  
2998 N N   . PRO A 377 ? 0.7399 0.9824 0.8665 -0.1459 -0.0342 -0.0358 673 PRO A N   
2999 C CA  . PRO A 377 ? 0.7007 0.8731 0.8143 -0.1276 -0.0378 -0.0317 673 PRO A CA  
3000 C C   . PRO A 377 ? 0.6970 0.8799 0.8305 -0.0908 -0.0412 -0.0322 673 PRO A C   
3001 O O   . PRO A 377 ? 0.5662 0.7730 0.7168 -0.0740 -0.0443 -0.0361 673 PRO A O   
3002 C CB  . PRO A 377 ? 0.7571 0.8785 0.8573 -0.1314 -0.0429 -0.0338 673 PRO A CB  
3003 C CG  . PRO A 377 ? 0.6815 0.8468 0.7946 -0.1441 -0.0434 -0.0401 673 PRO A CG  
3004 C CD  . PRO A 377 ? 0.6994 0.9350 0.8214 -0.1642 -0.0379 -0.0403 673 PRO A CD  
3005 N N   . ALA A 378 ? 0.5929 0.7520 0.7169 -0.0801 -0.0413 -0.0280 674 ALA A N   
3006 C CA  . ALA A 378 ? 0.5901 0.7488 0.7212 -0.0512 -0.0453 -0.0287 674 ALA A CA  
3007 C C   . ALA A 378 ? 0.6234 0.7359 0.7404 -0.0459 -0.0499 -0.0237 674 ALA A C   
3008 O O   . ALA A 378 ? 0.6325 0.7290 0.7333 -0.0574 -0.0472 -0.0196 674 ALA A O   
3009 C CB  . ALA A 378 ? 0.6140 0.8209 0.7471 -0.0381 -0.0399 -0.0316 674 ALA A CB  
3010 N N   . ASP A 379 ? 0.5871 0.6806 0.7077 -0.0312 -0.0573 -0.0236 675 ASP A N   
3011 C CA  . ASP A 379 ? 0.6041 0.6665 0.7155 -0.0279 -0.0640 -0.0189 675 ASP A CA  
3012 C C   . ASP A 379 ? 0.6493 0.7073 0.7484 -0.0168 -0.0671 -0.0201 675 ASP A C   
3013 O O   . ASP A 379 ? 0.5902 0.6418 0.6872 -0.0091 -0.0719 -0.0221 675 ASP A O   
3014 C CB  . ASP A 379 ? 0.6237 0.6766 0.7453 -0.0250 -0.0702 -0.0176 675 ASP A CB  
3015 C CG  . ASP A 379 ? 0.6484 0.6863 0.7634 -0.0217 -0.0775 -0.0121 675 ASP A CG  
3016 O OD1 . ASP A 379 ? 0.6484 0.6781 0.7497 -0.0217 -0.0800 -0.0101 675 ASP A OD1 
3017 O OD2 . ASP A 379 ? 0.6567 0.6956 0.7789 -0.0172 -0.0810 -0.0101 675 ASP A OD2 
3018 N N   . TRP A 380 ? 0.5938 0.6481 0.6771 -0.0174 -0.0642 -0.0187 676 TRP A N   
3019 C CA  . TRP A 380 ? 0.5920 0.6339 0.6534 -0.0056 -0.0666 -0.0211 676 TRP A CA  
3020 C C   . TRP A 380 ? 0.5763 0.5883 0.6274 -0.0065 -0.0784 -0.0196 676 TRP A C   
3021 O O   . TRP A 380 ? 0.5665 0.5582 0.5958 0.0014  -0.0823 -0.0232 676 TRP A O   
3022 C CB  . TRP A 380 ? 0.6174 0.6573 0.6617 -0.0089 -0.0621 -0.0188 676 TRP A CB  
3023 C CG  . TRP A 380 ? 0.6167 0.6497 0.6336 0.0066  -0.0604 -0.0234 676 TRP A CG  
3024 C CD1 . TRP A 380 ? 0.6219 0.6866 0.6324 0.0190  -0.0495 -0.0277 676 TRP A CD1 
3025 C CD2 . TRP A 380 ? 0.6412 0.6337 0.6274 0.0116  -0.0699 -0.0245 676 TRP A CD2 
3026 N NE1 . TRP A 380 ? 0.7056 0.7462 0.6803 0.0372  -0.0506 -0.0320 676 TRP A NE1 
3027 C CE2 . TRP A 380 ? 0.6746 0.6649 0.6310 0.0303  -0.0636 -0.0303 676 TRP A CE2 
3028 C CE3 . TRP A 380 ? 0.6020 0.5649 0.5808 0.0006  -0.0831 -0.0213 676 TRP A CE3 
3029 C CZ2 . TRP A 380 ? 0.7116 0.6552 0.6235 0.0385  -0.0709 -0.0341 676 TRP A CZ2 
3030 C CZ3 . TRP A 380 ? 0.6972 0.6216 0.6353 0.0023  -0.0911 -0.0242 676 TRP A CZ3 
3031 C CH2 . TRP A 380 ? 0.6557 0.5636 0.5579 0.0209  -0.0852 -0.0309 676 TRP A CH2 
3032 N N   . VAL A 381 ? 0.5876 0.5960 0.6478 -0.0164 -0.0849 -0.0140 677 VAL A N   
3033 C CA  . VAL A 381 ? 0.5801 0.5776 0.6341 -0.0232 -0.0966 -0.0117 677 VAL A CA  
3034 C C   . VAL A 381 ? 0.6423 0.6359 0.6968 -0.0248 -0.0986 -0.0144 677 VAL A C   
3035 O O   . VAL A 381 ? 0.5909 0.5613 0.6208 -0.0331 -0.1066 -0.0147 677 VAL A O   
3036 C CB  . VAL A 381 ? 0.6186 0.6326 0.6898 -0.0270 -0.1021 -0.0054 677 VAL A CB  
3037 C CG1 . VAL A 381 ? 0.6232 0.6458 0.6924 -0.0381 -0.1140 -0.0026 677 VAL A CG1 
3038 C CG2 . VAL A 381 ? 0.6612 0.6672 0.7205 -0.0239 -0.1019 -0.0013 677 VAL A CG2 
3039 N N   . TRP A 382 ? 0.6501 0.6616 0.7263 -0.0199 -0.0920 -0.0161 678 TRP A N   
3040 C CA  . TRP A 382 ? 0.6487 0.6565 0.7241 -0.0205 -0.0934 -0.0176 678 TRP A CA  
3041 C C   . TRP A 382 ? 0.6501 0.6441 0.7054 -0.0048 -0.0894 -0.0230 678 TRP A C   
3042 O O   . TRP A 382 ? 0.6769 0.6460 0.7100 -0.0031 -0.0935 -0.0236 678 TRP A O   
3043 C CB  . TRP A 382 ? 0.6398 0.6751 0.7462 -0.0219 -0.0897 -0.0167 678 TRP A CB  
3044 C CG  . TRP A 382 ? 0.6639 0.7145 0.7831 -0.0314 -0.0952 -0.0118 678 TRP A CG  
