data_9CVK
# 
_entry.id   9CVK 
# 
_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   9CVK         pdb_00009cvk 10.2210/pdb9cvk/pdb 
WWPDB D_1000286174 ?            ?                   
# 
_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                        9CVK 
_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 '(6P)-6-{3-chloro-5-[(methylamino)methyl]phenyl}-4-methylpyridin-2-amine' 261.750   1  ?          ?     ? ? 
5 non-polymer syn 'ACETATE ION'                                                             59.044    1  ?          ?     ? ? 
6 non-polymer syn 'ZINC ION'                                                                65.409    1  ?          ?     ? ? 
7 water       nat water                                                                     18.015    42 ?          ?     ? ? 
# 
_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 '(6P)-6-{3-chloro-5-[(methylamino)methyl]phenyl}-4-methylpyridin-2-amine' A1A0G 
5 'ACETATE ION'                                                             ACT   
6 'ZINC ION'                                                                ZN    
7 water                                                                     HOH   
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   CYS n 
1 2   PRO n 
1 3   ARG n 
1 4   PHE n 
1 5   LEU n 
1 6   LYS n 
1 7   VAL n 
1 8   LYS n 
1 9   ASN n 
1 10  TRP n 
1 11  GLU n 
1 12  THR n 
1 13  ASP n 
1 14  VAL n 
1 15  VAL n 
1 16  LEU n 
1 17  THR n 
1 18  ASP n 
1 19  THR n 
1 20  LEU n 
1 21  HIS n 
1 22  LEU n 
1 23  LYS n 
1 24  SER n 
1 25  THR n 
1 26  LEU n 
1 27  GLU n 
1 28  THR n 
1 29  GLY n 
1 30  CYS n 
1 31  THR n 
1 32  GLU n 
1 33  HIS n 
1 34  ILE n 
1 35  CYS n 
1 36  MET n 
1 37  GLY n 
1 38  SER n 
1 39  ILE n 
1 40  MET n 
1 41  LEU n 
1 42  PRO n 
1 43  SER n 
1 44  GLN n 
1 45  HIS n 
1 46  THR n 
1 47  ARG n 
1 48  LYS n 
1 49  PRO n 
1 50  GLU n 
1 51  ASP n 
1 52  VAL n 
1 53  ALA n 
1 54  THR n 
1 55  LYS n 
1 56  ASP n 
1 57  GLN n 
1 58  LEU n 
1 59  PHE n 
1 60  PRO n 
1 61  LEU n 
1 62  ALA n 
1 63  LYS n 
1 64  GLU n 
1 65  PHE n 
1 66  LEU n 
1 67  ASP n 
1 68  GLN n 
1 69  TYR n 
1 70  TYR n 
1 71  SER n 
1 72  SER n 
1 73  ILE n 
1 74  LYS n 
1 75  ARG n 
1 76  PHE n 
1 77  GLY n 
1 78  SER n 
1 79  LYS n 
1 80  ALA n 
1 81  HIS n 
1 82  MET n 
1 83  ASP n 
1 84  ARG n 
1 85  LEU n 
1 86  GLU n 
1 87  GLU n 
1 88  VAL n 
1 89  ASN n 
1 90  LYS n 
1 91  GLU n 
1 92  ILE n 
1 93  GLU n 
1 94  SER n 
1 95  THR n 
1 96  SER n 
1 97  THR n 
1 98  TYR n 
1 99  GLN n 
1 100 LEU n 
1 101 LYS n 
1 102 ASP n 
1 103 THR n 
1 104 GLU n 
1 105 LEU n 
1 106 ILE n 
1 107 TYR n 
1 108 GLY n 
1 109 ALA n 
1 110 LYS n 
1 111 HIS n 
1 112 ALA n 
1 113 TRP n 
1 114 ARG n 
1 115 ASN n 
1 116 ALA n 
1 117 SER n 
1 118 ARG n 
1 119 CYS n 
1 120 VAL n 
1 121 GLY n 
1 122 ARG n 
1 123 ILE n 
1 124 GLN n 
1 125 TRP n 
1 126 SER n 
1 127 LYS n 
1 128 LEU n 
1 129 GLN n 
1 130 VAL n 
1 131 PHE n 
1 132 ASP n 
1 133 ALA n 
1 134 ARG n 
1 135 ASP n 
1 136 CYS n 
1 137 THR n 
1 138 THR n 
1 139 ALA n 
1 140 HIS n 
1 141 GLY n 
1 142 MET n 
1 143 PHE n 
1 144 ASN n 
1 145 TYR n 
1 146 ILE n 
1 147 CYS n 
1 148 ASN n 
1 149 HIS n 
1 150 VAL n 
1 151 LYS n 
1 152 TYR n 
1 153 ALA n 
1 154 THR n 
1 155 ASN n 
1 156 LYS n 
1 157 GLY n 
1 158 ASN n 
1 159 LEU n 
1 160 ARG n 
1 161 SER n 
1 162 ALA n 
1 163 ILE n 
1 164 THR n 
1 165 ILE n 
1 166 PHE n 
1 167 PRO n 
1 168 GLN n 
1 169 ARG n 
1 170 THR n 
1 171 ASP n 
1 172 GLY n 
1 173 LYS n 
1 174 HIS n 
1 175 ASP n 
1 176 PHE n 
1 177 ARG n 
1 178 VAL n 
1 179 TRP n 
1 180 ASN n 
1 181 SER n 
1 182 GLN n 
1 183 LEU n 
1 184 ILE n 
1 185 ARG n 
1 186 TYR n 
1 187 ALA n 
1 188 GLY n 
1 189 TYR n 
1 190 LYS n 
1 191 GLN n 
1 192 PRO n 
1 193 ASP n 
1 194 GLY n 
1 195 SER n 
1 196 THR n 
1 197 LEU n 
1 198 GLY n 
1 199 ASP n 
1 200 PRO n 
1 201 ALA n 
1 202 ASN n 
1 203 VAL n 
1 204 GLN n 
1 205 PHE n 
1 206 THR n 
1 207 GLU n 
1 208 ILE n 
1 209 CYS n 
1 210 ILE n 
1 211 GLN n 
1 212 GLN n 
1 213 GLY n 
1 214 TRP n 
1 215 LYS n 
1 216 ALA n 
1 217 PRO n 
1 218 ARG n 
1 219 GLY n 
1 220 ARG n 
1 221 PHE n 
1 222 ASP n 
1 223 VAL n 
1 224 LEU n 
1 225 PRO n 
1 226 LEU n 
1 227 LEU n 
1 228 LEU n 
1 229 GLN n 
1 230 ALA n 
1 231 ASN n 
1 232 GLY n 
1 233 ASN n 
1 234 ASP n 
1 235 PRO n 
1 236 GLU n 
1 237 LEU n 
1 238 PHE n 
1 239 GLN n 
1 240 ILE n 
1 241 PRO n 
1 242 PRO n 
1 243 GLU n 
1 244 LEU n 
1 245 VAL n 
1 246 LEU n 
1 247 GLU n 
1 248 VAL n 
1 249 PRO n 
1 250 ILE n 
1 251 ARG n 
1 252 HIS n 
1 253 PRO n 
1 254 LYS n 
1 255 PHE n 
1 256 ASP n 
1 257 TRP n 
1 258 PHE n 
1 259 LYS n 
1 260 ASP n 
1 261 LEU n 
1 262 GLY n 
1 263 LEU n 
1 264 LYS n 
1 265 TRP n 
1 266 TYR n 
1 267 GLY n 
1 268 LEU n 
1 269 PRO n 
1 270 ALA n 
1 271 VAL n 
1 272 SER n 
1 273 ASN n 
1 274 MET n 
1 275 LEU n 
1 276 LEU n 
1 277 GLU n 
1 278 ILE n 
1 279 GLY n 
1 280 GLY n 
1 281 LEU n 
1 282 GLU n 
1 283 PHE n 
1 284 SER n 
1 285 ALA n 
1 286 CYS n 
1 287 PRO n 
1 288 PHE n 
1 289 SER n 
1 290 GLY n 
1 291 TRP n 
1 292 TYR n 
1 293 MET n 
1 294 GLY n 
1 295 THR n 
1 296 GLU n 
1 297 ILE n 
1 298 GLY n 
1 299 VAL n 
1 300 ARG n 
1 301 ASP n 
1 302 TYR n 
1 303 CYS n 
1 304 ASP n 
1 305 ASN n 
1 306 SER n 
1 307 ARG n 
1 308 TYR n 
1 309 ASN n 
1 310 ILE n 
1 311 LEU n 
1 312 GLU n 
1 313 GLU n 
1 314 VAL n 
1 315 ALA n 
1 316 LYS n 
1 317 LYS n 
1 318 MET n 
1 319 ASP n 
1 320 LEU n 
1 321 ASP n 
1 322 MET n 
1 323 ARG n 
1 324 LYS n 
1 325 THR n 
1 326 SER n 
1 327 SER n 
1 328 LEU n 
1 329 TRP n 
1 330 LYS n 
1 331 ASP n 
1 332 GLN n 
1 333 ALA n 
1 334 LEU n 
1 335 VAL n 
1 336 GLU n 
1 337 ILE n 
1 338 ASN n 
1 339 ILE n 
1 340 ALA n 
1 341 VAL n 
1 342 LEU n 
1 343 TYR n 
1 344 SER n 
1 345 PHE n 
1 346 GLN n 
1 347 SER n 
1 348 ASP n 
1 349 LYS n 
1 350 VAL n 
1 351 THR n 
1 352 ILE n 
1 353 VAL n 
1 354 ASP n 
1 355 HIS n 
1 356 HIS n 
1 357 SER n 
1 358 ALA n 
1 359 THR n 
1 360 GLU n 
1 361 SER n 
1 362 PHE n 
1 363 ILE n 
1 364 LYS n 
1 365 HIS n 
1 366 MET n 
1 367 GLU n 
1 368 ASN n 
1 369 GLU n 
1 370 TYR n 
1 371 ARG n 
1 372 CYS n 
1 373 ARG n 
1 374 GLY n 
1 375 GLY n 
1 376 CYS n 
1 377 PRO n 
1 378 ALA n 
1 379 ASP n 
1 380 TRP n 
1 381 VAL n 
1 382 TRP n 
1 383 ILE n 
1 384 VAL n 
1 385 PRO n 
1 386 PRO n 
1 387 MET n 
1 388 SER n 
1 389 GLY n 
1 390 SER n 
1 391 ILE n 
1 392 THR n 
1 393 PRO n 
1 394 VAL n 
1 395 PHE n 
1 396 HIS n 
1 397 GLN n 
1 398 GLU n 
1 399 MET n 
1 400 LEU n 
1 401 ASN n 
1 402 TYR n 
1 403 ARG n 
1 404 LEU n 
1 405 THR n 
1 406 PRO n 
1 407 SER n 
1 408 PHE n 
1 409 GLU n 
1 410 TYR n 
1 411 GLN n 
1 412 PRO n 
1 413 ASP n 
1 414 PRO n 
1 415 TRP n 
1 416 ASN n 
1 417 THR n 
1 418 HIS n 
1 419 VAL n 
1 420 TRP n 
1 421 LYS n 
1 422 GLY n 
# 
_entity_src_gen.entity_id                          1 
_entity_src_gen.pdbx_src_id                        1 
_entity_src_gen.pdbx_alt_source_flag               sample 
_entity_src_gen.pdbx_seq_type                      'Biological sequence' 
_entity_src_gen.pdbx_beg_seq_num                   1 
_entity_src_gen.pdbx_end_seq_num                   422 
_entity_src_gen.gene_src_common_name               'Norway rat' 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 'Nos1, Bnos' 
_entity_src_gen.gene_src_species                   ? 
_entity_src_gen.gene_src_strain                    ? 
_entity_src_gen.gene_src_tissue                    ? 
_entity_src_gen.gene_src_tissue_fraction           ? 
_entity_src_gen.gene_src_details                   ? 
_entity_src_gen.pdbx_gene_src_fragment             ? 
_entity_src_gen.pdbx_gene_src_scientific_name      'Rattus norvegicus' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     10116 
_entity_src_gen.pdbx_gene_src_variant              ? 
_entity_src_gen.pdbx_gene_src_cell_line            ? 
_entity_src_gen.pdbx_gene_src_atcc                 ? 
_entity_src_gen.pdbx_gene_src_organ                brain 
_entity_src_gen.pdbx_gene_src_organelle            ? 
_entity_src_gen.pdbx_gene_src_cell                 ? 
_entity_src_gen.pdbx_gene_src_cellular_location    ? 
_entity_src_gen.host_org_common_name               ? 
_entity_src_gen.pdbx_host_org_scientific_name      'Escherichia coli BL21(DE3)' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     469008 
_entity_src_gen.host_org_genus                     ? 
_entity_src_gen.pdbx_host_org_gene                 ? 
_entity_src_gen.pdbx_host_org_organ                ? 
_entity_src_gen.host_org_species                   ? 
_entity_src_gen.pdbx_host_org_tissue               ? 
_entity_src_gen.pdbx_host_org_tissue_fraction      ? 
_entity_src_gen.pdbx_host_org_strain               ? 
_entity_src_gen.pdbx_host_org_variant              ? 
_entity_src_gen.pdbx_host_org_cell_line            ? 
_entity_src_gen.pdbx_host_org_atcc                 ? 
_entity_src_gen.pdbx_host_org_culture_collection   ? 
_entity_src_gen.pdbx_host_org_cell                 ? 
_entity_src_gen.pdbx_host_org_organelle            ? 
_entity_src_gen.pdbx_host_org_cellular_location    ? 
_entity_src_gen.pdbx_host_org_vector_type          plasmid 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       pET22b 
_entity_src_gen.plasmid_details                    ? 
_entity_src_gen.pdbx_description                   ? 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
A1A0G non-polymer         . '(6P)-6-{3-chloro-5-[(methylamino)methyl]phenyl}-4-methylpyridin-2-amine' ?    'C14 H16 Cl N3'    
261.750 
ACT   non-polymer         . 'ACETATE ION'                                                             ?    'C2 H3 O2 -1'      
59.044  
ALA   'L-peptide linking' y ALANINE                                                                   ?    'C3 H7 N O2'       
89.093  
ARG   'L-peptide linking' y ARGININE                                                                  ?    'C6 H15 N4 O2 1'   
175.209 
ASN   'L-peptide linking' y ASPARAGINE                                                                ?    'C4 H8 N2 O3'      
132.118 
ASP   'L-peptide linking' y 'ASPARTIC ACID'                                                           ?    'C4 H7 N O4'       
133.103 
CYS   'L-peptide linking' y CYSTEINE                                                                  ?    'C3 H7 N O2 S'     
121.158 
GLN   'L-peptide linking' y GLUTAMINE                                                                 ?    'C5 H10 N2 O3'     
146.144 
GLU   'L-peptide linking' y 'GLUTAMIC ACID'                                                           ?    'C5 H9 N O4'       
147.129 
GLY   'peptide linking'   y GLYCINE                                                                   ?    'C2 H5 N O2'       
75.067  
H4B   non-polymer         . 5,6,7,8-TETRAHYDROBIOPTERIN                                               ?    'C9 H15 N5 O3'     
241.247 
HEM   non-polymer         . 'PROTOPORPHYRIN IX CONTAINING FE'                                         HEME 'C34 H32 Fe N4 O4' 
616.487 
HIS   'L-peptide linking' y HISTIDINE                                                                 ?    'C6 H10 N3 O2 1'   
156.162 
HOH   non-polymer         . WATER                                                                     ?    'H2 O'             
18.015  
ILE   'L-peptide linking' y ISOLEUCINE                                                                ?    'C6 H13 N O2'      
131.173 
LEU   'L-peptide linking' y LEUCINE                                                                   ?    'C6 H13 N O2'      
131.173 
LYS   'L-peptide linking' y LYSINE                                                                    ?    'C6 H15 N2 O2 1'   
147.195 
MET   'L-peptide linking' y METHIONINE                                                                ?    'C5 H11 N O2 S'    
149.211 
PHE   'L-peptide linking' y PHENYLALANINE                                                             ?    'C9 H11 N O2'      
165.189 
PRO   'L-peptide linking' y PROLINE                                                                   ?    'C5 H9 N O2'       
115.130 
SER   'L-peptide linking' y SERINE                                                                    ?    'C3 H7 N O3'       
105.093 
THR   'L-peptide linking' y THREONINE                                                                 ?    'C4 H9 N O3'       
119.119 
TRP   'L-peptide linking' y TRYPTOPHAN                                                                ?    'C11 H12 N2 O2'    
204.225 
TYR   'L-peptide linking' y TYROSINE                                                                  ?    'C9 H11 N O3'      
181.189 
VAL   'L-peptide linking' y VALINE                                                                    ?    'C5 H11 N O2'      
117.146 
ZN    non-polymer         . 'ZINC ION'                                                                ?    'Zn 2'             
65.409  
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   CYS 1   297 ?   ?   ?   A . n 
A 1 2   PRO 2   298 ?   ?   ?   A . n 
A 1 3   ARG 3   299 299 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 422 718 718 GLY GLY A . n 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        A1A0G 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   A1A0G 
_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 A1A0G 1  803 800 A1A0G 3V0 A . 
E 5 ACT   1  804 860 ACT   ACT A . 
F 6 ZN    1  805 900 ZN    ZN  A . 
G 7 HOH   1  901 30  HOH   HOH A . 
G 7 HOH   2  902 38  HOH   HOH A . 
G 7 HOH   3  903 3   HOH   HOH A . 
G 7 HOH   4  904 31  HOH   HOH A . 
G 7 HOH   5  905 27  HOH   HOH A . 
G 7 HOH   6  906 21  HOH   HOH A . 
G 7 HOH   7  907 37  HOH   HOH A . 
G 7 HOH   8  908 34  HOH   HOH A . 
G 7 HOH   9  909 24  HOH   HOH A . 
G 7 HOH   10 910 19  HOH   HOH A . 
G 7 HOH   11 911 35  HOH   HOH A . 
G 7 HOH   12 912 17  HOH   HOH A . 
G 7 HOH   13 913 16  HOH   HOH A . 
G 7 HOH   14 914 13  HOH   HOH A . 
G 7 HOH   15 915 42  HOH   HOH A . 
G 7 HOH   16 916 25  HOH   HOH A . 
G 7 HOH   17 917 7   HOH   HOH A . 
G 7 HOH   18 918 14  HOH   HOH A . 
G 7 HOH   19 919 1   HOH   HOH A . 
G 7 HOH   20 920 15  HOH   HOH A . 
G 7 HOH   21 921 29  HOH   HOH A . 
G 7 HOH   22 922 18  HOH   HOH A . 
G 7 HOH   23 923 26  HOH   HOH A . 
G 7 HOH   24 924 20  HOH   HOH A . 
G 7 HOH   25 925 40  HOH   HOH A . 
G 7 HOH   26 926 23  HOH   HOH A . 
G 7 HOH   27 927 12  HOH   HOH A . 
G 7 HOH   28 928 8   HOH   HOH A . 
G 7 HOH   29 929 36  HOH   HOH A . 
G 7 HOH   30 930 6   HOH   HOH A . 
G 7 HOH   31 931 5   HOH   HOH A . 
G 7 HOH   32 932 28  HOH   HOH A . 
G 7 HOH   33 933 4   HOH   HOH A . 
G 7 HOH   34 934 11  HOH   HOH A . 
G 7 HOH   35 935 2   HOH   HOH A . 
G 7 HOH   36 936 10  HOH   HOH A . 
G 7 HOH   37 937 33  HOH   HOH A . 
G 7 HOH   38 938 39  HOH   HOH A . 
G 7 HOH   39 939 9   HOH   HOH A . 
G 7 HOH   40 940 32  HOH   HOH A . 
G 7 HOH   41 941 22  HOH   HOH A . 
G 7 HOH   42 942 41  HOH   HOH A . 
# 
loop_
_software.citation_id 
_software.classification 
_software.compiler_name 
_software.compiler_version 
_software.contact_author 
_software.contact_author_email 
_software.date 
_software.description 
_software.dependencies 
_software.hardware 
_software.language 
_software.location 
_software.mods 
_software.name 
_software.os 
_software.os_version 
_software.type 
_software.version 
_software.pdbx_ordinal 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? Aimless ? ? ? .           1 
? refinement       ? ? ? ? ? ? ? ? ? ? ? PHENIX  ? ? ? 1.11.1_2575 2 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? XDS     ? ? ? .           3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? REFMAC  ? ? ? .           4 
# 
_cell.angle_alpha                  90.00 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   90.00 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.00 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     9CVK 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     48.737 
_cell.length_a_esd                 ? 
_cell.length_b                     113.321 
_cell.length_b_esd                 ? 
_cell.length_c                     163.105 
_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                         9CVK 
_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                   9CVK 
_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         2022-09-15 
_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                                       9CVK 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              1.90 
_reflns.d_resolution_low                               46.53 
_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                                     35691 
_reflns.observed_criterion                             ? 
_reflns.observed_criterion_F_max                       ? 
_reflns.observed_criterion_F_min                       ? 
_reflns.observed_criterion_I_max                       ? 
_reflns.observed_criterion_I_min                       ? 
_reflns.observed_criterion_sigma_F                     ? 
_reflns.observed_criterion_sigma_I                     ? 
_reflns.percent_possible_obs                           99.0 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                8.1 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          8.3 
_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                                0.106 
_reflns.pdbx_Rpim_I_all                                0.034 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       289665 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.998 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              0.100 
_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                                    1.90 
_reflns_shell.d_res_low                                     1.94 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           ? 
_reflns_shell.number_measured_all                           13799 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             2254 
_reflns_shell.percent_possible_obs                          98.0 
_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                               6.1 
_reflns_shell.pdbx_chi_squared                              ? 
_reflns_shell.pdbx_netI_over_sigmaI_all                     ? 
_reflns_shell.pdbx_netI_over_sigmaI_obs                     0.4 
_reflns_shell.pdbx_Rrim_I_all                               7.146 
_reflns_shell.pdbx_Rpim_I_all                               2.832 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.322 
_reflns_shell.pdbx_CC_star                                  ? 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          ? 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  6.546 
_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                                 9CVK 
_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                            1.901 
_refine.ls_d_res_low                             46.53 
_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                     33677 
_refine.ls_number_reflns_R_free                  3213 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    92.85 
_refine.ls_percent_reflns_R_free                 5.03 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.2216 
_refine.ls_R_factor_R_free                       0.2737 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.2187 
_refine.ls_R_Fsqd_factor_obs                     ? 
_refine.ls_R_I_factor_obs                        ? 
_refine.ls_redundancy_reflns_all                 ? 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.ls_restrained_S_all                      ? 
_refine.ls_restrained_S_obs                      ? 
_refine.ls_shift_over_esd_max                    ? 
_refine.ls_shift_over_esd_mean                   ? 
_refine.ls_structure_factor_coef                 ? 
_refine.ls_weighting_details                     ? 
_refine.ls_weighting_scheme                      ? 
_refine.ls_wR_factor_all                         ? 
_refine.ls_wR_factor_obs                         ? 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_wR_factor_R_work                      ? 
_refine.occupancy_max                            ? 
_refine.occupancy_min                            ? 
_refine.solvent_model_details                    'FLAT BULK SOLVENT MODEL' 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.pdbx_R_complete                          ? 
_refine.ls_R_factor_gt                           ? 
_refine.ls_goodness_of_fit_gt                    ? 
_refine.ls_goodness_of_fit_ref                   ? 
_refine.ls_shift_over_su_max                     ? 
_refine.ls_shift_over_su_max_lt                  ? 
_refine.ls_shift_over_su_mean                    ? 
_refine.ls_shift_over_su_mean_lt                 ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          0.06 
_refine.pdbx_ls_sigma_Fsqd                       ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_ls_cross_valid_method               'FREE R-VALUE' 
_refine.pdbx_method_to_determine_struct          'FOURIER SYNTHESIS' 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_stereochemistry_target_values       ML 
_refine.pdbx_R_Free_selection_details            random 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.pdbx_solvent_vdw_probe_radii             1.11 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             0.90 
_refine.pdbx_real_space_R                        ? 
_refine.pdbx_density_correlation                 ? 
_refine.pdbx_pd_number_of_powder_patterns        ? 
_refine.pdbx_pd_number_of_points                 ? 
_refine.pdbx_pd_meas_number_of_points            ? 
_refine.pdbx_pd_proc_ls_prof_R_factor            ? 
_refine.pdbx_pd_proc_ls_prof_wR_factor           ? 
_refine.pdbx_pd_Marquardt_correlation_coeff      ? 
_refine.pdbx_pd_Fsqrd_R_factor                   ? 
_refine.pdbx_pd_ls_matrix_band_width             ? 
_refine.pdbx_overall_phase_error                 44.62 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.pdbx_diffrn_id                           1 
_refine.overall_SU_B                             ? 
_refine.overall_SU_ML                            0.27 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.overall_SU_R_free                        ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.pdbx_average_fsc_overall                 ? 
_refine.pdbx_average_fsc_work                    ? 
_refine.pdbx_average_fsc_free                    ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.pdbx_number_atoms_protein        3382 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         83 
_refine_hist.number_atoms_solvent             42 
_refine_hist.number_atoms_total               3507 
_refine_hist.d_res_high                       1.901 
_refine_hist.d_res_low                        46.53 
# 
loop_
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.criterion 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.number 
_refine_ls_restr.rejects 
_refine_ls_restr.type 
_refine_ls_restr.weight 
_refine_ls_restr.pdbx_restraint_function 
'X-RAY DIFFRACTION' ? 0.006  ? 3577 ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 0.998  ? 4866 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 18.569 ? 2083 ? f_dihedral_angle_d ? ? 
'X-RAY DIFFRACTION' ? 0.051  ? 504  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.005  ? 615  ? 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' 1.901  1.929  . . 101 2209 75.00  . . . . 0.4516 . . . . . . . . . . . 0.5590 
'X-RAY DIFFRACTION' 1.9291 1.9592 . . 135 2127 76.00  . . . . 0.4464 . . . . . . . . . . . 0.4488 
'X-RAY DIFFRACTION' 1.9592 1.9913 . . 121 2282 80.00  . . . . 0.4210 . . . . . . . . . . . 0.4527 
'X-RAY DIFFRACTION' 1.9913 2.0257 . . 99  2280 80.00  . . . . 0.4104 . . . . . . . . . . . 0.4612 
'X-RAY DIFFRACTION' 2.0257 2.0625 . . 103 2413 84.00  . . . . 0.4241 . . . . . . . . . . . 0.4709 
'X-RAY DIFFRACTION' 2.0625 2.1022 . . 129 2397 85.00  . . . . 0.3900 . . . . . . . . . . . 0.4782 
'X-RAY DIFFRACTION' 2.1022 2.1451 . . 146 2546 90.00  . . . . 0.3850 . . . . . . . . . . . 0.4818 
'X-RAY DIFFRACTION' 2.1451 2.1917 . . 123 2646 92.00  . . . . 0.3593 . . . . . . . . . . . 0.4138 
'X-RAY DIFFRACTION' 2.1917 2.2427 . . 174 2639 95.00  . . . . 0.3409 . . . . . . . . . . . 0.4003 
'X-RAY DIFFRACTION' 2.2427 2.2988 . . 148 2802 98.00  . . . . 0.3118 . . . . . . . . . . . 0.4137 
'X-RAY DIFFRACTION' 2.2988 2.3609 . . 134 2781 97.00  . . . . 0.3069 . . . . . . . . . . . 0.3797 
'X-RAY DIFFRACTION' 2.3609 2.4304 . . 153 2768 98.00  . . . . 0.2792 . . . . . . . . . . . 0.3129 
'X-RAY DIFFRACTION' 2.4304 2.5088 . . 123 2723 97.00  . . . . 0.2649 . . . . . . . . . . . 0.3382 
'X-RAY DIFFRACTION' 2.5088 2.5985 . . 129 2694 94.00  . . . . 0.2857 . . . . . . . . . . . 0.3320 
'X-RAY DIFFRACTION' 2.5985 2.7025 . . 153 2817 99.00  . . . . 0.2746 . . . . . . . . . . . 0.4013 
'X-RAY DIFFRACTION' 2.7025 2.8255 . . 139 2797 99.00  . . . . 0.2764 . . . . . . . . . . . 0.3386 
'X-RAY DIFFRACTION' 2.8255 2.9745 . . 121 2843 99.00  . . . . 0.2733 . . . . . . . . . . . 0.3379 
'X-RAY DIFFRACTION' 2.9745 3.1608 . . 159 2785 99.00  . . . . 0.2651 . . . . . . . . . . . 0.3083 
'X-RAY DIFFRACTION' 3.1608 3.4047 . . 188 2780 99.00  . . . . 0.2263 . . . . . . . . . . . 0.2995 
'X-RAY DIFFRACTION' 3.4047 3.7472 . . 160 2831 100.00 . . . . 0.2011 . . . . . . . . . . . 0.2499 
'X-RAY DIFFRACTION' 3.7472 4.2892 . . 162 2803 100.00 . . . . 0.1682 . . . . . . . . . . . 0.2019 
'X-RAY DIFFRACTION' 4.2892 5.4026 . . 158 2845 100.00 . . . . 0.1522 . . . . . . . . . . . 0.2183 
'X-RAY DIFFRACTION' 5.4026 46.53  . . 155 2822 100.00 . . . . 0.1486 . . . . . . . . . . . 0.1997 
# 
_struct.entry_id                     9CVK 
_struct.title                        
;Structure of rat neuronal nitric oxide synthase R349A mutant heme domain bound with 6-(3-chloro-5-((methylamino)methyl)phenyl)-4-methylpyridin-2-amine dihydrochloride
;
_struct.pdbx_model_details           ? 
_struct.pdbx_formula_weight          ? 
_struct.pdbx_formula_weight_method   ? 
_struct.pdbx_model_type_details      ? 
_struct.pdbx_CASP_flag               N 
# 
_struct_keywords.entry_id        9CVK 
_struct_keywords.text            'nitric oxide synthase inhibitor binding, OXIDOREDUCTASE' 
_struct_keywords.pdbx_keywords   OXIDOREDUCTASE 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 2 ? 
C N N 3 ? 
D N N 4 ? 
E N N 5 ? 
F N N 6 ? 
G N N 7 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    NOS1_RAT 
_struct_ref.pdbx_db_accession          P29476 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;CPRFLKVKNWETDVVLTDTLHLKSTLETGCTEHICMGSIMLPSQHTRKPEDVRTKDQLFPLAKEFLDQYYSSIKRFGSKA
HMDRLEEVNKEIESTSTYQLKDTELIYGAKHAWRNASRCVGRIQWSKLQVFDARDCTTAHGMFNYICNHVKYATNKGNLR
SAITIFPQRTDGKHDFRVWNSQLIRYAGYKQPDGSTLGDPANVQFTEICIQQGWKAPRGRFDVLPLLLQANGNDPELFQI
PPELVLEVPIRHPKFDWFKDLGLKWYGLPAVSNMLLEIGGLEFSACPFSGWYMGTEIGVRDYCDNSRYNILEEVAKKMDL
DMRKTSSLWKDQALVEINIAVLYSFQSDKVTIVDHHSATESFIKHMENEYRCRGGCPADWVWIVPPMSGSITPVFHQEML
NYRLTPSFEYQPDPWNTHVWKG
;
_struct_ref.pdbx_align_begin           297 
# 
_struct_ref_seq.align_id                      1 
_struct_ref_seq.ref_id                        1 
_struct_ref_seq.pdbx_PDB_id_code              9CVK 
_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             9CVK 
_struct_ref_seq_dif.mon_id                       ALA 
_struct_ref_seq_dif.pdbx_pdb_strand_id           A 
_struct_ref_seq_dif.seq_num                      53 
_struct_ref_seq_dif.pdbx_pdb_ins_code            ? 
_struct_ref_seq_dif.pdbx_seq_db_name             UNP 
_struct_ref_seq_dif.pdbx_seq_db_accession_code   P29476 
_struct_ref_seq_dif.db_mon_id                    ARG 
_struct_ref_seq_dif.pdbx_seq_db_seq_num          349 
_struct_ref_seq_dif.details                      'engineered mutation' 
_struct_ref_seq_dif.pdbx_auth_seq_num            349 
_struct_ref_seq_dif.pdbx_ordinal                 1 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_defined_assembly 
_pdbx_struct_assembly.method_details       ? 
_pdbx_struct_assembly.oligomeric_details   monomeric 
_pdbx_struct_assembly.oligomeric_count     1 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,D,E,F,G 
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   'gel filtration' 
_pdbx_struct_assembly_auth_evidence.details                ? 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1  AA1 THR A 19  ? SER A 24  ? THR A 315 SER A 320 5 ? 6  
HELX_P HELX_P2  AA2 THR A 54  ? SER A 71  ? THR A 350 SER A 367 1 ? 18 
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 F ZN  . ZN ? ? A CYS 326 A ZN  805 1_555 ? ? ? ? ? ? ? 2.414 ? ? 
metalc2 metalc ? ? A CYS 30  SG ? ? ? 1_555 F ZN  . ZN ? ? A CYS 326 A ZN  805 3_455 ? ? ? ? ? ? ? 2.404 ? ? 
metalc3 metalc ? ? A CYS 35  SG ? ? ? 1_555 F ZN  . ZN ? ? A CYS 331 A ZN  805 1_555 ? ? ? ? ? ? ? 2.302 ? ? 
metalc4 metalc ? ? A CYS 35  SG ? ? ? 1_555 F ZN  . ZN ? ? A CYS 331 A ZN  805 3_455 ? ? ? ? ? ? ? 2.276 ? ? 
metalc5 metalc ? ? A CYS 119 SG ? ? ? 1_555 B HEM . FE ? ? A CYS 415 A HEM 801 1_555 ? ? ? ? ? ? ? 2.352 ? ? 
# 
_struct_conn_type.id          metalc 
_struct_conn_type.criteria    ? 
_struct_conn_type.reference   ? 
# 
loop_
_pdbx_struct_conn_angle.id 
_pdbx_struct_conn_angle.ptnr1_label_atom_id 
_pdbx_struct_conn_angle.ptnr1_label_alt_id 
_pdbx_struct_conn_angle.ptnr1_label_asym_id 
_pdbx_struct_conn_angle.ptnr1_label_comp_id 
_pdbx_struct_conn_angle.ptnr1_label_seq_id 
_pdbx_struct_conn_angle.ptnr1_auth_atom_id 
_pdbx_struct_conn_angle.ptnr1_auth_asym_id 
_pdbx_struct_conn_angle.ptnr1_auth_comp_id 
_pdbx_struct_conn_angle.ptnr1_auth_seq_id 
_pdbx_struct_conn_angle.ptnr1_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr1_symmetry 
_pdbx_struct_conn_angle.ptnr2_label_atom_id 
_pdbx_struct_conn_angle.ptnr2_label_alt_id 
_pdbx_struct_conn_angle.ptnr2_label_asym_id 
_pdbx_struct_conn_angle.ptnr2_label_comp_id 
_pdbx_struct_conn_angle.ptnr2_label_seq_id 
_pdbx_struct_conn_angle.ptnr2_auth_atom_id 
_pdbx_struct_conn_angle.ptnr2_auth_asym_id 
_pdbx_struct_conn_angle.ptnr2_auth_comp_id 
_pdbx_struct_conn_angle.ptnr2_auth_seq_id 
_pdbx_struct_conn_angle.ptnr2_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr2_symmetry 
_pdbx_struct_conn_angle.ptnr3_label_atom_id 
_pdbx_struct_conn_angle.ptnr3_label_alt_id 
_pdbx_struct_conn_angle.ptnr3_label_asym_id 
_pdbx_struct_conn_angle.ptnr3_label_comp_id 
_pdbx_struct_conn_angle.ptnr3_label_seq_id 
_pdbx_struct_conn_angle.ptnr3_auth_atom_id 
_pdbx_struct_conn_angle.ptnr3_auth_asym_id 
_pdbx_struct_conn_angle.ptnr3_auth_comp_id 
_pdbx_struct_conn_angle.ptnr3_auth_seq_id 
_pdbx_struct_conn_angle.ptnr3_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr3_symmetry 
_pdbx_struct_conn_angle.value 
_pdbx_struct_conn_angle.value_esd 
1  SG ? A CYS 30  ? A CYS 326 ? 1_555 ZN ? F ZN  . ? A ZN  805 ? 1_555 SG ? A CYS 30 ? A CYS 326 ? 1_555 0.0   ? 
2  SG ? A CYS 30  ? A CYS 326 ? 1_555 ZN ? F ZN  . ? A ZN  805 ? 1_555 SG ? A CYS 35 ? A CYS 331 ? 1_555 113.5 ? 
3  SG ? A CYS 30  ? A CYS 326 ? 1_555 ZN ? F ZN  . ? A ZN  805 ? 1_555 SG ? A CYS 35 ? A CYS 331 ? 1_555 113.5 ? 
4  SG ? A CYS 30  ? A CYS 326 ? 1_555 ZN ? F ZN  . ? A ZN  805 ? 1_555 SG ? A CYS 35 ? A CYS 331 ? 1_555 113.5 ? 
5  SG ? A CYS 30  ? A CYS 326 ? 1_555 ZN ? F ZN  . ? A ZN  805 ? 1_555 SG ? A CYS 35 ? A CYS 331 ? 1_555 113.5 ? 
6  SG ? A CYS 35  ? A CYS 331 ? 1_555 ZN ? F ZN  . ? A ZN  805 ? 1_555 SG ? A CYS 35 ? A CYS 331 ? 1_555 0.0   ? 
7  SG ? A CYS 119 ? A CYS 415 ? 1_555 FE ? B HEM . ? A HEM 801 ? 1_555 NA ? B HEM .  ? A HEM 801 ? 1_555 100.4 ? 
8  SG ? A CYS 119 ? A CYS 415 ? 1_555 FE ? B HEM . ? A HEM 801 ? 1_555 NB ? B HEM .  ? A HEM 801 ? 1_555 99.4  ? 
9  NA ? B HEM .   ? A HEM 801 ? 1_555 FE ? B HEM . ? A HEM 801 ? 1_555 NB ? B HEM .  ? A HEM 801 ? 1_555 85.4  ? 
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_555 102.7 ? 
11 NA ? B HEM .   ? A HEM 801 ? 1_555 FE ? B HEM . ? A HEM 801 ? 1_555 NC ? B HEM .  ? A HEM 801 ? 1_555 156.7 ? 
12 NB ? B HEM .   ? A HEM 801 ? 1_555 FE ? B HEM . ? A HEM 801 ? 1_555 NC ? B HEM .  ? A HEM 801 ? 1_555 87.9  ? 
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_555 109.1 ? 
14 NA ? B HEM .   ? A HEM 801 ? 1_555 FE ? B HEM . ? A HEM 801 ? 1_555 ND ? B HEM .  ? A HEM 801 ? 1_555 89.8  ? 
15 NB ? B HEM .   ? A HEM 801 ? 1_555 FE ? B HEM . ? A HEM 801 ? 1_555 ND ? B HEM .  ? A HEM 801 ? 1_555 151.5 ? 
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 85.5  ? 
# 
_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       -1.36 
# 
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   ? ASN A 9   ? LEU A 301 ASN A 305 
AA1 2 VAL A 14  ? ASP A 18  ? VAL A 310 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 PHE A 283 ? O PHE A 579 N LEU A 276 ? N LEU A 572 
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                   9CVK 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.has_protein_modification   N 
# 
loop_
_pdbx_validate_close_contact.id 
_pdbx_validate_close_contact.PDB_model_num 
_pdbx_validate_close_contact.auth_atom_id_1 
_pdbx_validate_close_contact.auth_asym_id_1 
_pdbx_validate_close_contact.auth_comp_id_1 
_pdbx_validate_close_contact.auth_seq_id_1 
_pdbx_validate_close_contact.PDB_ins_code_1 
_pdbx_validate_close_contact.label_alt_id_1 
_pdbx_validate_close_contact.auth_atom_id_2 
_pdbx_validate_close_contact.auth_asym_id_2 
_pdbx_validate_close_contact.auth_comp_id_2 
_pdbx_validate_close_contact.auth_seq_id_2 
_pdbx_validate_close_contact.PDB_ins_code_2 
_pdbx_validate_close_contact.label_alt_id_2 
_pdbx_validate_close_contact.dist 
1 1 O   A HIS 470 ? ? O A HOH 901 ? ? 2.04 
2 1 OE1 A GLN 628 ? ? O A HOH 902 ? ? 2.12 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1  1 PHE A 300 ? ? -150.95 64.95   
2  1 HIS A 341 ? ? -64.00  9.21    
3  1 SER A 392 ? ? 59.58   12.95   
4  1 LYS A 423 ? ? -100.79 78.87   
5  1 THR A 466 ? ? -115.58 -87.77  
6  1 SER A 491 ? ? -66.99  -172.26 
7  1 PRO A 513 ? ? -77.22  30.71   
8  1 ARG A 514 ? ? 5.49    70.93   
9  1 ARG A 516 ? ? -77.74  -89.21  
10 1 CYS A 582 ? ? -148.96 50.73   
11 1 ARG A 603 ? ? -110.44 -132.16 
12 1 ASN A 605 ? ? 63.42   64.15   
13 1 ASP A 615 ? ? 58.57   85.02   
14 1 ASP A 617 ? ? -62.49  83.09   
15 1 LEU A 624 ? ? 38.30   41.78   
16 1 CYS A 672 ? ? -161.94 100.46  
17 1 VAL A 715 ? ? -62.05  90.52   
18 1 LYS A 717 ? ? -141.08 55.36   
# 
_pdbx_struct_special_symmetry.id              1 
_pdbx_struct_special_symmetry.PDB_model_num   1 
_pdbx_struct_special_symmetry.auth_asym_id    A 
_pdbx_struct_special_symmetry.auth_comp_id    ZN 
_pdbx_struct_special_symmetry.auth_seq_id     805 
_pdbx_struct_special_symmetry.PDB_ins_code    ? 
_pdbx_struct_special_symmetry.label_asym_id   F 
_pdbx_struct_special_symmetry.label_comp_id   ZN 
_pdbx_struct_special_symmetry.label_seq_id    . 
# 
_pdbx_refine_tls.id               1 
_pdbx_refine_tls.pdbx_refine_id   'X-RAY DIFFRACTION' 
_pdbx_refine_tls.details          ? 
_pdbx_refine_tls.method           refined 
_pdbx_refine_tls.origin_x         -23.6246 
_pdbx_refine_tls.origin_y         -4.9769 
_pdbx_refine_tls.origin_z         22.2643 
_pdbx_refine_tls.T[1][1]          0.3405 
_pdbx_refine_tls.T[1][1]_esd      ? 
_pdbx_refine_tls.T[1][2]          -0.0499 
_pdbx_refine_tls.T[1][2]_esd      ? 
_pdbx_refine_tls.T[1][3]          -0.0617 
_pdbx_refine_tls.T[1][3]_esd      ? 
_pdbx_refine_tls.T[2][2]          0.4057 
_pdbx_refine_tls.T[2][2]_esd      ? 
_pdbx_refine_tls.T[2][3]          -0.0172 
_pdbx_refine_tls.T[2][3]_esd      ? 
_pdbx_refine_tls.T[3][3]          0.4701 
_pdbx_refine_tls.T[3][3]_esd      ? 
_pdbx_refine_tls.L[1][1]          0.7614 
_pdbx_refine_tls.L[1][1]_esd      ? 
_pdbx_refine_tls.L[1][2]          -0.1026 
_pdbx_refine_tls.L[1][2]_esd      ? 
_pdbx_refine_tls.L[1][3]          0.1495 
_pdbx_refine_tls.L[1][3]_esd      ? 
_pdbx_refine_tls.L[2][2]          1.1454 
_pdbx_refine_tls.L[2][2]_esd      ? 
_pdbx_refine_tls.L[2][3]          0.1162 
_pdbx_refine_tls.L[2][3]_esd      ? 
_pdbx_refine_tls.L[3][3]          8.3192 
_pdbx_refine_tls.L[3][3]_esd      ? 
_pdbx_refine_tls.S[1][1]          -0.0447 
_pdbx_refine_tls.S[1][1]_esd      ? 
_pdbx_refine_tls.S[1][2]          0.1651 
_pdbx_refine_tls.S[1][2]_esd      ? 
_pdbx_refine_tls.S[1][3]          -0.0184 
_pdbx_refine_tls.S[1][3]_esd      ? 
_pdbx_refine_tls.S[2][1]          0.0217 
_pdbx_refine_tls.S[2][1]_esd      ? 
_pdbx_refine_tls.S[2][2]          -0.0812 
_pdbx_refine_tls.S[2][2]_esd      ? 
_pdbx_refine_tls.S[2][3]          -0.0714 
_pdbx_refine_tls.S[2][3]_esd      ? 
_pdbx_refine_tls.S[3][1]          -0.4749 
_pdbx_refine_tls.S[3][1]_esd      ? 
_pdbx_refine_tls.S[3][2]          0.1791 
_pdbx_refine_tls.S[3][2]_esd      ? 
_pdbx_refine_tls.S[3][3]          0.0823 
_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 
# 
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 
A1A0G C11  C  Y N 1   
A1A0G C12  C  Y N 2   
A1A0G C13  C  Y N 3   
A1A0G C14  C  Y N 4   
A1A0G C15  C  Y N 5   
A1A0G C16  C  Y N 6   
A1A0G C17  C  N N 7   
A1A0G C02  C  Y N 8   
A1A0G C03  C  Y N 9   
A1A0G C04  C  Y N 10  
A1A0G C05  C  Y N 11  
A1A0G C06  C  Y N 12  
A1A0G C07  C  N N 13  
A1A0G C19  C  N N 14  
A1A0G N01  N  Y N 15  
A1A0G N02  N  N N 16  
A1A0G N18  N  N N 17  
A1A0G CL1  CL N N 18  
A1A0G H1   H  N N 19  
A1A0G H2   H  N N 20  
A1A0G H3   H  N N 21  
A1A0G H4   H  N N 22  
A1A0G H5   H  N N 23  
A1A0G H6   H  N N 24  
A1A0G H7   H  N N 25  
A1A0G H8   H  N N 26  
A1A0G H9   H  N N 27  
A1A0G H10  H  N N 28  
A1A0G H11  H  N N 29  
A1A0G H12  H  N N 30  
A1A0G H13  H  N N 31  
A1A0G H14  H  N N 32  
A1A0G H15  H  N N 33  
A1A0G H16  H  N N 34  
ACT   C    C  N N 35  
ACT   O    O  N N 36  
ACT   OXT  O  N N 37  
ACT   CH3  C  N N 38  
ACT   H1   H  N N 39  
ACT   H2   H  N N 40  
ACT   H3   H  N N 41  
ALA   N    N  N N 42  
ALA   CA   C  N S 43  
ALA   C    C  N N 44  
ALA   O    O  N N 45  
ALA   CB   C  N N 46  
ALA   OXT  O  N N 47  
ALA   H    H  N N 48  
ALA   H2   H  N N 49  
ALA   HA   H  N N 50  
ALA   HB1  H  N N 51  
ALA   HB2  H  N N 52  
ALA   HB3  H  N N 53  
ALA   HXT  H  N N 54  
ARG   N    N  N N 55  
ARG   CA   C  N S 56  
ARG   C    C  N N 57  
ARG   O    O  N N 58  
ARG   CB   C  N N 59  
ARG   CG   C  N N 60  
ARG   CD   C  N N 61  
ARG   NE   N  N N 62  
ARG   CZ   C  N N 63  
ARG   NH1  N  N N 64  
ARG   NH2  N  N N 65  
ARG   OXT  O  N N 66  
ARG   H    H  N N 67  
ARG   H2   H  N N 68  
ARG   HA   H  N N 69  
ARG   HB2  H  N N 70  
ARG   HB3  H  N N 71  
ARG   HG2  H  N N 72  
ARG   HG3  H  N N 73  
ARG   HD2  H  N N 74  
ARG   HD3  H  N N 75  
ARG   HE   H  N N 76  
ARG   HH11 H  N N 77  
ARG   HH12 H  N N 78  
ARG   HH21 H  N N 79  
ARG   HH22 H  N N 80  
ARG   HXT  H  N N 81  
ASN   N    N  N N 82  
ASN   CA   C  N S 83  
ASN   C    C  N N 84  
ASN   O    O  N N 85  
ASN   CB   C  N N 86  
ASN   CG   C  N N 87  
ASN   OD1  O  N N 88  
ASN   ND2  N  N N 89  
ASN   OXT  O  N N 90  
ASN   H    H  N N 91  
ASN   H2   H  N N 92  
ASN   HA   H  N N 93  
ASN   HB2  H  N N 94  
ASN   HB3  H  N N 95  
ASN   HD21 H  N N 96  
ASN   HD22 H  N N 97  
ASN   HXT  H  N N 98  
ASP   N    N  N N 99  
ASP   CA   C  N S 100 
ASP   C    C  N N 101 
ASP   O    O  N N 102 
ASP   CB   C  N N 103 
ASP   CG   C  N N 104 
ASP   OD1  O  N N 105 
ASP   OD2  O  N N 106 
ASP   OXT  O  N N 107 
ASP   H    H  N N 108 
ASP   H2   H  N N 109 
ASP   HA   H  N N 110 
ASP   HB2  H  N N 111 
ASP   HB3  H  N N 112 
ASP   HD2  H  N N 113 
ASP   HXT  H  N N 114 
CYS   N    N  N N 115 
CYS   CA   C  N R 116 
CYS   C    C  N N 117 
CYS   O    O  N N 118 
CYS   CB   C  N N 119 
CYS   SG   S  N N 120 
CYS   OXT  O  N N 121 
CYS   H    H  N N 122 
CYS   H2   H  N N 123 
CYS   HA   H  N N 124 
CYS   HB2  H  N N 125 
CYS   HB3  H  N N 126 
CYS   HG   H  N N 127 
CYS   HXT  H  N N 128 
GLN   N    N  N N 129 
GLN   CA   C  N S 130 
GLN   C    C  N N 131 
GLN   O    O  N N 132 
GLN   CB   C  N N 133 
GLN   CG   C  N N 134 
GLN   CD   C  N N 135 
GLN   OE1  O  N N 136 
GLN   NE2  N  N N 137 
GLN   OXT  O  N N 138 
GLN   H    H  N N 139 
GLN   H2   H  N N 140 
GLN   HA   H  N N 141 
GLN   HB2  H  N N 142 
GLN   HB3  H  N N 143 
GLN   HG2  H  N N 144 
GLN   HG3  H  N N 145 
GLN   HE21 H  N N 146 
GLN   HE22 H  N N 147 
GLN   HXT  H  N N 148 
GLU   N    N  N N 149 
GLU   CA   C  N S 150 
GLU   C    C  N N 151 
GLU   O    O  N N 152 
GLU   CB   C  N N 153 
GLU   CG   C  N N 154 
GLU   CD   C  N N 155 
GLU   OE1  O  N N 156 
GLU   OE2  O  N N 157 
GLU   OXT  O  N N 158 
GLU   H    H  N N 159 
GLU   H2   H  N N 160 
GLU   HA   H  N N 161 
GLU   HB2  H  N N 162 
GLU   HB3  H  N N 163 
GLU   HG2  H  N N 164 
GLU   HG3  H  N N 165 
GLU   HE2  H  N N 166 
GLU   HXT  H  N N 167 
GLY   N    N  N N 168 
GLY   CA   C  N N 169 
GLY   C    C  N N 170 
GLY   O    O  N N 171 
GLY   OXT  O  N N 172 
GLY   H    H  N N 173 
GLY   H2   H  N N 174 
GLY   HA2  H  N N 175 
GLY   HA3  H  N N 176 
GLY   HXT  H  N N 177 
H4B   N1   N  Y N 178 
H4B   C2   C  Y N 179 
H4B   N2   N  N N 180 
H4B   N3   N  Y N 181 
H4B   C4   C  Y N 182 
H4B   O4   O  N N 183 
H4B   C4A  C  Y N 184 
H4B   C8A  C  Y N 185 
H4B   N5   N  N N 186 
H4B   N8   N  N N 187 
H4B   C6   C  N R 188 
H4B   C7   C  N N 189 
H4B   C9   C  N R 190 
H4B   O9   O  N N 191 
H4B   C10  C  N S 192 
H4B   C11  C  N N 193 
H4B   O10  O  N N 194 
H4B   HN21 H  N N 195 
H4B   HN22 H  N N 196 
H4B   HN3  H  N N 197 
H4B   HN5  H  N N 198 
H4B   HN8  H  N N 199 
H4B   H6   H  N N 200 
H4B   H71  H  N N 201 
H4B   H72  H  N N 202 
H4B   H9   H  N N 203 
H4B   HO9  H  N N 204 
H4B   H10  H  N N 205 
H4B   H111 H  N N 206 
H4B   H112 H  N N 207 
H4B   H113 H  N N 208 
H4B   HO0  H  N N 209 
HEM   CHA  C  N N 210 
HEM   CHB  C  N N 211 
HEM   CHC  C  N N 212 
HEM   CHD  C  N N 213 
HEM   C1A  C  Y N 214 
HEM   C2A  C  Y N 215 
HEM   C3A  C  Y N 216 
HEM   C4A  C  Y N 217 
HEM   CMA  C  N N 218 
HEM   CAA  C  N N 219 
HEM   CBA  C  N N 220 
HEM   CGA  C  N N 221 
HEM   O1A  O  N N 222 
HEM   O2A  O  N N 223 
HEM   C1B  C  N N 224 
HEM   C2B  C  N N 225 
HEM   C3B  C  N N 226 
HEM   C4B  C  N N 227 
HEM   CMB  C  N N 228 
HEM   CAB  C  N N 229 
HEM   CBB  C  N N 230 
HEM   C1C  C  Y N 231 
HEM   C2C  C  Y N 232 
HEM   C3C  C  Y N 233 
HEM   C4C  C  Y N 234 
HEM   CMC  C  N N 235 
HEM   CAC  C  N N 236 
HEM   CBC  C  N N 237 
HEM   C1D  C  N N 238 
HEM   C2D  C  N N 239 
HEM   C3D  C  N N 240 
HEM   C4D  C  N N 241 
HEM   CMD  C  N N 242 
HEM   CAD  C  N N 243 
HEM   CBD  C  N N 244 
HEM   CGD  C  N N 245 
HEM   O1D  O  N N 246 
HEM   O2D  O  N N 247 
HEM   NA   N  Y N 248 
HEM   NB   N  N N 249 
HEM   NC   N  Y N 250 
HEM   ND   N  N N 251 
HEM   FE   FE N N 252 
HEM   HHB  H  N N 253 
HEM   HHC  H  N N 254 
HEM   HHD  H  N N 255 
HEM   HMA  H  N N 256 
HEM   HMAA H  N N 257 
HEM   HMAB H  N N 258 
HEM   HAA  H  N N 259 
HEM   HAAA H  N N 260 
HEM   HBA  H  N N 261 
HEM   HBAA H  N N 262 
HEM   HMB  H  N N 263 
HEM   HMBA H  N N 264 
HEM   HMBB H  N N 265 
HEM   HAB  H  N N 266 
HEM   HBB  H  N N 267 
HEM   HBBA H  N N 268 
HEM   HMC  H  N N 269 
HEM   HMCA H  N N 270 
HEM   HMCB H  N N 271 
HEM   HAC  H  N N 272 
HEM   HBC  H  N N 273 
HEM   HBCA H  N N 274 
HEM   HMD  H  N N 275 
HEM   HMDA H  N N 276 
HEM   HMDB H  N N 277 
HEM   HAD  H  N N 278 
HEM   HADA H  N N 279 
HEM   HBD  H  N N 280 
HEM   HBDA H  N N 281 
HEM   H2A  H  N N 282 
HEM   H2D  H  N N 283 
HEM   HHA  H  N N 284 
HIS   N    N  N N 285 
HIS   CA   C  N S 286 
HIS   C    C  N N 287 
HIS   O    O  N N 288 
HIS   CB   C  N N 289 
HIS   CG   C  Y N 290 
HIS   ND1  N  Y N 291 
HIS   CD2  C  Y N 292 
HIS   CE1  C  Y N 293 
HIS   NE2  N  Y N 294 
HIS   OXT  O  N N 295 
HIS   H    H  N N 296 
HIS   H2   H  N N 297 
HIS   HA   H  N N 298 
HIS   HB2  H  N N 299 
HIS   HB3  H  N N 300 
HIS   HD1  H  N N 301 
HIS   HD2  H  N N 302 
HIS   HE1  H  N N 303 
HIS   HE2  H  N N 304 
HIS   HXT  H  N N 305 
HOH   O    O  N N 306 
HOH   H1   H  N N 307 
HOH   H2   H  N N 308 
ILE   N    N  N N 309 
ILE   CA   C  N S 310 
ILE   C    C  N N 311 
ILE   O    O  N N 312 
ILE   CB   C  N S 313 
ILE   CG1  C  N N 314 
ILE   CG2  C  N N 315 
ILE   CD1  C  N N 316 
ILE   OXT  O  N N 317 
ILE   H    H  N N 318 
ILE   H2   H  N N 319 
ILE   HA   H  N N 320 
ILE   HB   H  N N 321 
ILE   HG12 H  N N 322 
ILE   HG13 H  N N 323 
ILE   HG21 H  N N 324 
ILE   HG22 H  N N 325 
ILE   HG23 H  N N 326 
ILE   HD11 H  N N 327 
ILE   HD12 H  N N 328 
ILE   HD13 H  N N 329 
ILE   HXT  H  N N 330 
LEU   N    N  N N 331 
LEU   CA   C  N S 332 
LEU   C    C  N N 333 
LEU   O    O  N N 334 
LEU   CB   C  N N 335 
LEU   CG   C  N N 336 
LEU   CD1  C  N N 337 
LEU   CD2  C  N N 338 
LEU   OXT  O  N N 339 
LEU   H    H  N N 340 
LEU   H2   H  N N 341 
LEU   HA   H  N N 342 
LEU   HB2  H  N N 343 
LEU   HB3  H  N N 344 
LEU   HG   H  N N 345 
LEU   HD11 H  N N 346 
LEU   HD12 H  N N 347 
LEU   HD13 H  N N 348 
LEU   HD21 H  N N 349 
LEU   HD22 H  N N 350 
LEU   HD23 H  N N 351 
LEU   HXT  H  N N 352 
LYS   N    N  N N 353 
LYS   CA   C  N S 354 
LYS   C    C  N N 355 
LYS   O    O  N N 356 
LYS   CB   C  N N 357 
LYS   CG   C  N N 358 
LYS   CD   C  N N 359 
LYS   CE   C  N N 360 
LYS   NZ   N  N N 361 
LYS   OXT  O  N N 362 
LYS   H    H  N N 363 
LYS   H2   H  N N 364 
LYS   HA   H  N N 365 
LYS   HB2  H  N N 366 
LYS   HB3  H  N N 367 
LYS   HG2  H  N N 368 
LYS   HG3  H  N N 369 
LYS   HD2  H  N N 370 
LYS   HD3  H  N N 371 
LYS   HE2  H  N N 372 
LYS   HE3  H  N N 373 
LYS   HZ1  H  N N 374 
LYS   HZ2  H  N N 375 
LYS   HZ3  H  N N 376 
LYS   HXT  H  N N 377 
MET   N    N  N N 378 
MET   CA   C  N S 379 
MET   C    C  N N 380 
MET   O    O  N N 381 
MET   CB   C  N N 382 
MET   CG   C  N N 383 
MET   SD   S  N N 384 
MET   CE   C  N N 385 
MET   OXT  O  N N 386 
MET   H    H  N N 387 
MET   H2   H  N N 388 
MET   HA   H  N N 389 
MET   HB2  H  N N 390 
MET   HB3  H  N N 391 
MET   HG2  H  N N 392 
MET   HG3  H  N N 393 
MET   HE1  H  N N 394 
MET   HE2  H  N N 395 
MET   HE3  H  N N 396 
MET   HXT  H  N N 397 
PHE   N    N  N N 398 
PHE   CA   C  N S 399 
PHE   C    C  N N 400 
PHE   O    O  N N 401 
PHE   CB   C  N N 402 
PHE   CG   C  Y N 403 
PHE   CD1  C  Y N 404 
PHE   CD2  C  Y N 405 
PHE   CE1  C  Y N 406 
PHE   CE2  C  Y N 407 
PHE   CZ   C  Y N 408 
PHE   OXT  O  N N 409 
PHE   H    H  N N 410 
PHE   H2   H  N N 411 
PHE   HA   H  N N 412 
PHE   HB2  H  N N 413 
PHE   HB3  H  N N 414 
PHE   HD1  H  N N 415 
PHE   HD2  H  N N 416 
PHE   HE1  H  N N 417 
PHE   HE2  H  N N 418 
PHE   HZ   H  N N 419 
PHE   HXT  H  N N 420 
PRO   N    N  N N 421 
PRO   CA   C  N S 422 
PRO   C    C  N N 423 
PRO   O    O  N N 424 
PRO   CB   C  N N 425 
PRO   CG   C  N N 426 
PRO   CD   C  N N 427 
PRO   OXT  O  N N 428 
PRO   H    H  N N 429 
PRO   HA   H  N N 430 
PRO   HB2  H  N N 431 
PRO   HB3  H  N N 432 
PRO   HG2  H  N N 433 
PRO   HG3  H  N N 434 
PRO   HD2  H  N N 435 
PRO   HD3  H  N N 436 
PRO   HXT  H  N N 437 
SER   N    N  N N 438 
SER   CA   C  N S 439 
SER   C    C  N N 440 
SER   O    O  N N 441 
SER   CB   C  N N 442 
SER   OG   O  N N 443 
SER   OXT  O  N N 444 
SER   H    H  N N 445 
SER   H2   H  N N 446 
SER   HA   H  N N 447 
SER   HB2  H  N N 448 
SER   HB3  H  N N 449 
SER   HG   H  N N 450 
SER   HXT  H  N N 451 
THR   N    N  N N 452 
THR   CA   C  N S 453 
THR   C    C  N N 454 
THR   O    O  N N 455 
THR   CB   C  N R 456 
THR   OG1  O  N N 457 
THR   CG2  C  N N 458 
THR   OXT  O  N N 459 
THR   H    H  N N 460 
THR   H2   H  N N 461 
THR   HA   H  N N 462 
THR   HB   H  N N 463 
THR   HG1  H  N N 464 
THR   HG21 H  N N 465 
THR   HG22 H  N N 466 
THR   HG23 H  N N 467 
THR   HXT  H  N N 468 
TRP   N    N  N N 469 
TRP   CA   C  N S 470 
TRP   C    C  N N 471 
TRP   O    O  N N 472 
TRP   CB   C  N N 473 
TRP   CG   C  Y N 474 
TRP   CD1  C  Y N 475 
TRP   CD2  C  Y N 476 
TRP   NE1  N  Y N 477 
TRP   CE2  C  Y N 478 
TRP   CE3  C  Y N 479 
TRP   CZ2  C  Y N 480 
TRP   CZ3  C  Y N 481 
TRP   CH2  C  Y N 482 
TRP   OXT  O  N N 483 
TRP   H    H  N N 484 
TRP   H2   H  N N 485 
TRP   HA   H  N N 486 
TRP   HB2  H  N N 487 
TRP   HB3  H  N N 488 
TRP   HD1  H  N N 489 
TRP   HE1  H  N N 490 
TRP   HE3  H  N N 491 
TRP   HZ2  H  N N 492 
TRP   HZ3  H  N N 493 
TRP   HH2  H  N N 494 
TRP   HXT  H  N N 495 
TYR   N    N  N N 496 
TYR   CA   C  N S 497 
TYR   C    C  N N 498 
TYR   O    O  N N 499 
TYR   CB   C  N N 500 
TYR   CG   C  Y N 501 
TYR   CD1  C  Y N 502 
TYR   CD2  C  Y N 503 
TYR   CE1  C  Y N 504 
TYR   CE2  C  Y N 505 
TYR   CZ   C  Y N 506 
TYR   OH   O  N N 507 
TYR   OXT  O  N N 508 
TYR   H    H  N N 509 
TYR   H2   H  N N 510 
TYR   HA   H  N N 511 
TYR   HB2  H  N N 512 
TYR   HB3  H  N N 513 
TYR   HD1  H  N N 514 
TYR   HD2  H  N N 515 
TYR   HE1  H  N N 516 
TYR   HE2  H  N N 517 
TYR   HH   H  N N 518 
TYR   HXT  H  N N 519 
VAL   N    N  N N 520 
VAL   CA   C  N S 521 
VAL   C    C  N N 522 
VAL   O    O  N N 523 
VAL   CB   C  N N 524 
VAL   CG1  C  N N 525 
VAL   CG2  C  N N 526 
VAL   OXT  O  N N 527 
VAL   H    H  N N 528 
VAL   H2   H  N N 529 
VAL   HA   H  N N 530 
VAL   HB   H  N N 531 
VAL   HG11 H  N N 532 
VAL   HG12 H  N N 533 
VAL   HG13 H  N N 534 
VAL   HG21 H  N N 535 
VAL   HG22 H  N N 536 
VAL   HG23 H  N N 537 
VAL   HXT  H  N N 538 
ZN    ZN   ZN N N 539 
# 
loop_
_chem_comp_bond.comp_id 
_chem_comp_bond.atom_id_1 
_chem_comp_bond.atom_id_2 
_chem_comp_bond.value_order 
_chem_comp_bond.pdbx_aromatic_flag 
_chem_comp_bond.pdbx_stereo_config 
_chem_comp_bond.pdbx_ordinal 
A1A0G C07 C04  sing N N 1   
A1A0G C04 C03  doub Y N 2   
A1A0G C04 C05  sing Y N 3   
A1A0G C03 C02  sing Y N 4   
A1A0G C05 C06  doub Y N 5   
A1A0G C02 N02  sing N N 6   
A1A0G C02 N01  doub Y N 7   
A1A0G C06 N01  sing Y N 8   
A1A0G C06 C11  sing N N 9   
A1A0G C11 C16  doub Y N 10  
A1A0G C11 C12  sing Y N 11  
A1A0G C16 C15  sing Y N 12  
A1A0G C12 C13  doub Y N 13  
A1A0G C15 C17  sing N N 14  
A1A0G C15 C14  doub Y N 15  
A1A0G C17 N18  sing N N 16  
A1A0G C13 C14  sing Y N 17  
A1A0G C13 CL1  sing N N 18  
A1A0G N18 C19  sing N N 19  
A1A0G C12 H1   sing N N 20  
A1A0G C14 H2   sing N N 21  
A1A0G C16 H3   sing N N 22  
A1A0G C17 H4   sing N N 23  
A1A0G C17 H5   sing N N 24  
A1A0G C03 H6   sing N N 25  
A1A0G C05 H7   sing N N 26  
A1A0G C07 H8   sing N N 27  
A1A0G C07 H9   sing N N 28  
A1A0G C07 H10  sing N N 29  
A1A0G C19 H11  sing N N 30  
A1A0G C19 H12  sing N N 31  
A1A0G C19 H13  sing N N 32  
A1A0G N02 H14  sing N N 33  
A1A0G N02 H15  sing N N 34  
A1A0G N18 H16  sing N N 35  
ACT   C   O    doub N N 36  
ACT   C   OXT  sing N N 37  
ACT   C   CH3  sing N N 38  
ACT   CH3 H1   sing N N 39  
ACT   CH3 H2   sing N N 40  
ACT   CH3 H3   sing N N 41  
ALA   N   CA   sing N N 42  
ALA   N   H    sing N N 43  
ALA   N   H2   sing N N 44  
ALA   CA  C    sing N N 45  
ALA   CA  CB   sing N N 46  
ALA   CA  HA   sing N N 47  
ALA   C   O    doub N N 48  
ALA   C   OXT  sing N N 49  
ALA   CB  HB1  sing N N 50  
ALA   CB  HB2  sing N N 51  
ALA   CB  HB3  sing N N 52  
ALA   OXT HXT  sing N N 53  
ARG   N   CA   sing N N 54  
ARG   N   H    sing N N 55  
ARG   N   H2   sing N N 56  
ARG   CA  C    sing N N 57  
ARG   CA  CB   sing N N 58  
ARG   CA  HA   sing N N 59  
ARG   C   O    doub N N 60  
ARG   C   OXT  sing N N 61  
ARG   CB  CG   sing N N 62  
ARG   CB  HB2  sing N N 63  
ARG   CB  HB3  sing N N 64  
ARG   CG  CD   sing N N 65  
ARG   CG  HG2  sing N N 66  
ARG   CG  HG3  sing N N 67  
ARG   CD  NE   sing N N 68  
ARG   CD  HD2  sing N N 69  
ARG   CD  HD3  sing N N 70  
ARG   NE  CZ   sing N N 71  
ARG   NE  HE   sing N N 72  
ARG   CZ  NH1  sing N N 73  
ARG   CZ  NH2  doub N N 74  
ARG   NH1 HH11 sing N N 75  
ARG   NH1 HH12 sing N N 76  
ARG   NH2 HH21 sing N N 77  
ARG   NH2 HH22 sing N N 78  
ARG   OXT HXT  sing N N 79  
ASN   N   CA   sing N N 80  
ASN   N   H    sing N N 81  
ASN   N   H2   sing N N 82  
ASN   CA  C    sing N N 83  
ASN   CA  CB   sing N N 84  
ASN   CA  HA   sing N N 85  
ASN   C   O    doub N N 86  
ASN   C   OXT  sing N N 87  
ASN   CB  CG   sing N N 88  
ASN   CB  HB2  sing N N 89  
ASN   CB  HB3  sing N N 90  
ASN   CG  OD1  doub N N 91  
ASN   CG  ND2  sing N N 92  
ASN   ND2 HD21 sing N N 93  
ASN   ND2 HD22 sing N N 94  
ASN   OXT HXT  sing N N 95  
ASP   N   CA   sing N N 96  
ASP   N   H    sing N N 97  
ASP   N   H2   sing N N 98  
ASP   CA  C    sing N N 99  
ASP   CA  CB   sing N N 100 
ASP   CA  HA   sing N N 101 
ASP   C   O    doub N N 102 
ASP   C   OXT  sing N N 103 
ASP   CB  CG   sing N N 104 
ASP   CB  HB2  sing N N 105 
ASP   CB  HB3  sing N N 106 
ASP   CG  OD1  doub N N 107 
ASP   CG  OD2  sing N N 108 
ASP   OD2 HD2  sing N N 109 
ASP   OXT HXT  sing N N 110 
CYS   N   CA   sing N N 111 
CYS   N   H    sing N N 112 
CYS   N   H2   sing N N 113 
CYS   CA  C    sing N N 114 
CYS   CA  CB   sing N N 115 
CYS   CA  HA   sing N N 116 
CYS   C   O    doub N N 117 
CYS   C   OXT  sing N N 118 
CYS   CB  SG   sing N N 119 
CYS   CB  HB2  sing N N 120 
CYS   CB  HB3  sing N N 121 
CYS   SG  HG   sing N N 122 
CYS   OXT HXT  sing N N 123 
GLN   N   CA   sing N N 124 
GLN   N   H    sing N N 125 
GLN   N   H2   sing N N 126 
GLN   CA  C    sing N N 127 
GLN   CA  CB   sing N N 128 
GLN   CA  HA   sing N N 129 
GLN   C   O    doub N N 130 
GLN   C   OXT  sing N N 131 
GLN   CB  CG   sing N N 132 
GLN   CB  HB2  sing N N 133 
GLN   CB  HB3  sing N N 134 
GLN   CG  CD   sing N N 135 
GLN   CG  HG2  sing N N 136 
GLN   CG  HG3  sing N N 137 
GLN   CD  OE1  doub N N 138 
GLN   CD  NE2  sing N N 139 
GLN   NE2 HE21 sing N N 140 
GLN   NE2 HE22 sing N N 141 
GLN   OXT HXT  sing N N 142 
GLU   N   CA   sing N N 143 
GLU   N   H    sing N N 144 
GLU   N   H2   sing N N 145 
GLU   CA  C    sing N N 146 
GLU   CA  CB   sing N N 147 
GLU   CA  HA   sing N N 148 
GLU   C   O    doub N N 149 
GLU   C   OXT  sing N N 150 
GLU   CB  CG   sing N N 151 
GLU   CB  HB2  sing N N 152 
GLU   CB  HB3  sing N N 153 
GLU   CG  CD   sing N N 154 
GLU   CG  HG2  sing N N 155 
GLU   CG  HG3  sing N N 156 
GLU   CD  OE1  doub N N 157 
GLU   CD  OE2  sing N N 158 
GLU   OE2 HE2  sing N N 159 
GLU   OXT HXT  sing N N 160 
GLY   N   CA   sing N N 161 
GLY   N   H    sing N N 162 
GLY   N   H2   sing N N 163 
GLY   CA  C    sing N N 164 
GLY   CA  HA2  sing N N 165 
GLY   CA  HA3  sing N N 166 
GLY   C   O    doub N N 167 
GLY   C   OXT  sing N N 168 
GLY   OXT HXT  sing N N 169 
H4B   N1  C2   doub Y N 170 
H4B   N1  C8A  sing Y N 171 
H4B   C2  N2   sing N N 172 
H4B   C2  N3   sing Y N 173 
H4B   N2  HN21 sing N N 174 
H4B   N2  HN22 sing N N 175 
H4B   N3  C4   sing Y N 176 
H4B   N3  HN3  sing N N 177 
H4B   C4  O4   doub N N 178 
H4B   C4  C4A  sing Y N 179 
H4B   C4A C8A  doub Y N 180 
H4B   C4A N5   sing N N 181 
H4B   C8A N8   sing N N 182 
H4B   N5  C6   sing N N 183 
H4B   N5  HN5  sing N N 184 
H4B   N8  C7   sing N N 185 
H4B   N8  HN8  sing N N 186 
H4B   C6  C7   sing N N 187 
H4B   C6  C9   sing N N 188 
H4B   C6  H6   sing N N 189 
H4B   C7  H71  sing N N 190 
H4B   C7  H72  sing N N 191 
H4B   C9  O9   sing N N 192 
H4B   C9  C10  sing N N 193 
H4B   C9  H9   sing N N 194 
H4B   O9  HO9  sing N N 195 
H4B   C10 C11  sing N N 196 
H4B   C10 O10  sing N N 197 
H4B   C10 H10  sing N N 198 
H4B   C11 H111 sing N N 199 
H4B   C11 H112 sing N N 200 
H4B   C11 H113 sing N N 201 
H4B   O10 HO0  sing N N 202 
HEM   CHA C1A  sing N N 203 
HEM   CHA C4D  doub N N 204 
HEM   CHA HHA  sing N N 205 
HEM   CHB C4A  sing N N 206 
HEM   CHB C1B  doub N N 207 
HEM   CHB HHB  sing N N 208 
HEM   CHC C4B  sing N N 209 
HEM   CHC C1C  doub N N 210 
HEM   CHC HHC  sing N N 211 
HEM   CHD C4C  doub N N 212 
HEM   CHD C1D  sing N N 213 
HEM   CHD HHD  sing N N 214 
HEM   C1A C2A  doub Y N 215 
HEM   C1A NA   sing Y N 216 
HEM   C2A C3A  sing Y N 217 
HEM   C2A CAA  sing N N 218 
HEM   C3A C4A  doub Y N 219 
HEM   C3A CMA  sing N N 220 
HEM   C4A NA   sing Y N 221 
HEM   CMA HMA  sing N N 222 
HEM   CMA HMAA sing N N 223 
HEM   CMA HMAB sing N N 224 
HEM   CAA CBA  sing N N 225 
HEM   CAA HAA  sing N N 226 
HEM   CAA HAAA sing N N 227 
HEM   CBA CGA  sing N N 228 
HEM   CBA HBA  sing N N 229 
HEM   CBA HBAA sing N N 230 
HEM   CGA O1A  doub N N 231 
HEM   CGA O2A  sing N N 232 
HEM   C1B C2B  sing N N 233 
HEM   C1B NB   sing N N 234 
HEM   C2B C3B  doub N N 235 
HEM   C2B CMB  sing N N 236 
HEM   C3B C4B  sing N N 237 
HEM   C3B CAB  sing N N 238 
HEM   C4B NB   doub N N 239 
HEM   CMB HMB  sing N N 240 
HEM   CMB HMBA sing N N 241 
HEM   CMB HMBB sing N N 242 
HEM   CAB CBB  doub N N 243 
HEM   CAB HAB  sing N N 244 
HEM   CBB HBB  sing N N 245 
HEM   CBB HBBA sing N N 246 
HEM   C1C C2C  sing Y N 247 
HEM   C1C NC   sing Y N 248 
HEM   C2C C3C  doub Y N 249 
HEM   C2C CMC  sing N N 250 
HEM   C3C C4C  sing Y N 251 
HEM   C3C CAC  sing N N 252 
HEM   C4C NC   sing Y N 253 
HEM   CMC HMC  sing N N 254 
HEM   CMC HMCA sing N N 255 
HEM   CMC HMCB sing N N 256 
HEM   CAC CBC  doub N N 257 
HEM   CAC HAC  sing N N 258 
HEM   CBC HBC  sing N N 259 
HEM   CBC HBCA sing N N 260 
HEM   C1D C2D  sing N N 261 
HEM   C1D ND   doub N N 262 
HEM   C2D C3D  doub N N 263 
HEM   C2D CMD  sing N N 264 
HEM   C3D C4D  sing N N 265 
HEM   C3D CAD  sing N N 266 
HEM   C4D ND   sing N N 267 
HEM   CMD HMD  sing N N 268 
HEM   CMD HMDA sing N N 269 
HEM   CMD HMDB sing N N 270 
HEM   CAD CBD  sing N N 271 
HEM   CAD HAD  sing N N 272 
HEM   CAD HADA sing N N 273 
HEM   CBD CGD  sing N N 274 
HEM   CBD HBD  sing N N 275 
HEM   CBD HBDA sing N N 276 
HEM   CGD O1D  doub N N 277 
HEM   CGD O2D  sing N N 278 
HEM   O2A H2A  sing N N 279 
HEM   O2D H2D  sing N N 280 
HEM   FE  NA   sing N N 281 
HEM   FE  NB   sing N N 282 
HEM   FE  NC   sing N N 283 
HEM   FE  ND   sing N N 284 
HIS   N   CA   sing N N 285 
HIS   N   H    sing N N 286 
HIS   N   H2   sing N N 287 
HIS   CA  C    sing N N 288 
HIS   CA  CB   sing N N 289 
HIS   CA  HA   sing N N 290 
HIS   C   O    doub N N 291 
HIS   C   OXT  sing N N 292 
HIS   CB  CG   sing N N 293 
HIS   CB  HB2  sing N N 294 
HIS   CB  HB3  sing N N 295 
HIS   CG  ND1  sing Y N 296 
HIS   CG  CD2  doub Y N 297 
HIS   ND1 CE1  doub Y N 298 
HIS   ND1 HD1  sing N N 299 
HIS   CD2 NE2  sing Y N 300 
HIS   CD2 HD2  sing N N 301 
HIS   CE1 NE2  sing Y N 302 
HIS   CE1 HE1  sing N N 303 
HIS   NE2 HE2  sing N N 304 
HIS   OXT HXT  sing N N 305 
HOH   O   H1   sing N N 306 
HOH   O   H2   sing N N 307 
ILE   N   CA   sing N N 308 
ILE   N   H    sing N N 309 
ILE   N   H2   sing N N 310 
ILE   CA  C    sing N N 311 
ILE   CA  CB   sing N N 312 
ILE   CA  HA   sing N N 313 
ILE   C   O    doub N N 314 
ILE   C   OXT  sing N N 315 
ILE   CB  CG1  sing N N 316 
ILE   CB  CG2  sing N N 317 
ILE   CB  HB   sing N N 318 
ILE   CG1 CD1  sing N N 319 
ILE   CG1 HG12 sing N N 320 
ILE   CG1 HG13 sing N N 321 
ILE   CG2 HG21 sing N N 322 
ILE   CG2 HG22 sing N N 323 
ILE   CG2 HG23 sing N N 324 
ILE   CD1 HD11 sing N N 325 
ILE   CD1 HD12 sing N N 326 
ILE   CD1 HD13 sing N N 327 
ILE   OXT HXT  sing N N 328 
LEU   N   CA   sing N N 329 
LEU   N   H    sing N N 330 
LEU   N   H2   sing N N 331 
LEU   CA  C    sing N N 332 
LEU   CA  CB   sing N N 333 
LEU   CA  HA   sing N N 334 
LEU   C   O    doub N N 335 
LEU   C   OXT  sing N N 336 
LEU   CB  CG   sing N N 337 
LEU   CB  HB2  sing N N 338 
LEU   CB  HB3  sing N N 339 
LEU   CG  CD1  sing N N 340 
LEU   CG  CD2  sing N N 341 
LEU   CG  HG   sing N N 342 
LEU   CD1 HD11 sing N N 343 
LEU   CD1 HD12 sing N N 344 
LEU   CD1 HD13 sing N N 345 
LEU   CD2 HD21 sing N N 346 
LEU   CD2 HD22 sing N N 347 
LEU   CD2 HD23 sing N N 348 
LEU   OXT HXT  sing N N 349 
LYS   N   CA   sing N N 350 
LYS   N   H    sing N N 351 
LYS   N   H2   sing N N 352 
LYS   CA  C    sing N N 353 
LYS   CA  CB   sing N N 354 
LYS   CA  HA   sing N N 355 
LYS   C   O    doub N N 356 
LYS   C   OXT  sing N N 357 
LYS   CB  CG   sing N N 358 
LYS   CB  HB2  sing N N 359 
LYS   CB  HB3  sing N N 360 
LYS   CG  CD   sing N N 361 
LYS   CG  HG2  sing N N 362 
LYS   CG  HG3  sing N N 363 
LYS   CD  CE   sing N N 364 
LYS   CD  HD2  sing N N 365 
LYS   CD  HD3  sing N N 366 
LYS   CE  NZ   sing N N 367 
LYS   CE  HE2  sing N N 368 
LYS   CE  HE3  sing N N 369 
LYS   NZ  HZ1  sing N N 370 
LYS   NZ  HZ2  sing N N 371 
LYS   NZ  HZ3  sing N N 372 
LYS   OXT HXT  sing N N 373 
MET   N   CA   sing N N 374 
MET   N   H    sing N N 375 
MET   N   H2   sing N N 376 
MET   CA  C    sing N N 377 
MET   CA  CB   sing N N 378 
MET   CA  HA   sing N N 379 
MET   C   O    doub N N 380 
MET   C   OXT  sing N N 381 
MET   CB  CG   sing N N 382 
MET   CB  HB2  sing N N 383 
MET   CB  HB3  sing N N 384 
MET   CG  SD   sing N N 385 
MET   CG  HG2  sing N N 386 
MET   CG  HG3  sing N N 387 
MET   SD  CE   sing N N 388 
MET   CE  HE1  sing N N 389 
MET   CE  HE2  sing N N 390 
MET   CE  HE3  sing N N 391 
MET   OXT HXT  sing N N 392 
PHE   N   CA   sing N N 393 
PHE   N   H    sing N N 394 
PHE   N   H2   sing N N 395 
PHE   CA  C    sing N N 396 
PHE   CA  CB   sing N N 397 
PHE   CA  HA   sing N N 398 
PHE   C   O    doub N N 399 
PHE   C   OXT  sing N N 400 
PHE   CB  CG   sing N N 401 
PHE   CB  HB2  sing N N 402 
PHE   CB  HB3  sing N N 403 
PHE   CG  CD1  doub Y N 404 
PHE   CG  CD2  sing Y N 405 
PHE   CD1 CE1  sing Y N 406 
PHE   CD1 HD1  sing N N 407 
PHE   CD2 CE2  doub Y N 408 
PHE   CD2 HD2  sing N N 409 
PHE   CE1 CZ   doub Y N 410 
PHE   CE1 HE1  sing N N 411 
PHE   CE2 CZ   sing Y N 412 
PHE   CE2 HE2  sing N N 413 
PHE   CZ  HZ   sing N N 414 
PHE   OXT HXT  sing N N 415 
PRO   N   CA   sing N N 416 
PRO   N   CD   sing N N 417 
PRO   N   H    sing N N 418 
PRO   CA  C    sing N N 419 
PRO   CA  CB   sing N N 420 
PRO   CA  HA   sing N N 421 
PRO   C   O    doub N N 422 
PRO   C   OXT  sing N N 423 
PRO   CB  CG   sing N N 424 
PRO   CB  HB2  sing N N 425 
PRO   CB  HB3  sing N N 426 
PRO   CG  CD   sing N N 427 
PRO   CG  HG2  sing N N 428 
PRO   CG  HG3  sing N N 429 
PRO   CD  HD2  sing N N 430 
PRO   CD  HD3  sing N N 431 
PRO   OXT HXT  sing N N 432 
SER   N   CA   sing N N 433 
SER   N   H    sing N N 434 
SER   N   H2   sing N N 435 
SER   CA  C    sing N N 436 
SER   CA  CB   sing N N 437 
SER   CA  HA   sing N N 438 
SER   C   O    doub N N 439 
SER   C   OXT  sing N N 440 
SER   CB  OG   sing N N 441 
SER   CB  HB2  sing N N 442 
SER   CB  HB3  sing N N 443 
SER   OG  HG   sing N N 444 
SER   OXT HXT  sing N N 445 
THR   N   CA   sing N N 446 
THR   N   H    sing N N 447 
THR   N   H2   sing N N 448 
THR   CA  C    sing N N 449 
THR   CA  CB   sing N N 450 
THR   CA  HA   sing N N 451 
THR   C   O    doub N N 452 
THR   C   OXT  sing N N 453 
THR   CB  OG1  sing N N 454 
THR   CB  CG2  sing N N 455 
THR   CB  HB   sing N N 456 
THR   OG1 HG1  sing N N 457 
THR   CG2 HG21 sing N N 458 
THR   CG2 HG22 sing N N 459 
THR   CG2 HG23 sing N N 460 
THR   OXT HXT  sing N N 461 
TRP   N   CA   sing N N 462 
TRP   N   H    sing N N 463 
TRP   N   H2   sing N N 464 
TRP   CA  C    sing N N 465 
TRP   CA  CB   sing N N 466 
TRP   CA  HA   sing N N 467 
TRP   C   O    doub N N 468 
TRP   C   OXT  sing N N 469 
TRP   CB  CG   sing N N 470 
TRP   CB  HB2  sing N N 471 
TRP   CB  HB3  sing N N 472 
TRP   CG  CD1  doub Y N 473 
TRP   CG  CD2  sing Y N 474 
TRP   CD1 NE1  sing Y N 475 
TRP   CD1 HD1  sing N N 476 
TRP   CD2 CE2  doub Y N 477 
TRP   CD2 CE3  sing Y N 478 
TRP   NE1 CE2  sing Y N 479 
TRP   NE1 HE1  sing N N 480 
TRP   CE2 CZ2  sing Y N 481 
TRP   CE3 CZ3  doub Y N 482 
TRP   CE3 HE3  sing N N 483 
TRP   CZ2 CH2  doub Y N 484 
TRP   CZ2 HZ2  sing N N 485 
TRP   CZ3 CH2  sing Y N 486 
TRP   CZ3 HZ3  sing N N 487 
TRP   CH2 HH2  sing N N 488 
TRP   OXT HXT  sing N N 489 
TYR   N   CA   sing N N 490 
TYR   N   H    sing N N 491 
TYR   N   H2   sing N N 492 
TYR   CA  C    sing N N 493 
TYR   CA  CB   sing N N 494 
TYR   CA  HA   sing N N 495 
TYR   C   O    doub N N 496 
TYR   C   OXT  sing N N 497 
TYR   CB  CG   sing N N 498 
TYR   CB  HB2  sing N N 499 
TYR   CB  HB3  sing N N 500 
TYR   CG  CD1  doub Y N 501 
TYR   CG  CD2  sing Y N 502 
TYR   CD1 CE1  sing Y N 503 
TYR   CD1 HD1  sing N N 504 
TYR   CD2 CE2  doub Y N 505 
TYR   CD2 HD2  sing N N 506 
TYR   CE1 CZ   doub Y N 507 
TYR   CE1 HE1  sing N N 508 
TYR   CE2 CZ   sing Y N 509 
TYR   CE2 HE2  sing N N 510 
TYR   CZ  OH   sing N N 511 
TYR   OH  HH   sing N N 512 
TYR   OXT HXT  sing N N 513 
VAL   N   CA   sing N N 514 
VAL   N   H    sing N N 515 
VAL   N   H2   sing N N 516 
VAL   CA  C    sing N N 517 
VAL   CA  CB   sing N N 518 
VAL   CA  HA   sing N N 519 
VAL   C   O    doub N N 520 
VAL   C   OXT  sing N N 521 
VAL   CB  CG1  sing N N 522 
VAL   CB  CG2  sing N N 523 
VAL   CB  HB   sing N N 524 
VAL   CG1 HG11 sing N N 525 
VAL   CG1 HG12 sing N N 526 
VAL   CG1 HG13 sing N N 527 
VAL   CG2 HG21 sing N N 528 
VAL   CG2 HG22 sing N N 529 
VAL   CG2 HG23 sing N N 530 
VAL   OXT HXT  sing N N 531 
# 
_pdbx_audit_support.funding_organization   
'National Institutes of Health/National Institute of General Medical Sciences (NIH/NIGMS)' 
_pdbx_audit_support.country                'United States' 
_pdbx_audit_support.grant_number           GM131920 
_pdbx_audit_support.ordinal                1 
# 
_pdbx_initial_refinement_model.id               1 
_pdbx_initial_refinement_model.entity_id_list   ? 
_pdbx_initial_refinement_model.type             'experimental model' 
_pdbx_initial_refinement_model.source_name      PDB 
_pdbx_initial_refinement_model.accession_code   7TS9 
_pdbx_initial_refinement_model.details          ? 
# 
_atom_sites.entry_id                    9CVK 
_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]   0.020518 
_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]   0.008824 
_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]   0.006131 
_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  
CL 
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   ? -39.030 -25.007 41.292 1.00 147.39 ? 299 ARG   A N   1 
ATOM   2    C  CA  . ARG   A 1 3   ? -38.800 -25.158 39.860 1.00 148.06 ? 299 ARG   A CA  1 
ATOM   3    C  C   . ARG   A 1 3   ? -39.568 -24.087 39.086 1.00 142.74 ? 299 ARG   A C   1 
ATOM   4    O  O   . ARG   A 1 3   ? -39.793 -24.210 37.882 1.00 152.68 ? 299 ARG   A O   1 
ATOM   5    C  CB  . ARG   A 1 3   ? -39.217 -26.562 39.398 1.00 157.68 ? 299 ARG   A CB  1 
ATOM   6    C  CG  . ARG   A 1 3   ? -38.491 -27.093 38.156 1.00 159.90 ? 299 ARG   A CG  1 
ATOM   7    C  CD  . ARG   A 1 3   ? -37.042 -27.498 38.452 1.00 162.45 ? 299 ARG   A CD  1 
ATOM   8    N  NE  . ARG   A 1 3   ? -36.144 -26.354 38.620 1.00 161.03 ? 299 ARG   A NE  1 
ATOM   9    C  CZ  . ARG   A 1 3   ? -35.106 -26.089 37.833 1.00 160.75 ? 299 ARG   A CZ  1 
ATOM   10   N  NH1 . ARG   A 1 3   ? -34.815 -26.894 36.819 1.00 163.56 ? 299 ARG   A NH1 1 
ATOM   11   N  NH2 . ARG   A 1 3   ? -34.352 -25.021 38.065 1.00 156.74 ? 299 ARG   A NH2 1 
ATOM   12   N  N   . PHE   A 1 4   ? -39.987 -23.044 39.796 1.00 128.71 ? 300 PHE   A N   1 
ATOM   13   C  CA  . PHE   A 1 4   ? -40.803 -21.964 39.248 1.00 119.81 ? 300 PHE   A CA  1 
ATOM   14   C  C   . PHE   A 1 4   ? -40.482 -20.693 40.038 1.00 118.51 ? 300 PHE   A C   1 
ATOM   15   O  O   . PHE   A 1 4   ? -41.325 -20.125 40.728 1.00 129.44 ? 300 PHE   A O   1 
ATOM   16   C  CB  . PHE   A 1 4   ? -42.291 -22.312 39.313 1.00 121.15 ? 300 PHE   A CB  1 
ATOM   17   C  CG  . PHE   A 1 4   ? -42.585 -23.799 39.408 1.00 129.19 ? 300 PHE   A CG  1 
ATOM   18   C  CD1 . PHE   A 1 4   ? -42.621 -24.439 40.645 1.00 131.23 ? 300 PHE   A CD1 1 
ATOM   19   C  CD2 . PHE   A 1 4   ? -42.837 -24.553 38.266 1.00 126.95 ? 300 PHE   A CD2 1 
ATOM   20   C  CE1 . PHE   A 1 4   ? -42.891 -25.800 40.738 1.00 131.12 ? 300 PHE   A CE1 1 
ATOM   21   C  CE2 . PHE   A 1 4   ? -43.110 -25.914 38.357 1.00 127.19 ? 300 PHE   A CE2 1 
ATOM   22   C  CZ  . PHE   A 1 4   ? -43.139 -26.537 39.592 1.00 126.39 ? 300 PHE   A CZ  1 
ATOM   23   N  N   . LEU   A 1 5   ? -39.237 -20.223 39.921 1.00 111.23 ? 301 LEU   A N   1 
ATOM   24   C  CA  . LEU   A 1 5   ? -38.654 -19.262 40.856 1.00 94.02  ? 301 LEU   A CA  1 
ATOM   25   C  C   . LEU   A 1 5   ? -39.376 -17.913 40.832 1.00 88.74  ? 301 LEU   A C   1 
ATOM   26   O  O   . LEU   A 1 5   ? -40.055 -17.547 39.869 1.00 86.64  ? 301 LEU   A O   1 
ATOM   27   C  CB  . LEU   A 1 5   ? -37.173 -19.053 40.536 1.00 78.84  ? 301 LEU   A CB  1 
ATOM   28   C  CG  . LEU   A 1 5   ? -36.345 -20.308 40.818 1.00 82.31  ? 301 LEU   A CG  1 
ATOM   29   C  CD1 . LEU   A 1 5   ? -35.152 -20.398 39.906 1.00 82.27  ? 301 LEU   A CD1 1 
ATOM   30   C  CD2 . LEU   A 1 5   ? -35.907 -20.346 42.272 1.00 81.86  ? 301 LEU   A CD2 1 
ATOM   31   N  N   . LYS   A 1 6   ? -39.199 -17.158 41.915 1.00 77.59  ? 302 LYS   A N   1 
ATOM   32   C  CA  . LYS   A 1 6   ? -39.811 -15.847 42.080 1.00 85.21  ? 302 LYS   A CA  1 
ATOM   33   C  C   . LYS   A 1 6   ? -38.737 -14.772 42.187 1.00 77.19  ? 302 LYS   A C   1 
ATOM   34   O  O   . LYS   A 1 6   ? -37.714 -14.960 42.858 1.00 69.99  ? 302 LYS   A O   1 
ATOM   35   C  CB  . LYS   A 1 6   ? -40.701 -15.798 43.333 1.00 94.96  ? 302 LYS   A CB  1 
ATOM   36   C  CG  . LYS   A 1 6   ? -41.793 -16.864 43.396 1.00 109.37 ? 302 LYS   A CG  1 
ATOM   37   C  CD  . LYS   A 1 6   ? -42.967 -16.554 42.470 1.00 113.44 ? 302 LYS   A CD  1 
ATOM   38   C  CE  . LYS   A 1 6   ? -44.147 -17.500 42.718 1.00 118.89 ? 302 LYS   A CE  1 
ATOM   39   N  NZ  . LYS   A 1 6   ? -44.893 -17.196 43.977 1.00 118.22 ? 302 LYS   A NZ  1 
ATOM   40   N  N   . VAL   A 1 7   ? -38.975 -13.641 41.528 1.00 71.56  ? 303 VAL   A N   1 
ATOM   41   C  CA  . VAL   A 1 7   ? -38.115 -12.471 41.628 1.00 66.70  ? 303 VAL   A CA  1 
ATOM   42   C  C   . VAL   A 1 7   ? -38.973 -11.296 42.067 1.00 72.28  ? 303 VAL   A C   1 
ATOM   43   O  O   . VAL   A 1 7   ? -40.052 -11.059 41.507 1.00 76.31  ? 303 VAL   A O   1 
ATOM   44   C  CB  . VAL   A 1 7   ? -37.378 -12.169 40.308 1.00 58.17  ? 303 VAL   A CB  1 
ATOM   45   C  CG1 . VAL   A 1 7   ? -36.681 -13.406 39.828 1.00 69.97  ? 303 VAL   A CG1 1 
ATOM   46   C  CG2 . VAL   A 1 7   ? -38.324 -11.636 39.205 1.00 66.09  ? 303 VAL   A CG2 1 
ATOM   47   N  N   . LYS   A 1 8   ? -38.507 -10.585 43.089 1.00 62.81  ? 304 LYS   A N   1 
ATOM   48   C  CA  . LYS   A 1 8   ? -39.252 -9.491  43.685 1.00 65.92  ? 304 LYS   A CA  1 
ATOM   49   C  C   . LYS   A 1 8   ? -38.629 -8.160  43.292 1.00 58.64  ? 304 LYS   A C   1 
ATOM   50   O  O   . LYS   A 1 8   ? -37.419 -8.058  43.068 1.00 61.83  ? 304 LYS   A O   1 
ATOM   51   C  CB  . LYS   A 1 8   ? -39.292 -9.622  45.213 1.00 63.75  ? 304 LYS   A CB  1 
ATOM   52   C  CG  . LYS   A 1 8   ? -40.108 -8.536  45.913 1.00 72.17  ? 304 LYS   A CG  1 
ATOM   53   C  CD  . LYS   A 1 8   ? -40.262 -8.815  47.413 1.00 70.49  ? 304 LYS   A CD  1 
ATOM   54   C  CE  . LYS   A 1 8   ? -41.004 -7.676  48.107 1.00 74.89  ? 304 LYS   A CE  1 
ATOM   55   N  NZ  . LYS   A 1 8   ? -41.086 -7.848  49.594 1.00 78.75  ? 304 LYS   A NZ  1 
ATOM   56   N  N   . ASN   A 1 9   ? -39.477 -7.151  43.168 1.00 56.39  ? 305 ASN   A N   1 
ATOM   57   C  CA  . ASN   A 1 9   ? -39.033 -5.766  43.132 1.00 67.51  ? 305 ASN   A CA  1 
ATOM   58   C  C   . ASN   A 1 9   ? -39.238 -5.199  44.531 1.00 69.86  ? 305 ASN   A C   1 
ATOM   59   O  O   . ASN   A 1 9   ? -40.366 -5.177  45.026 1.00 81.92  ? 305 ASN   A O   1 
ATOM   60   C  CB  . ASN   A 1 9   ? -39.815 -4.957  42.096 1.00 65.45  ? 305 ASN   A CB  1 
ATOM   61   C  CG  . ASN   A 1 9   ? -39.271 -3.554  41.926 1.00 73.95  ? 305 ASN   A CG  1 
ATOM   62   O  OD1 . ASN   A 1 9   ? -39.298 -2.751  42.857 1.00 79.84  ? 305 ASN   A OD1 1 
ATOM   63   N  ND2 . ASN   A 1 9   ? -38.774 -3.248  40.729 1.00 66.79  ? 305 ASN   A ND2 1 
ATOM   64   N  N   . TRP   A 1 10  ? -38.156 -4.756  45.174 1.00 74.77  ? 306 TRP   A N   1 
ATOM   65   C  CA  . TRP   A 1 10  ? -38.257 -4.249  46.540 1.00 84.02  ? 306 TRP   A CA  1 
ATOM   66   C  C   . TRP   A 1 10  ? -38.620 -2.773  46.615 1.00 93.86  ? 306 TRP   A C   1 
ATOM   67   O  O   . TRP   A 1 10  ? -38.841 -2.263  47.718 1.00 109.06 ? 306 TRP   A O   1 
ATOM   68   C  CB  . TRP   A 1 10  ? -36.951 -4.492  47.298 1.00 80.89  ? 306 TRP   A CB  1 
ATOM   69   C  CG  . TRP   A 1 10  ? -36.657 -5.934  47.490 1.00 76.82  ? 306 TRP   A CG  1 
ATOM   70   C  CD1 . TRP   A 1 10  ? -35.918 -6.724  46.673 1.00 68.02  ? 306 TRP   A CD1 1 
ATOM   71   C  CD2 . TRP   A 1 10  ? -37.099 -6.768  48.568 1.00 81.57  ? 306 TRP   A CD2 1 
ATOM   72   N  NE1 . TRP   A 1 10  ? -35.865 -8.002  47.173 1.00 66.29  ? 306 TRP   A NE1 1 
ATOM   73   C  CE2 . TRP   A 1 10  ? -36.583 -8.056  48.337 1.00 80.28  ? 306 TRP   A CE2 1 
ATOM   74   C  CE3 . TRP   A 1 10  ? -37.884 -6.552  49.702 1.00 78.48  ? 306 TRP   A CE3 1 
ATOM   75   C  CZ2 . TRP   A 1 10  ? -36.820 -9.123  49.199 1.00 83.79  ? 306 TRP   A CZ2 1 
ATOM   76   C  CZ3 . TRP   A 1 10  ? -38.118 -7.613  50.556 1.00 84.39  ? 306 TRP   A CZ3 1 
ATOM   77   C  CH2 . TRP   A 1 10  ? -37.592 -8.882  50.299 1.00 80.93  ? 306 TRP   A CH2 1 
ATOM   78   N  N   . GLU   A 1 11  ? -38.678 -2.077  45.483 1.00 93.77  ? 307 GLU   A N   1 
ATOM   79   C  CA  . GLU   A 1 11  ? -39.215 -0.723  45.486 1.00 91.82  ? 307 GLU   A CA  1 
ATOM   80   C  C   . GLU   A 1 11  ? -40.737 -0.741  45.423 1.00 93.67  ? 307 GLU   A C   1 
ATOM   81   O  O   . GLU   A 1 11  ? -41.397 0.089   46.059 1.00 99.15  ? 307 GLU   A O   1 
ATOM   82   C  CB  . GLU   A 1 11  ? -38.640 0.076   44.313 1.00 84.88  ? 307 GLU   A CB  1 
ATOM   83   C  CG  . GLU   A 1 11  ? -38.842 1.584   44.409 1.00 93.14  ? 307 GLU   A CG  1 
ATOM   84   C  CD  . GLU   A 1 11  ? -38.721 2.279   43.057 1.00 108.90 ? 307 GLU   A CD  1 
ATOM   85   O  OE1 . GLU   A 1 11  ? -39.615 3.085   42.721 1.00 115.53 ? 307 GLU   A OE1 1 
ATOM   86   O  OE2 . GLU   A 1 11  ? -37.740 2.015   42.324 1.00 110.20 ? 307 GLU   A OE2 1 
ATOM   87   N  N   . THR   A 1 12  ? -41.308 -1.701  44.688 1.00 86.07  ? 308 THR   A N   1 
ATOM   88   C  CA  . THR   A 1 12  ? -42.739 -1.737  44.410 1.00 84.60  ? 308 THR   A CA  1 
ATOM   89   C  C   . THR   A 1 12  ? -43.474 -2.932  45.010 1.00 85.54  ? 308 THR   A C   1 
ATOM   90   O  O   . THR   A 1 12  ? -44.704 -2.999  44.890 1.00 86.52  ? 308 THR   A O   1 
ATOM   91   C  CB  . THR   A 1 12  ? -42.983 -1.717  42.892 1.00 86.90  ? 308 THR   A CB  1 
ATOM   92   O  OG1 . THR   A 1 12  ? -42.292 -2.814  42.265 1.00 77.39  ? 308 THR   A OG1 1 
ATOM   93   C  CG2 . THR   A 1 12  ? -42.480 -0.408  42.302 1.00 88.11  ? 308 THR   A CG2 1 
ATOM   94   N  N   . ASP   A 1 13  ? -42.772 -3.871  45.648 1.00 96.79  ? 309 ASP   A N   1 
ATOM   95   C  CA  . ASP   A 1 13  ? -43.373 -5.090  46.193 1.00 106.74 ? 309 ASP   A CA  1 
ATOM   96   C  C   . ASP   A 1 13  ? -44.018 -5.947  45.103 1.00 109.12 ? 309 ASP   A C   1 
ATOM   97   O  O   . ASP   A 1 13  ? -44.913 -6.748  45.390 1.00 119.02 ? 309 ASP   A O   1 
ATOM   98   C  CB  . ASP   A 1 13  ? -44.400 -4.770  47.293 1.00 119.28 ? 309 ASP   A CB  1 
ATOM   99   C  CG  . ASP   A 1 13  ? -43.760 -4.530  48.658 1.00 123.86 ? 309 ASP   A CG  1 
ATOM   100  O  OD1 . ASP   A 1 13  ? -43.378 -5.518  49.322 1.00 124.51 ? 309 ASP   A OD1 1 
ATOM   101  O  OD2 . ASP   A 1 13  ? -43.648 -3.355  49.071 1.00 124.54 ? 309 ASP   A OD2 1 
ATOM   102  N  N   . VAL   A 1 14  ? -43.586 -5.789  43.850 1.00 103.71 ? 310 VAL   A N   1 
ATOM   103  C  CA  . VAL   A 1 14  ? -44.071 -6.622  42.754 1.00 99.23  ? 310 VAL   A CA  1 
ATOM   104  C  C   . VAL   A 1 14  ? -43.308 -7.936  42.756 1.00 96.16  ? 310 VAL   A C   1 
ATOM   105  O  O   . VAL   A 1 14  ? -42.101 -7.971  43.022 1.00 89.76  ? 310 VAL   A O   1 
ATOM   106  C  CB  . VAL   A 1 14  ? -43.915 -5.903  41.401 1.00 83.19  ? 310 VAL   A CB  1 
ATOM   107  C  CG1 . VAL   A 1 14  ? -44.189 -6.863  40.255 1.00 94.60  ? 310 VAL   A CG1 1 
ATOM   108  C  CG2 . VAL   A 1 14  ? -44.843 -4.717  41.302 1.00 83.21  ? 310 VAL   A CG2 1 
ATOM   109  N  N   . VAL   A 1 15  ? -44.009 -9.024  42.452 1.00 92.59  ? 311 VAL   A N   1 
ATOM   110  C  CA  . VAL   A 1 15  ? -43.389 -10.330 42.300 1.00 87.26  ? 311 VAL   A CA  1 
ATOM   111  C  C   . VAL   A 1 15  ? -43.722 -10.875 40.917 1.00 89.88  ? 311 VAL   A C   1 
ATOM   112  O  O   . VAL   A 1 15  ? -44.827 -10.676 40.395 1.00 96.35  ? 311 VAL   A O   1 
ATOM   113  C  CB  . VAL   A 1 15  ? -43.829 -11.301 43.414 1.00 83.46  ? 311 VAL   A CB  1 
ATOM   114  C  CG1 . VAL   A 1 15  ? -43.202 -12.671 43.216 1.00 83.75  ? 311 VAL   A CG1 1 
ATOM   115  C  CG2 . VAL   A 1 15  ? -43.415 -10.738 44.759 1.00 75.23  ? 311 VAL   A CG2 1 
ATOM   116  N  N   . LEU   A 1 16  ? -42.750 -11.542 40.317 1.00 76.68  ? 312 LEU   A N   1 
ATOM   117  C  CA  . LEU   A 1 16  ? -42.918 -12.166 39.018 1.00 86.31  ? 312 LEU   A CA  1 
ATOM   118  C  C   . LEU   A 1 16  ? -42.394 -13.590 39.103 1.00 85.86  ? 312 LEU   A C   1 
ATOM   119  O  O   . LEU   A 1 16  ? -41.400 -13.850 39.790 1.00 74.94  ? 312 LEU   A O   1 
ATOM   120  C  CB  . LEU   A 1 16  ? -42.187 -11.367 37.945 1.00 86.24  ? 312 LEU   A CB  1 
ATOM   121  C  CG  . LEU   A 1 16  ? -42.803 -10.000 37.630 1.00 98.50  ? 312 LEU   A CG  1 
ATOM   122  C  CD1 . LEU   A 1 16  ? -41.736 -9.021  37.189 1.00 94.42  ? 312 LEU   A CD1 1 
ATOM   123  C  CD2 . LEU   A 1 16  ? -43.874 -10.128 36.551 1.00 108.11 ? 312 LEU   A CD2 1 
ATOM   124  N  N   . THR   A 1 17  ? -43.071 -14.517 38.431 1.00 83.54  ? 313 THR   A N   1 
ATOM   125  C  CA  . THR   A 1 17  ? -42.685 -15.920 38.463 1.00 81.16  ? 313 THR   A CA  1 
ATOM   126  C  C   . THR   A 1 17  ? -41.934 -16.285 37.192 1.00 87.50  ? 313 THR   A C   1 
ATOM   127  O  O   . THR   A 1 17  ? -42.463 -16.130 36.084 1.00 90.42  ? 313 THR   A O   1 
ATOM   128  C  CB  . THR   A 1 17  ? -43.897 -16.830 38.614 1.00 85.65  ? 313 THR   A CB  1 
ATOM   129  O  OG1 . THR   A 1 17  ? -44.657 -16.429 39.755 1.00 86.01  ? 313 THR   A OG1 1 
ATOM   130  C  CG2 . THR   A 1 17  ? -43.433 -18.271 38.781 1.00 89.48  ? 313 THR   A CG2 1 
ATOM   131  N  N   . ASP   A 1 18  ? -40.714 -16.794 37.359 1.00 82.40  ? 314 ASP   A N   1 
ATOM   132  C  CA  . ASP   A 1 18  ? -39.847 -17.143 36.240 1.00 82.56  ? 314 ASP   A CA  1 
ATOM   133  C  C   . ASP   A 1 18  ? -39.910 -18.649 36.016 1.00 86.53  ? 314 ASP   A C   1 
ATOM   134  O  O   . ASP   A 1 18  ? -39.368 -19.425 36.810 1.00 86.58  ? 314 ASP   A O   1 
ATOM   135  C  CB  . ASP   A 1 18  ? -38.414 -16.683 36.498 1.00 78.27  ? 314 ASP   A CB  1 
ATOM   136  C  CG  . ASP   A 1 18  ? -37.554 -16.724 35.244 1.00 74.15  ? 314 ASP   A CG  1 
ATOM   137  O  OD1 . ASP   A 1 18  ? -37.358 -17.833 34.703 1.00 74.72  ? 314 ASP   A OD1 1 
ATOM   138  O  OD2 . ASP   A 1 18  ? -37.090 -15.649 34.790 1.00 63.62  ? 314 ASP   A OD2 1 
ATOM   139  N  N   . THR   A 1 19  ? -40.587 -19.057 34.939 1.00 87.49  ? 315 THR   A N   1 
ATOM   140  C  CA  . THR   A 1 19  ? -40.530 -20.431 34.458 1.00 94.40  ? 315 THR   A CA  1 
ATOM   141  C  C   . THR   A 1 19  ? -39.626 -20.595 33.244 1.00 92.59  ? 315 THR   A C   1 
ATOM   142  O  O   . THR   A 1 19  ? -39.227 -21.724 32.943 1.00 85.87  ? 315 THR   A O   1 
ATOM   143  C  CB  . THR   A 1 19  ? -41.933 -20.942 34.103 1.00 97.02  ? 315 THR   A CB  1 
ATOM   144  O  OG1 . THR   A 1 19  ? -42.771 -19.840 33.732 1.00 105.95 ? 315 THR   A OG1 1 
ATOM   145  C  CG2 . THR   A 1 19  ? -42.553 -21.673 35.278 1.00 93.00  ? 315 THR   A CG2 1 
ATOM   146  N  N   . LEU   A 1 20  ? -39.288 -19.489 32.563 1.00 88.20  ? 316 LEU   A N   1 
ATOM   147  C  CA  . LEU   A 1 20  ? -38.478 -19.536 31.350 1.00 76.42  ? 316 LEU   A CA  1 
ATOM   148  C  C   . LEU   A 1 20  ? -37.093 -20.119 31.601 1.00 74.86  ? 316 LEU   A C   1 
ATOM   149  O  O   . LEU   A 1 20  ? -36.513 -20.741 30.704 1.00 86.72  ? 316 LEU   A O   1 
ATOM   150  C  CB  . LEU   A 1 20  ? -38.357 -18.125 30.760 1.00 74.51  ? 316 LEU   A CB  1 
ATOM   151  C  CG  . LEU   A 1 20  ? -37.545 -17.908 29.478 1.00 70.52  ? 316 LEU   A CG  1 
ATOM   152  C  CD1 . LEU   A 1 20  ? -38.155 -18.640 28.265 1.00 67.40  ? 316 LEU   A CD1 1 
ATOM   153  C  CD2 . LEU   A 1 20  ? -37.369 -16.413 29.176 1.00 60.57  ? 316 LEU   A CD2 1 
ATOM   154  N  N   . HIS   A 1 21  ? -36.543 -19.917 32.800 1.00 73.58  ? 317 HIS   A N   1 
ATOM   155  C  CA  . HIS   A 1 21  ? -35.226 -20.449 33.133 1.00 70.58  ? 317 HIS   A CA  1 
ATOM   156  C  C   . HIS   A 1 21  ? -35.162 -21.961 32.967 1.00 74.55  ? 317 HIS   A C   1 
ATOM   157  O  O   . HIS   A 1 21  ? -34.063 -22.517 32.879 1.00 72.43  ? 317 HIS   A O   1 
ATOM   158  C  CB  . HIS   A 1 21  ? -34.857 -20.067 34.575 1.00 73.29  ? 317 HIS   A CB  1 
ATOM   159  C  CG  . HIS   A 1 21  ? -35.589 -20.853 35.618 1.00 64.48  ? 317 HIS   A CG  1 
ATOM   160  N  ND1 . HIS   A 1 21  ? -36.913 -20.630 35.932 1.00 71.27  ? 317 HIS   A ND1 1 
ATOM   161  C  CD2 . HIS   A 1 21  ? -35.175 -21.858 36.426 1.00 72.73  ? 317 HIS   A CD2 1 
ATOM   162  C  CE1 . HIS   A 1 21  ? -37.284 -21.469 36.884 1.00 78.59  ? 317 HIS   A CE1 1 
ATOM   163  N  NE2 . HIS   A 1 21  ? -36.248 -22.224 37.202 1.00 78.29  ? 317 HIS   A NE2 1 
ATOM   164  N  N   . LEU   A 1 22  ? -36.314 -22.634 32.932 1.00 80.17  ? 318 LEU   A N   1 
ATOM   165  C  CA  . LEU   A 1 22  ? -36.339 -24.079 32.740 1.00 94.73  ? 318 LEU   A CA  1 
ATOM   166  C  C   . LEU   A 1 22  ? -35.905 -24.468 31.332 1.00 93.57  ? 318 LEU   A C   1 
ATOM   167  O  O   . LEU   A 1 22  ? -35.299 -25.530 31.142 1.00 97.41  ? 318 LEU   A O   1 
ATOM   168  C  CB  . LEU   A 1 22  ? -37.742 -24.614 33.036 1.00 99.79  ? 318 LEU   A CB  1 
ATOM   169  C  CG  . LEU   A 1 22  ? -38.224 -24.411 34.471 1.00 93.87  ? 318 LEU   A CG  1 
ATOM   170  C  CD1 . LEU   A 1 22  ? -39.689 -24.793 34.628 1.00 93.88  ? 318 LEU   A CD1 1 
ATOM   171  C  CD2 . LEU   A 1 22  ? -37.345 -25.224 35.383 1.00 92.93  ? 318 LEU   A CD2 1 
ATOM   172  N  N   . LYS   A 1 23  ? -36.209 -23.631 30.337 1.00 93.81  ? 319 LYS   A N   1 
ATOM   173  C  CA  . LYS   A 1 23  ? -35.721 -23.865 28.983 1.00 96.15  ? 319 LYS   A CA  1 
ATOM   174  C  C   . LYS   A 1 23  ? -34.237 -23.558 28.842 1.00 86.73  ? 319 LYS   A C   1 
ATOM   175  O  O   . LYS   A 1 23  ? -33.690 -23.759 27.755 1.00 84.57  ? 319 LYS   A O   1 
ATOM   176  C  CB  . LYS   A 1 23  ? -36.512 -23.028 27.968 1.00 96.14  ? 319 LYS   A CB  1 
ATOM   177  C  CG  . LYS   A 1 23  ? -38.038 -23.194 28.024 1.00 103.40 ? 319 LYS   A CG  1 
ATOM   178  C  CD  . LYS   A 1 23  ? -38.484 -24.611 27.684 1.00 113.31 ? 319 LYS   A CD  1 
ATOM   179  C  CE  . LYS   A 1 23  ? -39.268 -24.664 26.376 1.00 117.15 ? 319 LYS   A CE  1 
ATOM   180  N  NZ  . LYS   A 1 23  ? -40.577 -23.954 26.458 1.00 119.75 ? 319 LYS   A NZ  1 
ATOM   181  N  N   . SER   A 1 24  ? -33.581 -23.079 29.900 1.00 82.43  ? 320 SER   A N   1 
ATOM   182  C  CA  . SER   A 1 24  ? -32.177 -22.700 29.804 1.00 81.48  ? 320 SER   A CA  1 
ATOM   183  C  C   . SER   A 1 24  ? -31.314 -23.905 29.478 1.00 91.83  ? 320 SER   A C   1 
ATOM   184  O  O   . SER   A 1 24  ? -31.561 -25.021 29.945 1.00 81.39  ? 320 SER   A O   1 
ATOM   185  C  CB  . SER   A 1 24  ? -31.686 -22.052 31.102 1.00 83.20  ? 320 SER   A CB  1 
ATOM   186  O  OG  . SER   A 1 24  ? -30.272 -21.926 31.094 1.00 82.81  ? 320 SER   A OG  1 
ATOM   187  N  N   . THR   A 1 25  ? -30.292 -23.662 28.665 1.00 112.12 ? 321 THR   A N   1 
ATOM   188  C  CA  . THR   A 1 25  ? -29.407 -24.713 28.188 1.00 120.70 ? 321 THR   A CA  1 
ATOM   189  C  C   . THR   A 1 25  ? -27.981 -24.494 28.670 1.00 114.18 ? 321 THR   A C   1 
ATOM   190  O  O   . THR   A 1 25  ? -27.455 -25.322 29.426 1.00 111.77 ? 321 THR   A O   1 
ATOM   191  C  CB  . THR   A 1 25  ? -29.485 -24.779 26.655 1.00 126.68 ? 321 THR   A CB  1 
ATOM   192  O  OG1 . THR   A 1 25  ? -28.326 -25.438 26.135 1.00 128.40 ? 321 THR   A OG1 1 
ATOM   193  C  CG2 . THR   A 1 25  ? -29.607 -23.372 26.051 1.00 124.34 ? 321 THR   A CG2 1 
ATOM   194  N  N   . LEU   A 1 26  ? -27.353 -23.384 28.283 1.00 106.36 ? 322 LEU   A N   1 
ATOM   195  C  CA  . LEU   A 1 26  ? -25.970 -23.118 28.641 1.00 104.37 ? 322 LEU   A CA  1 
ATOM   196  C  C   . LEU   A 1 26  ? -25.794 -23.016 30.153 1.00 103.85 ? 322 LEU   A C   1 
ATOM   197  O  O   . LEU   A 1 26  ? -26.749 -23.023 30.931 1.00 107.71 ? 322 LEU   A O   1 
ATOM   198  C  CB  . LEU   A 1 26  ? -25.485 -21.837 27.971 1.00 102.22 ? 322 LEU   A CB  1 
ATOM   199  C  CG  . LEU   A 1 26  ? -24.898 -21.955 26.577 1.00 106.34 ? 322 LEU   A CG  1 
ATOM   200  C  CD1 . LEU   A 1 26  ? -25.200 -20.687 25.797 1.00 103.77 ? 322 LEU   A CD1 1 
ATOM   201  C  CD2 . LEU   A 1 26  ? -23.393 -22.198 26.669 1.00 108.30 ? 322 LEU   A CD2 1 
ATOM   202  N  N   . GLU   A 1 27  ? -24.532 -22.918 30.553 1.00 94.17  ? 323 GLU   A N   1 
ATOM   203  C  CA  . GLU   A 1 27  ? -24.144 -22.828 31.947 1.00 91.54  ? 323 GLU   A CA  1 
ATOM   204  C  C   . GLU   A 1 27  ? -23.644 -21.421 32.261 1.00 87.88  ? 323 GLU   A C   1 
ATOM   205  O  O   . GLU   A 1 27  ? -23.200 -20.677 31.378 1.00 85.58  ? 323 GLU   A O   1 
ATOM   206  C  CB  . GLU   A 1 27  ? -23.092 -23.889 32.281 1.00 89.79  ? 323 GLU   A CB  1 
ATOM   207  C  CG  . GLU   A 1 27  ? -23.648 -25.308 32.208 1.00 94.40  ? 323 GLU   A CG  1 
ATOM   208  C  CD  . GLU   A 1 27  ? -22.670 -26.365 32.687 1.00 112.26 ? 323 GLU   A CD  1 
ATOM   209  O  OE1 . GLU   A 1 27  ? -21.863 -26.070 33.597 1.00 114.91 ? 323 GLU   A OE1 1 
ATOM   210  O  OE2 . GLU   A 1 27  ? -22.713 -27.497 32.154 1.00 122.13 ? 323 GLU   A OE2 1 
ATOM   211  N  N   . THR   A 1 28  ? -23.740 -21.059 33.542 1.00 73.19  ? 324 THR   A N   1 
ATOM   212  C  CA  . THR   A 1 28  ? -23.549 -19.682 33.985 1.00 67.80  ? 324 THR   A CA  1 
ATOM   213  C  C   . THR   A 1 28  ? -22.161 -19.393 34.538 1.00 73.79  ? 324 THR   A C   1 
ATOM   214  O  O   . THR   A 1 28  ? -21.729 -18.236 34.510 1.00 76.17  ? 324 THR   A O   1 
ATOM   215  C  CB  . THR   A 1 28  ? -24.576 -19.337 35.064 1.00 73.69  ? 324 THR   A CB  1 
ATOM   216  O  OG1 . THR   A 1 28  ? -24.319 -20.140 36.225 1.00 67.79  ? 324 THR   A OG1 1 
ATOM   217  C  CG2 . THR   A 1 28  ? -25.977 -19.615 34.560 1.00 77.93  ? 324 THR   A CG2 1 
ATOM   218  N  N   . GLY   A 1 29  ? -21.454 -20.400 35.042 1.00 80.01  ? 325 GLY   A N   1 
ATOM   219  C  CA  . GLY   A 1 29  ? -20.221 -20.193 35.751 1.00 78.08  ? 325 GLY   A CA  1 
ATOM   220  C  C   . GLY   A 1 29  ? -20.356 -20.349 37.252 1.00 78.34  ? 325 GLY   A C   1 
ATOM   221  O  O   . GLY   A 1 29  ? -19.394 -20.759 37.912 1.00 79.74  ? 325 GLY   A O   1 
ATOM   222  N  N   . CYS   A 1 30  ? -21.526 -20.038 37.804 1.00 78.27  ? 326 CYS   A N   1 
ATOM   223  C  CA  . CYS   A 1 30  ? -21.766 -20.245 39.222 1.00 79.97  ? 326 CYS   A CA  1 
ATOM   224  C  C   . CYS   A 1 30  ? -21.997 -21.719 39.516 1.00 80.28  ? 326 CYS   A C   1 
ATOM   225  O  O   . CYS   A 1 30  ? -22.422 -22.491 38.652 1.00 79.43  ? 326 CYS   A O   1 
ATOM   226  C  CB  . CYS   A 1 30  ? -22.981 -19.456 39.705 1.00 69.97  ? 326 CYS   A CB  1 
ATOM   227  S  SG  . CYS   A 1 30  ? -23.008 -17.727 39.241 1.00 63.26  ? 326 CYS   A SG  1 
ATOM   228  N  N   . THR   A 1 31  ? -21.722 -22.099 40.753 1.00 74.45  ? 327 THR   A N   1 
ATOM   229  C  CA  . THR   A 1 31  ? -22.117 -23.391 41.288 1.00 81.98  ? 327 THR   A CA  1 
ATOM   230  C  C   . THR   A 1 31  ? -22.961 -23.159 42.533 1.00 80.30  ? 327 THR   A C   1 
ATOM   231  O  O   . THR   A 1 31  ? -23.223 -22.021 42.936 1.00 81.36  ? 327 THR   A O   1 
ATOM   232  C  CB  . THR   A 1 31  ? -20.900 -24.270 41.593 1.00 78.38  ? 327 THR   A CB  1 
ATOM   233  O  OG1 . THR   A 1 31  ? -20.046 -23.603 42.524 1.00 82.37  ? 327 THR   A OG1 1 
ATOM   234  C  CG2 . THR   A 1 31  ? -20.117 -24.556 40.325 1.00 77.31  ? 327 THR   A CG2 1 
ATOM   235  N  N   . GLU   A 1 32  ? -23.396 -24.255 43.144 1.00 85.75  ? 328 GLU   A N   1 
ATOM   236  C  CA  . GLU   A 1 32  ? -24.125 -24.146 44.401 1.00 95.13  ? 328 GLU   A CA  1 
ATOM   237  C  C   . GLU   A 1 32  ? -23.267 -23.547 45.512 1.00 89.56  ? 328 GLU   A C   1 
ATOM   238  O  O   . GLU   A 1 32  ? -23.814 -23.102 46.525 1.00 87.10  ? 328 GLU   A O   1 
ATOM   239  C  CB  . GLU   A 1 32  ? -24.662 -25.522 44.813 1.00 107.46 ? 328 GLU   A CB  1 
ATOM   240  C  CG  . GLU   A 1 32  ? -25.528 -26.205 43.743 1.00 114.70 ? 328 GLU   A CG  1 
ATOM   241  C  CD  . GLU   A 1 32  ? -24.729 -27.109 42.807 1.00 126.05 ? 328 GLU   A CD  1 
ATOM   242  O  OE1 . GLU   A 1 32  ? -24.902 -28.347 42.883 1.00 132.85 ? 328 GLU   A OE1 1 
ATOM   243  O  OE2 . GLU   A 1 32  ? -23.926 -26.586 42.003 1.00 125.61 ? 328 GLU   A OE2 1 
ATOM   244  N  N   . HIS   A 1 33  ? -21.942 -23.493 45.334 1.00 87.18  ? 329 HIS   A N   1 
ATOM   245  C  CA  . HIS   A 1 33  ? -21.036 -23.023 46.373 1.00 88.57  ? 329 HIS   A CA  1 
ATOM   246  C  C   . HIS   A 1 33  ? -20.200 -21.811 45.974 1.00 83.15  ? 329 HIS   A C   1 
ATOM   247  O  O   . HIS   A 1 33  ? -19.413 -21.331 46.797 1.00 77.29  ? 329 HIS   A O   1 
ATOM   248  C  CB  . HIS   A 1 33  ? -20.106 -24.163 46.806 1.00 105.47 ? 329 HIS   A CB  1 
ATOM   249  C  CG  . HIS   A 1 33  ? -20.818 -25.458 47.052 1.00 122.99 ? 329 HIS   A CG  1 
ATOM   250  N  ND1 . HIS   A 1 33  ? -20.869 -26.469 46.116 1.00 129.49 ? 329 HIS   A ND1 1 
ATOM   251  C  CD2 . HIS   A 1 33  ? -21.527 -25.897 48.119 1.00 127.47 ? 329 HIS   A CD2 1 
ATOM   252  C  CE1 . HIS   A 1 33  ? -21.570 -27.480 46.599 1.00 132.71 ? 329 HIS   A CE1 1 
ATOM   253  N  NE2 . HIS   A 1 33  ? -21.981 -27.159 47.813 1.00 132.11 ? 329 HIS   A NE2 1 
ATOM   254  N  N   . ILE   A 1 34  ? -20.330 -21.296 44.753 1.00 74.95  ? 330 ILE   A N   1 
ATOM   255  C  CA  . ILE   A 1 34  ? -19.666 -20.039 44.414 1.00 70.24  ? 330 ILE   A CA  1 
ATOM   256  C  C   . ILE   A 1 34  ? -20.462 -19.332 43.328 1.00 69.41  ? 330 ILE   A C   1 
ATOM   257  O  O   . ILE   A 1 34  ? -20.928 -19.946 42.368 1.00 70.33  ? 330 ILE   A O   1 
ATOM   258  C  CB  . ILE   A 1 34  ? -18.193 -20.242 43.996 1.00 71.00  ? 330 ILE   A CB  1 
ATOM   259  C  CG1 . ILE   A 1 34  ? -17.532 -18.883 43.755 1.00 65.11  ? 330 ILE   A CG1 1 
ATOM   260  C  CG2 . ILE   A 1 34  ? -18.088 -21.111 42.745 1.00 86.16  ? 330 ILE   A CG2 1 
ATOM   261  C  CD1 . ILE   A 1 34  ? -16.027 -18.929 43.813 1.00 73.33  ? 330 ILE   A CD1 1 
ATOM   262  N  N   . CYS   A 1 35  ? -20.612 -18.028 43.487 1.00 69.75  ? 331 CYS   A N   1 
ATOM   263  C  CA  . CYS   A 1 35  ? -21.358 -17.209 42.552 1.00 62.24  ? 331 CYS   A CA  1 
ATOM   264  C  C   . CYS   A 1 35  ? -20.371 -16.335 41.795 1.00 66.32  ? 331 CYS   A C   1 
ATOM   265  O  O   . CYS   A 1 35  ? -19.596 -15.591 42.416 1.00 50.55  ? 331 CYS   A O   1 
ATOM   266  C  CB  . CYS   A 1 35  ? -22.398 -16.367 43.284 1.00 60.00  ? 331 CYS   A CB  1 
ATOM   267  S  SG  . CYS   A 1 35  ? -23.176 -15.140 42.213 1.00 53.22  ? 331 CYS   A SG  1 
ATOM   268  N  N   . MET   A 1 36  ? -20.403 -16.446 40.459 1.00 62.42  ? 332 MET   A N   1 
ATOM   269  C  CA  . MET   A 1 36  ? -19.538 -15.725 39.527 1.00 68.87  ? 332 MET   A CA  1 
ATOM   270  C  C   . MET   A 1 36  ? -20.232 -14.526 38.885 1.00 61.89  ? 332 MET   A C   1 
ATOM   271  O  O   . MET   A 1 36  ? -19.760 -14.019 37.853 1.00 48.06  ? 332 MET   A O   1 
ATOM   272  C  CB  . MET   A 1 36  ? -19.041 -16.666 38.424 1.00 75.51  ? 332 MET   A CB  1 
ATOM   273  C  CG  . MET   A 1 36  ? -18.487 -17.987 38.900 1.00 87.26  ? 332 MET   A CG  1 
ATOM   274  S  SD  . MET   A 1 36  ? -16.720 -17.955 39.224 1.00 97.47  ? 332 MET   A SD  1 
ATOM   275  C  CE  . MET   A 1 36  ? -16.483 -19.635 39.793 1.00 104.03 ? 332 MET   A CE  1 
ATOM   276  N  N   . GLY   A 1 37  ? -21.336 -14.059 39.470 1.00 61.77  ? 333 GLY   A N   1 
ATOM   277  C  CA  . GLY   A 1 37  ? -22.129 -13.005 38.855 1.00 58.23  ? 333 GLY   A CA  1 
ATOM   278  C  C   . GLY   A 1 37  ? -21.375 -11.730 38.528 1.00 59.13  ? 333 GLY   A C   1 
ATOM   279  O  O   . GLY   A 1 37  ? -21.892 -10.919 37.752 1.00 55.21  ? 333 GLY   A O   1 
ATOM   280  N  N   . SER   A 1 38  ? -20.191 -11.511 39.097 1.00 52.68  ? 334 SER   A N   1 
ATOM   281  C  CA  . SER   A 1 38  ? -19.428 -10.310 38.787 1.00 55.45  ? 334 SER   A CA  1 
ATOM   282  C  C   . SER   A 1 38  ? -18.146 -10.607 38.022 1.00 52.48  ? 334 SER   A C   1 
ATOM   283  O  O   . SER   A 1 38  ? -17.323 -9.705  37.850 1.00 55.93  ? 334 SER   A O   1 
ATOM   284  C  CB  . SER   A 1 38  ? -19.105 -9.517  40.054 1.00 59.15  ? 334 SER   A CB  1 
ATOM   285  O  OG  . SER   A 1 38  ? -18.212 -10.216 40.928 1.00 70.72  ? 334 SER   A OG  1 
ATOM   286  N  N   . ILE   A 1 39  ? -17.951 -11.837 37.556 1.00 40.97  ? 335 ILE   A N   1 
ATOM   287  C  CA  . ILE   A 1 39  ? -16.864 -12.109 36.622 1.00 53.77  ? 335 ILE   A CA  1 
ATOM   288  C  C   . ILE   A 1 39  ? -17.280 -11.585 35.252 1.00 57.42  ? 335 ILE   A C   1 
ATOM   289  O  O   . ILE   A 1 39  ? -18.356 -11.925 34.751 1.00 52.33  ? 335 ILE   A O   1 
ATOM   290  C  CB  . ILE   A 1 39  ? -16.539 -13.610 36.574 1.00 52.20  ? 335 ILE   A CB  1 
ATOM   291  C  CG1 . ILE   A 1 39  ? -16.162 -14.138 37.977 1.00 51.21  ? 335 ILE   A CG1 1 
ATOM   292  C  CG2 . ILE   A 1 39  ? -15.408 -13.873 35.578 1.00 51.23  ? 335 ILE   A CG2 1 
ATOM   293  C  CD1 . ILE   A 1 39  ? -14.984 -13.422 38.608 1.00 60.86  ? 335 ILE   A CD1 1 
ATOM   294  N  N   . MET   A 1 40  ? -16.430 -10.750 34.648 1.00 57.52  ? 336 MET   A N   1 
ATOM   295  C  CA  . MET   A 1 40  ? -16.812 -10.006 33.443 1.00 53.28  ? 336 MET   A CA  1 
ATOM   296  C  C   . MET   A 1 40  ? -17.006 -10.923 32.234 1.00 63.13  ? 336 MET   A C   1 
ATOM   297  O  O   . MET   A 1 40  ? -18.026 -10.845 31.529 1.00 55.13  ? 336 MET   A O   1 
ATOM   298  C  CB  . MET   A 1 40  ? -15.743 -8.951  33.144 1.00 64.19  ? 336 MET   A CB  1 
ATOM   299  C  CG  . MET   A 1 40  ? -15.868 -8.318  31.780 1.00 73.31  ? 336 MET   A CG  1 
ATOM   300  S  SD  . MET   A 1 40  ? -16.471 -6.635  31.931 1.00 78.04  ? 336 MET   A SD  1 
ATOM   301  C  CE  . MET   A 1 40  ? -14.982 -5.792  32.433 1.00 68.23  ? 336 MET   A CE  1 
ATOM   302  N  N   . LEU   A 1 41  ? -16.025 -11.779 31.961 1.00 66.67  ? 337 LEU   A N   1 
ATOM   303  C  CA  . LEU   A 1 41  ? -16.056 -12.683 30.814 1.00 82.14  ? 337 LEU   A CA  1 
ATOM   304  C  C   . LEU   A 1 41  ? -15.869 -14.104 31.328 1.00 95.09  ? 337 LEU   A C   1 
ATOM   305  O  O   . LEU   A 1 41  ? -14.829 -14.729 31.077 1.00 104.40 ? 337 LEU   A O   1 
ATOM   306  C  CB  . LEU   A 1 41  ? -14.969 -12.338 29.796 1.00 89.26  ? 337 LEU   A CB  1 
ATOM   307  C  CG  . LEU   A 1 41  ? -14.664 -10.872 29.460 1.00 88.89  ? 337 LEU   A CG  1 
ATOM   308  C  CD1 . LEU   A 1 41  ? -13.319 -10.773 28.743 1.00 86.60  ? 337 LEU   A CD1 1 
ATOM   309  C  CD2 . LEU   A 1 41  ? -15.768 -10.230 28.621 1.00 84.98  ? 337 LEU   A CD2 1 
ATOM   310  N  N   . PRO   A 1 42  ? -16.854 -14.642 32.053 1.00 100.47 ? 338 PRO   A N   1 
ATOM   311  C  CA  . PRO   A 1 42  ? -16.675 -15.961 32.668 1.00 104.10 ? 338 PRO   A CA  1 
ATOM   312  C  C   . PRO   A 1 42  ? -16.341 -17.005 31.616 1.00 114.06 ? 338 PRO   A C   1 
ATOM   313  O  O   . PRO   A 1 42  ? -16.685 -16.863 30.439 1.00 108.52 ? 338 PRO   A O   1 
ATOM   314  C  CB  . PRO   A 1 42  ? -18.029 -16.236 33.332 1.00 99.55  ? 338 PRO   A CB  1 
ATOM   315  C  CG  . PRO   A 1 42  ? -18.997 -15.372 32.597 1.00 96.23  ? 338 PRO   A CG  1 
ATOM   316  C  CD  . PRO   A 1 42  ? -18.233 -14.143 32.202 1.00 94.42  ? 338 PRO   A CD  1 
ATOM   317  N  N   . SER   A 1 43  ? -15.641 -18.053 32.054 1.00 124.20 ? 339 SER   A N   1 
ATOM   318  C  CA  . SER   A 1 43  ? -15.182 -19.124 31.176 1.00 132.29 ? 339 SER   A CA  1 
ATOM   319  C  C   . SER   A 1 43  ? -16.296 -19.617 30.258 1.00 132.74 ? 339 SER   A C   1 
ATOM   320  O  O   . SER   A 1 43  ? -16.030 -20.114 29.159 1.00 134.60 ? 339 SER   A O   1 
ATOM   321  C  CB  . SER   A 1 43  ? -14.625 -20.281 32.011 1.00 136.38 ? 339 SER   A CB  1 
ATOM   322  O  OG  . SER   A 1 43  ? -14.262 -21.379 31.194 1.00 140.82 ? 339 SER   A OG  1 
ATOM   323  N  N   . GLN   A 1 44  ? -17.548 -19.454 30.698 1.00 131.00 ? 340 GLN   A N   1 
ATOM   324  C  CA  . GLN   A 1 44  ? -18.702 -19.891 29.918 1.00 124.27 ? 340 GLN   A CA  1 
ATOM   325  C  C   . GLN   A 1 44  ? -19.062 -18.901 28.815 1.00 117.94 ? 340 GLN   A C   1 
ATOM   326  O  O   . GLN   A 1 44  ? -19.322 -19.314 27.679 1.00 117.58 ? 340 GLN   A O   1 
ATOM   327  C  CB  . GLN   A 1 44  ? -19.901 -20.117 30.845 1.00 120.21 ? 340 GLN   A CB  1 
ATOM   328  C  CG  . GLN   A 1 44  ? -20.004 -21.530 31.421 1.00 116.91 ? 340 GLN   A CG  1 
ATOM   329  C  CD  . GLN   A 1 44  ? -18.984 -21.810 32.510 1.00 122.73 ? 340 GLN   A CD  1 
ATOM   330  O  OE1 . GLN   A 1 44  ? -17.975 -21.113 32.634 1.00 129.02 ? 340 GLN   A OE1 1 
ATOM   331  N  NE2 . GLN   A 1 44  ? -19.249 -22.837 33.317 1.00 118.11 ? 340 GLN   A NE2 1 
ATOM   332  N  N   . HIS   A 1 45  ? -19.082 -17.587 29.122 1.00 119.24 ? 341 HIS   A N   1 
ATOM   333  C  CA  . HIS   A 1 45  ? -19.536 -16.536 28.190 1.00 121.00 ? 341 HIS   A CA  1 
ATOM   334  C  C   . HIS   A 1 45  ? -18.640 -16.402 26.903 1.00 123.93 ? 341 HIS   A C   1 
ATOM   335  O  O   . HIS   A 1 45  ? -18.850 -15.448 26.136 1.00 118.71 ? 341 HIS   A O   1 
ATOM   336  C  CB  . HIS   A 1 45  ? -19.618 -15.187 28.919 1.00 116.60 ? 341 HIS   A CB  1 
ATOM   337  C  CG  . HIS   A 1 45  ? -20.636 -14.242 28.349 1.00 108.14 ? 341 HIS   A CG  1 
ATOM   338  N  ND1 . HIS   A 1 45  ? -21.201 -14.413 27.103 1.00 105.40 ? 341 HIS   A ND1 1 
ATOM   339  C  CD2 . HIS   A 1 45  ? -21.193 -13.118 28.863 1.00 105.11 ? 341 HIS   A CD2 1 
ATOM   340  C  CE1 . HIS   A 1 45  ? -22.059 -13.435 26.874 1.00 100.95 ? 341 HIS   A CE1 1 
ATOM   341  N  NE2 . HIS   A 1 45  ? -22.073 -12.636 27.926 1.00 102.59 ? 341 HIS   A NE2 1 
ATOM   342  N  N   . THR   A 1 46  ? -17.692 -17.295 26.620 1.00 130.10 ? 342 THR   A N   1 
ATOM   343  C  CA  . THR   A 1 46  ? -16.792 -17.172 25.481 1.00 130.74 ? 342 THR   A CA  1 
ATOM   344  C  C   . THR   A 1 46  ? -16.937 -18.390 24.576 1.00 130.83 ? 342 THR   A C   1 
ATOM   345  O  O   . THR   A 1 46  ? -17.119 -19.515 25.057 1.00 138.09 ? 342 THR   A O   1 
ATOM   346  C  CB  . THR   A 1 46  ? -15.330 -17.027 25.954 1.00 132.22 ? 342 THR   A CB  1 
ATOM   347  O  OG1 . THR   A 1 46  ? -15.236 -15.960 26.907 1.00 130.30 ? 342 THR   A OG1 1 
ATOM   348  C  CG2 . THR   A 1 46  ? -14.396 -16.727 24.782 1.00 132.48 ? 342 THR   A CG2 1 
ATOM   349  N  N   . ARG   A 1 47  ? -16.870 -18.164 23.264 1.00 118.45 ? 343 ARG   A N   1 
ATOM   350  C  CA  . ARG   A 1 47  ? -16.872 -19.259 22.297 1.00 114.62 ? 343 ARG   A CA  1 
ATOM   351  C  C   . ARG   A 1 47  ? -15.460 -19.571 21.816 1.00 115.70 ? 343 ARG   A C   1 
ATOM   352  O  O   . ARG   A 1 47  ? -14.870 -18.800 21.061 1.00 115.43 ? 343 ARG   A O   1 
ATOM   353  C  CB  . ARG   A 1 47  ? -17.772 -18.936 21.096 1.00 104.65 ? 343 ARG   A CB  1 
ATOM   354  C  CG  . ARG   A 1 47  ? -19.254 -19.081 21.389 1.00 104.77 ? 343 ARG   A CG  1 
ATOM   355  C  CD  . ARG   A 1 47  ? -19.492 -20.186 22.416 1.00 112.44 ? 343 ARG   A CD  1 
ATOM   356  N  NE  . ARG   A 1 47  ? -20.902 -20.528 22.541 1.00 118.32 ? 343 ARG   A NE  1 
ATOM   357  C  CZ  . ARG   A 1 47  ? -21.419 -21.206 23.560 1.00 128.20 ? 343 ARG   A CZ  1 
ATOM   358  N  NH1 . ARG   A 1 47  ? -20.644 -21.607 24.561 1.00 133.29 ? 343 ARG   A NH1 1 
ATOM   359  N  NH2 . ARG   A 1 47  ? -22.717 -21.472 23.581 1.00 131.92 ? 343 ARG   A NH2 1 
ATOM   360  N  N   . VAL   A 1 52  ? -14.505 -25.832 18.214 1.00 121.08 ? 348 VAL   A N   1 
ATOM   361  C  CA  . VAL   A 1 52  ? -15.060 -26.235 16.927 1.00 132.85 ? 348 VAL   A CA  1 
ATOM   362  C  C   . VAL   A 1 52  ? -16.156 -27.295 17.126 1.00 143.18 ? 348 VAL   A C   1 
ATOM   363  O  O   . VAL   A 1 52  ? -16.040 -28.167 17.989 1.00 145.13 ? 348 VAL   A O   1 
ATOM   364  C  CB  . VAL   A 1 52  ? -13.931 -26.732 15.969 1.00 135.06 ? 348 VAL   A CB  1 
ATOM   365  C  CG1 . VAL   A 1 52  ? -12.993 -27.702 16.680 1.00 135.37 ? 348 VAL   A CG1 1 
ATOM   366  C  CG2 . VAL   A 1 52  ? -14.507 -27.350 14.691 1.00 128.39 ? 348 VAL   A CG2 1 
ATOM   367  N  N   . ALA   A 1 53  ? -17.219 -27.200 16.323 1.00 143.41 ? 349 ALA   A N   1 
ATOM   368  C  CA  . ALA   A 1 53  ? -18.406 -28.030 16.472 1.00 140.41 ? 349 ALA   A CA  1 
ATOM   369  C  C   . ALA   A 1 53  ? -18.212 -29.400 15.813 1.00 143.03 ? 349 ALA   A C   1 
ATOM   370  O  O   . ALA   A 1 53  ? -17.161 -29.709 15.242 1.00 148.37 ? 349 ALA   A O   1 
ATOM   371  C  CB  . ALA   A 1 53  ? -19.620 -27.315 15.885 1.00 132.96 ? 349 ALA   A CB  1 
ATOM   372  N  N   . THR   A 1 54  ? -19.238 -30.248 15.927 1.00 139.52 ? 350 THR   A N   1 
ATOM   373  C  CA  . THR   A 1 54  ? -19.291 -31.539 15.251 1.00 133.91 ? 350 THR   A CA  1 
ATOM   374  C  C   . THR   A 1 54  ? -20.690 -31.741 14.687 1.00 128.18 ? 350 THR   A C   1 
ATOM   375  O  O   . THR   A 1 54  ? -21.667 -31.184 15.194 1.00 122.58 ? 350 THR   A O   1 
ATOM   376  C  CB  . THR   A 1 54  ? -18.951 -32.725 16.177 1.00 133.47 ? 350 THR   A CB  1 
ATOM   377  O  OG1 . THR   A 1 54  ? -20.042 -32.969 17.071 1.00 131.77 ? 350 THR   A OG1 1 
ATOM   378  C  CG2 . THR   A 1 54  ? -17.683 -32.460 16.988 1.00 131.59 ? 350 THR   A CG2 1 
ATOM   379  N  N   . LYS   A 1 55  ? -20.778 -32.559 13.636 1.00 133.15 ? 351 LYS   A N   1 
ATOM   380  C  CA  . LYS   A 1 55  ? -22.070 -32.824 13.009 1.00 136.86 ? 351 LYS   A CA  1 
ATOM   381  C  C   . LYS   A 1 55  ? -23.039 -33.488 13.982 1.00 137.27 ? 351 LYS   A C   1 
ATOM   382  O  O   . LYS   A 1 55  ? -24.260 -33.328 13.854 1.00 133.26 ? 351 LYS   A O   1 
ATOM   383  C  CB  . LYS   A 1 55  ? -21.874 -33.688 11.761 1.00 140.45 ? 351 LYS   A CB  1 
ATOM   384  C  CG  . LYS   A 1 55  ? -20.879 -34.828 11.949 1.00 142.84 ? 351 LYS   A CG  1 
ATOM   385  C  CD  . LYS   A 1 55  ? -20.725 -35.677 10.689 1.00 144.44 ? 351 LYS   A CD  1 
ATOM   386  C  CE  . LYS   A 1 55  ? -19.845 -36.894 10.966 1.00 147.32 ? 351 LYS   A CE  1 
ATOM   387  N  NZ  . LYS   A 1 55  ? -19.693 -37.803 9.790  1.00 146.73 ? 351 LYS   A NZ  1 
ATOM   388  N  N   . ASP   A 1 56  ? -22.519 -34.221 14.967 1.00 141.85 ? 352 ASP   A N   1 
ATOM   389  C  CA  . ASP   A 1 56  ? -23.388 -34.876 15.938 1.00 146.08 ? 352 ASP   A CA  1 
ATOM   390  C  C   . ASP   A 1 56  ? -24.000 -33.857 16.893 1.00 137.14 ? 352 ASP   A C   1 
ATOM   391  O  O   . ASP   A 1 56  ? -25.206 -33.891 17.167 1.00 140.43 ? 352 ASP   A O   1 
ATOM   392  C  CB  . ASP   A 1 56  ? -22.609 -35.952 16.704 1.00 156.03 ? 352 ASP   A CB  1 
ATOM   393  C  CG  . ASP   A 1 56  ? -21.131 -35.994 16.329 1.00 159.51 ? 352 ASP   A CG  1 
ATOM   394  O  OD1 . ASP   A 1 56  ? -20.346 -36.632 17.067 1.00 161.02 ? 352 ASP   A OD1 1 
ATOM   395  O  OD2 . ASP   A 1 56  ? -20.748 -35.382 15.308 1.00 155.56 ? 352 ASP   A OD2 1 
ATOM   396  N  N   . GLN   A 1 57  ? -23.181 -32.935 17.403 1.00 122.90 ? 353 GLN   A N   1 
ATOM   397  C  CA  . GLN   A 1 57  ? -23.692 -31.881 18.272 1.00 109.10 ? 353 GLN   A CA  1 
ATOM   398  C  C   . GLN   A 1 57  ? -24.715 -31.005 17.563 1.00 100.02 ? 353 GLN   A C   1 
ATOM   399  O  O   . GLN   A 1 57  ? -25.595 -30.430 18.215 1.00 92.28  ? 353 GLN   A O   1 
ATOM   400  C  CB  . GLN   A 1 57  ? -22.539 -31.011 18.764 1.00 108.72 ? 353 GLN   A CB  1 
ATOM   401  C  CG  . GLN   A 1 57  ? -21.460 -31.744 19.535 1.00 118.95 ? 353 GLN   A CG  1 
ATOM   402  C  CD  . GLN   A 1 57  ? -20.109 -31.068 19.386 1.00 121.53 ? 353 GLN   A CD  1 
ATOM   403  O  OE1 . GLN   A 1 57  ? -19.845 -30.408 18.376 1.00 117.28 ? 353 GLN   A OE1 1 
ATOM   404  N  NE2 . GLN   A 1 57  ? -19.246 -31.227 20.388 1.00 120.28 ? 353 GLN   A NE2 1 
ATOM   405  N  N   . LEU   A 1 58  ? -24.624 -30.904 16.231 1.00 91.69  ? 354 LEU   A N   1 
ATOM   406  C  CA  . LEU   A 1 58  ? -25.311 -29.839 15.507 1.00 91.61  ? 354 LEU   A CA  1 
ATOM   407  C  C   . LEU   A 1 58  ? -26.819 -30.051 15.427 1.00 99.03  ? 354 LEU   A C   1 
ATOM   408  O  O   . LEU   A 1 58  ? -27.573 -29.070 15.455 1.00 95.66  ? 354 LEU   A O   1 
ATOM   409  C  CB  . LEU   A 1 58  ? -24.731 -29.708 14.097 1.00 93.95  ? 354 LEU   A CB  1 
ATOM   410  C  CG  . LEU   A 1 58  ? -24.111 -28.366 13.692 1.00 91.01  ? 354 LEU   A CG  1 
ATOM   411  C  CD1 . LEU   A 1 58  ? -22.726 -28.176 14.292 1.00 90.82  ? 354 LEU   A CD1 1 
ATOM   412  C  CD2 . LEU   A 1 58  ? -24.053 -28.283 12.158 1.00 87.43  ? 354 LEU   A CD2 1 
ATOM   413  N  N   . PHE   A 1 59  ? -27.290 -31.302 15.305 1.00 107.08 ? 355 PHE   A N   1 
ATOM   414  C  CA  . PHE   A 1 59  ? -28.724 -31.451 15.060 1.00 110.85 ? 355 PHE   A CA  1 
ATOM   415  C  C   . PHE   A 1 59  ? -29.603 -31.152 16.273 1.00 112.14 ? 355 PHE   A C   1 
ATOM   416  O  O   . PHE   A 1 59  ? -30.614 -30.457 16.110 1.00 112.89 ? 355 PHE   A O   1 
ATOM   417  C  CB  . PHE   A 1 59  ? -29.101 -32.836 14.537 1.00 113.86 ? 355 PHE   A CB  1 
ATOM   418  C  CG  . PHE   A 1 59  ? -30.542 -32.915 14.103 1.00 125.20 ? 355 PHE   A CG  1 
ATOM   419  C  CD1 . PHE   A 1 59  ? -30.957 -32.278 12.944 1.00 129.08 ? 355 PHE   A CD1 1 
ATOM   420  C  CD2 . PHE   A 1 59  ? -31.490 -33.574 14.870 1.00 128.55 ? 355 PHE   A CD2 1 
ATOM   421  C  CE1 . PHE   A 1 59  ? -32.281 -32.311 12.548 1.00 128.02 ? 355 PHE   A CE1 1 
ATOM   422  C  CE2 . PHE   A 1 59  ? -32.819 -33.617 14.471 1.00 130.56 ? 355 PHE   A CE2 1 
ATOM   423  C  CZ  . PHE   A 1 59  ? -33.211 -32.988 13.305 1.00 130.98 ? 355 PHE   A CZ  1 
ATOM   424  N  N   . PRO   A 1 60  ? -29.313 -31.670 17.479 1.00 113.55 ? 356 PRO   A N   1 
ATOM   425  C  CA  . PRO   A 1 60  ? -30.142 -31.267 18.629 1.00 104.52 ? 356 PRO   A CA  1 
ATOM   426  C  C   . PRO   A 1 60  ? -30.263 -29.760 18.754 1.00 95.63  ? 356 PRO   A C   1 
ATOM   427  O  O   . PRO   A 1 60  ? -31.365 -29.242 18.972 1.00 96.06  ? 356 PRO   A O   1 
ATOM   428  C  CB  . PRO   A 1 60  ? -29.416 -31.893 19.832 1.00 112.06 ? 356 PRO   A CB  1 
ATOM   429  C  CG  . PRO   A 1 60  ? -28.053 -32.222 19.341 1.00 112.37 ? 356 PRO   A CG  1 
ATOM   430  C  CD  . PRO   A 1 60  ? -28.226 -32.572 17.901 1.00 115.27 ? 356 PRO   A CD  1 
ATOM   431  N  N   . LEU   A 1 61  ? -29.149 -29.045 18.577 1.00 90.67  ? 357 LEU   A N   1 
ATOM   432  C  CA  . LEU   A 1 61  ? -29.175 -27.585 18.563 1.00 82.30  ? 357 LEU   A CA  1 
ATOM   433  C  C   . LEU   A 1 61  ? -30.052 -27.050 17.436 1.00 88.30  ? 357 LEU   A C   1 
ATOM   434  O  O   . LEU   A 1 61  ? -30.762 -26.052 17.617 1.00 86.75  ? 357 LEU   A O   1 
ATOM   435  C  CB  . LEU   A 1 61  ? -27.752 -27.056 18.428 1.00 72.32  ? 357 LEU   A CB  1 
ATOM   436  C  CG  . LEU   A 1 61  ? -26.848 -27.504 19.569 1.00 75.05  ? 357 LEU   A CG  1 
ATOM   437  C  CD1 . LEU   A 1 61  ? -25.386 -27.298 19.243 1.00 72.06  ? 357 LEU   A CD1 1 
ATOM   438  C  CD2 . LEU   A 1 61  ? -27.228 -26.732 20.830 1.00 90.42  ? 357 LEU   A CD2 1 
ATOM   439  N  N   . ALA   A 1 62  ? -30.006 -27.693 16.262 1.00 84.67  ? 358 ALA   A N   1 
ATOM   440  C  CA  . ALA   A 1 62  ? -30.865 -27.288 15.154 1.00 80.36  ? 358 ALA   A CA  1 
ATOM   441  C  C   . ALA   A 1 62  ? -32.325 -27.584 15.463 1.00 88.17  ? 358 ALA   A C   1 
ATOM   442  O  O   . ALA   A 1 62  ? -33.191 -26.715 15.303 1.00 89.80  ? 358 ALA   A O   1 
ATOM   443  C  CB  . ALA   A 1 62  ? -30.435 -27.991 13.864 1.00 88.13  ? 358 ALA   A CB  1 
ATOM   444  N  N   . LYS   A 1 63  ? -32.612 -28.813 15.905 1.00 99.83  ? 359 LYS   A N   1 
ATOM   445  C  CA  . LYS   A 1 63  ? -33.970 -29.203 16.273 1.00 107.21 ? 359 LYS   A CA  1 
ATOM   446  C  C   . LYS   A 1 63  ? -34.540 -28.275 17.340 1.00 103.86 ? 359 LYS   A C   1 
ATOM   447  O  O   . LYS   A 1 63  ? -35.624 -27.707 17.181 1.00 112.53 ? 359 LYS   A O   1 
ATOM   448  C  CB  . LYS   A 1 63  ? -33.973 -30.651 16.767 1.00 110.83 ? 359 LYS   A CB  1 
ATOM   449  C  CG  . LYS   A 1 63  ? -35.318 -31.117 17.279 1.00 110.70 ? 359 LYS   A CG  1 
ATOM   450  C  CD  . LYS   A 1 63  ? -35.275 -32.541 17.788 1.00 110.83 ? 359 LYS   A CD  1 
ATOM   451  C  CE  . LYS   A 1 63  ? -36.593 -33.243 17.509 1.00 113.24 ? 359 LYS   A CE  1 
ATOM   452  N  NZ  . LYS   A 1 63  ? -37.760 -32.380 17.840 1.00 113.23 ? 359 LYS   A NZ  1 
ATOM   453  N  N   . GLU   A 1 64  ? -33.802 -28.106 18.436 1.00 93.03  ? 360 GLU   A N   1 
ATOM   454  C  CA  . GLU   A 1 64  ? -34.237 -27.226 19.515 1.00 93.68  ? 360 GLU   A CA  1 
ATOM   455  C  C   . GLU   A 1 64  ? -34.562 -25.829 18.997 1.00 84.49  ? 360 GLU   A C   1 
ATOM   456  O  O   . GLU   A 1 64  ? -35.604 -25.257 19.333 1.00 83.27  ? 360 GLU   A O   1 
ATOM   457  C  CB  . GLU   A 1 64  ? -33.156 -27.180 20.597 1.00 104.20 ? 360 GLU   A CB  1 
ATOM   458  C  CG  . GLU   A 1 64  ? -33.303 -26.067 21.606 1.00 108.69 ? 360 GLU   A CG  1 
ATOM   459  C  CD  . GLU   A 1 64  ? -32.042 -25.881 22.423 1.00 116.62 ? 360 GLU   A CD  1 
ATOM   460  O  OE1 . GLU   A 1 64  ? -31.147 -26.753 22.335 1.00 119.19 ? 360 GLU   A OE1 1 
ATOM   461  O  OE2 . GLU   A 1 64  ? -31.948 -24.865 23.146 1.00 115.28 ? 360 GLU   A OE2 1 
ATOM   462  N  N   . PHE   A 1 65  ? -33.688 -25.268 18.159 1.00 82.32  ? 361 PHE   A N   1 
ATOM   463  C  CA  . PHE   A 1 65  ? -33.960 -23.954 17.587 1.00 74.94  ? 361 PHE   A CA  1 
ATOM   464  C  C   . PHE   A 1 65  ? -35.192 -23.989 16.688 1.00 83.40  ? 361 PHE   A C   1 
ATOM   465  O  O   . PHE   A 1 65  ? -36.080 -23.136 16.802 1.00 79.78  ? 361 PHE   A O   1 
ATOM   466  C  CB  . PHE   A 1 65  ? -32.746 -23.451 16.803 1.00 80.33  ? 361 PHE   A CB  1 
ATOM   467  C  CG  . PHE   A 1 65  ? -33.023 -22.214 15.994 1.00 78.88  ? 361 PHE   A CG  1 
ATOM   468  C  CD1 . PHE   A 1 65  ? -33.147 -20.982 16.617 1.00 85.25  ? 361 PHE   A CD1 1 
ATOM   469  C  CD2 . PHE   A 1 65  ? -33.165 -22.283 14.616 1.00 86.01  ? 361 PHE   A CD2 1 
ATOM   470  C  CE1 . PHE   A 1 65  ? -33.405 -19.843 15.886 1.00 84.91  ? 361 PHE   A CE1 1 
ATOM   471  C  CE2 . PHE   A 1 65  ? -33.425 -21.145 13.879 1.00 80.61  ? 361 PHE   A CE2 1 
ATOM   472  C  CZ  . PHE   A 1 65  ? -33.544 -19.919 14.523 1.00 74.62  ? 361 PHE   A CZ  1 
ATOM   473  N  N   . LEU   A 1 66  ? -35.257 -24.970 15.775 1.00 81.31  ? 362 LEU   A N   1 
ATOM   474  C  CA  . LEU   A 1 66  ? -36.371 -25.049 14.835 1.00 80.10  ? 362 LEU   A CA  1 
ATOM   475  C  C   . LEU   A 1 66  ? -37.701 -25.255 15.540 1.00 86.41  ? 362 LEU   A C   1 
ATOM   476  O  O   . LEU   A 1 66  ? -38.735 -24.774 15.065 1.00 93.02  ? 362 LEU   A O   1 
ATOM   477  C  CB  . LEU   A 1 66  ? -36.135 -26.185 13.839 1.00 94.03  ? 362 LEU   A CB  1 
ATOM   478  C  CG  . LEU   A 1 66  ? -35.006 -26.004 12.826 1.00 95.75  ? 362 LEU   A CG  1 
ATOM   479  C  CD1 . LEU   A 1 66  ? -34.922 -27.223 11.926 1.00 96.64  ? 362 LEU   A CD1 1 
ATOM   480  C  CD2 . LEU   A 1 66  ? -35.208 -24.731 12.015 1.00 91.71  ? 362 LEU   A CD2 1 
ATOM   481  N  N   . ASP   A 1 67  ? -37.701 -25.981 16.657 1.00 91.40  ? 363 ASP   A N   1 
ATOM   482  C  CA  . ASP   A 1 67  ? -38.941 -26.222 17.387 1.00 98.12  ? 363 ASP   A CA  1 
ATOM   483  C  C   . ASP   A 1 67  ? -39.493 -24.935 17.994 1.00 90.01  ? 363 ASP   A C   1 
ATOM   484  O  O   . ASP   A 1 67  ? -40.712 -24.723 18.000 1.00 89.43  ? 363 ASP   A O   1 
ATOM   485  C  CB  . ASP   A 1 67  ? -38.708 -27.279 18.466 1.00 101.97 ? 363 ASP   A CB  1 
ATOM   486  C  CG  . ASP   A 1 67  ? -38.781 -28.698 17.922 1.00 112.44 ? 363 ASP   A CG  1 
ATOM   487  O  OD1 . ASP   A 1 67  ? -39.893 -29.259 17.846 1.00 122.12 ? 363 ASP   A OD1 1 
ATOM   488  O  OD2 . ASP   A 1 67  ? -37.729 -29.254 17.556 1.00 115.67 ? 363 ASP   A OD2 1 
ATOM   489  N  N   . GLN   A 1 68  ? -38.621 -24.059 18.510 1.00 77.80  ? 364 GLN   A N   1 
ATOM   490  C  CA  . GLN   A 1 68  ? -39.120 -22.806 19.064 1.00 78.45  ? 364 GLN   A CA  1 
ATOM   491  C  C   . GLN   A 1 68  ? -39.475 -21.807 17.965 1.00 85.89  ? 364 GLN   A C   1 
ATOM   492  O  O   . GLN   A 1 68  ? -40.399 -21.003 18.141 1.00 88.01  ? 364 GLN   A O   1 
ATOM   493  C  CB  . GLN   A 1 68  ? -38.103 -22.209 20.051 1.00 78.43  ? 364 GLN   A CB  1 
ATOM   494  C  CG  . GLN   A 1 68  ? -36.759 -21.815 19.452 1.00 82.51  ? 364 GLN   A CG  1 
ATOM   495  C  CD  . GLN   A 1 68  ? -35.648 -21.660 20.493 1.00 84.70  ? 364 GLN   A CD  1 
ATOM   496  O  OE1 . GLN   A 1 68  ? -35.134 -20.559 20.711 1.00 80.48  ? 364 GLN   A OE1 1 
ATOM   497  N  NE2 . GLN   A 1 68  ? -35.252 -22.772 21.109 1.00 80.94  ? 364 GLN   A NE2 1 
ATOM   498  N  N   . TYR   A 1 69  ? -38.780 -21.851 16.824 1.00 85.42  ? 365 TYR   A N   1 
ATOM   499  C  CA  . TYR   A 1 69  ? -39.162 -20.986 15.713 1.00 90.76  ? 365 TYR   A CA  1 
ATOM   500  C  C   . TYR   A 1 69  ? -40.543 -21.347 15.179 1.00 95.00  ? 365 TYR   A C   1 
ATOM   501  O  O   . TYR   A 1 69  ? -41.368 -20.462 14.926 1.00 92.92  ? 365 TYR   A O   1 
ATOM   502  C  CB  . TYR   A 1 69  ? -38.131 -21.056 14.585 1.00 87.97  ? 365 TYR   A CB  1 
ATOM   503  C  CG  . TYR   A 1 69  ? -38.641 -20.406 13.319 1.00 88.39  ? 365 TYR   A CG  1 
ATOM   504  C  CD1 . TYR   A 1 69  ? -39.008 -19.065 13.309 1.00 85.84  ? 365 TYR   A CD1 1 
ATOM   505  C  CD2 . TYR   A 1 69  ? -38.780 -21.133 12.141 1.00 90.31  ? 365 TYR   A CD2 1 
ATOM   506  C  CE1 . TYR   A 1 69  ? -39.489 -18.462 12.163 1.00 83.10  ? 365 TYR   A CE1 1 
ATOM   507  C  CE2 . TYR   A 1 69  ? -39.261 -20.536 10.988 1.00 83.51  ? 365 TYR   A CE2 1 
ATOM   508  C  CZ  . TYR   A 1 69  ? -39.612 -19.201 11.011 1.00 86.35  ? 365 TYR   A CZ  1 
ATOM   509  O  OH  . TYR   A 1 69  ? -40.090 -18.591 9.881  1.00 92.82  ? 365 TYR   A OH  1 
ATOM   510  N  N   . TYR   A 1 70  ? -40.809 -22.638 14.977 1.00 104.32 ? 366 TYR   A N   1 
ATOM   511  C  CA  . TYR   A 1 70  ? -42.124 -23.024 14.483 1.00 108.76 ? 366 TYR   A CA  1 
ATOM   512  C  C   . TYR   A 1 70  ? -43.185 -22.847 15.557 1.00 114.57 ? 366 TYR   A C   1 
ATOM   513  O  O   . TYR   A 1 70  ? -44.343 -22.550 15.241 1.00 128.61 ? 366 TYR   A O   1 
ATOM   514  C  CB  . TYR   A 1 70  ? -42.094 -24.462 13.964 1.00 109.18 ? 366 TYR   A CB  1 
ATOM   515  C  CG  . TYR   A 1 70  ? -41.544 -24.534 12.555 1.00 106.74 ? 366 TYR   A CG  1 
ATOM   516  C  CD1 . TYR   A 1 70  ? -40.233 -24.925 12.311 1.00 100.18 ? 366 TYR   A CD1 1 
ATOM   517  C  CD2 . TYR   A 1 70  ? -42.328 -24.160 11.472 1.00 104.80 ? 366 TYR   A CD2 1 
ATOM   518  C  CE1 . TYR   A 1 70  ? -39.724 -24.969 11.022 1.00 98.60  ? 366 TYR   A CE1 1 
ATOM   519  C  CE2 . TYR   A 1 70  ? -41.834 -24.200 10.181 1.00 108.54 ? 366 TYR   A CE2 1 
ATOM   520  C  CZ  . TYR   A 1 70  ? -40.534 -24.605 9.959  1.00 104.62 ? 366 TYR   A CZ  1 
ATOM   521  O  OH  . TYR   A 1 70  ? -40.050 -24.636 8.660  1.00 100.57 ? 366 TYR   A OH  1 
ATOM   522  N  N   . SER   A 1 71  ? -42.811 -23.007 16.826 1.00 102.20 ? 367 SER   A N   1 
ATOM   523  C  CA  . SER   A 1 71  ? -43.726 -22.705 17.918 1.00 112.29 ? 367 SER   A CA  1 
ATOM   524  C  C   . SER   A 1 71  ? -43.966 -21.211 18.073 1.00 115.44 ? 367 SER   A C   1 
ATOM   525  O  O   . SER   A 1 71  ? -44.864 -20.822 18.829 1.00 126.52 ? 367 SER   A O   1 
ATOM   526  C  CB  . SER   A 1 71  ? -43.190 -23.287 19.231 1.00 104.34 ? 367 SER   A CB  1 
ATOM   527  O  OG  . SER   A 1 71  ? -44.107 -23.097 20.294 1.00 105.73 ? 367 SER   A OG  1 
ATOM   528  N  N   . SER   A 1 72  ? -43.185 -20.371 17.391 1.00 102.37 ? 368 SER   A N   1 
ATOM   529  C  CA  . SER   A 1 72  ? -43.381 -18.930 17.472 1.00 101.70 ? 368 SER   A CA  1 
ATOM   530  C  C   . SER   A 1 72  ? -44.308 -18.407 16.384 1.00 110.55 ? 368 SER   A C   1 
ATOM   531  O  O   . SER   A 1 72  ? -44.964 -17.381 16.587 1.00 120.91 ? 368 SER   A O   1 
ATOM   532  C  CB  . SER   A 1 72  ? -42.034 -18.199 17.408 1.00 99.22  ? 368 SER   A CB  1 
ATOM   533  O  OG  . SER   A 1 72  ? -41.623 -17.943 16.079 1.00 92.05  ? 368 SER   A OG  1 
ATOM   534  N  N   . ILE   A 1 73  ? -44.357 -19.069 15.232 1.00 107.10 ? 369 ILE   A N   1 
ATOM   535  C  CA  . ILE   A 1 73  ? -45.363 -18.792 14.220 1.00 111.38 ? 369 ILE   A CA  1 
ATOM   536  C  C   . ILE   A 1 73  ? -46.609 -19.656 14.432 1.00 114.68 ? 369 ILE   A C   1 
ATOM   537  O  O   . ILE   A 1 73  ? -47.442 -19.771 13.541 1.00 115.80 ? 369 ILE   A O   1 
ATOM   538  C  CB  . ILE   A 1 73  ? -44.796 -18.958 12.799 1.00 110.27 ? 369 ILE   A CB  1 
ATOM   539  C  CG1 . ILE   A 1 73  ? -44.257 -20.372 12.587 1.00 108.81 ? 369 ILE   A CG1 1 
ATOM   540  C  CG2 . ILE   A 1 73  ? -43.713 -17.913 12.509 1.00 106.48 ? 369 ILE   A CG2 1 
ATOM   541  C  CD1 . ILE   A 1 73  ? -43.406 -20.510 11.323 1.00 105.25 ? 369 ILE   A CD1 1 
ATOM   542  N  N   . LYS   A 1 74  ? -46.728 -20.269 15.609 1.00 114.83 ? 370 LYS   A N   1 
ATOM   543  C  CA  . LYS   A 1 74  ? -47.822 -21.167 15.968 1.00 125.02 ? 370 LYS   A CA  1 
ATOM   544  C  C   . LYS   A 1 74  ? -48.100 -22.186 14.864 1.00 134.12 ? 370 LYS   A C   1 
ATOM   545  O  O   . LYS   A 1 74  ? -49.251 -22.472 14.526 1.00 141.77 ? 370 LYS   A O   1 
ATOM   546  C  CB  . LYS   A 1 74  ? -49.081 -20.376 16.344 1.00 126.04 ? 370 LYS   A CB  1 
ATOM   547  C  CG  . LYS   A 1 74  ? -49.219 -20.074 17.843 1.00 126.61 ? 370 LYS   A CG  1 
ATOM   548  C  CD  . LYS   A 1 74  ? -48.087 -19.175 18.370 1.00 120.29 ? 370 LYS   A CD  1 
ATOM   549  C  CE  . LYS   A 1 74  ? -48.176 -18.960 19.890 1.00 116.18 ? 370 LYS   A CE  1 
ATOM   550  N  NZ  . LYS   A 1 74  ? -47.095 -18.068 20.444 1.00 98.77  ? 370 LYS   A NZ  1 
ATOM   551  N  N   . ARG   A 1 75  ? -47.022 -22.703 14.269 1.00 125.34 ? 371 ARG   A N   1 
ATOM   552  C  CA  . ARG   A 1 75  ? -47.070 -23.878 13.408 1.00 125.52 ? 371 ARG   A CA  1 
ATOM   553  C  C   . ARG   A 1 75  ? -46.087 -24.918 13.938 1.00 128.09 ? 371 ARG   A C   1 
ATOM   554  O  O   . ARG   A 1 75  ? -45.260 -25.458 13.195 1.00 122.20 ? 371 ARG   A O   1 
ATOM   555  C  CB  . ARG   A 1 75  ? -46.777 -23.503 11.956 1.00 115.99 ? 371 ARG   A CB  1 
ATOM   556  C  CG  . ARG   A 1 75  ? -47.843 -22.592 11.356 1.00 122.29 ? 371 ARG   A CG  1 
ATOM   557  C  CD  . ARG   A 1 75  ? -47.229 -21.380 10.668 1.00 126.26 ? 371 ARG   A CD  1 
ATOM   558  N  NE  . ARG   A 1 75  ? -47.400 -21.425 9.219  1.00 130.61 ? 371 ARG   A NE  1 
ATOM   559  C  CZ  . ARG   A 1 75  ? -46.605 -22.104 8.398  1.00 135.97 ? 371 ARG   A CZ  1 
ATOM   560  N  NH1 . ARG   A 1 75  ? -46.824 -22.093 7.089  1.00 136.69 ? 371 ARG   A NH1 1 
ATOM   561  N  NH2 . ARG   A 1 75  ? -45.588 -22.800 8.889  1.00 136.94 ? 371 ARG   A NH2 1 
ATOM   562  N  N   . PHE   A 1 76  ? -46.187 -25.181 15.242 1.00 135.62 ? 372 PHE   A N   1 
ATOM   563  C  CA  . PHE   A 1 76  ? -45.324 -26.130 15.934 1.00 139.55 ? 372 PHE   A CA  1 
ATOM   564  C  C   . PHE   A 1 76  ? -45.744 -27.559 15.599 1.00 147.23 ? 372 PHE   A C   1 
ATOM   565  O  O   . PHE   A 1 76  ? -46.933 -27.889 15.623 1.00 153.53 ? 372 PHE   A O   1 
ATOM   566  C  CB  . PHE   A 1 76  ? -45.407 -25.865 17.446 1.00 142.33 ? 372 PHE   A CB  1 
ATOM   567  C  CG  . PHE   A 1 76  ? -44.687 -26.873 18.318 1.00 141.20 ? 372 PHE   A CG  1 
ATOM   568  C  CD1 . PHE   A 1 76  ? -43.549 -27.535 17.887 1.00 138.44 ? 372 PHE   A CD1 1 
ATOM   569  C  CD2 . PHE   A 1 76  ? -45.156 -27.135 19.595 1.00 144.66 ? 372 PHE   A CD2 1 
ATOM   570  C  CE1 . PHE   A 1 76  ? -42.909 -28.451 18.700 1.00 136.36 ? 372 PHE   A CE1 1 
ATOM   571  C  CE2 . PHE   A 1 76  ? -44.518 -28.044 20.414 1.00 146.71 ? 372 PHE   A CE2 1 
ATOM   572  C  CZ  . PHE   A 1 76  ? -43.393 -28.703 19.966 1.00 143.18 ? 372 PHE   A CZ  1 
ATOM   573  N  N   . GLY   A 1 77  ? -44.765 -28.400 15.267 1.00 144.29 ? 373 GLY   A N   1 
ATOM   574  C  CA  . GLY   A 1 77  ? -45.004 -29.808 15.025 1.00 149.17 ? 373 GLY   A CA  1 
ATOM   575  C  C   . GLY   A 1 77  ? -45.788 -30.131 13.773 1.00 150.22 ? 373 GLY   A C   1 
ATOM   576  O  O   . GLY   A 1 77  ? -46.050 -31.313 13.516 1.00 155.10 ? 373 GLY   A O   1 
ATOM   577  N  N   . SER   A 1 78  ? -46.168 -29.129 12.985 1.00 140.86 ? 374 SER   A N   1 
ATOM   578  C  CA  . SER   A 1 78  ? -46.938 -29.367 11.778 1.00 136.17 ? 374 SER   A CA  1 
ATOM   579  C  C   . SER   A 1 78  ? -46.061 -30.036 10.721 1.00 126.29 ? 374 SER   A C   1 
ATOM   580  O  O   . SER   A 1 78  ? -44.885 -30.348 10.946 1.00 113.97 ? 374 SER   A O   1 
ATOM   581  C  CB  . SER   A 1 78  ? -47.520 -28.055 11.255 1.00 135.23 ? 374 SER   A CB  1 
ATOM   582  O  OG  . SER   A 1 78  ? -46.496 -27.174 10.827 1.00 128.91 ? 374 SER   A OG  1 
ATOM   583  N  N   . LYS   A 1 79  ? -46.657 -30.267 9.547  1.00 122.09 ? 375 LYS   A N   1 
ATOM   584  C  CA  . LYS   A 1 79  ? -45.908 -30.842 8.436  1.00 121.23 ? 375 LYS   A CA  1 
ATOM   585  C  C   . LYS   A 1 79  ? -44.808 -29.897 7.971  1.00 116.63 ? 375 LYS   A C   1 
ATOM   586  O  O   . LYS   A 1 79  ? -43.687 -30.334 7.690  1.00 112.78 ? 375 LYS   A O   1 
ATOM   587  C  CB  . LYS   A 1 79  ? -46.855 -31.177 7.283  1.00 123.90 ? 375 LYS   A CB  1 
ATOM   588  C  CG  . LYS   A 1 79  ? -46.197 -31.887 6.106  1.00 127.83 ? 375 LYS   A CG  1 
ATOM   589  C  CD  . LYS   A 1 79  ? -46.421 -33.391 6.171  1.00 138.11 ? 375 LYS   A CD  1 
ATOM   590  C  CE  . LYS   A 1 79  ? -46.032 -34.074 4.869  1.00 120.50 ? 375 LYS   A CE  1 
ATOM   591  N  NZ  . LYS   A 1 79  ? -44.570 -34.000 4.593  1.00 115.89 ? 375 LYS   A NZ  1 
ATOM   592  N  N   . ALA   A 1 80  ? -45.106 -28.597 7.892  1.00 119.22 ? 376 ALA   A N   1 
ATOM   593  C  CA  . ALA   A 1 80  ? -44.080 -27.631 7.512  1.00 119.00 ? 376 ALA   A CA  1 
ATOM   594  C  C   . ALA   A 1 80  ? -42.905 -27.672 8.481  1.00 116.54 ? 376 ALA   A C   1 
ATOM   595  O  O   . ALA   A 1 80  ? -41.750 -27.486 8.077  1.00 111.42 ? 376 ALA   A O   1 
ATOM   596  C  CB  . ALA   A 1 80  ? -44.678 -26.225 7.442  1.00 120.20 ? 376 ALA   A CB  1 
ATOM   597  N  N   . HIS   A 1 81  ? -43.178 -27.941 9.761  1.00 115.98 ? 377 HIS   A N   1 
ATOM   598  C  CA  . HIS   A 1 81  ? -42.106 -28.061 10.746 1.00 112.32 ? 377 HIS   A CA  1 
ATOM   599  C  C   . HIS   A 1 81  ? -41.349 -29.375 10.587 1.00 108.26 ? 377 HIS   A C   1 
ATOM   600  O  O   . HIS   A 1 81  ? -40.116 -29.384 10.505 1.00 101.53 ? 377 HIS   A O   1 
ATOM   601  C  CB  . HIS   A 1 81  ? -42.675 -27.938 12.161 1.00 116.49 ? 377 HIS   A CB  1 
ATOM   602  C  CG  . HIS   A 1 81  ? -41.659 -28.135 13.247 1.00 116.45 ? 377 HIS   A CG  1 
ATOM   603  N  ND1 . HIS   A 1 81  ? -42.014 -28.364 14.559 1.00 118.96 ? 377 HIS   A ND1 1 
ATOM   604  C  CD2 . HIS   A 1 81  ? -40.304 -28.135 13.221 1.00 114.07 ? 377 HIS   A CD2 1 
ATOM   605  C  CE1 . HIS   A 1 81  ? -40.925 -28.500 15.293 1.00 115.88 ? 377 HIS   A CE1 1 
ATOM   606  N  NE2 . HIS   A 1 81  ? -39.873 -28.364 14.507 1.00 115.77 ? 377 HIS   A NE2 1 
ATOM   607  N  N   . MET   A 1 82  ? -42.069 -30.498 10.556 1.00 113.83 ? 378 MET   A N   1 
ATOM   608  C  CA  . MET   A 1 82  ? -41.398 -31.791 10.466 1.00 119.64 ? 378 MET   A CA  1 
ATOM   609  C  C   . MET   A 1 82  ? -40.566 -31.907 9.189  1.00 125.07 ? 378 MET   A C   1 
ATOM   610  O  O   . MET   A 1 82  ? -39.483 -32.504 9.202  1.00 135.71 ? 378 MET   A O   1 
ATOM   611  C  CB  . MET   A 1 82  ? -42.426 -32.917 10.558 1.00 129.53 ? 378 MET   A CB  1 
ATOM   612  C  CG  . MET   A 1 82  ? -43.048 -33.045 11.938 1.00 138.59 ? 378 MET   A CG  1 
ATOM   613  S  SD  . MET   A 1 82  ? -41.798 -33.360 13.200 1.00 141.11 ? 378 MET   A SD  1 
ATOM   614  C  CE  . MET   A 1 82  ? -42.081 -31.997 14.332 1.00 141.03 ? 378 MET   A CE  1 
ATOM   615  N  N   . ASP   A 1 83  ? -41.043 -31.332 8.078  1.00 109.78 ? 379 ASP   A N   1 
ATOM   616  C  CA  . ASP   A 1 83  ? -40.259 -31.372 6.847  1.00 111.70 ? 379 ASP   A CA  1 
ATOM   617  C  C   . ASP   A 1 83  ? -38.978 -30.565 6.981  1.00 108.49 ? 379 ASP   A C   1 
ATOM   618  O  O   . ASP   A 1 83  ? -37.926 -30.964 6.467  1.00 103.32 ? 379 ASP   A O   1 
ATOM   619  C  CB  . ASP   A 1 83  ? -41.077 -30.855 5.665  1.00 118.94 ? 379 ASP   A CB  1 
ATOM   620  C  CG  . ASP   A 1 83  ? -41.758 -31.962 4.909  1.00 123.32 ? 379 ASP   A CG  1 
ATOM   621  O  OD1 . ASP   A 1 83  ? -42.954 -31.807 4.593  1.00 130.49 ? 379 ASP   A OD1 1 
ATOM   622  O  OD2 . ASP   A 1 83  ? -41.103 -32.993 4.649  1.00 130.21 ? 379 ASP   A OD2 1 
ATOM   623  N  N   . ARG   A 1 84  ? -39.053 -29.415 7.654  1.00 107.53 ? 380 ARG   A N   1 
ATOM   624  C  CA  . ARG   A 1 84  ? -37.864 -28.606 7.884  1.00 101.64 ? 380 ARG   A CA  1 
ATOM   625  C  C   . ARG   A 1 84  ? -36.906 -29.291 8.849  1.00 105.15 ? 380 ARG   A C   1 
ATOM   626  O  O   . ARG   A 1 84  ? -35.685 -29.134 8.730  1.00 111.30 ? 380 ARG   A O   1 
ATOM   627  C  CB  . ARG   A 1 84  ? -38.277 -27.237 8.420  1.00 101.27 ? 380 ARG   A CB  1 
ATOM   628  C  CG  . ARG   A 1 84  ? -37.128 -26.309 8.700  1.00 85.98  ? 380 ARG   A CG  1 
ATOM   629  C  CD  . ARG   A 1 84  ? -36.904 -25.371 7.538  1.00 90.92  ? 380 ARG   A CD  1 
ATOM   630  N  NE  . ARG   A 1 84  ? -35.637 -24.671 7.690  1.00 84.16  ? 380 ARG   A NE  1 
ATOM   631  C  CZ  . ARG   A 1 84  ? -34.510 -25.056 7.109  1.00 81.50  ? 380 ARG   A CZ  1 
ATOM   632  N  NH1 . ARG   A 1 84  ? -34.509 -26.122 6.323  1.00 79.71  ? 380 ARG   A NH1 1 
ATOM   633  N  NH2 . ARG   A 1 84  ? -33.390 -24.374 7.309  1.00 76.30  ? 380 ARG   A NH2 1 
ATOM   634  N  N   . LEU   A 1 85  ? -37.445 -30.039 9.814  1.00 105.66 ? 381 LEU   A N   1 
ATOM   635  C  CA  . LEU   A 1 85  ? -36.615 -30.852 10.694 1.00 101.16 ? 381 LEU   A CA  1 
ATOM   636  C  C   . LEU   A 1 85  ? -35.865 -31.912 9.902  1.00 104.93 ? 381 LEU   A C   1 
ATOM   637  O  O   . LEU   A 1 85  ? -34.645 -32.073 10.050 1.00 91.52  ? 381 LEU   A O   1 
ATOM   638  C  CB  . LEU   A 1 85  ? -37.489 -31.507 11.757 1.00 104.82 ? 381 LEU   A CB  1 
ATOM   639  C  CG  . LEU   A 1 85  ? -36.858 -31.607 13.137 1.00 100.32 ? 381 LEU   A CG  1 
ATOM   640  C  CD1 . LEU   A 1 85  ? -36.582 -30.210 13.630 1.00 88.10  ? 381 LEU   A CD1 1 
ATOM   641  C  CD2 . LEU   A 1 85  ? -37.784 -32.350 14.075 1.00 115.85 ? 381 LEU   A CD2 1 
ATOM   642  N  N   . GLU   A 1 86  ? -36.596 -32.658 9.064  1.00 115.89 ? 382 GLU   A N   1 
ATOM   643  C  CA  . GLU   A 1 86  ? -35.986 -33.648 8.182  1.00 121.54 ? 382 GLU   A CA  1 
ATOM   644  C  C   . GLU   A 1 86  ? -34.976 -33.004 7.241  1.00 110.18 ? 382 GLU   A C   1 
ATOM   645  O  O   . GLU   A 1 86  ? -33.858 -33.509 7.085  1.00 114.20 ? 382 GLU   A O   1 
ATOM   646  C  CB  . GLU   A 1 86  ? -37.071 -34.366 7.379  1.00 135.86 ? 382 GLU   A CB  1 
ATOM   647  C  CG  . GLU   A 1 86  ? -36.543 -35.363 6.356  1.00 147.11 ? 382 GLU   A CG  1 
ATOM   648  C  CD  . GLU   A 1 86  ? -36.554 -36.791 6.869  1.00 158.95 ? 382 GLU   A CD  1 
ATOM   649  O  OE1 . GLU   A 1 86  ? -36.435 -37.724 6.047  1.00 166.22 ? 382 GLU   A OE1 1 
ATOM   650  O  OE2 . GLU   A 1 86  ? -36.690 -36.983 8.095  1.00 161.78 ? 382 GLU   A OE2 1 
ATOM   651  N  N   . GLU   A 1 87  ? -35.351 -31.884 6.619  1.00 100.98 ? 383 GLU   A N   1 
ATOM   652  C  CA  . GLU   A 1 87  ? -34.497 -31.242 5.625  1.00 93.60  ? 383 GLU   A CA  1 
ATOM   653  C  C   . GLU   A 1 87  ? -33.136 -30.865 6.204  1.00 91.36  ? 383 GLU   A C   1 
ATOM   654  O  O   . GLU   A 1 87  ? -32.100 -31.037 5.546  1.00 89.39  ? 383 GLU   A O   1 
ATOM   655  C  CB  . GLU   A 1 87  ? -35.200 -30.004 5.067  1.00 94.86  ? 383 GLU   A CB  1 
ATOM   656  C  CG  . GLU   A 1 87  ? -34.422 -29.281 3.988  1.00 96.19  ? 383 GLU   A CG  1 
ATOM   657  C  CD  . GLU   A 1 87  ? -35.197 -28.113 3.413  1.00 98.18  ? 383 GLU   A CD  1 
ATOM   658  O  OE1 . GLU   A 1 87  ? -35.766 -27.337 4.215  1.00 80.28  ? 383 GLU   A OE1 1 
ATOM   659  O  OE2 . GLU   A 1 87  ? -35.242 -27.978 2.160  1.00 102.86 ? 383 GLU   A OE2 1 
ATOM   660  N  N   . VAL   A 1 88  ? -33.121 -30.327 7.429  1.00 82.90  ? 384 VAL   A N   1 
ATOM   661  C  CA  . VAL   A 1 88  ? -31.869 -29.886 8.045  1.00 86.84  ? 384 VAL   A CA  1 
ATOM   662  C  C   . VAL   A 1 88  ? -31.075 -31.078 8.568  1.00 96.76  ? 384 VAL   A C   1 
ATOM   663  O  O   . VAL   A 1 88  ? -29.842 -31.118 8.448  1.00 87.48  ? 384 VAL   A O   1 
ATOM   664  C  CB  . VAL   A 1 88  ? -32.148 -28.860 9.160  1.00 89.66  ? 384 VAL   A CB  1 
ATOM   665  C  CG1 . VAL   A 1 88  ? -30.906 -28.638 10.016 1.00 85.92  ? 384 VAL   A CG1 1 
ATOM   666  C  CG2 . VAL   A 1 88  ? -32.627 -27.546 8.563  1.00 86.99  ? 384 VAL   A CG2 1 
ATOM   667  N  N   . ASN   A 1 89  ? -31.761 -32.054 9.175  1.00 107.24 ? 385 ASN   A N   1 
ATOM   668  C  CA  . ASN   A 1 89  ? -31.135 -33.331 9.507  1.00 113.75 ? 385 ASN   A CA  1 
ATOM   669  C  C   . ASN   A 1 89  ? -30.363 -33.874 8.312  1.00 114.49 ? 385 ASN   A C   1 
ATOM   670  O  O   . ASN   A 1 89  ? -29.162 -34.153 8.397  1.00 112.31 ? 385 ASN   A O   1 
ATOM   671  C  CB  . ASN   A 1 89  ? -32.202 -34.337 9.950  1.00 123.35 ? 385 ASN   A CB  1 
ATOM   672  C  CG  . ASN   A 1 89  ? -31.616 -35.532 10.687 1.00 132.79 ? 385 ASN   A CG  1 
ATOM   673  O  OD1 . ASN   A 1 89  ? -30.765 -35.376 11.564 1.00 131.07 ? 385 ASN   A OD1 1 
ATOM   674  N  ND2 . ASN   A 1 89  ? -32.067 -36.735 10.328 1.00 138.00 ? 385 ASN   A ND2 1 
ATOM   675  N  N   . LYS   A 1 90  ? -31.053 -34.007 7.177  1.00 117.24 ? 386 LYS   A N   1 
ATOM   676  C  CA  . LYS   A 1 90  ? -30.418 -34.490 5.958  1.00 118.01 ? 386 LYS   A CA  1 
ATOM   677  C  C   . LYS   A 1 90  ? -29.214 -33.634 5.578  1.00 118.17 ? 386 LYS   A C   1 
ATOM   678  O  O   . LYS   A 1 90  ? -28.146 -34.166 5.255  1.00 117.09 ? 386 LYS   A O   1 
ATOM   679  C  CB  . LYS   A 1 90  ? -31.441 -34.514 4.822  1.00 123.01 ? 386 LYS   A CB  1 
ATOM   680  C  CG  . LYS   A 1 90  ? -32.541 -35.556 4.983  1.00 130.05 ? 386 LYS   A CG  1 
ATOM   681  C  CD  . LYS   A 1 90  ? -33.673 -35.331 3.983  1.00 125.81 ? 386 LYS   A CD  1 
ATOM   682  C  CE  . LYS   A 1 90  ? -34.469 -36.611 3.749  1.00 125.87 ? 386 LYS   A CE  1 
ATOM   683  N  NZ  . LYS   A 1 90  ? -35.804 -36.351 3.144  1.00 124.38 ? 386 LYS   A NZ  1 
ATOM   684  N  N   . GLU   A 1 91  ? -29.359 -32.304 5.625  1.00 116.33 ? 387 GLU   A N   1 
ATOM   685  C  CA  . GLU   A 1 91  ? -28.255 -31.431 5.228  1.00 112.66 ? 387 GLU   A CA  1 
ATOM   686  C  C   . GLU   A 1 91  ? -27.082 -31.512 6.204  1.00 110.70 ? 387 GLU   A C   1 
ATOM   687  O  O   . GLU   A 1 91  ? -25.926 -31.373 5.788  1.00 108.42 ? 387 GLU   A O   1 
ATOM   688  C  CB  . GLU   A 1 91  ? -28.741 -29.984 5.088  1.00 109.67 ? 387 GLU   A CB  1 
ATOM   689  C  CG  . GLU   A 1 91  ? -27.683 -29.024 4.524  1.00 104.50 ? 387 GLU   A CG  1 
ATOM   690  C  CD  . GLU   A 1 91  ? -28.165 -27.582 4.399  1.00 100.00 ? 387 GLU   A CD  1 
ATOM   691  O  OE1 . GLU   A 1 91  ? -27.378 -26.727 3.937  1.00 94.60  ? 387 GLU   A OE1 1 
ATOM   692  O  OE2 . GLU   A 1 91  ? -29.325 -27.301 4.764  1.00 100.84 ? 387 GLU   A OE2 1 
ATOM   693  N  N   . ILE   A 1 92  ? -27.345 -31.732 7.497  1.00 112.18 ? 388 ILE   A N   1 
ATOM   694  C  CA  . ILE   A 1 92  ? -26.246 -31.939 8.436  1.00 108.84 ? 388 ILE   A CA  1 
ATOM   695  C  C   . ILE   A 1 92  ? -25.584 -33.296 8.213  1.00 118.84 ? 388 ILE   A C   1 
ATOM   696  O  O   . ILE   A 1 92  ? -24.420 -33.491 8.577  1.00 126.10 ? 388 ILE   A O   1 
ATOM   697  C  CB  . ILE   A 1 92  ? -26.735 -31.779 9.888  1.00 103.89 ? 388 ILE   A CB  1 
ATOM   698  C  CG1 . ILE   A 1 92  ? -27.309 -30.375 10.106 1.00 103.81 ? 388 ILE   A CG1 1 