3045 C CD1 . TRP A 382 ? 0.6759 0.7372 0.7998 -0.0324 -0.0993 -0.0077 678 TRP A CD1 
3046 C CD2 . TRP A 382 ? 0.7051 0.7707 0.8329 -0.0390 -0.0970 -0.0100 678 TRP A CD2 
3047 N NE1 . TRP A 382 ? 0.6684 0.7591 0.8066 -0.0374 -0.1037 -0.0039 678 TRP A NE1 
3048 C CE2 . TRP A 382 ? 0.6880 0.7829 0.8293 -0.0437 -0.1016 -0.0053 678 TRP A CE2 
3049 C CE3 . TRP A 382 ? 0.6868 0.7469 0.8100 -0.0412 -0.0953 -0.0115 678 TRP A CE3 
3050 C CZ2 . TRP A 382 ? 0.6967 0.8237 0.8501 -0.0523 -0.1030 -0.0022 678 TRP A CZ2 
3051 C CZ3 . TRP A 382 ? 0.7252 0.8070 0.8569 -0.0525 -0.0968 -0.0080 678 TRP A CZ3 
3052 C CH2 . TRP A 382 ? 0.7232 0.8420 0.8715 -0.0587 -0.0999 -0.0036 678 TRP A CH2 
3053 N N   . ILE A 383 ? 0.6165 0.6277 0.6749 0.0076  -0.0816 -0.0263 679 ILE A N   
3054 C CA  . ILE A 383 ? 0.6471 0.6613 0.6893 0.0297  -0.0776 -0.0315 679 ILE A CA  
3055 C C   . ILE A 383 ? 0.7216 0.6885 0.7143 0.0438  -0.0820 -0.0342 679 ILE A C   
3056 O O   . ILE A 383 ? 0.7085 0.6499 0.6696 0.0639  -0.0838 -0.0374 679 ILE A O   
3057 C CB  . ILE A 383 ? 0.6340 0.6982 0.6972 0.0356  -0.0672 -0.0339 679 ILE A CB  
3058 C CG1 . ILE A 383 ? 0.5566 0.6531 0.6548 0.0195  -0.0642 -0.0325 679 ILE A CG1 
3059 C CG2 . ILE A 383 ? 0.6051 0.6885 0.6517 0.0650  -0.0630 -0.0394 679 ILE A CG2 
3060 C CD1 . ILE A 383 ? 0.6255 0.7375 0.7318 0.0283  -0.0654 -0.0351 679 ILE A CD1 
3061 N N   . VAL A 384 ? 0.6722 0.6192 0.6492 0.0353  -0.0848 -0.0332 680 VAL A N   
3062 C CA  . VAL A 384 ? 0.7237 0.6166 0.6437 0.0481  -0.0893 -0.0373 680 VAL A CA  
3063 C C   . VAL A 384 ? 0.7575 0.5932 0.6411 0.0339  -0.1009 -0.0355 680 VAL A C   
3064 O O   . VAL A 384 ? 0.7118 0.5529 0.6133 0.0040  -0.1076 -0.0299 680 VAL A O   
3065 C CB  . VAL A 384 ? 0.7294 0.6159 0.6393 0.0396  -0.0901 -0.0367 680 VAL A CB  
3066 C CG1 . VAL A 384 ? 0.7649 0.5818 0.6061 0.0472  -0.0974 -0.0416 680 VAL A CG1 
3067 C CG2 . VAL A 384 ? 0.7172 0.6535 0.6499 0.0527  -0.0774 -0.0382 680 VAL A CG2 
3068 N N   . PRO A 385 ? 0.8381 0.6187 0.6658 0.0539  -0.1036 -0.0397 681 PRO A N   
3069 C CA  . PRO A 385 ? 0.8801 0.5961 0.6620 0.0341  -0.1147 -0.0369 681 PRO A CA  
3070 C C   . PRO A 385 ? 0.9652 0.6459 0.7197 -0.0013 -0.1252 -0.0346 681 PRO A C   
3071 O O   . PRO A 385 ? 0.9861 0.6655 0.7321 0.0013  -0.1251 -0.0375 681 PRO A O   
3072 C CB  . PRO A 385 ? 0.9341 0.5837 0.6446 0.0713  -0.1152 -0.0428 681 PRO A CB  
3073 C CG  . PRO A 385 ? 0.9207 0.6349 0.6678 0.1111  -0.1032 -0.0471 681 PRO A CG  
3074 C CD  . PRO A 385 ? 0.8553 0.6367 0.6591 0.0982  -0.0961 -0.0465 681 PRO A CD  
3075 N N   . PRO A 386 ? 0.9721 0.6278 0.7098 -0.0371 -0.1347 -0.0291 682 PRO A N   
3076 C CA  . PRO A 386 ? 1.0035 0.6442 0.7215 -0.0779 -0.1461 -0.0260 682 PRO A CA  
3077 C C   . PRO A 386 ? 1.0964 0.6379 0.7195 -0.0838 -0.1556 -0.0312 682 PRO A C   
3078 O O   . PRO A 386 ? 1.1318 0.6536 0.7273 -0.1252 -0.1675 -0.0287 682 PRO A O   
3079 C CB  . PRO A 386 ? 0.9899 0.6528 0.7257 -0.1150 -0.1510 -0.0179 682 PRO A CB  
3080 C CG  . PRO A 386 ? 1.0252 0.6514 0.7368 -0.0955 -0.1466 -0.0186 682 PRO A CG  
3081 C CD  . PRO A 386 ? 0.9612 0.6129 0.7007 -0.0452 -0.1351 -0.0247 682 PRO A CD  
3082 N N   . MET A 387 ? 1.1398 0.6188 0.7076 -0.0429 -0.1513 -0.0386 683 MET A N   
3083 C CA  . MET A 387 ? 1.2214 0.5987 0.6911 -0.0374 -0.1588 -0.0458 683 MET A CA  
3084 C C   . MET A 387 ? 1.2458 0.6214 0.7043 0.0247  -0.1470 -0.0548 683 MET A C   
3085 O O   . MET A 387 ? 1.1656 0.6040 0.6777 0.0577  -0.1356 -0.0545 683 MET A O   
3086 C CB  . MET A 387 ? 1.3458 0.6102 0.7180 -0.0556 -0.1695 -0.0450 683 MET A CB  
3087 C CG  . MET A 387 ? 1.3218 0.5524 0.6675 -0.0077 -0.1628 -0.0469 683 MET A CG  
3088 S SD  . MET A 387 ? 1.6203 0.7036 0.8393 -0.0252 -0.1752 -0.0440 683 MET A SD  
3089 C CE  . MET A 387 ? 1.5948 0.5331 0.6765 -0.0100 -0.1842 -0.0552 683 MET A CE  
3090 N N   . SER A 388 ? 1.3201 0.6291 0.7075 0.0393  -0.1499 -0.0629 684 SER A N   
3091 C CA  . SER A 388 ? 1.3416 0.6464 0.7048 0.1016  -0.1385 -0.0724 684 SER A CA  
3092 C C   . SER A 388 ? 1.2410 0.6722 0.7055 0.1217  -0.1230 -0.0708 684 SER A C   
3093 O O   . SER A 388 ? 1.2437 0.7081 0.7144 0.1716  -0.1112 -0.0758 684 SER A O   
3094 C CB  . SER A 388 ? 1.3863 0.6252 0.6845 0.1471  -0.1373 -0.0764 684 SER A CB  
3095 O OG  . SER A 388 ? 1.5165 0.6217 0.7064 0.1264  -0.1519 -0.0772 684 SER A OG  
3096 N N   . GLY A 389 ? 1.1220 0.6243 0.6611 0.0831  -0.1235 -0.0636 685 GLY A N   
3097 C CA  . GLY A 389 ? 1.0535 0.6618 0.6800 0.0929  -0.1103 -0.0605 685 GLY A CA  
3098 C C   . GLY A 389 ? 1.0654 0.7081 0.6894 0.1392  -0.0959 -0.0674 685 GLY A C   
3099 O O   . GLY A 389 ? 1.0133 0.7138 0.6730 0.1656  -0.0857 -0.0678 685 GLY A O   
3100 N N   . SER A 390 ? 1.0988 0.7105 0.6775 0.1497  -0.0949 -0.0732 686 SER A N   
3101 C CA  . SER A 390 ? 1.0966 0.7612 0.6824 0.1878  -0.0792 -0.0786 686 SER A CA  
3102 C C   . SER A 390 ? 1.1298 0.7709 0.6609 0.2468  -0.0727 -0.0880 686 SER A C   
3103 O O   . SER A 390 ? 1.1558 0.8624 0.7003 0.2819  -0.0579 -0.0923 686 SER A O   
3104 C CB  . SER A 390 ? 1.0697 0.7158 0.6270 0.1791  -0.0792 -0.0812 686 SER A CB  
3105 O OG  . SER A 390 ? 1.1341 0.6726 0.6042 0.1766  -0.0923 -0.0873 686 SER A OG  
3106 N N   . ILE A 391 ? 1.2078 0.7581 0.6722 0.2604  -0.0832 -0.0912 687 ILE A N   
3107 C CA  . ILE A 391 ? 1.2156 0.7498 0.6305 0.3248  -0.0773 -0.0990 687 ILE A CA  
3108 C C   . ILE A 391 ? 1.2015 0.8068 0.6754 0.3362  -0.0736 -0.0938 687 ILE A C   
3109 O O   . ILE A 391 ? 1.2692 0.8667 0.7052 0.3910  -0.0710 -0.0988 687 ILE A O   
3110 C CB  . ILE A 391 ? 1.3612 0.7455 0.6522 0.3455  -0.0900 -0.1059 687 ILE A CB  
3111 C CG1 . ILE A 391 ? 1.4698 0.7861 0.7454 0.3040  -0.1052 -0.0983 687 ILE A CG1 
3112 C CG2 . ILE A 391 ? 1.4463 0.7526 0.6624 0.3414  -0.0936 -0.1139 687 ILE A CG2 
3113 C CD1 . ILE A 391 ? 1.6031 0.7625 0.7448 0.3240  -0.1175 -0.1040 687 ILE A CD1 
3114 N N   . THR A 392 ? 1.1401 0.8143 0.7025 0.2882  -0.0739 -0.0842 688 THR A N   
3115 C CA  . THR A 392 ? 1.0840 0.8482 0.7152 0.2936  -0.0679 -0.0799 688 THR A CA  
3116 C C   . THR A 392 ? 1.0070 0.8913 0.7134 0.2867  -0.0534 -0.0784 688 THR A C   
3117 O O   . THR A 392 ? 1.0027 0.8965 0.7252 0.2582  -0.0507 -0.0765 688 THR A O   
3118 C CB  . THR A 392 ? 1.0784 0.8309 0.7466 0.2465  -0.0774 -0.0711 688 THR A CB  
3119 O OG1 . THR A 392 ? 0.9398 0.7289 0.6646 0.1974  -0.0771 -0.0652 688 THR A OG1 
3120 C CG2 . THR A 392 ? 1.1383 0.7687 0.7276 0.2380  -0.0921 -0.0707 688 THR A CG2 
3121 N N   . PRO A 393 ? 0.9559 0.9327 0.7035 0.3106  -0.0445 -0.0788 689 PRO A N   
3122 C CA  . PRO A 393 ? 0.8998 0.9906 0.7066 0.3011  -0.0300 -0.0776 689 PRO A CA  
3123 C C   . PRO A 393 ? 0.8484 0.9724 0.7196 0.2405  -0.0300 -0.0690 689 PRO A C   
3124 O O   . PRO A 393 ? 0.8415 1.0331 0.7460 0.2222  -0.0193 -0.0667 689 PRO A O   
3125 C CB  . PRO A 393 ? 0.9162 1.0950 0.7439 0.3397  -0.0239 -0.0803 689 PRO A CB  
3126 C CG  . PRO A 393 ? 0.9243 1.0503 0.7463 0.3354  -0.0367 -0.0773 689 PRO A CG  
3127 C CD  . PRO A 393 ? 0.9779 0.9662 0.7244 0.3380  -0.0483 -0.0789 689 PRO A CD  
3128 N N   . VAL A 394 ? 0.8266 0.9050 0.7112 0.2102  -0.0411 -0.0638 690 VAL A N   
3129 C CA  . VAL A 394 ? 0.7635 0.8672 0.7007 0.1609  -0.0412 -0.0564 690 VAL A CA  
3130 C C   . VAL A 394 ? 0.8063 0.8713 0.7320 0.1358  -0.0432 -0.0533 690 VAL A C   
3131 O O   . VAL A 394 ? 0.7083 0.8013 0.6687 0.1038  -0.0402 -0.0474 690 VAL A O   
3132 C CB  . VAL A 394 ? 0.7869 0.8622 0.7420 0.1403  -0.0512 -0.0522 690 VAL A CB  
3133 C CG1 . VAL A 394 ? 0.7199 0.8496 0.6987 0.1563  -0.0489 -0.0537 690 VAL A CG1 
3134 C CG2 . VAL A 394 ? 0.8041 0.7879 0.7095 0.1435  -0.0633 -0.0526 690 VAL A CG2 
3135 N N   . PHE A 395 ? 0.8600 0.8559 0.7308 0.1500  -0.0493 -0.0571 691 PHE A N   
3136 C CA  . PHE A 395 ? 0.8350 0.7989 0.6914 0.1279  -0.0525 -0.0545 691 PHE A CA  
3137 C C   . PHE A 395 ? 0.8309 0.8547 0.7056 0.1255  -0.0390 -0.0533 691 PHE A C   