ATOM   699  C  CG2 . ILE   A 1 92  ? -25.596 -31.984 10.869 1.00 104.90 ? 388 ILE   A CG2 1 
ATOM   700  C  CD1 . ILE   A 1 92  ? -27.825 -30.147 11.498 1.00 91.44  ? 388 ILE   A CD1 1 
ATOM   701  N  N   . GLU   A 1 93  ? -26.295 -34.249 7.614  1.00 119.41 ? 389 GLU   A N   1 
ATOM   702  C  CA  . GLU   A 1 93  ? -25.628 -35.434 7.086  1.00 125.36 ? 389 GLU   A CA  1 
ATOM   703  C  C   . GLU   A 1 93  ? -24.835 -35.087 5.830  1.00 119.58 ? 389 GLU   A C   1 
ATOM   704  O  O   . GLU   A 1 93  ? -23.610 -35.250 5.784  1.00 114.44 ? 389 GLU   A O   1 
ATOM   705  C  CB  . GLU   A 1 93  ? -26.657 -36.528 6.792  1.00 129.62 ? 389 GLU   A CB  1 
ATOM   706  C  CG  . GLU   A 1 93  ? -27.562 -36.867 7.966  1.00 136.25 ? 389 GLU   A CG  1 
ATOM   707  C  CD  . GLU   A 1 93  ? -26.913 -37.820 8.946  1.00 144.51 ? 389 GLU   A CD  1 
ATOM   708  O  OE1 . GLU   A 1 93  ? -25.781 -38.270 8.665  1.00 148.30 ? 389 GLU   A OE1 1 
ATOM   709  O  OE2 . GLU   A 1 93  ? -27.536 -38.122 9.989  1.00 144.07 ? 389 GLU   A OE2 1 
ATOM   710  N  N   . SER   A 1 94  ? -25.526 -34.571 4.808  1.00 126.76 ? 390 SER   A N   1 
ATOM   711  C  CA  . SER   A 1 94  ? -24.915 -34.322 3.504  1.00 128.75 ? 390 SER   A CA  1 
ATOM   712  C  C   . SER   A 1 94  ? -23.726 -33.372 3.604  1.00 126.53 ? 390 SER   A C   1 
ATOM   713  O  O   . SER   A 1 94  ? -22.630 -33.673 3.116  1.00 126.05 ? 390 SER   A O   1 
ATOM   714  C  CB  . SER   A 1 94  ? -25.970 -33.764 2.545  1.00 132.10 ? 390 SER   A CB  1 
ATOM   715  O  OG  . SER   A 1 94  ? -25.370 -33.063 1.469  1.00 136.41 ? 390 SER   A OG  1 
ATOM   716  N  N   . THR   A 1 95  ? -23.928 -32.212 4.234  1.00 123.97 ? 391 THR   A N   1 
ATOM   717  C  CA  . THR   A 1 95  ? -22.925 -31.155 4.263  1.00 117.62 ? 391 THR   A CA  1 
ATOM   718  C  C   . THR   A 1 95  ? -22.221 -31.023 5.608  1.00 118.82 ? 391 THR   A C   1 
ATOM   719  O  O   . THR   A 1 95  ? -21.355 -30.155 5.750  1.00 114.75 ? 391 THR   A O   1 
ATOM   720  C  CB  . THR   A 1 95  ? -23.557 -29.802 3.901  1.00 107.60 ? 391 THR   A CB  1 
ATOM   721  O  OG1 . THR   A 1 95  ? -24.211 -29.251 5.058  1.00 93.17  ? 391 THR   A OG1 1 
ATOM   722  C  CG2 . THR   A 1 95  ? -24.567 -29.954 2.768  1.00 101.64 ? 391 THR   A CG2 1 
ATOM   723  N  N   . SER   A 1 96  ? -22.575 -31.843 6.597  1.00 121.63 ? 392 SER   A N   1 
ATOM   724  C  CA  . SER   A 1 96  ? -22.051 -31.770 7.960  1.00 123.00 ? 392 SER   A CA  1 
ATOM   725  C  C   . SER   A 1 96  ? -22.334 -30.427 8.630  1.00 121.31 ? 392 SER   A C   1 
ATOM   726  O  O   . SER   A 1 96  ? -21.750 -30.125 9.678  1.00 114.79 ? 392 SER   A O   1 
ATOM   727  C  CB  . SER   A 1 96  ? -20.548 -32.083 8.011  1.00 126.25 ? 392 SER   A CB  1 
ATOM   728  O  OG  . SER   A 1 96  ? -19.797 -31.172 7.228  1.00 124.03 ? 392 SER   A OG  1 
ATOM   729  N  N   . THR   A 1 97  ? -23.211 -29.615 8.048  1.00 115.31 ? 393 THR   A N   1 
ATOM   730  C  CA  . THR   A 1 97  ? -23.709 -28.379 8.643  1.00 95.15  ? 393 THR   A CA  1 
ATOM   731  C  C   . THR   A 1 97  ? -25.037 -28.055 7.967  1.00 87.83  ? 393 THR   A C   1 
ATOM   732  O  O   . THR   A 1 97  ? -25.668 -28.951 7.370  1.00 91.07  ? 393 THR   A O   1 
ATOM   733  C  CB  . THR   A 1 97  ? -22.669 -27.250 8.516  1.00 89.91  ? 393 THR   A CB  1 
ATOM   734  O  OG1 . THR   A 1 97  ? -23.231 -26.024 9.000  1.00 94.22  ? 393 THR   A OG1 1 
ATOM   735  C  CG2 . THR   A 1 97  ? -22.235 -27.069 7.075  1.00 91.14  ? 393 THR   A CG2 1 
ATOM   736  N  N   . TYR   A 1 98  ? -25.489 -26.810 8.049  1.00 84.67  ? 394 TYR   A N   1 
ATOM   737  C  CA  . TYR   A 1 98  ? -26.738 -26.446 7.393  1.00 82.99  ? 394 TYR   A CA  1 
ATOM   738  C  C   . TYR   A 1 98  ? -26.835 -24.931 7.269  1.00 79.65  ? 394 TYR   A C   1 
ATOM   739  O  O   . TYR   A 1 98  ? -25.979 -24.185 7.756  1.00 82.25  ? 394 TYR   A O   1 
ATOM   740  C  CB  . TYR   A 1 98  ? -27.952 -27.032 8.138  1.00 84.62  ? 394 TYR   A CB  1 
ATOM   741  C  CG  . TYR   A 1 98  ? -28.288 -26.375 9.446  1.00 86.16  ? 394 TYR   A CG  1 
ATOM   742  C  CD1 . TYR   A 1 98  ? -29.251 -25.376 9.515  1.00 88.56  ? 394 TYR   A CD1 1 
ATOM   743  C  CD2 . TYR   A 1 98  ? -27.659 -26.763 10.620 1.00 88.33  ? 394 TYR   A CD2 1 
ATOM   744  C  CE1 . TYR   A 1 98  ? -29.566 -24.768 10.721 1.00 86.03  ? 394 TYR   A CE1 1 
ATOM   745  C  CE2 . TYR   A 1 98  ? -27.965 -26.167 11.817 1.00 82.95  ? 394 TYR   A CE2 1 
ATOM   746  C  CZ  . TYR   A 1 98  ? -28.920 -25.172 11.869 1.00 76.77  ? 394 TYR   A CZ  1 
ATOM   747  O  OH  . TYR   A 1 98  ? -29.221 -24.583 13.079 1.00 80.88  ? 394 TYR   A OH  1 
ATOM   748  N  N   . GLN   A 1 99  ? -27.901 -24.486 6.608  1.00 76.02  ? 395 GLN   A N   1 
ATOM   749  C  CA  . GLN   A 1 99  ? -28.110 -23.084 6.277  1.00 78.40  ? 395 GLN   A CA  1 
ATOM   750  C  C   . GLN   A 1 99  ? -29.496 -22.644 6.734  1.00 74.83  ? 395 GLN   A C   1 
ATOM   751  O  O   . GLN   A 1 99  ? -30.489 -23.345 6.519  1.00 68.95  ? 395 GLN   A O   1 
ATOM   752  C  CB  . GLN   A 1 99  ? -27.936 -22.843 4.758  1.00 72.51  ? 395 GLN   A CB  1 
ATOM   753  C  CG  . GLN   A 1 99  ? -26.527 -23.140 4.218  1.00 69.29  ? 395 GLN   A CG  1 
ATOM   754  C  CD  . GLN   A 1 99  ? -25.462 -22.227 4.813  1.00 69.52  ? 395 GLN   A CD  1 
ATOM   755  O  OE1 . GLN   A 1 99  ? -25.692 -21.038 5.007  1.00 71.37  ? 395 GLN   A OE1 1 
ATOM   756  N  NE2 . GLN   A 1 99  ? -24.296 -22.785 5.113  1.00 73.47  ? 395 GLN   A NE2 1 
ATOM   757  N  N   . LEU   A 1 100 ? -29.555 -21.481 7.368  1.00 60.34  ? 396 LEU   A N   1 
ATOM   758  C  CA  . LEU   A 1 100 ? -30.808 -20.953 7.887  1.00 59.76  ? 396 LEU   A CA  1 
ATOM   759  C  C   . LEU   A 1 100 ? -31.625 -20.321 6.769  1.00 64.96  ? 396 LEU   A C   1 
ATOM   760  O  O   . LEU   A 1 100 ? -31.075 -19.668 5.874  1.00 66.88  ? 396 LEU   A O   1 
ATOM   761  C  CB  . LEU   A 1 100 ? -30.531 -19.910 8.969  1.00 55.15  ? 396 LEU   A CB  1 
ATOM   762  C  CG  . LEU   A 1 100 ? -29.861 -20.465 10.223 1.00 54.93  ? 396 LEU   A CG  1 
ATOM   763  C  CD1 . LEU   A 1 100 ? -29.331 -19.316 11.067 1.00 51.63  ? 396 LEU   A CD1 1 
ATOM   764  C  CD2 . LEU   A 1 100 ? -30.857 -21.325 11.006 1.00 54.13  ? 396 LEU   A CD2 1 
ATOM   765  N  N   . LYS   A 1 101 ? -32.944 -20.521 6.817  1.00 65.61  ? 397 LYS   A N   1 
ATOM   766  C  CA  . LYS   A 1 101 ? -33.825 -19.730 5.972  1.00 76.00  ? 397 LYS   A CA  1 
ATOM   767  C  C   . LYS   A 1 101 ? -33.753 -18.278 6.420  1.00 74.86  ? 397 LYS   A C   1 
ATOM   768  O  O   . LYS   A 1 101 ? -33.432 -17.981 7.573  1.00 64.80  ? 397 LYS   A O   1 
ATOM   769  C  CB  . LYS   A 1 101 ? -35.270 -20.230 6.054  1.00 76.96  ? 397 LYS   A CB  1 
ATOM   770  C  CG  . LYS   A 1 101 ? -35.511 -21.607 5.482  1.00 86.17  ? 397 LYS   A CG  1 
ATOM   771  C  CD  . LYS   A 1 101 ? -35.645 -21.560 3.974  1.00 91.38  ? 397 LYS   A CD  1 
ATOM   772  C  CE  . LYS   A 1 101 ? -35.461 -22.936 3.383  1.00 96.78  ? 397 LYS   A CE  1 
ATOM   773  N  NZ  . LYS   A 1 101 ? -34.719 -22.863 2.100  1.00 95.71  ? 397 LYS   A NZ  1 
ATOM   774  N  N   . ASP   A 1 102 ? -34.035 -17.361 5.494  1.00 63.43  ? 398 ASP   A N   1 
ATOM   775  C  CA  . ASP   A 1 102 ? -33.992 -15.949 5.859  1.00 62.12  ? 398 ASP   A CA  1 
ATOM   776  C  C   . ASP   A 1 102 ? -34.892 -15.665 7.057  1.00 69.71  ? 398 ASP   A C   1 
ATOM   777  O  O   . ASP   A 1 102 ? -34.476 -14.994 8.009  1.00 59.85  ? 398 ASP   A O   1 
ATOM   778  C  CB  . ASP   A 1 102 ? -34.363 -15.081 4.660  1.00 80.60  ? 398 ASP   A CB  1 
ATOM   779  C  CG  . ASP   A 1 102 ? -33.223 -14.969 3.670  1.00 93.05  ? 398 ASP   A CG  1 
ATOM   780  O  OD1 . ASP   A 1 102 ? -32.366 -15.883 3.656  1.00 94.57  ? 398 ASP   A OD1 1 
ATOM   781  O  OD2 . ASP   A 1 102 ? -33.161 -13.963 2.933  1.00 97.12  ? 398 ASP   A OD2 1 
ATOM   782  N  N   . THR   A 1 103 ? -36.108 -16.220 7.055  1.00 68.03  ? 399 THR   A N   1 
ATOM   783  C  CA  . THR   A 1 103 ? -36.996 -16.076 8.208  1.00 73.54  ? 399 THR   A CA  1 
ATOM   784  C  C   . THR   A 1 103 ? -36.353 -16.599 9.493  1.00 78.06  ? 399 THR   A C   1 
ATOM   785  O  O   . THR   A 1 103 ? -36.485 -15.987 10.560 1.00 76.74  ? 399 THR   A O   1 
ATOM   786  C  CB  . THR   A 1 103 ? -38.302 -16.816 7.943  1.00 76.25  ? 399 THR   A CB  1 
ATOM   787  O  OG1 . THR   A 1 103 ? -37.997 -18.164 7.573  1.00 81.33  ? 399 THR   A OG1 1 
ATOM   788  C  CG2 . THR   A 1 103 ? -39.081 -16.147 6.828  1.00 69.38  ? 399 THR   A CG2 1 
ATOM   789  N  N   . GLU   A 1 104 ? -35.670 -17.741 9.413  1.00 78.38  ? 400 GLU   A N   1 
ATOM   790  C  CA  . GLU   A 1 104 ? -35.012 -18.308 10.586 1.00 71.19  ? 400 GLU   A CA  1 
ATOM   791  C  C   . GLU   A 1 104 ? -33.878 -17.413 11.065 1.00 76.70  ? 400 GLU   A C   1 
ATOM   792  O  O   . GLU   A 1 104 ? -33.673 -17.249 12.278 1.00 75.65  ? 400 GLU   A O   1 
ATOM   793  C  CB  . GLU   A 1 104 ? -34.486 -19.706 10.259 1.00 67.27  ? 400 GLU   A CB  1 
ATOM   794  C  CG  . GLU   A 1 104 ? -35.571 -20.758 10.104 1.00 71.46  ? 400 GLU   A CG  1 
ATOM   795  C  CD  . GLU   A 1 104 ? -35.110 -21.969 9.311  1.00 80.79  ? 400 GLU   A CD  1 
ATOM   796  O  OE1 . GLU   A 1 104 ? -35.952 -22.860 9.062  1.00 76.81  ? 400 GLU   A OE1 1 
ATOM   797  O  OE2 . GLU   A 1 104 ? -33.915 -22.026 8.937  1.00 81.79  ? 400 GLU   A OE2 1 
ATOM   798  N  N   . LEU   A 1 105 ? -33.126 -16.836 10.125 1.00 70.62  ? 401 LEU   A N   1 
ATOM   799  C  CA  . LEU   A 1 105 ? -32.038 -15.932 10.487 1.00 71.43  ? 401 LEU   A CA  1 
ATOM   800  C  C   . LEU   A 1 105 ? -32.566 -14.713 11.235 1.00 66.07  ? 401 LEU   A C   1 
ATOM   801  O  O   . LEU   A 1 105 ? -32.015 -14.321 12.271 1.00 59.54  ? 401 LEU   A O   1 
ATOM   802  C  CB  . LEU   A 1 105 ? -31.266 -15.512 9.234  1.00 61.64  ? 401 LEU   A CB  1 
ATOM   803  C  CG  . LEU   A 1 105 ? -29.968 -14.726 9.450  1.00 60.41  ? 401 LEU   A CG  1 
ATOM   804  C  CD1 . LEU   A 1 105 ? -28.789 -15.651 9.708  1.00 56.75  ? 401 LEU   A CD1 1 
ATOM   805  C  CD2 . LEU   A 1 105 ? -29.704 -13.832 8.249  1.00 64.49  ? 401 LEU   A CD2 1 
ATOM   806  N  N   . ILE   A 1 106 ? -33.658 -14.121 10.740 1.00 60.50  ? 402 ILE   A N   1 
ATOM   807  C  CA  . ILE   A 1 106 ? -34.212 -12.915 11.356 1.00 58.73  ? 402 ILE   A CA  1 
ATOM   808  C  C   . ILE   A 1 106 ? -34.776 -13.234 12.743 1.00 64.72  ? 402 ILE   A C   1 
ATOM   809  O  O   . ILE   A 1 106 ? -34.574 -12.474 13.703 1.00 63.57  ? 402 ILE   A O   1 
ATOM   810  C  CB  . ILE   A 1 106 ? -35.260 -12.275 10.412 1.00 58.16  ? 402 ILE   A CB  1 
ATOM   811  C  CG1 . ILE   A 1 106 ? -34.624 -11.930 9.052  1.00 46.53  ? 402 ILE   A CG1 1 
ATOM   812  C  CG2 . ILE   A 1 106 ? -35.844 -11.008 11.039 1.00 65.27  ? 402 ILE   A CG2 1 
ATOM   813  C  CD1 . ILE   A 1 106 ? -35.635 -11.733 7.855  1.00 45.29  ? 402 ILE   A CD1 1 
ATOM   814  N  N   . TYR   A 1 107 ? -35.451 -14.381 12.883 1.00 63.79  ? 403 TYR   A N   1 
ATOM   815  C  CA  . TYR   A 1 107 ? -35.930 -14.815 14.196 1.00 70.62  ? 403 TYR   A CA  1 
ATOM   816  C  C   . TYR   A 1 107 ? -34.772 -15.021 15.170 1.00 72.55  ? 403 TYR   A C   1 
ATOM   817  O  O   . TYR   A 1 107 ? -34.754 -14.453 16.275 1.00 70.32  ? 403 TYR   A O   1 
ATOM   818  C  CB  . TYR   A 1 107 ? -36.741 -16.104 14.048 1.00 73.37  ? 403 TYR   A CB  1 
ATOM   819  C  CG  . TYR   A 1 107 ? -37.127 -16.755 15.348 1.00 81.58  ? 403 TYR   A CG  1 
ATOM   820  C  CD1 . TYR   A 1 107 ? -38.376 -16.540 15.909 1.00 91.81  ? 403 TYR   A CD1 1 
ATOM   821  C  CD2 . TYR   A 1 107 ? -36.242 -17.590 16.022 1.00 82.30  ? 403 TYR   A CD2 1 
ATOM   822  C  CE1 . TYR   A 1 107 ? -38.732 -17.139 17.102 1.00 88.52  ? 403 TYR   A CE1 1 
ATOM   823  C  CE2 . TYR   A 1 107 ? -36.583 -18.182 17.212 1.00 78.51  ? 403 TYR   A CE2 1 
ATOM   824  C  CZ  . TYR   A 1 107 ? -37.830 -17.957 17.752 1.00 83.74  ? 403 TYR   A CZ  1 
ATOM   825  O  OH  . TYR   A 1 107 ? -38.168 -18.555 18.943 1.00 81.55  ? 403 TYR   A OH  1 
ATOM   826  N  N   . GLY   A 1 108 ? -33.806 -15.863 14.787 1.00 63.00  ? 404 GLY   A N   1 
ATOM   827  C  CA  . GLY   A 1 108 ? -32.699 -16.165 15.687 1.00 62.04  ? 404 GLY   A CA  1 
ATOM   828  C  C   . GLY   A 1 108 ? -31.948 -14.926 16.133 1.00 60.79  ? 404 GLY   A C   1 
ATOM   829  O  O   . GLY   A 1 108 ? -31.605 -14.778 17.306 1.00 57.89  ? 404 GLY   A O   1 
ATOM   830  N  N   . ALA   A 1 109 ? -31.694 -14.009 15.197 1.00 64.34  ? 405 ALA   A N   1 
ATOM   831  C  CA  . ALA   A 1 109 ? -30.958 -12.792 15.524 1.00 61.51  ? 405 ALA   A CA  1 
ATOM   832  C  C   . ALA   A 1 109 ? -31.733 -11.931 16.512 1.00 60.43  ? 405 ALA   A C   1 
ATOM   833  O  O   . ALA   A 1 109 ? -31.169 -11.435 17.496 1.00 68.07  ? 405 ALA   A O   1 
ATOM   834  C  CB  . ALA   A 1 109 ? -30.656 -12.010 14.241 1.00 54.39  ? 405 ALA   A CB  1 
ATOM   835  N  N   . LYS   A 1 110 ? -33.034 -11.737 16.265 1.00 52.76  ? 406 LYS   A N   1 
ATOM   836  C  CA  . LYS   A 1 110 ? -33.845 -10.958 17.201 1.00 58.72  ? 406 LYS   A CA  1 
ATOM   837  C  C   . LYS   A 1 110 ? -33.828 -11.582 18.590 1.00 61.16  ? 406 LYS   A C   1 
ATOM   838  O  O   . LYS   A 1 110 ? -33.744 -10.875 19.612 1.00 50.20  ? 406 LYS   A O   1 
ATOM   839  C  CB  . LYS   A 1 110 ? -35.283 -10.850 16.690 1.00 54.81  ? 406 LYS   A CB  1 
ATOM   840  C  CG  . LYS   A 1 110 ? -35.480 -9.801  15.602 1.00 53.30  ? 406 LYS   A CG  1 
ATOM   841  C  CD  . LYS   A 1 110 ? -36.892 -9.823  15.030 1.00 53.73  ? 406 LYS   A CD  1 
ATOM   842  C  CE  . LYS   A 1 110 ? -36.968 -8.885  13.847 1.00 47.98  ? 406 LYS   A CE  1 
ATOM   843  N  NZ  . LYS   A 1 110 ? -38.377 -8.490  13.572 1.00 68.14  ? 406 LYS   A NZ  1 
ATOM   844  N  N   . HIS   A 1 111 ? -33.892 -12.911 18.643 1.00 57.83  ? 407 HIS   A N   1 
ATOM   845  C  CA  . HIS   A 1 111 ? -33.994 -13.621 19.904 1.00 57.21  ? 407 HIS   A CA  1 
ATOM   846  C  C   . HIS   A 1 111 ? -32.662 -13.737 20.622 1.00 59.51  ? 407 HIS   A C   1 
ATOM   847  O  O   . HIS   A 1 111 ? -32.645 -13.786 21.862 1.00 57.47  ? 407 HIS   A O   1 
ATOM   848  C  CB  . HIS   A 1 111 ? -34.625 -14.987 19.665 1.00 56.20  ? 407 HIS   A CB  1 
ATOM   849  C  CG  . HIS   A 1 111 ? -36.115 -14.931 19.641 1.00 64.19  ? 407 HIS   A CG  1 
ATOM   850  N  ND1 . HIS   A 1 111 ? -36.823 -14.487 18.543 1.00 66.41  ? 407 HIS   A ND1 1 
ATOM   851  C  CD2 . HIS   A 1 111 ? -37.031 -15.196 20.600 1.00 59.35  ? 407 HIS   A CD2 1 
ATOM   852  C  CE1 . HIS   A 1 111 ? -38.115 -14.514 18.818 1.00 69.41  ? 407 HIS   A CE1 1 
ATOM   853  N  NE2 . HIS   A 1 111 ? -38.269 -14.948 20.056 1.00 69.53  ? 407 HIS   A NE2 1 
ATOM   854  N  N   . ALA   A 1 112 ? -31.552 -13.725 19.881 1.00 50.09  ? 408 ALA   A N   1 
ATOM   855  C  CA  . ALA   A 1 112 ? -30.249 -13.543 20.506 1.00 57.59  ? 408 ALA   A CA  1 
ATOM   856  C  C   . ALA   A 1 112 ? -30.195 -12.231 21.284 1.00 62.39  ? 408 ALA   A C   1 
ATOM   857  O  O   . ALA   A 1 112 ? -29.715 -12.192 22.425 1.00 61.75  ? 408 ALA   A O   1 
ATOM   858  C  CB  . ALA   A 1 112 ? -29.160 -13.593 19.448 1.00 48.29  ? 408 ALA   A CB  1 
ATOM   859  N  N   . TRP   A 1 113 ? -30.691 -11.142 20.682 1.00 57.43  ? 409 TRP   A N   1 
ATOM   860  C  CA  . TRP   A 1 113 ? -30.817 -9.883  21.421 1.00 59.42  ? 409 TRP   A CA  1 
ATOM   861  C  C   . TRP   A 1 113 ? -31.774 -10.035 22.601 1.00 55.49  ? 409 TRP   A C   1 
ATOM   862  O  O   . TRP   A 1 113 ? -31.443 -9.672  23.735 1.00 59.40  ? 409 TRP   A O   1 
ATOM   863  C  CB  . TRP   A 1 113 ? -31.290 -8.774  20.480 1.00 57.70  ? 409 TRP   A CB  1 
ATOM   864  C  CG  . TRP   A 1 113 ? -31.399 -7.395  21.089 1.00 53.17  ? 409 TRP   A CG  1 
ATOM   865  C  CD1 . TRP   A 1 113 ? -30.927 -6.979  22.310 1.00 56.55  ? 409 TRP   A CD1 1 
ATOM   866  C  CD2 . TRP   A 1 113 ? -32.027 -6.251  20.496 1.00 52.22  ? 409 TRP   A CD2 1 
ATOM   867  N  NE1 . TRP   A 1 113 ? -31.223 -5.648  22.504 1.00 57.12  ? 409 TRP   A NE1 1 
ATOM   868  C  CE2 . TRP   A 1 113 ? -31.894 -5.179  21.404 1.00 50.09  ? 409 TRP   A CE2 1 
ATOM   869  C  CE3 . TRP   A 1 113 ? -32.681 -6.025  19.275 1.00 50.10  ? 409 TRP   A CE3 1 
ATOM   870  C  CZ2 . TRP   A 1 113 ? -32.403 -3.903  21.135 1.00 45.35  ? 409 TRP   A CZ2 1 
ATOM   871  C  CZ3 . TRP   A 1 113 ? -33.184 -4.764  19.016 1.00 62.76  ? 409 TRP   A CZ3 1 
ATOM   872  C  CH2 . TRP   A 1 113 ? -33.046 -3.720  19.943 1.00 56.45  ? 409 TRP   A CH2 1 
ATOM   873  N  N   . ARG   A 1 114 ? -32.977 -10.560 22.343 1.00 50.02  ? 410 ARG   A N   1 
ATOM   874  C  CA  . ARG   A 1 114 ? -33.961 -10.786 23.401 1.00 61.32  ? 410 ARG   A CA  1 
ATOM   875  C  C   . ARG   A 1 114 ? -33.356 -11.509 24.596 1.00 60.16  ? 410 ARG   A C   1 
ATOM   876  O  O   . ARG   A 1 114 ? -33.657 -11.186 25.758 1.00 57.42  ? 410 ARG   A O   1 
ATOM   877  C  CB  . ARG   A 1 114 ? -35.128 -11.591 22.843 1.00 60.75  ? 410 ARG   A CB  1 
ATOM   878  C  CG  . ARG   A 1 114 ? -36.355 -11.592 23.708 1.00 59.69  ? 410 ARG   A CG  1 
ATOM   879  C  CD  . ARG   A 1 114 ? -37.417 -12.484 23.075 1.00 69.25  ? 410 ARG   A CD  1 
ATOM   880  N  NE  . ARG   A 1 114 ? -38.697 -12.339 23.762 1.00 73.18  ? 410 ARG   A NE  1 
ATOM   881  C  CZ  . ARG   A 1 114 ? -39.801 -12.985 23.416 1.00 69.94  ? 410 ARG   A CZ  1 
ATOM   882  N  NH1 . ARG   A 1 114 ? -40.925 -12.797 24.090 1.00 66.64  ? 410 ARG   A NH1 1 
ATOM   883  N  NH2 . ARG   A 1 114 ? -39.776 -13.814 22.384 1.00 77.87  ? 410 ARG   A NH2 1 
ATOM   884  N  N   . ASN   A 1 115 ? -32.485 -12.474 24.330 1.00 49.38  ? 411 ASN   A N   1 
ATOM   885  C  CA  . ASN   A 1 115 ? -31.870 -13.277 25.376 1.00 60.67  ? 411 ASN   A CA  1 
ATOM   886  C  C   . ASN   A 1 115 ? -30.632 -12.630 26.001 1.00 54.70  ? 411 ASN   A C   1 
ATOM   887  O  O   . ASN   A 1 115 ? -30.028 -13.223 26.903 1.00 49.95  ? 411 ASN   A O   1 
ATOM   888  C  CB  . ASN   A 1 115 ? -31.522 -14.651 24.800 1.00 45.68  ? 411 ASN   A CB  1 
ATOM   889  C  CG  . ASN   A 1 115 ? -32.757 -15.448 24.444 1.00 57.78  ? 411 ASN   A CG  1 
ATOM   890  O  OD1 . ASN   A 1 115 ? -33.839 -15.206 24.983 1.00 72.17  ? 411 ASN   A OD1 1 
ATOM   891  N  ND2 . ASN   A 1 115 ? -32.609 -16.401 23.534 1.00 52.14  ? 411 ASN   A ND2 1 
ATOM   892  N  N   . ALA   A 1 116 ? -30.232 -11.443 25.550 1.00 53.70  ? 412 ALA   A N   1 
ATOM   893  C  CA  . ALA   A 1 116 ? -28.977 -10.839 25.987 1.00 49.42  ? 412 ALA   A CA  1 
ATOM   894  C  C   . ALA   A 1 116 ? -29.192 -10.272 27.384 1.00 52.30  ? 412 ALA   A C   1 
ATOM   895  O  O   . ALA   A 1 116 ? -29.700 -9.161  27.557 1.00 52.50  ? 412 ALA   A O   1 
ATOM   896  C  CB  . ALA   A 1 116 ? -28.522 -9.768  25.002 1.00 49.18  ? 412 ALA   A CB  1 
ATOM   897  N  N   . SER   A 1 117 ? -28.813 -11.044 28.394 1.00 52.53  ? 413 SER   A N   1 
ATOM   898  C  CA  . SER   A 1 117 ? -29.203 -10.708 29.753 1.00 52.70  ? 413 SER   A CA  1 
ATOM   899  C  C   . SER   A 1 117 ? -28.513 -9.443  30.257 1.00 50.78  ? 413 SER   A C   1 
ATOM   900  O  O   . SER   A 1 117 ? -29.031 -8.799  31.177 1.00 58.36  ? 413 SER   A O   1 
ATOM   901  C  CB  . SER   A 1 117 ? -28.935 -11.906 30.666 1.00 57.45  ? 413 SER   A CB  1 
ATOM   902  O  OG  . SER   A 1 117 ? -27.556 -12.223 30.741 1.00 56.78  ? 413 SER   A OG  1 
ATOM   903  N  N   . ARG   A 1 118 ? -27.390 -9.046  29.642 1.00 40.54  ? 414 ARG   A N   1 
ATOM   904  C  CA  . ARG   A 1 118 ? -26.674 -7.838  30.026 1.00 46.42  ? 414 ARG   A CA  1 
ATOM   905  C  C   . ARG   A 1 118 ? -27.164 -6.595  29.298 1.00 54.44  ? 414 ARG   A C   1 
ATOM   906  O  O   . ARG   A 1 118 ? -26.606 -5.520  29.521 1.00 41.11  ? 414 ARG   A O   1 
ATOM   907  C  CB  . ARG   A 1 118 ? -25.174 -8.007  29.772 1.00 49.27  ? 414 ARG   A CB  1 
ATOM   908  C  CG  . ARG   A 1 118 ? -24.553 -9.149  30.562 1.00 48.74  ? 414 ARG   A CG  1 
ATOM   909  C  CD  . ARG   A 1 118 ? -23.044 -9.173  30.400 1.00 53.78  ? 414 ARG   A CD  1 
ATOM   910  N  NE  . ARG   A 1 118 ? -22.426 -9.898  31.513 1.00 48.21  ? 414 ARG   A NE  1 
ATOM   911  C  CZ  . ARG   A 1 118 ? -21.139 -10.218 31.585 1.00 56.49  ? 414 ARG   A CZ  1 
ATOM   912  N  NH1 . ARG   A 1 118 ? -20.316 -9.883  30.600 1.00 56.25  ? 414 ARG   A NH1 1 
ATOM   913  N  NH2 . ARG   A 1 118 ? -20.680 -10.872 32.642 1.00 61.23  ? 414 ARG   A NH2 1 
ATOM   914  N  N   . CYS   A 1 119 ? -28.173 -6.709  28.427 1.00 44.28  ? 415 CYS   A N   1 
ATOM   915  C  CA  . CYS   A 1 119 ? -28.649 -5.576  27.637 1.00 48.83  ? 415 CYS   A CA  1 
ATOM   916  C  C   . CYS   A 1 119 ? -29.896 -4.981  28.267 1.00 43.61  ? 415 CYS   A C   1 
ATOM   917  O  O   . CYS   A 1 119 ? -30.929 -5.649  28.366 1.00 54.03  ? 415 CYS   A O   1 
ATOM   918  C  CB  . CYS   A 1 119 ? -28.960 -5.968  26.193 1.00 45.68  ? 415 CYS   A CB  1 
ATOM   919  S  SG  . CYS   A 1 119 ? -29.723 -4.548  25.316 1.00 46.68  ? 415 CYS   A SG  1 
ATOM   920  N  N   . VAL   A 1 120 ? -29.804 -3.708  28.647 1.00 44.18  ? 416 VAL   A N   1 
ATOM   921  C  CA  . VAL   A 1 120 ? -30.937 -3.003  29.235 1.00 46.30  ? 416 VAL   A CA  1 
ATOM   922  C  C   . VAL   A 1 120 ? -31.915 -2.492  28.182 1.00 52.32  ? 416 VAL   A C   1 
ATOM   923  O  O   . VAL   A 1 120 ? -33.055 -2.147  28.522 1.00 53.70  ? 416 VAL   A O   1 
ATOM   924  C  CB  . VAL   A 1 120 ? -30.433 -1.831  30.100 1.00 46.39  ? 416 VAL   A CB  1 
ATOM   925  C  CG1 . VAL   A 1 120 ? -30.051 -0.626  29.209 1.00 48.29  ? 416 VAL   A CG1 1 
ATOM   926  C  CG2 . VAL   A 1 120 ? -31.483 -1.439  31.152 1.00 48.76  ? 416 VAL   A CG2 1 
ATOM   927  N  N   . GLY   A 1 121 ? -31.512 -2.451  26.908 1.00 60.53  ? 417 GLY   A N   1 
ATOM   928  C  CA  . GLY   A 1 121 ? -32.322 -1.907  25.829 1.00 44.17  ? 417 GLY   A CA  1 
ATOM   929  C  C   . GLY   A 1 121 ? -33.349 -2.842  25.234 1.00 49.41  ? 417 GLY   A C   1 
ATOM   930  O  O   . GLY   A 1 121 ? -34.030 -2.458  24.280 1.00 59.91  ? 417 GLY   A O   1 
ATOM   931  N  N   . ARG   A 1 122 ? -33.537 -4.044  25.788 1.00 45.93  ? 418 ARG   A N   1 
ATOM   932  C  CA  . ARG   A 1 122 ? -34.178 -5.117  25.026 1.00 49.51  ? 418 ARG   A CA  1 
ATOM   933  C  C   . ARG   A 1 122 ? -35.653 -4.884  24.739 1.00 58.96  ? 418 ARG   A C   1 
ATOM   934  O  O   . ARG   A 1 122 ? -36.221 -5.640  23.941 1.00 55.97  ? 418 ARG   A O   1 
ATOM   935  C  CB  . ARG   A 1 122 ? -34.013 -6.452  25.743 1.00 42.75  ? 418 ARG   A CB  1 
ATOM   936  C  CG  . ARG   A 1 122 ? -32.601 -6.988  25.681 1.00 50.77  ? 418 ARG   A CG  1 
ATOM   937  C  CD  . ARG   A 1 122 ? -32.518 -8.291  26.419 1.00 54.64  ? 418 ARG   A CD  1 
ATOM   938  N  NE  . ARG   A 1 122 ? -32.331 -8.101  27.851 1.00 57.07  ? 418 ARG   A NE  1 
ATOM   939  C  CZ  . ARG   A 1 122 ? -32.517 -9.063  28.744 1.00 53.94  ? 418 ARG   A CZ  1 
ATOM   940  N  NH1 . ARG   A 1 122 ? -32.902 -10.272 28.334 1.00 39.16  ? 418 ARG   A NH1 1 
ATOM   941  N  NH2 . ARG   A 1 122 ? -32.315 -8.826  30.038 1.00 59.92  ? 418 ARG   A NH2 1 
ATOM   942  N  N   . ILE   A 1 123 ? -36.276 -3.852  25.319 1.00 59.84  ? 419 ILE   A N   1 
ATOM   943  C  CA  . ILE   A 1 123 ? -37.676 -3.576  25.021 1.00 57.43  ? 419 ILE   A CA  1 
ATOM   944  C  C   . ILE   A 1 123 ? -37.903 -3.388  23.514 1.00 62.54  ? 419 ILE   A C   1 
ATOM   945  O  O   . ILE   A 1 123 ? -39.044 -3.442  23.044 1.00 57.12  ? 419 ILE   A O   1 
ATOM   946  C  CB  . ILE   A 1 123 ? -38.147 -2.347  25.832 1.00 61.68  ? 419 ILE   A CB  1 
ATOM   947  C  CG1 . ILE   A 1 123 ? -39.675 -2.314  25.926 1.00 68.42  ? 419 ILE   A CG1 1 
ATOM   948  C  CG2 . ILE   A 1 123 ? -37.594 -1.054  25.230 1.00 59.59  ? 419 ILE   A CG2 1 
ATOM   949  C  CD1 . ILE   A 1 123 ? -40.286 -0.922  25.761 1.00 72.13  ? 419 ILE   A CD1 1 
ATOM   950  N  N   . GLN   A 1 124 ? -36.832 -3.196  22.746 1.00 57.60  ? 420 GLN   A N   1 
ATOM   951  C  CA  . GLN   A 1 124 ? -36.888 -2.996  21.308 1.00 71.54  ? 420 GLN   A CA  1 
ATOM   952  C  C   . GLN   A 1 124 ? -36.535 -4.252  20.519 1.00 68.19  ? 420 GLN   A C   1 
ATOM   953  O  O   . GLN   A 1 124 ? -36.413 -4.176  19.291 1.00 67.79  ? 420 GLN   A O   1 
ATOM   954  C  CB  . GLN   A 1 124 ? -35.941 -1.859  20.914 1.00 84.55  ? 420 GLN   A CB  1 
ATOM   955  C  CG  . GLN   A 1 124 ? -36.443 -0.454  21.221 1.00 91.94  ? 420 GLN   A CG  1 
ATOM   956  C  CD  . GLN   A 1 124 ? -37.328 0.106   20.118 1.00 101.14 ? 420 GLN   A CD  1 
ATOM   957  O  OE1 . GLN   A 1 124 ? -37.848 -0.633  19.282 1.00 103.48 ? 420 GLN   A OE1 1 
ATOM   958  N  NE2 . GLN   A 1 124 ? -37.504 1.421   20.114 1.00 104.99 ? 420 GLN   A NE2 1 
ATOM   959  N  N   . TRP   A 1 125 ? -36.392 -5.403  21.188 1.00 65.19  ? 421 TRP   A N   1 
ATOM   960  C  CA  . TRP   A 1 125 ? -35.763 -6.568  20.564 1.00 62.19  ? 421 TRP   A CA  1 
ATOM   961  C  C   . TRP   A 1 125 ? -36.480 -6.986  19.285 1.00 66.04  ? 421 TRP   A C   1 
ATOM   962  O  O   . TRP   A 1 125 ? -35.838 -7.395  18.312 1.00 72.51  ? 421 TRP   A O   1 
ATOM   963  C  CB  . TRP   A 1 125 ? -35.709 -7.738  21.549 1.00 49.26  ? 421 TRP   A CB  1 
ATOM   964  C  CG  . TRP   A 1 125 ? -37.033 -8.376  21.770 1.00 60.40  ? 421 TRP   A CG  1 
ATOM   965  C  CD1 . TRP   A 1 125 ? -37.933 -8.082  22.760 1.00 64.43  ? 421 TRP   A CD1 1 
ATOM   966  C  CD2 . TRP   A 1 125 ? -37.619 -9.423  20.990 1.00 64.83  ? 421 TRP   A CD2 1 
ATOM   967  N  NE1 . TRP   A 1 125 ? -39.044 -8.884  22.638 1.00 68.90  ? 421 TRP   A NE1 1 
ATOM   968  C  CE2 . TRP   A 1 125 ? -38.875 -9.715  21.559 1.00 66.71  ? 421 TRP   A CE2 1 
ATOM   969  C  CE3 . TRP   A 1 125 ? -37.206 -10.141 19.865 1.00 62.87  ? 421 TRP   A CE3 1 
ATOM   970  C  CZ2 . TRP   A 1 125 ? -39.717 -10.695 21.043 1.00 64.15  ? 421 TRP   A CZ2 1 
ATOM   971  C  CZ3 . TRP   A 1 125 ? -38.051 -11.119 19.353 1.00 67.40  ? 421 TRP   A CZ3 1 
ATOM   972  C  CH2 . TRP   A 1 125 ? -39.290 -11.380 19.941 1.00 69.30  ? 421 TRP   A CH2 1 
ATOM   973  N  N   . SER   A 1 126 ? -37.811 -6.887  19.261 1.00 73.74  ? 422 SER   A N   1 
ATOM   974  C  CA  . SER   A 1 126 ? -38.554 -7.284  18.069 1.00 73.39  ? 422 SER   A CA  1 
ATOM   975  C  C   . SER   A 1 126 ? -38.410 -6.278  16.930 1.00 77.14  ? 422 SER   A C   1 
ATOM   976  O  O   . SER   A 1 126 ? -38.709 -6.618  15.782 1.00 76.74  ? 422 SER   A O   1 
ATOM   977  C  CB  . SER   A 1 126 ? -40.035 -7.484  18.408 1.00 72.28  ? 422 SER   A CB  1 
ATOM   978  O  OG  . SER   A 1 126 ? -40.720 -6.248  18.574 1.00 68.36  ? 422 SER   A OG  1 
ATOM   979  N  N   . LYS   A 1 127 ? -37.958 -5.054  17.215 1.00 79.48  ? 423 LYS   A N   1 
ATOM   980  C  CA  . LYS   A 1 127 ? -37.725 -4.046  16.180 1.00 80.99  ? 423 LYS   A CA  1 
ATOM   981  C  C   . LYS   A 1 127 ? -36.225 -4.009  15.892 1.00 77.12  ? 423 LYS   A C   1 
ATOM   982  O  O   . LYS   A 1 127 ? -35.483 -3.140  16.359 1.00 76.83  ? 423 LYS   A O   1 
ATOM   983  C  CB  . LYS   A 1 127 ? -38.266 -2.687  16.612 1.00 82.80  ? 423 LYS   A CB  1 
ATOM   984  C  CG  . LYS   A 1 127 ? -39.778 -2.662  16.821 1.00 90.10  ? 423 LYS   A CG  1 
ATOM   985  C  CD  . LYS   A 1 127 ? -40.367 -1.263  16.623 1.00 97.23  ? 423 LYS   A CD  1 
ATOM   986  C  CE  . LYS   A 1 127 ? -40.294 -0.815  15.159 1.00 94.44  ? 423 LYS   A CE  1 
ATOM   987  N  NZ  . LYS   A 1 127 ? -39.286 0.272   14.954 1.00 82.46  ? 423 LYS   A NZ  1 
ATOM   988  N  N   . LEU   A 1 128 ? -35.784 -4.991  15.108 1.00 65.64  ? 424 LEU   A N   1 
ATOM   989  C  CA  . LEU   A 1 128 ? -34.393 -5.141  14.704 1.00 59.99  ? 424 LEU   A CA  1 
ATOM   990  C  C   . LEU   A 1 128 ? -34.364 -5.415  13.210 1.00 62.23  ? 424 LEU   A C   1 
ATOM   991  O  O   . LEU   A 1 128 ? -35.092 -6.287  12.726 1.00 59.66  ? 424 LEU   A O   1 
ATOM   992  C  CB  . LEU   A 1 128 ? -33.715 -6.290  15.458 1.00 54.25  ? 424 LEU   A CB  1 
ATOM   993  C  CG  . LEU   A 1 128 ? -32.293 -6.697  15.046 1.00 50.92  ? 424 LEU   A CG  1 
ATOM   994  C  CD1 . LEU   A 1 128 ? -31.313 -5.603  15.453 1.00 45.45  ? 424 LEU   A CD1 1 
ATOM   995  C  CD2 . LEU   A 1 128 ? -31.893 -8.007  15.751 1.00 52.76  ? 424 LEU   A CD2 1 
ATOM   996  N  N   . GLN   A 1 129 ? -33.529 -4.675  12.487 1.00 69.50  ? 425 GLN   A N   1 
ATOM   997  C  CA  . GLN   A 1 129 ? -33.396 -4.813  11.044 1.00 66.68  ? 425 GLN   A CA  1 
ATOM   998  C  C   . GLN   A 1 129 ? -32.219 -5.740  10.771 1.00 64.65  ? 425 GLN   A C   1 
ATOM   999  O  O   . GLN   A 1 129 ? -31.088 -5.452  11.180 1.00 57.56  ? 425 GLN   A O   1 
ATOM   1000 C  CB  . GLN   A 1 129 ? -33.196 -3.444  10.393 1.00 70.68  ? 425 GLN   A CB  1 
ATOM   1001 C  CG  . GLN   A 1 129 ? -33.091 -3.461  8.879  1.00 65.34  ? 425 GLN   A CG  1 
ATOM   1002 C  CD  . GLN   A 1 129 ? -34.229 -4.220  8.226  1.00 69.79  ? 425 GLN   A CD  1 
ATOM   1003 O  OE1 . GLN   A 1 129 ? -35.402 -4.010  8.547  1.00 70.36  ? 425 GLN   A OE1 1 
ATOM   1004 N  NE2 . GLN   A 1 129 ? -33.884 -5.129  7.323  1.00 70.44  ? 425 GLN   A NE2 1 
ATOM   1005 N  N   . VAL   A 1 130 ? -32.485 -6.863  10.119 1.00 61.93  ? 426 VAL   A N   1 
ATOM   1006 C  CA  . VAL   A 1 130 ? -31.481 -7.902  9.928  1.00 61.36  ? 426 VAL   A CA  1 
ATOM   1007 C  C   . VAL   A 1 130 ? -30.983 -7.820  8.492  1.00 61.44  ? 426 VAL   A C   1 
ATOM   1008 O  O   . VAL   A 1 130 ? -31.767 -7.967  7.550  1.00 57.26  ? 426 VAL   A O   1 
ATOM   1009 C  CB  . VAL   A 1 130 ? -32.053 -9.291  10.263 1.00 61.49  ? 426 VAL   A CB  1 
ATOM   1010 C  CG1 . VAL   A 1 130 ? -30.972 -10.368 10.202 1.00 53.20  ? 426 VAL   A CG1 1 
ATOM   1011 C  CG2 . VAL   A 1 130 ? -32.662 -9.272  11.647 1.00 49.25  ? 426 VAL   A CG2 1 
ATOM   1012 N  N   . PHE   A 1 131 ? -29.692 -7.537  8.318  1.00 57.51  ? 427 PHE   A N   1 
ATOM   1013 C  CA  . PHE   A 1 131 ? -29.077 -7.505  6.995  1.00 57.52  ? 427 PHE   A CA  1 
ATOM   1014 C  C   . PHE   A 1 131 ? -28.320 -8.801  6.776  1.00 59.83  ? 427 PHE   A C   1 
ATOM   1015 O  O   . PHE   A 1 131 ? -27.405 -9.133  7.540  1.00 49.65  ? 427 PHE   A O   1 
ATOM   1016 C  CB  . PHE   A 1 131 ? -28.139 -6.316  6.813  1.00 48.95  ? 427 PHE   A CB  1 
ATOM   1017 C  CG  . PHE   A 1 131 ? -28.843 -4.997  6.790  1.00 52.84  ? 427 PHE   A CG  1 
ATOM   1018 C  CD1 . PHE   A 1 131 ? -29.644 -4.631  5.712  1.00 50.61  ? 427 PHE   A CD1 1 
ATOM   1019 C  CD2 . PHE   A 1 131 ? -28.701 -4.114  7.844  1.00 52.80  ? 427 PHE   A CD2 1 
ATOM   1020 C  CE1 . PHE   A 1 131 ? -30.289 -3.412  5.706  1.00 53.09  ? 427 PHE   A CE1 1 
ATOM   1021 C  CE2 . PHE   A 1 131 ? -29.341 -2.897  7.839  1.00 59.90  ? 427 PHE   A CE2 1 
ATOM   1022 C  CZ  . PHE   A 1 131 ? -30.134 -2.539  6.792  1.00 53.99  ? 427 PHE   A CZ  1 
ATOM   1023 N  N   . ASP   A 1 132 ? -28.705 -9.515  5.726  1.00 55.97  ? 428 ASP   A N   1 
ATOM   1024 C  CA  . ASP   A 1 132 ? -28.163 -10.829 5.415  1.00 50.77  ? 428 ASP   A CA  1 
ATOM   1025 C  C   . ASP   A 1 132 ? -26.946 -10.627 4.530  1.00 50.26  ? 428 ASP   A C   1 
ATOM   1026 O  O   . ASP   A 1 132 ? -27.068 -10.427 3.317  1.00 52.75  ? 428 ASP   A O   1 
ATOM   1027 C  CB  . ASP   A 1 132 ? -29.225 -11.687 4.741  1.00 49.44  ? 428 ASP   A CB  1 
ATOM   1028 C  CG  . ASP   A 1 132 ? -28.731 -13.091 4.427  1.00 59.03  ? 428 ASP   A CG  1 
ATOM   1029 O  OD1 . ASP   A 1 132 ? -29.562 -13.933 4.025  1.00 56.69  ? 428 ASP   A OD1 1 
ATOM   1030 O  OD2 . ASP   A 1 132 ? -27.517 -13.356 4.588  1.00 60.27  ? 428 ASP   A OD2 1 
ATOM   1031 N  N   . ALA   A 1 133 ? -25.766 -10.682 5.131  1.00 51.52  ? 429 ALA   A N   1 
ATOM   1032 C  CA  . ALA   A 1 133 ? -24.518 -10.634 4.387  1.00 56.59  ? 429 ALA   A CA  1 
ATOM   1033 C  C   . ALA   A 1 133 ? -23.928 -12.017 4.189  1.00 52.82  ? 429 ALA   A C   1 
ATOM   1034 O  O   . ALA   A 1 133 ? -22.712 -12.150 4.009  1.00 55.43  ? 429 ALA   A O   1 
ATOM   1035 C  CB  . ALA   A 1 133 ? -23.512 -9.730  5.101  1.00 53.74  ? 429 ALA   A CB  1 
ATOM   1036 N  N   . ARG   A 1 134 ? -24.753 -13.059 4.238  1.00 44.92  ? 430 ARG   A N   1 
ATOM   1037 C  CA  . ARG   A 1 134 ? -24.170 -14.384 4.092  1.00 53.78  ? 430 ARG   A CA  1 
ATOM   1038 C  C   . ARG   A 1 134 ? -23.686 -14.692 2.668  1.00 56.54  ? 430 ARG   A C   1 
ATOM   1039 O  O   . ARG   A 1 134 ? -23.039 -15.727 2.485  1.00 57.44  ? 430 ARG   A O   1 
ATOM   1040 C  CB  . ARG   A 1 134 ? -25.168 -15.432 4.551  1.00 48.04  ? 430 ARG   A CB  1 
ATOM   1041 C  CG  . ARG   A 1 134 ? -25.262 -15.545 6.055  1.00 53.39  ? 430 ARG   A CG  1 
ATOM   1042 C  CD  . ARG   A 1 134 ? -26.306 -16.560 6.454  1.00 57.51  ? 430 ARG   A CD  1 
ATOM   1043 N  NE  . ARG   A 1 134 ? -27.623 -16.191 5.954  1.00 61.45  ? 430 ARG   A NE  1 
ATOM   1044 C  CZ  . ARG   A 1 134 ? -28.649 -17.033 5.872  1.00 62.14  ? 430 ARG   A CZ  1 
ATOM   1045 N  NH1 . ARG   A 1 134 ? -28.502 -18.291 6.268  1.00 65.37  ? 430 ARG   A NH1 1 
ATOM   1046 N  NH2 . ARG   A 1 134 ? -29.815 -16.619 5.384  1.00 56.96  ? 430 ARG   A NH2 1 
ATOM   1047 N  N   . ASP   A 1 135 ? -23.961 -13.836 1.669  1.00 52.08  ? 431 ASP   A N   1 
ATOM   1048 C  CA  . ASP   A 1 135 ? -23.417 -14.011 0.318  1.00 64.47  ? 431 ASP   A CA  1 
ATOM   1049 C  C   . ASP   A 1 135 ? -22.088 -13.287 0.118  1.00 66.73  ? 431 ASP   A C   1 
ATOM   1050 O  O   . ASP   A 1 135 ? -21.555 -13.284 -1.005 1.00 59.75  ? 431 ASP   A O   1 
ATOM   1051 C  CB  . ASP   A 1 135 ? -24.433 -13.519 -0.735 1.00 64.32  ? 431 ASP   A CB  1 
ATOM   1052 C  CG  . ASP   A 1 135 ? -24.880 -12.086 -0.479 1.00 75.54  ? 431 ASP   A CG  1 
ATOM   1053 O  OD1 . ASP   A 1 135 ? -24.784 -11.256 -1.399 1.00 77.33  ? 431 ASP   A OD1 1 
ATOM   1054 O  OD2 . ASP   A 1 135 ? -25.303 -11.787 0.671  1.00 74.51  ? 431 ASP   A OD2 1 
ATOM   1055 N  N   . CYS   A 1 136 ? -21.564 -12.672 1.178  1.00 56.00  ? 432 CYS   A N   1 
ATOM   1056 C  CA  . CYS   A 1 136 ? -20.332 -11.897 1.140  1.00 56.73  ? 432 CYS   A CA  1 
ATOM   1057 C  C   . CYS   A 1 136 ? -19.125 -12.824 1.057  1.00 59.14  ? 432 CYS   A C   1 
ATOM   1058 O  O   . CYS   A 1 136 ? -19.101 -13.903 1.649  1.00 70.41  ? 432 CYS   A O   1 
ATOM   1059 C  CB  . CYS   A 1 136 ? -20.234 -11.007 2.396  1.00 50.93  ? 432 CYS   A CB  1 
ATOM   1060 S  SG  . CYS   A 1 136 ? -18.857 -9.811  2.379  1.00 58.44  ? 432 CYS   A SG  1 
ATOM   1061 N  N   . THR   A 1 137 ? -18.115 -12.399 0.296  1.00 69.52  ? 433 THR   A N   1 
ATOM   1062 C  CA  . THR   A 1 137 ? -16.936 -13.234 0.090  1.00 48.81  ? 433 THR   A CA  1 
ATOM   1063 C  C   . THR   A 1 137 ? -15.599 -12.526 0.271  1.00 55.19  ? 433 THR   A C   1 
ATOM   1064 O  O   . THR   A 1 137 ? -14.572 -13.209 0.348  1.00 62.08  ? 433 THR   A O   1 
ATOM   1065 C  CB  . THR   A 1 137 ? -16.970 -13.849 -1.311 1.00 58.93  ? 433 THR   A CB  1 
ATOM   1066 O  OG1 . THR   A 1 137 ? -16.897 -12.803 -2.297 1.00 60.10  ? 433 THR   A OG1 1 
ATOM   1067 C  CG2 . THR   A 1 137 ? -18.249 -14.645 -1.505 1.00 65.46  ? 433 THR   A CG2 1 
ATOM   1068 N  N   . THR   A 1 138 ? -15.563 -11.199 0.328  1.00 64.56  ? 434 THR   A N   1 
ATOM   1069 C  CA  . THR   A 1 138 ? -14.323 -10.440 0.356  1.00 65.42  ? 434 THR   A CA  1 
ATOM   1070 C  C   . THR   A 1 138 ? -14.422 -9.376  1.431  1.00 62.20  ? 434 THR   A C   1 
ATOM   1071 O  O   . THR   A 1 138 ? -15.516 -9.013  1.876  1.00 69.84  ? 434 THR   A O   1 
ATOM   1072 C  CB  . THR   A 1 138 ? -14.032 -9.764  -1.000 1.00 71.34  ? 434 THR   A CB  1 
ATOM   1073 O  OG1 . THR   A 1 138 ? -15.159 -8.966  -1.384 1.00 73.09  ? 434 THR   A OG1 1 
ATOM   1074 C  CG2 . THR   A 1 138 ? -13.762 -10.801 -2.076 1.00 73.08  ? 434 THR   A CG2 1 
ATOM   1075 N  N   . ALA   A 1 139 ? -13.257 -8.889  1.858  1.00 71.49  ? 435 ALA   A N   1 
ATOM   1076 C  CA  . ALA   A 1 139 ? -13.242 -7.811  2.838  1.00 62.59  ? 435 ALA   A CA  1 
ATOM   1077 C  C   . ALA   A 1 139 ? -13.882 -6.552  2.264  1.00 67.99  ? 435 ALA   A C   1 
ATOM   1078 O  O   . ALA   A 1 139 ? -14.560 -5.807  2.980  1.00 69.84  ? 435 ALA   A O   1 
ATOM   1079 C  CB  . ALA   A 1 139 ? -11.811 -7.540  3.293  1.00 68.79  ? 435 ALA   A CB  1 
ATOM   1080 N  N   . HIS   A 1 140 ? -13.689 -6.309  0.965  1.00 64.54  ? 436 HIS   A N   1 
ATOM   1081 C  CA  . HIS   A 1 140 ? -14.367 -5.203  0.292  1.00 65.13  ? 436 HIS   A CA  1 
ATOM   1082 C  C   . HIS   A 1 140 ? -15.884 -5.339  0.376  1.00 58.40  ? 436 HIS   A C   1 
ATOM   1083 O  O   . HIS   A 1 140 ? -16.592 -4.348  0.586  1.00 53.49  ? 436 HIS   A O   1 
ATOM   1084 C  CB  . HIS   A 1 140 ? -13.925 -5.125  -1.167 1.00 66.50  ? 436 HIS   A CB  1 
ATOM   1085 C  CG  . HIS   A 1 140 ? -12.619 -4.423  -1.369 1.00 73.18  ? 436 HIS   A CG  1 
ATOM   1086 N  ND1 . HIS   A 1 140 ? -11.407 -4.988  -1.031 1.00 78.74  ? 436 HIS   A ND1 1 
ATOM   1087 C  CD2 . HIS   A 1 140 ? -12.336 -3.197  -1.870 1.00 69.67  ? 436 HIS   A CD2 1 
ATOM   1088 C  CE1 . HIS   A 1 140 ? -10.433 -4.145  -1.330 1.00 81.94  ? 436 HIS   A CE1 1 
ATOM   1089 N  NE2 . HIS   A 1 140 ? -10.970 -3.051  -1.840 1.00 75.40  ? 436 HIS   A NE2 1 
ATOM   1090 N  N   . GLY   A 1 141 ? -16.405 -6.553  0.187  1.00 60.89  ? 437 GLY   A N   1 
ATOM   1091 C  CA  . GLY   A 1 141 ? -17.828 -6.771  0.384  1.00 62.75  ? 437 GLY   A CA  1 
ATOM   1092 C  C   . GLY   A 1 141 ? -18.269 -6.514  1.813  1.00 66.50  ? 437 GLY   A C   1 
ATOM   1093 O  O   . GLY   A 1 141 ? -19.333 -5.935  2.048  1.00 67.99  ? 437 GLY   A O   1 
ATOM   1094 N  N   . MET   A 1 142 ? -17.474 -6.962  2.792  1.00 65.41  ? 438 MET   A N   1 
ATOM   1095 C  CA  . MET   A 1 142 ? -17.787 -6.631  4.179  1.00 57.83  ? 438 MET   A CA  1 
ATOM   1096 C  C   . MET   A 1 142 ? -17.844 -5.123  4.359  1.00 51.70  ? 438 MET   A C   1 
ATOM   1097 O  O   . MET   A 1 142 ? -18.824 -4.584  4.887  1.00 57.68  ? 438 MET   A O   1 
ATOM   1098 C  CB  . MET   A 1 142 ? -16.761 -7.251  5.135  1.00 53.69  ? 438 MET   A CB  1 
ATOM   1099 C  CG  . MET   A 1 142 ? -16.735 -8.759  5.135  1.00 47.75  ? 438 MET   A CG  1 
ATOM   1100 S  SD  . MET   A 1 142 ? -15.319 -9.362  6.083  1.00 60.59  ? 438 MET   A SD  1 
ATOM   1101 C  CE  . MET   A 1 142 ? -15.839 -8.910  7.730  1.00 71.69  ? 438 MET   A CE  1 
ATOM   1102 N  N   . PHE   A 1 143 ? -16.809 -4.420  3.887  1.00 54.20  ? 439 PHE   A N   1 
ATOM   1103 C  CA  . PHE   A 1 143 ? -16.799 -2.964  3.979  1.00 54.23  ? 439 PHE   A CA  1 
ATOM   1104 C  C   . PHE   A 1 143 ? -18.070 -2.360  3.401  1.00 64.27  ? 439 PHE   A C   1 
ATOM   1105 O  O   . PHE   A 1 143 ? -18.620 -1.396  3.950  1.00 58.34  ? 439 PHE   A O   1 
ATOM   1106 C  CB  . PHE   A 1 143 ? -15.572 -2.410  3.269  1.00 57.58  ? 439 PHE   A CB  1 
ATOM   1107 C  CG  . PHE   A 1 143 ? -15.590 -0.918  3.110  1.00 68.91  ? 439 PHE   A CG  1 
ATOM   1108 C  CD1 . PHE   A 1 143 ? -15.657 -0.342  1.855  1.00 70.77  ? 439 PHE   A CD1 1 
ATOM   1109 C  CD2 . PHE   A 1 143 ? -15.551 -0.089  4.213  1.00 50.54  ? 439 PHE   A CD2 1 
ATOM   1110 C  CE1 . PHE   A 1 143 ? -15.671 1.035   1.712  1.00 74.88  ? 439 PHE   A CE1 1 
ATOM   1111 C  CE2 . PHE   A 1 143 ? -15.556 1.281   4.071  1.00 62.15  ? 439 PHE   A CE2 1 
ATOM   1112 C  CZ  . PHE   A 1 143 ? -15.620 1.843   2.819  1.00 72.08  ? 439 PHE   A CZ  1 
ATOM   1113 N  N   . ASN   A 1 144 ? -18.567 -2.934  2.309  1.00 66.50  ? 440 ASN   A N   1 
ATOM   1114 C  CA  . ASN   A 1 144 ? -19.755 -2.390  1.669  1.00 56.99  ? 440 ASN   A CA  1 
ATOM   1115 C  C   . ASN   A 1 144 ? -21.003 -2.655  2.501  1.00 59.73  ? 440 ASN   A C   1 
ATOM   1116 O  O   . ASN   A 1 144 ? -21.851 -1.770  2.663  1.00 59.48  ? 440 ASN   A O   1 
ATOM   1117 C  CB  . ASN   A 1 144 ? -19.911 -2.984  0.279  1.00 60.97  ? 440 ASN   A CB  1 
ATOM   1118 C  CG  . ASN   A 1 144 ? -20.896 -2.215  -0.549 1.00 59.88  ? 440 ASN   A CG  1 
ATOM   1119 O  OD1 . ASN   A 1 144 ? -20.676 -1.041  -0.842 1.00 64.03  ? 440 ASN   A OD1 1 
ATOM   1120 N  ND2 . ASN   A 1 144 ? -22.003 -2.858  -0.913 1.00 65.59  ? 440 ASN   A ND2 1 
ATOM   1121 N  N   . TYR   A 1 145 ? -21.149 -3.882  3.006  1.00 56.89  ? 441 TYR   A N   1 
ATOM   1122 C  CA  . TYR   A 1 145 ? -22.300 -4.199  3.846  1.00 58.20  ? 441 TYR   A CA  1 
ATOM   1123 C  C   . TYR   A 1 145 ? -22.300 -3.351  5.107  1.00 62.35  ? 441 TYR   A C   1 
ATOM   1124 O  O   . TYR   A 1 145 ? -23.348 -2.845  5.533  1.00 67.16  ? 441 TYR   A O   1 
ATOM   1125 C  CB  . TYR   A 1 145 ? -22.296 -5.680  4.204  1.00 49.34  ? 441 TYR   A CB  1 
ATOM   1126 C  CG  . TYR   A 1 145 ? -23.024 -6.576  3.230  1.00 47.98  ? 441 TYR   A CG  1 
ATOM   1127 C  CD1 . TYR   A 1 145 ? -22.331 -7.473  2.447  1.00 42.81  ? 441 TYR   A CD1 1 
ATOM   1128 C  CD2 . TYR   A 1 145 ? -24.406 -6.539  3.124  1.00 54.92  ? 441 TYR   A CD2 1 
ATOM   1129 C  CE1 . TYR   A 1 145 ? -22.992 -8.316  1.557  1.00 51.11  ? 441 TYR   A CE1 1 
ATOM   1130 C  CE2 . TYR   A 1 145 ? -25.074 -7.366  2.263  1.00 56.45  ? 441 TYR   A CE2 1 
ATOM   1131 C  CZ  . TYR   A 1 145 ? -24.365 -8.256  1.472  1.00 57.48  ? 441 TYR   A CZ  1 
ATOM   1132 O  OH  . TYR   A 1 145 ? -25.039 -9.077  0.596  1.00 62.01  ? 441 TYR   A OH  1 
ATOM   1133 N  N   . ILE   A 1 146 ? -21.128 -3.194  5.724  1.00 56.27  ? 442 ILE   A N   1 
ATOM   1134 C  CA  . ILE   A 1 146 ? -21.023 -2.398  6.942  1.00 55.45  ? 442 ILE   A CA  1 
ATOM   1135 C  C   . ILE   A 1 146 ? -21.395 -0.947  6.664  1.00 62.47  ? 442 ILE   A C   1 
ATOM   1136 O  O   . ILE   A 1 146 ? -22.144 -0.332  7.432  1.00 54.60  ? 442 ILE   A O   1 
ATOM   1137 C  CB  . ILE   A 1 146 ? -19.609 -2.527  7.533  1.00 51.62  ? 442 ILE   A CB  1 
ATOM   1138 C  CG1 . ILE   A 1 146 ? -19.375 -3.960  8.024  1.00 54.91  ? 442 ILE   A CG1 1 
ATOM   1139 C  CG2 . ILE   A 1 146 ? -19.407 -1.523  8.652  1.00 47.38  ? 442 ILE   A CG2 1 
ATOM   1140 C  CD1 . ILE   A 1 146 ? -17.966 -4.236  8.498  1.00 58.01  ? 442 ILE   A CD1 1 
ATOM   1141 N  N   . CYS   A 1 147 ? -20.915 -0.391  5.536  1.00 63.82  ? 443 CYS   A N   1 
ATOM   1142 C  CA  . CYS   A 1 147 ? -21.247 0.990   5.186  1.00 53.39  ? 443 CYS   A CA  1 
ATOM   1143 C  C   . CYS   A 1 147 ? -22.746 1.169   5.024  1.00 50.81  ? 443 CYS   A C   1 
ATOM   1144 O  O   . CYS   A 1 147 ? -23.315 2.178   5.465  1.00 60.97  ? 443 CYS   A O   1 
ATOM   1145 C  CB  . CYS   A 1 147 ? -20.549 1.409   3.896  1.00 55.70  ? 443 CYS   A CB  1 
ATOM   1146 S  SG  . CYS   A 1 147 ? -18.880 2.011   4.067  1.00 61.56  ? 443 CYS   A SG  1 
ATOM   1147 N  N   . ASN   A 1 148 ? -23.399 0.202   4.386  1.00 51.73  ? 444 ASN   A N   1 
ATOM   1148 C  CA  . ASN   A 1 148 ? -24.847 0.256   4.258  1.00 52.43  ? 444 ASN   A CA  1 
ATOM   1149 C  C   . ASN   A 1 148 ? -25.513 0.118   5.614  1.00 53.96  ? 444 ASN   A C   1 
ATOM   1150 O  O   . ASN   A 1 148 ? -26.568 0.714   5.853  1.00 55.43  ? 444 ASN   A O   1 
ATOM   1151 C  CB  . ASN   A 1 148 ? -25.337 -0.839  3.318  1.00 59.82  ? 444 ASN   A CB  1 
ATOM   1152 C  CG  . ASN   A 1 148 ? -25.015 -0.533  1.853  1.00 57.84  ? 444 ASN   A CG  1 
ATOM   1153 O  OD1 . ASN   A 1 148 ? -24.508 0.542   1.530  1.00 60.78  ? 444 ASN   A OD1 1 
ATOM   1154 N  ND2 . ASN   A 1 148 ? -25.314 -1.473  0.970  1.00 57.76  ? 444 ASN   A ND2 1 
ATOM   1155 N  N   . HIS   A 1 149 ? -24.908 -0.670  6.506  1.00 48.90  ? 445 HIS   A N   1 
ATOM   1156 C  CA  . HIS   A 1 149 ? -25.420 -0.796  7.865  1.00 49.97  ? 445 HIS   A CA  1 
ATOM   1157 C  C   . HIS   A 1 149 ? -25.313 0.530   8.614  1.00 50.65  ? 445 HIS   A C   1 
ATOM   1158 O  O   . HIS   A 1 149 ? -26.291 0.989   9.216  1.00 52.77  ? 445 HIS   A O   1 
ATOM   1159 C  CB  . HIS   A 1 149 ? -24.662 -1.915  8.587  1.00 51.02  ? 445 HIS   A CB  1 
ATOM   1160 C  CG  . HIS   A 1 149 ? -25.046 -2.099  10.031 1.00 50.62  ? 445 HIS   A CG  1 
ATOM   1161 N  ND1 . HIS   A 1 149 ? -25.226 -3.345  10.588 1.00 46.84  ? 445 HIS   A ND1 1 
ATOM   1162 C  CD2 . HIS   A 1 149 ? -25.243 -1.206  11.035 1.00 52.46  ? 445 HIS   A CD2 1 
ATOM   1163 C  CE1 . HIS   A 1 149 ? -25.546 -3.214  11.866 1.00 51.87  ? 445 HIS   A CE1 1 
ATOM   1164 N  NE2 . HIS   A 1 149 ? -25.562 -1.926  12.163 1.00 56.05  ? 445 HIS   A NE2 1 
ATOM   1165 N  N   . VAL   A 1 150 ? -24.132 1.163   8.587  1.00 42.64  ? 446 VAL   A N   1 
ATOM   1166 C  CA  . VAL   A 1 150 ? -23.956 2.456   9.252  1.00 43.55  ? 446 VAL   A CA  1 
ATOM   1167 C  C   . VAL   A 1 150 ? -24.965 3.469   8.725  1.00 59.39  ? 446 VAL   A C   1 
ATOM   1168 O  O   . VAL   A 1 150 ? -25.676 4.116   9.490  1.00 63.93  ? 446 VAL   A O   1 
ATOM   1169 C  CB  . VAL   A 1 150 ? -22.512 2.963   9.079  1.00 54.57  ? 446 VAL   A CB  1 
ATOM   1170 C  CG1 . VAL   A 1 150 ? -22.381 4.355   9.639  1.00 52.23  ? 446 VAL   A CG1 1 
ATOM   1171 C  CG2 . VAL   A 1 150 ? -21.528 2.017   9.722  1.00 57.10  ? 446 VAL   A CG2 1 
ATOM   1172 N  N   . LYS   A 1 151 ? -25.054 3.619   7.404  1.00 60.16  ? 447 LYS   A N   1 
ATOM   1173 C  CA  . LYS   A 1 151 ? -25.981 4.613   6.863  1.00 60.62  ? 447 LYS   A CA  1 
ATOM   1174 C  C   . LYS   A 1 151 ? -27.414 4.313   7.281  1.00 60.51  ? 447 LYS   A C   1 
ATOM   1175 O  O   . LYS   A 1 151 ? -28.133 5.202   7.763  1.00 57.64  ? 447 LYS   A O   1 
ATOM   1176 C  CB  . LYS   A 1 151 ? -25.881 4.668   5.345  1.00 61.20  ? 447 LYS   A CB  1 
ATOM   1177 C  CG  . LYS   A 1 151 ? -26.420 5.960   4.765  1.00 66.98  ? 447 LYS   A CG  1 
ATOM   1178 C  CD  . LYS   A 1 151 ? -26.155 5.963   3.290  1.00 64.51  ? 447 LYS   A CD  1 
ATOM   1179 C  CE  . LYS   A 1 151 ? -26.255 7.349   2.668  1.00 69.14  ? 447 LYS   A CE  1 
ATOM   1180 N  NZ  . LYS   A 1 151 ? -25.817 7.227   1.259  1.00 61.53  ? 447 LYS   A NZ  1 
ATOM   1181 N  N   . TYR   A 1 152 ? -27.831 3.050   7.136  1.00 55.07  ? 448 TYR   A N   1 
ATOM   1182 C  CA  . TYR   A 1 152 ? -29.180 2.667   7.531  1.00 62.89  ? 448 TYR   A CA  1 
ATOM   1183 C  C   . TYR   A 1 152 ? -29.413 2.914   9.021  1.00 56.67  ? 448 TYR   A C   1 
ATOM   1184 O  O   . TYR   A 1 152 ? -30.316 3.673   9.392  1.00 67.32  ? 448 TYR   A O   1 
ATOM   1185 C  CB  . TYR   A 1 152 ? -29.448 1.204   7.181  1.00 62.37  ? 448 TYR   A CB  1 
ATOM   1186 C  CG  . TYR   A 1 152 ? -30.806 0.759   7.678  1.00 67.41  ? 448 TYR   A CG  1 
ATOM   1187 C  CD1 . TYR   A 1 152 ? -31.930 0.927   6.893  1.00 71.31  ? 448 TYR   A CD1 1 
ATOM   1188 C  CD2 . TYR   A 1 152 ? -30.972 0.215   8.951  1.00 57.97  ? 448 TYR   A CD2 1 
ATOM   1189 C  CE1 . TYR   A 1 152 ? -33.177 0.551   7.337  1.00 69.15  ? 448 TYR   A CE1 1 
ATOM   1190 C  CE2 . TYR   A 1 152 ? -32.227 -0.167  9.403  1.00 63.97  ? 448 TYR   A CE2 1 
ATOM   1191 C  CZ  . TYR   A 1 152 ? -33.328 0.002   8.581  1.00 68.53  ? 448 TYR   A CZ  1 
ATOM   1192 O  OH  . TYR   A 1 152 ? -34.597 -0.365  8.975  1.00 74.44  ? 448 TYR   A OH  1 
ATOM   1193 N  N   . ALA   A 1 153 ? -28.606 2.285   9.896  1.00 51.17  ? 449 ALA   A N   1 
ATOM   1194 C  CA  . ALA   A 1 153 ? -28.864 2.389   11.329 1.00 56.70  ? 449 ALA   A CA  1 
ATOM   1195 C  C   . ALA   A 1 153 ? -28.754 3.825   11.818 1.00 63.46  ? 449 ALA   A C   1 
ATOM   1196 O  O   . ALA   A 1 153 ? -29.378 4.186   12.823 1.00 59.44  ? 449 ALA   A O   1 
ATOM   1197 C  CB  . ALA   A 1 153 ? -27.901 1.507   12.140 1.00 46.91  ? 449 ALA   A CB  1 
ATOM   1198 N  N   . THR   A 1 154 ? -27.963 4.657   11.138 1.00 53.66  ? 450 THR   A N   1 
ATOM   1199 C  CA  . THR   A 1 154 ? -27.836 6.031   11.602 1.00 59.82  ? 450 THR   A CA  1 
ATOM   1200 C  C   . THR   A 1 154 ? -29.079 6.850   11.263 1.00 67.70  ? 450 THR   A C   1 
ATOM   1201 O  O   . THR   A 1 154 ? -29.580 7.594   12.113 1.00 73.20  ? 450 THR   A O   1 
ATOM   1202 C  CB  . THR   A 1 154 ? -26.572 6.652   11.023 1.00 61.54  ? 450 THR   A CB  1 
ATOM   1203 O  OG1 . THR   A 1 154 ? -25.438 5.910   11.491 1.00 63.12  ? 450 THR   A OG1 1 
ATOM   1204 C  CG2 . THR   A 1 154 ? -26.455 8.112   11.463 1.00 65.57  ? 450 THR   A CG2 1 
ATOM   1205 N  N   . ASN   A 1 155 ? -29.603 6.702   10.043 1.00 66.74  ? 451 ASN   A N   1 
ATOM   1206 C  CA  . ASN   A 1 155 ? -30.873 7.312   9.634  1.00 59.83  ? 451 ASN   A CA  1 
ATOM   1207 C  C   . ASN   A 1 155 ? -30.947 8.784   10.045 1.00 65.69  ? 451 ASN   A C   1 
ATOM   1208 O  O   . ASN   A 1 155 ? -31.937 9.255   10.608 1.00 73.22  ? 451 ASN   A O   1 
ATOM   1209 C  CB  . ASN   A 1 155 ? -32.060 6.516   10.186 1.00 60.15  ? 451 ASN   A CB  1 
ATOM   1210 C  CG  . ASN   A 1 155 ? -33.401 6.961   9.613  1.00 76.29  ? 451 ASN   A CG  1 
ATOM   1211 O  OD1 . ASN   A 1 155 ? -33.495 7.455   8.479  1.00 75.53  ? 451 ASN   A OD1 1 
ATOM   1212 N  ND2 . ASN   A 1 155 ? -34.455 6.780   10.406 1.00 76.75  ? 451 ASN   A ND2 1 
ATOM   1213 N  N   . LYS   A 1 156 ? -29.878 9.516   9.731  1.00 69.62  ? 452 LYS   A N   1 
ATOM   1214 C  CA  . LYS   A 1 156 ? -29.818 10.960  9.933  1.00 73.72  ? 452 LYS   A CA  1 
ATOM   1215 C  C   . LYS   A 1 156 ? -30.071 11.313  11.397 1.00 85.68  ? 452 LYS   A C   1 
ATOM   1216 O  O   . LYS   A 1 156 ? -30.712 12.317  11.711 1.00 97.56  ? 452 LYS   A O   1 
ATOM   1217 C  CB  . LYS   A 1 156 ? -30.804 11.699  9.026  1.00 85.67  ? 452 LYS   A CB  1 
ATOM   1218 C  CG  . LYS   A 1 156 ? -30.806 11.285  7.566  1.00 94.30  ? 452 LYS   A CG  1 
ATOM   1219 C  CD  . LYS   A 1 156 ? -31.443 12.364  6.686  1.00 97.06  ? 452 LYS   A CD  1 
ATOM   1220 C  CE  . LYS   A 1 156 ? -32.618 13.063  7.376  1.00 103.92 ? 452 LYS   A CE  1 
ATOM   1221 N  NZ  . LYS   A 1 156 ? -33.736 12.137  7.701  1.00 111.96 ? 452 LYS   A NZ  1 
ATOM   1222 N  N   . GLY   A 1 157 ? -29.589 10.456  12.301 1.00 77.55  ? 453 GLY   A N   1 
ATOM   1223 C  CA  . GLY   A 1 157 ? -29.758 10.650  13.721 1.00 76.40  ? 453 GLY   A CA  1 
ATOM   1224 C  C   . GLY   A 1 157 ? -30.994 10.003  14.303 1.00 80.66  ? 453 GLY   A C   1 
ATOM   1225 O  O   . GLY   A 1 157 ? -31.062 9.811   15.523 1.00 72.36  ? 453 GLY   A O   1 
ATOM   1226 N  N   . ASN   A 1 158 ? -31.973 9.646   13.469 1.00 84.47  ? 454 ASN   A N   1 
ATOM   1227 C  CA  . ASN   A 1 158 ? -33.119 8.886   13.962 1.00 84.40  ? 454 ASN   A CA  1 
ATOM   1228 C  C   . ASN   A 1 158 ? -32.711 7.417   13.964 1.00 78.30  ? 454 ASN   A C   1 
ATOM   1229 O  O   . ASN   A 1 158 ? -33.149 6.621   13.132 1.00 79.23  ? 454 ASN   A O   1 
ATOM   1230 C  CB  . ASN   A 1 158 ? -34.363 9.143   13.117 1.00 85.25  ? 454 ASN   A CB  1 
ATOM   1231 C  CG  . ASN   A 1 158 ? -35.564 8.338   13.593 1.00 94.98  ? 454 ASN   A CG  1 
ATOM   1232 O  OD1 . ASN   A 1 158 ? -35.640 7.940   14.765 1.00 95.52  ? 454 ASN   A OD1 1 
ATOM   1233 N  ND2 . ASN   A 1 158 ? -36.498 8.078   12.688 1.00 96.89  ? 454 ASN   A ND2 1 
ATOM   1234 N  N   . LEU   A 1 159 ? -31.859 7.057   14.935 1.00 60.85  ? 455 LEU   A N   1 
ATOM   1235 C  CA  . LEU   A 1 159 ? -31.155 5.783   14.877 1.00 59.83  ? 455 LEU   A CA  1 
ATOM   1236 C  C   . LEU   A 1 159 ? -32.133 4.614   14.850 1.00 59.96  ? 455 LEU   A C   1 
ATOM   1237 O  O   . LEU   A 1 159 ? -33.202 4.647   15.471 1.00 62.35  ? 455 LEU   A O   1 
ATOM   1238 C  CB  . LEU   A 1 159 ? -30.215 5.632   16.073 1.00 67.90  ? 455 LEU   A CB  1 
ATOM   1239 C  CG  . LEU   A 1 159 ? -28.796 6.204   16.019 1.00 71.29  ? 455 LEU   A CG  1 
ATOM   1240 C  CD1 . LEU   A 1 159 ? -28.742 7.505   15.267 1.00 66.93  ? 455 LEU   A CD1 1 
ATOM   1241 C  CD2 . LEU   A 1 159 ? -28.299 6.408   17.455 1.00 76.98  ? 455 LEU   A CD2 1 
ATOM   1242 N  N   . ARG   A 1 160 ? -31.750 3.573   14.122 1.00 56.12  ? 456 ARG   A N   1 
ATOM   1243 C  CA  . ARG   A 1 160 ? -32.554 2.372   13.967 1.00 51.07  ? 456 ARG   A CA  1 
ATOM   1244 C  C   . ARG   A 1 160 ? -31.705 1.164   14.307 1.00 49.28  ? 456 ARG   A C   1 
ATOM   1245 O  O   . ARG   A 1 160 ? -30.543 1.072   13.894 1.00 51.53  ? 456 ARG   A O   1 
ATOM   1246 C  CB  . ARG   A 1 160 ? -33.103 2.229   12.513 1.00 54.31  ? 456 ARG   A CB  1 
ATOM   1247 C  CG  . ARG   A 1 160 ? -33.958 3.409   12.133 1.00 68.19  ? 456 ARG   A CG  1 
ATOM   1248 C  CD  . ARG   A 1 160 ? -34.602 3.262   10.769 1.00 68.29  ? 456 ARG   A CD  1 
ATOM   1249 N  NE  . ARG   A 1 160 ? -33.630 3.398   9.693  1.00 60.72  ? 456 ARG   A NE  1 
ATOM   1250 C  CZ  . ARG   A 1 160 ? -33.961 3.721   8.450  1.00 67.38  ? 456 ARG   A CZ  1 
ATOM   1251 N  NH1 . ARG   A 1 160 ? -35.233 3.955   8.157  1.00 67.60  ? 456 ARG   A NH1 1 
ATOM   1252 N  NH2 . ARG   A 1 160 ? -33.026 3.835   7.516  1.00 55.16  ? 456 ARG   A NH2 1 
ATOM   1253 N  N   . SER   A 1 161 ? -32.305 0.219   15.017 1.00 51.21  ? 457 SER   A N   1 
ATOM   1254 C  CA  . SER   A 1 161 ? -31.593 -0.991  15.399 1.00 57.54  ? 457 SER   A CA  1 
ATOM   1255 C  C   . SER   A 1 161 ? -31.368 -1.855  14.173 1.00 51.10  ? 457 SER   A C   1 
ATOM   1256 O  O   . SER   A 1 161 ? -32.282 -2.037  13.360 1.00 51.21  ? 457 SER   A O   1 
ATOM   1257 C  CB  . SER   A 1 161 ? -32.382 -1.766  16.456 1.00 56.23  ? 457 SER   A CB  1 
ATOM   1258 O  OG  . SER   A 1 161 ? -32.787 -0.902  17.512 1.00 64.74  ? 457 SER   A OG  1 
ATOM   1259 N  N   . ALA   A 1 162 ? -30.158 -2.397  14.048 1.00 51.07  ? 458 ALA   A N   1 
ATOM   1260 C  CA  . ALA   A 1 162 ? -29.829 -3.242  12.912 1.00 52.77  ? 458 ALA   A CA  1 
ATOM   1261 C  C   . ALA   A 1 162 ? -28.722 -4.224  13.274 1.00 50.55  ? 458 ALA   A C   1 
ATOM   1262 O  O   . ALA   A 1 162 ? -27.958 -4.015  14.218 1.00 61.86  ? 458 ALA   A O   1 
ATOM   1263 C  CB  . ALA   A 1 162 ? -29.406 -2.392  11.709 1.00 50.44  ? 458 ALA   A CB  1 
ATOM   1264 N  N   . ILE   A 1 163 ? -28.633 -5.293  12.488 1.00 52.04  ? 459 ILE   A N   1 
ATOM   1265 C  CA  . ILE   A 1 163 ? -27.516 -6.224  12.542 1.00 48.31  ? 459 ILE   A CA  1 
ATOM   1266 C  C   . ILE   A 1 163 ? -27.210 -6.723  11.136 1.00 51.84  ? 459 ILE   A C   1 
ATOM   1267 O  O   . ILE   A 1 163 ? -28.119 -6.963  10.332 1.00 51.74  ? 459 ILE   A O   1 
ATOM   1268 C  CB  . ILE   A 1 163 ? -27.819 -7.406  13.475 1.00 43.13  ? 459 ILE   A CB  1 
ATOM   1269 C  CG1 . ILE   A 1 163 ? -26.598 -8.308  13.611 1.00 40.24  ? 459 ILE   A CG1 1 
ATOM   1270 C  CG2 . ILE   A 1 163 ? -28.975 -8.211  12.956 1.00 41.72  ? 459 ILE   A CG2 1 
ATOM   1271 C  CD1 . ILE   A 1 163 ? -26.802 -9.429  14.687 1.00 34.25  ? 459 ILE   A CD1 1 
ATOM   1272 N  N   . THR   A 1 164 ? -25.923 -6.882  10.842 1.00 49.78  ? 460 THR   A N   1 
ATOM   1273 C  CA  . THR   A 1 164 ? -25.470 -7.456  9.586  1.00 49.98  ? 460 THR   A CA  1 
ATOM   1274 C  C   . THR   A 1 164 ? -24.742 -8.754  9.881  1.00 52.33  ? 460 THR   A C   1 
ATOM   1275 O  O   . THR   A 1 164 ? -23.808 -8.766  10.694 1.00 62.99  ? 460 THR   A O   1 
ATOM   1276 C  CB  . THR   A 1 164 ? -24.555 -6.496  8.841  1.00 48.23  ? 460 THR   A CB  1 
ATOM   1277 O  OG1 . THR   A 1 164 ? -25.296 -5.313  8.516  1.00 51.42  ? 460 THR   A OG1 1 
ATOM   1278 C  CG2 . THR   A 1 164 ? -24.039 -7.161  7.572  1.00 53.41  ? 460 THR   A CG2 1 
ATOM   1279 N  N   . ILE   A 1 165 ? -25.167 -9.838  9.220  1.00 51.94  ? 461 ILE   A N   1 
ATOM   1280 C  CA  . ILE   A 1 165 ? -24.759 -11.196 9.579  1.00 44.01  ? 461 ILE   A CA  1 
ATOM   1281 C  C   . ILE   A 1 165 ? -23.952 -11.762 8.419  1.00 53.51  ? 461 ILE   A C   1 
ATOM   1282 O  O   . ILE   A 1 165 ? -24.511 -12.121 7.382  1.00 49.13  ? 461 ILE   A O   1 
ATOM   1283 C  CB  . ILE   A 1 165 ? -25.955 -12.090 9.918  1.00 51.46  ? 461 ILE   A CB  1 
ATOM   1284 C  CG1 . ILE   A 1 165 ? -26.664 -11.574 11.168 1.00 47.76  ? 461 ILE   A CG1 1 
ATOM   1285 C  CG2 . ILE   A 1 165 ? -25.493 -13.496 10.175 1.00 55.00  ? 461 ILE   A CG2 1 
ATOM   1286 C  CD1 . ILE   A 1 165 ? -28.053 -12.095 11.311 1.00 47.96  ? 461 ILE   A CD1 1 
ATOM   1287 N  N   . PHE   A 1 166 ? -22.644 -11.856 8.602  1.00 54.81  ? 462 PHE   A N   1 
ATOM   1288 C  CA  . PHE   A 1 166 ? -21.735 -12.376 7.601  1.00 47.84  ? 462 PHE   A CA  1 
ATOM   1289 C  C   . PHE   A 1 166 ? -21.746 -13.902 7.638  1.00 59.79  ? 462 PHE   A C   1 
ATOM   1290 O  O   . PHE   A 1 166 ? -22.441 -14.495 8.468  1.00 59.75  ? 462 PHE   A O   1 
ATOM   1291 C  CB  . PHE   A 1 166 ? -20.348 -11.779 7.829  1.00 45.52  ? 462 PHE   A CB  1 
ATOM   1292 C  CG  . PHE   A 1 166 ? -20.263 -10.324 7.458  1.00 61.63  ? 462 PHE   A CG  1 
ATOM   1293 C  CD1 . PHE   A 1 166 ? -20.253 -9.925  6.119  1.00 57.76  ? 462 PHE   A CD1 1 
ATOM   1294 C  CD2 . PHE   A 1 166 ? -20.227 -9.349  8.441  1.00 56.92  ? 462 PHE   A CD2 1 
ATOM   1295 C  CE1 . PHE   A 1 166 ? -20.197 -8.580  5.782  1.00 66.50  ? 462 PHE   A CE1 1 
ATOM   1296 C  CE2 . PHE   A 1 166 ? -20.167 -7.996  8.101  1.00 53.71  ? 462 PHE   A CE2 1 
ATOM   1297 C  CZ  . PHE   A 1 166 ? -20.153 -7.617  6.772  1.00 66.27  ? 462 PHE   A CZ  1 
ATOM   1298 N  N   . PRO   A 1 167 ? -21.048 -14.568 6.704  1.00 65.10  ? 463 PRO   A N   1 
ATOM   1299 C  CA  . PRO   A 1 167 ? -21.122 -16.035 6.643  1.00 63.82  ? 463 PRO   A CA  1 
ATOM   1300 C  C   . PRO   A 1 167 ? -20.719 -16.706 7.952  1.00 58.90  ? 463 PRO   A C   1 
ATOM   1301 O  O   . PRO   A 1 167 ? -19.820 -16.256 8.669  1.00 61.43  ? 463 PRO   A O   1 
ATOM   1302 C  CB  . PRO   A 1 167 ? -20.154 -16.382 5.509  1.00 62.50  ? 463 PRO   A CB  1 
ATOM   1303 C  CG  . PRO   A 1 167 ? -20.253 -15.230 4.606  1.00 71.33  ? 463 PRO   A CG  1 
ATOM   1304 C  CD  . PRO   A 1 167 ? -20.353 -14.034 5.511  1.00 63.99  ? 463 PRO   A CD  1 
ATOM   1305 N  N   . GLN   A 1 168 ? -21.403 -17.802 8.254  1.00 59.31  ? 464 GLN   A N   1 
ATOM   1306 C  CA  . GLN   A 1 168 ? -21.149 -18.549 9.473  1.00 52.66  ? 464 GLN   A CA  1 
ATOM   1307 C  C   . GLN   A 1 168 ? -19.798 -19.255 9.420  1.00 62.02  ? 464 GLN   A C   1 
ATOM   1308 O  O   . GLN   A 1 168 ? -19.248 -19.544 8.354  1.00 57.04  ? 464 GLN   A O   1 
ATOM   1309 C  CB  . GLN   A 1 168 ? -22.248 -19.583 9.704  1.00 51.64  ? 464 GLN   A CB  1 
ATOM   1310 C  CG  . GLN   A 1 168 ? -22.295 -20.675 8.656  1.00 51.98  ? 464 GLN   A CG  1 
ATOM   1311 C  CD  . GLN   A 1 168 ? -23.697 -21.201 8.422  1.00 68.66  ? 464 GLN   A CD  1 
ATOM   1312 O  OE1 . GLN   A 1 168 ? -24.679 -20.462 8.516  1.00 71.84  ? 464 GLN   A OE1 1 
ATOM   1313 N  NE2 . GLN   A 1 168 ? -23.796 -22.490 8.111  1.00 80.15  ? 464 GLN   A NE2 1 
ATOM   1314 N  N   . ARG   A 1 169 ? -19.262 -19.532 10.607 1.00 57.06  ? 465 ARG   A N   1 
ATOM   1315 C  CA  . ARG   A 1 169 ? -18.057 -20.339 10.693 1.00 65.67  ? 465 ARG   A CA  1 
ATOM   1316 C  C   . ARG   A 1 169 ? -18.314 -21.725 10.109 1.00 77.53  ? 465 ARG   A C   1 
ATOM   1317 O  O   . ARG   A 1 169 ? -19.380 -22.316 10.304 1.00 77.14  ? 465 ARG   A O   1 
ATOM   1318 C  CB  . ARG   A 1 169 ? -17.597 -20.451 12.154 1.00 74.59  ? 465 ARG   A CB  1 
ATOM   1319 C  CG  . ARG   A 1 169 ? -16.373 -21.338 12.310 1.00 83.99  ? 465 ARG   A CG  1 
ATOM   1320 C  CD  . ARG   A 1 169 ? -15.955 -21.517 13.740 1.00 84.54  ? 465 ARG   A CD  1 
ATOM   1321 N  NE  . ARG   A 1 169 ? -15.174 -20.391 14.238 1.00 88.74  ? 465 ARG   A NE  1 
ATOM   1322 C  CZ  . ARG   A 1 169 ? -15.573 -19.585 15.213 1.00 82.25  ? 465 ARG   A CZ  1 
ATOM   1323 N  NH1 . ARG   A 1 169 ? -16.745 -19.791 15.799 1.00 81.75  ? 465 ARG   A NH1 1 
ATOM   1324 N  NH2 . ARG   A 1 169 ? -14.799 -18.581 15.605 1.00 79.70  ? 465 ARG   A NH2 1 
ATOM   1325 N  N   . THR   A 1 170 ? -17.330 -22.235 9.371  1.00 82.95  ? 466 THR   A N   1 
ATOM   1326 C  CA  . THR   A 1 170 ? -17.377 -23.591 8.840  1.00 83.55  ? 466 THR   A CA  1 
ATOM   1327 C  C   . THR   A 1 170 ? -16.262 -24.418 9.465  1.00 86.84  ? 466 THR   A C   1 
ATOM   1328 O  O   . THR   A 1 170 ? -16.460 -25.067 10.496 1.00 88.54  ? 466 THR   A O   1 
ATOM   1329 C  CB  . THR   A 1 170 ? -17.235 -23.590 7.316  1.00 81.79  ? 466 THR   A CB  1 
ATOM   1330 O  OG1 . THR   A 1 170 ? -16.109 -22.786 6.946  1.00 80.02  ? 466 THR   A OG1 1 
ATOM   1331 C  CG2 . THR   A 1 170 ? -18.498 -23.050 6.644  1.00 80.23  ? 466 THR   A CG2 1 
ATOM   1332 N  N   . ASP   A 1 171 ? -15.077 -24.383 8.848  1.00 94.63  ? 467 ASP   A N   1 
ATOM   1333 C  CA  . ASP   A 1 171 ? -13.940 -25.131 9.373  1.00 105.50 ? 467 ASP   A CA  1 
ATOM   1334 C  C   . ASP   A 1 171 ? -13.351 -24.475 10.615 1.00 101.56 ? 467 ASP   A C   1 
ATOM   1335 O  O   . ASP   A 1 171 ? -12.862 -25.176 11.505 1.00 118.99 ? 467 ASP   A O   1 
ATOM   1336 C  CB  . ASP   A 1 171 ? -12.858 -25.262 8.304  1.00 118.29 ? 467 ASP   A CB  1 
ATOM   1337 C  CG  . ASP   A 1 171 ? -12.139 -23.954 8.052  1.00 126.57 ? 467 ASP   A CG  1 
ATOM   1338 O  OD1 . ASP   A 1 171 ? -12.813 -22.906 8.035  1.00 127.22 ? 467 ASP   A OD1 1 
ATOM   1339 O  OD2 . ASP   A 1 171 ? -10.899 -23.968 7.899  1.00 132.99 ? 467 ASP   A OD2 1 
ATOM   1340 N  N   . GLY   A 1 172 ? -13.380 -23.144 10.692 1.00 91.28  ? 468 GLY   A N   1 
ATOM   1341 C  CA  . GLY   A 1 172 ? -12.698 -22.429 11.756 1.00 88.96  ? 468 GLY   A CA  1 
ATOM   1342 C  C   . GLY   A 1 172 ? -11.547 -21.573 11.258 1.00 95.88  ? 468 GLY   A C   1 
ATOM   1343 O  O   . GLY   A 1 172 ? -11.389 -20.431 11.698 1.00 89.14  ? 468 GLY   A O   1 
ATOM   1344 N  N   . LYS   A 1 173 ? -10.731 -22.110 10.342 1.00 106.82 ? 469 LYS   A N   1 
ATOM   1345 C  CA  . LYS   A 1 173 ? -9.634  -21.345 9.755  1.00 117.60 ? 469 LYS   A CA  1 
ATOM   1346 C  C   . LYS   A 1 173 ? -10.097 -20.451 8.612  1.00 113.26 ? 469 LYS   A C   1 
ATOM   1347 O  O   . LYS   A 1 173 ? -9.334  -19.588 8.161  1.00 110.30 ? 469 LYS   A O   1 
ATOM   1348 C  CB  . LYS   A 1 173 ? -8.522  -22.289 9.274  1.00 132.90 ? 469 LYS   A CB  1 
ATOM   1349 C  CG  . LYS   A 1 173 ? -7.157  -21.621 9.107  1.00 143.36 ? 469 LYS   A CG  1 
ATOM   1350 C  CD  . LYS   A 1 173 ? -6.822  -20.725 10.301 1.00 145.72 ? 469 LYS   A CD  1 
ATOM   1351 C  CE  . LYS   A 1 173 ? -6.634  -19.266 9.877  1.00 143.31 ? 469 LYS   A CE  1 
ATOM   1352 N  NZ  . LYS   A 1 173 ? -6.661  -18.327 11.038 1.00 137.68 ? 469 LYS   A NZ  1 
ATOM   1353 N  N   . HIS   A 1 174 ? -11.318 -20.644 8.129  1.00 112.42 ? 470 HIS   A N   1 
ATOM   1354 C  CA  . HIS   A 1 174 ? -12.008 -19.673 7.294  1.00 111.17 ? 470 HIS   A CA  1 
ATOM   1355 C  C   . HIS   A 1 174 ? -13.046 -18.990 8.169  1.00 113.90 ? 470 HIS   A C   1 
ATOM   1356 O  O   . HIS   A 1 174 ? -14.024 -19.619 8.585  1.00 120.40 ? 470 HIS   A O   1 
ATOM   1357 C  CB  . HIS   A 1 174 ? -12.654 -20.340 6.083  1.00 108.88 ? 470 HIS   A CB  1 
ATOM   1358 C  CG  . HIS   A 1 174 ? -11.687 -21.108 5.247  1.00 111.85 ? 470 HIS   A CG  1 
ATOM   1359 N  ND1 . HIS   A 1 174 ? -11.650 -22.485 5.233  1.00 117.18 ? 470 HIS   A ND1 1 
ATOM   1360 C  CD2 . HIS   A 1 174 ? -10.693 -20.694 4.429  1.00 115.84 ? 470 HIS   A CD2 1 
ATOM   1361 C  CE1 . HIS   A 1 174 ? -10.689 -22.887 4.420  1.00 123.69 ? 470 HIS   A CE1 1 
ATOM   1362 N  NE2 . HIS   A 1 174 ? -10.093 -21.820 3.920  1.00 122.54 ? 470 HIS   A NE2 1 
ATOM   1363 N  N   . ASP   A 1 175 ? -12.819 -17.718 8.464  1.00 109.28 ? 471 ASP   A N   1 
ATOM   1364 C  CA  . ASP   A 1 175 ? -13.593 -17.038 9.490  1.00 94.22  ? 471 ASP   A CA  1 
ATOM   1365 C  C   . ASP   A 1 175 ? -13.756 -15.585 9.085  1.00 87.75  ? 471 ASP   A C   1 
ATOM   1366 O  O   . ASP   A 1 175 ? -12.761 -14.871 8.930  1.00 98.24  ? 471 ASP   A O   1 
ATOM   1367 C  CB  . ASP   A 1 175 ? -12.892 -17.141 10.844 1.00 96.07  ? 471 ASP   A CB  1 
ATOM   1368 C  CG  . ASP   A 1 175 ? -13.627 -18.031 11.824 1.00 89.14  ? 471 ASP   A CG  1 
ATOM   1369 O  OD1 . ASP   A 1 175 ? -14.126 -19.099 11.420 1.00 90.90  ? 471 ASP   A OD1 1 
ATOM   1370 O  OD2 . ASP   A 1 175 ? -13.692 -17.654 13.010 1.00 90.13  ? 471 ASP   A OD2 1 
ATOM   1371 N  N   . PHE   A 1 176 ? -14.998 -15.148 8.907  1.00 71.36  ? 472 PHE   A N   1 
ATOM   1372 C  CA  . PHE   A 1 176 ? -15.258 -13.724 8.753  1.00 69.51  ? 472 PHE   A CA  1 
ATOM   1373 C  C   . PHE   A 1 176 ? -15.206 -13.055 10.113 1.00 63.21  ? 472 PHE   A C   1 
ATOM   1374 O  O   . PHE   A 1 176 ? -15.906 -13.474 11.041 1.00 54.32  ? 472 PHE   A O   1 
ATOM   1375 C  CB  . PHE   A 1 176 ? -16.619 -13.489 8.112  1.00 70.60  ? 472 PHE   A CB  1 
ATOM   1376 C  CG  . PHE   A 1 176 ? -16.660 -13.839 6.671  1.00 62.49  ? 472 PHE   A CG  1 
ATOM   1377 C  CD1 . PHE   A 1 176 ? -16.686 -15.165 6.268  1.00 54.93  ? 472 PHE   A CD1 1 
ATOM   1378 C  CD2 . PHE   A 1 176 ? -16.655 -12.843 5.711  1.00 70.59  ? 472 PHE   A CD2 1 
ATOM   1379 C  CE1 . PHE   A 1 176 ? -16.720 -15.490 4.912  1.00 73.46  ? 472 PHE   A CE1 1 
ATOM   1380 C  CE2 . PHE   A 1 176 ? -16.688 -13.150 4.386  1.00 75.07  ? 472 PHE   A CE2 1 
ATOM   1381 C  CZ  . PHE   A 1 176 ? -16.720 -14.482 3.971  1.00 71.83  ? 472 PHE   A CZ  1 
ATOM   1382 N  N   . ARG   A 1 177 ? -14.366 -12.028 10.240 1.00 55.83  ? 473 ARG   A N   1 
ATOM   1383 C  CA  . ARG   A 1 177 ? -14.256 -11.298 11.497 1.00 58.84  ? 473 ARG   A CA  1 
ATOM   1384 C  C   . ARG   A 1 177 ? -14.109 -9.812  11.212 1.00 60.81  ? 473 ARG   A C   1 
ATOM   1385 O  O   . ARG   A 1 177 ? -13.334 -9.422  10.333 1.00 59.09  ? 473 ARG   A O   1 
ATOM   1386 C  CB  . ARG   A 1 177 ? -13.061 -11.790 12.331 1.00 65.70  ? 473 ARG   A CB  1 
ATOM   1387 C  CG  . ARG   A 1 177 ? -13.159 -13.224 12.835 1.00 54.17  ? 473 ARG   A CG  1 
ATOM   1388 C  CD  . ARG   A 1 177 ? -14.217 -13.346 13.919 1.00 66.13  ? 473 ARG   A CD  1 
ATOM   1389 N  NE  . ARG   A 1 177 ? -14.131 -12.272 14.906 1.00 67.99  ? 473 ARG   A NE  1 
ATOM   1390 C  CZ  . ARG   A 1 177 ? -13.358 -12.309 15.989 1.00 75.75  ? 473 ARG   A CZ  1 
ATOM   1391 N  NH1 . ARG   A 1 177 ? -12.589 -13.365 16.223 1.00 75.09  ? 473 ARG   A NH1 1 
ATOM   1392 N  NH2 . ARG   A 1 177 ? -13.353 -11.287 16.837 1.00 76.39  ? 473 ARG   A NH2 1 
ATOM   1393 N  N   . VAL   A 1 178 ? -14.864 -8.991  11.939 1.00 63.56  ? 474 VAL   A N   1 
ATOM   1394 C  CA  . VAL   A 1 178 ? -14.530 -7.577  12.092 1.00 62.52  ? 474 VAL   A CA  1 
ATOM   1395 C  C   . VAL   A 1 178 ? -13.544 -7.479  13.250 1.00 71.83  ? 474 VAL   A C   1 
ATOM   1396 O  O   . VAL   A 1 178 ? -13.876 -7.828  14.387 1.00 72.83  ? 474 VAL   A O   1 
ATOM   1397 C  CB  . VAL   A 1 178 ? -15.781 -6.721  12.356 1.00 63.17  ? 474 VAL   A CB  1 
ATOM   1398 C  CG1 . VAL   A 1 178 ? -15.437 -5.234  12.349 1.00 59.12  ? 474 VAL   A CG1 1 
ATOM   1399 C  CG2 . VAL   A 1 178 ? -16.876 -7.016  11.337 1.00 58.18  ? 474 VAL   A CG2 1 
ATOM   1400 N  N   . TRP   A 1 179 ? -12.320 -7.034  12.963 1.00 73.09  ? 475 TRP   A N   1 