3138 O O   . PHE A 395 ? 0.8143 0.8374 0.7021 0.0968  -0.0399 -0.0471 691 PHE A O   
3139 C CB  . PHE A 395 ? 0.9014 0.7825 0.6859 0.1449  -0.0606 -0.0608 691 PHE A CB  
3140 C CG  . PHE A 395 ? 0.9213 0.7690 0.6864 0.1215  -0.0664 -0.0587 691 PHE A CG  
3141 C CD1 . PHE A 395 ? 0.9284 0.7978 0.6807 0.1320  -0.0566 -0.0609 691 PHE A CD1 
3142 C CD2 . PHE A 395 ? 0.8725 0.6731 0.6298 0.0894  -0.0817 -0.0543 691 PHE A CD2 
3143 C CE1 . PHE A 395 ? 0.9403 0.7774 0.6705 0.1117  -0.0631 -0.0588 691 PHE A CE1 
3144 C CE2 . PHE A 395 ? 0.9883 0.7658 0.7268 0.0691  -0.0888 -0.0523 691 PHE A CE2 
3145 C CZ  . PHE A 395 ? 0.9232 0.7149 0.6471 0.0811  -0.0800 -0.0546 691 PHE A CZ  
3146 N N   . HIS A 396 ? 0.8372 0.9159 0.7095 0.1562  -0.0264 -0.0586 692 HIS A N   
3147 C CA  . HIS A 396 ? 0.8430 0.9842 0.7237 0.1550  -0.0117 -0.0580 692 HIS A CA  
3148 C C   . HIS A 396 ? 0.8166 1.0433 0.7524 0.1285  -0.0024 -0.0521 692 HIS A C   
3149 O O   . HIS A 396 ? 0.8071 1.1009 0.7517 0.1232  0.0115  -0.0509 692 HIS A O   
3150 C CB  . HIS A 396 ? 0.9350 1.0952 0.7756 0.2058  -0.0025 -0.0677 692 HIS A CB  
3151 C CG  . HIS A 396 ? 0.9588 1.0182 0.7303 0.2331  -0.0131 -0.0749 692 HIS A CG  
3152 N ND1 . HIS A 396 ? 0.9716 0.9700 0.7038 0.2212  -0.0177 -0.0755 692 HIS A ND1 
3153 C CD2 . HIS A 396 ? 0.9964 0.9968 0.7230 0.2678  -0.0212 -0.0815 692 HIS A CD2 
3154 C CE1 . HIS A 396 ? 1.0424 0.9494 0.7076 0.2445  -0.0281 -0.0830 692 HIS A CE1 
3155 N NE2 . HIS A 396 ? 1.0530 0.9544 0.7103 0.2732  -0.0302 -0.0864 692 HIS A NE2 
3156 N N   . GLN A 397 ? 0.7782 1.0020 0.7462 0.1086  -0.0096 -0.0484 693 GLN A N   
3157 C CA  . GLN A 397 ? 0.7327 1.0262 0.7444 0.0823  -0.0031 -0.0444 693 GLN A CA  
3158 C C   . GLN A 397 ? 0.6928 0.9518 0.7176 0.0382  -0.0076 -0.0357 693 GLN A C   
3159 O O   . GLN A 397 ? 0.6615 0.8628 0.6873 0.0319  -0.0195 -0.0337 693 GLN A O   
3160 C CB  . GLN A 397 ? 0.7217 1.0333 0.7524 0.0969  -0.0083 -0.0476 693 GLN A CB  
3161 C CG  . GLN A 397 ? 0.6838 1.0615 0.7549 0.0660  -0.0039 -0.0444 693 GLN A CG  
3162 C CD  . GLN A 397 ? 0.6923 1.1708 0.7749 0.0645  0.0105  -0.0454 693 GLN A CD  
3163 O OE1 . GLN A 397 ? 0.6852 1.2152 0.7604 0.1057  0.0158  -0.0514 693 GLN A OE1 
3164 N NE2 . GLN A 397 ? 0.6935 1.2002 0.7885 0.0174  0.0173  -0.0391 693 GLN A NE2 
3165 N N   . GLU A 398 ? 0.7515 1.0444 0.7806 0.0090  0.0021  -0.0303 694 GLU A N   
3166 C CA  . GLU A 398 ? 0.7339 0.9885 0.7655 -0.0292 -0.0019 -0.0219 694 GLU A CA  
3167 C C   . GLU A 398 ? 0.7360 1.0036 0.7941 -0.0453 -0.0053 -0.0220 694 GLU A C   
3168 O O   . GLU A 398 ? 0.7071 1.0427 0.7844 -0.0464 0.0010  -0.0256 694 GLU A O   
3169 C CB  . GLU A 398 ? 0.7400 1.0178 0.7571 -0.0592 0.0095  -0.0153 694 GLU A CB  
3170 C CG  . GLU A 398 ? 0.7786 1.0310 0.7640 -0.0462 0.0118  -0.0141 694 GLU A CG  
3171 C CD  . GLU A 398 ? 0.8069 1.0908 0.7753 -0.0757 0.0252  -0.0072 694 GLU A CD  
3172 O OE1 . GLU A 398 ? 0.8548 1.1790 0.8341 -0.1097 0.0323  -0.0034 694 GLU A OE1 
3173 O OE2 . GLU A 398 ? 0.8692 1.1355 0.8090 -0.0685 0.0284  -0.0054 694 GLU A OE2 
3174 N N   . MET A 399 ? 0.6891 0.8968 0.7473 -0.0550 -0.0157 -0.0186 695 MET A N   
3175 C CA  . MET A 399 ? 0.7062 0.9149 0.7834 -0.0668 -0.0197 -0.0196 695 MET A CA  
3176 C C   . MET A 399 ? 0.7392 0.8951 0.8006 -0.0933 -0.0230 -0.0130 695 MET A C   
3177 O O   . MET A 399 ? 0.7787 0.8820 0.8247 -0.0859 -0.0299 -0.0087 695 MET A O   
3178 C CB  . MET A 399 ? 0.6617 0.8490 0.7512 -0.0410 -0.0297 -0.0239 695 MET A CB  
3179 C CG  . MET A 399 ? 0.6786 0.8902 0.7669 -0.0085 -0.0292 -0.0301 695 MET A CG  
3180 S SD  . MET A 399 ? 0.6265 0.7873 0.7116 0.0115  -0.0421 -0.0322 695 MET A SD  
3181 C CE  . MET A 399 ? 0.6500 0.8127 0.7070 0.0503  -0.0411 -0.0386 695 MET A CE  
3182 N N   . LEU A 400 ? 0.7290 0.8977 0.7885 -0.1230 -0.0189 -0.0123 696 LEU A N   
3183 C CA  . LEU A 400 ? 0.7510 0.8563 0.7836 -0.1450 -0.0226 -0.0073 696 LEU A CA  
3184 C C   . LEU A 400 ? 0.7666 0.8477 0.8135 -0.1302 -0.0312 -0.0114 696 LEU A C   
3185 O O   . LEU A 400 ? 0.7246 0.8451 0.7943 -0.1311 -0.0307 -0.0173 696 LEU A O   
3186 C CB  . LEU A 400 ? 0.7985 0.9178 0.8101 -0.1896 -0.0148 -0.0052 696 LEU A CB  
3187 C CG  . LEU A 400 ? 0.8343 0.9757 0.8241 -0.2134 -0.0047 0.0008  696 LEU A CG  
3188 C CD1 . LEU A 400 ? 0.9170 1.0861 0.8884 -0.2655 0.0027  0.0025  696 LEU A CD1 
3189 C CD2 . LEU A 400 ? 0.8922 0.9539 0.8415 -0.2104 -0.0082 0.0094  696 LEU A CD2 
3190 N N   . ASN A 401 ? 0.7825 0.8065 0.8163 -0.1148 -0.0390 -0.0080 697 ASN A N   
3191 C CA  . ASN A 401 ? 0.7788 0.7806 0.8208 -0.1018 -0.0456 -0.0110 697 ASN A CA  
3192 C C   . ASN A 401 ? 0.8633 0.8097 0.8666 -0.1200 -0.0455 -0.0094 697 ASN A C   
3193 O O   . ASN A 401 ? 0.9065 0.8039 0.8692 -0.1290 -0.0452 -0.0029 697 ASN A O   
3194 C CB  . ASN A 401 ? 0.7697 0.7544 0.8199 -0.0729 -0.0540 -0.0086 697 ASN A CB  
3195 C CG  . ASN A 401 ? 0.6864 0.6763 0.7567 -0.0583 -0.0587 -0.0126 697 ASN A CG  
3196 O OD1 . ASN A 401 ? 0.7333 0.7451 0.8171 -0.0653 -0.0560 -0.0180 697 ASN A OD1 
3197 N ND2 . ASN A 401 ? 0.6713 0.6480 0.7434 -0.0388 -0.0658 -0.0097 697 ASN A ND2 
3198 N N   . TYR A 402 ? 0.8645 0.8114 0.8721 -0.1254 -0.0461 -0.0153 698 TYR A N   
3199 C CA  . TYR A 402 ? 0.8972 0.7789 0.8591 -0.1387 -0.0473 -0.0159 698 TYR A CA  
3200 C C   . TYR A 402 ? 0.9446 0.8375 0.9232 -0.1313 -0.0495 -0.0240 698 TYR A C   
3201 O O   . TYR A 402 ? 0.8705 0.8260 0.8918 -0.1284 -0.0488 -0.0284 698 TYR A O   
3202 C CB  . TYR A 402 ? 0.9631 0.8279 0.8853 -0.1845 -0.0415 -0.0136 698 TYR A CB  
3203 C CG  . TYR A 402 ? 0.9346 0.8844 0.8905 -0.2114 -0.0356 -0.0175 698 TYR A CG  
3204 C CD1 . TYR A 402 ? 0.8878 0.8646 0.8526 -0.2289 -0.0363 -0.0249 698 TYR A CD1 
3205 C CD2 . TYR A 402 ? 0.8448 0.8531 0.8216 -0.2161 -0.0295 -0.0141 698 TYR A CD2 
3206 C CE1 . TYR A 402 ? 0.8517 0.9175 0.8480 -0.2494 -0.0321 -0.0281 698 TYR A CE1 
3207 C CE2 . TYR A 402 ? 0.8367 0.9339 0.8438 -0.2334 -0.0239 -0.0178 698 TYR A CE2 
3208 C CZ  . TYR A 402 ? 0.8725 1.0016 0.8908 -0.2494 -0.0257 -0.0245 698 TYR A CZ  
3209 O OH  . TYR A 402 ? 0.8507 1.0795 0.9002 -0.2625 -0.0212 -0.0278 698 TYR A OH  
3210 N N   . ARG A 403 ? 0.9930 0.8203 0.9322 -0.1235 -0.0524 -0.0257 699 ARG A N   
3211 C CA  . ARG A 403 ? 1.0520 0.8823 1.0019 -0.1081 -0.0545 -0.0331 699 ARG A CA  
3212 C C   . ARG A 403 ? 1.0453 0.8604 0.9676 -0.1444 -0.0529 -0.0397 699 ARG A C   
3213 O O   . ARG A 403 ? 1.1479 0.8905 1.0077 -0.1668 -0.0528 -0.0395 699 ARG A O   
3214 C CB  . ARG A 403 ? 1.1681 0.9421 1.0885 -0.0722 -0.0581 -0.0324 699 ARG A CB  
3215 C CG  . ARG A 403 ? 1.1761 0.9672 1.1170 -0.0406 -0.0614 -0.0251 699 ARG A CG  
3216 C CD  . ARG A 403 ? 1.2247 1.0474 1.1948 -0.0053 -0.0639 -0.0271 699 ARG A CD  
3217 N NE  . ARG A 403 ? 1.2592 1.1413 1.2756 -0.0141 -0.0621 -0.0320 699 ARG A NE  
3218 C CZ  . ARG A 403 ? 1.2751 1.1882 1.3151 0.0059  -0.0625 -0.0345 699 ARG A CZ  
3219 N NH1 . ARG A 403 ? 1.3632 1.2685 1.3926 0.0376  -0.0641 -0.0331 699 ARG A NH1 
3220 N NH2 . ARG A 403 ? 1.1625 1.1190 1.2349 -0.0047 -0.0611 -0.0380 699 ARG A NH2 
3221 N N   . LEU A 404 ? 0.9442 0.8235 0.9065 -0.1518 -0.0525 -0.0453 700 LEU A N   
3222 C CA  . LEU A 404 ? 0.9402 0.8169 0.8814 -0.1845 -0.0530 -0.0526 700 LEU A CA  
3223 C C   . LEU A 404 ? 0.9548 0.8268 0.9029 -0.1616 -0.0556 -0.0598 700 LEU A C   
3224 O O   . LEU A 404 ? 0.9434 0.8354 0.9240 -0.1245 -0.0561 -0.0585 700 LEU A O   
3225 C CB  . LEU A 404 ? 0.8749 0.8401 0.8532 -0.2122 -0.0512 -0.0534 700 LEU A CB  
3226 C CG  . LEU A 404 ? 0.8795 0.8765 0.8581 -0.2391 -0.0466 -0.0473 700 LEU A CG  
3227 C CD1 . LEU A 404 ? 0.8185 0.9174 0.8351 -0.2587 -0.0453 -0.0503 700 LEU A CD1 
3228 C CD2 . LEU A 404 ? 0.9782 0.8991 0.8885 -0.2786 -0.0453 -0.0444 700 LEU A CD2 
3229 N N   . THR A 405 ? 0.9467 0.7927 0.8600 -0.1879 -0.0573 -0.0675 701 THR A N   
3230 C CA  . THR A 405 ? 0.9398 0.7801 0.8532 -0.1698 -0.0592 -0.0752 701 THR A CA  
3231 C C   . THR A 405 ? 0.9050 0.7994 0.8319 -0.2026 -0.0621 -0.0815 701 THR A C   