ATOM   1401 C  CA  . TRP   A 1 179 ? -11.318 -6.967  14.023 1.00 73.01  ? 475 TRP   A CA  1 
ATOM   1402 C  C   . TRP   A 1 179 ? -11.575 -5.821  14.997 1.00 69.77  ? 475 TRP   A C   1 
ATOM   1403 O  O   . TRP   A 1 179 ? -11.145 -5.896  16.153 1.00 69.91  ? 475 TRP   A O   1 
ATOM   1404 C  CB  . TRP   A 1 179 ? -9.913  -6.860  13.424 1.00 73.68  ? 475 TRP   A CB  1 
ATOM   1405 C  CG  . TRP   A 1 179 ? -9.405  -8.167  12.898 1.00 72.30  ? 475 TRP   A CG  1 
ATOM   1406 C  CD1 . TRP   A 1 179 ? -10.145 -9.158  12.326 1.00 68.43  ? 475 TRP   A CD1 1 
ATOM   1407 C  CD2 . TRP   A 1 179 ? -8.051  -8.639  12.923 1.00 72.80  ? 475 TRP   A CD2 1 
ATOM   1408 N  NE1 . TRP   A 1 179 ? -9.333  -10.211 11.973 1.00 82.34  ? 475 TRP   A NE1 1 
ATOM   1409 C  CE2 . TRP   A 1 179 ? -8.044  -9.918  12.336 1.00 79.39  ? 475 TRP   A CE2 1 
ATOM   1410 C  CE3 . TRP   A 1 179 ? -6.844  -8.103  13.379 1.00 73.39  ? 475 TRP   A CE3 1 
ATOM   1411 C  CZ2 . TRP   A 1 179 ? -6.880  -10.669 12.195 1.00 79.54  ? 475 TRP   A CZ2 1 
ATOM   1412 C  CZ3 . TRP   A 1 179 ? -5.691  -8.849  13.232 1.00 77.33  ? 475 TRP   A CZ3 1 
ATOM   1413 C  CH2 . TRP   A 1 179 ? -5.717  -10.118 12.646 1.00 75.89  ? 475 TRP   A CH2 1 
ATOM   1414 N  N   . ASN   A 1 180 ? -12.278 -4.774  14.559 1.00 59.62  ? 476 ASN   A N   1 
ATOM   1415 C  CA  . ASN   A 1 180 ? -12.687 -3.698  15.457 1.00 65.83  ? 476 ASN   A CA  1 
ATOM   1416 C  C   . ASN   A 1 180 ? -13.604 -4.229  16.556 1.00 63.02  ? 476 ASN   A C   1 
ATOM   1417 O  O   . ASN   A 1 180 ? -14.409 -5.141  16.336 1.00 57.56  ? 476 ASN   A O   1 
ATOM   1418 C  CB  . ASN   A 1 180 ? -13.420 -2.605  14.675 1.00 69.25  ? 476 ASN   A CB  1 
ATOM   1419 C  CG  . ASN   A 1 180 ? -12.584 -2.025  13.567 1.00 72.47  ? 476 ASN   A CG  1 
ATOM   1420 O  OD1 . ASN   A 1 180 ? -12.217 -2.730  12.623 1.00 80.98  ? 476 ASN   A OD1 1 
ATOM   1421 N  ND2 . ASN   A 1 180 ? -12.289 -0.733  13.657 1.00 67.95  ? 476 ASN   A ND2 1 
ATOM   1422 N  N   . SER   A 1 181 ? -13.491 -3.642  17.759 1.00 60.92  ? 477 SER   A N   1 
ATOM   1423 C  CA  . SER   A 1 181 ? -14.429 -4.016  18.815 1.00 56.59  ? 477 SER   A CA  1 
ATOM   1424 C  C   . SER   A 1 181 ? -15.798 -3.387  18.586 1.00 60.14  ? 477 SER   A C   1 
ATOM   1425 O  O   . SER   A 1 181 ? -16.823 -4.012  18.897 1.00 50.75  ? 477 SER   A O   1 
ATOM   1426 C  CB  . SER   A 1 181 ? -13.877 -3.640  20.195 1.00 54.68  ? 477 SER   A CB  1 
ATOM   1427 O  OG  . SER   A 1 181 ? -12.935 -2.581  20.125 1.00 71.25  ? 477 SER   A OG  1 
ATOM   1428 N  N   . GLN   A 1 182 ? -15.828 -2.169  18.037 1.00 63.93  ? 478 GLN   A N   1 
ATOM   1429 C  CA  . GLN   A 1 182 ? -17.028 -1.555  17.479 1.00 57.41  ? 478 GLN   A CA  1 
ATOM   1430 C  C   . GLN   A 1 182 ? -16.672 -0.940  16.129 1.00 53.84  ? 478 GLN   A C   1 
ATOM   1431 O  O   . GLN   A 1 182 ? -15.520 -0.568  15.892 1.00 60.75  ? 478 GLN   A O   1 
ATOM   1432 C  CB  . GLN   A 1 182 ? -17.621 -0.452  18.383 1.00 66.41  ? 478 GLN   A CB  1 
ATOM   1433 C  CG  . GLN   A 1 182 ? -17.725 -0.776  19.878 1.00 66.47  ? 478 GLN   A CG  1 
ATOM   1434 C  CD  . GLN   A 1 182 ? -18.076 0.455   20.724 1.00 66.67  ? 478 GLN   A CD  1 
ATOM   1435 O  OE1 . GLN   A 1 182 ? -18.561 1.477   20.200 1.00 58.76  ? 478 GLN   A OE1 1 
ATOM   1436 N  NE2 . GLN   A 1 182 ? -17.814 0.370   22.033 1.00 57.30  ? 478 GLN   A NE2 1 
ATOM   1437 N  N   . LEU   A 1 183 ? -17.682 -0.800  15.261 1.00 48.57  ? 479 LEU   A N   1 
ATOM   1438 C  CA  . LEU   A 1 183 ? -17.459 -0.244  13.927 1.00 53.85  ? 479 LEU   A CA  1 
ATOM   1439 C  C   . LEU   A 1 183 ? -16.920 1.173   14.010 1.00 63.17  ? 479 LEU   A C   1 
ATOM   1440 O  O   . LEU   A 1 183 ? -15.969 1.532   13.305 1.00 58.82  ? 479 LEU   A O   1 
ATOM   1441 C  CB  . LEU   A 1 183 ? -18.760 -0.265  13.116 1.00 47.40  ? 479 LEU   A CB  1 
ATOM   1442 C  CG  . LEU   A 1 183 ? -19.547 -1.564  12.941 1.00 56.08  ? 479 LEU   A CG  1 
ATOM   1443 C  CD1 . LEU   A 1 183 ? -20.803 -1.334  12.085 1.00 63.07  ? 479 LEU   A CD1 1 
ATOM   1444 C  CD2 . LEU   A 1 183 ? -18.672 -2.661  12.325 1.00 58.25  ? 479 LEU   A CD2 1 
ATOM   1445 N  N   . ILE   A 1 184 ? -17.505 1.994   14.873 1.00 53.35  ? 480 ILE   A N   1 
ATOM   1446 C  CA  . ILE   A 1 184 ? -17.041 3.356   15.071 1.00 47.42  ? 480 ILE   A CA  1 
ATOM   1447 C  C   . ILE   A 1 184 ? -16.463 3.441   16.478 1.00 59.35  ? 480 ILE   A C   1 
ATOM   1448 O  O   . ILE   A 1 184 ? -17.180 3.240   17.465 1.00 57.09  ? 480 ILE   A O   1 
ATOM   1449 C  CB  . ILE   A 1 184 ? -18.160 4.376   14.841 1.00 63.29  ? 480 ILE   A CB  1 
ATOM   1450 C  CG1 . ILE   A 1 184 ? -18.570 4.355   13.361 1.00 65.96  ? 480 ILE   A CG1 1 
ATOM   1451 C  CG2 . ILE   A 1 184 ? -17.675 5.758   15.207 1.00 66.98  ? 480 ILE   A CG2 1 
ATOM   1452 C  CD1 . ILE   A 1 184 ? -19.885 5.015   13.088 1.00 63.57  ? 480 ILE   A CD1 1 
ATOM   1453 N  N   . ARG   A 1 185 ? -15.159 3.704   16.553 1.00 62.88  ? 481 ARG   A N   1 
ATOM   1454 C  CA  . ARG   A 1 185 ? -14.407 3.894   17.784 1.00 70.11  ? 481 ARG   A CA  1 
ATOM   1455 C  C   . ARG   A 1 185 ? -13.293 4.900   17.520 1.00 77.99  ? 481 ARG   A C   1 
ATOM   1456 O  O   . ARG   A 1 185 ? -12.766 4.987   16.406 1.00 89.11  ? 481 ARG   A O   1 
ATOM   1457 C  CB  . ARG   A 1 185 ? -13.800 2.586   18.314 1.00 68.93  ? 481 ARG   A CB  1 
ATOM   1458 C  CG  . ARG   A 1 185 ? -14.805 1.620   18.925 1.00 81.22  ? 481 ARG   A CG  1 
ATOM   1459 C  CD  . ARG   A 1 185 ? -14.188 0.737   20.023 1.00 73.38  ? 481 ARG   A CD  1 
ATOM   1460 N  NE  . ARG   A 1 185 ? -14.195 1.402   21.321 1.00 75.35  ? 481 ARG   A NE  1 
ATOM   1461 C  CZ  . ARG   A 1 185 ? -13.911 0.798   22.474 1.00 79.80  ? 481 ARG   A CZ  1 
ATOM   1462 N  NH1 . ARG   A 1 185 ? -13.601 -0.496  22.499 1.00 68.90  ? 481 ARG   A NH1 1 
ATOM   1463 N  NH2 . ARG   A 1 185 ? -13.945 1.493   23.604 1.00 85.58  ? 481 ARG   A NH2 1 
ATOM   1464 N  N   . TYR   A 1 186 ? -12.945 5.661   18.554 1.00 64.97  ? 482 TYR   A N   1 
ATOM   1465 C  CA  . TYR   A 1 186 ? -11.854 6.617   18.484 1.00 77.17  ? 482 TYR   A CA  1 
ATOM   1466 C  C   . TYR   A 1 186 ? -10.519 5.933   18.760 1.00 79.80  ? 482 TYR   A C   1 
ATOM   1467 O  O   . TYR   A 1 186 ? -10.425 4.978   19.541 1.00 66.65  ? 482 TYR   A O   1 
ATOM   1468 C  CB  . TYR   A 1 186 ? -12.090 7.758   19.478 1.00 74.33  ? 482 TYR   A CB  1 
ATOM   1469 C  CG  . TYR   A 1 186 ? -13.308 8.581   19.122 1.00 86.08  ? 482 TYR   A CG  1 
ATOM   1470 C  CD1 . TYR   A 1 186 ? -14.273 8.902   20.073 1.00 91.31  ? 482 TYR   A CD1 1 
ATOM   1471 C  CD2 . TYR   A 1 186 ? -13.502 9.020   17.820 1.00 86.05  ? 482 TYR   A CD2 1 
ATOM   1472 C  CE1 . TYR   A 1 186 ? -15.390 9.650   19.730 1.00 93.01  ? 482 TYR   A CE1 1 
ATOM   1473 C  CE2 . TYR   A 1 186 ? -14.604 9.768   17.471 1.00 86.56  ? 482 TYR   A CE2 1 
ATOM   1474 C  CZ  . TYR   A 1 186 ? -15.548 10.078  18.424 1.00 86.18  ? 482 TYR   A CZ  1 
ATOM   1475 O  OH  . TYR   A 1 186 ? -16.647 10.824  18.062 1.00 85.83  ? 482 TYR   A OH  1 
ATOM   1476 N  N   . ALA   A 1 187 ? -9.481  6.445   18.110 1.00 75.08  ? 483 ALA   A N   1 
ATOM   1477 C  CA  . ALA   A 1 187 ? -8.162  5.840   18.169 1.00 84.68  ? 483 ALA   A CA  1 
ATOM   1478 C  C   . ALA   A 1 187 ? -7.479  6.146   19.493 1.00 89.42  ? 483 ALA   A C   1 
ATOM   1479 O  O   . ALA   A 1 187 ? -7.741  7.165   20.134 1.00 88.88  ? 483 ALA   A O   1 
ATOM   1480 C  CB  . ALA   A 1 187 ? -7.292  6.347   17.017 1.00 91.50  ? 483 ALA   A CB  1 
ATOM   1481 N  N   . GLY   A 1 188 ? -6.581  5.250   19.889 1.00 89.12  ? 484 GLY   A N   1 
ATOM   1482 C  CA  . GLY   A 1 188 ? -5.774  5.457   21.069 1.00 102.72 ? 484 GLY   A CA  1 
ATOM   1483 C  C   . GLY   A 1 188 ? -4.292  5.465   20.774 1.00 107.42 ? 484 GLY   A C   1 
ATOM   1484 O  O   . GLY   A 1 188 ? -3.736  4.465   20.310 1.00 103.64 ? 484 GLY   A O   1 
ATOM   1485 N  N   . TYR   A 1 189 ? -3.641  6.592   21.043 1.00 112.25 ? 485 TYR   A N   1 
ATOM   1486 C  CA  . TYR   A 1 189 ? -2.207  6.737   20.844 1.00 115.05 ? 485 TYR   A CA  1 
ATOM   1487 C  C   . TYR   A 1 189 ? -1.556  6.985   22.194 1.00 122.05 ? 485 TYR   A C   1 
ATOM   1488 O  O   . TYR   A 1 189 ? -1.899  7.950   22.888 1.00 107.75 ? 485 TYR   A O   1 
ATOM   1489 C  CB  . TYR   A 1 189 ? -1.880  7.886   19.887 1.00 120.11 ? 485 TYR   A CB  1 
ATOM   1490 C  CG  . TYR   A 1 189 ? -2.775  7.997   18.674 1.00 112.86 ? 485 TYR   A CG  1 
ATOM   1491 C  CD1 . TYR   A 1 189 ? -3.932  8.763   18.713 1.00 112.20 ? 485 TYR   A CD1 1 
ATOM   1492 C  CD2 . TYR   A 1 189 ? -2.448  7.363   17.482 1.00 116.17 ? 485 TYR   A CD2 1 
ATOM   1493 C  CE1 . TYR   A 1 189 ? -4.747  8.883   17.605 1.00 117.49 ? 485 TYR   A CE1 1 
ATOM   1494 C  CE2 . TYR   A 1 189 ? -3.257  7.480   16.367 1.00 117.55 ? 485 TYR   A CE2 1 
ATOM   1495 C  CZ  . TYR   A 1 189 ? -4.404  8.243   16.432 1.00 116.49 ? 485 TYR   A CZ  1 
ATOM   1496 O  OH  . TYR   A 1 189 ? -5.218  8.367   15.330 1.00 106.74 ? 485 TYR   A OH  1 
ATOM   1497 N  N   . LYS   A 1 190 ? -0.633  6.106   22.567 1.00 131.72 ? 486 LYS   A N   1 
ATOM   1498 C  CA  . LYS   A 1 190 ? 0.247   6.374   23.691 1.00 137.04 ? 486 LYS   A CA  1 
ATOM   1499 C  C   . LYS   A 1 190 ? 1.220   7.493   23.329 1.00 143.38 ? 486 LYS   A C   1 
ATOM   1500 O  O   . LYS   A 1 190 ? 1.588   7.673   22.165 1.00 145.05 ? 486 LYS   A O   1 
ATOM   1501 C  CB  . LYS   A 1 190 ? 1.005   5.104   24.071 1.00 136.74 ? 486 LYS   A CB  1 
ATOM   1502 C  CG  . LYS   A 1 190 ? 1.369   4.265   22.855 1.00 138.57 ? 486 LYS   A CG  1 
ATOM   1503 C  CD  . LYS   A 1 190 ? 2.330   3.141   23.188 1.00 138.46 ? 486 LYS   A CD  1 
ATOM   1504 C  CE  . LYS   A 1 190 ? 1.625   1.974   23.849 1.00 132.66 ? 486 LYS   A CE  1 
ATOM   1505 N  NZ  . LYS   A 1 190 ? 2.451   0.741   23.742 1.00 134.75 ? 486 LYS   A NZ  1 
ATOM   1506 N  N   . GLN   A 1 191 ? 1.631   8.253   24.336 1.00 144.80 ? 487 GLN   A N   1 
ATOM   1507 C  CA  . GLN   A 1 191 ? 2.490   9.407   24.116 1.00 148.18 ? 487 GLN   A CA  1 
ATOM   1508 C  C   . GLN   A 1 191 ? 3.939   9.073   24.436 1.00 150.75 ? 487 GLN   A C   1 
ATOM   1509 O  O   . GLN   A 1 191 ? 4.222   8.103   25.145 1.00 148.62 ? 487 GLN   A O   1 
ATOM   1510 C  CB  . GLN   A 1 191 ? 2.019   10.587  24.975 1.00 148.34 ? 487 GLN   A CB  1 
ATOM   1511 C  CG  . GLN   A 1 191 ? 0.700   11.207  24.519 1.00 148.18 ? 487 GLN   A CG  1 
ATOM   1512 C  CD  . GLN   A 1 191 ? 0.782   11.835  23.129 1.00 156.34 ? 487 GLN   A CD  1 
ATOM   1513 O  OE1 . GLN   A 1 191 ? 0.786   11.138  22.112 1.00 149.65 ? 487 GLN   A OE1 1 
ATOM   1514 N  NE2 . GLN   A 1 191 ? 0.839   13.161  23.086 1.00 165.61 ? 487 GLN   A NE2 1 
ATOM   1515 N  N   . PRO   A 1 192 ? 4.896   9.848   23.911 1.00 156.07 ? 488 PRO   A N   1 
ATOM   1516 C  CA  . PRO   A 1 192 ? 6.304   9.601   24.267 1.00 161.13 ? 488 PRO   A CA  1 
ATOM   1517 C  C   . PRO   A 1 192 ? 6.581   9.749   25.751 1.00 165.88 ? 488 PRO   A C   1 
ATOM   1518 O  O   . PRO   A 1 192 ? 7.540   9.152   26.257 1.00 171.07 ? 488 PRO   A O   1 
ATOM   1519 C  CB  . PRO   A 1 192 ? 7.064   10.648  23.440 1.00 166.75 ? 488 PRO   A CB  1 
ATOM   1520 C  CG  . PRO   A 1 192 ? 6.044   11.685  23.093 1.00 164.95 ? 488 PRO   A CG  1 
ATOM   1521 C  CD  . PRO   A 1 192 ? 4.768   10.929  22.919 1.00 158.47 ? 488 PRO   A CD  1 
ATOM   1522 N  N   . ASP   A 1 193 ? 5.768   10.522  26.467 1.00 162.34 ? 489 ASP   A N   1 
ATOM   1523 C  CA  . ASP   A 1 193 ? 5.897   10.661  27.910 1.00 159.58 ? 489 ASP   A CA  1 
ATOM   1524 C  C   . ASP   A 1 193 ? 5.082   9.629   28.676 1.00 145.85 ? 489 ASP   A C   1 
ATOM   1525 O  O   . ASP   A 1 193 ? 4.990   9.721   29.904 1.00 138.75 ? 489 ASP   A O   1 
ATOM   1526 C  CB  . ASP   A 1 193 ? 5.485   12.068  28.347 1.00 163.42 ? 489 ASP   A CB  1 
ATOM   1527 C  CG  . ASP   A 1 193 ? 4.119   12.461  27.826 1.00 160.32 ? 489 ASP   A CG  1 
ATOM   1528 O  OD1 . ASP   A 1 193 ? 3.956   12.554  26.587 1.00 157.74 ? 489 ASP   A OD1 1 
ATOM   1529 O  OD2 . ASP   A 1 193 ? 3.211   12.668  28.661 1.00 156.17 ? 489 ASP   A OD2 1 
ATOM   1530 N  N   . GLY   A 1 194 ? 4.482   8.660   27.983 1.00 142.96 ? 490 GLY   A N   1 
ATOM   1531 C  CA  . GLY   A 1 194 ? 3.771   7.569   28.601 1.00 144.25 ? 490 GLY   A CA  1 
ATOM   1532 C  C   . GLY   A 1 194 ? 2.260   7.713   28.601 1.00 146.49 ? 490 GLY   A C   1 
ATOM   1533 O  O   . GLY   A 1 194 ? 1.555   6.698   28.540 1.00 149.15 ? 490 GLY   A O   1 
ATOM   1534 N  N   . SER   A 1 195 ? 1.749   8.939   28.665 1.00 145.35 ? 491 SER   A N   1 
ATOM   1535 C  CA  . SER   A 1 195 ? 0.311   9.174   28.753 1.00 139.57 ? 491 SER   A CA  1 
ATOM   1536 C  C   . SER   A 1 195 ? -0.371  8.741   27.451 1.00 138.83 ? 491 SER   A C   1 
ATOM   1537 O  O   . SER   A 1 195 ? 0.240   8.143   26.561 1.00 141.41 ? 491 SER   A O   1 
ATOM   1538 C  CB  . SER   A 1 195 ? 0.039   10.636  29.092 1.00 137.21 ? 491 SER   A CB  1 
ATOM   1539 O  OG  . SER   A 1 195 ? 0.774   11.500  28.245 1.00 140.52 ? 491 SER   A OG  1 
ATOM   1540 N  N   . THR   A 1 196 ? -1.662  9.042   27.322 1.00 132.27 ? 492 THR   A N   1 
ATOM   1541 C  CA  . THR   A 1 196 ? -2.441  8.518   26.207 1.00 121.97 ? 492 THR   A CA  1 
ATOM   1542 C  C   . THR   A 1 196 ? -3.320  9.598   25.594 1.00 122.97 ? 492 THR   A C   1 
ATOM   1543 O  O   . THR   A 1 196 ? -4.026  10.316  26.309 1.00 126.27 ? 492 THR   A O   1 
ATOM   1544 C  CB  . THR   A 1 196 ? -3.305  7.333   26.656 1.00 110.61 ? 492 THR   A CB  1 
ATOM   1545 O  OG1 . THR   A 1 196 ? -2.460  6.273   27.124 1.00 110.89 ? 492 THR   A OG1 1 
ATOM   1546 C  CG2 . THR   A 1 196 ? -4.160  6.824   25.503 1.00 94.10  ? 492 THR   A CG2 1 
ATOM   1547 N  N   . LEU   A 1 197 ? -3.276  9.695   24.267 1.00 118.30 ? 493 LEU   A N   1 
ATOM   1548 C  CA  . LEU   A 1 197 ? -4.175  10.532  23.490 1.00 108.93 ? 493 LEU   A CA  1 
ATOM   1549 C  C   . LEU   A 1 197 ? -5.297  9.680   22.909 1.00 98.27  ? 493 LEU   A C   1 
ATOM   1550 O  O   . LEU   A 1 197 ? -5.096  8.520   22.538 1.00 96.95  ? 493 LEU   A O   1 
ATOM   1551 C  CB  . LEU   A 1 197 ? -3.416  11.250  22.369 1.00 111.48 ? 493 LEU   A CB  1 
ATOM   1552 C  CG  . LEU   A 1 197 ? -4.160  12.244  21.474 1.00 114.45 ? 493 LEU   A CG  1 
ATOM   1553 C  CD1 . LEU   A 1 197 ? -4.953  13.251  22.292 1.00 114.28 ? 493 LEU   A CD1 1 
ATOM   1554 C  CD2 . LEU   A 1 197 ? -3.181  12.957  20.549 1.00 115.95 ? 493 LEU   A CD2 1 
ATOM   1555 N  N   . GLY   A 1 198 ? -6.489  10.260  22.857 1.00 91.92  ? 494 GLY   A N   1 
ATOM   1556 C  CA  . GLY   A 1 198 ? -7.622  9.555   22.284 1.00 99.16  ? 494 GLY   A CA  1 
ATOM   1557 C  C   . GLY   A 1 198 ? -8.223  8.599   23.278 1.00 95.14  ? 494 GLY   A C   1 
ATOM   1558 O  O   . GLY   A 1 198 ? -8.444  8.950   24.442 1.00 104.31 ? 494 GLY   A O   1 
ATOM   1559 N  N   . ASP   A 1 199 ? -8.478  7.372   22.836 1.00 82.84  ? 495 ASP   A N   1 
ATOM   1560 C  CA  . ASP   A 1 199 ? -9.139  6.390   23.690 1.00 74.81  ? 495 ASP   A CA  1 
ATOM   1561 C  C   . ASP   A 1 199 ? -8.137  5.329   24.125 1.00 87.16  ? 495 ASP   A C   1 
ATOM   1562 O  O   . ASP   A 1 199 ? -7.688  4.532   23.288 1.00 84.26  ? 495 ASP   A O   1 
ATOM   1563 C  CB  . ASP   A 1 199 ? -10.322 5.748   22.957 1.00 71.30  ? 495 ASP   A CB  1 
ATOM   1564 C  CG  . ASP   A 1 199 ? -11.274 5.036   23.903 1.00 82.40  ? 495 ASP   A CG  1 
ATOM   1565 O  OD1 . ASP   A 1 199 ? -10.827 4.632   25.007 1.00 80.25  ? 495 ASP   A OD1 1 
ATOM   1566 O  OD2 . ASP   A 1 199 ? -12.468 4.887   23.553 1.00 72.93  ? 495 ASP   A OD2 1 
ATOM   1567 N  N   . PRO   A 1 200 ? -7.759  5.270   25.406 1.00 91.20  ? 496 PRO   A N   1 
ATOM   1568 C  CA  . PRO   A 1 200 ? -6.769  4.268   25.833 1.00 89.43  ? 496 PRO   A CA  1 
ATOM   1569 C  C   . PRO   A 1 200 ? -7.232  2.829   25.653 1.00 78.98  ? 496 PRO   A C   1 
ATOM   1570 O  O   . PRO   A 1 200 ? -6.384  1.933   25.564 1.00 82.90  ? 496 PRO   A O   1 
ATOM   1571 C  CB  . PRO   A 1 200 ? -6.541  4.606   27.313 1.00 95.74  ? 496 PRO   A CB  1 
ATOM   1572 C  CG  . PRO   A 1 200 ? -7.004  6.036   27.466 1.00 95.22  ? 496 PRO   A CG  1 
ATOM   1573 C  CD  . PRO   A 1 200 ? -8.130  6.195   26.491 1.00 89.01  ? 496 PRO   A CD  1 
ATOM   1574 N  N   . ALA   A 1 201 ? -8.542  2.579   25.591 1.00 75.31  ? 497 ALA   A N   1 
ATOM   1575 C  CA  . ALA   A 1 201 ? -9.035  1.224   25.345 1.00 81.77  ? 497 ALA   A CA  1 
ATOM   1576 C  C   . ALA   A 1 201 ? -8.442  0.624   24.073 1.00 85.77  ? 497 ALA   A C   1 
ATOM   1577 O  O   . ALA   A 1 201 ? -8.132  -0.571  24.023 1.00 93.94  ? 497 ALA   A O   1 
ATOM   1578 C  CB  . ALA   A 1 201 ? -10.564 1.232   25.249 1.00 71.00  ? 497 ALA   A CB  1 
ATOM   1579 N  N   . ASN   A 1 202 ? -8.253  1.446   23.047 1.00 86.89  ? 498 ASN   A N   1 
ATOM   1580 C  CA  . ASN   A 1 202 ? -7.967  0.978   21.700 1.00 87.25  ? 498 ASN   A CA  1 
ATOM   1581 C  C   . ASN   A 1 202 ? -6.499  1.089   21.321 1.00 89.73  ? 498 ASN   A C   1 
ATOM   1582 O  O   . ASN   A 1 202 ? -6.169  0.931   20.140 1.00 91.68  ? 498 ASN   A O   1 
ATOM   1583 C  CB  . ASN   A 1 202 ? -8.804  1.768   20.698 1.00 84.91  ? 498 ASN   A CB  1 
ATOM   1584 C  CG  . ASN   A 1 202 ? -10.274 1.775   21.042 1.00 77.90  ? 498 ASN   A CG  1 
ATOM   1585 O  OD1 . ASN   A 1 202 ? -10.872 0.726   21.285 1.00 71.49  ? 498 ASN   A OD1 1 
ATOM   1586 N  ND2 . ASN   A 1 202 ? -10.872 2.966   21.055 1.00 76.23  ? 498 ASN   A ND2 1 
ATOM   1587 N  N   . VAL   A 1 203 ? -5.615  1.369   22.285 1.00 76.93  ? 499 VAL   A N   1 
ATOM   1588 C  CA  . VAL   A 1 203 ? -4.216  1.639   21.954 1.00 80.71  ? 499 VAL   A CA  1 
ATOM   1589 C  C   . VAL   A 1 203 ? -3.601  0.455   21.222 1.00 86.34  ? 499 VAL   A C   1 
ATOM   1590 O  O   . VAL   A 1 203 ? -2.859  0.626   20.245 1.00 101.72 ? 499 VAL   A O   1 
ATOM   1591 C  CB  . VAL   A 1 203 ? -3.413  1.993   23.220 1.00 90.83  ? 499 VAL   A CB  1 
ATOM   1592 C  CG1 . VAL   A 1 203 ? -1.953  2.196   22.863 1.00 104.16 ? 499 VAL   A CG1 1 
ATOM   1593 C  CG2 . VAL   A 1 203 ? -3.972  3.240   23.875 1.00 91.65  ? 499 VAL   A CG2 1 
ATOM   1594 N  N   . GLN   A 1 204 ? -3.917  -0.763  21.664 1.00 74.36  ? 500 GLN   A N   1 
ATOM   1595 C  CA  . GLN   A 1 204 ? -3.387  -1.942  20.989 1.00 86.54  ? 500 GLN   A CA  1 
ATOM   1596 C  C   . GLN   A 1 204 ? -4.005  -2.104  19.607 1.00 90.15  ? 500 GLN   A C   1 
ATOM   1597 O  O   . GLN   A 1 204 ? -3.298  -2.411  18.639 1.00 93.25  ? 500 GLN   A O   1 
ATOM   1598 C  CB  . GLN   A 1 204 ? -3.622  -3.192  21.835 1.00 100.07 ? 500 GLN   A CB  1 
ATOM   1599 C  CG  . GLN   A 1 204 ? -2.566  -4.277  21.648 1.00 109.98 ? 500 GLN   A CG  1 
ATOM   1600 C  CD  . GLN   A 1 204 ? -3.175  -5.639  21.378 1.00 112.37 ? 500 GLN   A CD  1 
ATOM   1601 O  OE1 . GLN   A 1 204 ? -4.165  -5.751  20.654 1.00 118.52 ? 500 GLN   A OE1 1 
ATOM   1602 N  NE2 . GLN   A 1 204 ? -2.588  -6.681  21.958 1.00 110.11 ? 500 GLN   A NE2 1 
ATOM   1603 N  N   . PHE   A 1 205 ? -5.321  -1.893  19.489 1.00 86.27  ? 501 PHE   A N   1 
ATOM   1604 C  CA  . PHE   A 1 205 ? -5.961  -1.966  18.176 1.00 81.52  ? 501 PHE   A CA  1 
ATOM   1605 C  C   . PHE   A 1 205 ? -5.418  -0.888  17.242 1.00 87.68  ? 501 PHE   A C   1 
ATOM   1606 O  O   . PHE   A 1 205 ? -5.079  -1.165  16.085 1.00 91.43  ? 501 PHE   A O   1 
ATOM   1607 C  CB  . PHE   A 1 205 ? -7.481  -1.848  18.304 1.00 70.80  ? 501 PHE   A CB  1 
ATOM   1608 C  CG  . PHE   A 1 205 ? -8.195  -1.910  16.987 1.00 82.78  ? 501 PHE   A CG  1 
ATOM   1609 C  CD1 . PHE   A 1 205 ? -8.368  -3.124  16.339 1.00 89.40  ? 501 PHE   A CD1 1 
ATOM   1610 C  CD2 . PHE   A 1 205 ? -8.674  -0.756  16.378 1.00 88.23  ? 501 PHE   A CD2 1 
ATOM   1611 C  CE1 . PHE   A 1 205 ? -9.013  -3.189  15.106 1.00 88.34  ? 501 PHE   A CE1 1 
ATOM   1612 C  CE2 . PHE   A 1 205 ? -9.324  -0.818  15.148 1.00 88.87  ? 501 PHE   A CE2 1 
ATOM   1613 C  CZ  . PHE   A 1 205 ? -9.488  -2.036  14.514 1.00 86.52  ? 501 PHE   A CZ  1 
ATOM   1614 N  N   . THR   A 1 206 ? -5.337  0.353   17.729 1.00 89.99  ? 502 THR   A N   1 
ATOM   1615 C  CA  . THR   A 1 206 ? -4.768  1.436   16.930 1.00 92.83  ? 502 THR   A CA  1 
ATOM   1616 C  C   . THR   A 1 206 ? -3.371  1.084   16.437 1.00 103.16 ? 502 THR   A C   1 
ATOM   1617 O  O   . THR   A 1 206 ? -3.008  1.400   15.299 1.00 103.39 ? 502 THR   A O   1 
ATOM   1618 C  CB  . THR   A 1 206 ? -4.731  2.734   17.745 1.00 87.49  ? 502 THR   A CB  1 
ATOM   1619 O  OG1 . THR   A 1 206 ? -6.069  3.133   18.069 1.00 89.76  ? 502 THR   A OG1 1 
ATOM   1620 C  CG2 . THR   A 1 206 ? -4.053  3.852   16.967 1.00 86.92  ? 502 THR   A CG2 1 
ATOM   1621 N  N   . GLU   A 1 207 ? -2.572  0.424   17.278 1.00 109.59 ? 503 GLU   A N   1 
ATOM   1622 C  CA  . GLU   A 1 207 ? -1.235  0.033   16.849 1.00 119.44 ? 503 GLU   A CA  1 
ATOM   1623 C  C   . GLU   A 1 207 ? -1.292  -1.070  15.798 1.00 112.76 ? 503 GLU   A C   1 
ATOM   1624 O  O   . GLU   A 1 207 ? -0.435  -1.121  14.908 1.00 113.82 ? 503 GLU   A O   1 
ATOM   1625 C  CB  . GLU   A 1 207 ? -0.396  -0.395  18.057 1.00 125.82 ? 503 GLU   A CB  1 
ATOM   1626 C  CG  . GLU   A 1 207 ? 1.091   -0.568  17.757 1.00 139.62 ? 503 GLU   A CG  1 
ATOM   1627 C  CD  . GLU   A 1 207 ? 1.723   0.669   17.133 1.00 149.76 ? 503 GLU   A CD  1 
ATOM   1628 O  OE1 . GLU   A 1 207 ? 1.351   1.798   17.523 1.00 151.90 ? 503 GLU   A OE1 1 
ATOM   1629 O  OE2 . GLU   A 1 207 ? 2.592   0.512   16.248 1.00 152.84 ? 503 GLU   A OE2 1 
ATOM   1630 N  N   . ILE   A 1 208 ? -2.298  -1.947  15.874 1.00 103.24 ? 504 ILE   A N   1 
ATOM   1631 C  CA  . ILE   A 1 208 ? -2.460  -2.977  14.851 1.00 96.22  ? 504 ILE   A CA  1 
ATOM   1632 C  C   . ILE   A 1 208 ? -2.777  -2.340  13.504 1.00 92.76  ? 504 ILE   A C   1 
ATOM   1633 O  O   . ILE   A 1 208 ? -2.177  -2.694  12.485 1.00 93.85  ? 504 ILE   A O   1 
ATOM   1634 C  CB  . ILE   A 1 208 ? -3.539  -3.993  15.272 1.00 84.82  ? 504 ILE   A CB  1 
ATOM   1635 C  CG1 . ILE   A 1 208 ? -3.026  -4.853  16.434 1.00 82.83  ? 504 ILE   A CG1 1 
ATOM   1636 C  CG2 . ILE   A 1 208 ? -3.932  -4.861  14.086 1.00 76.84  ? 504 ILE   A CG2 1 
ATOM   1637 C  CD1 . ILE   A 1 208 ? -4.120  -5.553  17.224 1.00 88.29  ? 504 ILE   A CD1 1 
ATOM   1638 N  N   . CYS   A 1 209 ? -3.704  -1.376  13.482 1.00 88.03  ? 505 CYS   A N   1 
ATOM   1639 C  CA  . CYS   A 1 209 ? -4.044  -0.702  12.231 1.00 90.46  ? 505 CYS   A CA  1 
ATOM   1640 C  C   . CYS   A 1 209 ? -2.828  -0.024  11.611 1.00 102.17 ? 505 CYS   A C   1 
ATOM   1641 O  O   . CYS   A 1 209 ? -2.659  -0.046  10.383 1.00 101.01 ? 505 CYS   A O   1 
ATOM   1642 C  CB  . CYS   A 1 209 ? -5.164  0.314   12.460 1.00 84.60  ? 505 CYS   A CB  1 
ATOM   1643 S  SG  . CYS   A 1 209 ? -6.739  -0.421  12.968 1.00 85.55  ? 505 CYS   A SG  1 
ATOM   1644 N  N   . ILE   A 1 210 ? -1.964  0.579   12.436 1.00 108.21 ? 506 ILE   A N   1 
ATOM   1645 C  CA  . ILE   A 1 210 ? -0.762  1.202   11.886 1.00 117.99 ? 506 ILE   A CA  1 
ATOM   1646 C  C   . ILE   A 1 210 ? 0.213   0.137   11.391 1.00 121.70 ? 506 ILE   A C   1 
ATOM   1647 O  O   . ILE   A 1 210 ? 0.896   0.323   10.375 1.00 116.07 ? 506 ILE   A O   1 
ATOM   1648 C  CB  . ILE   A 1 210 ? -0.103  2.133   12.918 1.00 115.59 ? 506 ILE   A CB  1 
ATOM   1649 C  CG1 . ILE   A 1 210 ? -1.121  3.118   13.488 1.00 104.83 ? 506 ILE   A CG1 1 
ATOM   1650 C  CG2 . ILE   A 1 210 ? 1.038   2.913   12.271 1.00 126.75 ? 506 ILE   A CG2 1 
ATOM   1651 C  CD1 . ILE   A 1 210 ? -0.548  3.987   14.590 1.00 115.72 ? 506 ILE   A CD1 1 
ATOM   1652 N  N   . GLN   A 1 211 ? 0.291   -0.997  12.098 1.00 121.21 ? 507 GLN   A N   1 
ATOM   1653 C  CA  . GLN   A 1 211 ? 1.113   -2.115  11.645 1.00 123.62 ? 507 GLN   A CA  1 
ATOM   1654 C  C   . GLN   A 1 211 ? 0.639   -2.675  10.308 1.00 119.41 ? 507 GLN   A C   1 
ATOM   1655 O  O   . GLN   A 1 211 ? 1.425   -3.328  9.610  1.00 124.30 ? 507 GLN   A O   1 
ATOM   1656 C  CB  . GLN   A 1 211 ? 1.125   -3.223  12.705 1.00 125.72 ? 507 GLN   A CB  1 
ATOM   1657 C  CG  . GLN   A 1 211 ? 2.099   -2.983  13.857 1.00 131.18 ? 507 GLN   A CG  1 
ATOM   1658 C  CD  . GLN   A 1 211 ? 3.322   -3.887  13.787 1.00 136.18 ? 507 GLN   A CD  1 
ATOM   1659 O  OE1 . GLN   A 1 211 ? 3.283   -4.949  13.163 1.00 137.28 ? 507 GLN   A OE1 1 
ATOM   1660 N  NE2 . GLN   A 1 211 ? 4.415   -3.467  14.425 1.00 137.48 ? 507 GLN   A NE2 1 
ATOM   1661 N  N   . GLN   A 1 212 ? -0.624  -2.442  9.940  1.00 110.47 ? 508 GLN   A N   1 
ATOM   1662 C  CA  . GLN   A 1 212 ? -1.148  -2.789  8.622  1.00 104.37 ? 508 GLN   A CA  1 
ATOM   1663 C  C   . GLN   A 1 212 ? -1.204  -1.586  7.685  1.00 104.35 ? 508 GLN   A C   1 
ATOM   1664 O  O   . GLN   A 1 212 ? -1.839  -1.656  6.626  1.00 102.59 ? 508 GLN   A O   1 
ATOM   1665 C  CB  . GLN   A 1 212 ? -2.535  -3.425  8.746  1.00 95.04  ? 508 GLN   A CB  1 
ATOM   1666 C  CG  . GLN   A 1 212 ? -2.573  -4.683  9.603  1.00 105.31 ? 508 GLN   A CG  1 
ATOM   1667 C  CD  . GLN   A 1 212 ? -1.823  -5.837  8.975  1.00 117.29 ? 508 GLN   A CD  1 
ATOM   1668 O  OE1 . GLN   A 1 212 ? -2.381  -6.589  8.172  1.00 114.84 ? 508 GLN   A OE1 1 
ATOM   1669 N  NE2 . GLN   A 1 212 ? -0.549  -5.984  9.334  1.00 125.76 ? 508 GLN   A NE2 1 
ATOM   1670 N  N   . GLY   A 1 213 ? -0.568  -0.481  8.060  1.00 110.12 ? 509 GLY   A N   1 
ATOM   1671 C  CA  . GLY   A 1 213 ? -0.412  0.647   7.168  1.00 110.68 ? 509 GLY   A CA  1 
ATOM   1672 C  C   . GLY   A 1 213 ? -1.306  1.842   7.414  1.00 110.28 ? 509 GLY   A C   1 
ATOM   1673 O  O   . GLY   A 1 213 ? -1.307  2.759   6.588  1.00 102.47 ? 509 GLY   A O   1 
ATOM   1674 N  N   . TRP   A 1 214 ? -2.057  1.876   8.515  1.00 118.77 ? 510 TRP   A N   1 
ATOM   1675 C  CA  . TRP   A 1 214 ? -2.916  3.028   8.762  1.00 116.73 ? 510 TRP   A CA  1 
ATOM   1676 C  C   . TRP   A 1 214 ? -2.063  4.268   8.975  1.00 120.14 ? 510 TRP   A C   1 
ATOM   1677 O  O   . TRP   A 1 214 ? -1.069  4.239   9.708  1.00 117.79 ? 510 TRP   A O   1 
ATOM   1678 C  CB  . TRP   A 1 214 ? -3.829  2.809   9.970  1.00 107.24 ? 510 TRP   A CB  1 
ATOM   1679 C  CG  . TRP   A 1 214 ? -4.921  3.852   10.062 1.00 101.81 ? 510 TRP   A CG  1 
ATOM   1680 C  CD1 . TRP   A 1 214 ? -5.774  4.218   9.068  1.00 100.85 ? 510 TRP   A CD1 1 
ATOM   1681 C  CD2 . TRP   A 1 214 ? -5.269  4.660   11.201 1.00 105.64 ? 510 TRP   A CD2 1 
ATOM   1682 N  NE1 . TRP   A 1 214 ? -6.633  5.193   9.508  1.00 99.51  ? 510 TRP   A NE1 1 
ATOM   1683 C  CE2 . TRP   A 1 214 ? -6.344  5.485   10.814 1.00 103.33 ? 510 TRP   A CE2 1 
ATOM   1684 C  CE3 . TRP   A 1 214 ? -4.777  4.764   12.508 1.00 107.11 ? 510 TRP   A CE3 1 
ATOM   1685 C  CZ2 . TRP   A 1 214 ? -6.938  6.402   11.682 1.00 103.12 ? 510 TRP   A CZ2 1 
ATOM   1686 C  CZ3 . TRP   A 1 214 ? -5.369  5.677   13.374 1.00 103.21 ? 510 TRP   A CZ3 1 
ATOM   1687 C  CH2 . TRP   A 1 214 ? -6.438  6.481   12.957 1.00 104.20 ? 510 TRP   A CH2 1 
ATOM   1688 N  N   . LYS   A 1 215 ? -2.447  5.352   8.315  1.00 122.78 ? 511 LYS   A N   1 
ATOM   1689 C  CA  . LYS   A 1 215 ? -1.786  6.641   8.464  1.00 128.16 ? 511 LYS   A CA  1 
ATOM   1690 C  C   . LYS   A 1 215 ? -2.554  7.406   9.535  1.00 123.21 ? 511 LYS   A C   1 
ATOM   1691 O  O   . LYS   A 1 215 ? -3.618  7.973   9.274  1.00 119.34 ? 511 LYS   A O   1 
ATOM   1692 C  CB  . LYS   A 1 215 ? -1.737  7.372   7.130  1.00 130.08 ? 511 LYS   A CB  1 
ATOM   1693 C  CG  . LYS   A 1 215 ? -0.991  6.598   6.041  1.00 137.96 ? 511 LYS   A CG  1 
ATOM   1694 C  CD  . LYS   A 1 215 ? 0.528   6.769   6.144  1.00 145.80 ? 511 LYS   A CD  1 
ATOM   1695 C  CE  . LYS   A 1 215 ? 1.195   5.687   6.987  1.00 143.14 ? 511 LYS   A CE  1 
ATOM   1696 N  NZ  . LYS   A 1 215 ? 2.576   6.079   7.393  1.00 149.24 ? 511 LYS   A NZ  1 
ATOM   1697 N  N   . ALA   A 1 216 ? -2.014  7.405   10.743 1.00 120.90 ? 512 ALA   A N   1 
ATOM   1698 C  CA  . ALA   A 1 216 ? -2.745  7.896   11.900 1.00 114.24 ? 512 ALA   A CA  1 
ATOM   1699 C  C   . ALA   A 1 216 ? -2.704  9.418   11.948 1.00 114.44 ? 512 ALA   A C   1 
ATOM   1700 O  O   . ALA   A 1 216 ? -1.613  9.999   11.908 1.00 121.40 ? 512 ALA   A O   1 
ATOM   1701 C  CB  . ALA   A 1 216 ? -2.159  7.311   13.174 1.00 111.37 ? 512 ALA   A CB  1 
ATOM   1702 N  N   . PRO   A 1 217 ? -3.854  10.098  12.014 1.00 107.98 ? 513 PRO   A N   1 
ATOM   1703 C  CA  . PRO   A 1 217 ? -3.841  11.552  12.227 1.00 114.26 ? 513 PRO   A CA  1 
ATOM   1704 C  C   . PRO   A 1 217 ? -3.566  11.951  13.670 1.00 131.34 ? 513 PRO   A C   1 
ATOM   1705 O  O   . PRO   A 1 217 ? -4.045  13.002  14.109 1.00 136.19 ? 513 PRO   A O   1 
ATOM   1706 C  CB  . PRO   A 1 217 ? -5.248  11.986  11.789 1.00 108.41 ? 513 PRO   A CB  1 
ATOM   1707 C  CG  . PRO   A 1 217 ? -6.083  10.759  11.868 1.00 100.29 ? 513 PRO   A CG  1 
ATOM   1708 C  CD  . PRO   A 1 217 ? -5.176  9.605   11.590 1.00 100.55 ? 513 PRO   A CD  1 
ATOM   1709 N  N   . ARG   A 1 218 ? -2.785  11.126  14.386 1.00 137.95 ? 514 ARG   A N   1 
ATOM   1710 C  CA  . ARG   A 1 218 ? -2.433  11.243  15.804 1.00 133.10 ? 514 ARG   A CA  1 
ATOM   1711 C  C   . ARG   A 1 218 ? -3.154  12.377  16.525 1.00 128.95 ? 514 ARG   A C   1 
ATOM   1712 O  O   . ARG   A 1 218 ? -2.549  13.401  16.859 1.00 141.84 ? 514 ARG   A O   1 
ATOM   1713 C  CB  . ARG   A 1 218 ? -0.916  11.405  15.961 1.00 140.07 ? 514 ARG   A CB  1 
ATOM   1714 C  CG  . ARG   A 1 218 ? -0.411  11.229  17.397 1.00 143.02 ? 514 ARG   A CG  1 
ATOM   1715 C  CD  . ARG   A 1 218 ? 0.694   10.187  17.489 1.00 144.59 ? 514 ARG   A CD  1 
ATOM   1716 N  NE  . ARG   A 1 218 ? 0.747   9.339   16.300 1.00 145.17 ? 514 ARG   A NE  1 
ATOM   1717 C  CZ  . ARG   A 1 218 ? 1.219   8.097   16.291 1.00 142.67 ? 514 ARG   A CZ  1 
ATOM   1718 N  NH1 . ARG   A 1 218 ? 1.236   7.401   15.165 1.00 139.63 ? 514 ARG   A NH1 1 
ATOM   1719 N  NH2 . ARG   A 1 218 ? 1.662   7.547   17.413 1.00 146.54 ? 514 ARG   A NH2 1 
ATOM   1720 N  N   . GLY   A 1 219 ? -4.456  12.207  16.740 1.00 115.48 ? 515 GLY   A N   1 
ATOM   1721 C  CA  . GLY   A 1 219 ? -5.253  13.181  17.455 1.00 116.03 ? 515 GLY   A CA  1 
ATOM   1722 C  C   . GLY   A 1 219 ? -6.119  12.537  18.520 1.00 115.25 ? 515 GLY   A C   1 
ATOM   1723 O  O   . GLY   A 1 219 ? -5.867  11.401  18.937 1.00 107.81 ? 515 GLY   A O   1 
ATOM   1724 N  N   . ARG   A 1 220 ? -7.146  13.255  18.969 1.00 118.82 ? 516 ARG   A N   1 
ATOM   1725 C  CA  . ARG   A 1 220 ? -8.114  12.724  19.921 1.00 117.63 ? 516 ARG   A CA  1 
ATOM   1726 C  C   . ARG   A 1 220 ? -9.116  11.801  19.247 1.00 120.02 ? 516 ARG   A C   1 
ATOM   1727 O  O   . ARG   A 1 220 ? -8.911  10.584  19.151 1.00 125.23 ? 516 ARG   A O   1 
ATOM   1728 C  CB  . ARG   A 1 220 ? -8.880  13.863  20.585 1.00 116.02 ? 516 ARG   A CB  1 
ATOM   1729 C  CG  . ARG   A 1 220 ? -9.302  13.582  21.997 1.00 111.02 ? 516 ARG   A CG  1 
ATOM   1730 C  CD  . ARG   A 1 220 ? -8.348  14.284  22.933 1.00 113.10 ? 516 ARG   A CD  1 
ATOM   1731 N  NE  . ARG   A 1 220 ? -9.015  14.735  24.140 1.00 116.91 ? 516 ARG   A NE  1 
ATOM   1732 C  CZ  . ARG   A 1 220 ? -8.915  14.122  25.311 1.00 109.97 ? 516 ARG   A CZ  1 
ATOM   1733 N  NH1 . ARG   A 1 220 ? -8.163  13.034  25.426 1.00 102.97 ? 516 ARG   A NH1 1 
ATOM   1734 N  NH2 . ARG   A 1 220 ? -9.560  14.606  26.363 1.00 111.64 ? 516 ARG   A NH2 1 
ATOM   1735 N  N   . PHE   A 1 221 ? -10.205 12.405  18.771 1.00 111.49 ? 517 PHE   A N   1 
ATOM   1736 C  CA  . PHE   A 1 221 ? -11.361 11.687  18.247 1.00 92.76  ? 517 PHE   A CA  1 
ATOM   1737 C  C   . PHE   A 1 221 ? -11.181 11.394  16.752 1.00 103.17 ? 517 PHE   A C   1 
ATOM   1738 O  O   . PHE   A 1 221 ? -11.925 11.859  15.884 1.00 97.55  ? 517 PHE   A O   1 
ATOM   1739 C  CB  . PHE   A 1 221 ? -12.626 12.490  18.529 1.00 86.29  ? 517 PHE   A CB  1 
ATOM   1740 C  CG  . PHE   A 1 221 ? -12.745 12.961  19.962 1.00 94.47  ? 517 PHE   A CG  1 
ATOM   1741 C  CD1 . PHE   A 1 221 ? -12.605 14.301  20.284 1.00 96.03  ? 517 PHE   A CD1 1 
ATOM   1742 C  CD2 . PHE   A 1 221 ? -12.985 12.064  20.979 1.00 71.91  ? 517 PHE   A CD2 1 
ATOM   1743 C  CE1 . PHE   A 1 221 ? -12.716 14.739  21.596 1.00 97.31  ? 517 PHE   A CE1 1 
ATOM   1744 C  CE2 . PHE   A 1 221 ? -13.113 12.499  22.299 1.00 84.91  ? 517 PHE   A CE2 1 
ATOM   1745 C  CZ  . PHE   A 1 221 ? -12.968 13.837  22.609 1.00 77.01  ? 517 PHE   A CZ  1 
ATOM   1746 N  N   . ASP   A 1 222 ? -10.142 10.614  16.466 1.00 106.52 ? 518 ASP   A N   1 
ATOM   1747 C  CA  . ASP   A 1 222 ? -9.881  10.105  15.128 1.00 97.32  ? 518 ASP   A CA  1 
ATOM   1748 C  C   . ASP   A 1 222 ? -10.600 8.773   14.985 1.00 96.01  ? 518 ASP   A C   1 
ATOM   1749 O  O   . ASP   A 1 222 ? -10.272 7.809   15.691 1.00 83.22  ? 518 ASP   A O   1 
ATOM   1750 C  CB  . ASP   A 1 222 ? -8.381  9.932   14.898 1.00 94.79  ? 518 ASP   A CB  1 
ATOM   1751 C  CG  . ASP   A 1 222 ? -7.584  11.165  15.283 1.00 98.03  ? 518 ASP   A CG  1 
ATOM   1752 O  OD1 . ASP   A 1 222 ? -8.199  12.210  15.601 1.00 105.98 ? 518 ASP   A OD1 1 
ATOM   1753 O  OD2 . ASP   A 1 222 ? -6.334  11.086  15.269 1.00 93.81  ? 518 ASP   A OD2 1 
ATOM   1754 N  N   . VAL   A 1 223 ? -11.596 8.725   14.100 1.00 94.85  ? 519 VAL   A N   1 
ATOM   1755 C  CA  . VAL   A 1 223 ? -12.330 7.485   13.897 1.00 87.66  ? 519 VAL   A CA  1 
ATOM   1756 C  C   . VAL   A 1 223 ? -11.391 6.455   13.288 1.00 80.73  ? 519 VAL   A C   1 
ATOM   1757 O  O   . VAL   A 1 223 ? -10.626 6.757   12.364 1.00 79.86  ? 519 VAL   A O   1 
ATOM   1758 C  CB  . VAL   A 1 223 ? -13.563 7.712   13.012 1.00 82.72  ? 519 VAL   A CB  1 
ATOM   1759 C  CG1 . VAL   A 1 223 ? -14.451 6.483   13.051 1.00 70.16  ? 519 VAL   A CG1 1 
ATOM   1760 C  CG2 . VAL   A 1 223 ? -14.327 8.957   13.452 1.00 89.20  ? 519 VAL   A CG2 1 
ATOM   1761 N  N   . LEU   A 1 224 ? -11.420 5.247   13.828 1.00 82.31  ? 520 LEU   A N   1 
ATOM   1762 C  CA  . LEU   A 1 224 ? -10.518 4.207   13.390 1.00 79.17  ? 520 LEU   A CA  1 
ATOM   1763 C  C   . LEU   A 1 224 ? -10.979 3.635   12.056 1.00 78.00  ? 520 LEU   A C   1 
ATOM   1764 O  O   . LEU   A 1 224 ? -12.156 3.721   11.706 1.00 80.32  ? 520 LEU   A O   1 
ATOM   1765 C  CB  . LEU   A 1 224 ? -10.452 3.097   14.436 1.00 62.21  ? 520 LEU   A CB  1 
ATOM   1766 C  CG  . LEU   A 1 224 ? -9.711  3.455   15.727 1.00 70.89  ? 520 LEU   A CG  1 
ATOM   1767 C  CD1 . LEU   A 1 224 ? -10.341 2.693   16.871 1.00 57.53  ? 520 LEU   A CD1 1 
ATOM   1768 C  CD2 . LEU   A 1 224 ? -8.222  3.138   15.618 1.00 73.80  ? 520 LEU   A CD2 1 
ATOM   1769 N  N   . PRO   A 1 225 ? -10.068 3.048   11.289 1.00 85.00  ? 521 PRO   A N   1 
ATOM   1770 C  CA  . PRO   A 1 225 ? -10.483 2.340   10.082 1.00 85.63  ? 521 PRO   A CA  1 
ATOM   1771 C  C   . PRO   A 1 225 ? -10.988 0.952   10.425 1.00 84.06  ? 521 PRO   A C   1 
ATOM   1772 O  O   . PRO   A 1 225 ? -10.574 0.340   11.412 1.00 85.00  ? 521 PRO   A O   1 
ATOM   1773 C  CB  . PRO   A 1 225 ? -9.193  2.272   9.258  1.00 86.43  ? 521 PRO   A CB  1 
ATOM   1774 C  CG  . PRO   A 1 225 ? -8.129  2.193   10.296 1.00 89.65  ? 521 PRO   A CG  1 
ATOM   1775 C  CD  . PRO   A 1 225 ? -8.602  3.052   11.439 1.00 90.35  ? 521 PRO   A CD  1 
ATOM   1776 N  N   . LEU   A 1 226 ? -11.913 0.472   9.602  1.00 76.42  ? 522 LEU   A N   1 
ATOM   1777 C  CA  . LEU   A 1 226 ? -12.369 -0.904  9.710  1.00 72.47  ? 522 LEU   A CA  1 
ATOM   1778 C  C   . LEU   A 1 226 ? -11.237 -1.856  9.345  1.00 76.40  ? 522 LEU   A C   1 
ATOM   1779 O  O   . LEU   A 1 226 ? -10.535 -1.645  8.352  1.00 81.65  ? 522 LEU   A O   1 
ATOM   1780 C  CB  . LEU   A 1 226 ? -13.568 -1.134  8.792  1.00 69.81  ? 522 LEU   A CB  1 
ATOM   1781 C  CG  . LEU   A 1 226 ? -14.867 -0.389  9.112  1.00 67.78  ? 522 LEU   A CG  1 
ATOM   1782 C  CD1 . LEU   A 1 226 ? -15.837 -0.502  7.941  1.00 65.49  ? 522 LEU   A CD1 1 
ATOM   1783 C  CD2 . LEU   A 1 226 ? -15.512 -0.927  10.406 1.00 58.35  ? 522 LEU   A CD2 1 
ATOM   1784 N  N   . LEU   A 1 227 ? -11.044 -2.895  10.156 1.00 72.95  ? 523 LEU   A N   1 
ATOM   1785 C  CA  . LEU   A 1 227 ? -10.092 -3.963  9.849  1.00 73.97  ? 523 LEU   A CA  1 
ATOM   1786 C  C   . LEU   A 1 227 ? -10.899 -5.238  9.634  1.00 73.85  ? 523 LEU   A C   1 
ATOM   1787 O  O   . LEU   A 1 227 ? -11.333 -5.879  10.593 1.00 68.30  ? 523 LEU   A O   1 
ATOM   1788 C  CB  . LEU   A 1 227 ? -9.066  -4.138  10.959 1.00 69.52  ? 523 LEU   A CB  1 
ATOM   1789 C  CG  . LEU   A 1 227 ? -7.587  -4.171  10.565 1.00 80.02  ? 523 LEU   A CG  1 
ATOM   1790 C  CD1 . LEU   A 1 227 ? -6.835  -5.131  11.483 1.00 79.23  ? 523 LEU   A CD1 1 
ATOM   1791 C  CD2 . LEU   A 1 227 ? -7.364  -4.528  9.102  1.00 79.23  ? 523 LEU   A CD2 1 
ATOM   1792 N  N   . LEU   A 1 228 ? -11.080 -5.618  8.376  1.00 65.14  ? 524 LEU   A N   1 
ATOM   1793 C  CA  . LEU   A 1 228 ? -12.038 -6.648  8.004  1.00 64.10  ? 524 LEU   A CA  1 
ATOM   1794 C  C   . LEU   A 1 228 ? -11.304 -7.873  7.486  1.00 67.37  ? 524 LEU   A C   1 
ATOM   1795 O  O   . LEU   A 1 228 ? -10.551 -7.782  6.510  1.00 59.23  ? 524 LEU   A O   1 
ATOM   1796 C  CB  . LEU   A 1 228 ? -13.007 -6.111  6.953  1.00 58.76  ? 524 LEU   A CB  1 
ATOM   1797 C  CG  . LEU   A 1 228 ? -13.676 -4.821  7.431  1.00 59.78  ? 524 LEU   A CG  1 
ATOM   1798 C  CD1 . LEU   A 1 228 ? -14.676 -4.341  6.402  1.00 65.78  ? 524 LEU   A CD1 1 
ATOM   1799 C  CD2 . LEU   A 1 228 ? -14.341 -5.030  8.771  1.00 54.05  ? 524 LEU   A CD2 1 
ATOM   1800 N  N   . GLN   A 1 229 ? -11.526 -9.008  8.141  1.00 70.42  ? 525 GLN   A N   1 
ATOM   1801 C  CA  . GLN   A 1 229 ? -11.010 -10.299 7.710  1.00 75.54  ? 525 GLN   A CA  1 
ATOM   1802 C  C   . GLN   A 1 229 ? -12.148 -11.106 7.094  1.00 73.74  ? 525 GLN   A C   1 
ATOM   1803 O  O   . GLN   A 1 229 ? -13.195 -11.299 7.724  1.00 68.96  ? 525 GLN   A O   1 
ATOM   1804 C  CB  . GLN   A 1 229 ? -10.387 -11.047 8.891  1.00 73.74  ? 525 GLN   A CB  1 
ATOM   1805 C  CG  . GLN   A 1 229 ? -10.459 -12.558 8.794  1.00 75.99  ? 525 GLN   A CG  1 
ATOM   1806 C  CD  . GLN   A 1 229 ? -10.006 -13.247 10.064 1.00 91.90  ? 525 GLN   A CD  1 
ATOM   1807 O  OE1 . GLN   A 1 229 ? -9.412  -12.625 10.947 1.00 97.49  ? 525 GLN   A OE1 1 
ATOM   1808 N  NE2 . GLN   A 1 229 ? -10.293 -14.538 10.167 1.00 98.85  ? 525 GLN   A NE2 1 
ATOM   1809 N  N   . ALA   A 1 230 ? -11.944 -11.561 5.862  1.00 66.28  ? 526 ALA   A N   1 
ATOM   1810 C  CA  . ALA   A 1 230 ? -12.958 -12.278 5.100  1.00 59.24  ? 526 ALA   A CA  1 
ATOM   1811 C  C   . ALA   A 1 230 ? -12.477 -13.696 4.836  1.00 68.26  ? 526 ALA   A C   1 
ATOM   1812 O  O   . ALA   A 1 230 ? -11.360 -13.892 4.343  1.00 69.61  ? 526 ALA   A O   1 
ATOM   1813 C  CB  . ALA   A 1 230 ? -13.254 -11.558 3.777  1.00 62.60  ? 526 ALA   A CB  1 
ATOM   1814 N  N   . ASN   A 1 231 ? -13.314 -14.673 5.192  1.00 74.24  ? 527 ASN   A N   1 
ATOM   1815 C  CA  . ASN   A 1 231 ? -13.088 -16.093 4.907  1.00 79.48  ? 527 ASN   A CA  1 
ATOM   1816 C  C   . ASN   A 1 231 ? -11.685 -16.539 5.314  1.00 77.66  ? 527 ASN   A C   1 
ATOM   1817 O  O   . ASN   A 1 231 ? -11.006 -17.287 4.601  1.00 78.97  ? 527 ASN   A O   1 
ATOM   1818 C  CB  . ASN   A 1 231 ? -13.354 -16.410 3.437  1.00 86.79  ? 527 ASN   A CB  1 
ATOM   1819 C  CG  . ASN   A 1 231 ? -13.579 -17.892 3.197  1.00 91.71  ? 527 ASN   A CG  1 
ATOM   1820 O  OD1 . ASN   A 1 231 ? -14.274 -18.552 3.967  1.00 92.25  ? 527 ASN   A OD1 1 
ATOM   1821 N  ND2 . ASN   A 1 231 ? -12.979 -18.423 2.140  1.00 101.73 ? 527 ASN   A ND2 1 
ATOM   1822 N  N   . GLY   A 1 232 ? -11.255 -16.074 6.488  1.00 74.39  ? 528 GLY   A N   1 
ATOM   1823 C  CA  . GLY   A 1 232 ? -9.983  -16.457 7.057  1.00 71.14  ? 528 GLY   A CA  1 
ATOM   1824 C  C   . GLY   A 1 232 ? -8.782  -15.696 6.545  1.00 81.30  ? 528 GLY   A C   1 
ATOM   1825 O  O   . GLY   A 1 232 ? -7.723  -15.749 7.180  1.00 88.50  ? 528 GLY   A O   1 
ATOM   1826 N  N   . ASN   A 1 233 ? -8.902  -14.993 5.419  1.00 81.63  ? 529 ASN   A N   1 
ATOM   1827 C  CA  . ASN   A 1 233 ? -7.773  -14.257 4.872  1.00 85.26  ? 529 ASN   A CA  1 
ATOM   1828 C  C   . ASN   A 1 233 ? -7.347  -13.141 5.828  1.00 88.03  ? 529 ASN   A C   1 
ATOM   1829 O  O   . ASN   A 1 233 ? -8.039  -12.804 6.793  1.00 90.48  ? 529 ASN   A O   1 
ATOM   1830 C  CB  . ASN   A 1 233 ? -8.122  -13.681 3.498  1.00 82.01  ? 529 ASN   A CB  1 
ATOM   1831 C  CG  . ASN   A 1 233 ? -8.638  -14.733 2.539  1.00 84.39  ? 529 ASN   A CG  1 
ATOM   1832 O  OD1 . ASN   A 1 233 ? -8.015  -15.776 2.342  1.00 85.78  ? 529 ASN   A OD1 1 
ATOM   1833 N  ND2 . ASN   A 1 233 ? -9.792  -14.465 1.941  1.00 79.54  ? 529 ASN   A ND2 1 
ATOM   1834 N  N   . ASP   A 1 234 ? -6.177  -12.578 5.557  1.00 91.39  ? 530 ASP   A N   1 
ATOM   1835 C  CA  . ASP   A 1 234 ? -5.665  -11.515 6.404  1.00 101.34 ? 530 ASP   A CA  1 
ATOM   1836 C  C   . ASP   A 1 234 ? -6.552  -10.277 6.283  1.00 101.54 ? 530 ASP   A C   1 
ATOM   1837 O  O   . ASP   A 1 234 ? -7.045  -9.969  5.194  1.00 107.50 ? 530 ASP   A O   1 
ATOM   1838 C  CB  . ASP   A 1 234 ? -4.222  -11.182 6.025  1.00 108.82 ? 530 ASP   A CB  1 
ATOM   1839 C  CG  . ASP   A 1 234 ? -3.316  -12.402 6.052  1.00 111.72 ? 530 ASP   A CG  1 
ATOM   1840 O  OD1 . ASP   A 1 234 ? -2.260  -12.371 5.387  1.00 113.39 ? 530 ASP   A OD1 1 
ATOM   1841 O  OD2 . ASP   A 1 234 ? -3.663  -13.398 6.727  1.00 110.30 ? 530 ASP   A OD2 1 
ATOM   1842 N  N   . PRO   A 1 235 ? -6.788  -9.559  7.378  1.00 95.33  ? 531 PRO   A N   1 
ATOM   1843 C  CA  . PRO   A 1 235 ? -7.720  -8.429  7.326  1.00 89.03  ? 531 PRO   A CA  1 
ATOM   1844 C  C   . PRO   A 1 235 ? -7.128  -7.234  6.597  1.00 89.75  ? 531 PRO   A C   1 
ATOM   1845 O  O   . PRO   A 1 235 ? -5.908  -7.067  6.514  1.00 97.91  ? 531 PRO   A O   1 
ATOM   1846 C  CB  . PRO   A 1 235 ? -7.966  -8.113  8.804  1.00 89.57  ? 531 PRO   A CB  1 
ATOM   1847 C  CG  . PRO   A 1 235 ? -6.689  -8.504  9.455  1.00 93.76  ? 531 PRO   A CG  1 
ATOM   1848 C  CD  . PRO   A 1 235 ? -6.237  -9.748  8.730  1.00 94.65  ? 531 PRO   A CD  1 
ATOM   1849 N  N   . GLU   A 1 236 ? -8.018  -6.392  6.069  1.00 83.93  ? 532 GLU   A N   1 
ATOM   1850 C  CA  . GLU   A 1 236 ? -7.643  -5.266  5.223  1.00 78.81  ? 532 GLU   A CA  1 
ATOM   1851 C  C   . GLU   A 1 236 ? -8.307  -3.990  5.725  1.00 69.33  ? 532 GLU   A C   1 
ATOM   1852 O  O   . GLU   A 1 236 ? -9.441  -4.006  6.204  1.00 64.48  ? 532 GLU   A O   1 
ATOM   1853 C  CB  . GLU   A 1 236 ? -8.039  -5.517  3.761  1.00 78.82  ? 532 GLU   A CB  1 
ATOM   1854 C  CG  . GLU   A 1 236 ? -7.615  -6.877  3.233  1.00 78.65  ? 532 GLU   A CG  1 
ATOM   1855 C  CD  . GLU   A 1 236 ? -8.515  -7.366  2.115  1.00 81.02  ? 532 GLU   A CD  1 
ATOM   1856 O  OE1 . GLU   A 1 236 ? -8.904  -6.539  1.262  1.00 77.85  ? 532 GLU   A OE1 1 
ATOM   1857 O  OE2 . GLU   A 1 236 ? -8.847  -8.571  2.096  1.00 79.90  ? 532 GLU   A OE2 1 
ATOM   1858 N  N   . LEU   A 1 237 ? -7.591  -2.877  5.598  1.00 73.75  ? 533 LEU   A N   1 
ATOM   1859 C  CA  . LEU   A 1 237 ? -8.068  -1.600  6.114  1.00 71.88  ? 533 LEU   A CA  1 
ATOM   1860 C  C   . LEU   A 1 237 ? -9.053  -0.930  5.162  1.00 79.81  ? 533 LEU   A C   1 
ATOM   1861 O  O   . LEU   A 1 237 ? -8.855  -0.915  3.942  1.00 82.03  ? 533 LEU   A O   1 
ATOM   1862 C  CB  . LEU   A 1 237 ? -6.889  -0.663  6.358  1.00 70.14  ? 533 LEU   A CB  1 
ATOM   1863 C  CG  . LEU   A 1 237 ? -6.071  -1.023  7.598  1.00 74.70  ? 533 LEU   A CG  1 
ATOM   1864 C  CD1 . LEU   A 1 237 ? -4.846  -0.133  7.718  1.00 80.92  ? 533 LEU   A CD1 1 
ATOM   1865 C  CD2 . LEU   A 1 237 ? -6.951  -0.912  8.841  1.00 77.33  ? 533 LEU   A CD2 1 
ATOM   1866 N  N   . PHE   A 1 238 ? -10.113 -0.360  5.733  1.00 71.59  ? 534 PHE   A N   1 
ATOM   1867 C  CA  . PHE   A 1 238 ? -11.031 0.494   4.993  1.00 75.12  ? 534 PHE   A CA  1 
ATOM   1868 C  C   . PHE   A 1 238 ? -11.495 1.611   5.914  1.00 85.59  ? 534 PHE   A C   1 
ATOM   1869 O  O   . PHE   A 1 238 ? -11.795 1.372   7.088  1.00 81.99  ? 534 PHE   A O   1 
ATOM   1870 C  CB  . PHE   A 1 238 ? -12.257 -0.261  4.469  1.00 66.86  ? 534 PHE   A CB  1 
ATOM   1871 C  CG  . PHE   A 1 238 ? -11.945 -1.574  3.816  1.00 72.30  ? 534 PHE   A CG  1 
ATOM   1872 C  CD1 . PHE   A 1 238 ? -11.800 -2.731  4.578  1.00 70.78  ? 534 PHE   A CD1 1 
ATOM   1873 C  CD2 . PHE   A 1 238 ? -11.828 -1.659  2.435  1.00 66.61  ? 534 PHE   A CD2 1 
ATOM   1874 C  CE1 . PHE   A 1 238 ? -11.523 -3.943  3.974  1.00 77.47  ? 534 PHE   A CE1 1 
ATOM   1875 C  CE2 . PHE   A 1 238 ? -11.558 -2.870  1.820  1.00 68.23  ? 534 PHE   A CE2 1 
ATOM   1876 C  CZ  . PHE   A 1 238 ? -11.401 -4.010  2.572  1.00 64.90  ? 534 PHE   A CZ  1 
ATOM   1877 N  N   . GLN   A 1 239 ? -11.564 2.824   5.373  1.00 89.63  ? 535 GLN   A N   1 
ATOM   1878 C  CA  . GLN   A 1 239 ? -12.061 3.980   6.108  1.00 89.97  ? 535 GLN   A CA  1 
ATOM   1879 C  C   . GLN   A 1 239 ? -13.506 4.254   5.707  1.00 83.44  ? 535 GLN   A C   1 
ATOM   1880 O  O   . GLN   A 1 239 ? -13.794 4.509   4.532  1.00 77.32  ? 535 GLN   A O   1 
ATOM   1881 C  CB  . GLN   A 1 239 ? -11.200 5.212   5.845  1.00 100.03 ? 535 GLN   A CB  1 
ATOM   1882 C  CG  . GLN   A 1 239 ? -11.877 6.508   6.228  1.00 105.82 ? 535 GLN   A CG  1 
ATOM   1883 C  CD  . GLN   A 1 239 ? -11.475 7.652   5.326  1.00 111.02 ? 535 GLN   A CD  1 
ATOM   1884 O  OE1 . GLN   A 1 239 ? -12.162 8.672   5.250  1.00 109.97 ? 535 GLN   A OE1 1 
ATOM   1885 N  NE2 . GLN   A 1 239 ? -10.355 7.489   4.632  1.00 117.66 ? 535 GLN   A NE2 1 
ATOM   1886 N  N   . ILE   A 1 240 ? -14.403 4.182   6.682  1.00 72.54  ? 536 ILE   A N   1 
ATOM   1887 C  CA  . ILE   A 1 240 ? -15.809 4.574   6.584  1.00 69.15  ? 536 ILE   A CA  1 
ATOM   1888 C  C   . ILE   A 1 240 ? -15.883 5.989   6.031  1.00 75.84  ? 536 ILE   A C   1 
ATOM   1889 O  O   . ILE   A 1 240 ? -15.225 6.886   6.583  1.00 72.30  ? 536 ILE   A O   1 
ATOM   1890 C  CB  . ILE   A 1 240 ? -16.483 4.514   7.969  1.00 66.32  ? 536 ILE   A CB  1 
ATOM   1891 C  CG1 . ILE   A 1 240 ? -16.087 3.225   8.693  1.00 56.04  ? 536 ILE   A CG1 1 
ATOM   1892 C  CG2 . ILE   A 1 240 ? -18.005 4.686   7.865  1.00 52.16  ? 536 ILE   A CG2 1 
ATOM   1893 C  CD1 . ILE   A 1 240 ? -15.931 3.414   10.202 1.00 72.32  ? 536 ILE   A CD1 1 
ATOM   1894 N  N   . PRO   A 1 241 ? -16.653 6.238   4.967  1.00 67.16  ? 537 PRO   A N   1 
ATOM   1895 C  CA  . PRO   A 1 241 ? -16.839 7.614   4.493  1.00 78.01  ? 537 PRO   A CA  1 
ATOM   1896 C  C   . PRO   A 1 241 ? -17.244 8.512   5.646  1.00 81.30  ? 537 PRO   A C   1 
ATOM   1897 O  O   . PRO   A 1 241 ? -18.245 8.248   6.332  1.00 74.40  ? 537 PRO   A O   1 
ATOM   1898 C  CB  . PRO   A 1 241 ? -17.961 7.492   3.449  1.00 70.51  ? 537 PRO   A CB  1 
ATOM   1899 C  CG  . PRO   A 1 241 ? -17.884 6.078   2.987  1.00 73.55  ? 537 PRO   A CG  1 
ATOM   1900 C  CD  . PRO   A 1 241 ? -17.402 5.261   4.152  1.00 63.19  ? 537 PRO   A CD  1 
ATOM   1901 N  N   . PRO   A 1 242 ? -16.442 9.533   5.937  1.00 85.61  ? 538 PRO   A N   1 
ATOM   1902 C  CA  . PRO   A 1 242 ? -16.726 10.389  7.099  1.00 87.33  ? 538 PRO   A CA  1 
ATOM   1903 C  C   . PRO   A 1 242 ? -18.163 10.880  7.149  1.00 86.12  ? 538 PRO   A C   1 
ATOM   1904 O  O   . PRO   A 1 242 ? -18.740 10.967  8.241  1.00 83.52  ? 538 PRO   A O   1 
ATOM   1905 C  CB  . PRO   A 1 242 ? -15.735 11.544  6.921  1.00 90.69  ? 538 PRO   A CB  1 
ATOM   1906 C  CG  . PRO   A 1 242 ? -14.603 10.949  6.142  1.00 87.42  ? 538 PRO   A CG  1 
ATOM   1907 C  CD  . PRO   A 1 242 ? -15.204 9.913   5.240  1.00 83.66  ? 538 PRO   A CD  1 
ATOM   1908 N  N   . GLU   A 1 243 ? -18.774 11.175  5.992  1.00 81.10  ? 539 GLU   A N   1 
ATOM   1909 C  CA  . GLU   A 1 243 ? -20.168 11.609  5.967  1.00 72.04  ? 539 GLU   A CA  1 
ATOM   1910 C  C   . GLU   A 1 243 ? -21.113 10.556  6.546  1.00 76.88  ? 539 GLU   A C   1 
ATOM   1911 O  O   . GLU   A 1 243 ? -22.215 10.907  6.984  1.00 81.40  ? 539 GLU   A O   1 
ATOM   1912 C  CB  . GLU   A 1 243 ? -20.576 11.994  4.532  1.00 84.89  ? 539 GLU   A CB  1 
ATOM   1913 C  CG  . GLU   A 1 243 ? -20.609 10.836  3.559  1.00 84.01  ? 539 GLU   A CG  1 
ATOM   1914 C  CD  . GLU   A 1 243 ? -19.348 10.705  2.715  1.00 89.20  ? 539 GLU   A CD  1 
ATOM   1915 O  OE1 . GLU   A 1 243 ? -18.252 11.040  3.214  1.00 88.91  ? 539 GLU   A OE1 1 
ATOM   1916 O  OE2 . GLU   A 1 243 ? -19.465 10.265  1.538  1.00 85.45  ? 539 GLU   A OE2 1 
ATOM   1917 N  N   . LEU   A 1 244 ? -20.694 9.285   6.593  1.00 72.54  ? 540 LEU   A N   1 
ATOM   1918 C  CA  . LEU   A 1 244 ? -21.476 8.217   7.201  1.00 68.80  ? 540 LEU   A CA  1 
ATOM   1919 C  C   . LEU   A 1 244 ? -21.275 8.098   8.710  1.00 70.37  ? 540 LEU   A C   1 
ATOM   1920 O  O   . LEU   A 1 244 ? -22.099 7.457   9.373  1.00 71.78  ? 540 LEU   A O   1 
ATOM   1921 C  CB  . LEU   A 1 244 ? -21.135 6.869   6.554  1.00 71.03  ? 540 LEU   A CB  1 
ATOM   1922 C  CG  . LEU   A 1 244 ? -21.520 6.667   5.092  1.00 68.67  ? 540 LEU   A CG  1 
ATOM   1923 C  CD1 . LEU   A 1 244 ? -21.405 5.173   4.753  1.00 59.64  ? 540 LEU   A CD1 1 
ATOM   1924 C  CD2 . LEU   A 1 244 ? -22.928 7.202   4.877  1.00 68.83  ? 540 LEU   A CD2 1 
ATOM   1925 N  N   . VAL   A 1 245 ? -20.216 8.688   9.261  1.00 67.44  ? 541 VAL   A N   1 
ATOM   1926 C  CA  . VAL   A 1 245 ? -19.956 8.639   10.698 1.00 68.92  ? 541 VAL   A CA  1 
ATOM   1927 C  C   . VAL   A 1 245 ? -20.528 9.917   11.300 1.00 65.18  ? 541 VAL   A C   1 
ATOM   1928 O  O   . VAL   A 1 245 ? -19.927 10.981  11.194 1.00 63.35  ? 541 VAL   A O   1 
ATOM   1929 C  CB  . VAL   A 1 245 ? -18.465 8.481   11.003 1.00 72.21  ? 541 VAL   A CB  1 
ATOM   1930 C  CG1 . VAL   A 1 245 ? -18.205 8.637   12.509 1.00 73.02  ? 541 VAL   A CG1 1 
ATOM   1931 C  CG2 . VAL   A 1 245 ? -17.978 7.121   10.533 1.00 64.78  ? 541 VAL   A CG2 1 
ATOM   1932 N  N   . LEU   A 1 246 ? -21.692 9.799   11.946 1.00 72.57  ? 542 LEU   A N   1 
ATOM   1933 C  CA  . LEU   A 1 246 ? -22.349 10.924  12.601 1.00 70.04  ? 542 LEU   A CA  1 
ATOM   1934 C  C   . LEU   A 1 246 ? -21.774 11.127  13.997 1.00 67.60  ? 542 LEU   A C   1 
ATOM   1935 O  O   . LEU   A 1 246 ? -21.645 10.173  14.770 1.00 69.68  ? 542 LEU   A O   1 
ATOM   1936 C  CB  . LEU   A 1 246 ? -23.859 10.688  12.685 1.00 73.47  ? 542 LEU   A CB  1 
ATOM   1937 C  CG  . LEU   A 1 246 ? -24.686 11.607  13.589 1.00 77.47  ? 542 LEU   A CG  1 
ATOM   1938 C  CD1 . LEU   A 1 246 ? -24.697 13.019  13.019 1.00 78.81  ? 542 LEU   A CD1 1 
ATOM   1939 C  CD2 . LEU   A 1 246 ? -26.112 11.069  13.798 1.00 67.27  ? 542 LEU   A CD2 1 
ATOM   1940 N  N   . GLU   A 1 247 ? -21.445 12.375  14.317 1.00 77.09  ? 543 GLU   A N   1 
ATOM   1941 C  CA  . GLU   A 1 247 ? -20.846 12.736  15.594 1.00 74.02  ? 543 GLU   A CA  1 
ATOM   1942 C  C   . GLU   A 1 247 ? -21.620 13.890  16.221 1.00 80.89  ? 543 GLU   A C   1 
ATOM   1943 O  O   . GLU   A 1 247 ? -22.157 14.757  15.517 1.00 78.26  ? 543 GLU   A O   1 
ATOM   1944 C  CB  . GLU   A 1 247 ? -19.370 13.131  15.427 1.00 79.66  ? 543 GLU   A CB  1 
ATOM   1945 C  CG  . GLU   A 1 247 ? -18.476 12.006  14.934 1.00 83.70  ? 543 GLU   A CG  1 
ATOM   1946 C  CD  . GLU   A 1 247 ? -17.055 12.469  14.660 1.00 95.43  ? 543 GLU   A CD  1 
ATOM   1947 O  OE1 . GLU   A 1 247 ? -16.803 13.052  13.583 1.00 94.68  ? 543 GLU   A OE1 1 
ATOM   1948 O  OE2 . GLU   A 1 247 ? -16.188 12.251  15.534 1.00 94.25  ? 543 GLU   A OE2 1 
ATOM   1949 N  N   . VAL   A 1 248 ? -21.641 13.904  17.554 1.00 77.88  ? 544 VAL   A N   1 
ATOM   1950 C  CA  . VAL   A 1 248 ? -22.365 14.893  18.343 1.00 85.69  ? 544 VAL   A CA  1 
ATOM   1951 C  C   . VAL   A 1 248 ? -21.356 15.685  19.169 1.00 83.06  ? 544 VAL   A C   1 
ATOM   1952 O  O   . VAL   A 1 248 ? -20.666 15.106  20.013 1.00 75.93  ? 544 VAL   A O   1 
ATOM   1953 C  CB  . VAL   A 1 248 ? -23.410 14.248  19.270 1.00 80.38  ? 544 VAL   A CB  1 
ATOM   1954 C  CG1 . VAL   A 1 248 ? -24.149 15.337  20.064 1.00 87.72  ? 544 VAL   A CG1 1 
ATOM   1955 C  CG2 . VAL   A 1 248 ? -24.374 13.359  18.488 1.00 72.32  ? 544 VAL   A CG2 1 
ATOM   1956 N  N   . PRO   A 1 249 ? -21.212 16.993  18.950 1.00 86.68  ? 545 PRO   A N   1 
ATOM   1957 C  CA  . PRO   A 1 249 ? -20.346 17.794  19.815 1.00 89.86  ? 545 PRO   A CA  1 
ATOM   1958 C  C   . PRO   A 1 249 ? -21.058 18.037  21.132 1.00 91.09  ? 545 PRO   A C   1 
ATOM   1959 O  O   . PRO   A 1 249 ? -22.235 18.401  21.164 1.00 90.88  ? 545 PRO   A O   1 
ATOM   1960 C  CB  . PRO   A 1 249 ? -20.157 19.102  19.029 1.00 90.40  ? 545 PRO   A CB  1 
ATOM   1961 C  CG  . PRO   A 1 249 ? -20.753 18.858  17.682 1.00 88.06  ? 545 PRO   A CG  1 
ATOM   1962 C  CD  . PRO   A 1 249 ? -21.788 17.805  17.864 1.00 85.00  ? 545 PRO   A CD  1 
ATOM   1963 N  N   . ILE   A 1 250 ? -20.336 17.819  22.224 1.00 99.00  ? 546 ILE   A N   1 
ATOM   1964 C  CA  . ILE   A 1 250 ? -20.917 17.848  23.562 1.00 90.84  ? 546 ILE   A CA  1 
ATOM   1965 C  C   . ILE   A 1 250 ? -20.853 19.268  24.109 1.00 98.83  ? 546 ILE   A C   1 
ATOM   1966 O  O   . ILE   A 1 250 ? -19.766 19.844  24.247 1.00 91.44  ? 546 ILE   A O   1 
ATOM   1967 C  CB  . ILE   A 1 250 ? -20.201 16.861  24.496 1.00 90.94  ? 546 ILE   A CB  1 
ATOM   1968 C  CG1 . ILE   A 1 250 ? -20.147 15.473  23.845 1.00 78.77  ? 546 ILE   A CG1 1 
ATOM   1969 C  CG2 . ILE   A 1 250 ? -20.916 16.789  25.833 1.00 86.72  ? 546 ILE   A CG2 1 
ATOM   1970 C  CD1 . ILE   A 1 250 ? -21.504 14.947  23.422 1.00 75.39  ? 546 ILE   A CD1 1 
ATOM   1971 N  N   . ARG   A 1 251 ? -22.024 19.832  24.417 1.00 104.88 ? 547 ARG   A N   1 
ATOM   1972 C  CA  . ARG   A 1 251 ? -22.145 21.119  25.082 1.00 99.14  ? 547 ARG   A CA  1 
ATOM   1973 C  C   . ARG   A 1 251 ? -23.063 20.955  26.285 1.00 104.16 ? 547 ARG   A C   1 
ATOM   1974 O  O   . ARG   A 1 251 ? -23.780 19.958  26.414 1.00 94.79  ? 547 ARG   A O   1 
ATOM   1975 C  CB  . ARG   A 1 251 ? -22.670 22.234  24.143 1.00 104.05 ? 547 ARG   A CB  1 
ATOM   1976 C  CG  . ARG   A 1 251 ? -24.083 22.045  23.571 1.00 97.89  ? 547 ARG   A CG  1 
ATOM   1977 C  CD  . ARG   A 1 251 ? -24.066 21.256  22.247 1.00 100.33 ? 547 ARG   A CD  1 
ATOM   1978 N  NE  . ARG   A 1 251 ? -25.364 21.233  21.573 1.00 95.64  ? 547 ARG   A NE  1 
ATOM   1979 C  CZ  . ARG   A 1 251 ? -25.623 20.516  20.482 1.00 108.78 ? 547 ARG   A CZ  1 
ATOM   1980 N  NH1 . ARG   A 1 251 ? -26.825 20.557  19.924 1.00 117.91 ? 547 ARG   A NH1 1 
ATOM   1981 N  NH2 . ARG   A 1 251 ? -24.676 19.759  19.943 1.00 102.63 ? 547 ARG   A NH2 1 
ATOM   1982 N  N   . HIS   A 1 252 ? -23.001 21.942  27.200 1.00 102.54 ? 548 HIS   A N   1 
ATOM   1983 C  CA  . HIS   A 1 252 ? -23.864 21.914  28.366 1.00 99.65  ? 548 HIS   A CA  1 
ATOM   1984 C  C   . HIS   A 1 252 ? -24.920 23.011  28.285 1.00 115.11 ? 548 HIS   A C   1 
ATOM   1985 O  O   . HIS   A 1 252 ? -24.634 24.110  27.794 1.00 116.96 ? 548 HIS   A O   1 
ATOM   1986 C  CB  . HIS   A 1 252 ? -23.060 22.083  29.656 1.00 96.33  ? 548 HIS   A CB  1 
ATOM   1987 C  CG  . HIS   A 1 252 ? -23.779 21.601  30.871 1.00 111.18 ? 548 HIS   A CG  1 
ATOM   1988 N  ND1 . HIS   A 1 252 ? -24.687 22.378  31.558 1.00 115.34 ? 548 HIS   A ND1 1 
ATOM   1989 C  CD2 . HIS   A 1 252 ? -23.732 20.413  31.517 1.00 106.03 ? 548 HIS   A CD2 1 
ATOM   1990 C  CE1 . HIS   A 1 252 ? -25.166 21.689  32.578 1.00 107.10 ? 548 HIS   A CE1 1 
ATOM   1991 N  NE2 . HIS   A 1 252 ? -24.603 20.494  32.575 1.00 105.02 ? 548 HIS   A NE2 1 
ATOM   1992 N  N   . PRO   A 1 253 ? -26.142 22.741  28.759 1.00 113.89 ? 549 PRO   A N   1 
ATOM   1993 C  CA  . PRO   A 1 253 ? -27.222 23.733  28.647 1.00 112.87 ? 549 PRO   A CA  1 
ATOM   1994 C  C   . PRO   A 1 253 ? -27.090 24.907  29.599 1.00 120.11 ? 549 PRO   A C   1 
ATOM   1995 O  O   . PRO   A 1 253 ? -27.859 25.868  29.471 1.00 129.00 ? 549 PRO   A O   1 
ATOM   1996 C  CB  . PRO   A 1 253 ? -28.476 22.913  28.975 1.00 115.71 ? 549 PRO   A CB  1 
ATOM   1997 C  CG  . PRO   A 1 253 ? -27.969 21.818  29.872 1.00 108.00 ? 549 PRO   A CG  1 
ATOM   1998 C  CD  . PRO   A 1 253 ? -26.637 21.452  29.275 1.00 106.51 ? 549 PRO   A CD  1 
ATOM   1999 N  N   . LYS   A 1 254 ? -26.169 24.855  30.563 1.00 114.36 ? 550 LYS   A N   1 
ATOM   2000 C  CA  . LYS   A 1 254 ? -25.862 25.995  31.417 1.00 125.06 ? 550 LYS   A CA  1 
ATOM   2001 C  C   . LYS   A 1 254 ? -24.442 26.495  31.208 1.00 129.73 ? 550 LYS   A C   1 
ATOM   2002 O  O   . LYS   A 1 254 ? -24.237 27.683  30.933 1.00 142.98 ? 550 LYS   A O   1 
ATOM   2003 C  CB  . LYS   A 1 254 ? -26.050 25.631  32.905 1.00 129.83 ? 550 LYS   A CB  1 
ATOM   2004 C  CG  . LYS   A 1 254 ? -27.332 24.882  33.243 1.00 132.05 ? 550 LYS   A CG  1 
ATOM   2005 C  CD  . LYS   A 1 254 ? -28.563 25.730  33.003 1.00 143.69 ? 550 LYS   A CD  1 
ATOM   2006 C  CE  . LYS   A 1 254 ? -29.826 24.965  33.365 1.00 141.12 ? 550 LYS   A CE  1 
ATOM   2007 N  NZ  . LYS   A 1 254 ? -31.058 25.752  33.077 1.00 145.72 ? 550 LYS   A NZ  1 
ATOM   2008 N  N   . PHE   A 1 255 ? -23.453 25.615  31.321 1.00 117.70 ? 551 PHE   A N   1 
ATOM   2009 C  CA  . PHE   A 1 255 ? -22.050 26.015  31.385 1.00 120.27 ? 551 PHE   A CA  1 
ATOM   2010 C  C   . PHE   A 1 255 ? -21.528 26.245  29.973 1.00 122.61 ? 551 PHE   A C   1 
ATOM   2011 O  O   . PHE   A 1 255 ? -21.171 25.298  29.270 1.00 121.20 ? 551 PHE   A O   1 
ATOM   2012 C  CB  . PHE   A 1 255 ? -21.237 24.947  32.102 1.00 118.07 ? 551 PHE   A CB  1 
ATOM   2013 C  CG  . PHE   A 1 255 ? -21.730 24.633  33.501 1.00 122.52 ? 551 PHE   A CG  1 
ATOM   2014 C  CD1 . PHE   A 1 255 ? -22.719 23.685  33.699 1.00 126.70 ? 551 PHE   A CD1 1 
ATOM   2015 C  CD2 . PHE   A 1 255 ? -21.194 25.268  34.610 1.00 123.96 ? 551 PHE   A CD2 1 
ATOM   2016 C  CE1 . PHE   A 1 255 ? -23.173 23.373  34.971 1.00 124.06 ? 551 PHE   A CE1 1 
ATOM   2017 C  CE2 . PHE   A 1 255 ? -21.646 24.961  35.898 1.00 121.31 ? 551 PHE   A CE2 1 
ATOM   2018 C  CZ  . PHE   A 1 255 ? -22.639 24.014  36.072 1.00 119.44 ? 551 PHE   A CZ  1 
ATOM   2019 N  N   . ASP   A 1 256 ? -21.465 27.511  29.552 1.00 136.00 ? 552 ASP   A N   1 
ATOM   2020 C  CA  . ASP   A 1 256 ? -20.976 27.813  28.210 1.00 138.57 ? 552 ASP   A CA  1 
ATOM   2021 C  C   . ASP   A 1 256 ? -19.492 27.521  28.045 1.00 137.51 ? 552 ASP   A C   1 
ATOM   2022 O  O   . ASP   A 1 256 ? -19.012 27.490  26.910 1.00 139.73 ? 552 ASP   A O   1 
ATOM   2023 C  CB  . ASP   A 1 256 ? -21.255 29.274  27.849 1.00 150.99 ? 552 ASP   A CB  1 
ATOM   2024 C  CG  . ASP   A 1 256 ? -22.604 29.460  27.182 1.00 165.80 ? 552 ASP   A CG  1 
ATOM   2025 O  OD1 . ASP   A 1 256 ? -23.407 30.275  27.684 1.00 171.25 ? 552 ASP   A OD1 1 
ATOM   2026 O  OD2 . ASP   A 1 256 ? -22.864 28.776  26.163 1.00 166.83 ? 552 ASP   A OD2 1 
ATOM   2027 N  N   . TRP   A 1 257 ? -18.752 27.306  29.134 1.00 135.85 ? 553 TRP   A N   1 
ATOM   2028 C  CA  . TRP   A 1 257 ? -17.372 26.855  29.010 1.00 133.14 ? 553 TRP   A CA  1 
ATOM   2029 C  C   . TRP   A 1 257 ? -17.274 25.383  28.638 1.00 128.26 ? 553 TRP   A C   1 
ATOM   2030 O  O   . TRP   A 1 257 ? -16.178 24.908  28.319 1.00 124.20 ? 553 TRP   A O   1 
ATOM   2031 C  CB  . TRP   A 1 257 ? -16.615 27.101  30.312 1.00 128.80 ? 553 TRP   A CB  1 
ATOM   2032 C  CG  . TRP   A 1 257 ? -17.289 26.504  31.497 1.00 136.56 ? 553 TRP   A CG  1 
ATOM   2033 C  CD1 . TRP   A 1 257 ? -18.122 27.139  32.369 1.00 145.33 ? 553 TRP   A CD1 1 
ATOM   2034 C  CD2 . TRP   A 1 257 ? -17.194 25.146  31.948 1.00 131.49 ? 553 TRP   A CD2 1 
ATOM   2035 N  NE1 . TRP   A 1 257 ? -18.546 26.263  33.339 1.00 141.79 ? 553 TRP   A NE1 1 
ATOM   2036 C  CE2 . TRP   A 1 257 ? -17.992 25.032  33.101 1.00 133.47 ? 553 TRP   A CE2 1 
ATOM   2037 C  CE3 . TRP   A 1 257 ? -16.511 24.016  31.488 1.00 121.03 ? 553 TRP   A CE3 1 
ATOM   2038 C  CZ2 . TRP   A 1 257 ? -18.126 23.834  33.798 1.00 119.14 ? 553 TRP   A CZ2 1 
ATOM   2039 C  CZ3 . TRP   A 1 257 ? -16.647 22.828  32.183 1.00 111.07 ? 553 TRP   A CZ3 1 
ATOM   2040 C  CH2 . TRP   A 1 257 ? -17.448 22.746  33.319 1.00 112.14 ? 553 TRP   A CH2 1 
ATOM   2041 N  N   . PHE   A 1 258 ? -18.393 24.658  28.668 1.00 111.26 ? 554 PHE   A N   1 
ATOM   2042 C  CA  . PHE   A 1 258 ? -18.369 23.233  28.371 1.00 115.31 ? 554 PHE   A CA  1 
ATOM   2043 C  C   . PHE   A 1 258 ? -17.976 22.951  26.928 1.00 112.10 ? 554 PHE   A C   1 
ATOM   2044 O  O   . PHE   A 1 258 ? -17.364 21.915  26.657 1.00 110.09 ? 554 PHE   A O   1 
ATOM   2045 C  CB  . PHE   A 1 258 ? -19.731 22.614  28.663 1.00 105.21 ? 554 PHE   A CB  1 
ATOM   2046 C  CG  . PHE   A 1 258 ? -19.648 21.220  29.147 1.00 97.78  ? 554 PHE   A CG  1 
ATOM   2047 C  CD1 . PHE   A 1 258 ? -19.715 20.954  30.503 1.00 105.24 ? 554 PHE   A CD1 1 
ATOM   2048 C  CD2 . PHE   A 1 258 ? -19.460 20.169  28.263 1.00 95.37  ? 554 PHE   A CD2 1 
ATOM   2049 C  CE1 . PHE   A 1 258 ? -19.625 19.669  30.973 1.00 94.56  ? 554 PHE   A CE1 1 
ATOM   2050 C  CE2 . PHE   A 1 258 ? -19.376 18.868  28.719 1.00 95.66  ? 554 PHE   A CE2 1 
ATOM   2051 C  CZ  . PHE   A 1 258 ? -19.450 18.620  30.088 1.00 92.64  ? 554 PHE   A CZ  1 
ATOM   2052 N  N   . LYS   A 1 259 ? -18.323 23.841  25.992 1.00 107.74 ? 555 LYS   A N   1 
ATOM   2053 C  CA  . LYS   A 1 259 ? -17.949 23.610  24.599 1.00 119.82 ? 555 LYS   A CA  1 
ATOM   2054 C  C   . LYS   A 1 259 ? -16.437 23.650  24.428 1.00 129.66 ? 555 LYS   A C   1 
ATOM   2055 O  O   . LYS   A 1 259 ? -15.878 22.915  23.605 1.00 129.40 ? 555 LYS   A O   1 
ATOM   2056 C  CB  . LYS   A 1 259 ? -18.613 24.637  23.673 1.00 120.37 ? 555 LYS   A CB  1 
ATOM   2057 C  CG  . LYS   A 1 259 ? -19.404 25.732  24.361 1.00 126.13 ? 555 LYS   A CG  1 
ATOM   2058 C  CD  . LYS   A 1 259 ? -19.637 26.908  23.424 1.00 137.22 ? 555 LYS   A CD  1 
ATOM   2059 C  CE  . LYS   A 1 259 ? -20.768 27.790  23.915 1.00 148.23 ? 555 LYS   A CE  1 
ATOM   2060 N  NZ  . LYS   A 1 259 ? -21.993 26.978  24.164 1.00 148.33 ? 555 LYS   A NZ  1 
ATOM   2061 N  N   . ASP   A 1 260 ? -15.755 24.497  25.203 1.00 132.43 ? 556 ASP   A N   1 
ATOM   2062 C  CA  . ASP   A 1 260 ? -14.306 24.606  25.090 1.00 141.51 ? 556 ASP   A CA  1 
ATOM   2063 C  C   . ASP   A 1 260 ? -13.602 23.329  25.526 1.00 132.13 ? 556 ASP   A C   1 
ATOM   2064 O  O   . ASP   A 1 260 ? -12.425 23.142  25.199 1.00 132.00 ? 556 ASP   A O   1 
ATOM   2065 C  CB  . ASP   A 1 260 ? -13.810 25.800  25.906 1.00 155.61 ? 556 ASP   A CB  1 
ATOM   2066 C  CG  . ASP   A 1 260 ? -14.264 27.128  25.325 1.00 163.10 ? 556 ASP   A CG  1 
ATOM   2067 O  OD1 . ASP   A 1 260 ? -13.894 27.427  24.170 1.00 165.61 ? 556 ASP   A OD1 1 
ATOM   2068 O  OD2 . ASP   A 1 260 ? -15.003 27.863  26.017 1.00 165.73 ? 556 ASP   A OD2 1 
ATOM   2069 N  N   . LEU   A 1 261 ? -14.301 22.446  26.247 1.00 124.93 ? 557 LEU   A N   1 
ATOM   2070 C  CA  . LEU   A 1 261 ? -13.752 21.131  26.558 1.00 117.68 ? 557 LEU   A CA  1 
ATOM   2071 C  C   . LEU   A 1 261 ? -13.404 20.358  25.293 1.00 132.85 ? 557 LEU   A C   1 
ATOM   2072 O  O   . LEU   A 1 261 ? -12.521 19.494  25.316 1.00 141.02 ? 557 LEU   A O   1 
ATOM   2073 C  CB  . LEU   A 1 261 ? -14.743 20.341  27.406 1.00 101.80 ? 557 LEU   A CB  1 
ATOM   2074 C  CG  . LEU   A 1 261 ? -14.731 20.681  28.898 1.00 105.48 ? 557 LEU   A CG  1 
ATOM   2075 C  CD1 . LEU   A 1 261 ? -15.714 19.819  29.697 1.00 96.68  ? 557 LEU   A CD1 1 
ATOM   2076 C  CD2 . LEU   A 1 261 ? -13.320 20.530  29.442 1.00 112.07 ? 557 LEU   A CD2 1 
ATOM   2077 N  N   . GLY   A 1 262 ? -14.081 20.651  24.187 1.00 132.73 ? 558 GLY   A N   1 
ATOM   2078 C  CA  . GLY   A 1 262 ? -13.749 20.047  22.914 1.00 135.19 ? 558 GLY   A CA  1 
ATOM   2079 C  C   . GLY   A 1 262 ? -14.025 18.562  22.872 1.00 132.68 ? 558 GLY   A C   1 
ATOM   2080 O  O   . GLY   A 1 262 ? -13.229 17.797  22.321 1.00 135.48 ? 558 GLY   A O   1 
ATOM   2081 N  N   . LEU   A 1 263 ? -15.144 18.141  23.453 1.00 119.83 ? 559 LEU   A N   1 
ATOM   2082 C  CA  . LEU   A 1 263 ? -15.540 16.744  23.457 1.00 105.52 ? 559 LEU   A CA  1 
ATOM   2083 C  C   . LEU   A 1 263 ? -16.630 16.496  22.423 1.00 96.89  ? 559 LEU   A C   1 
ATOM   2084 O  O   . LEU   A 1 263 ? -17.423 17.385  22.098 1.00 88.67  ? 559 LEU   A O   1 
ATOM   2085 C  CB  . LEU   A 1 263 ? -16.034 16.310  24.840 1.00 99.71  ? 559 LEU   A CB  1 
ATOM   2086 C  CG  . LEU   A 1 263 ? -15.002 16.469  25.958 1.00 94.09  ? 559 LEU   A CG  1 
ATOM   2087 C  CD1 . LEU   A 1 263 ? -15.613 16.078  27.288 1.00 93.97  ? 559 LEU   A CD1 1 
ATOM   2088 C  CD2 . LEU   A 1 263 ? -13.742 15.657  25.669 1.00 88.86  ? 559 LEU   A CD2 1 
ATOM   2089 N  N   . LYS   A 1 264 ? -16.644 15.274  21.904 1.00 88.48  ? 560 LYS   A N   1 
ATOM   2090 C  CA  . LYS   A 1 264 ? -17.679 14.806  20.998 1.00 94.41  ? 560 LYS   A CA  1 
ATOM   2091 C  C   . LYS   A 1 264 ? -17.774 13.305  21.159 1.00 90.78  ? 560 LYS   A C   1 
ATOM   2092 O  O   . LYS   A 1 264 ? -16.881 12.666  21.722 1.00 91.27  ? 560 LYS   A O   1 
ATOM   2093 C  CB  . LYS   A 1 264 ? -17.379 15.153  19.534 1.00 81.80  ? 560 LYS   A CB  1 
ATOM   2094 C  CG  . LYS   A 1 264 ? -16.026 14.654  19.050 1.00 80.12  ? 560 LYS   A CG  1 
ATOM   2095 C  CD  . LYS   A 1 264 ? -15.799 14.978  17.569 1.00 96.99  ? 560 LYS   A CD  1 
ATOM   2096 C  CE  . LYS   A 1 264 ? -14.335 15.324  17.292 1.00 100.03 ? 560 LYS   A CE  1 
ATOM   2097 N  NZ  . LYS   A 1 264 ? -13.962 15.301  15.847 1.00 87.94  ? 560 LYS   A NZ  1 
ATOM   2098 N  N   . TRP   A 1 265 ? -18.871 12.750  20.669 1.00 82.63  ? 561 TRP   A N   1 
ATOM   2099 C  CA  . TRP   A 1 265 ? -18.985 11.307  20.588 1.00 71.38  ? 561 TRP   A CA  1 
ATOM   2100 C  C   . TRP   A 1 265 ? -19.703 10.967  19.291 1.00 75.42  ? 561 TRP   A C   1 
ATOM   2101 O  O   . TRP   A 1 265 ? -20.298 11.830  18.636 1.00 76.04  ? 561 TRP   A O   1 
ATOM   2102 C  CB  . TRP   A 1 265 ? -19.699 10.703  21.810 1.00 62.59  ? 561 TRP   A CB  1 