3232 O O   . THR A 405 ? 0.9381 0.8495 0.8515 -0.2459 -0.0628 -0.0814 701 THR A O   
3233 C CB  . THR A 405 ? 1.0428 0.7775 0.8827 -0.1609 -0.0598 -0.0801 701 THR A CB  
3234 O OG1 . THR A 405 ? 1.0131 0.7482 0.8614 -0.1245 -0.0593 -0.0856 701 THR A OG1 
3235 C CG2 . THR A 405 ? 1.0526 0.7315 0.8275 -0.2101 -0.0625 -0.0864 701 THR A CG2 
3236 N N   . PRO A 406 ? 0.9022 0.8346 0.8574 -0.1844 -0.0639 -0.0862 702 PRO A N   
3237 C CA  . PRO A 406 ? 0.8691 0.8027 0.8462 -0.1401 -0.0623 -0.0859 702 PRO A CA  
3238 C C   . PRO A 406 ? 0.8393 0.8100 0.8623 -0.1117 -0.0601 -0.0766 702 PRO A C   
3239 O O   . PRO A 406 ? 0.8211 0.8346 0.8709 -0.1210 -0.0602 -0.0716 702 PRO A O   
3240 C CB  . PRO A 406 ? 0.8446 0.8294 0.8433 -0.1439 -0.0656 -0.0913 702 PRO A CB  
3241 C CG  . PRO A 406 ? 0.8650 0.8452 0.8312 -0.1888 -0.0698 -0.0980 702 PRO A CG  
3242 C CD  . PRO A 406 ? 0.8750 0.8546 0.8342 -0.2154 -0.0684 -0.0925 702 PRO A CD  
3243 N N   . SER A 407 ? 0.8343 0.7934 0.8648 -0.0779 -0.0581 -0.0745 703 SER A N   
3244 C CA  . SER A 407 ? 0.8181 0.8046 0.8825 -0.0579 -0.0574 -0.0658 703 SER A CA  
3245 C C   . SER A 407 ? 0.7969 0.8035 0.8808 -0.0306 -0.0561 -0.0643 703 SER A C   
3246 O O   . SER A 407 ? 0.7875 0.7757 0.8526 -0.0189 -0.0540 -0.0696 703 SER A O   
3247 C CB  . SER A 407 ? 0.8802 0.8231 0.9208 -0.0531 -0.0567 -0.0613 703 SER A CB  
3248 O OG  . SER A 407 ? 0.9247 0.8210 0.9333 -0.0285 -0.0556 -0.0634 703 SER A OG  
3249 N N   . PHE A 408 ? 0.7843 0.8285 0.9015 -0.0228 -0.0572 -0.0572 704 PHE A N   
3250 C CA  . PHE A 408 ? 0.7439 0.8100 0.8773 -0.0040 -0.0561 -0.0531 704 PHE A CA  
3251 C C   . PHE A 408 ? 0.8218 0.8769 0.9512 0.0114  -0.0562 -0.0484 704 PHE A C   
3252 O O   . PHE A 408 ? 0.8426 0.8876 0.9716 0.0055  -0.0585 -0.0447 704 PHE A O   
3253 C CB  . PHE A 408 ? 0.6444 0.7460 0.8031 -0.0087 -0.0586 -0.0476 704 PHE A CB  
3254 C CG  . PHE A 408 ? 0.6843 0.7990 0.8439 -0.0162 -0.0597 -0.0510 704 PHE A CG  
3255 C CD1 . PHE A 408 ? 0.6628 0.7851 0.8183 -0.0116 -0.0574 -0.0533 704 PHE A CD1 
3256 C CD2 . PHE A 408 ? 0.6701 0.7956 0.8332 -0.0251 -0.0628 -0.0518 704 PHE A CD2 
3257 C CE1 . PHE A 408 ? 0.6179 0.7516 0.7707 -0.0169 -0.0596 -0.0558 704 PHE A CE1 
3258 C CE2 . PHE A 408 ? 0.6500 0.7945 0.8127 -0.0272 -0.0653 -0.0545 704 PHE A CE2 
3259 C CZ  . PHE A 408 ? 0.6269 0.7722 0.7834 -0.0236 -0.0643 -0.0563 704 PHE A CZ  
3260 N N   . GLU A 409 ? 0.8561 0.9180 0.9810 0.0332  -0.0535 -0.0487 705 GLU A N   
3261 C CA  . GLU A 409 ? 0.9023 0.9633 1.0218 0.0549  -0.0545 -0.0444 705 GLU A CA  
3262 C C   . GLU A 409 ? 0.8553 0.9780 1.0031 0.0657  -0.0538 -0.0391 705 GLU A C   
3263 O O   . GLU A 409 ? 0.7885 0.9409 0.9482 0.0609  -0.0504 -0.0402 705 GLU A O   
3264 C CB  . GLU A 409 ? 1.0831 1.0928 1.1582 0.0783  -0.0520 -0.0505 705 GLU A CB  
3265 C CG  . GLU A 409 ? 1.1218 1.0628 1.1568 0.0593  -0.0528 -0.0557 705 GLU A CG  
3266 C CD  . GLU A 409 ? 1.2126 1.1316 1.2414 0.0472  -0.0566 -0.0496 705 GLU A CD  
3267 O OE1 . GLU A 409 ? 1.2671 1.2147 1.3165 0.0599  -0.0594 -0.0421 705 GLU A OE1 
3268 O OE2 . GLU A 409 ? 1.1881 1.0648 1.1897 0.0219  -0.0569 -0.0521 705 GLU A OE2 
3269 N N   . TYR A 410 ? 0.9703 1.1158 1.1270 0.0768  -0.0575 -0.0326 706 TYR A N   
3270 C CA  . TYR A 410 ? 0.8940 1.1082 1.0742 0.0859  -0.0571 -0.0275 706 TYR A CA  
3271 C C   . TYR A 410 ? 0.9387 1.1657 1.1041 0.1220  -0.0510 -0.0321 706 TYR A C   
3272 O O   . TYR A 410 ? 1.0755 1.2442 1.2040 0.1432  -0.0489 -0.0389 706 TYR A O   
3273 C CB  . TYR A 410 ? 0.9636 1.2078 1.1567 0.0871  -0.0644 -0.0194 706 TYR A CB  
3274 C CG  . TYR A 410 ? 0.9210 1.1506 1.1221 0.0560  -0.0703 -0.0154 706 TYR A CG  
3275 C CD1 . TYR A 410 ? 0.8397 1.0861 1.0532 0.0276  -0.0711 -0.0131 706 TYR A CD1 
3276 C CD2 . TYR A 410 ? 1.0681 1.2618 1.2567 0.0570  -0.0752 -0.0138 706 TYR A CD2 
3277 C CE1 . TYR A 410 ? 0.8606 1.0846 1.0711 0.0056  -0.0765 -0.0106 706 TYR A CE1 
3278 C CE2 . TYR A 410 ? 0.9821 1.1632 1.1739 0.0330  -0.0797 -0.0112 706 TYR A CE2 
3279 C CZ  . TYR A 410 ? 0.9332 1.1280 1.1346 0.0097  -0.0804 -0.0102 706 TYR A CZ  
3280 O OH  . TYR A 410 ? 0.8854 1.0586 1.0800 -0.0076 -0.0848 -0.0087 706 TYR A OH  
3281 N N   . GLN A 411 ? 0.8144 1.1181 1.0033 0.1285  -0.0480 -0.0283 707 GLN A N   
3282 C CA  . GLN A 411 ? 0.8335 1.1675 1.0111 0.1685  -0.0409 -0.0325 707 GLN A CA  
3283 C C   . GLN A 411 ? 0.7803 1.2221 0.9931 0.1704  -0.0407 -0.0244 707 GLN A C   
3284 O O   . GLN A 411 ? 0.7440 1.2239 0.9837 0.1300  -0.0443 -0.0171 707 GLN A O   
3285 C CB  . GLN A 411 ? 0.8099 1.1228 0.9729 0.1665  -0.0323 -0.0408 707 GLN A CB  
3286 C CG  . GLN A 411 ? 0.7381 1.1009 0.9300 0.1310  -0.0296 -0.0362 707 GLN A CG  
3287 C CD  . GLN A 411 ? 0.7354 1.0700 0.9094 0.1277  -0.0227 -0.0441 707 GLN A CD  
3288 O OE1 . GLN A 411 ? 0.7536 1.0585 0.8972 0.1585  -0.0173 -0.0534 707 GLN A OE1 
3289 N NE2 . GLN A 411 ? 0.6843 1.0217 0.8700 0.0917  -0.0238 -0.0405 707 GLN A NE2 
3290 N N   . PRO A 412 ? 0.7806 1.2736 0.9894 0.2160  -0.0370 -0.0253 708 PRO A N   
3291 C CA  . PRO A 412 ? 0.7581 1.3745 1.0040 0.2158  -0.0369 -0.0170 708 PRO A CA  
3292 C C   . PRO A 412 ? 0.7567 1.4298 1.0266 0.1756  -0.0300 -0.0139 708 PRO A C   
3293 O O   . PRO A 412 ? 0.7641 1.3958 1.0190 0.1697  -0.0224 -0.0201 708 PRO A O   
3294 C CB  . PRO A 412 ? 0.8211 1.4759 1.0497 0.2831  -0.0312 -0.0216 708 PRO A CB  
3295 C CG  . PRO A 412 ? 0.8887 1.4203 1.0632 0.3165  -0.0331 -0.0300 708 PRO A CG  
3296 C CD  . PRO A 412 ? 0.8802 1.3196 1.0434 0.2711  -0.0331 -0.0342 708 PRO A CD  
3297 N N   . ASP A 413 ? 0.7483 1.5143 1.0504 0.1447  -0.0335 -0.0038 709 ASP A N   
3298 C CA  . ASP A 413 ? 0.7285 1.5574 1.0464 0.1065  -0.0263 0.0010  709 ASP A CA  
3299 C C   . ASP A 413 ? 0.7532 1.6470 1.0709 0.1477  -0.0121 -0.0041 709 ASP A C   
3300 O O   . ASP A 413 ? 0.7767 1.7262 1.0961 0.1979  -0.0101 -0.0059 709 ASP A O   
3301 C CB  . ASP A 413 ? 0.7312 1.6502 1.0759 0.0615  -0.0335 0.0132  709 ASP A CB  
3302 C CG  . ASP A 413 ? 0.7844 1.6290 1.1191 0.0137  -0.0460 0.0175  709 ASP A CG  
3303 O OD1 . ASP A 413 ? 0.7933 1.5394 1.1060 -0.0007 -0.0457 0.0136  709 ASP A OD1 
3304 O OD2 . ASP A 413 ? 0.7960 1.6834 1.1424 -0.0074 -0.0566 0.0245  709 ASP A OD2 
3305 N N   . PRO A 414 ? 0.7655 1.6471 1.0740 0.1313  -0.0021 -0.0067 710 PRO A N   
3306 C CA  . PRO A 414 ? 0.7884 1.7091 1.0864 0.1776  0.0124  -0.0146 710 PRO A CA  
3307 C C   . PRO A 414 ? 0.8166 1.8601 1.1284 0.1905  0.0189  -0.0086 710 PRO A C   
3308 O O   . PRO A 414 ? 0.8712 1.9305 1.1610 0.2442  0.0277  -0.0158 710 PRO A O   
3309 C CB  . PRO A 414 ? 0.7169 1.5961 1.0007 0.1431  0.0196  -0.0161 710 PRO A CB  
3310 C CG  . PRO A 414 ? 0.7069 1.5626 0.9997 0.0771  0.0100  -0.0057 710 PRO A CG  
3311 C CD  . PRO A 414 ? 0.7525 1.5708 1.0513 0.0768  -0.0040 -0.0038 710 PRO A CD  
3312 N N   . TRP A 415 ? 0.7663 1.8700 1.0949 0.1387  0.0138  0.0039  711 TRP A N   
3313 C CA  . TRP A 415 ? 0.7797 1.9841 1.1072 0.1428  0.0188  0.0097  711 TRP A CA  
3314 C C   . TRP A 415 ? 0.7945 2.0223 1.1153 0.1940  0.0133  0.0081  711 TRP A C   
3315 O O   . TRP A 415 ? 0.7890 2.1027 1.1041 0.2153  0.0182  0.0103  711 TRP A O   
3316 C CB  . TRP A 415 ? 0.7410 1.9974 1.0785 0.0678  0.0148  0.0232  711 TRP A CB  
3317 C CG  . TRP A 415 ? 0.6935 1.9079 1.0381 0.0286  -0.0003 0.0290  711 TRP A CG  
3318 C CD1 . TRP A 415 ? 0.7008 1.9491 1.0497 0.0277  -0.0099 0.0337  711 TRP A CD1 
3319 C CD2 . TRP A 415 ? 0.6931 1.8239 1.0367 -0.0143 -0.0080 0.0306  711 TRP A CD2 
3320 N NE1 . TRP A 415 ? 0.7311 1.9184 1.0811 -0.0132 -0.0228 0.0375  711 TRP A NE1 
3321 C CE2 . TRP A 415 ? 0.7251 1.8387 1.0704 -0.0386 -0.0222 0.0357  711 TRP A CE2 
3322 C CE3 . TRP A 415 ? 0.6959 1.7661 1.0343 -0.0330 -0.0048 0.0280  711 TRP A CE3 
3323 C CZ2 . TRP A 415 ? 0.7355 1.7696 1.0740 -0.0790 -0.0333 0.0378  711 TRP A CZ2 
3324 C CZ3 . TRP A 415 ? 0.7010 1.6963 1.0341 -0.0728 -0.0163 0.0307  711 TRP A CZ3 