ATOM   2103 C  CG  . TRP   A 1 265 ? -19.294 9.262   22.031 1.00 66.59  ? 561 TRP   A CG  1 
ATOM   2104 C  CD1 . TRP   A 1 265 ? -20.067 8.153   21.827 1.00 69.31  ? 561 TRP   A CD1 1 
ATOM   2105 C  CD2 . TRP   A 1 265 ? -18.002 8.780   22.437 1.00 68.67  ? 561 TRP   A CD2 1 
ATOM   2106 N  NE1 . TRP   A 1 265 ? -19.344 7.014   22.090 1.00 66.51  ? 561 TRP   A NE1 1 
ATOM   2107 C  CE2 . TRP   A 1 265 ? -18.074 7.370   22.470 1.00 69.86  ? 561 TRP   A CE2 1 
ATOM   2108 C  CE3 . TRP   A 1 265 ? -16.797 9.403   22.791 1.00 68.15  ? 561 TRP   A CE3 1 
ATOM   2109 C  CZ2 . TRP   A 1 265 ? -16.987 6.568   22.845 1.00 70.06  ? 561 TRP   A CZ2 1 
ATOM   2110 C  CZ3 . TRP   A 1 265 ? -15.714 8.602   23.156 1.00 70.93  ? 561 TRP   A CZ3 1 
ATOM   2111 C  CH2 . TRP   A 1 265 ? -15.822 7.198   23.184 1.00 63.48  ? 561 TRP   A CH2 1 
ATOM   2112 N  N   . TYR   A 1 266 ? -19.581 9.707   18.897 1.00 66.86  ? 562 TYR   A N   1 
ATOM   2113 C  CA  . TYR   A 1 266 ? -20.307 9.208   17.744 1.00 65.78  ? 562 TYR   A CA  1 
ATOM   2114 C  C   . TYR   A 1 266 ? -21.701 8.766   18.171 1.00 75.91  ? 562 TYR   A C   1 
ATOM   2115 O  O   . TYR   A 1 266 ? -21.907 8.305   19.297 1.00 65.89  ? 562 TYR   A O   1 
ATOM   2116 C  CB  . TYR   A 1 266 ? -19.551 8.048   17.102 1.00 58.33  ? 562 TYR   A CB  1 
ATOM   2117 C  CG  . TYR   A 1 266 ? -19.050 6.962   18.056 1.00 64.61  ? 562 TYR   A CG  1 
ATOM   2118 C  CD1 . TYR   A 1 266 ? -19.810 5.826   18.297 1.00 66.14  ? 562 TYR   A CD1 1 
ATOM   2119 C  CD2 . TYR   A 1 266 ? -17.798 7.051   18.661 1.00 57.74  ? 562 TYR   A CD2 1 
ATOM   2120 C  CE1 . TYR   A 1 266 ? -19.362 4.824   19.124 1.00 71.21  ? 562 TYR   A CE1 1 
ATOM   2121 C  CE2 . TYR   A 1 266 ? -17.341 6.042   19.498 1.00 65.60  ? 562 TYR   A CE2 1 
ATOM   2122 C  CZ  . TYR   A 1 266 ? -18.133 4.934   19.730 1.00 69.71  ? 562 TYR   A CZ  1 
ATOM   2123 O  OH  . TYR   A 1 266 ? -17.708 3.918   20.550 1.00 70.62  ? 562 TYR   A OH  1 
ATOM   2124 N  N   . GLY   A 1 267 ? -22.674 8.926   17.268 1.00 63.27  ? 563 GLY   A N   1 
ATOM   2125 C  CA  . GLY   A 1 267 ? -24.030 8.578   17.665 1.00 59.87  ? 563 GLY   A CA  1 
ATOM   2126 C  C   . GLY   A 1 267 ? -24.343 7.096   17.653 1.00 63.03  ? 563 GLY   A C   1 
ATOM   2127 O  O   . GLY   A 1 267 ? -25.256 6.669   18.364 1.00 65.13  ? 563 GLY   A O   1 
ATOM   2128 N  N   . LEU   A 1 268 ? -23.603 6.299   16.866 1.00 58.78  ? 564 LEU   A N   1 
ATOM   2129 C  CA  . LEU   A 1 268 ? -23.985 4.923   16.572 1.00 56.17  ? 564 LEU   A CA  1 
ATOM   2130 C  C   . LEU   A 1 268 ? -23.153 3.953   17.403 1.00 60.06  ? 564 LEU   A C   1 
ATOM   2131 O  O   . LEU   A 1 268 ? -21.961 3.759   17.098 1.00 55.14  ? 564 LEU   A O   1 
ATOM   2132 C  CB  . LEU   A 1 268 ? -23.817 4.618   15.076 1.00 56.66  ? 564 LEU   A CB  1 
ATOM   2133 C  CG  . LEU   A 1 268 ? -24.376 3.271   14.603 1.00 57.81  ? 564 LEU   A CG  1 
ATOM   2134 C  CD1 . LEU   A 1 268 ? -25.908 3.227   14.656 1.00 62.77  ? 564 LEU   A CD1 1 
ATOM   2135 C  CD2 . LEU   A 1 268 ? -23.875 2.930   13.203 1.00 58.24  ? 564 LEU   A CD2 1 
ATOM   2136 N  N   . PRO   A 1 269 ? -23.709 3.338   18.451 1.00 57.64  ? 565 PRO   A N   1 
ATOM   2137 C  CA  . PRO   A 1 269 ? -23.009 2.231   19.125 1.00 48.54  ? 565 PRO   A CA  1 
ATOM   2138 C  C   . PRO   A 1 269 ? -23.242 0.950   18.336 1.00 52.07  ? 565 PRO   A C   1 
ATOM   2139 O  O   . PRO   A 1 269 ? -24.385 0.523   18.151 1.00 49.79  ? 565 PRO   A O   1 
ATOM   2140 C  CB  . PRO   A 1 269 ? -23.671 2.174   20.508 1.00 53.98  ? 565 PRO   A CB  1 
ATOM   2141 C  CG  . PRO   A 1 269 ? -25.042 2.684   20.296 1.00 63.46  ? 565 PRO   A CG  1 
ATOM   2142 C  CD  . PRO   A 1 269 ? -24.957 3.707   19.151 1.00 63.19  ? 565 PRO   A CD  1 
ATOM   2143 N  N   . ALA   A 1 270 ? -22.162 0.335   17.869 1.00 49.16  ? 566 ALA   A N   1 
ATOM   2144 C  CA  . ALA   A 1 270 ? -22.273 -0.762  16.907 1.00 44.65  ? 566 ALA   A CA  1 
ATOM   2145 C  C   . ALA   A 1 270 ? -21.213 -1.785  17.286 1.00 49.12  ? 566 ALA   A C   1 
ATOM   2146 O  O   . ALA   A 1 270 ? -20.053 -1.650  16.884 1.00 47.12  ? 566 ALA   A O   1 
ATOM   2147 C  CB  . ALA   A 1 270 ? -22.091 -0.267  15.477 1.00 42.32  ? 566 ALA   A CB  1 
ATOM   2148 N  N   . VAL   A 1 271 ? -21.605 -2.770  18.090 1.00 46.79  ? 567 VAL   A N   1 
ATOM   2149 C  CA  . VAL   A 1 271 ? -20.665 -3.773  18.577 1.00 48.85  ? 567 VAL   A CA  1 
ATOM   2150 C  C   . VAL   A 1 271 ? -20.352 -4.723  17.437 1.00 51.07  ? 567 VAL   A C   1 
ATOM   2151 O  O   . VAL   A 1 271 ? -21.258 -5.186  16.732 1.00 57.27  ? 567 VAL   A O   1 
ATOM   2152 C  CB  . VAL   A 1 271 ? -21.237 -4.534  19.783 1.00 46.72  ? 567 VAL   A CB  1 
ATOM   2153 C  CG1 . VAL   A 1 271 ? -20.440 -5.809  20.021 1.00 47.33  ? 567 VAL   A CG1 1 
ATOM   2154 C  CG2 . VAL   A 1 271 ? -21.178 -3.657  21.039 1.00 47.60  ? 567 VAL   A CG2 1 
ATOM   2155 N  N   . SER   A 1 272 ? -19.070 -5.007  17.237 1.00 47.70  ? 568 SER   A N   1 
ATOM   2156 C  CA  . SER   A 1 272 ? -18.674 -5.820  16.100 1.00 49.59  ? 568 SER   A CA  1 
ATOM   2157 C  C   . SER   A 1 272 ? -17.820 -7.030  16.450 1.00 47.47  ? 568 SER   A C   1 
ATOM   2158 O  O   . SER   A 1 272 ? -17.549 -7.841  15.558 1.00 58.73  ? 568 SER   A O   1 
ATOM   2159 C  CB  . SER   A 1 272 ? -17.922 -4.954  15.084 1.00 64.06  ? 568 SER   A CB  1 
ATOM   2160 O  OG  . SER   A 1 272 ? -16.878 -4.265  15.741 1.00 59.37  ? 568 SER   A OG  1 
ATOM   2161 N  N   . ASN   A 1 273 ? -17.397 -7.193  17.713 1.00 54.77  ? 569 ASN   A N   1 
ATOM   2162 C  CA  . ASN   A 1 273 ? -16.438 -8.234  18.062 1.00 57.69  ? 569 ASN   A CA  1 
ATOM   2163 C  C   . ASN   A 1 273 ? -17.090 -9.486  18.625 1.00 60.22  ? 569 ASN   A C   1 
ATOM   2164 O  O   . ASN   A 1 273 ? -16.378 -10.441 18.949 1.00 56.01  ? 569 ASN   A O   1 
ATOM   2165 C  CB  . ASN   A 1 273 ? -15.404 -7.706  19.075 1.00 64.43  ? 569 ASN   A CB  1 
ATOM   2166 C  CG  . ASN   A 1 273 ? -16.033 -7.265  20.387 1.00 61.80  ? 569 ASN   A CG  1 
ATOM   2167 O  OD1 . ASN   A 1 273 ? -17.259 -7.185  20.505 1.00 52.04  ? 569 ASN   A OD1 1 
ATOM   2168 N  ND2 . ASN   A 1 273 ? -15.191 -6.965  21.381 1.00 56.80  ? 569 ASN   A ND2 1 
ATOM   2169 N  N   . MET   A 1 274 ? -18.413 -9.517  18.746 1.00 52.29  ? 570 MET   A N   1 
ATOM   2170 C  CA  . MET   A 1 274 ? -19.082 -10.626 19.398 1.00 48.28  ? 570 MET   A CA  1 
ATOM   2171 C  C   . MET   A 1 274 ? -19.530 -11.661 18.377 1.00 57.24  ? 570 MET   A C   1 
ATOM   2172 O  O   . MET   A 1 274 ? -19.333 -11.506 17.175 1.00 57.65  ? 570 MET   A O   1 
ATOM   2173 C  CB  . MET   A 1 274 ? -20.252 -10.113 20.220 1.00 53.61  ? 570 MET   A CB  1 
ATOM   2174 C  CG  . MET   A 1 274 ? -19.756 -9.371  21.480 1.00 52.45  ? 570 MET   A CG  1 
ATOM   2175 S  SD  . MET   A 1 274 ? -21.164 -8.914  22.456 1.00 54.60  ? 570 MET   A SD  1 
ATOM   2176 C  CE  . MET   A 1 274 ? -21.441 -10.466 23.325 1.00 56.41  ? 570 MET   A CE  1 
ATOM   2177 N  N   . LEU   A 1 275 ? -20.135 -12.738 18.874 1.00 57.02  ? 571 LEU   A N   1 
ATOM   2178 C  CA  . LEU   A 1 275 ? -20.464 -13.911 18.073 1.00 54.30  ? 571 LEU   A CA  1 
ATOM   2179 C  C   . LEU   A 1 275 ? -21.938 -14.230 18.257 1.00 58.35  ? 571 LEU   A C   1 
ATOM   2180 O  O   . LEU   A 1 275 ? -22.399 -14.382 19.390 1.00 59.11  ? 571 LEU   A O   1 
ATOM   2181 C  CB  . LEU   A 1 275 ? -19.598 -15.104 18.494 1.00 47.23  ? 571 LEU   A CB  1 
ATOM   2182 C  CG  . LEU   A 1 275 ? -19.404 -16.299 17.555 1.00 65.47  ? 571 LEU   A CG  1 
ATOM   2183 C  CD1 . LEU   A 1 275 ? -18.130 -17.040 17.922 1.00 83.62  ? 571 LEU   A CD1 1 
ATOM   2184 C  CD2 . LEU   A 1 275 ? -20.591 -17.241 17.592 1.00 60.06  ? 571 LEU   A CD2 1 
ATOM   2185 N  N   . LEU   A 1 276 ? -22.669 -14.329 17.149 1.00 47.30  ? 572 LEU   A N   1 
ATOM   2186 C  CA  . LEU   A 1 276 ? -24.074 -14.725 17.154 1.00 45.63  ? 572 LEU   A CA  1 
ATOM   2187 C  C   . LEU   A 1 276 ? -24.174 -16.243 17.011 1.00 54.80  ? 572 LEU   A C   1 
ATOM   2188 O  O   . LEU   A 1 276 ? -23.532 -16.831 16.134 1.00 63.64  ? 572 LEU   A O   1 
ATOM   2189 C  CB  . LEU   A 1 276 ? -24.812 -14.026 15.998 1.00 46.05  ? 572 LEU   A CB  1 
ATOM   2190 C  CG  . LEU   A 1 276 ? -26.204 -14.514 15.584 1.00 55.92  ? 572 LEU   A CG  1 
ATOM   2191 C  CD1 . LEU   A 1 276 ? -27.142 -14.377 16.756 1.00 61.05  ? 572 LEU   A CD1 1 
ATOM   2192 C  CD2 . LEU   A 1 276 ? -26.746 -13.764 14.362 1.00 49.19  ? 572 LEU   A CD2 1 
ATOM   2193 N  N   . GLU   A 1 277 ? -24.969 -16.879 17.869 1.00 57.56  ? 573 GLU   A N   1 
ATOM   2194 C  CA  . GLU   A 1 277 ? -25.223 -18.313 17.789 1.00 60.95  ? 573 GLU   A CA  1 
ATOM   2195 C  C   . GLU   A 1 277 ? -26.697 -18.553 17.508 1.00 61.27  ? 573 GLU   A C   1 
ATOM   2196 O  O   . GLU   A 1 277 ? -27.566 -18.021 18.208 1.00 67.12  ? 573 GLU   A O   1 
ATOM   2197 C  CB  . GLU   A 1 277 ? -24.825 -19.041 19.068 1.00 77.18  ? 573 GLU   A CB  1 
ATOM   2198 C  CG  . GLU   A 1 277 ? -23.443 -19.650 19.032 1.00 90.78  ? 573 GLU   A CG  1 
ATOM   2199 C  CD  . GLU   A 1 277 ? -23.296 -20.759 20.052 1.00 98.96  ? 573 GLU   A CD  1 
ATOM   2200 O  OE1 . GLU   A 1 277 ? -24.324 -21.386 20.381 1.00 100.74 ? 573 GLU   A OE1 1 
ATOM   2201 O  OE2 . GLU   A 1 277 ? -22.164 -20.999 20.525 1.00 101.30 ? 573 GLU   A OE2 1 
ATOM   2202 N  N   . ILE   A 1 278 ? -26.971 -19.355 16.484 1.00 57.05  ? 574 ILE   A N   1 
ATOM   2203 C  CA  . ILE   A 1 278 ? -28.328 -19.655 16.038 1.00 65.62  ? 574 ILE   A CA  1 
ATOM   2204 C  C   . ILE   A 1 278 ? -28.356 -21.136 15.688 1.00 72.42  ? 574 ILE   A C   1 
ATOM   2205 O  O   . ILE   A 1 278 ? -27.682 -21.562 14.743 1.00 76.42  ? 574 ILE   A O   1 
ATOM   2206 C  CB  . ILE   A 1 278 ? -28.756 -18.815 14.824 1.00 60.20  ? 574 ILE   A CB  1 
ATOM   2207 C  CG1 . ILE   A 1 278 ? -28.741 -17.326 15.157 1.00 57.02  ? 574 ILE   A CG1 1 
ATOM   2208 C  CG2 . ILE   A 1 278 ? -30.146 -19.220 14.370 1.00 62.61  ? 574 ILE   A CG2 1 
ATOM   2209 C  CD1 . ILE   A 1 278 ? -29.056 -16.476 13.957 1.00 59.92  ? 574 ILE   A CD1 1 
ATOM   2210 N  N   . GLY   A 1 279 ? -29.118 -21.917 16.447 1.00 72.13  ? 575 GLY   A N   1 
ATOM   2211 C  CA  . GLY   A 1 279 ? -29.231 -23.345 16.174 1.00 72.65  ? 575 GLY   A CA  1 
ATOM   2212 C  C   . GLY   A 1 279 ? -27.909 -24.045 15.962 1.00 75.24  ? 575 GLY   A C   1 
ATOM   2213 O  O   . GLY   A 1 279 ? -27.780 -24.854 15.035 1.00 86.17  ? 575 GLY   A O   1 
ATOM   2214 N  N   . GLY   A 1 280 ? -26.912 -23.752 16.799 1.00 76.70  ? 576 GLY   A N   1 
ATOM   2215 C  CA  . GLY   A 1 280 ? -25.613 -24.386 16.678 1.00 78.05  ? 576 GLY   A CA  1 
ATOM   2216 C  C   . GLY   A 1 280 ? -24.689 -23.757 15.664 1.00 73.79  ? 576 GLY   A C   1 
ATOM   2217 O  O   . GLY   A 1 280 ? -23.481 -24.025 15.694 1.00 83.04  ? 576 GLY   A O   1 
ATOM   2218 N  N   . LEU   A 1 281 ? -25.208 -22.923 14.778 1.00 65.78  ? 577 LEU   A N   1 
ATOM   2219 C  CA  . LEU   A 1 281 ? -24.370 -22.235 13.811 1.00 74.61  ? 577 LEU   A CA  1 
ATOM   2220 C  C   . LEU   A 1 281 ? -23.748 -21.002 14.449 1.00 72.70  ? 577 LEU   A C   1 
ATOM   2221 O  O   . LEU   A 1 281 ? -24.375 -20.304 15.254 1.00 68.64  ? 577 LEU   A O   1 
ATOM   2222 C  CB  . LEU   A 1 281 ? -25.180 -21.844 12.577 1.00 73.72  ? 577 LEU   A CB  1 
ATOM   2223 C  CG  . LEU   A 1 281 ? -25.860 -22.952 11.772 1.00 73.13  ? 577 LEU   A CG  1 
ATOM   2224 C  CD1 . LEU   A 1 281 ? -26.681 -22.340 10.634 1.00 68.56  ? 577 LEU   A CD1 1 
ATOM   2225 C  CD2 . LEU   A 1 281 ? -24.861 -23.976 11.227 1.00 69.07  ? 577 LEU   A CD2 1 
ATOM   2226 N  N   . GLU   A 1 282 ? -22.496 -20.739 14.090 1.00 70.28  ? 578 GLU   A N   1 
ATOM   2227 C  CA  . GLU   A 1 282 ? -21.718 -19.682 14.718 1.00 70.66  ? 578 GLU   A CA  1 
ATOM   2228 C  C   . GLU   A 1 282 ? -21.410 -18.607 13.691 1.00 59.97  ? 578 GLU   A C   1 
ATOM   2229 O  O   . GLU   A 1 282 ? -20.762 -18.879 12.674 1.00 63.74  ? 578 GLU   A O   1 
ATOM   2230 C  CB  . GLU   A 1 282 ? -20.433 -20.239 15.328 1.00 73.01  ? 578 GLU   A CB  1 
ATOM   2231 C  CG  . GLU   A 1 282 ? -20.685 -21.274 16.406 1.00 82.41  ? 578 GLU   A CG  1 
ATOM   2232 C  CD  . GLU   A 1 282 ? -19.441 -21.595 17.196 1.00 88.11  ? 578 GLU   A CD  1 
ATOM   2233 O  OE1 . GLU   A 1 282 ? -18.350 -21.591 16.582 1.00 88.96  ? 578 GLU   A OE1 1 
ATOM   2234 O  OE2 . GLU   A 1 282 ? -19.555 -21.841 18.421 1.00 81.11  ? 578 GLU   A OE2 1 
ATOM   2235 N  N   . PHE   A 1 283 ? -21.866 -17.391 13.963 1.00 54.86  ? 579 PHE   A N   1 
ATOM   2236 C  CA  . PHE   A 1 283 ? -21.629 -16.245 13.085 1.00 56.15  ? 579 PHE   A CA  1 
ATOM   2237 C  C   . PHE   A 1 283 ? -20.613 -15.348 13.790 1.00 54.17  ? 579 PHE   A C   1 
ATOM   2238 O  O   . PHE   A 1 283 ? -20.962 -14.549 14.659 1.00 54.42  ? 579 PHE   A O   1 
ATOM   2239 C  CB  . PHE   A 1 283 ? -22.932 -15.517 12.765 1.00 51.73  ? 579 PHE   A CB  1 
ATOM   2240 C  CG  . PHE   A 1 283 ? -23.918 -16.363 12.019 1.00 53.60  ? 579 PHE   A CG  1 
ATOM   2241 C  CD1 . PHE   A 1 283 ? -24.933 -17.031 12.684 1.00 48.22  ? 579 PHE   A CD1 1 
ATOM   2242 C  CD2 . PHE   A 1 283 ? -23.808 -16.516 10.647 1.00 61.31  ? 579 PHE   A CD2 1 
ATOM   2243 C  CE1 . PHE   A 1 283 ? -25.837 -17.837 11.972 1.00 56.53  ? 579 PHE   A CE1 1 
ATOM   2244 C  CE2 . PHE   A 1 283 ? -24.710 -17.300 9.933  1.00 67.64  ? 579 PHE   A CE2 1 
ATOM   2245 C  CZ  . PHE   A 1 283 ? -25.721 -17.963 10.600 1.00 70.27  ? 579 PHE   A CZ  1 
ATOM   2246 N  N   . SER   A 1 284 ? -19.348 -15.488 13.387 1.00 60.45  ? 580 SER   A N   1 
ATOM   2247 C  CA  . SER   A 1 284 ? -18.220 -14.816 14.024 1.00 53.00  ? 580 SER   A CA  1 
ATOM   2248 C  C   . SER   A 1 284 ? -18.155 -13.320 13.718 1.00 57.42  ? 580 SER   A C   1 
ATOM   2249 O  O   . SER   A 1 284 ? -17.402 -12.589 14.374 1.00 62.43  ? 580 SER   A O   1 
ATOM   2250 C  CB  . SER   A 1 284 ? -16.934 -15.495 13.560 1.00 55.96  ? 580 SER   A CB  1 
ATOM   2251 O  OG  . SER   A 1 284 ? -16.896 -15.564 12.131 1.00 61.45  ? 580 SER   A OG  1 
ATOM   2252 N  N   . ALA   A 1 285 ? -18.896 -12.849 12.723 1.00 64.28  ? 581 ALA   A N   1 
ATOM   2253 C  CA  . ALA   A 1 285 ? -18.898 -11.440 12.356 1.00 56.63  ? 581 ALA   A CA  1 
ATOM   2254 C  C   . ALA   A 1 285 ? -20.349 -11.042 12.168 1.00 61.88  ? 581 ALA   A C   1 
ATOM   2255 O  O   . ALA   A 1 285 ? -20.980 -11.430 11.174 1.00 56.18  ? 581 ALA   A O   1 
ATOM   2256 C  CB  . ALA   A 1 285 ? -18.081 -11.188 11.085 1.00 48.86  ? 581 ALA   A CB  1 
ATOM   2257 N  N   . CYS   A 1 286 ? -20.869 -10.280 13.110 1.00 55.67  ? 582 CYS   A N   1 
ATOM   2258 C  CA  . CYS   A 1 286 ? -22.290 -9.986  13.123 1.00 51.17  ? 582 CYS   A CA  1 
ATOM   2259 C  C   . CYS   A 1 286 ? -22.551 -8.611  13.719 1.00 52.99  ? 582 CYS   A C   1 
ATOM   2260 O  O   . CYS   A 1 286 ? -23.416 -8.482  14.599 1.00 49.32  ? 582 CYS   A O   1 
ATOM   2261 C  CB  . CYS   A 1 286 ? -23.024 -11.050 13.931 1.00 49.54  ? 582 CYS   A CB  1 
ATOM   2262 S  SG  . CYS   A 1 286 ? -22.286 -11.273 15.592 1.00 51.70  ? 582 CYS   A SG  1 
ATOM   2263 N  N   . PRO   A 1 287 ? -21.872 -7.560  13.259 1.00 52.17  ? 583 PRO   A N   1 
ATOM   2264 C  CA  . PRO   A 1 287 ? -21.989 -6.275  13.954 1.00 41.02  ? 583 PRO   A CA  1 
ATOM   2265 C  C   . PRO   A 1 287 ? -23.445 -5.848  14.091 1.00 46.96  ? 583 PRO   A C   1 
ATOM   2266 O  O   . PRO   A 1 287 ? -24.277 -6.101  13.215 1.00 44.76  ? 583 PRO   A O   1 
ATOM   2267 C  CB  . PRO   A 1 287 ? -21.174 -5.321  13.079 1.00 44.60  ? 583 PRO   A CB  1 
ATOM   2268 C  CG  . PRO   A 1 287 ? -21.218 -5.952  11.696 1.00 59.49  ? 583 PRO   A CG  1 
ATOM   2269 C  CD  . PRO   A 1 287 ? -21.180 -7.427  11.961 1.00 58.54  ? 583 PRO   A CD  1 
ATOM   2270 N  N   . PHE   A 1 288 ? -23.764 -5.269  15.249 1.00 43.88  ? 584 PHE   A N   1 
ATOM   2271 C  CA  . PHE   A 1 288 ? -25.127 -4.901  15.600 1.00 42.75  ? 584 PHE   A CA  1 
ATOM   2272 C  C   . PHE   A 1 288 ? -25.087 -3.545  16.272 1.00 51.30  ? 584 PHE   A C   1 
ATOM   2273 O  O   . PHE   A 1 288 ? -24.154 -3.239  17.022 1.00 47.93  ? 584 PHE   A O   1 
ATOM   2274 C  CB  . PHE   A 1 288 ? -25.822 -5.950  16.514 1.00 49.88  ? 584 PHE   A CB  1 
ATOM   2275 C  CG  . PHE   A 1 288 ? -25.066 -6.300  17.787 1.00 61.59  ? 584 PHE   A CG  1 
ATOM   2276 C  CD1 . PHE   A 1 288 ? -25.211 -5.543  18.955 1.00 51.85  ? 584 PHE   A CD1 1 
ATOM   2277 C  CD2 . PHE   A 1 288 ? -24.262 -7.429  17.828 1.00 59.32  ? 584 PHE   A CD2 1 
ATOM   2278 C  CE1 . PHE   A 1 288 ? -24.540 -5.901  20.138 1.00 46.34  ? 584 PHE   A CE1 1 
ATOM   2279 C  CE2 . PHE   A 1 288 ? -23.587 -7.782  18.971 1.00 50.16  ? 584 PHE   A CE2 1 
ATOM   2280 C  CZ  . PHE   A 1 288 ? -23.735 -7.026  20.147 1.00 51.28  ? 584 PHE   A CZ  1 
ATOM   2281 N  N   . SER   A 1 289 ? -26.090 -2.726  15.983 1.00 59.59  ? 585 SER   A N   1 
ATOM   2282 C  CA  . SER   A 1 289 ? -26.127 -1.382  16.514 1.00 61.79  ? 585 SER   A CA  1 
ATOM   2283 C  C   . SER   A 1 289 ? -27.502 -1.060  17.088 1.00 55.52  ? 585 SER   A C   1 
ATOM   2284 O  O   . SER   A 1 289 ? -28.524 -1.628  16.689 1.00 50.40  ? 585 SER   A O   1 
ATOM   2285 C  CB  . SER   A 1 289 ? -25.723 -0.367  15.424 1.00 59.31  ? 585 SER   A CB  1 
ATOM   2286 O  OG  . SER   A 1 289 ? -26.610 -0.391  14.318 1.00 52.80  ? 585 SER   A OG  1 
ATOM   2287 N  N   . GLY   A 1 290 ? -27.508 -0.147  18.057 1.00 49.28  ? 586 GLY   A N   1 
ATOM   2288 C  CA  . GLY   A 1 290 ? -28.739 0.481   18.489 1.00 54.37  ? 586 GLY   A CA  1 
ATOM   2289 C  C   . GLY   A 1 290 ? -28.572 1.981   18.653 1.00 62.02  ? 586 GLY   A C   1 
ATOM   2290 O  O   . GLY   A 1 290 ? -28.147 2.686   17.727 1.00 57.85  ? 586 GLY   A O   1 
ATOM   2291 N  N   . TRP   A 1 291 ? -28.914 2.480   19.836 1.00 50.20  ? 587 TRP   A N   1 
ATOM   2292 C  CA  . TRP   A 1 291 ? -28.622 3.855   20.213 1.00 51.85  ? 587 TRP   A CA  1 
ATOM   2293 C  C   . TRP   A 1 291 ? -28.052 3.842   21.623 1.00 56.01  ? 587 TRP   A C   1 
ATOM   2294 O  O   . TRP   A 1 291 ? -28.148 2.848   22.343 1.00 53.52  ? 587 TRP   A O   1 
ATOM   2295 C  CB  . TRP   A 1 291 ? -29.858 4.759   20.130 1.00 52.39  ? 587 TRP   A CB  1 
ATOM   2296 C  CG  . TRP   A 1 291 ? -31.065 4.207   20.781 1.00 66.37  ? 587 TRP   A CG  1 
ATOM   2297 C  CD1 . TRP   A 1 291 ? -31.390 4.281   22.116 1.00 62.69  ? 587 TRP   A CD1 1 
ATOM   2298 C  CD2 . TRP   A 1 291 ? -32.133 3.502   20.142 1.00 67.62  ? 587 TRP   A CD2 1 
ATOM   2299 N  NE1 . TRP   A 1 291 ? -32.594 3.659   22.335 1.00 67.15  ? 587 TRP   A NE1 1 
ATOM   2300 C  CE2 . TRP   A 1 291 ? -33.071 3.172   21.142 1.00 75.00  ? 587 TRP   A CE2 1 
ATOM   2301 C  CE3 . TRP   A 1 291 ? -32.386 3.111   18.822 1.00 74.37  ? 587 TRP   A CE3 1 
ATOM   2302 C  CZ2 . TRP   A 1 291 ? -34.243 2.467   20.863 1.00 77.54  ? 587 TRP   A CZ2 1 
ATOM   2303 C  CZ3 . TRP   A 1 291 ? -33.554 2.416   18.546 1.00 74.91  ? 587 TRP   A CZ3 1 
ATOM   2304 C  CH2 . TRP   A 1 291 ? -34.465 2.098   19.562 1.00 83.01  ? 587 TRP   A CH2 1 
ATOM   2305 N  N   . TYR   A 1 292 ? -27.442 4.950   22.006 1.00 61.78  ? 588 TYR   A N   1 
ATOM   2306 C  CA  . TYR   A 1 292 ? -26.725 4.994   23.268 1.00 65.27  ? 588 TYR   A CA  1 
ATOM   2307 C  C   . TYR   A 1 292 ? -27.674 5.229   24.431 1.00 59.88  ? 588 TYR   A C   1 
ATOM   2308 O  O   . TYR   A 1 292 ? -28.646 5.984   24.327 1.00 57.66  ? 588 TYR   A O   1 
ATOM   2309 C  CB  . TYR   A 1 292 ? -25.665 6.094   23.238 1.00 65.65  ? 588 TYR   A CB  1 
ATOM   2310 C  CG  . TYR   A 1 292 ? -24.277 5.619   22.858 1.00 65.10  ? 588 TYR   A CG  1 
ATOM   2311 C  CD1 . TYR   A 1 292 ? -23.694 6.012   21.659 1.00 54.88  ? 588 TYR   A CD1 1 
ATOM   2312 C  CD2 . TYR   A 1 292 ? -23.544 4.787   23.716 1.00 60.95  ? 588 TYR   A CD2 1 
ATOM   2313 C  CE1 . TYR   A 1 292 ? -22.420 5.612   21.320 1.00 57.97  ? 588 TYR   A CE1 1 
ATOM   2314 C  CE2 . TYR   A 1 292 ? -22.265 4.377   23.387 1.00 64.69  ? 588 TYR   A CE2 1 
ATOM   2315 C  CZ  . TYR   A 1 292 ? -21.715 4.786   22.177 1.00 61.17  ? 588 TYR   A CZ  1 
ATOM   2316 O  OH  . TYR   A 1 292 ? -20.448 4.376   21.841 1.00 59.24  ? 588 TYR   A OH  1 
ATOM   2317 N  N   . MET   A 1 293 ? -27.388 4.572   25.542 1.00 53.72  ? 589 MET   A N   1 
ATOM   2318 C  CA  . MET   A 1 293 ? -27.775 5.134   26.818 1.00 61.62  ? 589 MET   A CA  1 
ATOM   2319 C  C   . MET   A 1 293 ? -26.709 6.153   27.214 1.00 65.28  ? 589 MET   A C   1 
ATOM   2320 O  O   . MET   A 1 293 ? -25.512 5.918   27.017 1.00 71.18  ? 589 MET   A O   1 
ATOM   2321 C  CB  . MET   A 1 293 ? -27.916 4.038   27.873 1.00 58.12  ? 589 MET   A CB  1 
ATOM   2322 C  CG  . MET   A 1 293 ? -28.636 4.486   29.125 1.00 58.06  ? 589 MET   A CG  1 
ATOM   2323 S  SD  . MET   A 1 293 ? -29.006 3.097   30.216 1.00 54.09  ? 589 MET   A SD  1 
ATOM   2324 C  CE  . MET   A 1 293 ? -27.375 2.518   30.691 1.00 57.19  ? 589 MET   A CE  1 
ATOM   2325 N  N   . GLY   A 1 294 ? -27.156 7.307   27.724 1.00 59.88  ? 590 GLY   A N   1 
ATOM   2326 C  CA  . GLY   A 1 294 ? -26.235 8.402   28.007 1.00 50.81  ? 590 GLY   A CA  1 
ATOM   2327 C  C   . GLY   A 1 294 ? -25.028 7.982   28.816 1.00 57.63  ? 590 GLY   A C   1 
ATOM   2328 O  O   . GLY   A 1 294 ? -23.911 8.452   28.574 1.00 62.35  ? 590 GLY   A O   1 
ATOM   2329 N  N   . THR   A 1 295 ? -25.233 7.084   29.789 1.00 56.74  ? 591 THR   A N   1 
ATOM   2330 C  CA  . THR   A 1 295 ? -24.185 6.810   30.763 1.00 60.70  ? 591 THR   A CA  1 
ATOM   2331 C  C   . THR   A 1 295 ? -23.010 6.049   30.161 1.00 60.74  ? 591 THR   A C   1 
ATOM   2332 O  O   . THR   A 1 295 ? -21.890 6.142   30.676 1.00 54.14  ? 591 THR   A O   1 
ATOM   2333 C  CB  . THR   A 1 295 ? -24.765 6.052   31.952 1.00 55.01  ? 591 THR   A CB  1 
ATOM   2334 O  OG1 . THR   A 1 295 ? -25.472 4.902   31.495 1.00 52.17  ? 591 THR   A OG1 1 
ATOM   2335 C  CG2 . THR   A 1 295 ? -25.722 6.968   32.724 1.00 56.76  ? 591 THR   A CG2 1 
ATOM   2336 N  N   . GLU   A 1 296 ? -23.223 5.301   29.082 1.00 55.29  ? 592 GLU   A N   1 
ATOM   2337 C  CA  . GLU   A 1 296 ? -22.087 4.655   28.436 1.00 52.47  ? 592 GLU   A CA  1 
ATOM   2338 C  C   . GLU   A 1 296 ? -21.045 5.692   28.040 1.00 53.27  ? 592 GLU   A C   1 
ATOM   2339 O  O   . GLU   A 1 296 ? -19.848 5.514   28.301 1.00 70.09  ? 592 GLU   A O   1 
ATOM   2340 C  CB  . GLU   A 1 296 ? -22.557 3.864   27.222 1.00 58.90  ? 592 GLU   A CB  1 
ATOM   2341 C  CG  . GLU   A 1 296 ? -23.613 2.810   27.519 1.00 56.66  ? 592 GLU   A CG  1 
ATOM   2342 C  CD  . GLU   A 1 296 ? -24.173 2.244   26.198 1.00 63.43  ? 592 GLU   A CD  1 
ATOM   2343 O  OE1 . GLU   A 1 296 ? -23.480 1.410   25.592 1.00 46.81  ? 592 GLU   A OE1 1 
ATOM   2344 O  OE2 . GLU   A 1 296 ? -25.267 2.661   25.757 1.00 60.51  ? 592 GLU   A OE2 1 
ATOM   2345 N  N   . ILE   A 1 297 ? -21.492 6.801   27.433 1.00 58.28  ? 593 ILE   A N   1 
ATOM   2346 C  CA  . ILE   A 1 297 ? -20.591 7.901   27.077 1.00 58.74  ? 593 ILE   A CA  1 
ATOM   2347 C  C   . ILE   A 1 297 ? -20.188 8.697   28.311 1.00 68.13  ? 593 ILE   A C   1 
ATOM   2348 O  O   . ILE   A 1 297 ? -18.998 8.891   28.588 1.00 62.90  ? 593 ILE   A O   1 
ATOM   2349 C  CB  . ILE   A 1 297 ? -21.250 8.840   26.059 1.00 64.58  ? 593 ILE   A CB  1 
ATOM   2350 C  CG1 . ILE   A 1 297 ? -21.769 8.077   24.846 1.00 61.20  ? 593 ILE   A CG1 1 
ATOM   2351 C  CG2 . ILE   A 1 297 ? -20.261 9.894   25.625 1.00 71.54  ? 593 ILE   A CG2 1 
ATOM   2352 C  CD1 . ILE   A 1 297 ? -22.784 8.909   24.116 1.00 54.49  ? 593 ILE   A CD1 1 
ATOM   2353 N  N   . GLY   A 1 298 ? -21.183 9.240   29.017 1.00 72.59  ? 594 GLY   A N   1 
ATOM   2354 C  CA  . GLY   A 1 298 ? -20.902 10.252  30.023 1.00 75.59  ? 594 GLY   A CA  1 
ATOM   2355 C  C   . GLY   A 1 298 ? -20.229 9.690   31.257 1.00 68.41  ? 594 GLY   A C   1 
ATOM   2356 O  O   . GLY   A 1 298 ? -19.463 10.386  31.927 1.00 79.51  ? 594 GLY   A O   1 
ATOM   2357 N  N   . VAL   A 1 299 ? -20.499 8.427   31.580 1.00 70.03  ? 595 VAL   A N   1 
ATOM   2358 C  CA  . VAL   A 1 299 ? -19.933 7.850   32.799 1.00 73.93  ? 595 VAL   A CA  1 
ATOM   2359 C  C   . VAL   A 1 299 ? -18.719 6.985   32.480 1.00 66.51  ? 595 VAL   A C   1 
ATOM   2360 O  O   . VAL   A 1 299 ? -17.626 7.208   33.007 1.00 67.16  ? 595 VAL   A O   1 
ATOM   2361 C  CB  . VAL   A 1 299 ? -20.977 7.031   33.577 1.00 66.14  ? 595 VAL   A CB  1 
ATOM   2362 C  CG1 . VAL   A 1 299 ? -20.372 6.577   34.871 1.00 60.18  ? 595 VAL   A CG1 1 
ATOM   2363 C  CG2 . VAL   A 1 299 ? -22.236 7.850   33.835 1.00 59.41  ? 595 VAL   A CG2 1 
ATOM   2364 N  N   . ARG   A 1 300 ? -18.906 5.990   31.618 1.00 64.25  ? 596 ARG   A N   1 
ATOM   2365 C  CA  . ARG   A 1 300 ? -17.849 5.025   31.328 1.00 65.94  ? 596 ARG   A CA  1 
ATOM   2366 C  C   . ARG   A 1 300 ? -16.831 5.572   30.320 1.00 75.13  ? 596 ARG   A C   1 
ATOM   2367 O  O   . ARG   A 1 300 ? -15.641 5.706   30.637 1.00 69.51  ? 596 ARG   A O   1 
ATOM   2368 C  CB  . ARG   A 1 300 ? -18.476 3.712   30.828 1.00 58.84  ? 596 ARG   A CB  1 
ATOM   2369 C  CG  . ARG   A 1 300 ? -19.571 3.141   31.741 1.00 52.89  ? 596 ARG   A CG  1 
ATOM   2370 C  CD  . ARG   A 1 300 ? -19.021 2.903   33.174 1.00 55.30  ? 596 ARG   A CD  1 
ATOM   2371 N  NE  . ARG   A 1 300 ? -17.832 2.051   33.141 1.00 51.74  ? 596 ARG   A NE  1 
ATOM   2372 C  CZ  . ARG   A 1 300 ? -17.841 0.777   32.738 1.00 53.58  ? 596 ARG   A CZ  1 
ATOM   2373 N  NH1 . ARG   A 1 300 ? -18.975 0.188   32.373 1.00 57.15  ? 596 ARG   A NH1 1 
ATOM   2374 N  NH2 . ARG   A 1 300 ? -16.716 0.081   32.701 1.00 51.17  ? 596 ARG   A NH2 1 
ATOM   2375 N  N   . ASP   A 1 301 ? -17.282 5.889   29.096 1.00 52.39  ? 597 ASP   A N   1 
ATOM   2376 C  CA  . ASP   A 1 301 ? -16.367 6.417   28.077 1.00 59.08  ? 597 ASP   A CA  1 
ATOM   2377 C  C   . ASP   A 1 301 ? -15.602 7.637   28.588 1.00 59.86  ? 597 ASP   A C   1 
ATOM   2378 O  O   . ASP   A 1 301 ? -14.374 7.722   28.455 1.00 66.38  ? 597 ASP   A O   1 
ATOM   2379 C  CB  . ASP   A 1 301 ? -17.134 6.761   26.787 1.00 58.81  ? 597 ASP   A CB  1 
ATOM   2380 C  CG  . ASP   A 1 301 ? -17.609 5.526   26.034 1.00 57.07  ? 597 ASP   A CG  1 
ATOM   2381 O  OD1 . ASP   A 1 301 ? -16.946 4.469   26.138 1.00 67.15  ? 597 ASP   A OD1 1 
ATOM   2382 O  OD2 . ASP   A 1 301 ? -18.648 5.601   25.333 1.00 62.70  ? 597 ASP   A OD2 1 
ATOM   2383 N  N   . TYR   A 1 302 ? -16.306 8.584   29.199 1.00 65.68  ? 598 TYR   A N   1 
ATOM   2384 C  CA  . TYR   A 1 302 ? -15.668 9.836   29.588 1.00 72.70  ? 598 TYR   A CA  1 
ATOM   2385 C  C   . TYR   A 1 302 ? -14.935 9.764   30.929 1.00 81.35  ? 598 TYR   A C   1 
ATOM   2386 O  O   . TYR   A 1 302 ? -13.928 10.465  31.109 1.00 81.15  ? 598 TYR   A O   1 
ATOM   2387 C  CB  . TYR   A 1 302 ? -16.714 10.950  29.633 1.00 80.80  ? 598 TYR   A CB  1 
ATOM   2388 C  CG  . TYR   A 1 302 ? -17.049 11.511  28.265 1.00 90.01  ? 598 TYR   A CG  1 
ATOM   2389 C  CD1 . TYR   A 1 302 ? -18.231 12.207  28.049 1.00 88.43  ? 598 TYR   A CD1 1 
ATOM   2390 C  CD2 . TYR   A 1 302 ? -16.177 11.350  27.194 1.00 86.98  ? 598 TYR   A CD2 1 
ATOM   2391 C  CE1 . TYR   A 1 302 ? -18.540 12.733  26.798 1.00 87.74  ? 598 TYR   A CE1 1 
ATOM   2392 C  CE2 . TYR   A 1 302 ? -16.481 11.864  25.931 1.00 94.56  ? 598 TYR   A CE2 1 
ATOM   2393 C  CZ  . TYR   A 1 302 ? -17.664 12.551  25.749 1.00 88.94  ? 598 TYR   A CZ  1 
ATOM   2394 O  OH  . TYR   A 1 302 ? -17.976 13.074  24.518 1.00 70.11  ? 598 TYR   A OH  1 
ATOM   2395 N  N   . CYS   A 1 303 ? -15.405 8.952   31.885 1.00 76.07  ? 599 CYS   A N   1 
ATOM   2396 C  CA  . CYS   A 1 303 ? -14.932 9.087   33.263 1.00 73.94  ? 599 CYS   A CA  1 
ATOM   2397 C  C   . CYS   A 1 303 ? -14.317 7.833   33.874 1.00 74.16  ? 599 CYS   A C   1 
ATOM   2398 O  O   . CYS   A 1 303 ? -13.824 7.909   35.012 1.00 76.66  ? 599 CYS   A O   1 
ATOM   2399 C  CB  . CYS   A 1 303 ? -16.075 9.576   34.165 1.00 78.87  ? 599 CYS   A CB  1 
ATOM   2400 S  SG  . CYS   A 1 303 ? -16.751 11.186  33.674 1.00 82.83  ? 599 CYS   A SG  1 
ATOM   2401 N  N   . ASP   A 1 304 ? -14.319 6.694   33.175 1.00 71.56  ? 600 ASP   A N   1 
ATOM   2402 C  CA  . ASP   A 1 304 ? -13.463 5.587   33.587 1.00 80.00  ? 600 ASP   A CA  1 
ATOM   2403 C  C   . ASP   A 1 304 ? -12.022 6.075   33.687 1.00 85.50  ? 600 ASP   A C   1 
ATOM   2404 O  O   . ASP   A 1 304 ? -11.552 6.843   32.843 1.00 91.94  ? 600 ASP   A O   1 
ATOM   2405 C  CB  . ASP   A 1 304 ? -13.543 4.418   32.596 1.00 86.65  ? 600 ASP   A CB  1 
ATOM   2406 C  CG  . ASP   A 1 304 ? -14.652 3.427   32.923 1.00 84.44  ? 600 ASP   A CG  1 
ATOM   2407 O  OD1 . ASP   A 1 304 ? -15.507 3.738   33.779 1.00 76.15  ? 600 ASP   A OD1 1 
ATOM   2408 O  OD2 . ASP   A 1 304 ? -14.661 2.328   32.317 1.00 78.35  ? 600 ASP   A OD2 1 
ATOM   2409 N  N   . ASN   A 1 305 ? -11.328 5.642   34.741 1.00 85.06  ? 601 ASN   A N   1 
ATOM   2410 C  CA  . ASN   A 1 305 ? -9.931  6.030   34.916 1.00 82.53  ? 601 ASN   A CA  1 
ATOM   2411 C  C   . ASN   A 1 305 ? -9.086  5.615   33.720 1.00 78.78  ? 601 ASN   A C   1 
ATOM   2412 O  O   . ASN   A 1 305 ? -8.180  6.349   33.307 1.00 85.85  ? 601 ASN   A O   1 
ATOM   2413 C  CB  . ASN   A 1 305 ? -9.366  5.416   36.199 1.00 73.99  ? 601 ASN   A CB  1 
ATOM   2414 C  CG  . ASN   A 1 305 ? -9.599  6.293   37.410 1.00 94.43  ? 601 ASN   A CG  1 
ATOM   2415 O  OD1 . ASN   A 1 305 ? -9.656  7.519   37.297 1.00 105.95 ? 601 ASN   A OD1 1 
ATOM   2416 N  ND2 . ASN   A 1 305 ? -9.733  5.673   38.579 1.00 89.15  ? 601 ASN   A ND2 1 
ATOM   2417 N  N   . SER   A 1 306 ? -9.364  4.442   33.155 1.00 83.09  ? 602 SER   A N   1 
ATOM   2418 C  CA  . SER   A 1 306 ? -8.600  3.919   32.033 1.00 82.86  ? 602 SER   A CA  1 
ATOM   2419 C  C   . SER   A 1 306 ? -9.219  4.259   30.681 1.00 83.73  ? 602 SER   A C   1 
ATOM   2420 O  O   . SER   A 1 306 ? -8.781  3.711   29.665 1.00 84.21  ? 602 SER   A O   1 
ATOM   2421 C  CB  . SER   A 1 306 ? -8.436  2.401   32.172 1.00 83.44  ? 602 SER   A CB  1 
ATOM   2422 O  OG  . SER   A 1 306 ? -9.695  1.751   32.162 1.00 84.03  ? 602 SER   A OG  1 
ATOM   2423 N  N   . ARG   A 1 307 ? -10.228 5.134   30.643 1.00 77.11  ? 603 ARG   A N   1 
ATOM   2424 C  CA  . ARG   A 1 307 ? -10.714 5.661   29.371 1.00 83.13  ? 603 ARG   A CA  1 
ATOM   2425 C  C   . ARG   A 1 307 ? -10.346 7.135   29.259 1.00 84.61  ? 603 ARG   A C   1 
ATOM   2426 O  O   . ARG   A 1 307 ? -9.198  7.498   29.534 1.00 95.79  ? 603 ARG   A O   1 
ATOM   2427 C  CB  . ARG   A 1 307 ? -12.221 5.433   29.238 1.00 72.75  ? 603 ARG   A CB  1 
ATOM   2428 C  CG  . ARG   A 1 307 ? -12.605 3.971   29.347 1.00 76.32  ? 603 ARG   A CG  1 
ATOM   2429 C  CD  . ARG   A 1 307 ? -12.178 3.185   28.114 1.00 72.73  ? 603 ARG   A CD  1 
ATOM   2430 N  NE  . ARG   A 1 307 ? -12.723 3.791   26.913 1.00 68.55  ? 603 ARG   A NE  1 
ATOM   2431 C  CZ  . ARG   A 1 307 ? -13.993 3.679   26.545 1.00 67.28  ? 603 ARG   A CZ  1 
ATOM   2432 N  NH1 . ARG   A 1 307 ? -14.831 2.977   27.292 1.00 55.35  ? 603 ARG   A NH1 1 
ATOM   2433 N  NH2 . ARG   A 1 307 ? -14.430 4.269   25.435 1.00 72.17  ? 603 ARG   A NH2 1 
ATOM   2434 N  N   . TYR   A 1 308 ? -11.300 7.993   28.881 1.00 82.16  ? 604 TYR   A N   1 
ATOM   2435 C  CA  . TYR   A 1 308 ? -10.964 9.393   28.617 1.00 82.55  ? 604 TYR   A CA  1 
ATOM   2436 C  C   . TYR   A 1 308 ? -10.635 10.148  29.896 1.00 93.91  ? 604 TYR   A C   1 
ATOM   2437 O  O   . TYR   A 1 308 ? -9.752  11.017  29.890 1.00 100.30 ? 604 TYR   A O   1 
ATOM   2438 C  CB  . TYR   A 1 308 ? -12.096 10.085  27.858 1.00 86.72  ? 604 TYR   A CB  1 
ATOM   2439 C  CG  . TYR   A 1 308 ? -11.942 9.951   26.355 1.00 85.08  ? 604 TYR   A CG  1 
ATOM   2440 C  CD1 . TYR   A 1 308 ? -12.386 8.818   25.688 1.00 81.83  ? 604 TYR   A CD1 1 
ATOM   2441 C  CD2 . TYR   A 1 308 ? -11.334 10.951  25.614 1.00 98.07  ? 604 TYR   A CD2 1 
ATOM   2442 C  CE1 . TYR   A 1 308 ? -12.239 8.689   24.325 1.00 88.28  ? 604 TYR   A CE1 1 
ATOM   2443 C  CE2 . TYR   A 1 308 ? -11.178 10.830  24.237 1.00 99.43  ? 604 TYR   A CE2 1 
ATOM   2444 C  CZ  . TYR   A 1 308 ? -11.638 9.697   23.600 1.00 98.04  ? 604 TYR   A CZ  1 
ATOM   2445 O  OH  . TYR   A 1 308 ? -11.499 9.553   22.236 1.00 102.19 ? 604 TYR   A OH  1 
ATOM   2446 N  N   . ASN   A 1 309 ? -11.331 9.845   30.990 1.00 80.91  ? 605 ASN   A N   1 
ATOM   2447 C  CA  . ASN   A 1 309 ? -10.894 10.259  32.317 1.00 87.91  ? 605 ASN   A CA  1 
ATOM   2448 C  C   . ASN   A 1 309 ? -10.880 11.786  32.439 1.00 98.12  ? 605 ASN   A C   1 
ATOM   2449 O  O   . ASN   A 1 309 ? -9.834  12.419  32.624 1.00 110.82 ? 605 ASN   A O   1 
ATOM   2450 C  CB  . ASN   A 1 309 ? -9.517  9.658   32.611 1.00 86.87  ? 605 ASN   A CB  1 
ATOM   2451 C  CG  . ASN   A 1 309 ? -9.136  9.787   34.035 1.00 87.12  ? 605 ASN   A CG  1 
ATOM   2452 O  OD1 . ASN   A 1 309 ? -10.004 9.824   34.903 1.00 79.50  ? 605 ASN   A OD1 1 
ATOM   2453 N  ND2 . ASN   A 1 309 ? -7.835  9.884   34.300 1.00 88.04  ? 605 ASN   A ND2 1 
ATOM   2454 N  N   . ILE   A 1 310 ? -12.075 12.370  32.331 1.00 90.83  ? 606 ILE   A N   1 
ATOM   2455 C  CA  . ILE   A 1 310 ? -12.228 13.816  32.251 1.00 96.71  ? 606 ILE   A CA  1 
ATOM   2456 C  C   . ILE   A 1 310 ? -12.780 14.418  33.538 1.00 91.33  ? 606 ILE   A C   1 
ATOM   2457 O  O   . ILE   A 1 310 ? -13.067 15.616  33.564 1.00 99.94  ? 606 ILE   A O   1 
ATOM   2458 C  CB  . ILE   A 1 310 ? -13.110 14.211  31.058 1.00 95.67  ? 606 ILE   A CB  1 
ATOM   2459 C  CG1 . ILE   A 1 310 ? -14.536 13.704  31.269 1.00 94.65  ? 606 ILE   A CG1 1 
ATOM   2460 C  CG2 . ILE   A 1 310 ? -12.533 13.662  29.778 1.00 76.76  ? 606 ILE   A CG2 1 
ATOM   2461 C  CD1 . ILE   A 1 310 ? -15.507 14.223  30.244 1.00 73.51  ? 606 ILE   A CD1 1 
ATOM   2462 N  N   . LEU   A 1 311 ? -12.963 13.614  34.601 1.00 90.60  ? 607 LEU   A N   1 
ATOM   2463 C  CA  . LEU   A 1 311 ? -13.413 14.170  35.881 1.00 90.50  ? 607 LEU   A CA  1 
ATOM   2464 C  C   . LEU   A 1 311 ? -12.477 15.261  36.375 1.00 88.57  ? 607 LEU   A C   1 
ATOM   2465 O  O   . LEU   A 1 311 ? -12.944 16.261  36.928 1.00 92.44  ? 607 LEU   A O   1 
ATOM   2466 C  CB  . LEU   A 1 311 ? -13.538 13.081  36.949 1.00 74.18  ? 607 LEU   A CB  1 
ATOM   2467 C  CG  . LEU   A 1 311 ? -14.719 12.114  36.796 1.00 73.89  ? 607 LEU   A CG  1 
ATOM   2468 C  CD1 . LEU   A 1 311 ? -14.627 10.963  37.811 1.00 74.41  ? 607 LEU   A CD1 1 
ATOM   2469 C  CD2 . LEU   A 1 311 ? -16.039 12.867  36.914 1.00 73.98  ? 607 LEU   A CD2 1 
ATOM   2470 N  N   . GLU   A 1 312 ? -11.163 15.096  36.176 1.00 96.32  ? 608 GLU   A N   1 
ATOM   2471 C  CA  . GLU   A 1 312 ? -10.186 16.147  36.461 1.00 119.28 ? 608 GLU   A CA  1 
ATOM   2472 C  C   . GLU   A 1 312 ? -10.575 17.490  35.852 1.00 117.82 ? 608 GLU   A C   1 
ATOM   2473 O  O   . GLU   A 1 312 ? -10.871 18.449  36.576 1.00 112.18 ? 608 GLU   A O   1 
ATOM   2474 C  CB  . GLU   A 1 312 ? -8.799  15.763  35.932 1.00 132.68 ? 608 GLU   A CB  1 
ATOM   2475 C  CG  . GLU   A 1 312 ? -8.149  14.558  36.580 1.00 136.56 ? 608 GLU   A CG  1 
ATOM   2476 C  CD  . GLU   A 1 312 ? -7.432  14.897  37.866 1.00 148.62 ? 608 GLU   A CD  1 
ATOM   2477 O  OE1 . GLU   A 1 312 ? -7.956  15.719  38.645 1.00 152.43 ? 608 GLU   A OE1 1 
ATOM   2478 O  OE2 . GLU   A 1 312 ? -6.336  14.345  38.094 1.00 152.47 ? 608 GLU   A OE2 1 
ATOM   2479 N  N   . GLU   A 1 313 ? -10.571 17.562  34.516 1.00 119.80 ? 609 GLU   A N   1 
ATOM   2480 C  CA  . GLU   A 1 313 ? -10.719 18.848  33.841 1.00 133.19 ? 609 GLU   A CA  1 
ATOM   2481 C  C   . GLU   A 1 313 ? -12.117 19.429  33.997 1.00 130.71 ? 609 GLU   A C   1 
ATOM   2482 O  O   . GLU   A 1 313 ? -12.274 20.655  33.996 1.00 147.87 ? 609 GLU   A O   1 
ATOM   2483 C  CB  . GLU   A 1 313 ? -10.368 18.720  32.359 1.00 151.24 ? 609 GLU   A CB  1 
ATOM   2484 C  CG  . GLU   A 1 313 ? -8.875  18.800  32.049 1.00 164.18 ? 609 GLU   A CG  1 
ATOM   2485 C  CD  . GLU   A 1 313 ? -8.295  20.203  32.208 1.00 173.22 ? 609 GLU   A CD  1 
ATOM   2486 O  OE1 . GLU   A 1 313 ? -8.394  20.791  33.310 1.00 173.54 ? 609 GLU   A OE1 1 
ATOM   2487 O  OE2 . GLU   A 1 313 ? -7.730  20.716  31.219 1.00 175.30 ? 609 GLU   A OE2 1 
ATOM   2488 N  N   . VAL   A 1 314 ? -13.141 18.588  34.126 1.00 114.45 ? 610 VAL   A N   1 
ATOM   2489 C  CA  . VAL   A 1 314 ? -14.491 19.117  34.289 1.00 109.49 ? 610 VAL   A CA  1 
ATOM   2490 C  C   . VAL   A 1 314 ? -14.647 19.757  35.664 1.00 109.47 ? 610 VAL   A C   1 
ATOM   2491 O  O   . VAL   A 1 314 ? -15.145 20.882  35.789 1.00 102.87 ? 610 VAL   A O   1 
ATOM   2492 C  CB  . VAL   A 1 314 ? -15.536 18.017  34.053 1.00 105.46 ? 610 VAL   A CB  1 
ATOM   2493 C  CG1 . VAL   A 1 314 ? -16.925 18.526  34.413 1.00 106.25 ? 610 VAL   A CG1 1 
ATOM   2494 C  CG2 . VAL   A 1 314 ? -15.489 17.554  32.602 1.00 97.44  ? 610 VAL   A CG2 1 
ATOM   2495 N  N   . ALA   A 1 315 ? -14.222 19.046  36.717 1.00 100.00 ? 611 ALA   A N   1 
ATOM   2496 C  CA  . ALA   A 1 315 ? -14.281 19.604  38.062 1.00 108.76 ? 611 ALA   A CA  1 
ATOM   2497 C  C   . ALA   A 1 315 ? -13.443 20.865  38.169 1.00 118.25 ? 611 ALA   A C   1 
ATOM   2498 O  O   . ALA   A 1 315 ? -13.817 21.798  38.886 1.00 118.43 ? 611 ALA   A O   1 
ATOM   2499 C  CB  . ALA   A 1 315 ? -13.818 18.567  39.088 1.00 103.57 ? 611 ALA   A CB  1 
ATOM   2500 N  N   . LYS   A 1 316 ? -12.316 20.914  37.454 1.00 119.63 ? 612 LYS   A N   1 
ATOM   2501 C  CA  . LYS   A 1 316 ? -11.499 22.120  37.415 1.00 124.66 ? 612 LYS   A CA  1 
ATOM   2502 C  C   . LYS   A 1 316 ? -12.325 23.320  36.977 1.00 132.29 ? 612 LYS   A C   1 
ATOM   2503 O  O   . LYS   A 1 316 ? -12.523 24.272  37.741 1.00 136.71 ? 612 LYS   A O   1 
ATOM   2504 C  CB  . LYS   A 1 316 ? -10.305 21.917  36.475 1.00 116.55 ? 612 LYS   A CB  1 
ATOM   2505 C  CG  . LYS   A 1 316 ? -9.106  21.224  37.104 1.00 115.09 ? 612 LYS   A CG  1 
ATOM   2506 C  CD  . LYS   A 1 316 ? -7.813  21.637  36.410 1.00 121.59 ? 612 LYS   A CD  1 
ATOM   2507 C  CE  . LYS   A 1 316 ? -7.679  23.157  36.394 1.00 133.77 ? 612 LYS   A CE  1 
ATOM   2508 N  NZ  . LYS   A 1 316 ? -6.330  23.662  36.000 1.00 131.97 ? 612 LYS   A NZ  1 
ATOM   2509 N  N   . LYS   A 1 317 ? -12.840 23.269  35.745 1.00 125.70 ? 613 LYS   A N   1 
ATOM   2510 C  CA  . LYS   A 1 317 ? -13.607 24.381  35.196 1.00 132.84 ? 613 LYS   A CA  1 
ATOM   2511 C  C   . LYS   A 1 317 ? -14.866 24.673  36.002 1.00 138.07 ? 613 LYS   A C   1 
ATOM   2512 O  O   . LYS   A 1 317 ? -15.385 25.794  35.933 1.00 147.06 ? 613 LYS   A O   1 
ATOM   2513 C  CB  . LYS   A 1 317 ? -13.985 24.103  33.739 1.00 119.91 ? 613 LYS   A CB  1 
ATOM   2514 C  CG  . LYS   A 1 317 ? -12.956 24.527  32.709 1.00 126.46 ? 613 LYS   A CG  1 
ATOM   2515 C  CD  . LYS   A 1 317 ? -12.052 23.374  32.332 1.00 126.47 ? 613 LYS   A CD  1 
ATOM   2516 C  CE  . LYS   A 1 317 ? -10.954 23.837  31.394 1.00 136.61 ? 613 LYS   A CE  1 
ATOM   2517 N  NZ  . LYS   A 1 317 ? -10.202 22.694  30.802 1.00 137.40 ? 613 LYS   A NZ  1 
ATOM   2518 N  N   . MET   A 1 318 ? -15.376 23.691  36.750 1.00 135.72 ? 614 MET   A N   1 
ATOM   2519 C  CA  . MET   A 1 318 ? -16.485 23.940  37.662 1.00 130.38 ? 614 MET   A CA  1 
ATOM   2520 C  C   . MET   A 1 318 ? -16.049 24.665  38.919 1.00 130.20 ? 614 MET   A C   1 
ATOM   2521 O  O   . MET   A 1 318 ? -16.908 25.196  39.629 1.00 142.41 ? 614 MET   A O   1 
ATOM   2522 C  CB  . MET   A 1 318 ? -17.172 22.630  38.056 1.00 112.81 ? 614 MET   A CB  1 
ATOM   2523 C  CG  . MET   A 1 318 ? -17.923 21.976  36.900 1.00 117.92 ? 614 MET   A CG  1 
ATOM   2524 S  SD  . MET   A 1 318 ? -18.786 20.462  37.357 1.00 101.74 ? 614 MET   A SD  1 
ATOM   2525 C  CE  . MET   A 1 318 ? -19.902 21.083  38.615 1.00 103.58 ? 614 MET   A CE  1 
ATOM   2526 N  N   . ASP   A 1 319 ? -14.742 24.708  39.195 1.00 135.48 ? 615 ASP   A N   1 
ATOM   2527 C  CA  . ASP   A 1 319 ? -14.200 25.237  40.444 1.00 145.64 ? 615 ASP   A CA  1 
ATOM   2528 C  C   . ASP   A 1 319 ? -14.771 24.460  41.625 1.00 135.68 ? 615 ASP   A C   1 
ATOM   2529 O  O   . ASP   A 1 319 ? -15.768 24.876  42.224 1.00 133.08 ? 615 ASP   A O   1 
ATOM   2530 C  CB  . ASP   A 1 319 ? -14.492 26.736  40.576 1.00 155.78 ? 615 ASP   A CB  1 
ATOM   2531 C  CG  . ASP   A 1 319 ? -13.471 27.460  41.434 1.00 162.90 ? 615 ASP   A CG  1 
ATOM   2532 O  OD1 . ASP   A 1 319 ? -12.262 27.354  41.139 1.00 164.02 ? 615 ASP   A OD1 1 
ATOM   2533 O  OD2 . ASP   A 1 319 ? -13.879 28.148  42.394 1.00 165.85 ? 615 ASP   A OD2 1 
ATOM   2534 N  N   . LEU   A 1 320 ? -14.147 23.328  41.958 1.00 130.20 ? 616 LEU   A N   1 
ATOM   2535 C  CA  . LEU   A 1 320 ? -14.666 22.393  42.948 1.00 122.96 ? 616 LEU   A CA  1 
ATOM   2536 C  C   . LEU   A 1 320 ? -13.631 22.116  44.030 1.00 126.75 ? 616 LEU   A C   1 
ATOM   2537 O  O   . LEU   A 1 320 ? -12.422 22.161  43.783 1.00 133.17 ? 616 LEU   A O   1 
ATOM   2538 C  CB  . LEU   A 1 320 ? -15.085 21.056  42.296 1.00 104.14 ? 616 LEU   A CB  1 
ATOM   2539 C  CG  . LEU   A 1 320 ? -16.345 21.100  41.433 1.00 107.08 ? 616 LEU   A CG  1 
ATOM   2540 C  CD1 . LEU   A 1 320 ? -16.730 19.693  40.947 1.00 109.11 ? 616 LEU   A CD1 1 
ATOM   2541 C  CD2 . LEU   A 1 320 ? -17.505 21.753  42.159 1.00 104.30 ? 616 LEU   A CD2 1 
ATOM   2542 N  N   . ASP   A 1 321 ? -14.126 21.810  45.232 1.00 121.33 ? 617 ASP   A N   1 
ATOM   2543 C  CA  . ASP   A 1 321 ? -13.281 21.363  46.333 1.00 120.40 ? 617 ASP   A CA  1 
ATOM   2544 C  C   . ASP   A 1 321 ? -12.607 20.049  45.955 1.00 111.05 ? 617 ASP   A C   1 
ATOM   2545 O  O   . ASP   A 1 321 ? -13.098 18.973  46.312 1.00 99.05  ? 617 ASP   A O   1 
ATOM   2546 C  CB  . ASP   A 1 321 ? -14.114 21.196  47.612 1.00 126.05 ? 617 ASP   A CB  1 
ATOM   2547 C  CG  . ASP   A 1 321 ? -13.259 21.083  48.865 1.00 137.07 ? 617 ASP   A CG  1 
ATOM   2548 O  OD1 . ASP   A 1 321 ? -13.830 21.018  49.979 1.00 135.65 ? 617 ASP   A OD1 1 
ATOM   2549 O  OD2 . ASP   A 1 321 ? -12.017 21.077  48.739 1.00 142.48 ? 617 ASP   A OD2 1 
ATOM   2550 N  N   . MET   A 1 322 ? -11.494 20.118  45.222 1.00 120.82 ? 618 MET   A N   1 
ATOM   2551 C  CA  . MET   A 1 322 ? -10.856 18.916  44.697 1.00 126.05 ? 618 MET   A CA  1 
ATOM   2552 C  C   . MET   A 1 322 ? -9.766  18.358  45.607 1.00 135.20 ? 618 MET   A C   1 
ATOM   2553 O  O   . MET   A 1 322 ? -9.241  17.276  45.320 1.00 135.82 ? 618 MET   A O   1 
ATOM   2554 C  CB  . MET   A 1 322 ? -10.270 19.183  43.297 1.00 123.46 ? 618 MET   A CB  1 
ATOM   2555 C  CG  . MET   A 1 322 ? -11.288 19.112  42.163 1.00 119.01 ? 618 MET   A CG  1 
ATOM   2556 S  SD  . MET   A 1 322 ? -10.557 19.234  40.510 1.00 122.69 ? 618 MET   A SD  1 
ATOM   2557 C  CE  . MET   A 1 322 ? -9.512  17.782  40.456 1.00 121.76 ? 618 MET   A CE  1 
ATOM   2558 N  N   . ARG   A 1 323 ? -9.418  19.052  46.695 1.00 138.75 ? 619 ARG   A N   1 
ATOM   2559 C  CA  . ARG   A 1 323 ? -8.404  18.523  47.599 1.00 142.84 ? 619 ARG   A CA  1 
ATOM   2560 C  C   . ARG   A 1 323 ? -8.914  17.318  48.382 1.00 140.49 ? 619 ARG   A C   1 
ATOM   2561 O  O   . ARG   A 1 323 ? -8.140  16.400  48.678 1.00 144.11 ? 619 ARG   A O   1 
ATOM   2562 C  CB  . ARG   A 1 323 ? -7.936  19.615  48.564 1.00 153.32 ? 619 ARG   A CB  1 
ATOM   2563 C  CG  . ARG   A 1 323 ? -7.206  20.775  47.914 1.00 159.35 ? 619 ARG   A CG  1 
ATOM   2564 C  CD  . ARG   A 1 323 ? -7.545  22.076  48.618 1.00 165.47 ? 619 ARG   A CD  1 
ATOM   2565 N  NE  . ARG   A 1 323 ? -8.986  22.305  48.625 1.00 166.46 ? 619 ARG   A NE  1 
ATOM   2566 C  CZ  . ARG   A 1 323 ? -9.567  23.428  49.032 1.00 173.79 ? 619 ARG   A CZ  1 
ATOM   2567 N  NH1 . ARG   A 1 323 ? -8.830  24.438  49.468 1.00 181.23 ? 619 ARG   A NH1 1 
ATOM   2568 N  NH2 . ARG   A 1 323 ? -10.887 23.542  48.999 1.00 173.10 ? 619 ARG   A NH2 1 
ATOM   2569 N  N   . LYS   A 1 324 ? -10.200 17.299  48.723 1.00 134.45 ? 620 LYS   A N   1 
ATOM   2570 C  CA  . LYS   A 1 324 ? -10.775 16.275  49.585 1.00 126.67 ? 620 LYS   A CA  1 
ATOM   2571 C  C   . LYS   A 1 324 ? -11.551 15.257  48.759 1.00 116.47 ? 620 LYS   A C   1 
ATOM   2572 O  O   . LYS   A 1 324 ? -12.301 15.620  47.848 1.00 118.11 ? 620 LYS   A O   1 
ATOM   2573 C  CB  . LYS   A 1 324 ? -11.696 16.905  50.635 1.00 126.96 ? 620 LYS   A CB  1 
ATOM   2574 C  CG  . LYS   A 1 324 ? -11.048 17.178  51.988 1.00 133.01 ? 620 LYS   A CG  1 
ATOM   2575 C  CD  . LYS   A 1 324 ? -9.845  18.103  51.886 1.00 138.63 ? 620 LYS   A CD  1 
ATOM   2576 C  CE  . LYS   A 1 324 ? -9.172  18.287  53.244 1.00 128.55 ? 620 LYS   A CE  1 
ATOM   2577 N  NZ  . LYS   A 1 324 ? -7.918  19.085  53.150 1.00 129.61 ? 620 LYS   A NZ  1 
ATOM   2578 N  N   . THR   A 1 325 ? -11.355 13.975  49.082 1.00 103.61 ? 621 THR   A N   1 
ATOM   2579 C  CA  . THR   A 1 325 ? -12.100 12.909  48.416 1.00 96.45  ? 621 THR   A CA  1 
ATOM   2580 C  C   . THR   A 1 325 ? -13.590 12.997  48.725 1.00 97.13  ? 621 THR   A C   1 
ATOM   2581 O  O   . THR   A 1 325 ? -14.438 12.763  47.848 1.00 76.38  ? 621 THR   A O   1 
ATOM   2582 C  CB  . THR   A 1 325 ? -11.544 11.544  48.839 1.00 103.15 ? 621 THR   A CB  1 
ATOM   2583 O  OG1 . THR   A 1 325 ? -12.474 10.505  48.501 1.00 96.14  ? 621 THR   A OG1 1 
ATOM   2584 C  CG2 . THR   A 1 325 ? -11.262 11.502  50.351 1.00 118.59 ? 621 THR   A CG2 1 
ATOM   2585 N  N   . SER   A 1 326 ? -13.919 13.347  49.973 1.00 106.11 ? 622 SER   A N   1 
ATOM   2586 C  CA  . SER   A 1 326 ? -15.267 13.425  50.523 1.00 94.57  ? 622 SER   A CA  1 
ATOM   2587 C  C   . SER   A 1 326 ? -16.021 14.683  50.113 1.00 90.05  ? 622 SER   A C   1 
ATOM   2588 O  O   . SER   A 1 326 ? -17.154 14.877  50.567 1.00 81.37  ? 622 SER   A O   1 
ATOM   2589 C  CB  . SER   A 1 326 ? -15.200 13.351  52.055 1.00 87.61  ? 622 SER   A CB  1 
ATOM   2590 O  OG  . SER   A 1 326 ? -14.063 14.044  52.530 1.00 90.93  ? 622 SER   A OG  1 
ATOM   2591 N  N   . SER   A 1 327 ? -15.436 15.548  49.284 1.00 93.09  ? 623 SER   A N   1 
ATOM   2592 C  CA  . SER   A 1 327 ? -16.234 16.660  48.786 1.00 91.53  ? 623 SER   A CA  1 
ATOM   2593 C  C   . SER   A 1 327 ? -17.152 16.259  47.640 1.00 94.32  ? 623 SER   A C   1 
ATOM   2594 O  O   . SER   A 1 327 ? -17.815 17.141  47.077 1.00 93.78  ? 623 SER   A O   1 
ATOM   2595 C  CB  . SER   A 1 327 ? -15.323 17.807  48.345 1.00 108.70 ? 623 SER   A CB  1 
ATOM   2596 O  OG  . SER   A 1 327 ? -14.579 17.458  47.189 1.00 111.87 ? 623 SER   A OG  1 
ATOM   2597 N  N   . LEU   A 1 328 ? -17.206 14.963  47.304 1.00 89.39  ? 624 LEU   A N   1 
ATOM   2598 C  CA  . LEU   A 1 328 ? -17.891 14.410  46.132 1.00 86.17  ? 624 LEU   A CA  1 
ATOM   2599 C  C   . LEU   A 1 328 ? -17.752 15.295  44.903 1.00 101.94 ? 624 LEU   A C   1 
ATOM   2600 O  O   . LEU   A 1 328 ? -18.716 15.477  44.153 1.00 113.97 ? 624 LEU   A O   1 
ATOM   2601 C  CB  . LEU   A 1 328 ? -19.370 14.160  46.433 1.00 77.43  ? 624 LEU   A CB  1 
ATOM   2602 C  CG  . LEU   A 1 328 ? -19.488 13.418  47.773 1.00 78.33  ? 624 LEU   A CG  1 
ATOM   2603 C  CD1 . LEU   A 1 328 ? -20.932 13.115  48.127 1.00 74.69  ? 624 LEU   A CD1 1 
ATOM   2604 C  CD2 . LEU   A 1 328 ? -18.692 12.133  47.657 1.00 70.56  ? 624 LEU   A CD2 1 
ATOM   2605 N  N   . TRP   A 1 329 ? -16.552 15.837  44.681 1.00 104.15 ? 625 TRP   A N   1 
ATOM   2606 C  CA  . TRP   A 1 329 ? -16.324 16.601  43.462 1.00 103.05 ? 625 TRP   A CA  1 
ATOM   2607 C  C   . TRP   A 1 329 ? -16.367 15.703  42.235 1.00 108.03 ? 625 TRP   A C   1 
ATOM   2608 O  O   . TRP   A 1 329 ? -16.777 16.152  41.158 1.00 110.75 ? 625 TRP   A O   1 
ATOM   2609 C  CB  . TRP   A 1 329 ? -14.990 17.344  43.534 1.00 102.55 ? 625 TRP   A CB  1 
ATOM   2610 C  CG  . TRP   A 1 329 ? -13.795 16.450  43.640 1.00 100.32 ? 625 TRP   A CG  1 
ATOM   2611 C  CD1 . TRP   A 1 329 ? -13.180 16.046  44.782 1.00 112.78 ? 625 TRP   A CD1 1 
ATOM   2612 C  CD2 . TRP   A 1 329 ? -13.060 15.858  42.560 1.00 103.17 ? 625 TRP   A CD2 1 
ATOM   2613 N  NE1 . TRP   A 1 329 ? -12.111 15.237  44.489 1.00 112.62 ? 625 TRP   A NE1 1 
ATOM   2614 C  CE2 . TRP   A 1 329 ? -12.016 15.103  43.132 1.00 104.68 ? 625 TRP   A CE2 1 
ATOM   2615 C  CE3 . TRP   A 1 329 ? -13.185 15.888  41.168 1.00 88.08  ? 625 TRP   A CE3 1 
ATOM   2616 C  CZ2 . TRP   A 1 329 ? -11.103 14.386  42.362 1.00 102.94 ? 625 TRP   A CZ2 1 
ATOM   2617 C  CZ3 . TRP   A 1 329 ? -12.274 15.179  40.403 1.00 90.00  ? 625 TRP   A CZ3 1 
ATOM   2618 C  CH2 . TRP   A 1 329 ? -11.247 14.440  41.000 1.00 96.88  ? 625 TRP   A CH2 1 
ATOM   2619 N  N   . LYS   A 1 330 ? -15.952 14.440  42.375 1.00 100.83 ? 626 LYS   A N   1 
ATOM   2620 C  CA  . LYS   A 1 330 ? -16.051 13.509  41.257 1.00 92.10  ? 626 LYS   A CA  1 
ATOM   2621 C  C   . LYS   A 1 330 ? -17.504 13.239  40.898 1.00 80.85  ? 626 LYS   A C   1 
ATOM   2622 O  O   . LYS   A 1 330 ? -17.859 13.190  39.714 1.00 87.21  ? 626 LYS   A O   1 
ATOM   2623 C  CB  . LYS   A 1 330 ? -15.338 12.199  41.589 1.00 88.25  ? 626 LYS   A CB  1 
ATOM   2624 C  CG  . LYS   A 1 330 ? -13.829 12.253  41.481 1.00 79.50  ? 626 LYS   A CG  1 
ATOM   2625 C  CD  . LYS   A 1 330 ? -13.234 10.872  41.721 1.00 82.55  ? 626 LYS   A CD  1 
ATOM   2626 C  CE  . LYS   A 1 330 ? -11.724 10.863  41.519 1.00 89.25  ? 626 LYS   A CE  1 
ATOM   2627 N  NZ  . LYS   A 1 330 ? -11.133 9.525   41.822 1.00 88.29  ? 626 LYS   A NZ  1 
ATOM   2628 N  N   . ASP   A 1 331 ? -18.354 13.045  41.908 1.00 76.06  ? 627 ASP   A N   1 
ATOM   2629 C  CA  . ASP   A 1 331 ? -19.770 12.793  41.657 1.00 75.41  ? 627 ASP   A CA  1 
ATOM   2630 C  C   . ASP   A 1 331 ? -20.428 13.989  40.990 1.00 75.04  ? 627 ASP   A C   1 
ATOM   2631 O  O   . ASP   A 1 331 ? -21.152 13.847  39.995 1.00 85.18  ? 627 ASP   A O   1 
ATOM   2632 C  CB  . ASP   A 1 331 ? -20.481 12.466  42.970 1.00 79.43  ? 627 ASP   A CB  1 
ATOM   2633 C  CG  . ASP   A 1 331 ? -19.819 11.323  43.714 1.00 77.40  ? 627 ASP   A CG  1 
ATOM   2634 O  OD1 . ASP   A 1 331 ? -18.708 11.542  44.232 1.00 74.74  ? 627 ASP   A OD1 1 
ATOM   2635 O  OD2 . ASP   A 1 331 ? -20.393 10.212  43.751 1.00 69.37  ? 627 ASP   A OD2 1 
ATOM   2636 N  N   . GLN   A 1 332 ? -20.185 15.180  41.531 1.00 79.61  ? 628 GLN   A N   1 
ATOM   2637 C  CA  . GLN   A 1 332 ? -20.857 16.369  41.029 1.00 92.25  ? 628 GLN   A CA  1 
ATOM   2638 C  C   . GLN   A 1 332 ? -20.461 16.657  39.590 1.00 89.39  ? 628 GLN   A C   1 
ATOM   2639 O  O   . GLN   A 1 332 ? -21.286 17.117  38.789 1.00 85.64  ? 628 GLN   A O   1 
ATOM   2640 C  CB  . GLN   A 1 332 ? -20.533 17.555  41.931 1.00 98.35  ? 628 GLN   A CB  1 
ATOM   2641 C  CG  . GLN   A 1 332 ? -21.676 18.501  42.110 1.00 95.20  ? 628 GLN   A CG  1 
ATOM   2642 C  CD  . GLN   A 1 332 ? -21.418 19.464  43.258 1.00 110.66 ? 628 GLN   A CD  1 
ATOM   2643 O  OE1 . GLN   A 1 332 ? -20.273 19.811  43.548 1.00 132.56 ? 628 GLN   A OE1 1 
ATOM   2644 N  NE2 . GLN   A 1 332 ? -22.480 19.886  43.920 1.00 105.30 ? 628 GLN   A NE2 1 
ATOM   2645 N  N   . ALA   A 1 333 ? -19.204 16.377  39.234 1.00 86.70  ? 629 ALA   A N   1 
ATOM   2646 C  CA  . ALA   A 1 333 ? -18.777 16.604  37.862 1.00 93.41  ? 629 ALA   A CA  1 
ATOM   2647 C  C   . ALA   A 1 333 ? -19.206 15.468  36.942 1.00 87.52  ? 629 ALA   A C   1 
ATOM   2648 O  O   . ALA   A 1 333 ? -19.310 15.684  35.730 1.00 82.11  ? 629 ALA   A O   1 
ATOM   2649 C  CB  . ALA   A 1 333 ? -17.258 16.816  37.801 1.00 81.27  ? 629 ALA   A CB  1 
ATOM   2650 N  N   . LEU   A 1 334 ? -19.494 14.282  37.495 1.00 81.46  ? 630 LEU   A N   1 
ATOM   2651 C  CA  . LEU   A 1 334 ? -20.033 13.186  36.693 1.00 73.07  ? 630 LEU   A CA  1 
ATOM   2652 C  C   . LEU   A 1 334 ? -21.459 13.478  36.232 1.00 79.40  ? 630 LEU   A C   1 
ATOM   2653 O  O   . LEU   A 1 334 ? -21.846 13.104  35.112 1.00 78.44  ? 630 LEU   A O   1 
ATOM   2654 C  CB  . LEU   A 1 334 ? -19.984 11.878  37.491 1.00 69.79  ? 630 LEU   A CB  1 
ATOM   2655 C  CG  . LEU   A 1 334 ? -20.506 10.625  36.777 1.00 70.45  ? 630 LEU   A CG  1 
ATOM   2656 C  CD1 . LEU   A 1 334 ? -19.477 10.057  35.810 1.00 64.26  ? 630 LEU   A CD1 1 
ATOM   2657 C  CD2 . LEU   A 1 334 ? -20.941 9.566   37.774 1.00 68.61  ? 630 LEU   A CD2 1 
ATOM   2658 N  N   . VAL   A 1 335 ? -22.262 14.124  37.086 1.00 70.33  ? 631 VAL   A N   1 
ATOM   2659 C  CA  . VAL   A 1 335 ? -23.646 14.416  36.718 1.00 78.06  ? 631 VAL   A CA  1 
ATOM   2660 C  C   . VAL   A 1 335 ? -23.696 15.469  35.616 1.00 82.13  ? 631 VAL   A C   1 
ATOM   2661 O  O   . VAL   A 1 335 ? -24.342 15.269  34.576 1.00 81.23  ? 631 VAL   A O   1 
ATOM   2662 C  CB  . VAL   A 1 335 ? -24.466 14.849  37.943 1.00 83.71  ? 631 VAL   A CB  1 
ATOM   2663 C  CG1 . VAL   A 1 335 ? -25.780 15.464  37.493 1.00 84.59  ? 631 VAL   A CG1 1 
ATOM   2664 C  CG2 . VAL   A 1 335 ? -24.711 13.652  38.870 1.00 77.23  ? 631 VAL   A CG2 1 
ATOM   2665 N  N   . GLU   A 1 336 ? -23.003 16.599  35.817 1.00 76.44  ? 632 GLU   A N   1 
ATOM   2666 C  CA  . GLU   A 1 336 ? -22.922 17.620  34.762 1.00 82.63  ? 632 GLU   A CA  1 
ATOM   2667 C  C   . GLU   A 1 336 ? -22.517 17.025  33.418 1.00 86.42  ? 632 GLU   A C   1 
ATOM   2668 O  O   . GLU   A 1 336 ? -23.073 17.394  32.373 1.00 85.51  ? 632 GLU   A O   1 
ATOM   2669 C  CB  . GLU   A 1 336 ? -21.927 18.718  35.135 1.00 89.72  ? 632 GLU   A CB  1 
ATOM   2670 C  CG  . GLU   A 1 336 ? -22.213 19.423  36.446 1.00 100.87 ? 632 GLU   A CG  1 
ATOM   2671 C  CD  . GLU   A 1 336 ? -23.518 20.196  36.422 1.00 110.19 ? 632 GLU   A CD  1 
ATOM   2672 O  OE1 . GLU   A 1 336 ? -24.081 20.429  35.317 1.00 99.92  ? 632 GLU   A OE1 1 
ATOM   2673 O  OE2 . GLU   A 1 336 ? -23.986 20.566  37.520 1.00 114.23 ? 632 GLU   A OE2 1 
ATOM   2674 N  N   . ILE   A 1 337 ? -21.536 16.117  33.422 1.00 85.51  ? 633 ILE   A N   1 
ATOM   2675 C  CA  . ILE   A 1 337 ? -21.077 15.505  32.175 1.00 86.86  ? 633 ILE   A CA  1 
ATOM   2676 C  C   . ILE   A 1 337 ? -22.214 14.748  31.498 1.00 89.12  ? 633 ILE   A C   1 
ATOM   2677 O  O   . ILE   A 1 337 ? -22.382 14.818  30.276 1.00 84.59  ? 633 ILE   A O   1 
ATOM   2678 C  CB  . ILE   A 1 337 ? -19.859 14.595  32.434 1.00 74.83  ? 633 ILE   A CB  1 
ATOM   2679 C  CG1 . ILE   A 1 337 ? -18.571 15.427  32.550 1.00 83.71  ? 633 ILE   A CG1 1 
ATOM   2680 C  CG2 . ILE   A 1 337 ? -19.713 13.548  31.330 1.00 77.00  ? 633 ILE   A CG2 1 
ATOM   2681 C  CD1 . ILE   A 1 337 ? -17.473 14.758  33.393 1.00 77.23  ? 633 ILE   A CD1 1 
ATOM   2682 N  N   . ASN   A 1 338 ? -23.023 14.030  32.275 1.00 86.42  ? 634 ASN   A N   1 
ATOM   2683 C  CA  . ASN   A 1 338 ? -24.108 13.275  31.667 1.00 78.06  ? 634 ASN   A CA  1 
ATOM   2684 C  C   . ASN   A 1 338 ? -25.287 14.160  31.258 1.00 79.59  ? 634 ASN   A C   1 
ATOM   2685 O  O   . ASN   A 1 338 ? -25.956 13.853  30.261 1.00 72.31  ? 634 ASN   A O   1 
ATOM   2686 C  CB  . ASN   A 1 338 ? -24.526 12.141  32.600 1.00 77.41  ? 634 ASN   A CB  1 
ATOM   2687 C  CG  . ASN   A 1 338 ? -23.514 11.001  32.596 1.00 70.50  ? 634 ASN   A CG  1 
ATOM   2688 O  OD1 . ASN   A 1 338 ? -23.675 10.007  31.897 1.00 70.81  ? 634 ASN   A OD1 1 
ATOM   2689 N  ND2 . ASN   A 1 338 ? -22.445 11.166  33.363 1.00 69.01  ? 634 ASN   A ND2 1 
ATOM   2690 N  N   . ILE   A 1 339 ? -25.552 15.259  31.973 1.00 84.85  ? 635 ILE   A N   1 
ATOM   2691 C  CA  . ILE   A 1 339 ? -26.539 16.217  31.480 1.00 80.55  ? 635 ILE   A CA  1 
ATOM   2692 C  C   . ILE   A 1 339 ? -26.117 16.748  30.118 1.00 83.96  ? 635 ILE   A C   1 
ATOM   2693 O  O   . ILE   A 1 339 ? -26.948 16.931  29.218 1.00 84.89  ? 635 ILE   A O   1 
ATOM   2694 C  CB  . ILE   A 1 339 ? -26.736 17.365  32.485 1.00 83.50  ? 635 ILE   A CB  1 
ATOM   2695 C  CG1 . ILE   A 1 339 ? -27.366 16.855  33.788 1.00 78.83  ? 635 ILE   A CG1 1 
ATOM   2696 C  CG2 . ILE   A 1 339 ? -27.602 18.469  31.887 1.00 82.61  ? 635 ILE   A CG2 1 
ATOM   2697 C  CD1 . ILE   A 1 339 ? -27.840 17.964  34.667 1.00 87.02  ? 635 ILE   A CD1 1 
ATOM   2698 N  N   . ALA   A 1 340 ? -24.809 16.971  29.945 1.00 81.36  ? 636 ALA   A N   1 
ATOM   2699 C  CA  . ALA   A 1 340 ? -24.280 17.547  28.716 1.00 93.02  ? 636 ALA   A CA  1 
ATOM   2700 C  C   . ALA   A 1 340 ? -24.353 16.561  27.553 1.00 81.40  ? 636 ALA   A C   1 
ATOM   2701 O  O   . ALA   A 1 340 ? -24.715 16.946  26.435 1.00 81.80  ? 636 ALA   A O   1 
ATOM   2702 C  CB  . ALA   A 1 340 ? -22.844 18.026  28.952 1.00 87.10  ? 636 ALA   A CB  1 
ATOM   2703 N  N   . VAL   A 1 341 ? -24.016 15.288  27.790 1.00 83.27  ? 637 VAL   A N   1 
ATOM   2704 C  CA  . VAL   A 1 341 ? -24.124 14.291  26.727 1.00 76.75  ? 637 VAL   A CA  1 
ATOM   2705 C  C   . VAL   A 1 341 ? -25.561 14.215  26.228 1.00 88.96  ? 637 VAL   A C   1 
ATOM   2706 O  O   . VAL   A 1 341 ? -25.837 14.403  25.036 1.00 87.29  ? 637 VAL   A O   1 
ATOM   2707 C  CB  . VAL   A 1 341 ? -23.628 12.914  27.203 1.00 79.06  ? 637 VAL   A CB  1 
ATOM   2708 C  CG1 . VAL   A 1 341 ? -23.777 11.907  26.059 1.00 87.39  ? 637 VAL   A CG1 1 
ATOM   2709 C  CG2 . VAL   A 1 341 ? -22.182 12.978  27.648 1.00 82.38  ? 637 VAL   A CG2 1 
ATOM   2710 N  N   . LEU   A 1 342 ? -26.499 13.967  27.145 1.00 81.60  ? 638 LEU   A N   1 
ATOM   2711 C  CA  . LEU   A 1 342 ? -27.919 13.940  26.806 1.00 80.83  ? 638 LEU   A CA  1 
ATOM   2712 C  C   . LEU   A 1 342 ? -28.336 15.179  26.018 1.00 90.78  ? 638 LEU   A C   1 
ATOM   2713 O  O   . LEU   A 1 342 ? -28.830 15.077  24.891 1.00 86.31  ? 638 LEU   A O   1 
ATOM   2714 C  CB  . LEU   A 1 342 ? -28.744 13.823  28.087 1.00 78.96  ? 638 LEU   A CB  1 
ATOM   2715 C  CG  . LEU   A 1 342 ? -28.606 12.444  28.727 1.00 69.78  ? 638 LEU   A CG  1 
ATOM   2716 C  CD1 . LEU   A 1 342 ? -29.503 12.351  29.918 1.00 69.05  ? 638 LEU   A CD1 1 
ATOM   2717 C  CD2 . LEU   A 1 342 ? -28.964 11.400  27.680 1.00 62.87  ? 638 LEU   A CD2 1 
ATOM   2718 N  N   . TYR   A 1 343 ? -28.148 16.364  26.612 1.00 100.43 ? 639 TYR   A N   1 
ATOM   2719 C  CA  . TYR   A 1 343 ? -28.604 17.596  25.975 1.00 106.72 ? 639 TYR   A CA  1 
ATOM   2720 C  C   . TYR   A 1 343 ? -28.049 17.734  24.567 1.00 98.54  ? 639 TYR   A C   1 
ATOM   2721 O  O   . TYR   A 1 343 ? -28.775 18.108  23.641 1.00 99.60  ? 639 TYR   A O   1 
ATOM   2722 C  CB  . TYR   A 1 343 ? -28.209 18.809  26.812 1.00 114.36 ? 639 TYR   A CB  1 
ATOM   2723 C  CG  . TYR   A 1 343 ? -28.445 20.150  26.124 1.00 110.56 ? 639 TYR   A CG  1 
ATOM   2724 C  CD1 . TYR   A 1 343 ? -29.723 20.696  26.032 1.00 98.15  ? 639 TYR   A CD1 1 
ATOM   2725 C  CD2 . TYR   A 1 343 ? -27.387 20.877  25.595 1.00 113.93 ? 639 TYR   A CD2 1 
ATOM   2726 C  CE1 . TYR   A 1 343 ? -29.940 21.918  25.446 1.00 105.90 ? 639 TYR   A CE1 1 
ATOM   2727 C  CE2 . TYR   A 1 343 ? -27.596 22.104  24.991 1.00 119.10 ? 639 TYR   A CE2 1 
ATOM   2728 C  CZ  . TYR   A 1 343 ? -28.876 22.623  24.919 1.00 118.77 ? 639 TYR   A CZ  1 
ATOM   2729 O  OH  . TYR   A 1 343 ? -29.095 23.848  24.314 1.00 125.37 ? 639 TYR   A OH  1 
ATOM   2730 N  N   . SER   A 1 344 ? -26.755 17.448  24.392 1.00 98.29  ? 640 SER   A N   1 
ATOM   2731 C  CA  . SER   A 1 344 ? -26.139 17.620  23.079 1.00 91.11  ? 640 SER   A CA  1 
ATOM   2732 C  C   . SER   A 1 344 ? -26.780 16.695  22.057 1.00 84.20  ? 640 SER   A C   1 
ATOM   2733 O  O   . SER   A 1 344 ? -27.145 17.131  20.956 1.00 82.39  ? 640 SER   A O   1 
ATOM   2734 C  CB  . SER   A 1 344 ? -24.632 17.378  23.158 1.00 86.64  ? 640 SER   A CB  1 
ATOM   2735 O  OG  . SER   A 1 344 ? -24.060 18.133  24.218 1.00 101.80 ? 640 SER   A OG  1 
ATOM   2736 N  N   . PHE   A 1 345 ? -26.934 15.410  22.411 1.00 76.78  ? 641 PHE   A N   1 
ATOM   2737 C  CA  . PHE   A 1 345 ? -27.548 14.446  21.495 1.00 73.82  ? 641 PHE   A CA  1 
ATOM   2738 C  C   . PHE   A 1 345 ? -28.979 14.849  21.149 1.00 84.16  ? 641 PHE   A C   1 
ATOM   2739 O  O   . PHE   A 1 345 ? -29.374 14.838  19.975 1.00 87.82  ? 641 PHE   A O   1 
ATOM   2740 C  CB  . PHE   A 1 345 ? -27.548 13.041  22.099 1.00 67.92  ? 641 PHE   A CB  1 
ATOM   2741 C  CG  . PHE   A 1 345 ? -26.310 12.212  21.807 1.00 72.80  ? 641 PHE   A CG  1 
ATOM   2742 C  CD1 . PHE   A 1 345 ? -25.066 12.569  22.335 1.00 78.10  ? 641 PHE   A CD1 1 
ATOM   2743 C  CD2 . PHE   A 1 345 ? -26.415 11.025  21.080 1.00 72.52  ? 641 PHE   A CD2 1 
ATOM   2744 C  CE1 . PHE   A 1 345 ? -23.936 11.793  22.089 1.00 76.65  ? 641 PHE   A CE1 1 
ATOM   2745 C  CE2 . PHE   A 1 345 ? -25.299 10.224  20.841 1.00 58.81  ? 641 PHE   A CE2 1 
ATOM   2746 C  CZ  . PHE   A 1 345 ? -24.046 10.620  21.340 1.00 63.14  ? 641 PHE   A CZ  1 
ATOM   2747 N  N   . GLN   A 1 346 ? -29.776 15.202  22.165 1.00 85.83  ? 642 GLN   A N   1 
ATOM   2748 C  CA  . GLN   A 1 346 ? -31.180 15.550  21.940 1.00 82.81  ? 642 GLN   A CA  1 
ATOM   2749 C  C   . GLN   A 1 346 ? -31.324 16.796  21.076 1.00 88.01  ? 642 GLN   A C   1 
ATOM   2750 O  O   . GLN   A 1 346 ? -32.235 16.876  20.241 1.00 89.22  ? 642 GLN   A O   1 
ATOM   2751 C  CB  . GLN   A 1 346 ? -31.897 15.756  23.269 1.00 94.38  ? 642 GLN   A CB  1 
ATOM   2752 C  CG  . GLN   A 1 346 ? -32.024 14.492  24.097 1.00 90.87  ? 642 GLN   A CG  1 
ATOM   2753 C  CD  . GLN   A 1 346 ? -32.413 14.791  25.522 1.00 106.65 ? 642 GLN   A CD  1 
ATOM   2754 O  OE1 . GLN   A 1 346 ? -31.601 15.278  26.306 1.00 118.46 ? 642 GLN   A OE1 1 
ATOM   2755 N  NE2 . GLN   A 1 346 ? -33.661 14.505  25.867 1.00 111.41 ? 642 GLN   A NE2 1 
ATOM   2756 N  N   . SER   A 1 347 ? -30.452 17.788  21.275 1.00 88.81  ? 643 SER   A N   1 
ATOM   2757 C  CA  . SER   A 1 347 ? -30.556 19.029  20.518 1.00 95.13  ? 643 SER   A CA  1 
ATOM   2758 C  C   . SER   A 1 347 ? -30.154 18.856  19.053 1.00 98.03  ? 643 SER   A C   1 
ATOM   2759 O  O   . SER   A 1 347 ? -30.470 19.731  18.233 1.00 108.39 ? 643 SER   A O   1 
ATOM   2760 C  CB  . SER   A 1 347 ? -29.704 20.123  21.175 1.00 97.82  ? 643 SER   A CB  1 
ATOM   2761 O  OG  . SER   A 1 347 ? -30.250 20.555  22.421 1.00 115.84 ? 643 SER   A OG  1 
ATOM   2762 N  N   . ASP   A 1 348 ? -29.471 17.760  18.704 1.00 100.02 ? 644 ASP   A N   1 
ATOM   2763 C  CA  . ASP   A 1 348 ? -29.165 17.429  17.313 1.00 102.93 ? 644 ASP   A CA  1 
ATOM   2764 C  C   . ASP   A 1 348 ? -30.113 16.385  16.733 1.00 99.09  ? 644 ASP   A C   1 
ATOM   2765 O  O   . ASP   A 1 348 ? -29.906 15.939  15.599 1.00 97.88  ? 644 ASP   A O   1 
ATOM   2766 C  CB  . ASP   A 1 348 ? -27.723 16.930  17.170 1.00 99.12  ? 644 ASP   A CB  1 
ATOM   2767 C  CG  . ASP   A 1 348 ? -26.686 17.978  17.556 1.00 100.02 ? 644 ASP   A CG  1 
ATOM   2768 O  OD1 . ASP   A 1 348 ? -27.016 19.187  17.623 1.00 100.04 ? 644 ASP   A OD1 1 
ATOM   2769 O  OD2 . ASP   A 1 348 ? -25.520 17.587  17.778 1.00 93.82  ? 644 ASP   A OD2 1 
ATOM   2770 N  N   . LYS   A 1 349 ? -31.136 15.979  17.487 1.00 108.43 ? 645 LYS   A N   1 
ATOM   2771 C  CA  . LYS   A 1 349 ? -32.086 14.941  17.085 1.00 114.22 ? 645 LYS   A CA  1 
ATOM   2772 C  C   . LYS   A 1 349 ? -31.413 13.589  16.874 1.00 103.81 ? 645 LYS   A C   1 
ATOM   2773 O  O   . LYS   A 1 349 ? -31.915 12.757  16.107 1.00 98.62  ? 645 LYS   A O   1 
ATOM   2774 C  CB  . LYS   A 1 349 ? -32.862 15.344  15.822 1.00 122.25 ? 645 LYS   A CB  1 
ATOM   2775 C  CG  . LYS   A 1 349 ? -34.377 15.300  15.961 1.00 132.25 ? 645 LYS   A CG  1 
ATOM   2776 C  CD  . LYS   A 1 349 ? -34.855 16.209  17.083 1.00 140.61 ? 645 LYS   A CD  1 
ATOM   2777 C  CE  . LYS   A 1 349 ? -36.324 16.574  16.920 1.00 148.73 ? 645 LYS   A CE  1 
ATOM   2778 N  NZ  . LYS   A 1 349 ? -37.194 15.373  16.779 1.00 149.29 ? 645 LYS   A NZ  1 
ATOM   2779 N  N   . VAL   A 1 350 ? -30.276 13.354  17.532 1.00 89.24  ? 646 VAL   A N   1 
ATOM   2780 C  CA  . VAL   A 1 350 ? -29.623 12.048  17.518 1.00 71.95  ? 646 VAL   A CA  1 
ATOM   2781 C  C   . VAL   A 1 350 ? -30.180 11.222  18.668 1.00 78.14  ? 646 VAL   A C   1 
ATOM   2782 O  O   . VAL   A 1 350 ? -30.264 11.696  19.804 1.00 80.85  ? 646 VAL   A O   1 
ATOM   2783 C  CB  . VAL   A 1 350 ? -28.097 12.178  17.645 1.00 67.09  ? 646 VAL   A CB  1 
ATOM   2784 C  CG1 . VAL   A 1 350 ? -27.431 10.794  17.578 1.00 62.17  ? 646 VAL   A CG1 1 
ATOM   2785 C  CG2 . VAL   A 1 350 ? -27.534 13.136  16.636 1.00 65.00  ? 646 VAL   A CG2 1 
ATOM   2786 N  N   . THR   A 1 351 ? -30.549 9.985   18.371 1.00 75.55  ? 647 THR   A N   1 
ATOM   2787 C  CA  . THR   A 1 351 ? -31.287 9.168   19.319 1.00 72.18  ? 647 THR   A CA  1 
ATOM   2788 C  C   . THR   A 1 351 ? -30.404 8.804   20.505 1.00 68.62  ? 647 THR   A C   1 
ATOM   2789 O  O   . THR   A 1 351 ? -29.307 8.249   20.353 1.00 66.93  ? 647 THR   A O   1 
ATOM   2790 C  CB  . THR   A 1 351 ? -31.819 7.900   18.641 1.00 74.78  ? 647 THR   A CB  1 
ATOM   2791 O  OG1 . THR   A 1 351 ? -32.630 8.259   17.513 1.00 82.26  ? 647 THR   A OG1 1 
ATOM   2792 C  CG2 . THR   A 1 351 ? -32.650 7.072   19.626 1.00 65.39  ? 647 THR   A CG2 1 
ATOM   2793 N  N   . ILE   A 1 352 ? -30.893 9.121   21.699 1.00 69.64  ? 648 ILE   A N   1 
ATOM   2794 C  CA  . ILE   A 1 352 ? -30.229 8.748   22.936 1.00 59.61  ? 648 ILE   A CA  1 
ATOM   2795 C  C   . ILE   A 1 352 ? -31.315 8.565   23.990 1.00 68.22  ? 648 ILE   A C   1 
ATOM   2796 O  O   . ILE   A 1 352 ? -32.382 9.181   23.917 1.00 69.93  ? 648 ILE   A O   1 
ATOM   2797 C  CB  . ILE   A 1 352 ? -29.182 9.808   23.363 1.00 66.99  ? 648 ILE   A CB  1 
ATOM   2798 C  CG1 . ILE   A 1 352 ? -28.242 9.260   24.451 1.00 60.79  ? 648 ILE   A CG1 1 
ATOM   2799 C  CG2 . ILE   A 1 352 ? -29.861 11.053  23.870 1.00 66.12  ? 648 ILE   A CG2 1 
ATOM   2800 C  CD1 . ILE   A 1 352 ? -26.912 10.004  24.493 1.00 61.29  ? 648 ILE   A CD1 1 
ATOM   2801 N  N   . VAL   A 1 353 ? -31.053 7.688   24.958 1.00 67.52  ? 649 VAL   A N   1 
ATOM   2802 C  CA  . VAL   A 1 353 ? -31.957 7.456   26.078 1.00 63.45  ? 649 VAL   A CA  1 
ATOM   2803 C  C   . VAL   A 1 353 ? -31.179 7.724   27.357 1.00 72.36  ? 649 VAL   A C   1 