3325 C CH2 . TRP A 415 ? 0.7502 1.7256 1.0817 -0.0945 -0.0304 0.0353  711 TRP A CH2 
3326 N N   . ASN A 416 ? 0.8191 1.9750 1.1371 0.2151  0.0029  0.0047  712 ASN A N   
3327 C CA  . ASN A 416 ? 0.8613 2.0244 1.1634 0.2701  -0.0021 0.0027  712 ASN A CA  
3328 C C   . ASN A 416 ? 0.9440 2.0586 1.2076 0.3438  0.0054  -0.0091 712 ASN A C   
3329 O O   . ASN A 416 ? 0.9840 2.1107 1.2223 0.3960  0.0034  -0.0107 712 ASN A O   
3330 C CB  . ASN A 416 ? 0.8633 1.9639 1.1704 0.2625  -0.0169 0.0049  712 ASN A CB  
3331 C CG  . ASN A 416 ? 0.8144 1.9472 1.1485 0.1916  -0.0259 0.0155  712 ASN A CG  
3332 O OD1 . ASN A 416 ? 0.8031 2.0208 1.1465 0.1564  -0.0230 0.0229  712 ASN A OD1 
3333 N ND2 . ASN A 416 ? 0.7963 1.8571 1.1358 0.1695  -0.0374 0.0162  712 ASN A ND2 
3334 N N   . THR A 417 ? 1.0219 2.0783 1.2737 0.3489  0.0135  -0.0176 713 THR A N   
3335 C CA  . THR A 417 ? 1.0772 2.0500 1.2805 0.4126  0.0183  -0.0306 713 THR A CA  
3336 C C   . THR A 417 ? 1.1173 2.1067 1.3019 0.4302  0.0329  -0.0380 713 THR A C   
3337 O O   . THR A 417 ? 1.2253 2.1422 1.3585 0.4843  0.0371  -0.0495 713 THR A O   
3338 C CB  . THR A 417 ? 1.1673 2.0200 1.3598 0.4087  0.0120  -0.0374 713 THR A CB  
3339 O OG1 . THR A 417 ? 1.1038 1.9660 1.3347 0.3489  0.0127  -0.0345 713 THR A OG1 
3340 C CG2 . THR A 417 ? 1.1312 1.9468 1.3229 0.4128  -0.0026 -0.0323 713 THR A CG2 
3341 N N   . HIS A 418 ? 1.0494 2.1242 1.2659 0.3852  0.0403  -0.0315 714 HIS A N   
3342 C CA  . HIS A 418 ? 1.0629 2.1487 1.2648 0.3925  0.0543  -0.0379 714 HIS A CA  
3343 C C   . HIS A 418 ? 1.0749 2.2473 1.2587 0.4318  0.0607  -0.0369 714 HIS A C   
3344 O O   . HIS A 418 ? 1.0770 2.3607 1.2883 0.4011  0.0611  -0.0258 714 HIS A O   
3345 C CB  . HIS A 418 ? 0.9964 2.1195 1.2349 0.3205  0.0583  -0.0304 714 HIS A CB  
3346 C CG  . HIS A 418 ? 1.0063 2.1586 1.2329 0.3202  0.0731  -0.0342 714 HIS A CG  
3347 N ND1 . HIS A 418 ? 1.0286 2.1219 1.2133 0.3733  0.0818  -0.0489 714 HIS A ND1 
3348 C CD2 . HIS A 418 ? 1.0075 2.2343 1.2518 0.2711  0.0802  -0.0252 714 HIS A CD2 
3349 C CE1 . HIS A 418 ? 0.9881 2.1255 1.1702 0.3591  0.0942  -0.0490 714 HIS A CE1 
3350 N NE2 . HIS A 418 ? 0.9612 2.1810 1.1799 0.2971  0.0936  -0.0342 714 HIS A NE2 
3351 N N   . VAL A 419 ? 1.1541 2.2722 1.2855 0.4991  0.0648  -0.0484 715 VAL A N   
3352 C CA  . VAL A 419 ? 1.1648 2.3598 1.2724 0.5435  0.0712  -0.0488 715 VAL A CA  
3353 C C   . VAL A 419 ? 1.1861 2.4660 1.3202 0.5030  0.0827  -0.0446 715 VAL A C   
3354 O O   . VAL A 419 ? 1.1551 2.3836 1.2742 0.5000  0.0917  -0.0528 715 VAL A O   
3355 C CB  . VAL A 419 ? 1.1923 2.2899 1.2274 0.6191  0.0733  -0.0627 715 VAL A CB  
3356 C CG1 . VAL A 419 ? 1.2081 2.3888 1.2191 0.6632  0.0807  -0.0631 715 VAL A CG1 
3357 C CG2 . VAL A 419 ? 1.1831 2.2013 1.1824 0.6589  0.0611  -0.0644 715 VAL A CG2 
3358 N N   . TRP A 420 ? 1.2918 2.6994 1.4605 0.4689  0.0820  -0.0318 716 TRP A N   
3359 C CA  . TRP A 420 ? 1.3068 2.7900 1.5046 0.4082  0.0897  -0.0239 716 TRP A CA  
3360 C C   . TRP A 420 ? 1.4728 3.0319 1.6509 0.4407  0.1007  -0.0262 716 TRP A C   
3361 O O   . TRP A 420 ? 1.5230 3.0723 1.6629 0.5129  0.1022  -0.0345 716 TRP A O   
3362 C CB  . TRP A 420 ? 1.2536 2.8238 1.4899 0.3453  0.0818  -0.0086 716 TRP A CB  
3363 C CG  . TRP A 420 ? 1.2116 2.7710 1.4724 0.2636  0.0827  -0.0006 716 TRP A CG  
3364 C CD1 . TRP A 420 ? 1.2064 2.7704 1.4646 0.2328  0.0933  0.0000  716 TRP A CD1 
3365 C CD2 . TRP A 420 ? 1.1965 2.7326 1.4804 0.2025  0.0721  0.0085  716 TRP A CD2 
3366 N NE1 . TRP A 420 ? 1.1677 2.7090 1.4424 0.1568  0.0895  0.0095  716 TRP A NE1 
3367 C CE2 . TRP A 420 ? 1.1727 2.6946 1.4622 0.1374  0.0762  0.0146  716 TRP A CE2 
3368 C CE3 . TRP A 420 ? 1.2191 2.7404 1.5146 0.1975  0.0592  0.0122  716 TRP A CE3 
3369 C CZ2 . TRP A 420 ? 1.1766 2.6642 1.4777 0.0694  0.0670  0.0241  716 TRP A CZ2 
3370 C CZ3 . TRP A 420 ? 1.2266 2.7187 1.5383 0.1294  0.0505  0.0209  716 TRP A CZ3 
3371 C CH2 . TRP A 420 ? 1.2278 2.7003 1.5397 0.0669  0.0540  0.0267  716 TRP A CH2 
# 