ATOM   2804 O  O   . VAL   A 1 353 ? -29.995 7.380   27.446 1.00 63.23  ? 649 VAL   A O   1 
ATOM   2805 C  CB  . VAL   A 1 353 ? -32.538 6.019   26.029 1.00 65.43  ? 649 VAL   A CB  1 
ATOM   2806 C  CG1 . VAL   A 1 353 ? -31.466 4.962   26.295 1.00 60.55  ? 649 VAL   A CG1 1 
ATOM   2807 C  CG2 . VAL   A 1 353 ? -33.716 5.852   26.982 1.00 64.94  ? 649 VAL   A CG2 1 
ATOM   2808 N  N   . ASP   A 1 354 ? -31.816 8.409   28.312 1.00 76.46  ? 650 ASP   A N   1 
ATOM   2809 C  CA  . ASP   A 1 354 ? -31.234 8.651   29.620 1.00 69.04  ? 650 ASP   A CA  1 
ATOM   2810 C  C   . ASP   A 1 354 ? -31.394 7.394   30.471 1.00 71.87  ? 650 ASP   A C   1 
ATOM   2811 O  O   . ASP   A 1 354 ? -32.229 6.533   30.185 1.00 78.96  ? 650 ASP   A O   1 
ATOM   2812 C  CB  . ASP   A 1 354 ? -31.889 9.855   30.300 1.00 73.53  ? 650 ASP   A CB  1 
ATOM   2813 C  CG  . ASP   A 1 354 ? -33.304 9.569   30.784 1.00 75.89  ? 650 ASP   A CG  1 
ATOM   2814 O  OD1 . ASP   A 1 354 ? -34.280 10.110  30.222 1.00 77.81  ? 650 ASP   A OD1 1 
ATOM   2815 O  OD2 . ASP   A 1 354 ? -33.450 8.802   31.745 1.00 66.71  ? 650 ASP   A OD2 1 
ATOM   2816 N  N   . HIS   A 1 355 ? -30.579 7.281   31.522 1.00 63.45  ? 651 HIS   A N   1 
ATOM   2817 C  CA  . HIS   A 1 355 ? -30.567 6.024   32.276 1.00 58.24  ? 651 HIS   A CA  1 
ATOM   2818 C  C   . HIS   A 1 355 ? -31.841 5.810   33.092 1.00 72.45  ? 651 HIS   A C   1 
ATOM   2819 O  O   . HIS   A 1 355 ? -32.124 4.669   33.481 1.00 76.69  ? 651 HIS   A O   1 
ATOM   2820 C  CB  . HIS   A 1 355 ? -29.335 5.947   33.181 1.00 63.02  ? 651 HIS   A CB  1 
ATOM   2821 C  CG  . HIS   A 1 355 ? -29.125 7.160   34.030 1.00 57.05  ? 651 HIS   A CG  1 
ATOM   2822 N  ND1 . HIS   A 1 355 ? -28.716 8.369   33.508 1.00 57.53  ? 651 HIS   A ND1 1 
ATOM   2823 C  CD2 . HIS   A 1 355 ? -29.246 7.349   35.368 1.00 62.34  ? 651 HIS   A CD2 1 
ATOM   2824 C  CE1 . HIS   A 1 355 ? -28.593 9.251   34.487 1.00 70.45  ? 651 HIS   A CE1 1 
ATOM   2825 N  NE2 . HIS   A 1 355 ? -28.926 8.665   35.622 1.00 59.74  ? 651 HIS   A NE2 1 
ATOM   2826 N  N   . HIS   A 1 356 ? -32.618 6.872   33.349 1.00 66.18  ? 652 HIS   A N   1 
ATOM   2827 C  CA  . HIS   A 1 356 ? -33.918 6.720   34.000 1.00 65.37  ? 652 HIS   A CA  1 
ATOM   2828 C  C   . HIS   A 1 356 ? -34.958 6.157   33.035 1.00 71.77  ? 652 HIS   A C   1 
ATOM   2829 O  O   . HIS   A 1 356 ? -35.671 5.192   33.355 1.00 67.57  ? 652 HIS   A O   1 
ATOM   2830 C  CB  . HIS   A 1 356 ? -34.369 8.062   34.570 1.00 71.09  ? 652 HIS   A CB  1 
ATOM   2831 C  CG  . HIS   A 1 356 ? -33.363 8.676   35.492 1.00 76.89  ? 652 HIS   A CG  1 
ATOM   2832 N  ND1 . HIS   A 1 356 ? -33.111 8.189   36.757 1.00 75.47  ? 652 HIS   A ND1 1 
ATOM   2833 C  CD2 . HIS   A 1 356 ? -32.523 9.721   35.313 1.00 75.64  ? 652 HIS   A CD2 1 
ATOM   2834 C  CE1 . HIS   A 1 356 ? -32.164 8.918   37.320 1.00 77.45  ? 652 HIS   A CE1 1 
ATOM   2835 N  NE2 . HIS   A 1 356 ? -31.783 9.845   36.458 1.00 82.81  ? 652 HIS   A NE2 1 
ATOM   2836 N  N   . SER   A 1 357 ? -35.059 6.743   31.837 1.00 63.12  ? 653 SER   A N   1 
ATOM   2837 C  CA  . SER   A 1 357 ? -36.059 6.255   30.899 1.00 75.50  ? 653 SER   A CA  1 
ATOM   2838 C  C   . SER   A 1 357 ? -35.743 4.834   30.460 1.00 58.90  ? 653 SER   A C   1 
ATOM   2839 O  O   . SER   A 1 357 ? -36.646 3.999   30.361 1.00 63.95  ? 653 SER   A O   1 
ATOM   2840 C  CB  . SER   A 1 357 ? -36.166 7.181   29.691 1.00 71.42  ? 653 SER   A CB  1 
ATOM   2841 O  OG  . SER   A 1 357 ? -37.288 6.810   28.911 1.00 80.80  ? 653 SER   A OG  1 
ATOM   2842 N  N   . ALA   A 1 358 ? -34.462 4.533   30.238 1.00 62.79  ? 654 ALA   A N   1 
ATOM   2843 C  CA  . ALA   A 1 358 ? -34.078 3.200   29.782 1.00 63.95  ? 654 ALA   A CA  1 
ATOM   2844 C  C   . ALA   A 1 358 ? -34.372 2.143   30.844 1.00 65.06  ? 654 ALA   A C   1 
ATOM   2845 O  O   . ALA   A 1 358 ? -34.935 1.085   30.534 1.00 52.99  ? 654 ALA   A O   1 
ATOM   2846 C  CB  . ALA   A 1 358 ? -32.595 3.177   29.400 1.00 58.31  ? 654 ALA   A CB  1 
ATOM   2847 N  N   . THR   A 1 359 ? -34.017 2.411   32.107 1.00 56.53  ? 655 THR   A N   1 
ATOM   2848 C  CA  . THR   A 1 359 ? -34.228 1.394   33.132 1.00 54.86  ? 655 THR   A CA  1 
ATOM   2849 C  C   . THR   A 1 359 ? -35.707 1.207   33.437 1.00 53.54  ? 655 THR   A C   1 
ATOM   2850 O  O   . THR   A 1 359 ? -36.123 0.103   33.802 1.00 61.80  ? 655 THR   A O   1 
ATOM   2851 C  CB  . THR   A 1 359 ? -33.443 1.734   34.395 1.00 55.70  ? 655 THR   A CB  1 
ATOM   2852 O  OG1 . THR   A 1 359 ? -33.732 3.076   34.817 1.00 61.78  ? 655 THR   A OG1 1 
ATOM   2853 C  CG2 . THR   A 1 359 ? -31.963 1.579   34.127 1.00 56.05  ? 655 THR   A CG2 1 
ATOM   2854 N  N   . GLU   A 1 360 ? -36.513 2.261   33.303 1.00 60.55  ? 656 GLU   A N   1 
ATOM   2855 C  CA  . GLU   A 1 360 ? -37.956 2.087   33.423 1.00 69.28  ? 656 GLU   A CA  1 
ATOM   2856 C  C   . GLU   A 1 360 ? -38.483 1.191   32.310 1.00 69.80  ? 656 GLU   A C   1 
ATOM   2857 O  O   . GLU   A 1 360 ? -39.276 0.274   32.558 1.00 64.93  ? 656 GLU   A O   1 
ATOM   2858 C  CB  . GLU   A 1 360 ? -38.662 3.444   33.412 1.00 72.53  ? 656 GLU   A CB  1 
ATOM   2859 C  CG  . GLU   A 1 360 ? -40.176 3.330   33.301 1.00 80.16  ? 656 GLU   A CG  1 
ATOM   2860 C  CD  . GLU   A 1 360 ? -40.888 4.665   33.455 1.00 93.86  ? 656 GLU   A CD  1 
ATOM   2861 O  OE1 . GLU   A 1 360 ? -41.746 4.781   34.359 1.00 112.38 ? 656 GLU   A OE1 1 
ATOM   2862 O  OE2 . GLU   A 1 360 ? -40.591 5.598   32.674 1.00 88.03  ? 656 GLU   A OE2 1 
ATOM   2863 N  N   . SER   A 1 361 ? -38.041 1.427   31.071 1.00 75.91  ? 657 SER   A N   1 
ATOM   2864 C  CA  A SER   A 1 361 ? -38.499 0.581   29.978 0.48 68.47  ? 657 SER   A CA  1 
ATOM   2865 C  CA  B SER   A 1 361 ? -38.468 0.580   29.960 0.52 68.26  ? 657 SER   A CA  1 
ATOM   2866 C  C   . SER   A 1 361 ? -38.135 -0.882  30.223 1.00 70.91  ? 657 SER   A C   1 
ATOM   2867 O  O   . SER   A 1 361 ? -38.889 -1.782  29.833 1.00 66.64  ? 657 SER   A O   1 
ATOM   2868 C  CB  A SER   A 1 361 ? -37.925 1.090   28.650 0.48 65.45  ? 657 SER   A CB  1 
ATOM   2869 C  CB  B SER   A 1 361 ? -37.814 1.034   28.650 0.52 64.88  ? 657 SER   A CB  1 
ATOM   2870 O  OG  A SER   A 1 361 ? -38.335 2.430   28.393 0.48 64.37  ? 657 SER   A OG  1 
ATOM   2871 O  OG  B SER   A 1 361 ? -36.634 0.287   28.376 0.52 53.26  ? 657 SER   A OG  1 
ATOM   2872 N  N   . PHE   A 1 362 ? -37.004 -1.137  30.894 1.00 68.07  ? 658 PHE   A N   1 
ATOM   2873 C  CA  . PHE   A 1 362 ? -36.579 -2.516  31.119 1.00 61.47  ? 658 PHE   A CA  1 
ATOM   2874 C  C   . PHE   A 1 362 ? -37.448 -3.210  32.158 1.00 62.42  ? 658 PHE   A C   1 
ATOM   2875 O  O   . PHE   A 1 362 ? -37.689 -4.420  32.063 1.00 64.72  ? 658 PHE   A O   1 
ATOM   2876 C  CB  . PHE   A 1 362 ? -35.111 -2.574  31.538 1.00 47.40  ? 658 PHE   A CB  1 
ATOM   2877 C  CG  . PHE   A 1 362 ? -34.600 -3.974  31.703 1.00 59.09  ? 658 PHE   A CG  1 
ATOM   2878 C  CD1 . PHE   A 1 362 ? -34.271 -4.748  30.591 1.00 56.23  ? 658 PHE   A CD1 1 
ATOM   2879 C  CD2 . PHE   A 1 362 ? -34.480 -4.537  32.957 1.00 62.36  ? 658 PHE   A CD2 1 
ATOM   2880 C  CE1 . PHE   A 1 362 ? -33.806 -6.045  30.746 1.00 54.92  ? 658 PHE   A CE1 1 
ATOM   2881 C  CE2 . PHE   A 1 362 ? -34.023 -5.840  33.108 1.00 68.52  ? 658 PHE   A CE2 1 
ATOM   2882 C  CZ  . PHE   A 1 362 ? -33.688 -6.594  31.991 1.00 65.41  ? 658 PHE   A CZ  1 
ATOM   2883 N  N   . ILE   A 1 363 ? -37.907 -2.472  33.170 1.00 71.07  ? 659 ILE   A N   1 
ATOM   2884 C  CA  . ILE   A 1 363 ? -38.865 -3.037  34.113 1.00 76.06  ? 659 ILE   A CA  1 
ATOM   2885 C  C   . ILE   A 1 363 ? -40.166 -3.354  33.394 1.00 75.71  ? 659 ILE   A C   1 
ATOM   2886 O  O   . ILE   A 1 363 ? -40.726 -4.448  33.527 1.00 84.80  ? 659 ILE   A O   1 
ATOM   2887 C  CB  . ILE   A 1 363 ? -39.092 -2.076  35.293 1.00 70.70  ? 659 ILE   A CB  1 
ATOM   2888 C  CG1 . ILE   A 1 363 ? -37.774 -1.788  36.012 1.00 68.44  ? 659 ILE   A CG1 1 
ATOM   2889 C  CG2 . ILE   A 1 363 ? -40.126 -2.657  36.249 1.00 81.43  ? 659 ILE   A CG2 1 
ATOM   2890 C  CD1 . ILE   A 1 363 ? -37.307 -2.906  36.927 1.00 67.93  ? 659 ILE   A CD1 1 
ATOM   2891 N  N   . LYS   A 1 364 ? -40.667 -2.389  32.622 1.00 75.29  ? 660 LYS   A N   1 
ATOM   2892 C  CA  . LYS   A 1 364 ? -41.823 -2.634  31.762 1.00 81.01  ? 660 LYS   A CA  1 
ATOM   2893 C  C   . LYS   A 1 364 ? -41.578 -3.830  30.852 1.00 71.02  ? 660 LYS   A C   1 
ATOM   2894 O  O   . LYS   A 1 364 ? -42.424 -4.724  30.746 1.00 79.37  ? 660 LYS   A O   1 
ATOM   2895 C  CB  . LYS   A 1 364 ? -42.142 -1.387  30.934 1.00 79.81  ? 660 LYS   A CB  1 
ATOM   2896 C  CG  . LYS   A 1 364 ? -43.545 -1.374  30.339 1.00 82.87  ? 660 LYS   A CG  1 
ATOM   2897 C  CD  . LYS   A 1 364 ? -44.597 -1.092  31.413 1.00 95.74  ? 660 LYS   A CD  1 
ATOM   2898 C  CE  . LYS   A 1 364 ? -45.980 -0.938  30.799 1.00 100.04 ? 660 LYS   A CE  1 
ATOM   2899 N  NZ  . LYS   A 1 364 ? -45.943 -0.014  29.628 1.00 97.23  ? 660 LYS   A NZ  1 
ATOM   2900 N  N   . HIS   A 1 365 ? -40.408 -3.864  30.197 1.00 68.01  ? 661 HIS   A N   1 
ATOM   2901 C  CA  . HIS   A 1 365 ? -40.045 -5.000  29.345 1.00 66.30  ? 661 HIS   A CA  1 
ATOM   2902 C  C   . HIS   A 1 365 ? -40.017 -6.301  30.133 1.00 70.56  ? 661 HIS   A C   1 
ATOM   2903 O  O   . HIS   A 1 365 ? -40.468 -7.341  29.640 1.00 63.05  ? 661 HIS   A O   1 
ATOM   2904 C  CB  . HIS   A 1 365 ? -38.682 -4.774  28.694 1.00 67.13  ? 661 HIS   A CB  1 
ATOM   2905 C  CG  . HIS   A 1 365 ? -38.135 -5.983  27.991 1.00 67.63  ? 661 HIS   A CG  1 
ATOM   2906 N  ND1 . HIS   A 1 365 ? -38.754 -6.557  26.900 1.00 67.90  ? 661 HIS   A ND1 1 
ATOM   2907 C  CD2 . HIS   A 1 365 ? -37.020 -6.720  28.220 1.00 63.99  ? 661 HIS   A CD2 1 
ATOM   2908 C  CE1 . HIS   A 1 365 ? -38.041 -7.591  26.487 1.00 69.96  ? 661 HIS   A CE1 1 
ATOM   2909 N  NE2 . HIS   A 1 365 ? -36.991 -7.720  27.280 1.00 61.73  ? 661 HIS   A NE2 1 
ATOM   2910 N  N   . MET   A 1 366 ? -39.482 -6.270  31.359 1.00 63.36  ? 662 MET   A N   1 
ATOM   2911 C  CA  . MET   A 1 366 ? -39.480 -7.479  32.173 1.00 56.77  ? 662 MET   A CA  1 
ATOM   2912 C  C   . MET   A 1 366 ? -40.900 -7.969  32.409 1.00 60.20  ? 662 MET   A C   1 
ATOM   2913 O  O   . MET   A 1 366 ? -41.184 -9.164  32.273 1.00 54.63  ? 662 MET   A O   1 
ATOM   2914 C  CB  . MET   A 1 366 ? -38.769 -7.230  33.506 1.00 58.71  ? 662 MET   A CB  1 
ATOM   2915 C  CG  . MET   A 1 366 ? -37.330 -7.712  33.544 1.00 52.12  ? 662 MET   A CG  1 
ATOM   2916 S  SD  . MET   A 1 366 ? -36.536 -7.259  35.102 1.00 68.99  ? 662 MET   A SD  1 
ATOM   2917 C  CE  . MET   A 1 366 ? -36.093 -8.886  35.722 1.00 71.78  ? 662 MET   A CE  1 
ATOM   2918 N  N   . GLU   A 1 367 ? -41.808 -7.052  32.764 1.00 80.22  ? 663 GLU   A N   1 
ATOM   2919 C  CA  . GLU   A 1 367 ? -43.199 -7.425  33.009 1.00 94.81  ? 663 GLU   A CA  1 
ATOM   2920 C  C   . GLU   A 1 367 ? -43.792 -8.145  31.807 1.00 93.34  ? 663 GLU   A C   1 
ATOM   2921 O  O   . GLU   A 1 367 ? -44.484 -9.159  31.951 1.00 92.12  ? 663 GLU   A O   1 
ATOM   2922 C  CB  . GLU   A 1 367 ? -44.040 -6.187  33.326 1.00 103.58 ? 663 GLU   A CB  1 
ATOM   2923 C  CG  . GLU   A 1 367 ? -43.684 -5.433  34.582 1.00 107.62 ? 663 GLU   A CG  1 
ATOM   2924 C  CD  . GLU   A 1 367 ? -44.533 -4.179  34.741 1.00 113.55 ? 663 GLU   A CD  1 
ATOM   2925 O  OE1 . GLU   A 1 367 ? -45.580 -4.067  34.058 1.00 114.24 ? 663 GLU   A OE1 1 
ATOM   2926 O  OE2 . GLU   A 1 367 ? -44.144 -3.302  35.542 1.00 111.80 ? 663 GLU   A OE2 1 
ATOM   2927 N  N   . ASN   A 1 368 ? -43.543 -7.616  30.607 1.00 95.00  ? 664 ASN   A N   1 
ATOM   2928 C  CA  . ASN   A 1 368 ? -44.037 -8.258  29.394 1.00 86.16  ? 664 ASN   A CA  1 
ATOM   2929 C  C   . ASN   A 1 368 ? -43.418 -9.640  29.213 1.00 85.72  ? 664 ASN   A C   1 
ATOM   2930 O  O   . ASN   A 1 368 ? -44.114 -10.599 28.854 1.00 83.80  ? 664 ASN   A O   1 
ATOM   2931 C  CB  . ASN   A 1 368 ? -43.745 -7.369  28.183 1.00 87.52  ? 664 ASN   A CB  1 
ATOM   2932 C  CG  . ASN   A 1 368 ? -44.376 -5.991  28.302 1.00 88.68  ? 664 ASN   A CG  1 
ATOM   2933 O  OD1 . ASN   A 1 368 ? -45.413 -5.824  28.950 1.00 91.95  ? 664 ASN   A OD1 1 
ATOM   2934 N  ND2 . ASN   A 1 368 ? -43.753 -4.996  27.672 1.00 72.70  ? 664 ASN   A ND2 1 
ATOM   2935 N  N   . GLU   A 1 369 ? -42.113 -9.765  29.476 1.00 82.10  ? 665 GLU   A N   1 
ATOM   2936 C  CA  . GLU   A 1 369 ? -41.425 -11.038 29.276 1.00 67.34  ? 665 GLU   A CA  1 
ATOM   2937 C  C   . GLU   A 1 369 ? -41.877 -12.092 30.285 1.00 86.61  ? 665 GLU   A C   1 
ATOM   2938 O  O   . GLU   A 1 369 ? -41.935 -13.280 29.960 1.00 95.82  ? 665 GLU   A O   1 
ATOM   2939 C  CB  . GLU   A 1 369 ? -39.914 -10.838 29.368 1.00 64.76  ? 665 GLU   A CB  1 
ATOM   2940 C  CG  . GLU   A 1 369 ? -39.264 -10.151 28.200 1.00 81.10  ? 665 GLU   A CG  1 
ATOM   2941 C  CD  . GLU   A 1 369 ? -38.832 -11.128 27.123 1.00 80.75  ? 665 GLU   A CD  1 
ATOM   2942 O  OE1 . GLU   A 1 369 ? -37.879 -11.914 27.360 1.00 92.94  ? 665 GLU   A OE1 1 
ATOM   2943 O  OE2 . GLU   A 1 369 ? -39.471 -11.119 26.064 1.00 68.09  ? 665 GLU   A OE2 1 
ATOM   2944 N  N   . TYR   A 1 370 ? -42.176 -11.697 31.525 1.00 96.16  ? 666 TYR   A N   1 
ATOM   2945 C  CA  . TYR   A 1 370 ? -42.694 -12.689 32.465 1.00 93.42  ? 666 TYR   A CA  1 
ATOM   2946 C  C   . TYR   A 1 370 ? -44.129 -13.077 32.121 1.00 98.75  ? 666 TYR   A C   1 
ATOM   2947 O  O   . TYR   A 1 370 ? -44.539 -14.219 32.363 1.00 99.48  ? 666 TYR   A O   1 
ATOM   2948 C  CB  . TYR   A 1 370 ? -42.586 -12.173 33.899 1.00 86.47  ? 666 TYR   A CB  1 
ATOM   2949 C  CG  . TYR   A 1 370 ? -41.202 -12.355 34.486 1.00 79.78  ? 666 TYR   A CG  1 
ATOM   2950 C  CD1 . TYR   A 1 370 ? -40.149 -11.522 34.115 1.00 70.30  ? 666 TYR   A CD1 1 
ATOM   2951 C  CD2 . TYR   A 1 370 ? -40.942 -13.367 35.397 1.00 84.23  ? 666 TYR   A CD2 1 
ATOM   2952 C  CE1 . TYR   A 1 370 ? -38.881 -11.694 34.645 1.00 67.94  ? 666 TYR   A CE1 1 
ATOM   2953 C  CE2 . TYR   A 1 370 ? -39.679 -13.541 35.934 1.00 79.78  ? 666 TYR   A CE2 1 
ATOM   2954 C  CZ  . TYR   A 1 370 ? -38.657 -12.709 35.554 1.00 73.14  ? 666 TYR   A CZ  1 
ATOM   2955 O  OH  . TYR   A 1 370 ? -37.406 -12.897 36.086 1.00 83.43  ? 666 TYR   A OH  1 
ATOM   2956 N  N   . ARG   A 1 371 ? -44.886 -12.160 31.517 1.00 102.97 ? 667 ARG   A N   1 
ATOM   2957 C  CA  . ARG   A 1 371 ? -46.264 -12.412 31.112 1.00 111.28 ? 667 ARG   A CA  1 
ATOM   2958 C  C   . ARG   A 1 371 ? -46.342 -13.332 29.893 1.00 109.65 ? 667 ARG   A C   1 
ATOM   2959 O  O   . ARG   A 1 371 ? -46.798 -14.475 30.010 1.00 113.50 ? 667 ARG   A O   1 
ATOM   2960 C  CB  . ARG   A 1 371 ? -46.969 -11.079 30.835 1.00 120.19 ? 667 ARG   A CB  1 
ATOM   2961 C  CG  . ARG   A 1 371 ? -48.422 -11.183 30.399 1.00 131.73 ? 667 ARG   A CG  1 
ATOM   2962 C  CD  . ARG   A 1 371 ? -48.907 -9.860  29.817 1.00 139.40 ? 667 ARG   A CD  1 
ATOM   2963 N  NE  . ARG   A 1 371 ? -48.036 -9.386  28.740 1.00 145.79 ? 667 ARG   A NE  1 
ATOM   2964 C  CZ  . ARG   A 1 371 ? -48.147 -9.751  27.463 1.00 153.95 ? 667 ARG   A CZ  1 
ATOM   2965 N  NH1 . ARG   A 1 371 ? -49.096 -10.601 27.088 1.00 160.33 ? 667 ARG   A NH1 1 
ATOM   2966 N  NH2 . ARG   A 1 371 ? -47.306 -9.266  26.554 1.00 149.54 ? 667 ARG   A NH2 1 
ATOM   2967 N  N   . CYS   A 1 372 ? -45.883 -12.863 28.726 1.00 102.46 ? 668 CYS   A N   1 
ATOM   2968 C  CA  A CYS   A 1 372 ? -46.035 -13.609 27.481 0.43 104.05 ? 668 CYS   A CA  1 
ATOM   2969 C  CA  B CYS   A 1 372 ? -46.024 -13.593 27.472 0.57 104.00 ? 668 CYS   A CA  1 
ATOM   2970 C  C   . CYS   A 1 372 ? -44.846 -14.518 27.171 1.00 99.03  ? 668 CYS   A C   1 
ATOM   2971 O  O   . CYS   A 1 372 ? -44.794 -15.091 26.077 1.00 105.36 ? 668 CYS   A O   1 
ATOM   2972 C  CB  A CYS   A 1 372 ? -46.272 -12.645 26.310 0.43 104.10 ? 668 CYS   A CB  1 
ATOM   2973 C  CB  B CYS   A 1 372 ? -46.219 -12.611 26.308 0.57 104.00 ? 668 CYS   A CB  1 
ATOM   2974 S  SG  A CYS   A 1 372 ? -47.948 -12.686 25.590 0.43 112.73 ? 668 CYS   A SG  1 
ATOM   2975 S  SG  B CYS   A 1 372 ? -44.790 -11.563 25.917 0.57 94.67  ? 668 CYS   A SG  1 
ATOM   2976 N  N   . ARG   A 1 373 ? -43.898 -14.674 28.104 1.00 80.00  ? 669 ARG   A N   1 
ATOM   2977 C  CA  . ARG   A 1 373 ? -42.764 -15.579 27.890 1.00 77.29  ? 669 ARG   A CA  1 
ATOM   2978 C  C   . ARG   A 1 373 ? -42.401 -16.426 29.101 1.00 91.59  ? 669 ARG   A C   1 
ATOM   2979 O  O   . ARG   A 1 373 ? -41.745 -17.460 28.926 1.00 94.91  ? 669 ARG   A O   1 
ATOM   2980 C  CB  . ARG   A 1 373 ? -41.513 -14.801 27.446 1.00 78.49  ? 669 ARG   A CB  1 
ATOM   2981 C  CG  . ARG   A 1 373 ? -40.446 -15.664 26.761 1.00 83.49  ? 669 ARG   A CG  1 
ATOM   2982 C  CD  . ARG   A 1 373 ? -39.155 -14.902 26.454 1.00 78.30  ? 669 ARG   A CD  1 
ATOM   2983 N  NE  . ARG   A 1 373 ? -38.323 -15.637 25.501 1.00 80.86  ? 669 ARG   A NE  1 
ATOM   2984 C  CZ  . ARG   A 1 373 ? -37.030 -15.409 25.282 1.00 78.29  ? 669 ARG   A CZ  1 
ATOM   2985 N  NH1 . ARG   A 1 373 ? -36.395 -14.457 25.956 1.00 73.32  ? 669 ARG   A NH1 1 
ATOM   2986 N  NH2 . ARG   A 1 373 ? -36.372 -16.137 24.380 1.00 66.39  ? 669 ARG   A NH2 1 
ATOM   2987 N  N   . GLY   A 1 374 ? -42.791 -16.043 30.314 1.00 95.26  ? 670 GLY   A N   1 
ATOM   2988 C  CA  . GLY   A 1 374 ? -42.476 -16.812 31.497 1.00 99.44  ? 670 GLY   A CA  1 
ATOM   2989 C  C   . GLY   A 1 374 ? -41.185 -16.437 32.185 1.00 98.23  ? 670 GLY   A C   1 
ATOM   2990 O  O   . GLY   A 1 374 ? -40.763 -17.150 33.101 1.00 103.62 ? 670 GLY   A O   1 
ATOM   2991 N  N   . GLY   A 1 375 ? -40.549 -15.352 31.779 1.00 85.09  ? 671 GLY   A N   1 
ATOM   2992 C  CA  . GLY   A 1 375 ? -39.300 -14.946 32.386 1.00 81.14  ? 671 GLY   A CA  1 
ATOM   2993 C  C   . GLY   A 1 375 ? -38.563 -13.989 31.480 1.00 75.97  ? 671 GLY   A C   1 
ATOM   2994 O  O   . GLY   A 1 375 ? -39.013 -13.660 30.384 1.00 70.95  ? 671 GLY   A O   1 
ATOM   2995 N  N   . CYS   A 1 376 ? -37.413 -13.547 31.972 1.00 65.29  ? 672 CYS   A N   1 
ATOM   2996 C  CA  . CYS   A 1 376 ? -36.536 -12.644 31.246 1.00 57.72  ? 672 CYS   A CA  1 
ATOM   2997 C  C   . CYS   A 1 376 ? -35.151 -12.697 31.870 1.00 63.25  ? 672 CYS   A C   1 
ATOM   2998 O  O   . CYS   A 1 376 ? -34.916 -12.053 32.896 1.00 57.96  ? 672 CYS   A O   1 
ATOM   2999 C  CB  . CYS   A 1 376 ? -37.066 -11.210 31.271 1.00 61.49  ? 672 CYS   A CB  1 
ATOM   3000 S  SG  . CYS   A 1 376 ? -35.952 -9.994  30.521 1.00 62.78  ? 672 CYS   A SG  1 
ATOM   3001 N  N   . PRO   A 1 377 ? -34.209 -13.428 31.283 1.00 63.78  ? 673 PRO   A N   1 
ATOM   3002 C  CA  . PRO   A 1 377 ? -32.860 -13.482 31.865 1.00 49.57  ? 673 PRO   A CA  1 
ATOM   3003 C  C   . PRO   A 1 377 ? -32.247 -12.092 31.938 1.00 49.98  ? 673 PRO   A C   1 
ATOM   3004 O  O   . PRO   A 1 377 ? -32.299 -11.318 30.973 1.00 51.85  ? 673 PRO   A O   1 
ATOM   3005 C  CB  . PRO   A 1 377 ? -32.093 -14.384 30.894 1.00 65.62  ? 673 PRO   A CB  1 
ATOM   3006 C  CG  . PRO   A 1 377 ? -32.814 -14.215 29.568 1.00 58.38  ? 673 PRO   A CG  1 
ATOM   3007 C  CD  . PRO   A 1 377 ? -34.266 -14.002 29.922 1.00 62.84  ? 673 PRO   A CD  1 
ATOM   3008 N  N   . ALA   A 1 378 ? -31.664 -11.770 33.089 1.00 60.87  ? 674 ALA   A N   1 
ATOM   3009 C  CA  . ALA   A 1 378 ? -31.189 -10.413 33.314 1.00 54.94  ? 674 ALA   A CA  1 
ATOM   3010 C  C   . ALA   A 1 378 ? -30.008 -10.424 34.276 1.00 46.77  ? 674 ALA   A C   1 
ATOM   3011 O  O   . ALA   A 1 378 ? -30.011 -11.138 35.287 1.00 48.28  ? 674 ALA   A O   1 
ATOM   3012 C  CB  . ALA   A 1 378 ? -32.315 -9.521  33.837 1.00 55.24  ? 674 ALA   A CB  1 
ATOM   3013 N  N   . ASP   A 1 379 ? -28.995 -9.642  33.943 1.00 41.08  ? 675 ASP   A N   1 
ATOM   3014 C  CA  . ASP   A 1 379 ? -27.741 -9.595  34.685 1.00 39.23  ? 675 ASP   A CA  1 
ATOM   3015 C  C   . ASP   A 1 379 ? -27.776 -8.252  35.397 1.00 47.26  ? 675 ASP   A C   1 
ATOM   3016 O  O   . ASP   A 1 379 ? -27.546 -7.208  34.782 1.00 48.44  ? 675 ASP   A O   1 
ATOM   3017 C  CB  . ASP   A 1 379 ? -26.539 -9.718  33.746 1.00 45.96  ? 675 ASP   A CB  1 
ATOM   3018 C  CG  . ASP   A 1 379 ? -25.233 -9.865  34.485 1.00 55.61  ? 675 ASP   A CG  1 
ATOM   3019 O  OD1 . ASP   A 1 379 ? -24.296 -10.497 33.946 1.00 56.65  ? 675 ASP   A OD1 1 
ATOM   3020 O  OD2 . ASP   A 1 379 ? -25.150 -9.358  35.623 1.00 54.54  ? 675 ASP   A OD2 1 
ATOM   3021 N  N   . TRP   A 1 380 ? -28.137 -8.289  36.679 1.00 42.94  ? 676 TRP   A N   1 
ATOM   3022 C  CA  . TRP   A 1 380 ? -28.172 -7.088  37.502 1.00 36.76  ? 676 TRP   A CA  1 
ATOM   3023 C  C   . TRP   A 1 380 ? -26.866 -6.304  37.431 1.00 40.51  ? 676 TRP   A C   1 
ATOM   3024 O  O   . TRP   A 1 380 ? -26.863 -5.065  37.452 1.00 44.72  ? 676 TRP   A O   1 
ATOM   3025 C  CB  . TRP   A 1 380 ? -28.445 -7.515  38.952 1.00 36.41  ? 676 TRP   A CB  1 
ATOM   3026 C  CG  . TRP   A 1 380 ? -28.926 -6.442  39.871 1.00 42.32  ? 676 TRP   A CG  1 
ATOM   3027 C  CD1 . TRP   A 1 380 ? -30.216 -6.228  40.264 1.00 41.34  ? 676 TRP   A CD1 1 
ATOM   3028 C  CD2 . TRP   A 1 380 ? -28.125 -5.484  40.574 1.00 42.10  ? 676 TRP   A CD2 1 
ATOM   3029 N  NE1 . TRP   A 1 380 ? -30.268 -5.180  41.154 1.00 51.16  ? 676 TRP   A NE1 1 
ATOM   3030 C  CE2 . TRP   A 1 380 ? -28.997 -4.709  41.368 1.00 54.14  ? 676 TRP   A CE2 1 
ATOM   3031 C  CE3 . TRP   A 1 380 ? -26.755 -5.200  40.606 1.00 46.49  ? 676 TRP   A CE3 1 
ATOM   3032 C  CZ2 . TRP   A 1 380 ? -28.542 -3.665  42.191 1.00 47.20  ? 676 TRP   A CZ2 1 
ATOM   3033 C  CZ3 . TRP   A 1 380 ? -26.302 -4.160  41.436 1.00 41.07  ? 676 TRP   A CZ3 1 
ATOM   3034 C  CH2 . TRP   A 1 380 ? -27.190 -3.411  42.208 1.00 45.23  ? 676 TRP   A CH2 1 
ATOM   3035 N  N   . VAL   A 1 381 ? -25.736 -7.014  37.478 1.00 49.08  ? 677 VAL   A N   1 
ATOM   3036 C  CA  . VAL   A 1 381 ? -24.431 -6.358  37.532 1.00 41.76  ? 677 VAL   A CA  1 
ATOM   3037 C  C   . VAL   A 1 381 ? -24.256 -5.437  36.349 1.00 54.71  ? 677 VAL   A C   1 
ATOM   3038 O  O   . VAL   A 1 381 ? -23.649 -4.361  36.481 1.00 44.09  ? 677 VAL   A O   1 
ATOM   3039 C  CB  . VAL   A 1 381 ? -23.309 -7.408  37.591 1.00 43.16  ? 677 VAL   A CB  1 
ATOM   3040 C  CG1 . VAL   A 1 381 ? -21.969 -6.770  37.265 1.00 42.80  ? 677 VAL   A CG1 1 
ATOM   3041 C  CG2 . VAL   A 1 381 ? -23.289 -8.097  38.981 1.00 40.39  ? 677 VAL   A CG2 1 
ATOM   3042 N  N   . TRP   A 1 382 ? -24.832 -5.815  35.193 1.00 47.52  ? 678 TRP   A N   1 
ATOM   3043 C  CA  . TRP   A 1 382 ? -24.773 -5.029  33.967 1.00 46.21  ? 678 TRP   A CA  1 
ATOM   3044 C  C   . TRP   A 1 382 ? -26.002 -4.164  33.720 1.00 48.15  ? 678 TRP   A C   1 
ATOM   3045 O  O   . TRP   A 1 382 ? -25.885 -3.131  33.052 1.00 44.30  ? 678 TRP   A O   1 
ATOM   3046 C  CB  . TRP   A 1 382 ? -24.577 -5.940  32.743 1.00 51.23  ? 678 TRP   A CB  1 
ATOM   3047 C  CG  . TRP   A 1 382 ? -23.151 -6.276  32.479 1.00 51.85  ? 678 TRP   A CG  1 
ATOM   3048 C  CD1 . TRP   A 1 382 ? -22.303 -6.987  33.299 1.00 50.74  ? 678 TRP   A CD1 1 
ATOM   3049 C  CD2 . TRP   A 1 382 ? -22.376 -5.891  31.336 1.00 46.42  ? 678 TRP   A CD2 1 
ATOM   3050 N  NE1 . TRP   A 1 382 ? -21.054 -7.080  32.714 1.00 59.34  ? 678 TRP   A NE1 1 
ATOM   3051 C  CE2 . TRP   A 1 382 ? -21.077 -6.418  31.510 1.00 56.38  ? 678 TRP   A CE2 1 
ATOM   3052 C  CE3 . TRP   A 1 382 ? -22.659 -5.171  30.174 1.00 51.41  ? 678 TRP   A CE3 1 
ATOM   3053 C  CZ2 . TRP   A 1 382 ? -20.064 -6.234  30.571 1.00 57.43  ? 678 TRP   A CZ2 1 
ATOM   3054 C  CZ3 . TRP   A 1 382 ? -21.647 -4.996  29.229 1.00 59.91  ? 678 TRP   A CZ3 1 
ATOM   3055 C  CH2 . TRP   A 1 382 ? -20.369 -5.524  29.435 1.00 60.78  ? 678 TRP   A CH2 1 
ATOM   3056 N  N   . ILE   A 1 383 ? -27.179 -4.544  34.220 1.00 44.88  ? 679 ILE   A N   1 
ATOM   3057 C  CA  . ILE   A 1 383 ? -28.373 -3.741  33.948 1.00 42.93  ? 679 ILE   A CA  1 
ATOM   3058 C  C   . ILE   A 1 383 ? -28.366 -2.454  34.783 1.00 53.30  ? 679 ILE   A C   1 
ATOM   3059 O  O   . ILE   A 1 383 ? -28.817 -1.404  34.316 1.00 50.07  ? 679 ILE   A O   1 
ATOM   3060 C  CB  . ILE   A 1 383 ? -29.646 -4.582  34.196 1.00 45.21  ? 679 ILE   A CB  1 
ATOM   3061 C  CG1 . ILE   A 1 383 ? -29.746 -5.746  33.210 1.00 40.41  ? 679 ILE   A CG1 1 
ATOM   3062 C  CG2 . ILE   A 1 383 ? -30.923 -3.716  34.193 1.00 44.40  ? 679 ILE   A CG2 1 
ATOM   3063 C  CD1 . ILE   A 1 383 ? -30.022 -5.339  31.746 1.00 57.83  ? 679 ILE   A CD1 1 
ATOM   3064 N  N   . VAL   A 1 384 ? -27.877 -2.506  36.024 1.00 43.44  ? 680 VAL   A N   1 
ATOM   3065 C  CA  . VAL   A 1 384 ? -27.877 -1.258  36.817 1.00 48.89  ? 680 VAL   A CA  1 
ATOM   3066 C  C   . VAL   A 1 384 ? -26.926 -0.247  36.178 1.00 52.15  ? 680 VAL   A C   1 
ATOM   3067 O  O   . VAL   A 1 384 ? -25.739 -0.566  35.948 1.00 48.08  ? 680 VAL   A O   1 
ATOM   3068 C  CB  . VAL   A 1 384 ? -27.487 -1.533  38.275 1.00 45.90  ? 680 VAL   A CB  1 
ATOM   3069 C  CG1 . VAL   A 1 384 ? -27.409 -0.219  39.109 1.00 43.04  ? 680 VAL   A CG1 1 
ATOM   3070 C  CG2 . VAL   A 1 384 ? -28.499 -2.485  38.903 1.00 52.25  ? 680 VAL   A CG2 1 
ATOM   3071 N  N   . PRO   A 1 385 ? -27.375 0.973   35.888 1.00 56.99  ? 681 PRO   A N   1 
ATOM   3072 C  CA  . PRO   A 1 385 ? -26.492 1.993   35.269 1.00 58.25  ? 681 PRO   A CA  1 
ATOM   3073 C  C   . PRO   A 1 385 ? -25.304 2.309   36.167 1.00 66.24  ? 681 PRO   A C   1 
ATOM   3074 O  O   . PRO   A 1 385 ? -25.372 2.115   37.384 1.00 55.14  ? 681 PRO   A O   1 
ATOM   3075 C  CB  . PRO   A 1 385 ? -27.412 3.212   35.134 1.00 60.54  ? 681 PRO   A CB  1 
ATOM   3076 C  CG  . PRO   A 1 385 ? -28.814 2.655   35.244 1.00 63.11  ? 681 PRO   A CG  1 
ATOM   3077 C  CD  . PRO   A 1 385 ? -28.712 1.509   36.197 1.00 49.84  ? 681 PRO   A CD  1 
ATOM   3078 N  N   . PRO   A 1 386 ? -24.191 2.782   35.605 1.00 58.91  ? 682 PRO   A N   1 
ATOM   3079 C  CA  . PRO   A 1 386 ? -22.976 3.008   36.404 1.00 51.26  ? 682 PRO   A CA  1 
ATOM   3080 C  C   . PRO   A 1 386 ? -22.967 4.305   37.198 1.00 54.30  ? 682 PRO   A C   1 
ATOM   3081 O  O   . PRO   A 1 386 ? -21.908 4.693   37.706 1.00 58.77  ? 682 PRO   A O   1 
ATOM   3082 C  CB  . PRO   A 1 386 ? -21.883 3.035   35.322 1.00 51.67  ? 682 PRO   A CB  1 
ATOM   3083 C  CG  . PRO   A 1 386 ? -22.582 3.655   34.153 1.00 53.31  ? 682 PRO   A CG  1 
ATOM   3084 C  CD  . PRO   A 1 386 ? -23.991 3.122   34.191 1.00 51.04  ? 682 PRO   A CD  1 
ATOM   3085 N  N   . MET   A 1 387 ? -24.093 5.003   37.306 1.00 48.33  ? 683 MET   A N   1 
ATOM   3086 C  CA  . MET   A 1 387 ? -24.241 6.121   38.230 1.00 47.00  ? 683 MET   A CA  1 
ATOM   3087 C  C   . MET   A 1 387 ? -25.675 6.094   38.718 1.00 67.54  ? 683 MET   A C   1 
ATOM   3088 O  O   . MET   A 1 387 ? -26.556 5.519   38.070 1.00 59.79  ? 683 MET   A O   1 
ATOM   3089 C  CB  . MET   A 1 387 ? -23.940 7.486   37.572 1.00 59.41  ? 683 MET   A CB  1 
ATOM   3090 C  CG  . MET   A 1 387 ? -24.986 7.863   36.528 1.00 63.38  ? 683 MET   A CG  1 
ATOM   3091 S  SD  . MET   A 1 387 ? -24.669 9.423   35.668 1.00 82.18  ? 683 MET   A SD  1 
ATOM   3092 C  CE  . MET   A 1 387 ? -24.449 10.512  37.064 1.00 77.36  ? 683 MET   A CE  1 
ATOM   3093 N  N   . SER   A 1 388 ? -25.886 6.679   39.888 1.00 64.53  ? 684 SER   A N   1 
ATOM   3094 C  CA  . SER   A 1 388 ? -27.216 6.868   40.472 1.00 67.71  ? 684 SER   A CA  1 
ATOM   3095 C  C   . SER   A 1 388 ? -28.004 5.568   40.570 1.00 63.72  ? 684 SER   A C   1 
ATOM   3096 O  O   . SER   A 1 388 ? -29.230 5.580   40.437 1.00 68.45  ? 684 SER   A O   1 
ATOM   3097 C  CB  . SER   A 1 388 ? -28.019 7.897   39.672 1.00 60.68  ? 684 SER   A CB  1 
ATOM   3098 O  OG  . SER   A 1 388 ? -27.238 9.040   39.384 1.00 72.94  ? 684 SER   A OG  1 
ATOM   3099 N  N   . GLY   A 1 389 ? -27.304 4.452   40.795 1.00 60.46  ? 685 GLY   A N   1 
ATOM   3100 C  CA  . GLY   A 1 389 ? -27.932 3.139   40.717 1.00 55.39  ? 685 GLY   A CA  1 
ATOM   3101 C  C   . GLY   A 1 389 ? -29.304 3.052   41.360 1.00 66.43  ? 685 GLY   A C   1 
ATOM   3102 O  O   . GLY   A 1 389 ? -30.282 2.664   40.715 1.00 57.29  ? 685 GLY   A O   1 
ATOM   3103 N  N   . SER   A 1 390 ? -29.402 3.427   42.638 1.00 63.79  ? 686 SER   A N   1 
ATOM   3104 C  CA  . SER   A 1 390 ? -30.596 3.130   43.419 1.00 53.80  ? 686 SER   A CA  1 
ATOM   3105 C  C   . SER   A 1 390 ? -31.714 4.141   43.229 1.00 56.34  ? 686 SER   A C   1 
ATOM   3106 O  O   . SER   A 1 390 ? -32.792 3.948   43.802 1.00 64.86  ? 686 SER   A O   1 
ATOM   3107 C  CB  . SER   A 1 390 ? -30.257 3.045   44.911 1.00 58.81  ? 686 SER   A CB  1 
ATOM   3108 O  OG  . SER   A 1 390 ? -29.647 4.247   45.314 1.00 65.55  ? 686 SER   A OG  1 
ATOM   3109 N  N   . ILE   A 1 391 ? -31.491 5.224   42.480 1.00 57.24  ? 687 ILE   A N   1 
ATOM   3110 C  CA  . ILE   A 1 391 ? -32.577 6.115   42.114 1.00 57.59  ? 687 ILE   A CA  1 
ATOM   3111 C  C   . ILE   A 1 391 ? -33.169 5.742   40.764 1.00 59.30  ? 687 ILE   A C   1 
ATOM   3112 O  O   . ILE   A 1 391 ? -33.973 6.502   40.219 1.00 73.40  ? 687 ILE   A O   1 
ATOM   3113 C  CB  . ILE   A 1 391 ? -32.153 7.595   42.129 1.00 75.10  ? 687 ILE   A CB  1 
ATOM   3114 C  CG1 . ILE   A 1 391 ? -31.214 7.913   40.962 1.00 77.03  ? 687 ILE   A CG1 1 
ATOM   3115 C  CG2 . ILE   A 1 391 ? -31.610 8.026   43.521 1.00 75.88  ? 687 ILE   A CG2 1 
ATOM   3116 C  CD1 . ILE   A 1 391 ? -31.065 9.400   40.701 1.00 83.20  ? 687 ILE   A CD1 1 
ATOM   3117 N  N   . THR   A 1 392 ? -32.794 4.561   40.214 1.00 63.45  ? 688 THR   A N   1 
ATOM   3118 C  CA  . THR   A 1 392 ? -33.377 3.907   39.048 1.00 62.41  ? 688 THR   A CA  1 
ATOM   3119 C  C   . THR   A 1 392 ? -34.034 2.599   39.468 1.00 58.82  ? 688 THR   A C   1 
ATOM   3120 O  O   . THR   A 1 392 ? -33.517 1.896   40.342 1.00 62.09  ? 688 THR   A O   1 
ATOM   3121 C  CB  . THR   A 1 392 ? -32.343 3.602   37.949 1.00 64.88  ? 688 THR   A CB  1 
ATOM   3122 O  OG1 . THR   A 1 392 ? -31.488 2.532   38.376 1.00 58.80  ? 688 THR   A OG1 1 
ATOM   3123 C  CG2 . THR   A 1 392 ? -31.500 4.823   37.622 1.00 65.07  ? 688 THR   A CG2 1 
ATOM   3124 N  N   . PRO   A 1 393 ? -35.156 2.230   38.842 1.00 64.48  ? 689 PRO   A N   1 
ATOM   3125 C  CA  . PRO   A 1 393 ? -35.940 1.094   39.351 1.00 68.56  ? 689 PRO   A CA  1 
ATOM   3126 C  C   . PRO   A 1 393 ? -35.274 -0.265  39.183 1.00 68.36  ? 689 PRO   A C   1 
ATOM   3127 O  O   . PRO   A 1 393 ? -35.713 -1.224  39.836 1.00 69.89  ? 689 PRO   A O   1 
ATOM   3128 C  CB  . PRO   A 1 393 ? -37.237 1.176   38.534 1.00 75.51  ? 689 PRO   A CB  1 
ATOM   3129 C  CG  . PRO   A 1 393 ? -36.815 1.835   37.262 1.00 80.75  ? 689 PRO   A CG  1 
ATOM   3130 C  CD  . PRO   A 1 393 ? -35.802 2.862   37.679 1.00 71.84  ? 689 PRO   A CD  1 
ATOM   3131 N  N   . VAL   A 1 394 ? -34.243 -0.390  38.340 1.00 59.09  ? 690 VAL   A N   1 
ATOM   3132 C  CA  . VAL   A 1 394 ? -33.627 -1.703  38.142 1.00 51.71  ? 690 VAL   A CA  1 
ATOM   3133 C  C   . VAL   A 1 394 ? -32.766 -2.097  39.336 1.00 55.49  ? 690 VAL   A C   1 
ATOM   3134 O  O   . VAL   A 1 394 ? -32.557 -3.293  39.576 1.00 50.29  ? 690 VAL   A O   1 
ATOM   3135 C  CB  . VAL   A 1 394 ? -32.788 -1.742  36.853 1.00 47.06  ? 690 VAL   A CB  1 
ATOM   3136 C  CG1 . VAL   A 1 394 ? -33.683 -1.719  35.594 1.00 51.80  ? 690 VAL   A CG1 1 
ATOM   3137 C  CG2 . VAL   A 1 394 ? -31.821 -0.582  36.863 1.00 50.87  ? 690 VAL   A CG2 1 
ATOM   3138 N  N   . PHE   A 1 395 ? -32.217 -1.116  40.075 1.00 56.40  ? 691 PHE   A N   1 
ATOM   3139 C  CA  . PHE   A 1 395 ? -31.472 -1.422  41.299 1.00 50.97  ? 691 PHE   A CA  1 
ATOM   3140 C  C   . PHE   A 1 395 ? -32.293 -2.308  42.219 1.00 53.32  ? 691 PHE   A C   1 
ATOM   3141 O  O   . PHE   A 1 395 ? -31.759 -3.225  42.861 1.00 45.40  ? 691 PHE   A O   1 
ATOM   3142 C  CB  . PHE   A 1 395 ? -31.076 -0.122  42.018 1.00 50.88  ? 691 PHE   A CB  1 
ATOM   3143 C  CG  . PHE   A 1 395 ? -30.277 -0.324  43.298 1.00 55.97  ? 691 PHE   A CG  1 
ATOM   3144 C  CD1 . PHE   A 1 395 ? -28.895 -0.184  43.304 1.00 47.78  ? 691 PHE   A CD1 1 
ATOM   3145 C  CD2 . PHE   A 1 395 ? -30.918 -0.611  44.493 1.00 55.96  ? 691 PHE   A CD2 1 
ATOM   3146 C  CE1 . PHE   A 1 395 ? -28.165 -0.354  44.489 1.00 58.95  ? 691 PHE   A CE1 1 
ATOM   3147 C  CE2 . PHE   A 1 395 ? -30.189 -0.789  45.680 1.00 53.89  ? 691 PHE   A CE2 1 
ATOM   3148 C  CZ  . PHE   A 1 395 ? -28.808 -0.661  45.662 1.00 51.90  ? 691 PHE   A CZ  1 
ATOM   3149 N  N   . HIS   A 1 396 ? -33.598 -2.056  42.276 1.00 58.19  ? 692 HIS   A N   1 
ATOM   3150 C  CA  . HIS   A 1 396 ? -34.496 -2.626  43.273 1.00 48.85  ? 692 HIS   A CA  1 
ATOM   3151 C  C   . HIS   A 1 396 ? -35.168 -3.897  42.795 1.00 57.84  ? 692 HIS   A C   1 
ATOM   3152 O  O   . HIS   A 1 396 ? -35.950 -4.500  43.540 1.00 60.15  ? 692 HIS   A O   1 
ATOM   3153 C  CB  . HIS   A 1 396 ? -35.527 -1.573  43.648 1.00 64.03  ? 692 HIS   A CB  1 
ATOM   3154 C  CG  . HIS   A 1 396 ? -34.904 -0.327  44.185 1.00 65.55  ? 692 HIS   A CG  1 
ATOM   3155 N  ND1 . HIS   A 1 396 ? -34.209 -0.303  45.376 1.00 63.13  ? 692 HIS   A ND1 1 
ATOM   3156 C  CD2 . HIS   A 1 396 ? -34.829 0.926   43.682 1.00 63.57  ? 692 HIS   A CD2 1 
ATOM   3157 C  CE1 . HIS   A 1 396 ? -33.760 0.921   45.598 1.00 67.25  ? 692 HIS   A CE1 1 
ATOM   3158 N  NE2 . HIS   A 1 396 ? -34.116 1.685   44.580 1.00 68.73  ? 692 HIS   A NE2 1 
ATOM   3159 N  N   . GLN   A 1 397 ? -34.841 -4.327  41.583 1.00 54.60  ? 693 GLN   A N   1 
ATOM   3160 C  CA  . GLN   A 1 397 ? -35.471 -5.459  40.934 1.00 54.72  ? 693 GLN   A CA  1 
ATOM   3161 C  C   . GLN   A 1 397 ? -34.525 -6.648  40.968 1.00 52.58  ? 693 GLN   A C   1 
ATOM   3162 O  O   . GLN   A 1 397 ? -33.456 -6.617  40.339 1.00 50.32  ? 693 GLN   A O   1 
ATOM   3163 C  CB  . GLN   A 1 397 ? -35.815 -5.104  39.489 1.00 56.68  ? 693 GLN   A CB  1 
ATOM   3164 C  CG  . GLN   A 1 397 ? -36.398 -6.251  38.691 1.00 59.58  ? 693 GLN   A CG  1 
ATOM   3165 C  CD  . GLN   A 1 397 ? -37.829 -6.554  39.077 1.00 64.52  ? 693 GLN   A CD  1 
ATOM   3166 O  OE1 . GLN   A 1 397 ? -38.708 -5.694  38.981 1.00 70.94  ? 693 GLN   A OE1 1 
ATOM   3167 N  NE2 . GLN   A 1 397 ? -38.073 -7.780  39.519 1.00 68.07  ? 693 GLN   A NE2 1 
ATOM   3168 N  N   . GLU   A 1 398 ? -34.922 -7.691  41.689 1.00 51.52  ? 694 GLU   A N   1 
ATOM   3169 C  CA  . GLU   A 1 398 ? -34.257 -8.982  41.575 1.00 57.29  ? 694 GLU   A CA  1 
ATOM   3170 C  C   . GLU   A 1 398 ? -34.383 -9.521  40.154 1.00 60.67  ? 694 GLU   A C   1 
ATOM   3171 O  O   . GLU   A 1 398 ? -35.472 -9.517  39.571 1.00 66.02  ? 694 GLU   A O   1 
ATOM   3172 C  CB  . GLU   A 1 398 ? -34.859 -9.965  42.570 1.00 52.97  ? 694 GLU   A CB  1 
ATOM   3173 C  CG  . GLU   A 1 398 ? -34.626 -9.544  44.022 1.00 62.30  ? 694 GLU   A CG  1 
ATOM   3174 C  CD  . GLU   A 1 398 ? -35.379 -10.391 44.999 1.00 62.53  ? 694 GLU   A CD  1 
ATOM   3175 O  OE1 . GLU   A 1 398 ? -35.177 -10.201 46.210 1.00 69.73  ? 694 GLU   A OE1 1 
ATOM   3176 O  OE2 . GLU   A 1 398 ? -36.166 -11.251 44.563 1.00 70.04  ? 694 GLU   A OE2 1 
ATOM   3177 N  N   . MET   A 1 399 ? -33.265 -9.985  39.601 1.00 63.97  ? 695 MET   A N   1 
ATOM   3178 C  CA  . MET   A 1 399 ? -33.206 -10.470 38.228 1.00 60.67  ? 695 MET   A CA  1 
ATOM   3179 C  C   . MET   A 1 399 ? -32.517 -11.822 38.226 1.00 59.32  ? 695 MET   A C   1 
ATOM   3180 O  O   . MET   A 1 399 ? -31.436 -11.969 38.802 1.00 56.66  ? 695 MET   A O   1 
ATOM   3181 C  CB  . MET   A 1 399 ? -32.441 -9.506  37.307 1.00 52.52  ? 695 MET   A CB  1 
ATOM   3182 C  CG  . MET   A 1 399 ? -32.919 -8.071  37.308 1.00 47.86  ? 695 MET   A CG  1 
ATOM   3183 S  SD  . MET   A 1 399 ? -31.705 -7.024  36.518 1.00 50.65  ? 695 MET   A SD  1 
ATOM   3184 C  CE  . MET   A 1 399 ? -32.336 -5.406  36.978 1.00 51.90  ? 695 MET   A CE  1 
ATOM   3185 N  N   . LEU   A 1 400 ? -33.118 -12.793 37.545 1.00 48.37  ? 696 LEU   A N   1 
ATOM   3186 C  CA  . LEU   A 1 400 ? -32.509 -14.107 37.390 1.00 56.93  ? 696 LEU   A CA  1 
ATOM   3187 C  C   . LEU   A 1 400 ? -31.681 -14.124 36.115 1.00 64.51  ? 696 LEU   A C   1 
ATOM   3188 O  O   . LEU   A 1 400 ? -32.212 -13.874 35.025 1.00 55.92  ? 696 LEU   A O   1 
ATOM   3189 C  CB  . LEU   A 1 400 ? -33.567 -15.200 37.319 1.00 58.32  ? 696 LEU   A CB  1 
ATOM   3190 C  CG  . LEU   A 1 400 ? -34.375 -15.515 38.570 1.00 64.80  ? 696 LEU   A CG  1 
ATOM   3191 C  CD1 . LEU   A 1 400 ? -35.433 -16.560 38.270 1.00 65.17  ? 696 LEU   A CD1 1 
ATOM   3192 C  CD2 . LEU   A 1 400 ? -33.466 -15.970 39.695 1.00 60.39  ? 696 LEU   A CD2 1 
ATOM   3193 N  N   . ASN   A 1 401 ? -30.387 -14.402 36.245 1.00 63.16  ? 697 ASN   A N   1 
ATOM   3194 C  CA  . ASN   A 1 401 ? -29.536 -14.568 35.075 1.00 53.15  ? 697 ASN   A CA  1 
ATOM   3195 C  C   . ASN   A 1 401 ? -29.481 -16.037 34.695 1.00 60.34  ? 697 ASN   A C   1 
ATOM   3196 O  O   . ASN   A 1 401 ? -29.152 -16.892 35.523 1.00 50.56  ? 697 ASN   A O   1 
ATOM   3197 C  CB  . ASN   A 1 401 ? -28.118 -14.046 35.297 1.00 53.43  ? 697 ASN   A CB  1 
ATOM   3198 C  CG  . ASN   A 1 401 ? -27.427 -13.738 33.990 1.00 54.06  ? 697 ASN   A CG  1 
ATOM   3199 O  OD1 . ASN   A 1 401 ? -28.082 -13.700 32.950 1.00 54.66  ? 697 ASN   A OD1 1 
ATOM   3200 N  ND2 . ASN   A 1 401 ? -26.114 -13.529 34.021 1.00 50.95  ? 697 ASN   A ND2 1 
ATOM   3201 N  N   . TYR   A 1 402 ? -29.808 -16.320 33.439 1.00 64.18  ? 698 TYR   A N   1 
ATOM   3202 C  CA  . TYR   A 1 402 ? -29.596 -17.634 32.874 1.00 58.04  ? 698 TYR   A CA  1 
ATOM   3203 C  C   . TYR   A 1 402 ? -29.354 -17.453 31.380 1.00 62.61  ? 698 TYR   A C   1 
ATOM   3204 O  O   . TYR   A 1 402 ? -29.651 -16.404 30.794 1.00 55.03  ? 698 TYR   A O   1 
ATOM   3205 C  CB  . TYR   A 1 402 ? -30.772 -18.574 33.173 1.00 62.20  ? 698 TYR   A CB  1 
ATOM   3206 C  CG  . TYR   A 1 402 ? -32.144 -17.967 32.968 1.00 70.56  ? 698 TYR   A CG  1 
ATOM   3207 C  CD1 . TYR   A 1 402 ? -32.770 -18.038 31.728 1.00 66.08  ? 698 TYR   A CD1 1 
ATOM   3208 C  CD2 . TYR   A 1 402 ? -32.820 -17.331 34.012 1.00 62.77  ? 698 TYR   A CD2 1 
ATOM   3209 C  CE1 . TYR   A 1 402 ? -34.026 -17.499 31.525 1.00 67.41  ? 698 TYR   A CE1 1 
ATOM   3210 C  CE2 . TYR   A 1 402 ? -34.087 -16.787 33.820 1.00 70.52  ? 698 TYR   A CE2 1 
ATOM   3211 C  CZ  . TYR   A 1 402 ? -34.684 -16.880 32.566 1.00 73.03  ? 698 TYR   A CZ  1 
ATOM   3212 O  OH  . TYR   A 1 402 ? -35.937 -16.353 32.330 1.00 71.12  ? 698 TYR   A OH  1 
ATOM   3213 N  N   . ARG   A 1 403 ? -28.759 -18.462 30.767 1.00 51.61  ? 699 ARG   A N   1 
ATOM   3214 C  CA  . ARG   A 1 403 ? -28.293 -18.322 29.395 1.00 59.39  ? 699 ARG   A CA  1 
ATOM   3215 C  C   . ARG   A 1 403 ? -29.231 -19.079 28.472 1.00 63.35  ? 699 ARG   A C   1 
ATOM   3216 O  O   . ARG   A 1 403 ? -29.391 -20.294 28.604 1.00 67.41  ? 699 ARG   A O   1 
ATOM   3217 C  CB  . ARG   A 1 403 ? -26.852 -18.808 29.262 1.00 64.49  ? 699 ARG   A CB  1 
ATOM   3218 C  CG  . ARG   A 1 403 ? -25.919 -17.996 30.129 1.00 81.94  ? 699 ARG   A CG  1 
ATOM   3219 C  CD  . ARG   A 1 403 ? -24.794 -17.397 29.323 1.00 93.07  ? 699 ARG   A CD  1 
ATOM   3220 N  NE  . ARG   A 1 403 ? -23.807 -18.418 29.004 1.00 107.17 ? 699 ARG   A NE  1 
ATOM   3221 C  CZ  . ARG   A 1 403 ? -22.794 -18.235 28.168 1.00 113.04 ? 699 ARG   A CZ  1 
ATOM   3222 N  NH1 . ARG   A 1 403 ? -22.646 -17.063 27.561 1.00 112.79 ? 699 ARG   A NH1 1 
ATOM   3223 N  NH2 . ARG   A 1 403 ? -21.940 -19.224 27.932 1.00 113.79 ? 699 ARG   A NH2 1 
ATOM   3224 N  N   . LEU   A 1 404 ? -29.874 -18.358 27.565 1.00 68.78  ? 700 LEU   A N   1 
ATOM   3225 C  CA  . LEU   A 1 404 ? -30.710 -18.974 26.554 1.00 56.07  ? 700 LEU   A CA  1 
ATOM   3226 C  C   . LEU   A 1 404 ? -30.075 -18.800 25.182 1.00 67.41  ? 700 LEU   A C   1 
ATOM   3227 O  O   . LEU   A 1 404 ? -29.205 -17.949 24.969 1.00 57.80  ? 700 LEU   A O   1 
ATOM   3228 C  CB  . LEU   A 1 404 ? -32.114 -18.371 26.540 1.00 61.02  ? 700 LEU   A CB  1 
ATOM   3229 C  CG  . LEU   A 1 404 ? -32.923 -18.282 27.831 1.00 58.51  ? 700 LEU   A CG  1 
ATOM   3230 C  CD1 . LEU   A 1 404 ? -34.243 -17.606 27.525 1.00 54.03  ? 700 LEU   A CD1 1 
ATOM   3231 C  CD2 . LEU   A 1 404 ? -33.149 -19.660 28.436 1.00 66.38  ? 700 LEU   A CD2 1 
ATOM   3232 N  N   . THR   A 1 405 ? -30.532 -19.625 24.247 1.00 61.93  ? 701 THR   A N   1 
ATOM   3233 C  CA  . THR   A 1 405 ? -30.105 -19.535 22.875 1.00 63.37  ? 701 THR   A CA  1 
ATOM   3234 C  C   . THR   A 1 405 ? -31.336 -19.347 21.994 1.00 67.94  ? 701 THR   A C   1 
ATOM   3235 O  O   . THR   A 1 405 ? -32.426 -19.807 22.355 1.00 60.17  ? 701 THR   A O   1 
ATOM   3236 C  CB  . THR   A 1 405 ? -29.329 -20.795 22.475 1.00 67.76  ? 701 THR   A CB  1 
ATOM   3237 O  OG1 . THR   A 1 405 ? -28.653 -20.569 21.239 1.00 68.94  ? 701 THR   A OG1 1 
ATOM   3238 C  CG2 . THR   A 1 405 ? -30.258 -21.991 22.338 1.00 66.21  ? 701 THR   A CG2 1 
ATOM   3239 N  N   . PRO   A 1 406 ? -31.218 -18.636 20.853 1.00 66.81  ? 702 PRO   A N   1 
ATOM   3240 C  CA  . PRO   A 1 406 ? -30.058 -17.942 20.272 1.00 64.42  ? 702 PRO   A CA  1 
ATOM   3241 C  C   . PRO   A 1 406 ? -29.427 -16.886 21.184 1.00 63.58  ? 702 PRO   A C   1 
ATOM   3242 O  O   . PRO   A 1 406 ? -30.109 -16.341 22.049 1.00 62.59  ? 702 PRO   A O   1 
ATOM   3243 C  CB  . PRO   A 1 406 ? -30.645 -17.280 19.026 1.00 60.99  ? 702 PRO   A CB  1 
ATOM   3244 C  CG  . PRO   A 1 406 ? -31.785 -18.140 18.639 1.00 62.93  ? 702 PRO   A CG  1 
ATOM   3245 C  CD  . PRO   A 1 406 ? -32.356 -18.685 19.907 1.00 62.19  ? 702 PRO   A CD  1 
ATOM   3246 N  N   . SER   A 1 407 ? -28.145 -16.589 20.971 1.00 60.85  ? 703 SER   A N   1 
ATOM   3247 C  CA  . SER   A 1 407 ? -27.412 -15.740 21.894 1.00 62.85  ? 703 SER   A CA  1 
ATOM   3248 C  C   . SER   A 1 407 ? -26.241 -15.054 21.203 1.00 57.19  ? 703 SER   A C   1 
ATOM   3249 O  O   . SER   A 1 407 ? -25.727 -15.511 20.169 1.00 53.70  ? 703 SER   A O   1 
ATOM   3250 C  CB  . SER   A 1 407 ? -26.885 -16.539 23.086 1.00 59.79  ? 703 SER   A CB  1 
ATOM   3251 O  OG  . SER   A 1 407 ? -25.714 -17.243 22.713 1.00 71.83  ? 703 SER   A OG  1 
ATOM   3252 N  N   . PHE   A 1 408 ? -25.822 -13.949 21.820 1.00 53.86  ? 704 PHE   A N   1 
ATOM   3253 C  CA  . PHE   A 1 408 ? -24.564 -13.279 21.527 1.00 52.88  ? 704 PHE   A CA  1 
ATOM   3254 C  C   . PHE   A 1 408 ? -23.538 -13.723 22.554 1.00 54.14  ? 704 PHE   A C   1 
ATOM   3255 O  O   . PHE   A 1 408 ? -23.787 -13.638 23.765 1.00 51.71  ? 704 PHE   A O   1 
ATOM   3256 C  CB  . PHE   A 1 408 ? -24.710 -11.756 21.570 1.00 44.70  ? 704 PHE   A CB  1 
ATOM   3257 C  CG  . PHE   A 1 408 ? -25.582 -11.212 20.479 1.00 52.47  ? 704 PHE   A CG  1 
ATOM   3258 C  CD1 . PHE   A 1 408 ? -26.883 -10.796 20.747 1.00 48.13  ? 704 PHE   A CD1 1 
ATOM   3259 C  CD2 . PHE   A 1 408 ? -25.100 -11.127 19.173 1.00 53.92  ? 704 PHE   A CD2 1 
ATOM   3260 C  CE1 . PHE   A 1 408 ? -27.693 -10.315 19.716 1.00 55.69  ? 704 PHE   A CE1 1 
ATOM   3261 C  CE2 . PHE   A 1 408 ? -25.897 -10.638 18.155 1.00 49.85  ? 704 PHE   A CE2 1 
ATOM   3262 C  CZ  . PHE   A 1 408 ? -27.190 -10.227 18.427 1.00 55.13  ? 704 PHE   A CZ  1 
ATOM   3263 N  N   . GLU   A 1 409 ? -22.396 -14.196 22.074 1.00 47.68  ? 705 GLU   A N   1 
ATOM   3264 C  CA  . GLU   A 1 409 ? -21.316 -14.621 22.940 1.00 56.70  ? 705 GLU   A CA  1 
ATOM   3265 C  C   . GLU   A 1 409 ? -20.078 -13.785 22.659 1.00 61.51  ? 705 GLU   A C   1 
ATOM   3266 O  O   . GLU   A 1 409 ? -19.969 -13.119 21.626 1.00 54.80  ? 705 GLU   A O   1 
ATOM   3267 C  CB  . GLU   A 1 409 ? -21.013 -16.112 22.754 1.00 53.33  ? 705 GLU   A CB  1 
ATOM   3268 C  CG  . GLU   A 1 409 ? -22.234 -17.014 22.899 1.00 64.40  ? 705 GLU   A CG  1 
ATOM   3269 C  CD  . GLU   A 1 409 ? -22.746 -17.135 24.339 1.00 75.82  ? 705 GLU   A CD  1 
ATOM   3270 O  OE1 . GLU   A 1 409 ? -22.112 -16.587 25.276 1.00 69.39  ? 705 GLU   A OE1 1 
ATOM   3271 O  OE2 . GLU   A 1 409 ? -23.795 -17.793 24.527 1.00 80.44  ? 705 GLU   A OE2 1 
ATOM   3272 N  N   . TYR   A 1 410 ? -19.169 -13.783 23.622 1.00 50.12  ? 706 TYR   A N   1 
ATOM   3273 C  CA  . TYR   A 1 410 ? -17.854 -13.213 23.397 1.00 48.83  ? 706 TYR   A CA  1 
ATOM   3274 C  C   . TYR   A 1 410 ? -16.985 -14.229 22.676 1.00 56.68  ? 706 TYR   A C   1 
ATOM   3275 O  O   . TYR   A 1 410 ? -17.280 -15.427 22.642 1.00 62.32  ? 706 TYR   A O   1 
ATOM   3276 C  CB  . TYR   A 1 410 ? -17.207 -12.802 24.731 1.00 60.81  ? 706 TYR   A CB  1 
ATOM   3277 C  CG  . TYR   A 1 410 ? -17.695 -11.461 25.241 1.00 59.28  ? 706 TYR   A CG  1 
ATOM   3278 C  CD1 . TYR   A 1 410 ? -18.543 -11.374 26.343 1.00 70.79  ? 706 TYR   A CD1 1 
ATOM   3279 C  CD2 . TYR   A 1 410 ? -17.322 -10.284 24.600 1.00 72.63  ? 706 TYR   A CD2 1 
ATOM   3280 C  CE1 . TYR   A 1 410 ? -18.991 -10.142 26.800 1.00 71.63  ? 706 TYR   A CE1 1 
ATOM   3281 C  CE2 . TYR   A 1 410 ? -17.767 -9.056  25.038 1.00 77.44  ? 706 TYR   A CE2 1 
ATOM   3282 C  CZ  . TYR   A 1 410 ? -18.602 -8.982  26.137 1.00 74.67  ? 706 TYR   A CZ  1 
ATOM   3283 O  OH  . TYR   A 1 410 ? -19.037 -7.732  26.556 1.00 62.16  ? 706 TYR   A OH  1 
ATOM   3284 N  N   . GLN   A 1 411 ? -15.896 -13.741 22.098 1.00 53.59  ? 707 GLN   A N   1 
ATOM   3285 C  CA  . GLN   A 1 411 ? -14.989 -14.600 21.360 1.00 54.12  ? 707 GLN   A CA  1 
ATOM   3286 C  C   . GLN   A 1 411 ? -13.616 -13.961 21.426 1.00 61.55  ? 707 GLN   A C   1 
ATOM   3287 O  O   . GLN   A 1 411 ? -13.514 -12.733 21.534 1.00 70.78  ? 707 GLN   A O   1 
ATOM   3288 C  CB  . GLN   A 1 411 ? -15.432 -14.774 19.891 1.00 56.38  ? 707 GLN   A CB  1 
ATOM   3289 C  CG  . GLN   A 1 411 ? -15.478 -13.472 19.137 1.00 61.40  ? 707 GLN   A CG  1 
ATOM   3290 C  CD  . GLN   A 1 411 ? -15.924 -13.621 17.693 1.00 69.93  ? 707 GLN   A CD  1 
ATOM   3291 O  OE1 . GLN   A 1 411 ? -15.800 -14.693 17.084 1.00 68.44  ? 707 GLN   A OE1 1 
ATOM   3292 N  NE2 . GLN   A 1 411 ? -16.439 -12.535 17.133 1.00 70.23  ? 707 GLN   A NE2 1 
ATOM   3293 N  N   . PRO   A 1 412 ? -12.552 -14.756 21.376 1.00 70.45  ? 708 PRO   A N   1 
ATOM   3294 C  CA  . PRO   A 1 412 ? -11.201 -14.184 21.411 1.00 79.84  ? 708 PRO   A CA  1 
ATOM   3295 C  C   . PRO   A 1 412 ? -11.009 -13.123 20.338 1.00 79.60  ? 708 PRO   A C   1 
ATOM   3296 O  O   . PRO   A 1 412 ? -11.625 -13.167 19.272 1.00 83.59  ? 708 PRO   A O   1 
ATOM   3297 C  CB  . PRO   A 1 412 ? -10.299 -15.398 21.161 1.00 87.94  ? 708 PRO   A CB  1 
ATOM   3298 C  CG  . PRO   A 1 412 ? -11.092 -16.557 21.701 1.00 85.92  ? 708 PRO   A CG  1 
ATOM   3299 C  CD  . PRO   A 1 412 ? -12.545 -16.228 21.443 1.00 76.22  ? 708 PRO   A CD  1 
ATOM   3300 N  N   . ASP   A 1 413 ? -10.162 -12.149 20.647 1.00 81.55  ? 709 ASP   A N   1 
ATOM   3301 C  CA  . ASP   A 1 413 ? -9.775  -11.166 19.650 1.00 87.36  ? 709 ASP   A CA  1 
ATOM   3302 C  C   . ASP   A 1 413 ? -9.027  -11.861 18.516 1.00 91.15  ? 709 ASP   A C   1 
ATOM   3303 O  O   . ASP   A 1 413 ? -8.205  -12.751 18.767 1.00 93.32  ? 709 ASP   A O   1 
ATOM   3304 C  CB  . ASP   A 1 413 ? -8.903  -10.078 20.277 1.00 97.82  ? 709 ASP   A CB  1 
ATOM   3305 C  CG  . ASP   A 1 413 ? -9.682  -9.178  21.220 1.00 95.30  ? 709 ASP   A CG  1 
ATOM   3306 O  OD1 . ASP   A 1 413 ? -10.911 -9.038  21.032 1.00 90.70  ? 709 ASP   A OD1 1 
ATOM   3307 O  OD2 . ASP   A 1 413 ? -9.067  -8.606  22.144 1.00 93.19  ? 709 ASP   A OD2 1 
ATOM   3308 N  N   . PRO   A 1 414 ? -9.284  -11.485 17.262 1.00 90.77  ? 710 PRO   A N   1 
ATOM   3309 C  CA  . PRO   A 1 414 ? -8.763  -12.281 16.137 1.00 95.71  ? 710 PRO   A CA  1 
ATOM   3310 C  C   . PRO   A 1 414 ? -7.247  -12.334 16.067 1.00 96.80  ? 710 PRO   A C   1 
ATOM   3311 O  O   . PRO   A 1 414 ? -6.696  -13.326 15.572 1.00 104.89 ? 710 PRO   A O   1 
ATOM   3312 C  CB  . PRO   A 1 414 ? -9.356  -11.582 14.902 1.00 88.65  ? 710 PRO   A CB  1 
ATOM   3313 C  CG  . PRO   A 1 414 ? -10.465 -10.711 15.422 1.00 87.55  ? 710 PRO   A CG  1 
ATOM   3314 C  CD  . PRO   A 1 414 ? -10.080 -10.331 16.816 1.00 91.08  ? 710 PRO   A CD  1 
ATOM   3315 N  N   . TRP   A 1 415 ? -6.549  -11.304 16.547 1.00 85.81  ? 711 TRP   A N   1 
ATOM   3316 C  CA  . TRP   A 1 415 ? -5.097  -11.285 16.422 1.00 93.78  ? 711 TRP   A CA  1 
ATOM   3317 C  C   . TRP   A 1 415 ? -4.400  -12.230 17.395 1.00 94.54  ? 711 TRP   A C   1 
ATOM   3318 O  O   . TRP   A 1 415 ? -3.199  -12.474 17.236 1.00 91.28  ? 711 TRP   A O   1 
ATOM   3319 C  CB  . TRP   A 1 415 ? -4.571  -9.858  16.605 1.00 97.06  ? 711 TRP   A CB  1 
ATOM   3320 C  CG  . TRP   A 1 415 ? -5.060  -9.169  17.838 1.00 97.70  ? 711 TRP   A CG  1 
ATOM   3321 C  CD1 . TRP   A 1 415 ? -4.494  -9.213  19.080 1.00 99.84  ? 711 TRP   A CD1 1 
ATOM   3322 C  CD2 . TRP   A 1 415 ? -6.212  -8.321  17.953 1.00 96.20  ? 711 TRP   A CD2 1 
ATOM   3323 N  NE1 . TRP   A 1 415 ? -5.224  -8.452  19.959 1.00 90.94  ? 711 TRP   A NE1 1 
ATOM   3324 C  CE2 . TRP   A 1 415 ? -6.282  -7.893  19.294 1.00 90.17  ? 711 TRP   A CE2 1 
ATOM   3325 C  CE3 . TRP   A 1 415 ? -7.189  -7.884  17.052 1.00 97.01  ? 711 TRP   A CE3 1 
ATOM   3326 C  CZ2 . TRP   A 1 415 ? -7.289  -7.049  19.756 1.00 85.91  ? 711 TRP   A CZ2 1 
ATOM   3327 C  CZ3 . TRP   A 1 415 ? -8.191  -7.045  17.514 1.00 88.67  ? 711 TRP   A CZ3 1 
ATOM   3328 C  CH2 . TRP   A 1 415 ? -8.233  -6.639  18.854 1.00 91.95  ? 711 TRP   A CH2 1 
ATOM   3329 N  N   . ASN   A 1 416 ? -5.108  -12.763 18.390 1.00 97.68  ? 712 ASN   A N   1 
ATOM   3330 C  CA  . ASN   A 1 416 ? -4.536  -13.771 19.275 1.00 106.05 ? 712 ASN   A CA  1 
ATOM   3331 C  C   . ASN   A 1 416 ? -4.732  -15.184 18.751 1.00 104.26 ? 712 ASN   A C   1 
ATOM   3332 O  O   . ASN   A 1 416 ? -4.143  -16.123 19.301 1.00 111.15 ? 712 ASN   A O   1 
ATOM   3333 C  CB  . ASN   A 1 416 ? -5.151  -13.667 20.675 1.00 106.65 ? 712 ASN   A CB  1 
ATOM   3334 C  CG  . ASN   A 1 416 ? -5.096  -12.262 21.230 1.00 107.78 ? 712 ASN   A CG  1 
ATOM   3335 O  OD1 . ASN   A 1 416 ? -4.155  -11.513 20.963 1.00 112.20 ? 712 ASN   A OD1 1 
ATOM   3336 N  ND2 . ASN   A 1 416 ? -6.110  -11.892 22.003 1.00 104.55 ? 712 ASN   A ND2 1 
ATOM   3337 N  N   . THR   A 1 417 ? -5.535  -15.347 17.700 1.00 87.11  ? 713 THR   A N   1 
ATOM   3338 C  CA  . THR   A 1 417 ? -5.945  -16.652 17.217 1.00 95.38  ? 713 THR   A CA  1 
ATOM   3339 C  C   . THR   A 1 417 ? -5.698  -16.864 15.731 1.00 102.06 ? 713 THR   A C   1 
ATOM   3340 O  O   . THR   A 1 417 ? -5.726  -18.013 15.277 1.00 112.57 ? 713 THR   A O   1 
ATOM   3341 C  CB  . THR   A 1 417 ? -7.439  -16.867 17.506 1.00 92.85  ? 713 THR   A CB  1 
ATOM   3342 O  OG1 . THR   A 1 417 ? -8.101  -15.595 17.533 1.00 85.24  ? 713 THR   A OG1 1 
ATOM   3343 C  CG2 . THR   A 1 417 ? -7.636  -17.578 18.832 1.00 94.56  ? 713 THR   A CG2 1 
ATOM   3344 N  N   . HIS   A 1 418 ? -5.446  -15.804 14.969 1.00 103.64 ? 714 HIS   A N   1 
ATOM   3345 C  CA  . HIS   A 1 418 ? -5.355  -15.877 13.513 1.00 97.01  ? 714 HIS   A CA  1 
ATOM   3346 C  C   . HIS   A 1 418 ? -4.014  -16.472 13.096 1.00 111.94 ? 714 HIS   A C   1 
ATOM   3347 O  O   . HIS   A 1 418 ? -2.967  -15.836 13.269 1.00 111.42 ? 714 HIS   A O   1 
ATOM   3348 C  CB  . HIS   A 1 418 ? -5.548  -14.482 12.921 1.00 94.95  ? 714 HIS   A CB  1 
ATOM   3349 C  CG  . HIS   A 1 418 ? -5.440  -14.428 11.428 1.00 96.30  ? 714 HIS   A CG  1 
ATOM   3350 N  ND1 . HIS   A 1 418 ? -5.910  -15.431 10.608 1.00 98.43  ? 714 HIS   A ND1 1 
ATOM   3351 C  CD2 . HIS   A 1 418 ? -4.931  -13.479 10.607 1.00 99.15  ? 714 HIS   A CD2 1 
ATOM   3352 C  CE1 . HIS   A 1 418 ? -5.687  -15.105 9.346  1.00 101.13 ? 714 HIS   A CE1 1 
ATOM   3353 N  NE2 . HIS   A 1 418 ? -5.095  -13.925 9.318  1.00 97.93  ? 714 HIS   A NE2 1 
ATOM   3354 N  N   . VAL   A 1 419 ? -4.041  -17.686 12.533 1.00 122.53 ? 715 VAL   A N   1 
ATOM   3355 C  CA  . VAL   A 1 419 ? -2.862  -18.262 11.888 1.00 127.18 ? 715 VAL   A CA  1 
ATOM   3356 C  C   . VAL   A 1 419 ? -2.494  -17.353 10.721 1.00 132.11 ? 715 VAL   A C   1 
ATOM   3357 O  O   . VAL   A 1 419 ? -2.992  -17.515 9.600  1.00 126.74 ? 715 VAL   A O   1 
ATOM   3358 C  CB  . VAL   A 1 419 ? -3.096  -19.716 11.427 1.00 121.68 ? 715 VAL   A CB  1 
ATOM   3359 C  CG1 . VAL   A 1 419 ? -1.918  -20.214 10.597 1.00 123.79 ? 715 VAL   A CG1 1 
ATOM   3360 C  CG2 . VAL   A 1 419 ? -3.302  -20.636 12.628 1.00 114.59 ? 715 VAL   A CG2 1 
ATOM   3361 N  N   . TRP   A 1 420 ? -1.638  -16.374 10.998 1.00 141.62 ? 716 TRP   A N   1 
ATOM   3362 C  CA  . TRP   A 1 420 ? -1.275  -15.332 10.054 1.00 147.62 ? 716 TRP   A CA  1 
ATOM   3363 C  C   . TRP   A 1 420 ? -0.162  -15.816 9.132  1.00 164.60 ? 716 TRP   A C   1 
ATOM   3364 O  O   . TRP   A 1 420 ? 0.647   -16.678 9.493  1.00 168.81 ? 716 TRP   A O   1 
ATOM   3365 C  CB  . TRP   A 1 420 ? -0.830  -14.076 10.806 1.00 146.10 ? 716 TRP   A CB  1 
ATOM   3366 C  CG  . TRP   A 1 420 ? -1.345  -12.804 10.219 1.00 145.13 ? 716 TRP   A CG  1 
ATOM   3367 C  CD1 . TRP   A 1 420 ? -1.696  -12.585 8.922  1.00 147.09 ? 716 TRP   A CD1 1 
ATOM   3368 C  CD2 . TRP   A 1 420 ? -1.584  -11.573 10.913 1.00 141.07 ? 716 TRP   A CD2 1 
ATOM   3369 N  NE1 . TRP   A 1 420 ? -2.130  -11.292 8.760  1.00 144.72 ? 716 TRP   A NE1 1 
ATOM   3370 C  CE2 . TRP   A 1 420 ? -2.072  -10.649 9.968  1.00 138.66 ? 716 TRP   A CE2 1 
ATOM   3371 C  CE3 . TRP   A 1 420 ? -1.429  -11.163 12.239 1.00 139.46 ? 716 TRP   A CE3 1 
ATOM   3372 C  CZ2 . TRP   A 1 420 ? -2.405  -9.341  10.304 1.00 133.78 ? 716 TRP   A CZ2 1 
ATOM   3373 C  CZ3 . TRP   A 1 420 ? -1.760  -9.864  12.572 1.00 139.75 ? 716 TRP   A CZ3 1 
ATOM   3374 C  CH2 . TRP   A 1 420 ? -2.243  -8.968  11.608 1.00 136.18 ? 716 TRP   A CH2 1 
ATOM   3375 N  N   . LYS   A 1 421 ? -0.127  -15.254 7.925  1.00 87.88  ? 717 LYS   A N   1 
ATOM   3376 C  CA  . LYS   A 1 421 ? 0.899   -15.605 6.945  1.00 96.03  ? 717 LYS   A CA  1 
ATOM   3377 C  C   . LYS   A 1 421 ? 1.344   -14.352 6.190  1.00 98.10  ? 717 LYS   A C   1 
ATOM   3378 O  O   . LYS   A 1 421 ? 1.310   -14.290 4.957  1.00 88.68  ? 717 LYS   A O   1 
ATOM   3379 C  CB  . LYS   A 1 421 ? 0.393   -16.688 5.998  1.00 94.74  ? 717 LYS   A CB  1 
ATOM   3380 C  CG  . LYS   A 1 421 ? 0.216   -18.029 6.679  1.00 103.80 ? 717 LYS   A CG  1 
ATOM   3381 C  CD  . LYS   A 1 421 ? -0.413  -19.070 5.786  1.00 109.40 ? 717 LYS   A CD  1 
ATOM   3382 C  CE  . LYS   A 1 421 ? -0.775  -20.321 6.578  1.00 112.58 ? 717 LYS   A CE  1 
ATOM   3383 N  NZ  . LYS   A 1 421 ? -0.791  -21.512 5.685  1.00 117.08 ? 717 LYS   A NZ  1 
ATOM   3384 N  N   . GLY   A 1 422 ? 1.777   -13.341 6.946  1.00 97.04  ? 718 GLY   A N   1 
ATOM   3385 C  CA  . GLY   A 1 422 ? 2.305   -12.105 6.389  1.00 104.22 ? 718 GLY   A CA  1 
ATOM   3386 C  C   . GLY   A 1 422 ? 1.442   -11.492 5.300  1.00 114.68 ? 718 GLY   A C   1 
ATOM   3387 O  O   . GLY   A 1 422 ? 1.622   -11.782 4.117  1.00 111.85 ? 718 GLY   A O   1 
ATOM   3388 O  OXT . GLY   A 1 422 ? 0.540   -10.702 5.577  1.00 115.86 ? 718 GLY   A OXT 1 
HETATM 3389 C  CHA . HEM   B 2 .   ? -25.208 -4.404  26.256 1.00 50.93  ? 801 HEM   A CHA 1 
HETATM 3390 C  CHB . HEM   B 2 .   ? -28.161 -0.621  25.740 1.00 59.70  ? 801 HEM   A CHB 1 
HETATM 3391 C  CHC . HEM   B 2 .   ? -29.454 -2.390  21.393 1.00 62.16  ? 801 HEM   A CHC 1 
HETATM 3392 C  CHD . HEM   B 2 .   ? -27.113 -6.526  22.289 1.00 57.04  ? 801 HEM   A CHD 1 
HETATM 3393 C  C1A . HEM   B 2 .   ? -25.764 -3.158  26.459 1.00 61.27  ? 801 HEM   A C1A 1 
HETATM 3394 C  C2A . HEM   B 2 .   ? -25.363 -2.132  27.414 1.00 62.49  ? 801 HEM   A C2A 1 
HETATM 3395 C  C3A . HEM   B 2 .   ? -26.190 -1.093  27.264 1.00 63.65  ? 801 HEM   A C3A 1 
HETATM 3396 C  C4A . HEM   B 2 .   ? -27.139 -1.409  26.215 1.00 63.96  ? 801 HEM   A C4A 1 
HETATM 3397 C  CMA . HEM   B 2 .   ? -26.123 0.216   28.086 1.00 43.89  ? 801 HEM   A CMA 1 
HETATM 3398 C  CAA . HEM   B 2 .   ? -24.200 -2.167  28.433 1.00 57.17  ? 801 HEM   A CAA 1 
HETATM 3399 C  CBA . HEM   B 2 .   ? -22.866 -1.905  27.725 1.00 66.92  ? 801 HEM   A CBA 1 
HETATM 3400 C  CGA . HEM   B 2 .   ? -21.837 -1.324  28.673 1.00 74.05  ? 801 HEM   A CGA 1 
HETATM 3401 O  O1A . HEM   B 2 .   ? -22.197 -0.455  29.517 1.00 75.36  ? 801 HEM   A O1A 1 
HETATM 3402 O  O2A . HEM   B 2 .   ? -20.636 -1.705  28.579 1.00 72.53  ? 801 HEM   A O2A 1 
HETATM 3403 C  C1B . HEM   B 2 .   ? -28.767 -0.763  24.513 1.00 64.34  ? 801 HEM   A C1B 1 
HETATM 3404 C  C2B . HEM   B 2 .   ? -29.689 0.185   23.925 1.00 63.61  ? 801 HEM   A C2B 1 
HETATM 3405 C  C3B . HEM   B 2 .   ? -30.061 -0.298  22.727 1.00 67.68  ? 801 HEM   A C3B 1 
HETATM 3406 C  C4B . HEM   B 2 .   ? -29.372 -1.570  22.504 1.00 64.59  ? 801 HEM   A C4B 1 
HETATM 3407 C  CMB . HEM   B 2 .   ? -30.166 1.504   24.575 1.00 53.60  ? 801 HEM   A CMB 1 
HETATM 3408 C  CAB . HEM   B 2 .   ? -31.049 0.426   21.779 1.00 70.37  ? 801 HEM   A CAB 1 
HETATM 3409 C  CBB . HEM   B 2 .   ? -31.620 -0.181  20.737 1.00 69.69  ? 801 HEM   A CBB 1 
HETATM 3410 C  C1C . HEM   B 2 .   ? -28.914 -3.644  21.232 1.00 57.78  ? 801 HEM   A C1C 1 
HETATM 3411 C  C2C . HEM   B 2 .   ? -29.010 -4.463  20.031 1.00 53.98  ? 801 HEM   A C2C 1 
HETATM 3412 C  C3C . HEM   B 2 .   ? -28.363 -5.628  20.275 1.00 58.87  ? 801 HEM   A C3C 1 
HETATM 3413 C  C4C . HEM   B 2 .   ? -27.846 -5.562  21.640 1.00 48.73  ? 801 HEM   A C4C 1 
HETATM 3414 C  CMC . HEM   B 2 .   ? -29.753 -3.967  18.765 1.00 51.89  ? 801 HEM   A CMC 1 
HETATM 3415 C  CAC . HEM   B 2 .   ? -28.155 -6.865  19.369 1.00 63.94  ? 801 HEM   A CAC 1 
HETATM 3416 C  CBC . HEM   B 2 .   ? -28.668 -6.971  18.137 1.00 60.96  ? 801 HEM   A CBC 1 
HETATM 3417 C  C1D . HEM   B 2 .   ? -26.400 -6.314  23.450 1.00 55.33  ? 801 HEM   A C1D 1 
HETATM 3418 C  C2D . HEM   B 2 .   ? -25.546 -7.269  24.103 1.00 51.93  ? 801 HEM   A C2D 1 
HETATM 3419 C  C3D . HEM   B 2 .   ? -25.018 -6.678  25.208 1.00 53.03  ? 801 HEM   A C3D 1 
HETATM 3420 C  C4D . HEM   B 2 .   ? -25.523 -5.330  25.272 1.00 50.31  ? 801 HEM   A C4D 1 
HETATM 3421 C  CMD . HEM   B 2 .   ? -25.339 -8.707  23.581 1.00 40.23  ? 801 HEM   A CMD 1 
HETATM 3422 C  CAD . HEM   B 2 .   ? -24.071 -7.229  26.301 1.00 55.55  ? 801 HEM   A CAD 1 
HETATM 3423 C  CBD . HEM   B 2 .   ? -22.787 -7.901  25.852 1.00 64.85  ? 801 HEM   A CBD 1 
HETATM 3424 C  CGD . HEM   B 2 .   ? -22.377 -8.843  26.977 1.00 68.36  ? 801 HEM   A CGD 1 
HETATM 3425 O  O1D . HEM   B 2 .   ? -23.058 -9.892  27.186 1.00 59.35  ? 801 HEM   A O1D 1 
HETATM 3426 O  O2D . HEM   B 2 .   ? -21.357 -8.543  27.645 1.00 65.94  ? 801 HEM   A O2D 1 
HETATM 3427 N  NA  . HEM   B 2 .   ? -26.849 -2.674  25.758 1.00 66.32  ? 801 HEM   A NA  1 
HETATM 3428 N  NB  . HEM   B 2 .   ? -28.590 -1.820  23.618 1.00 61.15  ? 801 HEM   A NB  1 
HETATM 3429 N  NC  . HEM   B 2 .   ? -28.203 -4.347  22.176 1.00 54.76  ? 801 HEM   A NC  1 
HETATM 3430 N  ND  . HEM   B 2 .   ? -26.365 -5.140  24.182 1.00 47.87  ? 801 HEM   A ND  1 
HETATM 3431 FE FE  . HEM   B 2 .   ? -27.846 -3.718  24.168 1.00 52.10  ? 801 HEM   A FE  1 
HETATM 3432 N  N1  . H4B   C 3 .   ? -22.037 -3.157  33.650 1.00 61.31  ? 802 H4B   A N1  1 
HETATM 3433 C  C2  . H4B   C 3 .   ? -22.070 -2.646  32.387 1.00 54.69  ? 802 H4B   A C2  1 
HETATM 3434 N  N2  . H4B   C 3 .   ? -23.234 -2.247  31.826 1.00 47.20  ? 802 H4B   A N2  1 
HETATM 3435 N  N3  . H4B   C 3 .   ? -20.948 -2.519  31.661 1.00 54.42  ? 802 H4B   A N3  1 
HETATM 3436 C  C4  . H4B   C 3 .   ? -19.763 -2.894  32.167 1.00 55.52  ? 802 H4B   A C4  1 
HETATM 3437 O  O4  . H4B   C 3 .   ? -18.719 -2.770  31.473 1.00 46.67  ? 802 H4B   A O4  1 
HETATM 3438 C  C4A . H4B   C 3 .   ? -19.710 -3.424  33.442 1.00 57.26  ? 802 H4B   A C4A 1 
HETATM 3439 C  C8A . H4B   C 3 .   ? -20.866 -3.554  34.192 1.00 60.50  ? 802 H4B   A C8A 1 
HETATM 3440 N  N5  . H4B   C 3 .   ? -18.540 -3.830  33.961 1.00 47.99  ? 802 H4B   A N5  1 
HETATM 3441 N  N8  . H4B   C 3 .   ? -20.822 -4.057  35.469 1.00 53.50  ? 802 H4B   A N8  1 
HETATM 3442 C  C6  . H4B   C 3 .   ? -18.601 -4.868  34.982 1.00 56.18  ? 802 H4B   A C6  1 
HETATM 3443 C  C7  . H4B   C 3 .   ? -19.574 -4.472  36.108 1.00 50.68  ? 802 H4B   A C7  1 
HETATM 3444 C  C9  . H4B   C 3 .   ? -17.229 -5.072  35.609 1.00 44.52  ? 802 H4B   A C9  1 
HETATM 3445 O  O9  . H4B   C 3 .   ? -16.851 -3.768  36.076 1.00 48.67  ? 802 H4B   A O9  1 
HETATM 3446 C  C10 . H4B   C 3 .   ? -17.332 -6.002  36.815 1.00 51.57  ? 802 H4B   A C10 1 
HETATM 3447 C  C11 . H4B   C 3 .   ? -15.975 -6.231  37.491 1.00 64.44  ? 802 H4B   A C11 1 
HETATM 3448 O  O10 . H4B   C 3 .   ? -17.902 -7.279  36.470 1.00 52.39  ? 802 H4B   A O10 1 
HETATM 3449 C  C11 . A1A0G D 4 .   ? -22.637 -1.558  23.873 1.00 63.99  ? 803 A1A0G A C11 1 
HETATM 3450 C  C12 . A1A0G D 4 .   ? -22.338 -2.890  24.098 1.00 54.62  ? 803 A1A0G A C12 1 
HETATM 3451 C  C13 . A1A0G D 4 .   ? -21.141 -3.221  24.731 1.00 76.94  ? 803 A1A0G A C13 1 
HETATM 3452 C  C14 . A1A0G D 4 .   ? -20.246 -2.230  25.122 1.00 82.13  ? 803 A1A0G A C14 1 
HETATM 3453 C  C15 . A1A0G D 4 .   ? -20.547 -0.889  24.890 1.00 79.64  ? 803 A1A0G A C15 1 
HETATM 3454 C  C16 . A1A0G D 4 .   ? -21.742 -0.561  24.255 1.00 69.91  ? 803 A1A0G A C16 1 
HETATM 3455 C  C17 . A1A0G D 4 .   ? -19.573 0.195   25.315 1.00 72.50  ? 803 A1A0G A C17 1 
HETATM 3456 C  C02 . A1A0G D 4 .   ? -25.760 0.271   23.105 1.00 70.09  ? 803 A1A0G A C02 1 
HETATM 3457 C  C03 . A1A0G D 4 .   ? -26.247 -0.409  21.986 1.00 63.26  ? 803 A1A0G A C03 1 
HETATM 3458 C  C04 . A1A0G D 4 .   ? -25.542 -1.484  21.474 1.00 63.37  ? 803 A1A0G A C04 1 
HETATM 3459 C  C05 . A1A0G D 4 .   ? -24.358 -1.876  22.093 1.00 61.35  ? 803 A1A0G A C05 1 
HETATM 3460 C  C06 . A1A0G D 4 .   ? -23.905 -1.174  23.204 1.00 68.06  ? 803 A1A0G A C06 1 
HETATM 3461 C  C07 . A1A0G D 4 .   ? -26.060 -2.220  20.259 1.00 54.15  ? 803 A1A0G A C07 1 
HETATM 3462 C  C19 . A1A0G D 4 .   ? -19.715 1.707   27.185 1.00 82.13  ? 803 A1A0G A C19 1 
HETATM 3463 N  N01 . A1A0G D 4 .   ? -24.609 -0.121  23.691 1.00 65.81  ? 803 A1A0G A N01 1 
HETATM 3464 N  N02 . A1A0G D 4 .   ? -26.441 1.324   23.601 1.00 70.17  ? 803 A1A0G A N02 1 
HETATM 3465 N  N18 . A1A0G D 4 .   ? -20.305 1.347   25.877 1.00 70.24  ? 803 A1A0G A N18 1 
HETATM 3466 CL CL1 . A1A0G D 4 .   ? -20.748 -4.940  25.053 1.00 87.97  ? 803 A1A0G A CL1 1 
HETATM 3467 C  C   . ACT   E 5 .   ? -34.788 2.225   25.147 1.00 110.26 ? 804 ACT   A C   1 
HETATM 3468 O  O   . ACT   E 5 .   ? -34.502 3.305   24.577 1.00 106.58 ? 804 ACT   A O   1 
HETATM 3469 O  OXT . ACT   E 5 .   ? -35.160 2.182   26.342 1.00 107.59 ? 804 ACT   A OXT 1 
HETATM 3470 C  CH3 . ACT   E 5 .   ? -34.677 0.942   24.377 1.00 107.64 ? 804 ACT   A CH3 1 
HETATM 3471 ZN ZN  . ZN    F 6 .   ? -24.385 -16.464 40.770 0.50 50.76  ? 805 ZN    A ZN  1 
HETATM 3472 O  O   . HOH   G 7 .   ? -15.271 -21.120 9.192  1.00 71.77  ? 901 HOH   A O   1 
HETATM 3473 O  O   . HOH   G 7 .   ? -18.555 19.089  44.568 1.00 77.48  ? 902 HOH   A O   1 
HETATM 3474 O  O   . HOH   G 7 .   ? -30.138 -12.954 40.403 1.00 59.75  ? 903 HOH   A O   1 
HETATM 3475 O  O   . HOH   G 7 .   ? -18.425 12.715  11.133 1.00 72.93  ? 904 HOH   A O   1 
HETATM 3476 O  O   . HOH   G 7 .   ? -28.689 0.942   15.327 1.00 47.86  ? 905 HOH   A O   1 
HETATM 3477 O  O   . HOH   G 7 .   ? -38.701 -22.725 8.417  1.00 68.81  ? 906 HOH   A O   1 
HETATM 3478 O  O   . HOH   G 7 .   ? -10.510 12.832  35.966 1.00 85.25  ? 907 HOH   A O   1 
HETATM 3479 O  O   . HOH   G 7 .   ? -19.043 -9.719  15.153 1.00 53.05  ? 908 HOH   A O   1 
HETATM 3480 O  O   . HOH   G 7 .   ? -24.470 -12.287 32.304 1.00 52.57  ? 909 HOH   A O   1 
HETATM 3481 O  O   . HOH   G 7 .   ? -26.451 -34.492 13.863 1.00 78.64  ? 910 HOH   A O   1 
HETATM 3482 O  O   . HOH   G 7 .   ? -11.912 3.322   35.428 1.00 81.47  ? 911 HOH   A O   1 
HETATM 3483 O  O   . HOH   G 7 .   ? -41.136 -6.261  39.053 1.00 68.73  ? 912 HOH   A O   1 
HETATM 3484 O  O   . HOH   G 7 .   ? -34.754 6.537   37.663 1.00 69.37  ? 913 HOH   A O   1 
HETATM 3485 O  O   . HOH   G 7 .   ? -24.614 -10.954 37.508 1.00 53.49  ? 914 HOH   A O   1 
HETATM 3486 O  O   . HOH   G 7 .   ? -27.993 -13.406 23.839 1.00 56.93  ? 915 HOH   A O   1 
HETATM 3487 O  O   . HOH   G 7 .   ? -25.464 -4.199  5.954  1.00 59.62  ? 916 HOH   A O   1 
HETATM 3488 O  O   . HOH   G 7 .   ? -15.671 3.550   22.078 1.00 86.67  ? 917 HOH   A O   1 
HETATM 3489 O  O   . HOH   G 7 .   ? -19.666 -8.379  34.487 1.00 52.82  ? 918 HOH   A O   1 
HETATM 3490 O  O   . HOH   G 7 .   ? -21.895 -15.034 -2.899 1.00 58.28  ? 919 HOH   A O   1 
HETATM 3491 O  O   . HOH   G 7 .   ? -38.134 -0.721  41.033 1.00 61.73  ? 920 HOH   A O   1 
HETATM 3492 O  O   . HOH   G 7 .   ? -17.299 -16.729 9.313  1.00 76.31  ? 921 HOH   A O   1 
HETATM 3493 O  O   . HOH   G 7 .   ? -15.886 -30.371 19.447 1.00 74.71  ? 922 HOH   A O   1 
HETATM 3494 O  O   . HOH   G 7 .   ? -27.650 -8.517  0.249  1.00 82.98  ? 923 HOH   A O   1 
HETATM 3495 O  O   . HOH   G 7 .   ? -23.838 -18.497 6.870  1.00 53.65  ? 924 HOH   A O   1 
HETATM 3496 O  O   . HOH   G 7 .   ? -34.896 -11.867 35.730 1.00 63.83  ? 925 HOH   A O   1 
HETATM 3497 O  O   . HOH   G 7 .   ? -29.535 -15.671 27.945 1.00 57.09  ? 926 HOH   A O   1 
HETATM 3498 O  O   . HOH   G 7 .   ? -21.540 -10.188 35.118 1.00 50.60  ? 927 HOH   A O   1 
HETATM 3499 O  O   . HOH   G 7 .   ? -23.991 2.692   30.966 1.00 48.57  ? 928 HOH   A O   1 
HETATM 3500 O  O   . HOH   G 7 .   ? -15.506 1.435   29.461 1.00 56.85  ? 929 HOH   A O   1 
HETATM 3501 O  O   . HOH   G 7 .   ? -18.820 3.177   23.985 1.00 52.54  ? 930 HOH   A O   1 
HETATM 3502 O  O   . HOH   G 7 .   ? -12.711 -20.549 20.944 1.00 82.01  ? 931 HOH   A O   1 
HETATM 3503 O  O   . HOH   G 7 .   ? -20.264 -14.465 10.874 1.00 69.61  ? 932 HOH   A O   1 
HETATM 3504 O  O   . HOH   G 7 .   ? -28.585 -10.733 38.001 1.00 62.81  ? 933 HOH   A O   1 
HETATM 3505 O  O   . HOH   G 7 .   ? -24.177 -1.908  37.871 1.00 53.15  ? 934 HOH   A O   1 
HETATM 3506 O  O   . HOH   G 7 .   ? -23.366 -0.659  34.405 1.00 46.50  ? 935 HOH   A O   1 
HETATM 3507 O  O   . HOH   G 7 .   ? -21.803 0.518   32.629 1.00 52.48  ? 936 HOH   A O   1 
HETATM 3508 O  O   . HOH   G 7 .   ? -20.465 -8.433  17.013 1.00 55.32  ? 937 HOH   A O   1 
HETATM 3509 O  O   . HOH   G 7 .   ? -27.704 23.637  21.507 1.00 70.38  ? 938 HOH   A O   1 
HETATM 3510 O  O   . HOH   G 7 .   ? -25.341 0.242   32.175 1.00 53.34  ? 939 HOH   A O   1 
HETATM 3511 O  O   . HOH   G 7 .   ? -19.550 14.535  12.299 1.00 56.95  ? 940 HOH   A O   1 
HETATM 3512 O  O   . HOH   G 7 .   ? -35.786 -7.402  9.377  1.00 70.60  ? 941 HOH   A O   1 
HETATM 3513 O  O   . HOH   G 7 .   ? -44.216 -12.082 22.954 1.00 95.82  ? 942 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   ? 2.1328 1.8748 1.5924 -0.6132 0.0784  -0.0248 299 ARG A N   
2    C CA  . ARG A 3   ? 2.1423 1.8730 1.6104 -0.6045 0.0715  -0.0299 299 ARG A CA  
3    C C   . ARG A 3   ? 1.9983 1.8694 1.5558 -0.6019 0.0715  -0.0374 299 ARG A C   
4    O O   . ARG A 3   ? 2.1147 2.0051 1.6813 -0.6058 0.0675  -0.0430 299 ARG A O   
5    C CB  . ARG A 3   ? 2.3173 1.9781 1.6958 -0.6424 0.0722  -0.0321 299 ARG A CB  
6    C CG  . ARG A 3   ? 2.3804 1.9643 1.7306 -0.6249 0.0647  -0.0337 299 ARG A CG  
7    C CD  . ARG A 3   ? 2.4707 1.9263 1.7752 -0.5827 0.0588  -0.0268 299 ARG A CD  
8    N NE  . ARG A 3   ? 2.4195 1.9015 1.7975 -0.5355 0.0537  -0.0245 299 ARG A NE  
9    C CZ  . ARG A 3   ? 2.4210 1.8680 1.8187 -0.4945 0.0451  -0.0254 299 ARG A CZ  
10   N NH1 . ARG A 3   ? 2.4934 1.8770 1.8442 -0.4913 0.0414  -0.0282 299 ARG A NH1 
11   N NH2 . ARG A 3   ? 2.3404 1.8148 1.8004 -0.4575 0.0402  -0.0239 299 ARG A NH2 
12   N N   . PHE A 4   ? 1.7676 1.7364 1.3863 -0.5927 0.0762  -0.0373 300 PHE A N   
13   C CA  . PHE A 4   ? 1.5810 1.6913 1.2799 -0.5830 0.0768  -0.0444 300 PHE A CA  
14   C C   . PHE A 4   ? 1.5252 1.6917 1.2859 -0.5487 0.0792  -0.0417 300 PHE A C   
15   O O   . PHE A 4   ? 1.6219 1.8849 1.4113 -0.5512 0.0869  -0.0430 300 PHE A O   
16   C CB  . PHE A 4   ? 1.5726 1.7711 1.2593 -0.6228 0.0829  -0.0498 300 PHE A CB  
17   C CG  . PHE A 4   ? 1.7336 1.8483 1.3268 -0.6709 0.0848  -0.0491 300 PHE A CG  
18   C CD1 . PHE A 4   ? 1.7969 1.8567 1.3324 -0.6944 0.0906  -0.0443 300 PHE A CD1 
19   C CD2 . PHE A 4   ? 1.7256 1.8145 1.2836 -0.6929 0.0810  -0.0535 300 PHE A CD2 
20   C CE1 . PHE A 4   ? 1.8540 1.8321 1.2957 -0.7386 0.0918  -0.0444 300 PHE A CE1 
21   C CE2 . PHE A 4   ? 1.7871 1.7949 1.2508 -0.7382 0.0830  -0.0532 300 PHE A CE2 
22   C CZ  . PHE A 4   ? 1.8156 1.7671 1.2197 -0.7610 0.0881  -0.0489 300 PHE A CZ  
23   N N   . LEU A 5   ? 1.4487 1.5521 1.2255 -0.4996 0.0700  -0.0386 301 LEU A N   
24   C CA  . LEU A 5   ? 1.2189 1.3273 1.0261 -0.4478 0.0674  -0.0346 301 LEU A CA  
25   C C   . LEU A 5   ? 1.0873 1.3214 0.9632 -0.4176 0.0688  -0.0401 301 LEU A C   
26   O O   . LEU A 5   ? 1.0221 1.3362 0.9334 -0.4196 0.0679  -0.0469 301 LEU A O   
27   C CB  . LEU A 5   ? 1.0544 1.0774 0.8639 -0.3986 0.0547  -0.0313 301 LEU A CB  
28   C CG  . LEU A 5   ? 1.1660 1.0603 0.9012 -0.4131 0.0531  -0.0249 301 LEU A CG  
29   C CD1 . LEU A 5   ? 1.1866 1.0173 0.9219 -0.3777 0.0415  -0.0248 301 LEU A CD1 
30   C CD2 . LEU A 5   ? 1.1840 1.0343 0.8918 -0.4014 0.0550  -0.0172 301 LEU A CD2 
31   N N   . LYS A 6   ? 0.9377 1.1838 0.8266 -0.3857 0.0702  -0.0371 302 LYS A N   
32   C CA  . LYS A 6   ? 0.9835 1.3310 0.9231 -0.3491 0.0716  -0.0419 302 LYS A CA  
33   C C   . LYS A 6   ? 0.8885 1.1945 0.8498 -0.2890 0.0603  -0.0403 302 LYS A C   
34   O O   . LYS A 6   ? 0.8337 1.0549 0.7707 -0.2778 0.0558  -0.0341 302 LYS A O   
35   C CB  . LYS A 6   ? 1.0902 1.4976 1.0203 -0.3655 0.0846  -0.0411 302 LYS A CB  
36   C CG  . LYS A 6   ? 1.2662 1.7204 1.1690 -0.4340 0.0972  -0.0419 302 LYS A CG  
37   C CD  . LYS A 6   ? 1.2611 1.8453 1.2036 -0.4454 0.1004  -0.0505 302 LYS A CD  
38   C CE  . LYS A 6   ? 1.3225 1.9609 1.2340 -0.5079 0.1100  -0.0523 302 LYS A CE  
39   N NZ  . LYS A 6   ? 1.2909 1.9990 1.2020 -0.5070 0.1204  -0.0518 302 LYS A NZ  
40   N N   . VAL A 7   ? 0.7835 1.1494 0.7859 -0.2514 0.0556  -0.0458 303 VAL A N   
41   C CA  . VAL A 7   ? 0.7277 1.0615 0.7453 -0.1987 0.0457  -0.0450 303 VAL A CA  
42   C C   . VAL A 7   ? 0.7657 1.1792 0.8015 -0.1655 0.0498  -0.0499 303 VAL A C   
43   O O   . VAL A 7   ? 0.7793 1.2844 0.8359 -0.1651 0.0544  -0.0559 303 VAL A O   
44   C CB  . VAL A 7   ? 0.6233 0.9278 0.6592 -0.1801 0.0342  -0.0462 303 VAL A CB  
45   C CG1 . VAL A 7   ? 0.8033 1.0383 0.8169 -0.2106 0.0317  -0.0425 303 VAL A CG1 
46   C CG2 . VAL A 7   ? 0.6852 1.0747 0.7513 -0.1711 0.0344  -0.0533 303 VAL A CG2 
47   N N   . LYS A 8   ? 0.6609 1.0410 0.6847 -0.1365 0.0480  -0.0477 304 LYS A N   
48   C CA  . LYS A 8   ? 0.6790 1.1188 0.7069 -0.1006 0.0523  -0.0523 304 LYS A CA  
49   C C   . LYS A 8   ? 0.5979 1.0020 0.6282 -0.0504 0.0406  -0.0542 304 LYS A C   
50   O O   . LYS A 8   ? 0.6671 0.9907 0.6913 -0.0464 0.0300  -0.0502 304 LYS A O   
51   C CB  . LYS A 8   ? 0.6647 1.0903 0.6671 -0.1057 0.0598  -0.0492 304 LYS A CB  
52   C CG  . LYS A 8   ? 0.7515 1.2389 0.7516 -0.0660 0.0658  -0.0547 304 LYS A CG  
53   C CD  . LYS A 8   ? 0.7405 1.2228 0.7149 -0.0773 0.0753  -0.0517 304 LYS A CD  
54   C CE  . LYS A 8   ? 0.7804 1.3179 0.7472 -0.0310 0.0809  -0.0578 304 LYS A CE  
55   N NZ  . LYS A 8   ? 0.8417 1.3695 0.7810 -0.0378 0.0897  -0.0552 304 LYS A NZ  
56   N N   . ASN A 9   ? 0.5471 1.0136 0.5821 -0.0125 0.0427  -0.0605 305 ASN A N   
57   C CA  . ASN A 9   ? 0.7080 1.1311 0.7261 0.0377  0.0336  -0.0624 305 ASN A CA  
58   C C   . ASN A 9   ? 0.7493 1.1663 0.7388 0.0602  0.0387  -0.0636 305 ASN A C   
59   O O   . ASN A 9   ? 0.8740 1.3734 0.8650 0.0690  0.0501  -0.0678 305 ASN A O   
60   C CB  . ASN A 9   ? 0.6589 1.1408 0.6871 0.0733  0.0316  -0.0686 305 ASN A CB  
61   C CG  . ASN A 9   ? 0.7988 1.2144 0.7965 0.1217  0.0210  -0.0699 305 ASN A CG  
62   O OD1 . ASN A 9   ? 0.8935 1.2825 0.8575 0.1523  0.0216  -0.0716 305 ASN A OD1 
63   N ND2 . ASN A 9   ? 0.7171 1.1004 0.7201 0.1271  0.0114  -0.0690 305 ASN A ND2 
64   N N   . TRP A 10  ? 0.8508 1.1764 0.8137 0.0682  0.0305  -0.0601 306 TRP A N   
65   C CA  . TRP A 10  ? 0.9841 1.2934 0.9149 0.0873  0.0344  -0.0612 306 TRP A CA  
66   C C   . TRP A 10  ? 1.1223 1.4236 1.0203 0.1438  0.0314  -0.0677 306 TRP A C   
67   O O   . TRP A 10  ? 1.3288 1.6204 1.1946 0.1659  0.0354  -0.0702 306 TRP A O   
68   C CB  . TRP A 10  ? 0.9810 1.1990 0.8933 0.0678  0.0265  -0.0549 306 TRP A CB  
69   C CG  . TRP A 10  ? 0.9244 1.1414 0.8531 0.0206  0.0305  -0.0485 306 TRP A CG  
70   C CD1 . TRP A 10  ? 0.8166 1.0046 0.7633 -0.0065 0.0244  -0.0439 306 TRP A CD1 
71   C CD2 . TRP A 10  ? 0.9801 1.2193 0.8998 -0.0036 0.0418  -0.0459 306 TRP A CD2 
72   N NE1 . TRP A 10  ? 0.7973 0.9801 0.7414 -0.0435 0.0305  -0.0387 306 TRP A NE1 
73   C CE2 . TRP A 10  ? 0.9703 1.1826 0.8973 -0.0450 0.0412  -0.0395 306 TRP A CE2 
74   C CE3 . TRP A 10  ? 0.9346 1.2113 0.8360 0.0065  0.0527  -0.0484 306 TRP A CE3 
75   C CZ2 . TRP A 10  ? 1.0198 1.2328 0.9311 -0.0784 0.0507  -0.0348 306 TRP A CZ2 
76   C CZ3 . TRP A 10  ? 1.0089 1.2959 0.9015 -0.0293 0.0628  -0.0437 306 TRP A CZ3 
77   C CH2 . TRP A 10  ? 0.9760 1.2275 0.8713 -0.0723 0.0615  -0.0367 306 TRP A CH2 
78   N N   . GLU A 11  ? 1.1222 1.4203 1.0204 0.1692  0.0243  -0.0705 307 GLU A N   
79   C CA  . GLU A 11  ? 1.1128 1.4055 0.9706 0.2278  0.0226  -0.0770 307 GLU A CA  
80   C C   . GLU A 11  ? 1.0909 1.5048 0.9635 0.2548  0.0351  -0.0834 307 GLU A C   
81   O O   . GLU A 11  ? 1.1665 1.5977 1.0031 0.3028  0.0397  -0.0892 307 GLU A O   
82   C CB  . GLU A 11  ? 1.0506 1.2822 0.8925 0.2455  0.0096  -0.0767 307 GLU A CB  
83   C CG  . GLU A 11  ? 1.1947 1.3730 0.9714 0.3046  0.0045  -0.0821 307 GLU A CG  
84   C CD  . GLU A 11  ? 1.4090 1.5568 1.1717 0.3261  -0.0050 -0.0824 307 GLU A CD  
85   O OE1 . GLU A 11  ? 1.4943 1.6683 1.2270 0.3801  -0.0037 -0.0881 307 GLU A OE1 
86   O OE2 . GLU A 11  ? 1.4360 1.5359 1.2152 0.2915  -0.0135 -0.0768 307 GLU A OE2 
87   N N   . THR A 12  ? 0.9485 1.4504 0.8712 0.2240  0.0408  -0.0828 308 THR A N   
88   C CA  . THR A 12  ? 0.8795 1.5126 0.8224 0.2449  0.0511  -0.0890 308 THR A CA  
89   C C   . THR A 12  ? 0.8479 1.5785 0.8237 0.1989  0.0658  -0.0882 308 THR A C   
90   O O   . THR A 12  ? 0.8125 1.6684 0.8064 0.2111  0.0755  -0.0935 308 THR A O   
91   C CB  . THR A 12  ? 0.8879 1.5577 0.8562 0.2494  0.0447  -0.0904 308 THR A CB  
92   O OG1 . THR A 12  ? 0.7647 1.4084 0.7672 0.1889  0.0413  -0.0845 308 THR A OG1 
93   C CG2 . THR A 12  ? 0.9464 1.5293 0.8722 0.3010  0.0318  -0.0917 308 THR A CG2 
94   N N   . ASP A 13  ? 1.0061 1.6854 0.9861 0.1465  0.0677  -0.0816 309 ASP A N   
95   C CA  . ASP A 13  ? 1.1012 1.8529 1.1016 0.0943  0.0813  -0.0795 309 ASP A CA  
96   C C   . ASP A 13  ? 1.0903 1.9266 1.1292 0.0563  0.0843  -0.0805 309 ASP A C   
97   O O   . ASP A 13  ? 1.1794 2.1099 1.2327 0.0192  0.0970  -0.0812 309 ASP A O   
98   C CB  . ASP A 13  ? 1.2360 2.0728 1.2234 0.1180  0.0954  -0.0841 309 ASP A CB  
99   C CG  . ASP A 13  ? 1.3339 2.0884 1.2839 0.1251  0.0964  -0.0811 309 ASP A CG  
100  O OD1 . ASP A 13  ? 1.3525 2.0768 1.3014 0.0745  0.1010  -0.0747 309 ASP A OD1 
101  O OD2 . ASP A 13  ? 1.3669 2.0825 1.2825 0.1817  0.0923  -0.0852 309 ASP A OD2 
102  N N   . VAL A 14  ? 1.0279 1.8326 1.0802 0.0618  0.0728  -0.0806 310 VAL A N   
103  C CA  . VAL A 14  ? 0.9386 1.8088 1.0230 0.0232  0.0737  -0.0816 310 VAL A CA  
104  C C   . VAL A 14  ? 0.9231 1.7237 1.0070 -0.0421 0.0733  -0.0747 310 VAL A C   
105  O O   . VAL A 14  ? 0.8857 1.5722 0.9524 -0.0437 0.0656  -0.0691 310 VAL A O   
106  C CB  . VAL A 14  ? 0.7351 1.5964 0.8295 0.0582  0.0615  -0.0845 310 VAL A CB  
107  C CG1 . VAL A 14  ? 0.8546 1.7614 0.9783 0.0122  0.0606  -0.0849 310 VAL A CG1 
108  C CG2 . VAL A 14  ? 0.7113 1.6509 0.7996 0.1243  0.0624  -0.0917 310 VAL A CG2 
109  N N   . VAL A 15  ? 0.8505 1.7193 0.9482 -0.0958 0.0812  -0.0752 311 VAL A N   
110  C CA  . VAL A 15  ? 0.8100 1.6086 0.8967 -0.1566 0.0807  -0.0694 311 VAL A CA  
111  C C   . VAL A 15  ? 0.8241 1.6608 0.9301 -0.1845 0.0770  -0.0725 311 VAL A C   
112  O O   . VAL A 15  ? 0.8590 1.8140 0.9878 -0.1821 0.0808  -0.0788 311 VAL A O   
113  C CB  . VAL A 15  ? 0.7633 1.5795 0.8283 -0.2072 0.0944  -0.0659 311 VAL A CB  
114  C CG1 . VAL A 15  ? 0.8042 1.5338 0.8440 -0.2668 0.0933  -0.0599 311 VAL A CG1 
115  C CG2 . VAL A 15  ? 0.6811 1.4520 0.7252 -0.1769 0.0968  -0.0628 311 VAL A CG2 
116  N N   . LEU A 16  ? 0.6929 1.4323 0.7884 -0.2080 0.0692  -0.0684 312 LEU A N   
117  C CA  . LEU A 16  ? 0.8062 1.5612 0.9120 -0.2378 0.0652  -0.0711 312 LEU A CA  
118  C C   . LEU A 16  ? 0.8400 1.5109 0.9115 -0.2968 0.0672  -0.0660 312 LEU A C   
119  O O   . LEU A 16  ? 0.7441 1.3136 0.7896 -0.2942 0.0651  -0.0596 312 LEU A O   
120  C CB  . LEU A 16  ? 0.8138 1.5269 0.9361 -0.1938 0.0518  -0.0721 312 LEU A CB  
121  C CG  . LEU A 16  ? 0.9357 1.7260 1.0808 -0.1357 0.0488  -0.0775 312 LEU A CG  
122  C CD1 . LEU A 16  ? 0.9132 1.6189 1.0554 -0.0876 0.0366  -0.0753 312 LEU A CD1 
123  C CD2 . LEU A 16  ? 1.0128 1.9127 1.1819 -0.1466 0.0492  -0.0843 312 LEU A CD2 
124  N N   . THR A 17  ? 0.7993 1.5105 0.8644 -0.3493 0.0708  -0.0691 313 THR A N   
125  C CA  . THR A 17  ? 0.8139 1.4377 0.8322 -0.4074 0.0731  -0.0650 313 THR A CA  
126  C C   . THR A 17  ? 0.9194 1.4726 0.9327 -0.4074 0.0624  -0.0659 313 THR A C   
127  O O   . THR A 17  ? 0.9271 1.5438 0.9644 -0.4104 0.0588  -0.0721 313 THR A O   
128  C CB  . THR A 17  ? 0.8627 1.5402 0.8514 -0.4621 0.0809  -0.0674 313 THR A CB  
129  O OG1 . THR A 17  ? 0.8399 1.5930 0.8349 -0.4571 0.0899  -0.0674 313 THR A OG1 
130  C CG2 . THR A 17  ? 0.9744 1.5309 0.8945 -0.5114 0.0817  -0.0624 313 THR A CG2 
131  N N   . ASP A 18  ? 0.9082 1.3344 0.8882 -0.4028 0.0575  -0.0598 314 ASP A N   
132  C CA  . ASP A 18  ? 0.9379 1.2899 0.9093 -0.3961 0.0479  -0.0602 314 ASP A CA  
133  C C   . ASP A 18  ? 1.0310 1.3147 0.9419 -0.4557 0.0514  -0.0597 314 ASP A C   
134  O O   . ASP A 18  ? 1.0794 1.2712 0.9390 -0.4710 0.0541  -0.0535 314 ASP A O   
135  C CB  . ASP A 18  ? 0.9122 1.1769 0.8849 -0.3472 0.0395  -0.0544 314 ASP A CB  
136  C CG  . ASP A 18  ? 0.8744 1.0906 0.8524 -0.3287 0.0297  -0.0556 314 ASP A CG  
137  O OD1 . ASP A 18  ? 0.9146 1.0712 0.8530 -0.3597 0.0296  -0.0561 314 ASP A OD1 
138  O OD2 . ASP A 18  ? 0.7222 0.9568 0.7384 -0.2842 0.0225  -0.0562 314 ASP A OD2 
139  N N   . THR A 19  ? 1.0320 1.3523 0.9401 -0.4825 0.0503  -0.0656 315 THR A N   
140  C CA  . THR A 19  ? 1.1719 1.4037 1.0112 -0.5169 0.0502  -0.0648 315 THR A CA  
141  C C   . THR A 19  ? 1.1717 1.3385 1.0080 -0.5003 0.0410  -0.0669 315 THR A C   
142  O O   . THR A 19  ? 1.1411 1.2085 0.9132 -0.5186 0.0403  -0.0652 315 THR A O   
143  C CB  . THR A 19  ? 1.1881 1.4899 1.0084 -0.5535 0.0547  -0.0693 315 THR A CB  
144  O OG1 . THR A 19  ? 1.2349 1.6701 1.1206 -0.5314 0.0536  -0.0748 315 THR A OG1 
145  C CG2 . THR A 19  ? 1.1573 1.4490 0.9273 -0.5914 0.0636  -0.0662 315 THR A CG2 
146  N N   . LEU A 20  ? 1.0775 1.2968 0.9770 -0.4642 0.0340  -0.0706 316 LEU A N   
147  C CA  . LEU A 20  ? 0.9444 1.1141 0.8452 -0.4433 0.0251  -0.0729 316 LEU A CA  
148  C C   . LEU A 20  ? 0.9820 1.0230 0.8395 -0.4219 0.0219  -0.0669 316 LEU A C   
149  O O   . LEU A 20  ? 1.1646 1.1389 0.9915 -0.4218 0.0176  -0.0688 316 LEU A O   
150  C CB  . LEU A 20  ? 0.8729 1.1155 0.8425 -0.3902 0.0186  -0.0746 316 LEU A CB  
151  C CG  . LEU A 20  ? 0.8296 1.0389 0.8109 -0.3610 0.0098  -0.0763 316 LEU A CG  
152  C CD1 . LEU A 20  ? 0.7924 1.0141 0.7545 -0.3994 0.0085  -0.0838 316 LEU A CD1 
153  C CD2 . LEU A 20  ? 0.6644 0.9329 0.7039 -0.3084 0.0041  -0.0758 316 LEU A CD2 
154  N N   . HIS A 21  ? 0.9778 0.9868 0.8311 -0.4004 0.0236  -0.0599 317 HIS A N   
155  C CA  . HIS A 21  ? 0.9901 0.8886 0.8030 -0.3756 0.0199  -0.0538 317 HIS A CA  
156  C C   . HIS A 21  ? 1.1032 0.8993 0.8302 -0.4136 0.0224  -0.0541 317 HIS A C   
157  O O   . HIS A 21  ? 1.1213 0.8230 0.8076 -0.3882 0.0182  -0.0509 317 HIS A O   
158  C CB  . HIS A 21  ? 1.0263 0.9156 0.8429 -0.3556 0.0218  -0.0466 317 HIS A CB  
159  C CG  . HIS A 21  ? 0.9378 0.8070 0.7052 -0.4007 0.0310  -0.0441 317 HIS A CG  
160  N ND1 . HIS A 21  ? 0.9878 0.9464 0.7738 -0.4370 0.0391  -0.0474 317 HIS A ND1 
161  C CD2 . HIS A 21  ? 1.0986 0.8695 0.7952 -0.4149 0.0337  -0.0383 317 HIS A CD2 
162  C CE1 . HIS A 21  ? 1.1129 1.0305 0.8428 -0.4767 0.0471  -0.0436 317 HIS A CE1 
163  N NE2 . HIS A 21  ? 1.1683 0.9659 0.8405 -0.4640 0.0438  -0.0378 317 HIS A NE2 
164  N N   . LEU A 22  ? 1.1794 0.9933 0.8734 -0.4710 0.0292  -0.0577 318 LEU A N   
165  C CA  . LEU A 22  ? 1.4256 1.1433 1.0305 -0.4939 0.0316  -0.0558 318 LEU A CA  
166  C C   . LEU A 22  ? 1.4301 1.1068 1.0185 -0.4841 0.0256  -0.0608 318 LEU A C   
167  O O   . LEU A 22  ? 1.5406 1.1071 1.0534 -0.4801 0.0246  -0.0587 318 LEU A O   
168  C CB  . LEU A 22  ? 1.4818 1.2489 1.0607 -0.5426 0.0400  -0.0565 318 LEU A CB  
169  C CG  . LEU A 22  ? 1.3950 1.1951 0.9764 -0.5563 0.0471  -0.0519 318 LEU A CG  
170  C CD1 . LEU A 22  ? 1.3770 1.2484 0.9415 -0.6041 0.0546  -0.0548 318 LEU A CD1 
171  C CD2 . LEU A 22  ? 1.4489 1.1238 0.9580 -0.5485 0.0476  -0.0442 318 LEU A CD2 
172  N N   . LYS A 23  ? 1.3825 1.1454 1.0364 -0.4774 0.0216  -0.0674 319 LYS A N   
173  C CA  . LYS A 23  ? 1.4268 1.1552 1.0712 -0.4649 0.0156  -0.0727 319 LYS A CA  
174  C C   . LYS A 23  ? 1.3257 0.9928 0.9769 -0.4145 0.0089  -0.0714 319 LYS A C   
175  O O   . LYS A 23  ? 1.3124 0.9472 0.9535 -0.3960 0.0043  -0.0752 319 LYS A O   
176  C CB  . LYS A 23  ? 1.3661 1.2093 1.0774 -0.4694 0.0129  -0.0796 319 LYS A CB  
177  C CG  . LYS A 23  ? 1.4292 1.3568 1.1426 -0.5089 0.0192  -0.0807 319 LYS A CG  
178  C CD  . LYS A 23  ? 1.6058 1.4654 1.2339 -0.5482 0.0233  -0.0804 319 LYS A CD  
179  C CE  . LYS A 23  ? 1.6324 1.5488 1.2700 -0.5664 0.0213  -0.0867 319 LYS A CE  
180  N NZ  . LYS A 23  ? 1.6018 1.6558 1.2922 -0.5813 0.0242  -0.0893 319 LYS A NZ  
181  N N   . SER A 24  ? 1.2652 0.9296 0.9373 -0.3796 0.0087  -0.0637 320 SER A N   
182  C CA  . SER A 24  ? 1.2566 0.8921 0.9470 -0.3191 0.0026  -0.0594 320 SER A CA  
183  C C   . SER A 24  ? 1.4553 0.9704 1.0633 -0.3070 0.0010  -0.0593 320 SER A C   
184  O O   . SER A 24  ? 1.3803 0.8072 0.9049 -0.3368 0.0048  -0.0585 320 SER A O   
185  C CB  . SER A 24  ? 1.2632 0.9160 0.9822 -0.2911 0.0023  -0.0515 320 SER A CB  
186  O OG  . SER A 24  ? 1.2694 0.8861 0.9910 -0.2394 -0.0037 -0.0471 320 SER A OG  
187  N N   . THR A 25  ? 1.7077 1.2178 1.3344 -0.2617 -0.0044 -0.0599 321 THR A N   
188  C CA  . THR A 25  ? 1.8760 1.2820 1.4282 -0.2387 -0.0062 -0.0608 321 THR A CA  
189  C C   . THR A 25  ? 1.7950 1.1864 1.3568 -0.1777 -0.0106 -0.0540 321 THR A C   
190  O O   . THR A 25  ? 1.8156 1.1218 1.3094 -0.1626 -0.0106 -0.0497 321 THR A O   
191  C CB  . THR A 25  ? 1.9471 1.3626 1.5034 -0.2406 -0.0081 -0.0690 321 THR A CB  
192  O OG1 . THR A 25  ? 2.0110 1.3502 1.5174 -0.1970 -0.0107 -0.0693 321 THR A OG1 
193  C CG2 . THR A 25  ? 1.8429 1.3796 1.5020 -0.2276 -0.0108 -0.0700 321 THR A CG2 
194  N N   . LEU A 26  ? 1.6418 1.1162 1.2832 -0.1439 -0.0147 -0.0527 322 LEU A N   
195  C CA  . LEU A 26  ? 1.6106 1.0886 1.2664 -0.0902 -0.0194 -0.0468 322 LEU A CA  
196  C C   . LEU A 26  ? 1.6077 1.0784 1.2597 -0.0849 -0.0200 -0.0393 322 LEU A C   
197  O O   . LEU A 26  ? 1.6587 1.1291 1.3046 -0.1217 -0.0161 -0.0383 322 LEU A O   
198  C CB  . LEU A 26  ? 1.5226 1.0972 1.2642 -0.0686 -0.0231 -0.0467 322 LEU A CB  
199  C CG  . LEU A 26  ? 1.5736 1.1510 1.3158 -0.0468 -0.0242 -0.0512 322 LEU A CG  
200  C CD1 . LEU A 26  ? 1.4849 1.1536 1.3044 -0.0551 -0.0254 -0.0529 322 LEU A CD1 
201  C CD2 . LEU A 26  ? 1.6075 1.1718 1.3358 0.0065  -0.0277 -0.0472 322 LEU A CD2 
202  N N   . GLU A 27  ? 1.4836 0.9550 1.1394 -0.0377 -0.0251 -0.0341 323 GLU A N   
203  C CA  . GLU A 27  ? 1.4542 0.9193 1.1047 -0.0246 -0.0275 -0.0267 323 GLU A CA  
204  C C   . GLU A 27  ? 1.3464 0.9103 1.0825 -0.0099 -0.0323 -0.0233 323 GLU A C   
205  O O   . GLU A 27  ? 1.2800 0.9043 1.0672 0.0030  -0.0348 -0.0252 323 GLU A O   
206  C CB  . GLU A 27  ? 1.4831 0.8685 1.0598 0.0186  -0.0307 -0.0232 323 GLU A CB  
207  C CG  . GLU A 27  ? 1.6170 0.8809 1.0887 0.0002  -0.0260 -0.0257 323 GLU A CG  
208  C CD  . GLU A 27  ? 1.9031 1.0745 1.2877 0.0477  -0.0294 -0.0216 323 GLU A CD  
209  O OE1 . GLU A 27  ? 1.9220 1.1206 1.3234 0.0822  -0.0348 -0.0149 323 GLU A OE1 
210  O OE2 . GLU A 27  ? 2.0927 1.1613 1.3864 0.0519  -0.0273 -0.0252 323 GLU A OE2 
211  N N   . THR A 28  ? 1.1537 0.7282 0.8989 -0.0149 -0.0334 -0.0181 324 THR A N   
212  C CA  . THR A 28  ? 1.0345 0.6911 0.8506 -0.0127 -0.0374 -0.0156 324 THR A CA  
213  C C   . THR A 28  ? 1.0984 0.7787 0.9265 0.0260  -0.0456 -0.0100 324 THR A C   
214  O O   . THR A 28  ? 1.0866 0.8361 0.9712 0.0298  -0.0501 -0.0089 324 THR A O   
215  C CB  . THR A 28  ? 1.1054 0.7679 0.9265 -0.0436 -0.0335 -0.0143 324 THR A CB  
216  O OG1 . THR A 28  ? 1.0687 0.6715 0.8356 -0.0362 -0.0338 -0.0090 324 THR A OG1 
217  C CG2 . THR A 28  ? 1.1643 0.8205 0.9761 -0.0842 -0.0254 -0.0199 324 THR A CG2 
218  N N   . GLY A 29  ? 1.2145 0.8391 0.9864 0.0541  -0.0481 -0.0065 325 GLY A N   
219  C CA  . GLY A 29  ? 1.1779 0.8313 0.9576 0.0901  -0.0565 -0.0010 325 GLY A CA  
220  C C   . GLY A 29  ? 1.1998 0.8238 0.9528 0.0871  -0.0583 0.0044  325 GLY A C   
221  O O   . GLY A 29  ? 1.2302 0.8435 0.9560 0.1224  -0.0649 0.0092  325 GLY A O   
222  N N   . CYS A 30  ? 1.1999 0.8151 0.9588 0.0480  -0.0525 0.0037  326 CYS A N   
223  C CA  . CYS A 30  ? 1.2425 0.8250 0.9709 0.0419  -0.0526 0.0086  326 CYS A CA  
224  C C   . CYS A 30  ? 1.3109 0.7899 0.9494 0.0441  -0.0485 0.0108  326 CYS A C   
225  O O   . CYS A 30  ? 1.3294 0.7584 0.9302 0.0338  -0.0431 0.0069  326 CYS A O   
226  C CB  . CYS A 30  ? 1.0958 0.7067 0.8561 0.0009  -0.0465 0.0068  326 CYS A CB  
227  S SG  . CYS A 30  ? 0.9492 0.6579 0.7965 -0.0065 -0.0497 0.0033  326 CYS A SG  
228  N N   . THR A 31  ? 1.2633 0.7043 0.8611 0.0561  -0.0514 0.0170  327 THR A N   
229  C CA  . THR A 31  ? 1.4263 0.7589 0.9298 0.0498  -0.0466 0.0203  327 THR A CA  
230  C C   . THR A 31  ? 1.4088 0.7355 0.9068 0.0156  -0.0417 0.0238  327 THR A C   
231  O O   . THR A 31  ? 1.3740 0.7780 0.9393 0.0018  -0.0422 0.0229  327 THR A O   
232  C CB  . THR A 31  ? 1.4206 0.6973 0.8602 0.1053  -0.0549 0.0255  327 THR A CB  
233  O OG1 . THR A 31  ? 1.4392 0.7755 0.9149 0.1329  -0.0645 0.0304  327 THR A OG1 
234  C CG2 . THR A 31  ? 1.4041 0.6888 0.8445 0.1411  -0.0582 0.0214  327 THR A CG2 
235  N N   . GLU A 32  ? 1.5399 0.7684 0.9498 0.0018  -0.0366 0.0278  328 GLU A N   
236  C CA  . GLU A 32  ? 1.6668 0.8854 1.0622 -0.0286 -0.0313 0.0321  328 GLU A CA  
237  C C   . GLU A 32  ? 1.5760 0.8316 0.9953 0.0047  -0.0409 0.0376  328 GLU A C   
238  O O   . GLU A 32  ? 1.5349 0.8092 0.9652 -0.0176 -0.0374 0.0400  328 GLU A O   
239  C CB  . GLU A 32  ? 1.9014 0.9966 1.1849 -0.0515 -0.0241 0.0362  328 GLU A CB  
240  C CG  . GLU A 32  ? 2.0203 1.0701 1.2675 -0.0916 -0.0151 0.0304  328 GLU A CG  
241  C CD  . GLU A 32  ? 2.2095 1.1831 1.3968 -0.0549 -0.0203 0.0289  328 GLU A CD  
242  O OE1 . GLU A 32  ? 2.3677 1.2297 1.4503 -0.0639 -0.0168 0.0305  328 GLU A OE1 
243  O OE2 . GLU A 32  ? 2.1643 1.1988 1.4096 -0.0164 -0.0275 0.0252  328 GLU A OE2 
244  N N   . HIS A 33  ? 1.5362 0.8108 0.9652 0.0568  -0.0529 0.0393  329 HIS A N   
245  C CA  . HIS A 33  ? 1.5367 0.8472 0.9813 0.0886  -0.0637 0.0445  329 HIS A CA  
246  C C   . HIS A 33  ? 1.4014 0.8227 0.9352 0.1076  -0.0732 0.0413  329 HIS A C   
247  O O   . HIS A 33  ? 1.3081 0.7697 0.8590 0.1294  -0.0833 0.0449  329 HIS A O   
248  C CB  . HIS A 33  ? 1.8053 1.0375 1.1647 0.1368  -0.0711 0.0511  329 HIS A CB  
249  C CG  . HIS A 33  ? 2.1053 1.2088 1.3590 0.1193  -0.0622 0.0546  329 HIS A CG  
250  N ND1 . HIS A 33  ? 2.2359 1.2590 1.4252 0.1261  -0.0585 0.0524  329 HIS A ND1 
251  C CD2 . HIS A 33  ? 2.2037 1.2408 1.3989 0.0910  -0.0559 0.0600  329 HIS A CD2 
252  C CE1 . HIS A 33  ? 2.3479 1.2552 1.4391 0.1004  -0.0508 0.0564  329 HIS A CE1 
253  N NE2 . HIS A 33  ? 2.3363 1.2526 1.4307 0.0780  -0.0488 0.0614  329 HIS A NE2 
254  N N   . ILE A 34  ? 1.2636 0.7340 0.8503 0.0974  -0.0708 0.0349  330 ILE A N   
255  C CA  . ILE A 34  ? 1.1437 0.7147 0.8104 0.1046  -0.0786 0.0322  330 ILE A CA  
256  C C   . ILE A 34  ? 1.1031 0.7125 0.8219 0.0728  -0.0712 0.0253  330 ILE A C   
257  O O   . ILE A 34  ? 1.1318 0.7080 0.8325 0.0649  -0.0644 0.0219  330 ILE A O   
258  C CB  . ILE A 34  ? 1.1408 0.7461 0.8108 0.1529  -0.0898 0.0339  330 ILE A CB  
259  C CG1 . ILE A 34  ? 1.0050 0.7157 0.7532 0.1495  -0.0975 0.0317  330 ILE A CG1 
260  C CG2 . ILE A 34  ? 1.3542 0.9232 0.9961 0.1701  -0.0856 0.0309  330 ILE A CG2 
261  C CD1 . ILE A 34  ? 1.0886 0.8545 0.8431 0.1922  -0.1102 0.0347  330 ILE A CD1 
262  N N   . CYS A 35  ? 1.0657 0.7410 0.8434 0.0558  -0.0732 0.0230  331 CYS A N   
263  C CA  . CYS A 35  ? 0.9420 0.6558 0.7670 0.0301  -0.0675 0.0170  331 CYS A CA  
264  C C   . CYS A 35  ? 0.9551 0.7354 0.8292 0.0439  -0.0759 0.0155  331 CYS A C   
265  O O   . CYS A 35  ? 0.7353 0.5559 0.6293 0.0512  -0.0850 0.0178  331 CYS A O   
266  C CB  . CYS A 35  ? 0.9028 0.6315 0.7456 0.0014  -0.0624 0.0152  331 CYS A CB  
267  S SG  . CYS A 35  ? 0.7798 0.5632 0.6792 -0.0195 -0.0581 0.0081  331 CYS A SG  
268  N N   . MET A 36  ? 0.8970 0.6880 0.7866 0.0442  -0.0727 0.0118  332 MET A N   
269  C CA  . MET A 36  ? 0.9444 0.7960 0.8763 0.0535  -0.0784 0.0104  332 MET A CA  
270  C C   . MET A 36  ? 0.8304 0.7162 0.8048 0.0267  -0.0753 0.0061  332 MET A C   
271  O O   . MET A 36  ? 0.6328 0.5572 0.6360 0.0283  -0.0773 0.0044  332 MET A O   
272  C CB  . MET A 36  ? 1.0384 0.8770 0.9534 0.0763  -0.0768 0.0092  332 MET A CB  
273  C CG  . MET A 36  ? 1.2237 1.0107 1.0810 0.1088  -0.0788 0.0128  332 MET A CG  
274  S SD  . MET A 36  ? 1.3305 1.1775 1.1953 0.1528  -0.0916 0.0174  332 MET A SD  
275  C CE  . MET A 36  ? 1.4724 1.2302 1.2501 0.1932  -0.0918 0.0211  332 MET A CE  
276  N N   . GLY A 37  ? 0.8331 0.7059 0.8080 0.0047  -0.0703 0.0043  333 GLY A N   
277  C CA  . GLY A 37  ? 0.7698 0.6677 0.7750 -0.0139 -0.0669 -0.0001 333 GLY A CA  
278  C C   . GLY A 37  ? 0.7571 0.6975 0.7921 -0.0148 -0.0747 0.0002  333 GLY A C   
279  O O   . GLY A 37  ? 0.6966 0.6513 0.7500 -0.0252 -0.0724 -0.0031 333 GLY A O   
280  N N   . SER A 38  ? 0.6683 0.6290 0.7041 -0.0059 -0.0840 0.0041  334 SER A N   
281  C CA  . SER A 38  ? 0.6832 0.6833 0.7403 -0.0149 -0.0915 0.0046  334 SER A CA  
282  C C   . SER A 38  ? 0.6269 0.6695 0.6978 -0.0028 -0.0965 0.0069  334 SER A C   
283  O O   . SER A 38  ? 0.6522 0.7350 0.7377 -0.0141 -0.1035 0.0082  334 SER A O   
284  C CB  . SER A 38  ? 0.7325 0.7347 0.7803 -0.0235 -0.0993 0.0063  334 SER A CB  
285  O OG  . SER A 38  ? 0.8796 0.8916 0.9156 -0.0084 -0.1059 0.0105  334 SER A OG  
286  N N   . ILE A 39  ? 0.4869 0.5212 0.5486 0.0190  -0.0930 0.0072  335 ILE A N   
287  C CA  . ILE A 39  ? 0.6297 0.7085 0.7048 0.0346  -0.0956 0.0082  335 ILE A CA  
288  C C   . ILE A 39  ? 0.6662 0.7540 0.7616 0.0204  -0.0902 0.0049  335 ILE A C   
289  O O   . ILE A 39  ? 0.6167 0.6663 0.7054 0.0162  -0.0823 0.0013  335 ILE A O   
290  C CB  . ILE A 39  ? 0.6268 0.6825 0.6738 0.0686  -0.0936 0.0091  335 ILE A CB  
291  C CG1 . ILE A 39  ? 0.6287 0.6687 0.6484 0.0854  -0.0995 0.0131  335 ILE A CG1 
292  C CG2 . ILE A 39  ? 0.5926 0.7013 0.6524 0.0906  -0.0956 0.0095  335 ILE A CG2 
293  C CD1 . ILE A 39  ? 0.7222 0.8295 0.7608 0.0864  -0.1110 0.0166  335 ILE A CD1 
294  N N   . MET A 40  ? 0.6423 0.7831 0.7601 0.0105  -0.0945 0.0062  336 MET A N   
295  C CA  . MET A 40  ? 0.5817 0.7280 0.7147 -0.0069 -0.0904 0.0040  336 MET A CA  
296  C C   . MET A 40  ? 0.7084 0.8481 0.8419 0.0099  -0.0831 0.0012  336 MET A C   
297  O O   . MET A 40  ? 0.6169 0.7275 0.7503 0.0014  -0.0770 -0.0025 336 MET A O   
298  C CB  . MET A 40  ? 0.6961 0.8982 0.8446 -0.0256 -0.0968 0.0071  336 MET A CB  
299  C CG  . MET A 40  ? 0.8049 1.0165 0.9640 -0.0402 -0.0928 0.0060  336 MET A CG  
300  S SD  . MET A 40  ? 0.8802 1.0589 1.0259 -0.0755 -0.0957 0.0062  336 MET A SD  
301  C CE  . MET A 40  ? 0.7380 0.9714 0.8830 -0.1017 -0.1059 0.0112  336 MET A CE  
302  N N   . LEU A 41  ? 0.7443 0.9132 0.8755 0.0357  -0.0840 0.0024  337 LEU A N   
303  C CA  . LEU A 41  ? 0.9455 1.1056 1.0697 0.0554  -0.0776 -0.0007 337 LEU A CA  
304  C C   . LEU A 41  ? 1.1327 1.2580 1.2222 0.0892  -0.0770 -0.0009 337 LEU A C   
305  O O   . LEU A 41  ? 1.2425 1.3996 1.3247 0.1207  -0.0787 0.0002  337 LEU A O   
306  C CB  . LEU A 41  ? 1.0057 1.2340 1.1517 0.0596  -0.0782 0.0006  337 LEU A CB  
307  C CG  . LEU A 41  ? 0.9777 1.2503 1.1494 0.0255  -0.0812 0.0031  337 LEU A CG  
308  C CD1 . LEU A 41  ? 0.9159 1.2697 1.1048 0.0320  -0.0822 0.0056  337 LEU A CD1 
309  C CD2 . LEU A 41  ? 0.9401 1.1749 1.1139 0.0034  -0.0761 0.0002  337 LEU A CD2 
310  N N   . PRO A 42  ? 1.2319 1.2913 1.2941 0.0848  -0.0744 -0.0021 338 PRO A N   
311  C CA  . PRO A 42  ? 1.3088 1.3210 1.3255 0.1144  -0.0745 -0.0013 338 PRO A CA  
312  C C   . PRO A 42  ? 1.4507 1.4432 1.4400 0.1434  -0.0703 -0.0044 338 PRO A C   
313  O O   . PRO A 42  ? 1.3751 1.3715 1.3767 0.1332  -0.0653 -0.0084 338 PRO A O   
314  C CB  . PRO A 42  ? 1.2819 1.2259 1.2746 0.0918  -0.0698 -0.0029 338 PRO A CB  
315  C CG  . PRO A 42  ? 1.2260 1.1811 1.2492 0.0597  -0.0653 -0.0066 338 PRO A CG  
316  C CD  . PRO A 42  ? 1.1658 1.1898 1.2319 0.0538  -0.0703 -0.0047 338 PRO A CD  
317  N N   . SER A 43  ? 1.6011 1.5700 1.5480 0.1830  -0.0728 -0.0026 339 SER A N   
318  C CA  . SER A 43  ? 1.7254 1.6682 1.6329 0.2208  -0.0696 -0.0056 339 SER A CA  
319  C C   . SER A 43  ? 1.7627 1.6361 1.6446 0.2006  -0.0612 -0.0118 339 SER A C   
320  O O   . SER A 43  ? 1.7941 1.6605 1.6595 0.2200  -0.0576 -0.0158 339 SER A O   
321  C CB  . SER A 43  ? 1.8144 1.7080 1.6593 0.2654  -0.0732 -0.0029 339 SER A CB  
322  O OG  . SER A 43  ? 1.9027 1.7532 1.6948 0.3060  -0.0698 -0.0065 339 SER A OG  
323  N N   . GLN A 44  ? 1.7565 1.5855 1.6356 0.1610  -0.0581 -0.0128 340 GLN A N   
324  C CA  . GLN A 44  ? 1.6976 1.4703 1.5538 0.1351  -0.0510 -0.0188 340 GLN A CA  
325  C C   . GLN A 44  ? 1.5803 1.4093 1.4916 0.1109  -0.0488 -0.0221 340 GLN A C   
326  O O   . GLN A 44  ? 1.5871 1.3966 1.4839 0.1103  -0.0447 -0.0274 340 GLN A O   
327  C CB  . GLN A 44  ? 1.6729 1.3899 1.5047 0.1015  -0.0483 -0.0185 340 GLN A CB  
328  C CG  . GLN A 44  ? 1.6924 1.3103 1.4392 0.1148  -0.0466 -0.0179 340 GLN A CG  
329  C CD  . GLN A 44  ? 1.7748 1.3889 1.4995 0.1528  -0.0530 -0.0114 340 GLN A CD  
330  O OE1 . GLN A 44  ? 1.8133 1.5051 1.5837 0.1759  -0.0590 -0.0082 340 GLN A OE1 
331  N NE2 . GLN A 44  ? 1.7710 1.2951 1.4216 0.1572  -0.0520 -0.0092 340 GLN A NE2 
332  N N   . HIS A 45  ? 1.5566 1.4494 1.5245 0.0913  -0.0519 -0.0191 341 HIS A N   
333  C CA  . HIS A 45  ? 1.5496 1.4859 1.5621 0.0672  -0.0503 -0.0214 341 HIS A CA  
334  C C   . HIS A 45  ? 1.5669 1.5462 1.5955 0.0849  -0.0497 -0.0225 341 HIS A C   
335  O O   . HIS A 45  ? 1.4768 1.4938 1.5400 0.0668  -0.0491 -0.0231 341 HIS A O   
336  C CB  . HIS A 45  ? 1.4656 1.4458 1.5188 0.0475  -0.0545 -0.0175 341 HIS A CB  
337  C CG  . HIS A 45  ? 1.3457 1.3386 1.4246 0.0198  -0.0523 -0.0202 341 HIS A CG  
338  N ND1 . HIS A 45  ? 1.3129 1.3003 1.3916 0.0134  -0.0481 -0.0251 341 HIS A ND1 
339  C CD2 . HIS A 45  ? 1.2949 1.3039 1.3950 0.0008  -0.0543 -0.0189 341 HIS A CD2 
340  C CE1 . HIS A 45  ? 1.2436 1.2477 1.3444 -0.0067 -0.0479 -0.0263 341 HIS A CE1 
341  N NE2 . HIS A 45  ? 1.2570 1.2718 1.3689 -0.0130 -0.0514 -0.0227 341 HIS A NE2 
342  N N   . THR A 46  ? 1.6559 1.6303 1.6571 0.1209  -0.0496 -0.0228 342 THR A N   
343  C CA  . THR A 46  ? 1.6422 1.6667 1.6587 0.1400  -0.0482 -0.0236 342 THR A CA  
344  C C   . THR A 46  ? 1.6788 1.6462 1.6460 0.1617  -0.0430 -0.0299 342 THR A C   
345  O O   . THR A 46  ? 1.8137 1.7086 1.7245 0.1785  -0.0424 -0.0316 342 THR A O   
346  C CB  . THR A 46  ? 1.6338 1.7254 1.6644 0.1694  -0.0530 -0.0184 342 THR A CB  
347  O OG1 . THR A 46  ? 1.5841 1.7165 1.6501 0.1452  -0.0587 -0.0131 342 THR A OG1 
348  C CG2 . THR A 46  ? 1.6059 1.7681 1.6597 0.1832  -0.0507 -0.0187 342 THR A CG2 
349  N N   . ARG A 47  ? 1.5088 1.5016 1.4903 0.1601  -0.0393 -0.0333 343 ARG A N   
350  C CA  . ARG A 47  ? 1.4933 1.4358 1.4259 0.1831  -0.0346 -0.0398 343 ARG A CA  
351  C C   . ARG A 47  ? 1.4925 1.4836 1.4200 0.2304  -0.0336 -0.0391 343 ARG A C   
352  O O   . ARG A 47  ? 1.4489 1.5178 1.4192 0.2286  -0.0322 -0.0375 343 ARG A O   
353  C CB  . ARG A 47  ? 1.3655 1.3009 1.3099 0.1535  -0.0308 -0.0451 343 ARG A CB  
354  C CG  . ARG A 47  ? 1.3912 1.2687 1.3207 0.1152  -0.0306 -0.0485 343 ARG A CG  
355  C CD  . ARG A 47  ? 1.5341 1.3331 1.4051 0.1225  -0.0311 -0.0490 343 ARG A CD  
356  N NE  . ARG A 47  ? 1.6350 1.3787 1.4818 0.0831  -0.0294 -0.0533 343 ARG A NE  
357  C CZ  . ARG A 47  ? 1.7946 1.4772 1.5993 0.0716  -0.0295 -0.0526 343 ARG A CZ  
358  N NH1 . ARG A 47  ? 1.8739 1.5362 1.6543 0.1002  -0.0317 -0.0475 343 ARG A NH1 
359  N NH2 . ARG A 47  ? 1.8601 1.5065 1.6458 0.0303  -0.0273 -0.0567 343 ARG A NH2 
360  N N   . VAL A 52  ? 1.8198 1.4302 1.3504 0.4273  -0.0143 -0.0757 348 VAL A N   
361  C CA  . VAL A 52  ? 1.9997 1.5552 1.4927 0.4148  -0.0096 -0.0850 348 VAL A CA  
362  C C   . VAL A 52  ? 2.2131 1.6162 1.6109 0.3883  -0.0105 -0.0911 348 VAL A C   
363  O O   . VAL A 52  ? 2.2919 1.6076 1.6146 0.4121  -0.0127 -0.0900 348 VAL A O   
364  C CB  . VAL A 52  ? 2.0319 1.6088 1.4910 0.4815  -0.0048 -0.0896 348 VAL A CB  
365  C CG1 . VAL A 52  ? 2.0750 1.6082 1.4601 0.5535  -0.0064 -0.0886 348 VAL A CG1 
366  C CG2 . VAL A 52  ? 1.9942 1.4904 1.3934 0.4732  -0.0003 -0.1005 348 VAL A CG2 
367  N N   . ALA A 53  ? 2.2258 1.5993 1.6240 0.3368  -0.0090 -0.0973 349 ALA A N   
368  C CA  . ALA A 53  ? 2.2555 1.5038 1.5757 0.2935  -0.0099 -0.1031 349 ALA A CA  
369  C C   . ALA A 53  ? 2.3742 1.4923 1.5681 0.3279  -0.0076 -0.1126 349 ALA A C   
370  O O   . ALA A 53  ? 2.4470 1.5749 1.6154 0.3913  -0.0049 -0.1150 349 ALA A O   
371  C CB  . ALA A 53  ? 2.1300 1.4159 1.5062 0.2243  -0.0102 -0.1060 349 ALA A CB  
372  N N   . THR A 54  ? 2.4000 1.3932 1.5079 0.2850  -0.0086 -0.1180 350 THR A N   
373  C CA  . THR A 54  ? 2.3939 1.2923 1.4018 0.2894  -0.0087 -0.1164 350 THR A CA  
374  C C   . THR A 54  ? 2.3457 1.1940 1.3304 0.2135  -0.0089 -0.1231 350 THR A C   
375  O O   . THR A 54  ? 2.2542 1.1229 1.2803 0.1554  -0.0101 -0.1252 350 THR A O   
376  C CB  . THR A 54  ? 2.4482 1.2589 1.3640 0.3121  -0.0116 -0.1043 350 THR A CB  
377  O OG1 . THR A 54  ? 2.4530 1.2084 1.3451 0.2497  -0.0131 -0.1007 350 THR A OG1 
378  C CG2 . THR A 54  ? 2.3935 1.2668 1.3394 0.3786  -0.0132 -0.0969 350 THR A CG2 
379  N N   . LYS A 55  ? 2.4510 1.2396 1.3685 0.2141  -0.0083 -0.1255 351 LYS A N   
380  C CA  . LYS A 55  ? 2.5192 1.2684 1.4124 0.1425  -0.0091 -0.1310 351 LYS A CA  
381  C C   . LYS A 55  ? 2.5631 1.2463 1.4063 0.0860  -0.0106 -0.1230 351 LYS A C   
382  O O   . LYS A 55  ? 2.5031 1.1975 1.3628 0.0155  -0.0112 -0.1264 351 LYS A O   
383  C CB  . LYS A 55  ? 2.6097 1.2976 1.4290 0.1595  -0.0084 -0.1334 351 LYS A CB  
384  C CG  . LYS A 55  ? 2.6983 1.3063 1.4226 0.2216  -0.0088 -0.1232 351 LYS A CG  
385  C CD  . LYS A 55  ? 2.7666 1.3088 1.4128 0.2376  -0.0085 -0.1253 351 LYS A CD  
386  C CE  . LYS A 55  ? 2.8703 1.3207 1.4064 0.2962  -0.0103 -0.1140 351 LYS A CE  
387  N NZ  . LYS A 55  ? 2.9185 1.2914 1.3653 0.3138  -0.0105 -0.1146 351 LYS A NZ  
388  N N   . ASP A 56  ? 2.6611 1.2844 1.4440 0.1158  -0.0112 -0.1118 352 ASP A N   
389  C CA  . ASP A 56  ? 2.7539 1.3139 1.4828 0.0642  -0.0115 -0.1035 352 ASP A CA  
390  C C   . ASP A 56  ? 2.5839 1.2233 1.4036 0.0246  -0.0115 -0.1042 352 ASP A C   
391  O O   . ASP A 56  ? 2.6240 1.2653 1.4464 -0.0452 -0.0106 -0.1035 352 ASP A O   
392  C CB  . ASP A 56  ? 2.9431 1.4125 1.5729 0.1114  -0.0127 -0.0919 352 ASP A CB  
393  C CG  . ASP A 56  ? 2.9839 1.4686 1.6083 0.2010  -0.0140 -0.0914 352 ASP A CG  
394  O OD1 . ASP A 56  ? 3.0382 1.4778 1.6019 0.2493  -0.0161 -0.0826 352 ASP A OD1 
395  O OD2 . ASP A 56  ? 2.8938 1.4425 1.5742 0.2236  -0.0128 -0.0999 352 ASP A OD2 
396  N N   . GLN A 57  ? 2.3547 1.0659 1.2490 0.0689  -0.0122 -0.1049 353 GLN A N   
397  C CA  . GLN A 57  ? 2.1262 0.9124 1.1068 0.0359  -0.0127 -0.1055 353 GLN A CA  
398  C C   . GLN A 57  ? 1.9641 0.8210 1.0151 -0.0211 -0.0129 -0.1156 353 GLN A C   
399  O O   . GLN A 57  ? 1.8341 0.7380 0.9340 -0.0711 -0.0134 -0.1147 353 GLN A O   
400  C CB  . GLN A 57  ? 2.0779 0.9298 1.1233 0.0978  -0.0137 -0.1049 353 GLN A CB  
401  C CG  . GLN A 57  ? 2.2409 1.0484 1.2302 0.1591  -0.0149 -0.0946 353 GLN A CG  
402  C CD  . GLN A 57  ? 2.2287 1.1146 1.2741 0.2327  -0.0154 -0.0954 353 GLN A CD  
403  O OE1 . GLN A 57  ? 2.1375 1.0847 1.2340 0.2470  -0.0136 -0.1038 353 GLN A OE1 
404  N NE2 . GLN A 57  ? 2.2135 1.1063 1.2503 0.2789  -0.0179 -0.0863 353 GLN A NE2 
405  N N   . LEU A 58  ? 1.8530 0.7226 0.9082 -0.0134 -0.0129 -0.1247 354 LEU A N   
406  C CA  . LEU A 58  ? 1.7961 0.7532 0.9313 -0.0507 -0.0145 -0.1346 354 LEU A CA  
407  C C   . LEU A 58  ? 1.8893 0.8535 1.0198 -0.1309 -0.0155 -0.1352 354 LEU A C   
408  O O   . LEU A 58  ? 1.7893 0.8458 0.9995 -0.1688 -0.0176 -0.1382 354 LEU A O   
409  C CB  . LEU A 58  ? 1.8152 0.7955 0.9591 -0.0160 -0.0138 -0.1410 354 LEU A CB  
410  C CG  . LEU A 58  ? 1.6884 0.8137 0.9560 0.0155  -0.0134 -0.1352 354 LEU A CG  
411  C CD1 . LEU A 58  ? 1.6702 0.8221 0.9584 0.0832  -0.0116 -0.1270 354 LEU A CD1 
412  C CD2 . LEU A 58  ? 1.6367 0.7797 0.9055 0.0217  -0.0128 -0.1434 354 LEU A CD2 
413  N N   . PHE A 59  ? 2.0477 0.9306 1.0904 -0.1560 -0.0138 -0.1299 355 PHE A N   
414  C CA  . PHE A 59  ? 2.0854 0.9956 1.1306 -0.2304 -0.0139 -0.1304 355 PHE A CA  
415  C C   . PHE A 59  ? 2.0741 1.0318 1.1549 -0.2758 -0.0125 -0.1237 355 PHE A C   
416  O O   . PHE A 59  ? 2.0308 1.0814 1.1770 -0.3214 -0.0137 -0.1271 355 PHE A O   
417  C CB  . PHE A 59  ? 2.1919 1.0048 1.1296 -0.2530 -0.0121 -0.1267 355 PHE A CB  
418  C CG  . PHE A 59  ? 2.3184 1.1747 1.2641 -0.3269 -0.0120 -0.1283 355 PHE A CG  
419  C CD1 . PHE A 59  ? 2.3254 1.2539 1.3251 -0.3421 -0.0155 -0.1384 355 PHE A CD1 
420  C CD2 . PHE A 59  ? 2.3828 1.2174 1.2844 -0.3800 -0.0083 -0.1198 355 PHE A CD2 
421  C CE1 . PHE A 59  ? 2.2898 1.2723 1.3019 -0.4059 -0.0158 -0.1395 355 PHE A CE1 
422  C CE2 . PHE A 59  ? 2.3866 1.2755 1.2986 -0.4458 -0.0075 -0.1212 355 PHE A CE2 
423  C CZ  . PHE A 59  ? 2.3475 1.3127 1.3164 -0.4572 -0.0115 -0.1308 355 PHE A CZ  
424  N N   . PRO A 60  ? 2.1243 1.0271 1.1628 -0.2650 -0.0098 -0.1139 356 PRO A N   
425  C CA  . PRO A 60  ? 1.9773 0.9365 1.0574 -0.3062 -0.0079 -0.1084 356 PRO A CA  
426  C C   . PRO A 60  ? 1.7854 0.8647 0.9833 -0.3058 -0.0108 -0.1138 356 PRO A C   
427  O O   . PRO A 60  ? 1.7448 0.9094 0.9955 -0.3529 -0.0102 -0.1137 356 PRO A O   
428  C CB  . PRO A 60  ? 2.1189 0.9983 1.1406 -0.2744 -0.0059 -0.0985 356 PRO A CB  
429  C CG  . PRO A 60  ? 2.1575 0.9724 1.1396 -0.2045 -0.0080 -0.0999 356 PRO A CG  
430  C CD  . PRO A 60  ? 2.2090 1.0065 1.1641 -0.2120 -0.0089 -0.1071 356 PRO A CD  
431  N N   . LEU A 61  ? 1.7061 0.7966 0.9422 -0.2516 -0.0138 -0.1183 357 LEU A N   
432  C CA  . LEU A 61  ? 1.5205 0.7351 0.8714 -0.2439 -0.0163 -0.1190 357 LEU A CA  
433  C C   . LEU A 61  ? 1.5541 0.8485 0.9525 -0.2774 -0.0189 -0.1262 357 LEU A C   
434  O O   . LEU A 61  ? 1.4695 0.8747 0.9518 -0.2968 -0.0200 -0.1239 357 LEU A O   
435  C CB  . LEU A 61  ? 1.3713 0.6124 0.7640 -0.1703 -0.0168 -0.1135 357 LEU A CB  
436  C CG  . LEU A 61  ? 1.4398 0.6188 0.7929 -0.1318 -0.0155 -0.1060 357 LEU A CG  
437  C CD1 . LEU A 61  ? 1.3918 0.5842 0.7618 -0.0597 -0.0161 -0.1030 357 LEU A CD1 
438  C CD2 . LEU A 61  ? 1.5900 0.8377 1.0077 -0.1481 -0.0154 -0.0976 357 LEU A CD2 
439  N N   . ALA A 62  ? 1.5456 0.7841 0.8874 -0.2808 -0.0202 -0.1353 358 ALA A N   
440  C CA  . ALA A 62  ? 1.4561 0.7642 0.8332 -0.3144 -0.0236 -0.1428 358 ALA A CA  
441  C C   . ALA A 62  ? 1.5409 0.8912 0.9180 -0.3772 -0.0221 -0.1393 358 ALA A C   
442  O O   . ALA A 62  ? 1.5003 0.9617 0.9500 -0.4022 -0.0247 -0.1411 358 ALA A O   
443  C CB  . ALA A 62  ? 1.5993 0.8367 0.9125 -0.2992 -0.0245 -0.1511 358 ALA A CB  
444  N N   . LYS A 63  ? 1.7428 1.0122 1.0381 -0.3984 -0.0171 -0.1325 359 LYS A N   
445  C CA  . LYS A 63  ? 1.8269 1.1344 1.1122 -0.4568 -0.0133 -0.1273 359 LYS A CA  
446  C C   . LYS A 63  ? 1.7254 1.1327 1.0881 -0.4695 -0.0121 -0.1233 359 LYS A C   
447  O O   . LYS A 63  ? 1.7813 1.2954 1.1988 -0.5004 -0.0124 -0.1245 359 LYS A O   
448  C CB  . LYS A 63  ? 1.9494 1.1384 1.1232 -0.4729 -0.0077 -0.1195 359 LYS A CB  
449  C CG  . LYS A 63  ? 1.9446 1.1653 1.0962 -0.5352 -0.0023 -0.1140 359 LYS A CG  
450  C CD  . LYS A 63  ? 2.0284 1.1233 1.0593 -0.5526 0.0030  -0.1059 359 LYS A CD  
451  C CE  . LYS A 63  ? 2.0708 1.1786 1.0532 -0.6203 0.0074  -0.1042 359 LYS A CE  
452  N NZ  . LYS A 63  ? 1.9939 1.2464 1.0620 -0.6562 0.0091  -0.1056 359 LYS A NZ  
453  N N   . GLU A 64  ? 1.5979 0.9730 0.9640 -0.4417 -0.0107 -0.1183 360 GLU A N   
454  C CA  . GLU A 64  ? 1.5544 1.0155 0.9894 -0.4493 -0.0094 -0.1142 360 GLU A CA  
455  C C   . GLU A 64  ? 1.3626 0.9493 0.8985 -0.4431 -0.0146 -0.1198 360 GLU A C   
456  O O   . GLU A 64  ? 1.2963 0.9841 0.8836 -0.4670 -0.0132 -0.1179 360 GLU A O   
457  C CB  . GLU A 64  ? 1.7118 1.1120 1.1354 -0.4115 -0.0086 -0.1091 360 GLU A CB  
458  C CG  . GLU A 64  ? 1.7145 1.1991 1.2161 -0.4077 -0.0087 -0.1059 360 GLU A CG  
459  C CD  . GLU A 64  ? 1.8343 1.2645 1.3323 -0.3610 -0.0096 -0.1015 360 GLU A CD  
460  O OE1 . GLU A 64  ? 1.9281 1.2484 1.3521 -0.3347 -0.0097 -0.1013 360 GLU A OE1 
461  O OE2 . GLU A 64  ? 1.7658 1.2754 1.3389 -0.3398 -0.0095 -0.0949 360 GLU A OE2 
462  N N   . PHE A 65  ? 1.3283 0.9110 0.8886 -0.4084 -0.0204 -0.1266 361 PHE A N   
463  C CA  . PHE A 65  ? 1.1636 0.8667 0.8169 -0.3925 -0.0246 -0.1277 361 PHE A CA  
464  C C   . PHE A 65  ? 1.2461 1.0154 0.9072 -0.4336 -0.0272 -0.1342 361 PHE A C   
465  O O   . PHE A 65  ? 1.1415 1.0232 0.8665 -0.4418 -0.0283 -0.1328 361 PHE A O   
466  C CB  . PHE A 65  ? 1.2258 0.9209 0.9055 -0.3328 -0.0266 -0.1254 361 PHE A CB  
467  C CG  . PHE A 65  ? 1.1456 0.9472 0.9042 -0.3164 -0.0308 -0.1255 361 PHE A CG  
468  C CD1 . PHE A 65  ? 1.1735 1.0596 1.0059 -0.2966 -0.0313 -0.1184 361 PHE A CD1 
469  C CD2 . PHE A 65  ? 1.2357 1.0456 0.9869 -0.3199 -0.0344 -0.1327 361 PHE A CD2 
470  C CE1 . PHE A 65  ? 1.1211 1.0918 1.0134 -0.2790 -0.0355 -0.1181 361 PHE A CE1 
471  C CE2 . PHE A 65  ? 1.1149 1.0164 0.9316 -0.3031 -0.0386 -0.1321 361 PHE A CE2 
472  C CZ  . PHE A 65  ? 0.9904 0.9695 0.8754 -0.2818 -0.0392 -0.1245 361 PHE A CZ  
473  N N   . LEU A 66  ? 1.2621 0.9679 0.8595 -0.4484 -0.0269 -0.1379 362 LEU A N   
474  C CA  . LEU A 66  ? 1.2229 0.9931 0.8274 -0.4793 -0.0285 -0.1410 362 LEU A CA  
475  C C   . LEU A 66  ? 1.2805 1.1139 0.8888 -0.5199 -0.0227 -0.1351 362 LEU A C   
476  O O   . LEU A 66  ? 1.3165 1.2524 0.9655 -0.5358 -0.0242 -0.1367 362 LEU A O   
477  C CB  . LEU A 66  ? 1.4580 1.1330 0.9817 -0.4898 -0.0284 -0.1452 362 LEU A CB  
478  C CG  . LEU A 66  ? 1.4988 1.1248 1.0144 -0.4511 -0.0337 -0.1534 362 LEU A CG  
479  C CD1 . LEU A 66  ? 1.5709 1.1020 0.9989 -0.4629 -0.0324 -0.1565 362 LEU A CD1 
480  C CD2 . LEU A 66  ? 1.3839 1.1199 0.9807 -0.4384 -0.0410 -0.1592 362 LEU A CD2 
481  N N   . ASP A 67  ? 1.3789 1.1534 0.9404 -0.5356 -0.0158 -0.1285 363 ASP A N   
482  C CA  . ASP A 67  ? 1.4464 1.2784 1.0035 -0.5764 -0.0092 -0.1235 363 ASP A CA  
483  C C   . ASP A 67  ? 1.2710 1.2309 0.9180 -0.5626 -0.0098 -0.1223 363 ASP A C   
484  O O   . ASP A 67  ? 1.2243 1.2802 0.8933 -0.5871 -0.0071 -0.1222 363 ASP A O   
485  C CB  . ASP A 67  ? 1.5543 1.2855 1.0344 -0.5936 -0.0021 -0.1166 363 ASP A CB  
486  C CG  . ASP A 67  ? 1.7564 1.3829 1.1329 -0.6245 0.0008  -0.1160 363 ASP A CG  
487  O OD1 . ASP A 67  ? 1.8810 1.5355 1.2235 -0.6737 0.0055  -0.1148 363 ASP A OD1 
488  O OD2 . ASP A 67  ? 1.8514 1.3677 1.1761 -0.5988 -0.0015 -0.1169 363 ASP A OD2 
489  N N   . GLN A 68  ? 1.0989 1.0626 0.7944 -0.5219 -0.0130 -0.1212 364 GLN A N   
490  C CA  . GLN A 68  ? 1.0422 1.1213 0.8171 -0.5046 -0.0138 -0.1196 364 GLN A CA  
491  C C   . GLN A 68  ? 1.0854 1.2584 0.9196 -0.4844 -0.0209 -0.1245 364 GLN A C   
492  O O   . GLN A 68  ? 1.0599 1.3414 0.9425 -0.4791 -0.0205 -0.1237 364 GLN A O   
493  C CB  . GLN A 68  ? 1.0428 1.0930 0.8441 -0.4716 -0.0145 -0.1159 364 GLN A CB  
494  C CG  . GLN A 68  ? 1.1080 1.1066 0.9203 -0.4354 -0.0214 -0.1196 364 GLN A CG  
495  C CD  . GLN A 68  ? 1.1560 1.0949 0.9674 -0.4031 -0.0192 -0.1128 364 GLN A CD  
496  O OE1 . GLN A 68  ? 1.0687 1.0506 0.9385 -0.3575 -0.0207 -0.1069 364 GLN A OE1 
497  N NE2 . GLN A 68  ? 1.1667 1.0020 0.9068 -0.4200 -0.0153 -0.1114 364 GLN A NE2 
498  N N   . TYR A 69  ? 1.0957 1.2281 0.9218 -0.4707 -0.0273 -0.1298 365 TYR A N   
499  C CA  . TYR A 69  ? 1.1195 1.3361 0.9930 -0.4536 -0.0343 -0.1342 365 TYR A CA  
500  C C   . TYR A 69  ? 1.1547 1.4376 1.0172 -0.4862 -0.0321 -0.1356 365 TYR A C   
501  O O   . TYR A 69  ? 1.0763 1.4669 0.9874 -0.4727 -0.0344 -0.1358 365 TYR A O   
502  C CB  . TYR A 69  ? 1.1095 1.2646 0.9683 -0.4360 -0.0410 -0.1403 365 TYR A CB  
503  C CG  . TYR A 69  ? 1.0780 1.3101 0.9702 -0.4260 -0.0480 -0.1448 365 TYR A CG  
504  C CD1 . TYR A 69  ? 0.9897 1.3233 0.9487 -0.3949 -0.0523 -0.1427 365 TYR A CD1 
505  C CD2 . TYR A 69  ? 1.1269 1.3266 0.9780 -0.4453 -0.0503 -0.1506 365 TYR A CD2 
506  C CE1 . TYR A 69  ? 0.9247 1.3247 0.9082 -0.3814 -0.0590 -0.1458 365 TYR A CE1 
507  C CE2 . TYR A 69  ? 1.0074 1.2782 0.8874 -0.4356 -0.0570 -0.1543 365 TYR A CE2 
508  C CZ  . TYR A 69  ? 0.9880 1.3588 0.9340 -0.4029 -0.0614 -0.1517 365 TYR A CZ  
509  O OH  . TYR A 69  ? 1.0400 1.4773 1.0094 -0.3886 -0.0683 -0.1545 365 TYR A OH  
510  N N   . TYR A 70  ? 1.3172 1.5357 1.1109 -0.5276 -0.0275 -0.1364 366 TYR A N   
511  C CA  . TYR A 70  ? 1.3567 1.6401 1.1354 -0.5644 -0.0247 -0.1377 366 TYR A CA  
512  C C   . TYR A 70  ? 1.3982 1.7624 1.1925 -0.5816 -0.0173 -0.1335 366 TYR A C   
513  O O   . TYR A 70  ? 1.5351 2.0023 1.3494 -0.5935 -0.0163 -0.1351 366 TYR A O   
514  C CB  . TYR A 70  ? 1.4231 1.6092 1.1161 -0.6062 -0.0217 -0.1392 366 TYR A CB  
515  C CG  . TYR A 70  ? 1.4082 1.5567 1.0908 -0.5936 -0.0294 -0.1457 366 TYR A CG  
516  C CD1 . TYR A 70  ? 1.3753 1.4085 1.0224 -0.5726 -0.0321 -0.1480 366 TYR A CD1 
517  C CD2 . TYR A 70  ? 1.3470 1.5796 1.0551 -0.5989 -0.0339 -0.1500 366 TYR A CD2 
518  C CE1 . TYR A 70  ? 1.3701 1.3711 1.0052 -0.5594 -0.0388 -0.1549 366 TYR A CE1 
519  C CE2 . TYR A 70  ? 1.4086 1.6087 1.1067 -0.5873 -0.0412 -0.1562 366 TYR A CE2 
520  C CZ  . TYR A 70  ? 1.4099 1.4941 1.0712 -0.5683 -0.0435 -0.1590 366 TYR A CZ  
521  O OH  . TYR A 70  ? 1.3730 1.4270 1.0212 -0.5557 -0.0503 -0.1662 366 TYR A OH  
522  N N   . SER A 71  ? 1.2591 1.5813 1.0429 -0.5815 -0.0121 -0.1285 367 SER A N   
523  C CA  . SER A 71  ? 1.3539 1.7556 1.1568 -0.5917 -0.0055 -0.1251 367 SER A CA  
524  C C   . SER A 71  ? 1.3311 1.8407 1.2142 -0.5454 -0.0095 -0.1254 367 SER A C   
525  O O   . SER A 71  ? 1.4370 2.0307 1.3396 -0.5479 -0.0046 -0.1240 367 SER A O   
526  C CB  . SER A 71  ? 1.2927 1.6127 1.0590 -0.6025 0.0007  -0.1196 367 SER A CB  
527  O OG  . SER A 71  ? 1.2822 1.6759 1.0593 -0.6172 0.0076  -0.1169 367 SER A OG  
528  N N   . SER A 72  ? 1.1532 1.6597 1.0768 -0.5024 -0.0181 -0.1272 368 SER A N   
529  C CA  . SER A 72  ? 1.0923 1.6900 1.0818 -0.4551 -0.0224 -0.1267 368 SER A CA  
530  C C   . SER A 72  ? 1.1659 1.8574 1.1770 -0.4452 -0.0266 -0.1307 368 SER A C   
531  O O   . SER A 72  ? 1.2531 2.0375 1.3033 -0.4137 -0.0274 -0.1302 368 SER A O   
532  C CB  . SER A 72  ? 1.0683 1.6151 1.0866 -0.4129 -0.0294 -0.1256 368 SER A CB  
533  O OG  . SER A 72  ? 0.9775 1.5165 1.0036 -0.3968 -0.0377 -0.1296 368 SER A OG  
534  N N   . ILE A 73  ? 1.1402 1.8063 1.1230 -0.4683 -0.0295 -0.1347 369 ILE A N   
535  C CA  . ILE A 73  ? 1.1611 1.9159 1.1548 -0.4689 -0.0322 -0.1385 369 ILE A CA  
536  C C   . ILE A 73  ? 1.1991 2.0014 1.1569 -0.5205 -0.0237 -0.1395 369 ILE A C   
537  O O   . ILE A 73  ? 1.1949 2.0582 1.1469 -0.5355 -0.0247 -0.1432 369 ILE A O   
538  C CB  . ILE A 73  ? 1.1647 1.8762 1.1487 -0.4654 -0.0404 -0.1428 369 ILE A CB  
539  C CG1 . ILE A 73  ? 1.2046 1.8044 1.1255 -0.5101 -0.0377 -0.1443 369 ILE A CG1 
540  C CG2 . ILE A 73  ? 1.1113 1.8005 1.1340 -0.4123 -0.0492 -0.1421 369 ILE A CG2 
541  C CD1 . ILE A 73  ? 1.1843 1.7220 1.0926 -0.4999 -0.0460 -0.1491 369 ILE A CD1 
542  N N   . LYS A 74  ? 1.2191 1.9941 1.1498 -0.5492 -0.0154 -0.1362 370 LYS A N   
543  C CA  . LYS A 74  ? 1.3509 2.1610 1.2382 -0.6040 -0.0065 -0.1365 370 LYS A CA  
544  C C   . LYS A 74  ? 1.4936 2.2720 1.3305 -0.6491 -0.0068 -0.1397 370 LYS A C   
545  O O   . LYS A 74  ? 1.5692 2.4269 1.3906 -0.6820 -0.0031 -0.1421 370 LYS A O   
546  C CB  . LYS A 74  ? 1.3049 2.2578 1.2264 -0.5913 -0.0035 -0.1378 370 LYS A CB  
547  C CG  . LYS A 74  ? 1.3012 2.2759 1.2336 -0.5833 0.0025  -0.1343 370 LYS A CG  
548  C CD  . LYS A 74  ? 1.2234 2.1500 1.1972 -0.5291 -0.0023 -0.1309 370 LYS A CD  
549  C CE  . LYS A 74  ? 1.1650 2.1043 1.1452 -0.5247 0.0040  -0.1273 370 LYS A CE  
550  N NZ  . LYS A 74  ? 0.9459 1.8423 0.9647 -0.4746 -0.0002 -0.1237 370 LYS A NZ  
551  N N   . ARG A 75  ? 1.4294 2.0934 1.2396 -0.6488 -0.0114 -0.1401 371 ARG A N   
552  C CA  . ARG A 75  ? 1.4755 2.0728 1.2208 -0.6945 -0.0107 -0.1423 371 ARG A CA  
553  C C   . ARG A 75  ? 1.5789 2.0277 1.2602 -0.7129 -0.0075 -0.1390 371 ARG A C   
554  O O   . ARG A 75  ? 1.5491 1.8994 1.1946 -0.7117 -0.0117 -0.1409 371 ARG A O   
555  C CB  . ARG A 75  ? 1.3458 1.9494 1.1119 -0.6717 -0.0203 -0.1475 371 ARG A CB  
556  C CG  . ARG A 75  ? 1.3610 2.1078 1.1777 -0.6555 -0.0231 -0.1505 371 ARG A CG  
557  C CD  . ARG A 75  ? 1.3834 2.1544 1.2594 -0.5938 -0.0337 -0.1525 371 ARG A CD  
558  N NE  . ARG A 75  ? 1.4348 2.2216 1.3064 -0.5964 -0.0405 -0.1575 371 ARG A NE  
559  C CZ  . ARG A 75  ? 1.5478 2.2363 1.3820 -0.6086 -0.0450 -0.1605 371 ARG A CZ  
560  N NH1 . ARG A 75  ? 1.5506 2.2608 1.3822 -0.6103 -0.0515 -0.1654 371 ARG A NH1 
561  N NH2 . ARG A 75  ? 1.6135 2.1804 1.4092 -0.6169 -0.0429 -0.1589 371 ARG A NH2 
562  N N   . PHE A 76  ? 1.6852 2.1187 1.3491 -0.7267 -0.0002 -0.1341 372 PHE A N   
563  C CA  . PHE A 76  ? 1.8021 2.0986 1.4017 -0.7404 0.0036  -0.1298 372 PHE A CA  
564  C C   . PHE A 76  ? 1.9554 2.1800 1.4585 -0.8005 0.0088  -0.1290 372 PHE A C   
565  O O   . PHE A 76  ? 2.0191 2.3135 1.5010 -0.8457 0.0143  -0.1292 372 PHE A O   
566  C CB  . PHE A 76  ? 1.8260 2.1416 1.4404 -0.7357 0.0095  -0.1249 372 PHE A CB  
567  C CG  . PHE A 76  ? 1.8800 2.0629 1.4222 -0.7525 0.0144  -0.1196 372 PHE A CG  
568  C CD1 . PHE A 76  ? 1.9061 1.9553 1.3988 -0.7412 0.0112  -0.1192 372 PHE A CD1 
569  C CD2 . PHE A 76  ? 1.9274 2.1210 1.4482 -0.7760 0.0220  -0.1152 372 PHE A CD2 
570  C CE1 . PHE A 76  ? 1.9446 1.8716 1.3649 -0.7506 0.0155  -0.1138 372 PHE A CE1 
571  C CE2 . PHE A 76  ? 2.0177 2.0888 1.4679 -0.7890 0.0262  -0.1099 372 PHE A CE2 
572  C CZ  . PHE A 76  ? 2.0348 1.9715 1.4337 -0.7746 0.0229  -0.1088 372 PHE A CZ  
573  N N   . GLY A 77  ? 1.9860 2.0706 1.4256 -0.8002 0.0072  -0.1282 373 GLY A N   
574  C CA  . GLY A 77  ? 2.1145 2.1050 1.4482 -0.8529 0.0122  -0.1260 373 GLY A CA  
575  C C   . GLY A 77  ? 2.1214 2.1514 1.4351 -0.8876 0.0106  -0.1304 373 GLY A C   
576  O O   . GLY A 77  ? 2.2406 2.1923 1.4601 -0.9360 0.0148  -0.1284 373 GLY A O   
577  N N   . SER A 78  ? 1.9377 2.0828 1.3315 -0.8643 0.0046  -0.1359 374 SER A N   
578  C CA  . SER A 78  ? 1.8671 2.0597 1.2471 -0.8951 0.0027  -0.1403 374 SER A CA  
579  C C   . SER A 78  ? 1.8008 1.8705 1.1270 -0.8900 -0.0028 -0.1431 374 SER A C   
580  O O   . SER A 78  ? 1.6950 1.6447 0.9906 -0.8620 -0.0044 -0.1416 374 SER A O   
581  C CB  . SER A 78  ? 1.7712 2.1172 1.2499 -0.8632 -0.0030 -0.1451 374 SER A CB  
582  O OG  . SER A 78  ? 1.6769 2.0075 1.2137 -0.8016 -0.0122 -0.1481 374 SER A OG  
583  N N   . LYS A 79  ? 1.7418 1.8439 1.0531 -0.9164 -0.0055 -0.1474 375 LYS A N   
584  C CA  . LYS A 79  ? 1.7828 1.7784 1.0448 -0.9103 -0.0112 -0.1512 375 LYS A CA  
585  C C   . LYS A 79  ? 1.7046 1.6940 1.0328 -0.8419 -0.0209 -0.1564 375 LYS A C   
586  O O   . LYS A 79  ? 1.7109 1.5781 0.9963 -0.8179 -0.0237 -0.1579 375 LYS A O   
587  C CB  . LYS A 79  ? 1.8069 1.8537 1.0469 -0.9533 -0.0126 -0.1551 375 LYS A CB  
588  C CG  . LYS A 79  ? 1.9156 1.8485 1.0927 -0.9538 -0.0180 -0.1592 375 LYS A CG  
589  C CD  . LYS A 79  ? 2.1273 1.9420 1.1784 -1.0137 -0.0108 -0.1541 375 LYS A CD  
590  C CE  . LYS A 79  ? 1.9569 1.6775 0.9438 -1.0202 -0.0160 -0.1588 375 LYS A CE  
591  N NZ  . LYS A 79  ? 1.9370 1.5479 0.9184 -0.9585 -0.0220 -0.1622 375 LYS A NZ  
592  N N   . ALA A 80  ? 1.6613 1.7804 1.0880 -0.8084 -0.0258 -0.1591 376 ALA A N   
593  C CA  . ALA A 80  ? 1.6391 1.7566 1.1257 -0.7463 -0.0347 -0.1634 376 ALA A CA  
594  C C   . ALA A 80  ? 1.6421 1.6667 1.1193 -0.7149 -0.0328 -0.1601 376 ALA A C   
595  O O   . ALA A 80  ? 1.5994 1.5567 1.0775 -0.6755 -0.0382 -0.1640 376 ALA A O   
596  C CB  . ALA A 80  ? 1.5710 1.8403 1.1557 -0.7163 -0.0393 -0.1646 376 ALA A CB  
597  N N   . HIS A 81  ? 1.6410 1.6609 1.1047 -0.7325 -0.0247 -0.1532 377 HIS A N   
598  C CA  . HIS A 81  ? 1.6297 1.5596 1.0784 -0.7053 -0.0224 -0.1494 377 HIS A CA  
599  C C   . HIS A 81  ? 1.6659 1.4363 1.0110 -0.7164 -0.0199 -0.1484 377 HIS A C   
600  O O   . HIS A 81  ? 1.6135 1.2984 0.9458 -0.6753 -0.0230 -0.1503 377 HIS A O   
601  C CB  . HIS A 81  ? 1.6621 1.6382 1.1258 -0.7204 -0.0149 -0.1425 377 HIS A CB  
602  C CG  . HIS A 81  ? 1.6991 1.5834 1.1421 -0.6968 -0.0121 -0.1378 377 HIS A CG  
603  N ND1 . HIS A 81  ? 1.7349 1.6214 1.1638 -0.7154 -0.0046 -0.1312 377 HIS A ND1 
604  C CD2 . HIS A 81  ? 1.7039 1.4947 1.1357 -0.6552 -0.0158 -0.1391 377 HIS A CD2 
605  C CE1 . HIS A 81  ? 1.7319 1.5284 1.1427 -0.6861 -0.0042 -0.1280 377 HIS A CE1 
606  N NE2 . HIS A 81  ? 1.7492 1.4881 1.1615 -0.6486 -0.0107 -0.1327 377 HIS A NE2 
607  N N   . MET A 82  ? 1.7779 1.5050 1.0420 -0.7702 -0.0139 -0.1450 378 MET A N   
608  C CA  . MET A 82  ? 1.9418 1.5089 1.0950 -0.7792 -0.0111 -0.1423 378 MET A CA  
609  C C   . MET A 82  ? 2.0387 1.5407 1.1725 -0.7487 -0.0181 -0.1496 378 MET A C   
610  O O   . MET A 82  ? 2.2359 1.6118 1.3087 -0.7192 -0.0180 -0.1489 378 MET A O   
611  C CB  . MET A 82  ? 2.1055 1.6448 1.1714 -0.8480 -0.0037 -0.1372 378 MET A CB  
612  C CG  . MET A 82  ? 2.2124 1.7823 1.2711 -0.8773 0.0045  -0.1298 378 MET A CG  
613  S SD  . MET A 82  ? 2.2979 1.7447 1.3188 -0.8371 0.0071  -0.1232 378 MET A SD  
614  C CE  . MET A 82  ? 2.2105 1.7971 1.3508 -0.8143 0.0077  -0.1226 378 MET A CE  
615  N N   . ASP A 83  ? 1.8001 1.3882 0.9830 -0.7517 -0.0242 -0.1567 379 ASP A N   
616  C CA  . ASP A 83  ? 1.8479 1.3810 1.0152 -0.7214 -0.0310 -0.1647 379 ASP A CA  
617  C C   . ASP A 83  ? 1.7960 1.3139 1.0122 -0.6558 -0.0354 -0.1686 379 ASP A C   
618  O O   . ASP A 83  ? 1.7798 1.1971 0.9487 -0.6225 -0.0370 -0.1726 379 ASP A O   
619  C CB  . ASP A 83  ? 1.8900 1.5265 1.1026 -0.7378 -0.0372 -0.1714 379 ASP A CB  
620  C CG  . ASP A 83  ? 1.9897 1.5778 1.1182 -0.7903 -0.0351 -0.1713 379 ASP A CG  
621  O OD1 . ASP A 83  ? 2.0387 1.7281 1.1910 -0.8309 -0.0350 -0.1715 379 ASP A OD1 
622  O OD2 . ASP A 83  ? 2.1548 1.6033 1.1892 -0.7898 -0.0333 -0.1707 379 ASP A OD2 
623  N N   . ARG A 84  ? 1.7198 1.3385 1.0275 -0.6355 -0.0370 -0.1676 380 ARG A N   
624  C CA  . ARG A 84  ? 1.6337 1.2423 0.9861 -0.5787 -0.0404 -0.1705 380 ARG A CA  
625  C C   . ARG A 84  ? 1.7366 1.2277 1.0310 -0.5585 -0.0347 -0.1654 380 ARG A C   
626  O O   . ARG A 84  ? 1.8364 1.2684 1.1240 -0.5107 -0.0362 -0.1691 380 ARG A O   
627  C CB  . ARG A 84  ? 1.5493 1.2923 1.0061 -0.5662 -0.0432 -0.1690 380 ARG A CB  
628  C CG  . ARG A 84  ? 1.3398 1.0824 0.8445 -0.5140 -0.0466 -0.1714 380 ARG A CG  
629  C CD  . ARG A 84  ? 1.3658 1.1692 0.9194 -0.4886 -0.0551 -0.1793 380 ARG A CD  
630  N NE  . ARG A 84  ? 1.2801 1.0599 0.8577 -0.4420 -0.0570 -0.1824 380 ARG A NE  
631  C CZ  . ARG A 84  ? 1.2936 0.9811 0.8221 -0.4138 -0.0565 -0.1889 380 ARG A CZ  
632  N NH1 . ARG A 84  ? 1.3218 0.9304 0.7765 -0.4251 -0.0551 -0.1924 380 ARG A NH1 
633  N NH2 . ARG A 84  ? 1.2115 0.9039 0.7835 -0.3535 -0.0521 -0.1798 380 ARG A NH2 
634  N N   . LEU A 85  ? 1.7686 1.2280 1.0182 -0.5927 -0.0277 -0.1567 381 LEU A N   
635  C CA  . LEU A 85  ? 1.7754 1.1137 0.9543 -0.5755 -0.0225 -0.1505 381 LEU A CA  
636  C C   . LEU A 85  ? 1.9000 1.1054 0.9816 -0.5592 -0.0224 -0.1525 381 LEU A C   
637  O O   . LEU A 85  ? 1.7665 0.8910 0.8198 -0.5083 -0.0222 -0.1529 381 LEU A O   
638  C CB  . LEU A 85  ? 1.8372 1.1689 0.9767 -0.6228 -0.0152 -0.1409 381 LEU A CB  
639  C CG  . LEU A 85  ? 1.8014 1.0826 0.9279 -0.6006 -0.0110 -0.1336 381 LEU A CG  
640  C CD1 . LEU A 85  ? 1.5762 0.9584 0.8126 -0.5681 -0.0145 -0.1359 381 LEU A CD1 
641  C CD2 . LEU A 85  ? 2.0193 1.2886 1.0938 -0.6524 -0.0035 -0.1249 381 LEU A CD2 
642  N N   . GLU A 86  ? 2.0647 1.2479 1.0909 -0.6006 -0.0221 -0.1534 382 GLU A N   
643  C CA  . GLU A 86  ? 2.2085 1.2694 1.1400 -0.5867 -0.0224 -0.1555 382 GLU A CA  
644  C C   . GLU A 86  ? 2.0506 1.1164 1.0194 -0.5298 -0.0280 -0.1658 382 GLU A C   
645  O O   . GLU A 86  ? 2.1545 1.1188 1.0657 -0.4826 -0.0267 -0.1662 382 GLU A O   
646  C CB  . GLU A 86  ? 2.4085 1.4661 1.2874 -0.6466 -0.0219 -0.1555 382 GLU A CB  
647  C CG  . GLU A 86  ? 2.6253 1.5595 1.4047 -0.6357 -0.0228 -0.1579 382 GLU A CG  
648  C CD  . GLU A 86  ? 2.8656 1.6605 1.5133 -0.6593 -0.0166 -0.1471 382 GLU A CD  
649  O OE1 . GLU A 86  ? 3.0223 1.7176 1.5756 -0.6661 -0.0168 -0.1472 382 GLU A OE1 
650  O OE2 . GLU A 86  ? 2.9105 1.6924 1.5440 -0.6712 -0.0117 -0.1384 382 GLU A OE2 
651  N N   . GLU A 87  ? 1.8630 1.0490 0.9246 -0.5309 -0.0337 -0.1736 383 GLU A N   
652  C CA  . GLU A 87  ? 1.7554 0.9528 0.8483 -0.4834 -0.0388 -0.1840 383 GLU A CA  
653  C C   . GLU A 87  ? 1.7358 0.8950 0.8403 -0.4207 -0.0368 -0.1844 383 GLU A C   
654  O O   . GLU A 87  ? 1.7422 0.8408 0.8133 -0.3733 -0.0362 -0.1898 383 GLU A O   
655  C CB  . GLU A 87  ? 1.6904 1.0312 0.8826 -0.4964 -0.0456 -0.1900 383 GLU A CB  
656  C CG  . GLU A 87  ? 1.6910 1.0511 0.9128 -0.4536 -0.0508 -0.2006 383 GLU A CG  
657  C CD  . GLU A 87  ? 1.6407 1.1390 0.9508 -0.4673 -0.0584 -0.2046 383 GLU A CD  
658  O OE1 . GLU A 87  ? 1.3598 0.9510 0.7394 -0.4786 -0.0594 -0.1995 383 GLU A OE1 
659  O OE2 . GLU A 87  ? 1.6957 1.2095 1.0029 -0.4639 -0.0634 -0.2122 383 GLU A OE2 
660  N N   . VAL A 88  ? 1.5991 0.7991 0.7518 -0.4179 -0.0350 -0.1787 384 VAL A N   
661  C CA  . VAL A 88  ? 1.6517 0.8267 0.8211 -0.3605 -0.0332 -0.1787 384 VAL A CA  
662  C C   . VAL A 88  ? 1.8528 0.8968 0.9269 -0.3323 -0.0275 -0.1718 384 VAL A C   
663  O O   . VAL A 88  ? 1.7586 0.7531 0.8121 -0.2720 -0.0257 -0.1738 384 VAL A O   
664  C CB  . VAL A 88  ? 1.6291 0.8945 0.8829 -0.3680 -0.0340 -0.1748 384 VAL A CB  
665  C CG1 . VAL A 88  ? 1.5956 0.8188 0.8502 -0.3150 -0.0310 -0.1725 384 VAL A CG1 
666  C CG2 . VAL A 88  ? 1.5221 0.9143 0.8689 -0.3766 -0.0405 -0.1813 384 VAL A CG2 
667  N N   . ASN A 89  ? 2.0240 1.0144 1.0362 -0.3728 -0.0243 -0.1626 385 ASN A N   
668  C CA  . ASN A 89  ? 2.1877 1.0435 1.0908 -0.3508 -0.0200 -0.1548 385 ASN A CA  
669  C C   . ASN A 89  ? 2.2410 1.0246 1.0845 -0.3113 -0.0206 -0.1603 385 ASN A C   
670  O O   . ASN A 89  ? 2.2461 0.9675 1.0537 -0.2483 -0.0187 -0.1587 385 ASN A O   
671  C CB  . ASN A 89  ? 2.3484 1.1577 1.1807 -0.4135 -0.0169 -0.1457 385 ASN A CB  
672  C CG  . ASN A 89  ? 2.5493 1.2250 1.2712 -0.3934 -0.0128 -0.1349 385 ASN A CG  
673  O OD1 . ASN A 89  ? 2.5313 1.1880 1.2606 -0.3481 -0.0117 -0.1307 385 ASN A OD1 
674  N ND2 . ASN A 89  ? 2.6827 1.2642 1.2966 -0.4266 -0.0109 -0.1298 385 ASN A ND2 
675  N N   . LYS A 90  ? 2.2736 1.0727 1.1081 -0.3458 -0.0233 -0.1664 386 LYS A N   
676  C CA  . LYS A 90  ? 2.3225 1.0590 1.1023 -0.3122 -0.0239 -0.1722 386 LYS A CA  
677  C C   . LYS A 90  ? 2.2936 1.0685 1.1276 -0.2422 -0.0239 -0.1802 386 LYS A C   
678  O O   . LYS A 90  ? 2.3227 1.0254 1.1008 -0.1844 -0.0211 -0.1795 386 LYS A O   
679  C CB  . LYS A 90  ? 2.3726 1.1458 1.1555 -0.3641 -0.0277 -0.1788 386 LYS A CB  
680  C CG  . LYS A 90  ? 2.5045 1.2252 1.2116 -0.4312 -0.0262 -0.1709 386 LYS A CG  
681  C CD  . LYS A 90  ? 2.4173 1.2103 1.1525 -0.4862 -0.0304 -0.1775 386 LYS A CD  
682  C CE  . LYS A 90  ? 2.4824 1.1899 1.1103 -0.5421 -0.0280 -0.1709 386 LYS A CE  
683  N NZ  . LYS A 90  ? 2.4199 1.2210 1.0850 -0.6072 -0.0311 -0.1746 386 LYS A NZ  
684  N N   . GLU A 91  ? 2.1966 1.0876 1.1359 -0.2449 -0.0267 -0.1868 387 GLU A N   
685  C CA  . GLU A 91  ? 2.1205 1.0524 1.1077 -0.1833 -0.0256 -0.1941 387 GLU A CA  
686  C C   . GLU A 91  ? 2.1109 1.0072 1.0878 -0.1236 -0.0206 -0.1876 387 GLU A C   
687  O O   . GLU A 91  ? 2.0849 0.9762 1.0586 -0.0593 -0.0170 -0.1904 387 GLU A O   
688  C CB  . GLU A 91  ? 2.0058 1.0637 1.0975 -0.2046 -0.0303 -0.2012 387 GLU A CB  
689  C CG  . GLU A 91  ? 1.9018 1.0190 1.0498 -0.1453 -0.0278 -0.2042 387 GLU A CG  
690  C CD  . GLU A 91  ? 1.7516 1.0208 1.0271 -0.1591 -0.0310 -0.1967 387 GLU A CD  
691  O OE1 . GLU A 91  ? 1.6375 0.9788 0.9781 -0.1149 -0.0278 -0.1907 387 GLU A OE1 
692  O OE2 . GLU A 91  ? 1.7366 1.0524 1.0424 -0.2133 -0.0365 -0.1968 387 GLU A OE2 
693  N N   . ILE A 92  ? 2.1366 1.0162 1.1097 -0.1416 -0.0201 -0.1782 388 ILE A N   
694  C CA  . ILE A 92  ? 2.1133 0.9543 1.0678 -0.0842 -0.0163 -0.1708 388 ILE A CA  
695  C C   . ILE A 92  ? 2.3146 1.0405 1.1601 -0.0466 -0.0137 -0.1641 388 ILE A C   
696  O O   . ILE A 92  ? 2.4209 1.1231 1.2471 0.0193  -0.0111 -0.1593 388 ILE A O   
697  C CB  . ILE A 92  ? 2.0376 0.8932 1.0166 -0.1146 -0.0167 -0.1625 388 ILE A CB  
698  C CG1 . ILE A 92  ? 1.9616 0.9343 1.0482 -0.1449 -0.0198 -0.1683 388 ILE A CG1 
699  C CG2 . ILE A 92  ? 2.0685 0.8886 1.0288 -0.0543 -0.0138 -0.1545 388 ILE A CG2 
700  C CD1 . ILE A 92  ? 1.7869 0.7837 0.9035 -0.1748 -0.0199 -0.1602 388 ILE A CD1 
701  N N   . GLU A 93  ? 2.3701 1.0262 1.1406 -0.0859 -0.0149 -0.1628 389 GLU A N   
702  C CA  . GLU A 93  ? 2.5169 1.0650 1.1812 -0.0462 -0.0134 -0.1583 389 GLU A CA  
703  C C   . GLU A 93  ? 2.4277 1.0056 1.1104 0.0038  -0.0121 -0.1677 389 GLU A C   
704  O O   . GLU A 93  ? 2.3733 0.9372 1.0377 0.0768  -0.0093 -0.1649 389 GLU A O   
705  C CB  . GLU A 93  ? 2.6302 1.0916 1.2033 -0.1072 -0.0147 -0.1540 389 GLU A CB  
706  C CG  . GLU A 93  ? 2.7272 1.1689 1.2808 -0.1644 -0.0144 -0.1446 389 GLU A CG  
707  C CD  . GLU A 93  ? 2.8963 1.2354 1.3589 -0.1297 -0.0126 -0.1315 389 GLU A CD  
708  O OE1 . GLU A 93  ? 2.9800 1.2634 1.3915 -0.0601 -0.0123 -0.1293 389 GLU A OE1 
709  O OE2 . GLU A 93  ? 2.9052 1.2234 1.3453 -0.1705 -0.0115 -0.1232 389 GLU A OE2 
710  N N   . SER A 94  ? 2.4881 1.1179 1.2104 -0.0341 -0.0142 -0.1784 390 SER A N   
711  C CA  . SER A 94  ? 2.5032 1.1555 1.2332 0.0051  -0.0127 -0.1875 390 SER A CA  
712  C C   . SER A 94  ? 2.4248 1.1574 1.2254 0.0727  -0.0082 -0.1902 390 SER A C   
713  O O   . SER A 94  ? 2.4332 1.1505 1.2055 0.1381  -0.0040 -0.1889 390 SER A O   
714  C CB  . SER A 94  ? 2.5122 1.2226 1.2843 -0.0531 -0.0169 -0.1983 390 SER A CB  
715  O OG  . SER A 94  ? 2.5340 1.3025 1.3462 -0.0156 -0.0151 -0.2081 390 SER A OG  
716  N N   . THR A 95  ? 2.3316 1.1553 1.2235 0.0575  -0.0089 -0.1930 391 THR A N   
717  C CA  . THR A 95  ? 2.1974 1.1097 1.1621 0.1121  -0.0042 -0.1960 391 THR A CA  
718  C C   . THR A 95  ? 2.2018 1.1256 1.1870 0.1476  -0.0020 -0.1868 391 THR A C   
719  O O   . THR A 95  ? 2.0979 1.1099 1.1523 0.1914  0.0022  -0.1849 391 THR A O   
720  C CB  . THR A 95  ? 1.9978 1.0259 1.0647 0.0743  -0.0069 -0.2001 391 THR A CB  
721  O OG1 . THR A 95  ? 1.7774 0.8552 0.9073 0.0344  -0.0107 -0.1913 391 THR A OG1 
722  C CG2 . THR A 95  ? 1.9374 0.9475 0.9769 0.0234  -0.0119 -0.2113 391 THR A CG2 
723  N N   . SER A 96  ? 2.2787 1.1295 1.2132 0.1271  -0.0047 -0.1775 392 SER A N   
724  C CA  . SER A 96  ? 2.2892 1.1456 1.2384 0.1531  -0.0040 -0.1683 392 SER A CA  
725  C C   . SER A 96  ? 2.2031 1.1545 1.2517 0.1318  -0.0048 -0.1717 392 SER A C   
726  O O   . SER A 96  ? 2.0956 1.0838 1.1820 0.1592  -0.0040 -0.1618 392 SER A O   
727  C CB  . SER A 96  ? 2.3353 1.1960 1.2657 0.2390  0.0000  -0.1617 392 SER A CB  
728  O OG  . SER A 96  ? 2.2528 1.2105 1.2493 0.2786  0.0050  -0.1682 392 SER A OG  
729  N N   . THR A 97  ? 2.0756 1.1083 1.1975 0.0806  -0.0077 -0.1728 393 THR A N   
730  C CA  . THR A 97  ? 1.7404 0.8947 0.9802 0.0480  -0.0103 -0.1632 393 THR A CA  
731  C C   . THR A 97  ? 1.6296 0.8148 0.8926 -0.0175 -0.0151 -0.1691 393 THR A C   
732  O O   . THR A 97  ? 1.7283 0.8259 0.9061 -0.0484 -0.0172 -0.1801 393 THR A O   
733  C CB  . THR A 97  ? 1.6005 0.8765 0.9391 0.0939  -0.0070 -0.1539 393 THR A CB  
734  O OG1 . THR A 97  ? 1.5861 0.9666 1.0273 0.0601  -0.0101 -0.1456 393 THR A OG1 
735  C CG2 . THR A 97  ? 1.6045 0.9104 0.9479 0.1168  -0.0040 -0.1593 393 THR A CG2 
736  N N   . TYR A 98  ? 1.5143 0.8192 0.8838 -0.0389 -0.0175 -0.1625 394 TYR A N   
737  C CA  . TYR A 98  ? 1.4703 0.8179 0.8650 -0.0939 -0.0229 -0.1679 394 TYR A CA  
738  C C   . TYR A 98  ? 1.3449 0.8262 0.8552 -0.0914 -0.0244 -0.1594 394 TYR A C   
739  O O   . TYR A 98  ? 1.3412 0.8757 0.9083 -0.0553 -0.0214 -0.1495 394 TYR A O   
740  C CB  . TYR A 98  ? 1.5190 0.8227 0.8733 -0.1554 -0.0267 -0.1714 394 TYR A CB  
741  C CG  . TYR A 98  ? 1.4973 0.8612 0.9153 -0.1693 -0.0270 -0.1615 394 TYR A CG  
742  C CD1 . TYR A 98  ? 1.4655 0.9354 0.9640 -0.2028 -0.0310 -0.1588 394 TYR A CD1 
743  C CD2 . TYR A 98  ? 1.5500 0.8633 0.9427 -0.1463 -0.0236 -0.1551 394 TYR A CD2 
744  C CE1 . TYR A 98  ? 1.3981 0.9206 0.9500 -0.2125 -0.0309 -0.1504 394 TYR A CE1 
745  C CE2 . TYR A 98  ? 1.4460 0.8120 0.8937 -0.1590 -0.0239 -0.1465 394 TYR A CE2 
746  C CZ  . TYR A 98  ? 1.3070 0.7763 0.8337 -0.1924 -0.0272 -0.1444 394 TYR A CZ  
747  O OH  . TYR A 98  ? 1.3260 0.8445 0.9024 -0.2018 -0.0270 -0.1363 394 TYR A OH  
748  N N   . GLN A 99  ? 1.2725 0.8051 0.8107 -0.1310 -0.0298 -0.1637 395 GLN A N   
749  C CA  . GLN A 99  ? 1.2340 0.8797 0.8650 -0.1281 -0.0323 -0.1571 395 GLN A CA  
750  C C   . GLN A 99  ? 1.1583 0.8602 0.8245 -0.1757 -0.0385 -0.1573 395 GLN A C   
751  O O   . GLN A 99  ? 1.1074 0.7828 0.7297 -0.2204 -0.0425 -0.1663 395 GLN A O   
752  C CB  . GLN A 99  ? 1.1525 0.8186 0.7839 -0.1159 -0.0330 -0.1619 395 GLN A CB  
753  C CG  . GLN A 99  ? 1.1321 0.7635 0.7372 -0.0642 -0.0257 -0.1614 395 GLN A CG  
754  C CD  . GLN A 99  ? 1.0941 0.7848 0.7626 -0.0256 -0.0210 -0.1486 395 GLN A CD  
755  O OE1 . GLN A 99  ? 1.0675 0.8372 0.8070 -0.0326 -0.0233 -0.1405 395 GLN A OE1 
756  N NE2 . GLN A 99  ? 1.1676 0.8192 0.8049 0.0155  -0.0147 -0.1471 395 GLN A NE2 
757  N N   . LEU A 100 ? 0.9233 0.7044 0.6649 -0.1665 -0.0392 -0.1475 396 LEU A N   
758  C CA  . LEU A 100 ? 0.8819 0.7274 0.6613 -0.2015 -0.0443 -0.1469 396 LEU A CA  
759  C C   . LEU A 100 ? 0.9160 0.8296 0.7227 -0.2142 -0.0508 -0.1510 396 LEU A C   
760  O O   . LEU A 100 ? 0.9250 0.8622 0.7541 -0.1855 -0.0508 -0.1483 396 LEU A O   
761  C CB  . LEU A 100 ? 0.7856 0.6826 0.6273 -0.1811 -0.0428 -0.1353 396 LEU A CB  
762  C CG  . LEU A 100 ? 0.8086 0.6501 0.6285 -0.1712 -0.0378 -0.1308 396 LEU A CG  
763  C CD1 . LEU A 100 ? 0.7292 0.6217 0.6107 -0.1445 -0.0367 -0.1194 396 LEU A CD1 
764  C CD2 . LEU A 100 ? 0.8218 0.6323 0.6026 -0.2161 -0.0384 -0.1357 396 LEU A CD2 
765  N N   . LYS A 101 ? 0.9138 0.8628 0.7163 -0.2579 -0.0563 -0.1573 397 LYS A N   
766  C CA  . LYS A 101 ? 1.0043 1.0395 0.8440 -0.2651 -0.0637 -0.1596 397 LYS A CA  
767  C C   . LYS A 101 ? 0.9422 1.0504 0.8518 -0.2326 -0.0644 -0.1486 397 LYS A C   
768  O O   . LYS A 101 ? 0.8086 0.9142 0.7393 -0.2213 -0.0604 -0.1412 397 LYS A O   
769  C CB  . LYS A 101 ? 1.0084 1.0830 0.8326 -0.3194 -0.0696 -0.1684 397 LYS A CB  
770  C CG  . LYS A 101 ? 1.1756 1.1774 0.9211 -0.3611 -0.0707 -0.1804 397 LYS A CG  
771  C CD  . LYS A 101 ? 1.2409 1.2567 0.9745 -0.3599 -0.0767 -0.1875 397 LYS A CD  
772  C CE  . LYS A 101 ? 1.3742 1.2858 1.0172 -0.3878 -0.0760 -0.1987 397 LYS A CE  
773  N NZ  . LYS A 101 ? 1.3754 1.2580 1.0031 -0.3550 -0.0760 -0.2012 397 LYS A NZ  
774  N N   . ASP A 102 ? 0.7682 0.9348 0.7071 -0.2165 -0.0698 -0.1475 398 ASP A N   
775  C CA  . ASP A 102 ? 0.7155 0.9377 0.7069 -0.1849 -0.0711 -0.1372 398 ASP A CA  
776  C C   . ASP A 102 ? 0.7866 1.0588 0.8034 -0.1979 -0.0725 -0.1356 398 ASP A C   
777  O O   . ASP A 102 ? 0.6531 0.9258 0.6951 -0.1767 -0.0692 -0.1270 398 ASP A O   
778  C CB  . ASP A 102 ? 0.9276 1.2005 0.9342 -0.1686 -0.0780 -0.1371 398 ASP A CB  
779  C CG  . ASP A 102 ? 1.1047 1.3336 1.0973 -0.1447 -0.0744 -0.1342 398 ASP A CG  
780  O OD1 . ASP A 102 ? 1.1558 1.3197 1.1178 -0.1473 -0.0679 -0.1367 398 ASP A OD1 
781  O OD2 . ASP A 102 ? 1.1412 1.3995 1.1496 -0.1215 -0.0777 -0.1291 398 ASP A OD2 
782  N N   . THR A 103 ? 0.7542 1.0692 0.7614 -0.2355 -0.0770 -0.1443 399 THR A N   
783  C CA  . THR A 103 ? 0.7989 1.1679 0.8272 -0.2516 -0.0769 -0.1436 399 THR A CA  
784  C C   . THR A 103 ? 0.8811 1.1875 0.8972 -0.2572 -0.0687 -0.1393 399 THR A C   
785  O O   . THR A 103 ? 0.8454 1.1803 0.8902 -0.2448 -0.0665 -0.1331 399 THR A O   
786  C CB  . THR A 103 ? 0.8210 1.2436 0.8325 -0.3009 -0.0819 -0.1545 399 THR A CB  
787  O OG1 . THR A 103 ? 0.9315 1.2732 0.8855 -0.3375 -0.0797 -0.1620 399 THR A OG1 
788  C CG2 . THR A 103 ? 0.6997 1.2059 0.7308 -0.2909 -0.0916 -0.1582 399 THR A CG2 
789  N N   . GLU A 104 ? 0.9305 1.1488 0.8988 -0.2735 -0.0643 -0.1426 400 GLU A N   
790  C CA  . GLU A 104 ? 0.8679 1.0203 0.8166 -0.2750 -0.0572 -0.1384 400 GLU A CA  
791  C C   . GLU A 104 ? 0.9312 1.0706 0.9126 -0.2277 -0.0538 -0.1275 400 GLU A C   
792  O O   . GLU A 104 ? 0.9160 1.0490 0.9096 -0.2221 -0.0503 -0.1216 400 GLU A O   
793  C CB  . GLU A 104 ? 0.8747 0.9274 0.7539 -0.2945 -0.0540 -0.1447 400 GLU A CB  
794  C CG  . GLU A 104 ? 0.9464 0.9914 0.7775 -0.3531 -0.0564 -0.1552 400 GLU A CG  
795  C CD  . GLU A 104 ? 1.1237 1.0682 0.8777 -0.3674 -0.0557 -0.1633 400 GLU A CD  
796  O OE1 . GLU A 104 ? 1.0961 1.0229 0.7994 -0.4201 -0.0583 -0.1727 400 GLU A OE1 
797  O OE2 . GLU A 104 ? 1.1608 1.0457 0.9012 -0.3267 -0.0524 -0.1605 400 GLU A OE2 
798  N N   . LEU A 105 ? 0.8513 0.9876 0.8442 -0.1966 -0.0549 -0.1246 401 LEU A N   
799  C CA  . LEU A 105 ? 0.8542 0.9843 0.8754 -0.1583 -0.0521 -0.1143 401 LEU A CA  
800  C C   . LEU A 105 ? 0.7525 0.9418 0.8161 -0.1468 -0.0546 -0.1079 401 LEU A C   
801  O O   . LEU A 105 ? 0.6692 0.8465 0.7467 -0.1331 -0.0517 -0.1008 401 LEU A O   
802  C CB  . LEU A 105 ? 0.7318 0.8563 0.7540 -0.1343 -0.0525 -0.1127 401 LEU A CB  
803  C CG  . LEU A 105 ? 0.7131 0.8271 0.7551 -0.1017 -0.0487 -0.1024 401 LEU A CG  
804  C CD1 . LEU A 105 ? 0.6952 0.7509 0.7102 -0.0921 -0.0424 -0.1022 401 LEU A CD1 
805  C CD2 . LEU A 105 ? 0.7528 0.8912 0.8064 -0.0845 -0.0509 -0.0995 401 LEU A CD2 
806  N N   . ILE A 106 ? 0.6549 0.9087 0.7352 -0.1503 -0.0605 -0.1109 402 ILE A N   
807  C CA  . ILE A 106 ? 0.6039 0.9116 0.7160 -0.1316 -0.0634 -0.1056 402 ILE A CA  
808  C C   . ILE A 106 ? 0.6732 0.9952 0.7905 -0.1488 -0.0604 -0.1061 402 ILE A C   
809  O O   . ILE A 106 ? 0.6517 0.9774 0.7862 -0.1298 -0.0590 -0.0994 402 ILE A O   
810  C CB  . ILE A 106 ? 0.5706 0.9465 0.6929 -0.1251 -0.0711 -0.1094 402 ILE A CB  
811  C CG1 . ILE A 106 ? 0.4333 0.7881 0.5466 -0.1076 -0.0735 -0.1079 402 ILE A CG1 
812  C CG2 . ILE A 106 ? 0.6364 1.0620 0.7817 -0.0975 -0.0742 -0.1042 402 ILE A CG2 
813  C CD1 . ILE A 106 ? 0.3988 0.8116 0.5105 -0.1087 -0.0817 -0.1141 402 ILE A CD1 
814  N N   . TYR A 107 ? 0.6674 0.9919 0.7643 -0.1877 -0.0591 -0.1138 403 TYR A N   
815  C CA  . TYR A 107 ? 0.7523 1.0837 0.8473 -0.2097 -0.0550 -0.1139 403 TYR A CA  
816  C C   . TYR A 107 ? 0.8038 1.0632 0.8895 -0.1977 -0.0492 -0.1070 403 TYR A C   
817  O O   . TYR A 107 ? 0.7652 1.0370 0.8694 -0.1854 -0.0472 -0.1015 403 TYR A O   
818  C CB  . TYR A 107 ? 0.7979 1.1301 0.8597 -0.2610 -0.0543 -0.1233 403 TYR A CB  
819  C CG  . TYR A 107 ? 0.9097 1.2329 0.9570 -0.2913 -0.0487 -0.1232 403 TYR A CG  
820  C CD1 . TYR A 107 ? 1.0037 1.4143 1.0704 -0.3118 -0.0489 -0.1258 403 TYR A CD1 
821  C CD2 . TYR A 107 ? 0.9619 1.1920 0.9732 -0.2976 -0.0432 -0.1202 403 TYR A CD2 
822  C CE1 . TYR A 107 ? 0.9694 1.3733 1.0205 -0.3425 -0.0428 -0.1252 403 TYR A CE1 
823  C CE2 . TYR A 107 ? 0.9252 1.1406 0.9174 -0.3255 -0.0380 -0.1193 403 TYR A CE2 
824  C CZ  . TYR A 107 ? 0.9560 1.2573 0.9683 -0.3504 -0.0374 -0.1217 403 TYR A CZ  
825  O OH  . TYR A 107 ? 0.9403 1.2272 0.9309 -0.3807 -0.0312 -0.1202 403 TYR A OH  
826  N N   . GLY A 108 ? 0.7181 0.9035 0.7720 -0.1995 -0.0467 -0.1076 404 GLY A N   
827  C CA  . GLY A 108 ? 0.7308 0.8538 0.7725 -0.1860 -0.0420 -0.1015 404 GLY A CA  
828  C C   . GLY A 108 ? 0.6981 0.8361 0.7756 -0.1500 -0.0426 -0.0923 404 GLY A C   
829  O O   . GLY A 108 ? 0.6638 0.7888 0.7469 -0.1438 -0.0403 -0.0871 404 GLY A O   
830  N N   . ALA A 109 ? 0.7285 0.8908 0.8255 -0.1285 -0.0460 -0.0902 405 ALA A N   
831  C CA  . ALA A 109 ? 0.6827 0.8510 0.8034 -0.1001 -0.0469 -0.0814 405 ALA A CA  
832  C C   . ALA A 109 ? 0.6501 0.8561 0.7900 -0.0957 -0.0485 -0.0789 405 ALA A C   
833  O O   . ALA A 109 ? 0.7495 0.9405 0.8963 -0.0842 -0.0474 -0.0726 405 ALA A O   
834  C CB  . ALA A 109 ? 0.5860 0.7674 0.7133 -0.0833 -0.0501 -0.0798 405 ALA A CB  
835  N N   . LYS A 110 ? 0.5327 0.7923 0.6798 -0.1032 -0.0514 -0.0840 406 LYS A N   
836  C CA  . LYS A 110 ? 0.5890 0.8909 0.7511 -0.0942 -0.0522 -0.0825 406 LYS A CA  
837  C C   . LYS A 110 ? 0.6270 0.9119 0.7849 -0.1103 -0.0471 -0.0817 406 LYS A C   
838  O O   . LYS A 110 ? 0.4851 0.7713 0.6511 -0.0953 -0.0464 -0.0770 406 LYS A O   
839  C CB  . LYS A 110 ? 0.5124 0.8882 0.6821 -0.1001 -0.0557 -0.0893 406 LYS A CB  
840  C CG  . LYS A 110 ? 0.4832 0.8847 0.6572 -0.0716 -0.0622 -0.0884 406 LYS A CG  
841  C CD  . LYS A 110 ? 0.4589 0.9428 0.6399 -0.0765 -0.0666 -0.0958 406 LYS A CD  
842  C CE  . LYS A 110 ? 0.3824 0.8801 0.5603 -0.0462 -0.0736 -0.0944 406 LYS A CE  
843  N NZ  . LYS A 110 ? 0.6043 1.1941 0.7908 -0.0342 -0.0793 -0.0998 406 LYS A NZ  
844  N N   . HIS A 111 ? 0.5996 0.8604 0.7374 -0.1411 -0.0436 -0.0862 407 HIS A N   
845  C CA  . HIS A 111 ? 0.6026 0.8433 0.7276 -0.1606 -0.0385 -0.0855 407 HIS A CA  
846  C C   . HIS A 111 ? 0.6562 0.8326 0.7722 -0.1459 -0.0365 -0.0787 407 HIS A C   
847  O O   . HIS A 111 ? 0.6342 0.8011 0.7482 -0.1484 -0.0337 -0.0755 407 HIS A O   
848  C CB  . HIS A 111 ? 0.6035 0.8340 0.6980 -0.2024 -0.0360 -0.0928 407 HIS A CB  
849  C CG  . HIS A 111 ? 0.6739 0.9855 0.7794 -0.2261 -0.0365 -0.0988 407 HIS A CG  
850  N ND1 . HIS A 111 ? 0.6762 1.0494 0.7976 -0.2227 -0.0417 -0.1037 407 HIS A ND1 
851  C CD2 . HIS A 111 ? 0.5998 0.9511 0.7043 -0.2513 -0.0324 -0.1004 407 HIS A CD2 
852  C CE1 . HIS A 111 ? 0.6844 1.1375 0.8155 -0.2444 -0.0413 -0.1085 407 HIS A CE1 
853  N NE2 . HIS A 111 ? 0.6925 1.1353 0.8139 -0.2637 -0.0351 -0.1066 407 HIS A NE2 
854  N N   . ALA A 112 ? 0.5502 0.6908 0.6621 -0.1293 -0.0380 -0.0763 408 ALA A N   
855  C CA  . ALA A 112 ? 0.6580 0.7601 0.7699 -0.1097 -0.0374 -0.0692 408 ALA A CA  
856  C C   . ALA A 112 ? 0.7027 0.8293 0.8387 -0.0924 -0.0396 -0.0633 408 ALA A C   
857  O O   . ALA A 112 ? 0.7013 0.8091 0.8357 -0.0884 -0.0386 -0.0589 408 ALA A O   
858  C CB  . ALA A 112 ? 0.5488 0.6294 0.6568 -0.0943 -0.0384 -0.0679 408 ALA A CB  
859  N N   . TRP A 113 ? 0.6224 0.7855 0.7742 -0.0805 -0.0431 -0.0634 409 TRP A N   
860  C CA  . TRP A 113 ? 0.6397 0.8165 0.8014 -0.0634 -0.0454 -0.0590 409 TRP A CA  
861  C C   . TRP A 113 ? 0.5820 0.7815 0.7449 -0.0714 -0.0427 -0.0611 409 TRP A C   
862  O O   . TRP A 113 ? 0.6371 0.8210 0.7986 -0.0650 -0.0421 -0.0570 409 TRP A O   
863  C CB  . TRP A 113 ? 0.6078 0.8109 0.7736 -0.0462 -0.0499 -0.0591 409 TRP A CB  
864  C CG  . TRP A 113 ? 0.5523 0.7542 0.7136 -0.0243 -0.0530 -0.0548 409 TRP A CG  
865  C CD1 . TRP A 113 ? 0.6051 0.7825 0.7612 -0.0202 -0.0526 -0.0505 409 TRP A CD1 
866  C CD2 . TRP A 113 ? 0.5377 0.7562 0.6903 -0.0016 -0.0575 -0.0548 409 TRP A CD2 
867  N NE1 . TRP A 113 ? 0.6188 0.7914 0.7603 0.0020  -0.0563 -0.0482 409 TRP A NE1 
868  C CE2 . TRP A 113 ? 0.5239 0.7188 0.6606 0.0159  -0.0594 -0.0505 409 TRP A CE2 
869  C CE3 . TRP A 113 ? 0.5018 0.7490 0.6529 0.0076  -0.0607 -0.0579 409 TRP A CE3 
870  C CZ2 . TRP A 113 ? 0.4729 0.6640 0.5861 0.0444  -0.0640 -0.0494 409 TRP A CZ2 
871  C CZ3 . TRP A 113 ? 0.6673 0.9177 0.7998 0.0373  -0.0656 -0.0563 409 TRP A CZ3 
872  C CH2 . TRP A 113 ? 0.6051 0.8238 0.7159 0.0566  -0.0670 -0.0520 409 TRP A CH2 
873  N N   . ARG A 114 ? 0.4983 0.7397 0.6627 -0.0874 -0.0410 -0.0676 410 ARG A N   
874  C CA  . ARG A 114 ? 0.6298 0.9049 0.7953 -0.0996 -0.0370 -0.0701 410 ARG A CA  
875  C C   . ARG A 114 ? 0.6348 0.8644 0.7867 -0.1127 -0.0328 -0.0666 410 ARG A C   
876  O O   . ARG A 114 ? 0.5961 0.8363 0.7495 -0.1093 -0.0304 -0.0648 410 ARG A O   
877  C CB  . ARG A 114 ? 0.6067 0.9306 0.7709 -0.1275 -0.0353 -0.0777 410 ARG A CB  
878  C CG  . ARG A 114 ? 0.5704 0.9568 0.7408 -0.1391 -0.0313 -0.0809 410 ARG A CG  
879  C CD  . ARG A 114 ? 0.6756 1.1135 0.8419 -0.1757 -0.0300 -0.0886 410 ARG A CD  
880  N NE  . ARG A 114 ? 0.6934 1.2160 0.8710 -0.1854 -0.0263 -0.0921 410 ARG A NE  
881  C CZ  . ARG A 114 ? 0.6298 1.2206 0.8068 -0.2208 -0.0247 -0.0990 410 ARG A CZ  
882  N NH1 . ARG A 114 ? 0.5542 1.2340 0.7440 -0.2277 -0.0207 -0.1018 410 ARG A NH1 
883  N NH2 . ARG A 114 ? 0.7413 1.3146 0.9029 -0.2503 -0.0272 -0.1034 410 ARG A NH2 
884  N N   . ASN A 115 ? 0.5214 0.6986 0.6561 -0.1239 -0.0320 -0.0657 411 ASN A N   
885  C CA  . ASN A 115 ? 0.6877 0.8158 0.8016 -0.1328 -0.0287 -0.0624 411 ASN A CA  
886  C C   . ASN A 115 ? 0.6199 0.7186 0.7398 -0.1080 -0.0317 -0.0552 411 ASN A C   
887  O O   . ASN A 115 ? 0.5781 0.6388 0.6811 -0.1099 -0.0302 -0.0518 411 ASN A O   
888  C CB  . ASN A 115 ? 0.5247 0.6046 0.6065 -0.1511 -0.0269 -0.0652 411 ASN A CB  
889  C CG  . ASN A 115 ? 0.6766 0.7772 0.7415 -0.1868 -0.0238 -0.0723 411 ASN A CG  
890  O OD1 . ASN A 115 ? 0.8381 0.9901 0.9138 -0.2018 -0.0213 -0.0743 411 ASN A OD1 
891  N ND2 . ASN A 115 ? 0.6273 0.6911 0.6628 -0.2016 -0.0238 -0.0766 411 ASN A ND2 
892  N N   . ALA A 116 ? 0.5962 0.7097 0.7346 -0.0867 -0.0362 -0.0526 412 ALA A N   
893  C CA  . ALA A 116 ? 0.5493 0.6381 0.6902 -0.0704 -0.0397 -0.0461 412 ALA A CA  
894  C C   . ALA A 116 ? 0.5858 0.6757 0.7259 -0.0666 -0.0397 -0.0435 412 ALA A C   
895  O O   . ALA A 116 ? 0.5801 0.6894 0.7254 -0.0555 -0.0415 -0.0435 412 ALA A O   
896  C CB  . ALA A 116 ? 0.5397 0.6379 0.6910 -0.0564 -0.0441 -0.0441 412 ALA A CB  
897  N N   . SER A 117 ? 0.6014 0.6656 0.7288 -0.0733 -0.0376 -0.0413 413 SER A N   
898  C CA  . SER A 117 ? 0.6042 0.6705 0.7276 -0.0732 -0.0363 -0.0398 413 SER A CA  
899  C C   . SER A 117 ? 0.5806 0.6408 0.7079 -0.0569 -0.0419 -0.0355 413 SER A C   
900  O O   . SER A 117 ? 0.6761 0.7424 0.7990 -0.0520 -0.0415 -0.0356 413 SER A O   
901  C CB  . SER A 117 ? 0.6823 0.7159 0.7845 -0.0849 -0.0330 -0.0381 413 SER A CB  
902  O OG  . SER A 117 ? 0.6868 0.6886 0.7819 -0.0740 -0.0371 -0.0335 413 SER A OG  
903  N N   . ARG A 118 ? 0.4533 0.5023 0.5847 -0.0502 -0.0470 -0.0321 414 ARG A N   
904  C CA  . ARG A 118 ? 0.5323 0.5716 0.6600 -0.0427 -0.0528 -0.0280 414 ARG A CA  
905  C C   . ARG A 118 ? 0.6332 0.6781 0.7572 -0.0344 -0.0552 -0.0291 414 ARG A C   
906  O O   . ARG A 118 ? 0.4755 0.5010 0.5854 -0.0315 -0.0603 -0.0258 414 ARG A O   
907  C CB  . ARG A 118 ? 0.5695 0.6020 0.7005 -0.0440 -0.0570 -0.0233 414 ARG A CB  
908  C CG  . ARG A 118 ? 0.5674 0.5902 0.6943 -0.0440 -0.0562 -0.0215 414 ARG A CG  
909  C CD  . ARG A 118 ? 0.6271 0.6581 0.7582 -0.0399 -0.0611 -0.0169 414 ARG A CD  
910  N NE  . ARG A 118 ? 0.5628 0.5847 0.6844 -0.0344 -0.0628 -0.0142 414 ARG A NE  
911  C CZ  . ARG A 118 ? 0.6619 0.6991 0.7852 -0.0257 -0.0669 -0.0105 414 ARG A CZ  
912  N NH1 . ARG A 118 ? 0.6450 0.7110 0.7813 -0.0249 -0.0688 -0.0092 414 ARG A NH1 
913  N NH2 . ARG A 118 ? 0.7293 0.7571 0.8399 -0.0169 -0.0692 -0.0081 414 ARG A NH2 
914  N N   . CYS A 119 ? 0.4948 0.5623 0.6251 -0.0310 -0.0523 -0.0337 415 CYS A N   
915  C CA  . CYS A 119 ? 0.5545 0.6251 0.6757 -0.0176 -0.0551 -0.0345 415 CYS A CA  
916  C C   . CYS A 119 ? 0.4868 0.5726 0.5975 -0.0020 -0.0537 -0.0381 415 CYS A C   
917  O O   . CYS A 119 ? 0.6019 0.7262 0.7249 -0.0042 -0.0487 -0.0429 415 CYS A O   
918  C CB  . CYS A 119 ? 0.5035 0.5956 0.6363 -0.0189 -0.0541 -0.0373 415 CYS A CB  
919  S SG  . CYS A 119 ? 0.5217 0.6162 0.6356 0.0037  -0.0581 -0.0382 415 CYS A SG  
920  N N   . VAL A 120 ? 0.5133 0.5693 0.5963 0.0134  -0.0580 -0.0362 416 VAL A N   
921  C CA  . VAL A 120 ? 0.5425 0.6093 0.6074 0.0370  -0.0568 -0.0398 416 VAL A CA  
922  C C   . VAL A 120 ? 0.6118 0.7053 0.6708 0.0595  -0.0577 -0.0433 416 VAL A C   
923  O O   . VAL A 120 ? 0.6212 0.7468 0.6724 0.0830  -0.0556 -0.0477 416 VAL A O   
924  C CB  . VAL A 120 ? 0.5756 0.5867 0.6005 0.0471  -0.0616 -0.0369 416 VAL A CB  
925  C CG1 . VAL A 120 ? 0.6273 0.5921 0.6151 0.0575  -0.0681 -0.0340 416 VAL A CG1 
926  C CG2 . VAL A 120 ? 0.6071 0.6306 0.6151 0.0704  -0.0585 -0.0411 416 VAL A CG2 
927  N N   . GLY A 121 ? 0.7170 0.8039 0.7791 0.0550  -0.0606 -0.0416 417 GLY A N   
928  C CA  . GLY A 121 ? 0.5067 0.6133 0.5585 0.0778  -0.0629 -0.0441 417 GLY A CA  
929  C C   . GLY A 121 ? 0.5375 0.7173 0.6225 0.0743  -0.0592 -0.0501 417 GLY A C   
930  O O   . GLY A 121 ? 0.6639 0.8692 0.7431 0.0932  -0.0619 -0.0524 417 GLY A O   
931  N N   . ARG A 122 ? 0.4726 0.6861 0.5864 0.0498  -0.0534 -0.0528 418 ARG A N   
932  C CA  . ARG A 122 ? 0.4912 0.7587 0.6311 0.0317  -0.0505 -0.0577 418 ARG A CA  
933  C C   . ARG A 122 ? 0.5850 0.9259 0.7294 0.0499  -0.0502 -0.0639 418 ARG A C   
934  O O   . ARG A 122 ? 0.5252 0.9141 0.6874 0.0336  -0.0494 -0.0684 418 ARG A O   
935  C CB  . ARG A 122 ? 0.3991 0.6706 0.5546 -0.0014 -0.0445 -0.0587 418 ARG A CB  
936  C CG  . ARG A 122 ? 0.5198 0.7348 0.6744 -0.0182 -0.0452 -0.0538 418 ARG A CG  
937  C CD  . ARG A 122 ? 0.5690 0.7794 0.7276 -0.0446 -0.0398 -0.0546 418 ARG A CD  
938  N NE  . ARG A 122 ? 0.6081 0.8012 0.7592 -0.0420 -0.0381 -0.0517 418 ARG A NE  
939  C CZ  . ARG A 122 ? 0.5701 0.7617 0.7179 -0.0616 -0.0328 -0.0522 418 ARG A CZ  
940  N NH1 . ARG A 122 ? 0.3801 0.5811 0.5266 -0.0871 -0.0289 -0.0556 418 ARG A NH1 
941  N NH2 . ARG A 122 ? 0.6541 0.8289 0.7936 -0.0574 -0.0316 -0.0493 418 ARG A NH2 
942  N N   . ILE A 123 ? 0.5985 0.9511 0.7240 0.0846  -0.0513 -0.0646 419 ILE A N   
943  C CA  . ILE A 123 ? 0.5395 0.9739 0.6687 0.1093  -0.0514 -0.0706 419 ILE A CA  
944  C C   . ILE A 123 ? 0.5979 1.0511 0.7271 0.1197  -0.0574 -0.0720 419 ILE A C   
945  O O   . ILE A 123 ? 0.4980 1.0339 0.6381 0.1322  -0.0582 -0.0776 419 ILE A O   
946  C CB  . ILE A 123 ? 0.6062 1.0345 0.7031 0.1558  -0.0524 -0.0707 419 ILE A CB  
947  C CG1 . ILE A 123 ? 0.6519 1.1880 0.7597 0.1796  -0.0498 -0.0778 419 ILE A CG1 
948  C CG2 . ILE A 123 ? 0.6198 0.9724 0.6719 0.1899  -0.0604 -0.0662 419 ILE A CG2 
949  C CD1 . ILE A 123 ? 0.7119 1.2496 0.7791 0.2435  -0.0551 -0.0790 419 ILE A CD1 
950  N N   . GLN A 124 ? 0.5621 0.9467 0.6799 0.1131  -0.0614 -0.0669 420 GLN A N   
951  C CA  . GLN A 124 ? 0.7382 1.1284 0.8517 0.1214  -0.0669 -0.0671 420 GLN A CA  
952  C C   . GLN A 124 ? 0.6824 1.0848 0.8239 0.0805  -0.0650 -0.0690 420 GLN A C   
953  O O   . GLN A 124 ? 0.6795 1.0790 0.8174 0.0830  -0.0691 -0.0689 420 GLN A O   
954  C CB  . GLN A 124 ? 0.9453 1.2483 1.0188 0.1410  -0.0721 -0.0598 420 GLN A CB  
955  C CG  . GLN A 124 ? 1.0623 1.3421 1.0888 0.1901  -0.0765 -0.0586 420 GLN A CG  
956  C CD  . GLN A 124 ? 1.1728 1.4884 1.1816 0.2264  -0.0826 -0.0610 420 GLN A CD  
957  O OE1 . GLN A 124 ? 1.1693 1.5520 1.2102 0.2141  -0.0830 -0.0653 420 GLN A OE1 
958  N NE2 . GLN A 124 ? 1.2571 1.5237 1.2085 0.2721  -0.0878 -0.0582 420 GLN A NE2 
959  N N   . TRP A 125 ? 0.6346 1.0453 0.7970 0.0447  -0.0589 -0.0710 421 TRP A N   
960  C CA  . TRP A 125 ? 0.5991 0.9908 0.7731 0.0088  -0.0570 -0.0718 421 TRP A CA  
961  C C   . TRP A 125 ? 0.6285 1.0705 0.8103 0.0013  -0.0600 -0.0776 421 TRP A C   
962  O O   . TRP A 125 ? 0.7211 1.1334 0.9006 -0.0108 -0.0613 -0.0772 421 TRP A O   
963  C CB  . TRP A 125 ? 0.4328 0.8229 0.6159 -0.0248 -0.0503 -0.0734 421 TRP A CB  
964  C CG  . TRP A 125 ? 0.5447 1.0114 0.7388 -0.0430 -0.0472 -0.0805 421 TRP A CG  
965  C CD1 . TRP A 125 ? 0.5768 1.0957 0.7757 -0.0348 -0.0440 -0.0823 421 TRP A CD1 
966  C CD2 . TRP A 125 ? 0.5867 1.0912 0.7855 -0.0760 -0.0467 -0.0869 421 TRP A CD2 
967  N NE1 . TRP A 125 ? 0.6043 1.1997 0.8140 -0.0631 -0.0412 -0.0892 421 TRP A NE1 
968  C CE2 . TRP A 125 ? 0.5808 1.1654 0.7886 -0.0908 -0.0433 -0.0922 421 TRP A CE2 
969  C CE3 . TRP A 125 ? 0.5724 1.0511 0.7652 -0.0955 -0.0487 -0.0891 421 TRP A CE3 
970  C CZ2 . TRP A 125 ? 0.5294 1.1687 0.7391 -0.1300 -0.0424 -0.0994 421 TRP A CZ2 
971  C CZ3 . TRP A 125 ? 0.6152 1.1392 0.8064 -0.1313 -0.0481 -0.0967 421 TRP A CZ3 
972  C CH2 . TRP A 125 ? 0.6100 1.2136 0.8093 -0.1506 -0.0453 -0.1017 421 TRP A CH2 
973  N N   . SER A 126 ? 0.6959 1.2199 0.8861 0.0090  -0.0612 -0.0835 422 SER A N   
974  C CA  . SER A 126 ? 0.6698 1.2515 0.8673 -0.0004 -0.0652 -0.0896 422 SER A CA  
975  C C   . SER A 126 ? 0.7263 1.2950 0.9096 0.0353  -0.0727 -0.0870 422 SER A C   
976  O O   . SER A 126 ? 0.7109 1.3079 0.8969 0.0269  -0.0767 -0.0910 422 SER A O   
977  C CB  . SER A 126 ? 0.6150 1.3040 0.8274 -0.0047 -0.0645 -0.0968 422 SER A CB  
978  O OG  . SER A 126 ? 0.5525 1.2854 0.7594 0.0459  -0.0683 -0.0962 422 SER A OG  
979  N N   . LYS A 127 ? 0.7790 1.2999 0.9410 0.0729  -0.0750 -0.0804 423 LYS A N   
980  C CA  . LYS A 127 ? 0.8168 1.3072 0.9531 0.1051  -0.0818 -0.0764 423 LYS A CA  
981  C C   . LYS A 127 ? 0.8022 1.2016 0.9265 0.0903  -0.0802 -0.0692 423 LYS A C   
982  O O   . LYS A 127 ? 0.8278 1.1635 0.9277 0.1047  -0.0804 -0.0623 423 LYS A O   
983  C CB  . LYS A 127 ? 0.8498 1.3400 0.9563 0.1562  -0.0859 -0.0740 423 LYS A CB  
984  C CG  . LYS A 127 ? 0.9026 1.4992 1.0214 0.1784  -0.0876 -0.0814 423 LYS A CG  
985  C CD  . LYS A 127 ? 1.0064 1.6037 1.0842 0.2418  -0.0945 -0.0796 423 LYS A CD  
986  C CE  . LYS A 127 ? 0.9845 1.5643 1.0393 0.2600  -0.1026 -0.0775 423 LYS A CE  
987  N NZ  . LYS A 127 ? 0.8905 1.3508 0.8919 0.2804  -0.1052 -0.0681 423 LYS A NZ  
988  N N   . LEU A 128 ? 0.6529 1.0497 0.7916 0.0597  -0.0785 -0.0714 424 LEU A N   
989  C CA  . LEU A 128 ? 0.6060 0.9356 0.7380 0.0449  -0.0761 -0.0659 424 LEU A CA  
990  C C   . LEU A 128 ? 0.6325 0.9705 0.7615 0.0405  -0.0790 -0.0680 424 LEU A C   
991  O O   . LEU A 128 ? 0.5791 0.9657 0.7219 0.0245  -0.0797 -0.0757 424 LEU A O   
992  C CB  . LEU A 128 ? 0.5338 0.8446 0.6829 0.0129  -0.0694 -0.0668 424 LEU A CB  
993  C CG  . LEU A 128 ? 0.5100 0.7685 0.6561 -0.0015 -0.0662 -0.0626 424 LEU A CG  
994  C CD1 . LEU A 128 ? 0.4619 0.6727 0.5924 0.0114  -0.0667 -0.0535 424 LEU A CD1 
995  C CD2 . LEU A 128 ? 0.5333 0.7809 0.6903 -0.0271 -0.0604 -0.0654 424 LEU A CD2 
996  N N   . GLN A 129 ? 0.7478 1.0379 0.8552 0.0513  -0.0805 -0.0612 425 GLN A N   
997  C CA  . GLN A 129 ? 0.7140 1.0056 0.8141 0.0495  -0.0828 -0.0621 425 GLN A CA  
998  C C   . GLN A 129 ? 0.6953 0.9562 0.8047 0.0224  -0.0764 -0.0616 425 GLN A C   
999  O O   . GLN A 129 ? 0.6217 0.8394 0.7259 0.0185  -0.0726 -0.0547 425 GLN A O   
1000 C CB  . GLN A 129 ? 0.7889 1.0443 0.8524 0.0770  -0.0876 -0.0544 425 GLN A CB  
1001 C CG  . GLN A 129 ? 0.7253 0.9807 0.7765 0.0779  -0.0902 -0.0544 425 GLN A CG  
1002 C CD  . GLN A 129 ? 0.7530 1.0770 0.8217 0.0758  -0.0944 -0.0644 425 GLN A CD  
1003 O OE1 . GLN A 129 ? 0.7413 1.1177 0.8143 0.0933  -0.0995 -0.0688 425 GLN A OE1 
1004 N NE2 . GLN A 129 ? 0.7572 1.0849 0.8342 0.0537  -0.0923 -0.0685 425 GLN A NE2 
1005 N N   . VAL A 130 ? 0.6495 0.9342 0.7691 0.0043  -0.0755 -0.0692 426 VAL A N   
1006 C CA  . VAL A 130 ? 0.6511 0.9067 0.7736 -0.0162 -0.0692 -0.0705 426 VAL A CA  
1007 C C   . VAL A 130 ? 0.6604 0.9046 0.7693 -0.0130 -0.0695 -0.0696 426 VAL A C   
1008 O O   . VAL A 130 ? 0.6000 0.8720 0.7036 -0.0124 -0.0741 -0.0751 426 VAL A O   
1009 C CB  . VAL A 130 ? 0.6447 0.9174 0.7743 -0.0406 -0.0672 -0.0799 426 VAL A CB  
1010 C CG1 . VAL A 130 ? 0.5567 0.7866 0.6782 -0.0542 -0.0607 -0.0811 426 VAL A CG1 
1011 C CG2 . VAL A 130 ? 0.4797 0.7703 0.6211 -0.0442 -0.0667 -0.0803 426 VAL A CG2 
1012 N N   . PHE A 131 ? 0.6244 0.8338 0.7269 -0.0114 -0.0648 -0.0625 427 PHE A N   
1013 C CA  . PHE A 131 ? 0.6323 0.8318 0.7213 -0.0100 -0.0632 -0.0611 427 PHE A CA  
1014 C C   . PHE A 131 ? 0.6645 0.8530 0.7557 -0.0219 -0.0565 -0.0661 427 PHE A C   
1015 O O   . PHE A 131 ? 0.5387 0.7114 0.6365 -0.0245 -0.0511 -0.0633 427 PHE A O   
1016 C CB  . PHE A 131 ? 0.5370 0.7112 0.6117 -0.0029 -0.0616 -0.0497 427 PHE A CB  
1017 C CG  . PHE A 131 ? 0.5952 0.7626 0.6498 0.0133  -0.0686 -0.0446 427 PHE A CG  
1018 C CD1 . PHE A 131 ? 0.5686 0.7483 0.6061 0.0265  -0.0745 -0.0464 427 PHE A CD1 
1019 C CD2 . PHE A 131 ? 0.6049 0.7496 0.6515 0.0183  -0.0697 -0.0382 427 PHE A CD2 
1020 C CE1 . PHE A 131 ? 0.6130 0.7809 0.6233 0.0487  -0.0814 -0.0416 427 PHE A CE1 
1021 C CE2 . PHE A 131 ? 0.7109 0.8378 0.7273 0.0383  -0.0762 -0.0338 427 PHE A CE2 
1022 C CZ  . PHE A 131 ? 0.6390 0.7764 0.6360 0.0558  -0.0820 -0.0353 427 PHE A CZ  
1023 N N   . ASP A 132 ? 0.6169 0.8122 0.6974 -0.0266 -0.0575 -0.0738 428 ASP A N   
1024 C CA  . ASP A 132 ? 0.5612 0.7371 0.6310 -0.0345 -0.0520 -0.0806 428 ASP A CA  
1025 C C   . ASP A 132 ? 0.5610 0.7267 0.6220 -0.0245 -0.0460 -0.0758 428 ASP A C   
1026 O O   . ASP A 132 ? 0.5948 0.7665 0.6430 -0.0216 -0.0473 -0.0770 428 ASP A O   
1027 C CB  . ASP A 132 ? 0.5462 0.7307 0.6015 -0.0482 -0.0564 -0.0921 428 ASP A CB  
1028 C CG  . ASP A 132 ? 0.6885 0.8365 0.7180 -0.0561 -0.0512 -0.1002 428 ASP A CG  
1029 O OD1 . ASP A 132 ? 0.6668 0.8111 0.6761 -0.0742 -0.0548 -0.1104 428 ASP A OD1 
1030 O OD2 . ASP A 132 ? 0.7140 0.8372 0.7388 -0.0439 -0.0440 -0.0966 428 ASP A OD2 
1031 N N   . ALA A 133 ? 0.5779 0.7344 0.6454 -0.0195 -0.0395 -0.0703 429 ALA A N   
1032 C CA  . ALA A 133 ? 0.6433 0.8025 0.7042 -0.0111 -0.0323 -0.0662 429 ALA A CA  
1033 C C   . ALA A 133 ? 0.6065 0.7493 0.6514 -0.0031 -0.0262 -0.0740 429 ALA A C   
1034 O O   . ALA A 133 ? 0.6367 0.7890 0.6803 0.0089  -0.0188 -0.0706 429 ALA A O   
1035 C CB  . ALA A 133 ? 0.5984 0.7693 0.6741 -0.0109 -0.0292 -0.0549 429 ALA A CB  
1036 N N   . ARG A 134 ? 0.5206 0.6384 0.5478 -0.0094 -0.0291 -0.0844 430 ARG A N   
1037 C CA  . ARG A 134 ? 0.6535 0.7388 0.6511 0.0010  -0.0235 -0.0918 430 ARG A CA  
1038 C C   . ARG A 134 ? 0.6972 0.7801 0.6711 0.0126  -0.0190 -0.0959 430 ARG A C   
1039 O O   . ARG A 134 ? 0.7282 0.7826 0.6716 0.0289  -0.0134 -0.1016 430 ARG A O   
1040 C CB  . ARG A 134 ? 0.6017 0.6490 0.5748 -0.0149 -0.0277 -0.1017 430 ARG A CB  
1041 C CG  . ARG A 134 ? 0.6683 0.7069 0.6535 -0.0199 -0.0285 -0.0986 430 ARG A CG  
1042 C CD  . ARG A 134 ? 0.7426 0.7442 0.6983 -0.0425 -0.0320 -0.1080 430 ARG A CD  
1043 N NE  . ARG A 134 ? 0.7802 0.8104 0.7443 -0.0660 -0.0391 -0.1122 430 ARG A NE  
1044 C CZ  . ARG A 134 ? 0.8049 0.8161 0.7402 -0.0933 -0.0429 -0.1219 430 ARG A CZ  
1045 N NH1 . ARG A 134 ? 0.8820 0.8308 0.7709 -0.1018 -0.0400 -0.1280 430 ARG A NH1 
1046 N NH2 . ARG A 134 ? 0.7208 0.7750 0.6686 -0.1126 -0.0499 -0.1254 430 ARG A NH2 
1047 N N   . ASP A 135 ? 0.6297 0.7380 0.6111 0.0079  -0.0212 -0.0929 431 ASP A N   
1048 C CA  . ASP A 135 ? 0.7929 0.9036 0.7532 0.0192  -0.0160 -0.0954 431 ASP A CA  
1049 C C   . ASP A 135 ? 0.8041 0.9508 0.7804 0.0323  -0.0074 -0.0850 431 ASP A C   
1050 O O   . ASP A 135 ? 0.7168 0.8750 0.6785 0.0413  -0.0018 -0.0854 431 ASP A O   
1051 C CB  . ASP A 135 ? 0.7903 0.9090 0.7444 0.0068  -0.0230 -0.0980 431 ASP A CB  
1052 C CG  . ASP A 135 ? 0.9135 1.0612 0.8954 -0.0009 -0.0288 -0.0875 431 ASP A CG  
1053 O OD1 . ASP A 135 ? 0.9326 1.0949 0.9107 0.0012  -0.0289 -0.0821 431 ASP A OD1 
1054 O OD2 . ASP A 135 ? 0.8929 1.0435 0.8946 -0.0074 -0.0329 -0.0846 431 ASP A OD2 
1055 N N   . CYS A 136 ? 0.6522 0.8195 0.6560 0.0304  -0.0065 -0.0758 432 CYS A N   
1056 C CA  . CYS A 136 ? 0.6423 0.8512 0.6621 0.0337  0.0007  -0.0652 432 CYS A CA  
1057 C C   . CYS A 136 ? 0.6707 0.8955 0.6807 0.0585  0.0104  -0.0683 432 CYS A C   
1058 O O   . CYS A 136 ? 0.8271 1.0247 0.8233 0.0743  0.0106  -0.0755 432 CYS A O   
1059 C CB  . CYS A 136 ? 0.5557 0.7770 0.6024 0.0207  -0.0029 -0.0557 432 CYS A CB  
1060 S SG  . CYS A 136 ? 0.6289 0.9012 0.6902 0.0101  0.0038  -0.0415 432 CYS A SG  
1061 N N   . THR A 137 ? 0.7867 1.0560 0.7988 0.0634  0.0188  -0.0627 433 THR A N   
1062 C CA  . THR A 137 ? 0.5182 0.8162 0.5201 0.0930  0.0289  -0.0658 433 THR A CA  
1063 C C   . THR A 137 ? 0.5654 0.9393 0.5922 0.0911  0.0368  -0.0550 433 THR A C   
1064 O O   . THR A 137 ? 0.6412 1.0529 0.6648 0.1198  0.0445  -0.0572 433 THR A O   
1065 C CB  . THR A 137 ? 0.6622 0.9466 0.6305 0.1086  0.0341  -0.0741 433 THR A CB  
1066 O OG1 . THR A 137 ? 0.6649 0.9796 0.6392 0.0896  0.0366  -0.0667 433 THR A OG1 
1067 C CG2 . THR A 137 ? 0.7789 0.9911 0.7172 0.1062  0.0259  -0.0859 433 THR A CG2 
1068 N N   . THR A 138 ? 0.6699 1.0677 0.7155 0.0588  0.0350  -0.0437 434 THR A N   
1069 C CA  . THR A 138 ? 0.6505 1.1218 0.7133 0.0460  0.0425  -0.0331 434 THR A CA  
1070 C C   . THR A 138 ? 0.6039 1.0741 0.6855 0.0143  0.0356  -0.0234 434 THR A C   
1071 O O   . THR A 138 ? 0.7204 1.1337 0.7994 0.0023  0.0258  -0.0238 434 THR A O   
1072 C CB  . THR A 138 ? 0.7217 1.2179 0.7708 0.0308  0.0496  -0.0280 434 THR A CB  
1073 O OG1 . THR A 138 ? 0.7676 1.2068 0.8028 0.0077  0.0414  -0.0254 434 THR A OG1 
1074 C CG2 . THR A 138 ? 0.7476 1.2529 0.7761 0.0641  0.0580  -0.0376 434 THR A CG2 
1075 N N   . ALA A 139 ? 0.6934 1.2311 0.7918 0.0013  0.0406  -0.0151 435 ALA A N   
1076 C CA  . ALA A 139 ? 0.5783 1.1130 0.6868 -0.0330 0.0342  -0.0057 435 ALA A CA  
1077 C C   . ALA A 139 ? 0.6693 1.1593 0.7546 -0.0671 0.0305  0.0018  435 ALA A C   
1078 O O   . ALA A 139 ? 0.7111 1.1525 0.7902 -0.0850 0.0215  0.0055  435 ALA A O   
1079 C CB  . ALA A 139 ? 0.6208 1.2448 0.7479 -0.0455 0.0404  0.0014  435 ALA A CB  
1080 N N   . HIS A 140 ? 0.6278 1.1299 0.6945 -0.0730 0.0374  0.0040  436 HIS A N   
1081 C CA  . HIS A 140 ? 0.6634 1.1129 0.6982 -0.0986 0.0335  0.0106  436 HIS A CA  
1082 C C   . HIS A 140 ? 0.6066 0.9803 0.6321 -0.0826 0.0225  0.0039  436 HIS A C   
1083 O O   . HIS A 140 ? 0.5685 0.8909 0.5730 -0.0989 0.0145  0.0095  436 HIS A O   
1084 C CB  . HIS A 140 ? 0.6784 1.1545 0.6939 -0.1020 0.0434  0.0128  436 HIS A CB  
1085 C CG  . HIS A 140 ? 0.7422 1.2847 0.7537 -0.1356 0.0533  0.0238  436 HIS A CG  
1086 N ND1 . HIS A 140 ? 0.7722 1.4066 0.8128 -0.1291 0.0620  0.0230  436 HIS A ND1 
1087 C CD2 . HIS A 140 ? 0.7125 1.2446 0.6900 -0.1780 0.0557  0.0359  436 HIS A CD2 
1088 C CE1 . HIS A 140 ? 0.7981 1.4868 0.8283 -0.1692 0.0698  0.0339  436 HIS A CE1 
1089 N NE2 . HIS A 140 ? 0.7512 1.3736 0.7402 -0.2020 0.0663  0.0421  436 HIS A NE2 
1090 N N   . GLY A 141 ? 0.6372 1.0034 0.6729 -0.0508 0.0217  -0.0082 437 GLY A N   
1091 C CA  . GLY A 141 ? 0.6813 0.9905 0.7123 -0.0398 0.0112  -0.0152 437 GLY A CA  
1092 C C   . GLY A 141 ? 0.7314 1.0188 0.7766 -0.0450 0.0031  -0.0141 437 GLY A C   
1093 O O   . GLY A 141 ? 0.7676 1.0131 0.8025 -0.0486 -0.0058 -0.0135 437 GLY A O   
1094 N N   . MET A 142 ? 0.6997 1.0184 0.7674 -0.0420 0.0061  -0.0140 438 MET A N   
1095 C CA  . MET A 142 ? 0.6061 0.9060 0.6854 -0.0493 -0.0010 -0.0119 438 MET A CA  
1096 C C   . MET A 142 ? 0.5425 0.8197 0.6024 -0.0774 -0.0052 -0.0011 438 MET A C   
1097 O O   . MET A 142 ? 0.6366 0.8684 0.6865 -0.0785 -0.0137 -0.0008 438 MET A O   
1098 C CB  . MET A 142 ? 0.5314 0.8743 0.6342 -0.0425 0.0028  -0.0122 438 MET A CB  
1099 C CG  . MET A 142 ? 0.4525 0.8002 0.5616 -0.0103 0.0058  -0.0229 438 MET A CG  
1100 S SD  . MET A 142 ? 0.5883 0.9963 0.7176 0.0042  0.0109  -0.0214 438 MET A SD  
1101 C CE  . MET A 142 ? 0.7347 1.1126 0.8765 -0.0101 0.0011  -0.0183 438 MET A CE  
1102 N N   . PHE A 143 ? 0.5683 0.8747 0.6163 -0.1004 0.0011  0.0080  439 PHE A N   
1103 C CA  . PHE A 143 ? 0.5917 0.8628 0.6060 -0.1316 -0.0025 0.0188  439 PHE A CA  
1104 C C   . PHE A 143 ? 0.7521 0.9569 0.7330 -0.1238 -0.0098 0.0187  439 PHE A C   
1105 O O   . PHE A 143 ? 0.7039 0.8558 0.6568 -0.1321 -0.0174 0.0233  439 PHE A O   
1106 C CB  . PHE A 143 ? 0.6252 0.9380 0.6245 -0.1613 0.0066  0.0280  439 PHE A CB  
1107 C CG  . PHE A 143 ? 0.8035 1.0639 0.7508 -0.1972 0.0035  0.0394  439 PHE A CG  
1108 C CD1 . PHE A 143 ? 0.8479 1.0849 0.7560 -0.2081 0.0069  0.0449  439 PHE A CD1 
1109 C CD2 . PHE A 143 ? 0.5884 0.8142 0.5179 -0.2196 -0.0029 0.0448  439 PHE A CD2 
1110 C CE1 . PHE A 143 ? 0.9410 1.1157 0.7882 -0.2409 0.0039  0.0560  439 PHE A CE1 
1111 C CE2 . PHE A 143 ? 0.7769 0.9397 0.6448 -0.2528 -0.0060 0.0552  439 PHE A CE2 
1112 C CZ  . PHE A 143 ? 0.9268 1.0608 0.7510 -0.2633 -0.0026 0.0610  439 PHE A CZ  
1113 N N   . ASN A 144 ? 0.7799 0.9869 0.7602 -0.1047 -0.0082 0.0127  440 ASN A N   
1114 C CA  . ASN A 144 ? 0.6869 0.8426 0.6359 -0.0943 -0.0157 0.0124  440 ASN A CA  
1115 C C   . ASN A 144 ? 0.7253 0.8568 0.6873 -0.0735 -0.0255 0.0049  440 ASN A C   
1116 O O   . ASN A 144 ? 0.7468 0.8334 0.6798 -0.0687 -0.0337 0.0080  440 ASN A O   
1117 C CB  . ASN A 144 ? 0.7333 0.9046 0.6789 -0.0815 -0.0117 0.0075  440 ASN A CB  
1118 C CG  . ASN A 144 ? 0.7482 0.8732 0.6538 -0.0746 -0.0190 0.0099  440 ASN A CG  
1119 O OD1 . ASN A 144 ? 0.8272 0.9163 0.6893 -0.0912 -0.0195 0.0208  440 ASN A OD1 
1120 N ND2 . ASN A 144 ? 0.8179 0.9416 0.7326 -0.0507 -0.0252 0.0000  440 ASN A ND2 
1121 N N   . TYR A 145 ? 0.6671 0.8271 0.6672 -0.0595 -0.0246 -0.0050 441 TYR A N   
1122 C CA  . TYR A 145 ? 0.6843 0.8294 0.6977 -0.0451 -0.0326 -0.0120 441 TYR A CA  
1123 C C   . TYR A 145 ? 0.7464 0.8682 0.7543 -0.0534 -0.0369 -0.0060 441 TYR A C   
1124 O O   . TYR A 145 ? 0.8205 0.9150 0.8162 -0.0428 -0.0448 -0.0070 441 TYR A O   
1125 C CB  . TYR A 145 ? 0.5528 0.7238 0.5980 -0.0349 -0.0297 -0.0225 441 TYR A CB  
1126 C CG  . TYR A 145 ? 0.5351 0.7099 0.5781 -0.0231 -0.0306 -0.0325 441 TYR A CG  
1127 C CD1 . TYR A 145 ? 0.4637 0.6559 0.5070 -0.0184 -0.0231 -0.0369 441 TYR A CD1 
1128 C CD2 . TYR A 145 ? 0.6281 0.7923 0.6661 -0.0161 -0.0392 -0.0380 441 TYR A CD2 
1129 C CE1 . TYR A 145 ? 0.5732 0.7614 0.6072 -0.0101 -0.0244 -0.0469 441 TYR A CE1 
1130 C CE2 . TYR A 145 ? 0.6466 0.8176 0.6805 -0.0108 -0.0409 -0.0476 441 TYR A CE2 
1131 C CZ  . TYR A 145 ? 0.6590 0.8365 0.6886 -0.0093 -0.0337 -0.0522 441 TYR A CZ  
1132 O OH  . TYR A 145 ? 0.7205 0.8971 0.7384 -0.0065 -0.0360 -0.0624 441 TYR A OH  
1133 N N   . ILE A 146 ? 0.6621 0.7986 0.6774 -0.0712 -0.0320 -0.0002 442 ILE A N   
1134 C CA  . ILE A 146 ? 0.6629 0.7751 0.6689 -0.0827 -0.0362 0.0052  442 ILE A CA  
1135 C C   . ILE A 146 ? 0.7883 0.8440 0.7414 -0.0903 -0.0415 0.0134  442 ILE A C   
1136 O O   . ILE A 146 ? 0.7079 0.7242 0.6423 -0.0817 -0.0486 0.0137  442 ILE A O   
1137 C CB  . ILE A 146 ? 0.5966 0.7455 0.6194 -0.1034 -0.0303 0.0098  442 ILE A CB  
1138 C CG1 . ILE A 146 ? 0.6097 0.8013 0.6755 -0.0867 -0.0270 0.0013  442 ILE A CG1 
1139 C CG2 . ILE A 146 ? 0.5598 0.6779 0.5624 -0.1223 -0.0352 0.0164  442 ILE A CG2 
1140 C CD1 . ILE A 146 ? 0.6258 0.8677 0.7105 -0.0983 -0.0213 0.0048  442 ILE A CD1 
1141 N N   . CYS A 147 ? 0.8188 0.8652 0.7407 -0.1039 -0.0379 0.0200  443 CYS A N   
1142 C CA  . CYS A 147 ? 0.7307 0.7096 0.5883 -0.1103 -0.0429 0.0285  443 CYS A CA  
1143 C C   . CYS A 147 ? 0.7142 0.6607 0.5556 -0.0752 -0.0518 0.0234  443 CYS A C   
1144 O O   . CYS A 147 ? 0.8780 0.7654 0.6732 -0.0666 -0.0589 0.0273  443 CYS A O   
1145 C CB  . CYS A 147 ? 0.7714 0.7477 0.5973 -0.1303 -0.0368 0.0360  443 CYS A CB  
1146 S SG  . CYS A 147 ? 0.8466 0.8377 0.6545 -0.1820 -0.0286 0.0472  443 CYS A SG  
1147 N N   . ASN A 148 ? 0.7016 0.6875 0.5764 -0.0539 -0.0518 0.0145  444 ASN A N   
1148 C CA  . ASN A 148 ? 0.7163 0.6922 0.5836 -0.0219 -0.0606 0.0085  444 ASN A CA  
1149 C C   . ASN A 148 ? 0.7277 0.7071 0.6156 -0.0093 -0.0653 0.0035  444 ASN A C   
1150 O O   . ASN A 148 ? 0.7620 0.7187 0.6255 0.0155  -0.0731 0.0024  444 ASN A O   
1151 C CB  . ASN A 148 ? 0.7837 0.8066 0.6825 -0.0099 -0.0597 -0.0008 444 ASN A CB  
1152 C CG  . ASN A 148 ? 0.7721 0.7851 0.6402 -0.0137 -0.0572 0.0038  444 ASN A CG  
1153 O OD1 . ASN A 148 ? 0.8405 0.8086 0.6603 -0.0254 -0.0564 0.0146  444 ASN A OD1 
1154 N ND2 . ASN A 148 ? 0.7515 0.8014 0.6416 -0.0063 -0.0560 -0.0042 444 ASN A ND2 
1155 N N   . HIS A 149 ? 0.6393 0.6492 0.5695 -0.0233 -0.0604 0.0003  445 HIS A N   
1156 C CA  . HIS A 149 ? 0.6464 0.6579 0.5942 -0.0153 -0.0638 -0.0035 445 HIS A CA  
1157 C C   . HIS A 149 ? 0.6899 0.6434 0.5911 -0.0177 -0.0679 0.0044  445 HIS A C   
1158 O O   . HIS A 149 ? 0.7288 0.6627 0.6136 0.0051  -0.0741 0.0022  445 HIS A O   
1159 C CB  . HIS A 149 ? 0.6312 0.6811 0.6262 -0.0297 -0.0576 -0.0074 445 HIS A CB  
1160 C CG  . HIS A 149 ? 0.6200 0.6708 0.6324 -0.0253 -0.0600 -0.0106 445 HIS A CG  
1161 N ND1 . HIS A 149 ? 0.5476 0.6326 0.5996 -0.0236 -0.0576 -0.0184 445 HIS A ND1 
1162 C CD2 . HIS A 149 ? 0.6621 0.6791 0.6521 -0.0230 -0.0642 -0.0069 445 HIS A CD2 
1163 C CE1 . HIS A 149 ? 0.6121 0.6895 0.6694 -0.0211 -0.0600 -0.0190 445 HIS A CE1 
1164 N NE2 . HIS A 149 ? 0.6899 0.7283 0.7116 -0.0195 -0.0640 -0.0125 445 HIS A NE2 
1165 N N   . VAL A 150 ? 0.6063 0.5324 0.4812 -0.0460 -0.0644 0.0134  446 VAL A N   
1166 C CA  . VAL A 150 ? 0.6598 0.5178 0.4772 -0.0548 -0.0686 0.0210  446 VAL A CA  
1167 C C   . VAL A 150 ? 0.9014 0.6991 0.6562 -0.0267 -0.0759 0.0233  446 VAL A C   
1168 O O   . VAL A 150 ? 0.9835 0.7398 0.7059 -0.0052 -0.0820 0.0226  446 VAL A O   
1169 C CB  . VAL A 150 ? 0.8122 0.6557 0.6057 -0.0978 -0.0635 0.0306  446 VAL A CB  
1170 C CG1 . VAL A 150 ? 0.8359 0.5941 0.5543 -0.1117 -0.0686 0.0384  446 VAL A CG1 
1171 C CG2 . VAL A 150 ? 0.8025 0.7116 0.6552 -0.1183 -0.0575 0.0282  446 VAL A CG2 
1172 N N   . LYS A 151 ? 0.9203 0.7121 0.6534 -0.0225 -0.0755 0.0260  447 LYS A N   
1173 C CA  . LYS A 151 ? 0.9687 0.7001 0.6346 0.0087  -0.0832 0.0289  447 LYS A CA  
1174 C C   . LYS A 151 ? 0.9500 0.7116 0.6375 0.0539  -0.0899 0.0195  447 LYS A C   
1175 O O   . LYS A 151 ? 0.9478 0.6585 0.5837 0.0833  -0.0968 0.0206  447 LYS A O   
1176 C CB  . LYS A 151 ? 0.9833 0.7134 0.6288 0.0074  -0.0817 0.0325  447 LYS A CB  
1177 C CG  . LYS A 151 ? 1.1164 0.7597 0.6689 0.0303  -0.0890 0.0398  447 LYS A CG  
1178 C CD  . LYS A 151 ? 1.0912 0.7347 0.6252 0.0226  -0.0864 0.0443  447 LYS A CD  
1179 C CE  . LYS A 151 ? 1.2213 0.7593 0.6465 0.0308  -0.0915 0.0552  447 LYS A CE  
1180 N NZ  . LYS A 151 ? 1.1253 0.6722 0.5403 0.0150  -0.0868 0.0599  447 LYS A NZ  
1181 N N   . TYR A 152 ? 0.8292 0.6741 0.5889 0.0589  -0.0877 0.0099  448 TYR A N   
1182 C CA  . TYR A 152 ? 0.9051 0.7942 0.6903 0.0938  -0.0932 0.0006  448 TYR A CA  
1183 C C   . TYR A 152 ? 0.8301 0.7068 0.6163 0.1010  -0.0945 -0.0010 448 TYR A C   
1184 O O   . TYR A 152 ? 0.9858 0.8384 0.7336 0.1365  -0.1009 -0.0017 448 TYR A O   
1185 C CB  . TYR A 152 ? 0.8472 0.8198 0.7030 0.0858  -0.0899 -0.0092 448 TYR A CB  
1186 C CG  . TYR A 152 ? 0.8834 0.9107 0.7670 0.1119  -0.0948 -0.0189 448 TYR A CG  
1187 C CD1 . TYR A 152 ? 0.9274 0.9838 0.7982 0.1423  -0.1020 -0.0227 448 TYR A CD1 
1188 C CD2 . TYR A 152 ? 0.7431 0.7970 0.6627 0.1057  -0.0924 -0.0237 448 TYR A CD2 
1189 C CE1 . TYR A 152 ? 0.8703 0.9904 0.7668 0.1635  -0.1064 -0.0315 448 TYR A CE1 
1190 C CE2 . TYR A 152 ? 0.7923 0.9029 0.7353 0.1257  -0.0960 -0.0321 448 TYR A CE2 
1191 C CZ  . TYR A 152 ? 0.8410 0.9892 0.7737 0.1535  -0.1029 -0.0362 448 TYR A CZ  
1192 O OH  . TYR A 152 ? 0.8839 1.1036 0.8408 0.1712  -0.1065 -0.0447 448 TYR A OH  
1193 N N   . ALA A 153 ? 0.7413 0.6350 0.5681 0.0711  -0.0884 -0.0018 449 ALA A N   
1194 C CA  . ALA A 153 ? 0.8109 0.6996 0.6437 0.0773  -0.0894 -0.0042 449 ALA A CA  
1195 C C   . ALA A 153 ? 0.9511 0.7526 0.7077 0.0873  -0.0939 0.0030  449 ALA A C   
1196 O O   . ALA A 153 ? 0.9092 0.6977 0.6516 0.1095  -0.0970 0.0002  449 ALA A O   
1197 C CB  . ALA A 153 ? 0.6612 0.5774 0.5437 0.0437  -0.0827 -0.0052 449 ALA A CB  
1198 N N   . THR A 154 ? 0.8670 0.6039 0.5678 0.0696  -0.0941 0.0121  450 THR A N   
1199 C CA  . THR A 154 ? 1.0069 0.6450 0.6209 0.0746  -0.0988 0.0190  450 THR A CA  
1200 C C   . THR A 154 ? 1.1399 0.7387 0.6935 0.1288  -0.1067 0.0180  450 THR A C   
1201 O O   . THR A 154 ? 1.2426 0.7912 0.7476 0.1559  -0.1112 0.0173  450 THR A O   
1202 C CB  . THR A 154 ? 1.0640 0.6436 0.6308 0.0314  -0.0961 0.0295  450 THR A CB  
1203 O OG1 . THR A 154 ? 1.0488 0.6767 0.6728 -0.0130 -0.0893 0.0297  450 THR A OG1 
1204 C CG2 . THR A 154 ? 1.1900 0.6507 0.6507 0.0317  -0.1015 0.0367  450 THR A CG2 
1205 N N   . ASN A 155 ? 1.1188 0.7433 0.6735 0.1486  -0.1087 0.0173  451 ASN A N   
1206 C CA  . ASN A 155 ? 1.0515 0.6624 0.5594 0.2067  -0.1170 0.0152  451 ASN A CA  
1207 C C   . ASN A 155 ? 1.2035 0.6929 0.5996 0.2311  -0.1229 0.0218  451 ASN A C   
1208 O O   . ASN A 155 ? 1.3132 0.7918 0.6771 0.2818  -0.1285 0.0177  451 ASN A O   
1209 C CB  . ASN A 155 ? 1.0006 0.7106 0.5743 0.2393  -0.1184 0.0037  451 ASN A CB  
1210 C CG  . ASN A 155 ? 1.2096 0.9386 0.7503 0.3001  -0.1269 0.0003  451 ASN A CG  
1211 O OD1 . ASN A 155 ? 1.2269 0.9226 0.7203 0.3157  -0.1313 0.0050  451 ASN A OD1 
1212 N ND2 . ASN A 155 ? 1.1875 0.9763 0.7525 0.3359  -0.1291 -0.0079 451 ASN A ND2 
1213 N N   . LYS A 156 ? 1.3062 0.7021 0.6369 0.1937  -0.1213 0.0321  452 LYS A N   
1214 C CA  . LYS A 156 ? 1.4463 0.7038 0.6509 0.2081  -0.1270 0.0397  452 LYS A CA  
1215 C C   . LYS A 156 ? 1.6151 0.8409 0.7996 0.2237  -0.1290 0.0356  452 LYS A C   
1216 O O   . LYS A 156 ? 1.8252 0.9647 0.9168 0.2699  -0.1357 0.0363  452 LYS A O   
1217 C CB  . LYS A 156 ? 1.6385 0.8498 0.7667 0.2681  -0.1353 0.0416  452 LYS A CB  
1218 C CG  . LYS A 156 ? 1.7252 0.9804 0.8776 0.2637  -0.1346 0.0440  452 LYS A CG  
1219 C CD  . LYS A 156 ? 1.8277 0.9923 0.8678 0.3138  -0.1435 0.0500  452 LYS A CD  
1220 C CE  . LYS A 156 ? 1.9458 1.0762 0.9266 0.3881  -0.1522 0.0452  452 LYS A CE  
1221 N NZ  . LYS A 156 ? 1.9667 1.2410 1.0464 0.4287  -0.1538 0.0326  452 LYS A NZ  
1222 N N   . GLY A 157 ? 1.4606 0.7562 0.7299 0.1891  -0.1230 0.0309  453 GLY A N   
1223 C CA  . GLY A 157 ? 1.4546 0.7318 0.7163 0.1985  -0.1239 0.0266  453 GLY A CA  
1224 C C   . GLY A 157 ? 1.4566 0.8271 0.7809 0.2478  -0.1245 0.0157  453 GLY A C   
1225 O O   . GLY A 157 ? 1.3385 0.7250 0.6861 0.2472  -0.1228 0.0110  453 GLY A O   
1226 N N   . ASN A 158 ? 1.4732 0.9110 0.8252 0.2877  -0.1268 0.0115  454 ASN A N   
1227 C CA  . ASN A 158 ? 1.4121 0.9603 0.8342 0.3240  -0.1264 0.0008  454 ASN A CA  
1228 C C   . ASN A 158 ? 1.2613 0.9160 0.7979 0.2775  -0.1189 -0.0035 454 ASN A C   
1229 O O   . ASN A 158 ? 1.2274 0.9641 0.8189 0.2794  -0.1183 -0.0075 454 ASN A O   
1230 C CB  . ASN A 158 ? 1.4187 1.0014 0.8188 0.3852  -0.1330 -0.0023 454 ASN A CB  
1231 C CG  . ASN A 158 ? 1.4741 1.1860 0.9486 0.4165  -0.1323 -0.0135 454 ASN A CG  
1232 O OD1 . ASN A 158 ? 1.4567 1.2029 0.9697 0.4079  -0.1278 -0.0183 454 ASN A OD1 
1233 N ND2 . ASN A 158 ? 1.4665 1.2544 0.9606 0.4495  -0.1366 -0.0175 454 ASN A ND2 
1234 N N   . LEU A 159 ? 1.0322 0.6810 0.5988 0.2363  -0.1137 -0.0030 455 LEU A N   
1235 C CA  . LEU A 159 ? 0.9658 0.6869 0.6205 0.1890  -0.1068 -0.0048 455 LEU A CA  
1236 C C   . LEU A 159 ? 0.9035 0.7380 0.6366 0.2029  -0.1047 -0.0144 455 LEU A C   
1237 O O   . LEU A 159 ? 0.9199 0.7918 0.6574 0.2380  -0.1064 -0.0206 455 LEU A O   
1238 C CB  . LEU A 159 ? 1.0702 0.7707 0.7391 0.1523  -0.1029 -0.0032 455 LEU A CB  
1239 C CG  . LEU A 159 ? 1.1512 0.7779 0.7795 0.1077  -0.1021 0.0059  455 LEU A CG  
1240 C CD1 . LEU A 159 ? 1.1614 0.6897 0.6919 0.1186  -0.1074 0.0133  455 LEU A CD1 
1241 C CD2 . LEU A 159 ? 1.2362 0.8330 0.8557 0.0902  -0.1018 0.0060  455 LEU A CD2 
1242 N N   . ARG A 160 ? 0.8175 0.7066 0.6082 0.1732  -0.1007 -0.0159 456 ARG A N   
1243 C CA  . ARG A 160 ? 0.6981 0.6858 0.5563 0.1747  -0.0986 -0.0249 456 ARG A CA  
1244 C C   . ARG A 160 ? 0.6459 0.6637 0.5629 0.1307  -0.0914 -0.0265 456 ARG A C   
1245 O O   . ARG A 160 ? 0.6846 0.6724 0.6010 0.1018  -0.0885 -0.0211 456 ARG A O   
1246 C CB  . ARG A 160 ? 0.7277 0.7493 0.5864 0.1884  -0.1023 -0.0267 456 ARG A CB  
1247 C CG  . ARG A 160 ? 0.9344 0.9268 0.7296 0.2386  -0.1103 -0.0249 456 ARG A CG  
1248 C CD  . ARG A 160 ? 0.9212 0.9558 0.7176 0.2561  -0.1151 -0.0272 456 ARG A CD  
1249 N NE  . ARG A 160 ? 0.8491 0.8333 0.6247 0.2318  -0.1140 -0.0201 456 ARG A NE  
1250 C CZ  . ARG A 160 ? 0.9439 0.9255 0.6908 0.2507  -0.1192 -0.0184 456 ARG A CZ  
1251 N NH1 . ARG A 160 ? 0.9346 0.9633 0.6707 0.2964  -0.1269 -0.0233 456 ARG A NH1 
1252 N NH2 . ARG A 160 ? 0.8106 0.7470 0.5381 0.2256  -0.1168 -0.0116 456 ARG A NH2 
1253 N N   . SER A 161 ? 0.6338 0.7138 0.5981 0.1268  -0.0885 -0.0339 457 SER A N   
1254 C CA  . SER A 161 ? 0.6908 0.7930 0.7024 0.0907  -0.0821 -0.0358 457 SER A CA  
1255 C C   . SER A 161 ? 0.5922 0.7220 0.6272 0.0740  -0.0804 -0.0381 457 SER A C   
1256 O O   . SER A 161 ? 0.5787 0.7489 0.6180 0.0868  -0.0835 -0.0430 457 SER A O   
1257 C CB  . SER A 161 ? 0.6460 0.7994 0.6911 0.0896  -0.0794 -0.0427 457 SER A CB  
1258 O OG  . SER A 161 ? 0.7687 0.9027 0.7884 0.1123  -0.0811 -0.0416 457 SER A OG  
1259 N N   . ALA A 162 ? 0.5932 0.7054 0.6418 0.0472  -0.0757 -0.0350 458 ALA A N   
1260 C CA  . ALA A 162 ? 0.6025 0.7343 0.6680 0.0334  -0.0731 -0.0375 458 ALA A CA  
1261 C C   . ALA A 162 ? 0.5671 0.6969 0.6567 0.0093  -0.0668 -0.0373 458 ALA A C   
1262 O O   . ALA A 162 ? 0.7175 0.8261 0.8069 0.0016  -0.0650 -0.0328 458 ALA A O   
1263 C CB  . ALA A 162 ? 0.5937 0.6959 0.6269 0.0389  -0.0754 -0.0315 458 ALA A CB  
1264 N N   . ILE A 163 ? 0.5737 0.7245 0.6792 -0.0003 -0.0638 -0.0424 459 ILE A N   
1265 C CA  . ILE A 163 ? 0.5238 0.6695 0.6424 -0.0150 -0.0579 -0.0423 459 ILE A CA  
1266 C C   . ILE A 163 ? 0.5673 0.7197 0.6825 -0.0174 -0.0558 -0.0447 459 ILE A C   
1267 O O   . ILE A 163 ? 0.5615 0.7306 0.6737 -0.0141 -0.0586 -0.0505 459 ILE A O   
1268 C CB  . ILE A 163 ? 0.4493 0.6046 0.5847 -0.0231 -0.0554 -0.0484 459 ILE A CB  
1269 C CG1 . ILE A 163 ? 0.4151 0.5586 0.5553 -0.0299 -0.0499 -0.0476 459 ILE A CG1 
1270 C CG2 . ILE A 163 ? 0.4225 0.6020 0.5604 -0.0275 -0.0567 -0.0576 459 ILE A CG2 
1271 C CD1 . ILE A 163 ? 0.3396 0.4770 0.4849 -0.0365 -0.0477 -0.0522 459 ILE A CD1 
1272 N N   . THR A 164 ? 0.5437 0.6887 0.6589 -0.0227 -0.0508 -0.0405 460 THR A N   
1273 C CA  . THR A 164 ? 0.5455 0.6972 0.6563 -0.0231 -0.0471 -0.0430 460 THR A CA  
1274 C C   . THR A 164 ? 0.5722 0.7248 0.6911 -0.0243 -0.0414 -0.0472 460 THR A C   
1275 O O   . THR A 164 ? 0.7045 0.8577 0.8311 -0.0247 -0.0387 -0.0427 460 THR A O   
1276 C CB  . THR A 164 ? 0.5292 0.6768 0.6264 -0.0255 -0.0452 -0.0343 460 THR A CB  
1277 O OG1 . THR A 164 ? 0.5814 0.7142 0.6582 -0.0208 -0.0511 -0.0305 460 THR A OG1 
1278 C CG2 . THR A 164 ? 0.5922 0.7516 0.6856 -0.0242 -0.0401 -0.0373 460 THR A CG2 
1279 N N   . ILE A 165 ? 0.5707 0.7208 0.6821 -0.0237 -0.0402 -0.0560 461 ILE A N   
1280 C CA  . ILE A 165 ? 0.4776 0.6122 0.5824 -0.0217 -0.0360 -0.0617 461 ILE A CA  
1281 C C   . ILE A 165 ? 0.6032 0.7365 0.6933 -0.0124 -0.0307 -0.0642 461 ILE A C   
1282 O O   . ILE A 165 ? 0.5544 0.6826 0.6295 -0.0146 -0.0316 -0.0706 461 ILE A O   
1283 C CB  . ILE A 165 ? 0.5799 0.7002 0.6750 -0.0327 -0.0388 -0.0708 461 ILE A CB  
1284 C CG1 . ILE A 165 ? 0.5251 0.6538 0.6356 -0.0395 -0.0424 -0.0682 461 ILE A CG1 
1285 C CG2 . ILE A 165 ? 0.6436 0.7302 0.7159 -0.0304 -0.0344 -0.0763 461 ILE A CG2 
1286 C CD1 . ILE A 165 ? 0.5272 0.6625 0.6325 -0.0549 -0.0458 -0.0761 461 ILE A CD1 
1287 N N   . PHE A 166 ? 0.6154 0.7584 0.7088 -0.0011 -0.0253 -0.0596 462 PHE A N   
1288 C CA  . PHE A 166 ? 0.5291 0.6797 0.6089 0.0130  -0.0189 -0.0614 462 PHE A CA  
1289 C C   . PHE A 166 ? 0.7024 0.8164 0.7528 0.0259  -0.0164 -0.0711 462 PHE A C   
1290 O O   . PHE A 166 ? 0.7154 0.7982 0.7564 0.0187  -0.0196 -0.0753 462 PHE A O   
1291 C CB  . PHE A 166 ? 0.4814 0.6708 0.5774 0.0192  -0.0142 -0.0523 462 PHE A CB  
1292 C CG  . PHE A 166 ? 0.6740 0.8861 0.7814 0.0026  -0.0157 -0.0432 462 PHE A CG  
1293 C CD1 . PHE A 166 ? 0.6258 0.8463 0.7226 0.0000  -0.0134 -0.0424 462 PHE A CD1 
1294 C CD2 . PHE A 166 ? 0.6087 0.8247 0.7292 -0.0109 -0.0197 -0.0356 462 PHE A CD2 
1295 C CE1 . PHE A 166 ? 0.7343 0.9625 0.8298 -0.0161 -0.0149 -0.0335 462 PHE A CE1 
1296 C CE2 . PHE A 166 ? 0.5679 0.7883 0.6844 -0.0272 -0.0214 -0.0272 462 PHE A CE2 
1297 C CZ  . PHE A 166 ? 0.7305 0.9548 0.8327 -0.0299 -0.0190 -0.0259 462 PHE A CZ  
1298 N N   . PRO A 167 ? 0.7780 0.8893 0.8060 0.0442  -0.0105 -0.0752 463 PRO A N   
1299 C CA  . PRO A 167 ? 0.7938 0.8530 0.7779 0.0581  -0.0086 -0.0853 463 PRO A CA  
1300 C C   . PRO A 167 ? 0.7427 0.7783 0.7169 0.0707  -0.0083 -0.0846 463 PRO A C   
1301 O O   . PRO A 167 ? 0.7539 0.8267 0.7534 0.0821  -0.0067 -0.0767 463 PRO A O   
1302 C CB  . PRO A 167 ? 0.7792 0.8513 0.7444 0.0833  -0.0012 -0.0876 463 PRO A CB  
1303 C CG  . PRO A 167 ? 0.8676 0.9831 0.8594 0.0689  -0.0014 -0.0823 463 PRO A CG  
1304 C CD  . PRO A 167 ? 0.7506 0.8977 0.7829 0.0508  -0.0055 -0.0720 463 PRO A CD  
1305 N N   . GLN A 168 ? 0.7833 0.7546 0.7154 0.0661  -0.0102 -0.0928 464 GLN A N   
1306 C CA  . GLN A 168 ? 0.7190 0.6528 0.6293 0.0772  -0.0103 -0.0925 464 GLN A CA  
1307 C C   . GLN A 168 ? 0.8486 0.7767 0.7311 0.1214  -0.0045 -0.0926 464 GLN A C   
1308 O O   . GLN A 168 ? 0.7905 0.7233 0.6534 0.1429  0.0003  -0.0965 464 GLN A O   
1309 C CB  . GLN A 168 ? 0.7479 0.6060 0.6082 0.0559  -0.0132 -0.1013 464 GLN A CB  
1310 C CG  . GLN A 168 ? 0.7939 0.5914 0.5899 0.0646  -0.0109 -0.1120 464 GLN A CG  
1311 C CD  . GLN A 168 ? 1.0320 0.7823 0.7944 0.0235  -0.0155 -0.1207 464 GLN A CD  
1312 O OE1 . GLN A 168 ? 1.0451 0.8368 0.8476 -0.0093 -0.0201 -0.1191 464 GLN A OE1 
1313 N NE2 . GLN A 168 ? 1.2328 0.8963 0.9161 0.0253  -0.0143 -0.1302 464 GLN A NE2 
1314 N N   . ARG A 169 ? 0.7888 0.7107 0.6683 0.1379  -0.0050 -0.0884 465 ARG A N   
1315 C CA  . ARG A 169 ? 0.9123 0.8257 0.7572 0.1861  -0.0005 -0.0892 465 ARG A CA  
1316 C C   . ARG A 169 ? 1.1217 0.9407 0.8836 0.2032  0.0015  -0.1004 465 ARG A C   
1317 O O   . ARG A 169 ? 1.1551 0.8985 0.8772 0.1753  -0.0019 -0.1061 465 ARG A O   
1318 C CB  . ARG A 169 ? 1.0230 0.9383 0.8728 0.1994  -0.0032 -0.0831 465 ARG A CB  
1319 C CG  . ARG A 169 ? 1.1582 1.0663 0.9668 0.2561  0.0004  -0.0841 465 ARG A CG  
1320 C CD  . ARG A 169 ? 1.1662 1.0723 0.9736 0.2715  -0.0033 -0.0784 465 ARG A CD  
1321 N NE  . ARG A 169 ? 1.1604 1.1726 1.0387 0.2687  -0.0047 -0.0687 465 ARG A NE  
1322 C CZ  . ARG A 169 ? 1.0570 1.0908 0.9775 0.2358  -0.0098 -0.0622 465 ARG A CZ  
1323 N NH1 . ARG A 169 ? 1.0788 1.0445 0.9827 0.2059  -0.0132 -0.0642 465 ARG A NH1 
1324 N NH2 . ARG A 169 ? 0.9762 1.1004 0.9516 0.2314  -0.0113 -0.0540 465 ARG A NH2 
1325 N N   . THR A 170 ? 1.1987 1.0228 0.9301 0.2478  0.0073  -0.1037 466 THR A N   
1326 C CA  . THR A 170 ? 1.2699 0.9953 0.9092 0.2738  0.0096  -0.1146 466 THR A CA  
1327 C C   . THR A 170 ? 1.3344 1.0380 0.9271 0.3338  0.0121  -0.1139 466 THR A C   
1328 O O   . THR A 170 ? 1.3929 1.0281 0.9433 0.3379  0.0086  -0.1135 466 THR A O   
1329 C CB  . THR A 170 ? 1.2468 0.9858 0.8752 0.2825  0.0145  -0.1209 466 THR A CB  
1330 O OG1 . THR A 170 ? 1.1687 1.0177 0.8539 0.3081  0.0200  -0.1140 466 THR A OG1 
1331 C CG2 . THR A 170 ? 1.2201 0.9564 0.8718 0.2265  0.0106  -0.1239 466 THR A CG2 
1332 N N   . ASP A 171 ? 1.4100 1.1764 1.0090 0.3822  0.0184  -0.1135 467 ASP A N   
1333 C CA  . ASP A 171 ? 1.5633 1.3258 1.1196 0.4482  0.0207  -0.1130 467 ASP A CA  
1334 C C   . ASP A 171 ? 1.4659 1.3096 1.0835 0.4513  0.0172  -0.1018 467 ASP A C   
1335 O O   . ASP A 171 ? 1.7123 1.5217 1.2872 0.4912  0.0151  -0.1007 467 ASP A O   
1336 C CB  . ASP A 171 ? 1.7084 1.5301 1.2562 0.5002  0.0291  -0.1162 467 ASP A CB  
1337 C CG  . ASP A 171 ? 1.7283 1.7046 1.3760 0.4884  0.0325  -0.1070 467 ASP A CG  
1338 O OD1 . ASP A 171 ? 1.7030 1.7158 1.4151 0.4293  0.0295  -0.1017 467 ASP A OD1 
1339 O OD2 . ASP A 171 ? 1.7780 1.8394 1.4356 0.5380  0.0382  -0.1048 467 ASP A OD2 
1340 N N   . GLY A 172 ? 1.2709 1.2164 0.9810 0.4105  0.0161  -0.0935 468 GLY A N   
1341 C CA  . GLY A 172 ? 1.1931 1.2256 0.9614 0.4117  0.0129  -0.0832 468 GLY A CA  
1342 C C   . GLY A 172 ? 1.2147 1.3848 1.0435 0.4242  0.0179  -0.0774 468 GLY A C   
1343 O O   . GLY A 172 ? 1.0794 1.3306 0.9768 0.3892  0.0153  -0.0686 468 GLY A O   
1344 N N   . LYS A 173 ? 1.3542 1.5510 1.1533 0.4724  0.0253  -0.0823 469 LYS A N   
1345 C CA  . LYS A 173 ? 1.4269 1.7616 1.2798 0.4816  0.0317  -0.0772 469 LYS A CA  
1346 C C   . LYS A 173 ? 1.3505 1.7127 1.2401 0.4344  0.0358  -0.0765 469 LYS A C   
1347 O O   . LYS A 173 ? 1.2589 1.7338 1.1983 0.4239  0.0407  -0.0704 469 LYS A O   
1348 C CB  . LYS A 173 ? 1.6267 1.9905 1.4322 0.5584  0.0388  -0.0827 469 LYS A CB  
1349 C CG  . LYS A 173 ? 1.6900 2.2090 1.5483 0.5641  0.0414  -0.0733 469 LYS A CG  
1350 C CD  . LYS A 173 ? 1.6721 2.2712 1.5933 0.5333  0.0349  -0.0632 469 LYS A CD  
1351 C CE  . LYS A 173 ? 1.5789 2.2887 1.5777 0.4777  0.0387  -0.0559 469 LYS A CE  
1352 N NZ  . LYS A 173 ? 1.4742 2.2303 1.5268 0.4360  0.0312  -0.0472 469 LYS A NZ  
1353 N N   . HIS A 174 ? 1.3817 1.6456 1.2441 0.4048  0.0336  -0.0825 470 HIS A N   
1354 C CA  . HIS A 174 ? 1.3485 1.6274 1.2481 0.3527  0.0342  -0.0805 470 HIS A CA  
1355 C C   . HIS A 174 ? 1.3839 1.6297 1.3142 0.3008  0.0252  -0.0757 470 HIS A C   
1356 O O   . HIS A 174 ? 1.5094 1.6610 1.4041 0.2915  0.0201  -0.0811 470 HIS A O   
1357 C CB  . HIS A 174 ? 1.3617 1.5656 1.2098 0.3578  0.0375  -0.0910 470 HIS A CB  
1358 C CG  . HIS A 174 ? 1.4063 1.6302 1.2133 0.4148  0.0466  -0.0971 470 HIS A CG  
1359 N ND1 . HIS A 174 ? 1.5313 1.6649 1.2562 0.4631  0.0475  -0.1072 470 HIS A ND1 
1360 C CD2 . HIS A 174 ? 1.4151 1.7394 1.2469 0.4330  0.0557  -0.0944 470 HIS A CD2 
1361 C CE1 . HIS A 174 ? 1.6074 1.7843 1.3081 0.5136  0.0567  -0.1111 470 HIS A CE1 
1362 N NE2 . HIS A 174 ? 1.5296 1.8285 1.2979 0.4956  0.0621  -0.1035 470 HIS A NE2 
1363 N N   . ASP A 175 ? 1.2797 1.6019 1.2705 0.2667  0.0236  -0.0658 471 ASP A N   
1364 C CA  . ASP A 175 ? 1.0868 1.3878 1.1054 0.2269  0.0153  -0.0606 471 ASP A CA  
1365 C C   . ASP A 175 ? 0.9726 1.3243 1.0371 0.1823  0.0147  -0.0529 471 ASP A C   
1366 O O   . ASP A 175 ? 1.0674 1.5042 1.1609 0.1783  0.0184  -0.0459 471 ASP A O   
1367 C CB  . ASP A 175 ? 1.0964 1.4274 1.1265 0.2433  0.0117  -0.0555 471 ASP A CB  
1368 C CG  . ASP A 175 ? 1.0513 1.2913 1.0445 0.2513  0.0061  -0.0598 471 ASP A CG  
1369 O OD1 . ASP A 175 ? 1.1187 1.2778 1.0572 0.2694  0.0076  -0.0686 471 ASP A OD1 
1370 O OD2 . ASP A 175 ? 1.0542 1.3014 1.0688 0.2371  0.0004  -0.0543 471 ASP A OD2 
1371 N N   . PHE A 176 ? 0.7816 1.0821 0.8476 0.1489  0.0101  -0.0541 472 PHE A N   
1372 C CA  . PHE A 176 ? 0.7366 1.0680 0.8363 0.1092  0.0077  -0.0462 472 PHE A CA  
1373 C C   . PHE A 176 ? 0.6443 0.9885 0.7689 0.0911  0.0015  -0.0391 472 PHE A C   
1374 O O   . PHE A 176 ? 0.5505 0.8459 0.6674 0.0912  -0.0037 -0.0419 472 PHE A O   
1375 C CB  . PHE A 176 ? 0.7719 1.0492 0.8615 0.0870  0.0040  -0.0502 472 PHE A CB  
1376 C CG  . PHE A 176 ? 0.6778 0.9502 0.7464 0.0964  0.0093  -0.0557 472 PHE A CG  
1377 C CD1 . PHE A 176 ? 0.6082 0.8406 0.6383 0.1252  0.0123  -0.0658 472 PHE A CD1 
1378 C CD2 . PHE A 176 ? 0.7671 1.0682 0.8468 0.0768  0.0111  -0.0508 472 PHE A CD2 
1379 C CE1 . PHE A 176 ? 0.8531 1.0782 0.8596 0.1342  0.0171  -0.0717 472 PHE A CE1 
1380 C CE2 . PHE A 176 ? 0.8317 1.1292 0.8912 0.0854  0.0159  -0.0557 472 PHE A CE2 
1381 C CZ  . PHE A 176 ? 0.8144 1.0761 0.8388 0.1144  0.0189  -0.0665 472 PHE A CZ  
1382 N N   . ARG A 177 ? 0.5207 0.9295 0.6709 0.0729  0.0024  -0.0301 473 ARG A N   
1383 C CA  . ARG A 177 ? 0.5487 0.9691 0.7180 0.0523  -0.0039 -0.0234 473 ARG A CA  
1384 C C   . ARG A 177 ? 0.5611 1.0073 0.7421 0.0125  -0.0048 -0.0147 473 ARG A C   
1385 O O   . ARG A 177 ? 0.5214 1.0190 0.7049 0.0047  0.0011  -0.0109 473 ARG A O   
1386 C CB  . ARG A 177 ? 0.6136 1.0905 0.7923 0.0750  -0.0032 -0.0215 473 ARG A CB  
1387 C CG  . ARG A 177 ? 0.4882 0.9263 0.6438 0.1167  -0.0035 -0.0289 473 ARG A CG  
1388 C CD  . ARG A 177 ? 0.6653 1.0332 0.8141 0.1057  -0.0107 -0.0304 473 ARG A CD  
1389 N NE  . ARG A 177 ? 0.6728 1.0636 0.8468 0.0760  -0.0166 -0.0229 473 ARG A NE  
1390 C CZ  . ARG A 177 ? 0.7556 1.1828 0.9396 0.0837  -0.0200 -0.0190 473 ARG A CZ  
1391 N NH1 . ARG A 177 ? 0.7443 1.1926 0.9160 0.1244  -0.0182 -0.0216 473 ARG A NH1 
1392 N NH2 . ARG A 177 ? 0.7538 1.1937 0.9550 0.0529  -0.0258 -0.0129 473 ARG A NH2 
1393 N N   . VAL A 178 ? 0.6090 1.0152 0.7907 -0.0123 -0.0119 -0.0115 474 VAL A N   
1394 C CA  . VAL A 178 ? 0.5904 1.0125 0.7727 -0.0496 -0.0144 -0.0023 474 VAL A CA  
1395 C C   . VAL A 178 ? 0.6872 1.1576 0.8845 -0.0557 -0.0170 0.0020  474 VAL A C   
1396 O O   . VAL A 178 ? 0.7064 1.1528 0.9081 -0.0461 -0.0224 -0.0001 474 VAL A O   
1397 C CB  . VAL A 178 ? 0.6267 0.9794 0.7940 -0.0674 -0.0212 -0.0014 474 VAL A CB  
1398 C CG1 . VAL A 178 ? 0.5815 0.9325 0.7324 -0.1050 -0.0235 0.0080  474 VAL A CG1 
1399 C CG2 . VAL A 178 ? 0.5812 0.8928 0.7364 -0.0555 -0.0202 -0.0073 474 VAL A CG2 
1400 N N   . TRP A 179 ? 0.6759 1.2205 0.8808 -0.0725 -0.0132 0.0080  475 TRP A N   
1401 C CA  . TRP A 179 ? 0.6495 1.2545 0.8699 -0.0791 -0.0164 0.0118  475 TRP A CA  
1402 C C   . TRP A 179 ? 0.6235 1.1938 0.8336 -0.1179 -0.0247 0.0173  475 TRP A C   
1403 O O   . TRP A 179 ? 0.6141 1.2079 0.8343 -0.1188 -0.0301 0.0184  475 TRP A O   
1404 C CB  . TRP A 179 ? 0.6188 1.3291 0.8514 -0.0877 -0.0096 0.0162  475 TRP A CB  
1405 C CG  . TRP A 179 ? 0.5819 1.3405 0.8247 -0.0375 -0.0025 0.0100  475 TRP A CG  
1406 C CD1 . TRP A 179 ? 0.5553 1.2586 0.7861 0.0008  0.0007  0.0018  475 TRP A CD1 
1407 C CD2 . TRP A 179 ? 0.5451 1.4153 0.8058 -0.0179 0.0020  0.0110  475 TRP A CD2 
1408 N NE1 . TRP A 179 ? 0.7112 1.4726 0.9447 0.0446  0.0070  -0.0025 475 TRP A NE1 
1409 C CE2 . TRP A 179 ? 0.6314 1.4999 0.8852 0.0376  0.0081  0.0031  475 TRP A CE2 
1410 C CE3 . TRP A 179 ? 0.5115 1.4865 0.7904 -0.0422 0.0012  0.0175  475 TRP A CE3 
1411 C CZ2 . TRP A 179 ? 0.5978 1.5637 0.8608 0.0768  0.0136  0.0014  475 TRP A CZ2 
1412 C CZ3 . TRP A 179 ? 0.5365 1.5873 0.8145 -0.0061 0.0062  0.0156  475 TRP A CZ3 
1413 C CH2 . TRP A 179 ? 0.5188 1.5722 0.7925 0.0548  0.0123  0.0079  475 TRP A CH2 
1414 N N   . ASN A 180 ? 0.5236 1.0337 0.7080 -0.1468 -0.0264 0.0206  476 ASN A N   
1415 C CA  . ASN A 180 ? 0.6276 1.0841 0.7896 -0.1773 -0.0345 0.0246  476 ASN A CA  
1416 C C   . ASN A 180 ? 0.6064 1.0131 0.7749 -0.1519 -0.0403 0.0189  476 ASN A C   
1417 O O   . ASN A 180 ? 0.5432 0.9234 0.7204 -0.1190 -0.0384 0.0121  476 ASN A O   
1418 C CB  . ASN A 180 ? 0.7066 1.0944 0.8301 -0.2002 -0.0350 0.0281  476 ASN A CB  
1419 C CG  . ASN A 180 ? 0.7392 1.1661 0.8484 -0.2299 -0.0288 0.0346  476 ASN A CG  
1420 O OD1 . ASN A 180 ? 0.8241 1.3008 0.9522 -0.2123 -0.0210 0.0324  476 ASN A OD1 
1421 N ND2 . ASN A 180 ? 0.7044 1.1039 0.7737 -0.2764 -0.0319 0.0424  476 ASN A ND2 
1422 N N   . SER A 181 ? 0.5871 0.9800 0.7474 -0.1708 -0.0474 0.0216  477 SER A N   
1423 C CA  . SER A 181 ? 0.5486 0.8910 0.7107 -0.1503 -0.0523 0.0169  477 SER A CA  
1424 C C   . SER A 181 ? 0.6294 0.8906 0.7652 -0.1498 -0.0543 0.0152  477 SER A C   
1425 O O   . SER A 181 ? 0.5189 0.7479 0.6616 -0.1244 -0.0547 0.0092  477 SER A O   
1426 C CB  . SER A 181 ? 0.5207 0.8755 0.6813 -0.1673 -0.0593 0.0197  477 SER A CB  
1427 O OG  . SER A 181 ? 0.7273 1.1098 0.8702 -0.2105 -0.0615 0.0267  477 SER A OG  
1428 N N   . GLN A 182 ? 0.6996 0.9286 0.8008 -0.1773 -0.0555 0.0204  478 GLN A N   
1429 C CA  . GLN A 182 ? 0.6498 0.8104 0.7211 -0.1706 -0.0567 0.0193  478 GLN A CA  
1430 C C   . GLN A 182 ? 0.6122 0.7729 0.6605 -0.1889 -0.0528 0.0243  478 GLN A C   
1431 O O   . GLN A 182 ? 0.6886 0.8881 0.7316 -0.2192 -0.0507 0.0302  478 GLN A O   
1432 C CB  . GLN A 182 ? 0.8005 0.8921 0.8308 -0.1813 -0.0639 0.0211  478 GLN A CB  
1433 C CG  . GLN A 182 ? 0.7967 0.8881 0.8409 -0.1740 -0.0682 0.0181  478 GLN A CG  
1434 C CD  . GLN A 182 ? 0.8386 0.8616 0.8329 -0.1889 -0.0751 0.0205  478 GLN A CD  
1435 O OE1 . GLN A 182 ? 0.7750 0.7373 0.7204 -0.1944 -0.0770 0.0230  478 GLN A OE1 
1436 N NE2 . GLN A 182 ? 0.7166 0.7441 0.7166 -0.1935 -0.0793 0.0197  478 GLN A NE2 
1437 N N   . LEU A 183 ? 0.5644 0.6844 0.5967 -0.1720 -0.0522 0.0220  479 LEU A N   
1438 C CA  . LEU A 183 ? 0.6422 0.7552 0.6485 -0.1859 -0.0486 0.0268  479 LEU A CA  
1439 C C   . LEU A 183 ? 0.7931 0.8636 0.7436 -0.2261 -0.0517 0.0359  479 LEU A C   
1440 O O   . LEU A 183 ? 0.7333 0.8308 0.6706 -0.2569 -0.0473 0.0422  479 LEU A O   
1441 C CB  . LEU A 183 ? 0.5784 0.6504 0.5722 -0.1582 -0.0495 0.0226  479 LEU A CB  
1442 C CG  . LEU A 183 ? 0.6657 0.7642 0.7010 -0.1238 -0.0476 0.0130  479 LEU A CG  
1443 C CD1 . LEU A 183 ? 0.7724 0.8356 0.7881 -0.1037 -0.0500 0.0099  479 LEU A CD1 
1444 C CD2 . LEU A 183 ? 0.6601 0.8225 0.7305 -0.1207 -0.0401 0.0107  479 LEU A CD2 
1445 N N   . ILE A 184 ? 0.7045 0.7064 0.6161 -0.2281 -0.0589 0.0366  480 ILE A N   
1446 C CA  . ILE A 184 ? 0.6715 0.6145 0.5158 -0.2678 -0.0629 0.0447  480 ILE A CA  
1447 C C   . ILE A 184 ? 0.8166 0.7715 0.6668 -0.2873 -0.0674 0.0446  480 ILE A C   
1448 O O   . ILE A 184 ? 0.7926 0.7247 0.6520 -0.2623 -0.0718 0.0393  480 ILE A O   
1449 C CB  . ILE A 184 ? 0.9299 0.7690 0.7058 -0.2521 -0.0682 0.0458  480 ILE A CB  
1450 C CG1 . ILE A 184 ? 0.9690 0.8021 0.7351 -0.2378 -0.0643 0.0470  480 ILE A CG1 
1451 C CG2 . ILE A 184 ? 1.0304 0.7911 0.7236 -0.2935 -0.0731 0.0535  480 ILE A CG2 
1452 C CD1 . ILE A 184 ? 0.9827 0.7346 0.6980 -0.2038 -0.0698 0.0457  480 ILE A CD1 
1453 N N   . ARG A 185 ? 0.8477 0.8469 0.6945 -0.3328 -0.0661 0.0504  481 ARG A N   
1454 C CA  . ARG A 185 ? 0.9324 0.9519 0.7794 -0.3611 -0.0711 0.0515  481 ARG A CA  
1455 C C   . ARG A 185 ? 1.0493 1.0681 0.8460 -0.4252 -0.0714 0.0604  481 ARG A C   
1456 O O   . ARG A 185 ? 1.1807 1.2317 0.9735 -0.4454 -0.0649 0.0652  481 ARG A O   
1457 C CB  . ARG A 185 ? 0.8557 0.9819 0.7816 -0.3430 -0.0685 0.0470  481 ARG A CB  
1458 C CG  . ARG A 185 ? 1.0003 1.1196 0.9659 -0.2907 -0.0695 0.0386  481 ARG A CG  
1459 C CD  . ARG A 185 ? 0.8625 1.0499 0.8756 -0.2824 -0.0713 0.0356  481 ARG A CD  
1460 N NE  . ARG A 185 ? 0.9106 1.0576 0.8949 -0.3004 -0.0795 0.0362  481 ARG A NE  
1461 C CZ  . ARG A 185 ? 0.9450 1.1282 0.9589 -0.2906 -0.0831 0.0335  481 ARG A CZ  
1462 N NH1 . ARG A 185 ? 0.7644 1.0200 0.8333 -0.2609 -0.0793 0.0302  481 ARG A NH1 
1463 N NH2 . ARG A 185 ? 1.0433 1.1836 1.0248 -0.3090 -0.0908 0.0340  481 ARG A NH2 
1464 N N   . TYR A 186 ? 0.9109 0.8921 0.6655 -0.4600 -0.0789 0.0624  482 TYR A N   
1465 C CA  . TYR A 186 ? 1.0832 1.0645 0.7846 -0.5186 -0.0791 0.0696  482 TYR A CA  
1466 C C   . TYR A 186 ? 1.0515 1.1678 0.8126 -0.5274 -0.0748 0.0695  482 TYR A C   
1467 O O   . TYR A 186 ? 0.8415 1.0243 0.6664 -0.5012 -0.0763 0.0644  482 TYR A O   
1468 C CB  . TYR A 186 ? 1.1094 0.9850 0.7298 -0.5339 -0.0876 0.0700  482 TYR A CB  
1469 C CG  . TYR A 186 ? 1.3308 1.0656 0.8743 -0.5199 -0.0914 0.0706  482 TYR A CG  
1470 C CD1 . TYR A 186 ? 1.4387 1.0833 0.9475 -0.4944 -0.0992 0.0660  482 TYR A CD1 
1471 C CD2 . TYR A 186 ? 1.3582 1.0506 0.8606 -0.5268 -0.0871 0.0757  482 TYR A CD2 
1472 C CE1 . TYR A 186 ? 1.5271 1.0460 0.9611 -0.4697 -0.1023 0.0662  482 TYR A CE1 
1473 C CE2 . TYR A 186 ? 1.4334 0.9958 0.8596 -0.5060 -0.0908 0.0769  482 TYR A CE2 
1474 C CZ  . TYR A 186 ? 1.4676 0.9467 0.8603 -0.4729 -0.0982 0.0718  482 TYR A CZ  
1475 O OH  . TYR A 186 ? 1.5281 0.8888 0.8443 -0.4374 -0.1013 0.0718  482 TYR A OH  
1476 N N   . ALA A 187 ? 0.9885 1.1422 0.7221 -0.5630 -0.0699 0.0749  483 ALA A N   
1477 C CA  . ALA A 187 ? 1.0499 1.3353 0.8324 -0.5696 -0.0650 0.0753  483 ALA A CA  
1478 C C   . ALA A 187 ? 1.1087 1.4112 0.8778 -0.5876 -0.0712 0.0751  483 ALA A C   
1479 O O   . ALA A 187 ? 1.1555 1.3651 0.8562 -0.6120 -0.0781 0.0767  483 ALA A O   
1480 C CB  . ALA A 187 ? 1.1352 1.4551 0.8863 -0.6049 -0.0585 0.0808  483 ALA A CB  
1481 N N   . GLY A 188 ? 1.0449 1.4661 0.8752 -0.5732 -0.0686 0.0733  484 GLY A N   
1482 C CA  . GLY A 188 ? 1.2081 1.6647 1.0301 -0.5914 -0.0735 0.0739  484 GLY A CA  
1483 C C   . GLY A 188 ? 1.2297 1.7972 1.0547 -0.6181 -0.0687 0.0775  484 GLY A C   
1484 O O   . GLY A 188 ? 1.1270 1.8000 1.0110 -0.5900 -0.0623 0.0757  484 GLY A O   
1485 N N   . TYR A 189 ? 1.3216 1.8654 1.0779 -0.6719 -0.0722 0.0823  485 TYR A N   
1486 C CA  . TYR A 189 ? 1.3244 1.9736 1.0733 -0.7058 -0.0689 0.0859  485 TYR A CA  
1487 C C   . TYR A 189 ? 1.4087 2.0846 1.1441 -0.7261 -0.0749 0.0868  485 TYR A C   
1488 O O   . TYR A 189 ? 1.2812 1.8603 0.9527 -0.7565 -0.0819 0.0886  485 TYR A O   
1489 C CB  . TYR A 189 ? 1.4283 2.0358 1.0996 -0.7606 -0.0679 0.0910  485 TYR A CB  
1490 C CG  . TYR A 189 ? 1.3640 1.9002 1.0238 -0.7487 -0.0643 0.0909  485 TYR A CG  
1491 C CD1 . TYR A 189 ? 1.4236 1.8135 1.0262 -0.7516 -0.0694 0.0910  485 TYR A CD1 
1492 C CD2 . TYR A 189 ? 1.3663 1.9808 1.0669 -0.7338 -0.0558 0.0906  485 TYR A CD2 
1493 C CE1 . TYR A 189 ? 1.5169 1.8420 1.1052 -0.7404 -0.0662 0.0912  485 TYR A CE1 
1494 C CE2 . TYR A 189 ? 1.4094 1.9594 1.0977 -0.7250 -0.0523 0.0910  485 TYR A CE2 
1495 C CZ  . TYR A 189 ? 1.4626 1.8685 1.0948 -0.7291 -0.0575 0.0915  485 TYR A CZ  
1496 O OH  . TYR A 189 ? 1.3659 1.7073 0.9824 -0.7192 -0.0540 0.0923  485 TYR A OH  
1497 N N   . LYS A 190 ? 1.4696 2.2739 1.2612 -0.7067 -0.0722 0.0855  486 LYS A N   
1498 C CA  . LYS A 190 ? 1.5256 2.3796 1.3019 -0.7334 -0.0766 0.0874  486 LYS A CA  
1499 C C   . LYS A 190 ? 1.6240 2.4958 1.3278 -0.8033 -0.0764 0.0937  486 LYS A C   
1500 O O   . LYS A 190 ? 1.6398 2.5419 1.3295 -0.8210 -0.0712 0.0956  486 LYS A O   
1501 C CB  . LYS A 190 ? 1.4510 2.4419 1.3025 -0.6900 -0.0734 0.0842  486 LYS A CB  
1502 C CG  . LYS A 190 ? 1.4304 2.5087 1.3261 -0.6586 -0.0645 0.0826  486 LYS A CG  
1503 C CD  . LYS A 190 ? 1.3638 2.5817 1.3154 -0.6191 -0.0613 0.0799  486 LYS A CD  
1504 C CE  . LYS A 190 ? 1.2751 2.4810 1.2845 -0.5523 -0.0635 0.0737  486 LYS A CE  
1505 N NZ  . LYS A 190 ? 1.2430 2.5749 1.3017 -0.5015 -0.0585 0.0705  486 LYS A NZ  
1506 N N   . GLN A 191 ? 1.6653 2.5170 1.3193 -0.8450 -0.0824 0.0967  487 GLN A N   
1507 C CA  . GLN A 191 ? 1.7346 2.5887 1.3067 -0.9178 -0.0835 0.1025  487 GLN A CA  
1508 C C   . GLN A 191 ? 1.7071 2.7188 1.3017 -0.9365 -0.0809 0.1045  487 GLN A C   
1509 O O   . GLN A 191 ? 1.6292 2.7265 1.2912 -0.8948 -0.0800 0.1015  487 GLN A O   
1510 C CB  . GLN A 191 ? 1.8099 2.5305 1.2958 -0.9581 -0.0920 0.1051  487 GLN A CB  
1511 C CG  . GLN A 191 ? 1.8785 2.4367 1.3150 -0.9504 -0.0950 0.1040  487 GLN A CG  
1512 C CD  . GLN A 191 ? 2.0094 2.5372 1.3936 -0.9817 -0.0920 0.1062  487 GLN A CD  
1513 O OE1 . GLN A 191 ? 1.8865 2.4749 1.3248 -0.9544 -0.0854 0.1045  487 GLN A OE1 
1514 N NE2 . GLN A 191 ? 2.1967 2.6255 1.4702 -1.0391 -0.0972 0.1098  487 GLN A NE2 
1515 N N   . PRO A 192 ? 1.7793 2.8354 1.3153 -0.9986 -0.0798 0.1091  488 PRO A N   
1516 C CA  . PRO A 192 ? 1.7863 2.9986 1.3373 -1.0205 -0.0775 0.1111  488 PRO A CA  
1517 C C   . PRO A 192 ? 1.8466 3.0664 1.3895 -1.0335 -0.0827 0.1125  488 PRO A C   
1518 O O   . PRO A 192 ? 1.8533 3.2097 1.4369 -1.0248 -0.0805 0.1123  488 PRO A O   
1519 C CB  . PRO A 192 ? 1.8804 3.1052 1.3501 -1.0959 -0.0773 0.1159  488 PRO A CB  
1520 C CG  . PRO A 192 ? 1.9433 2.9893 1.3349 -1.1225 -0.0821 0.1170  488 PRO A CG  
1521 C CD  . PRO A 192 ? 1.8646 2.8387 1.3178 -1.0501 -0.0807 0.1122  488 PRO A CD  
1522 N N   . ASP A 193 ? 1.8671 2.9446 1.3564 -1.0517 -0.0896 0.1136  489 ASP A N   
1523 C CA  . ASP A 193 ? 1.8373 2.9074 1.3187 -1.0608 -0.0952 0.1145  489 ASP A CA  
1524 C C   . ASP A 193 ? 1.6422 2.6967 1.2026 -0.9875 -0.0973 0.1084  489 ASP A C   
1525 O O   . ASP A 193 ? 1.5621 2.5921 1.1177 -0.9890 -0.1031 0.1081  489 ASP A O   
1526 C CB  . ASP A 193 ? 1.9717 2.8933 1.3443 -1.1194 -0.1023 0.1187  489 ASP A CB  
1527 C CG  . ASP A 193 ? 1.9973 2.7564 1.3378 -1.0991 -0.1048 0.1165  489 ASP A CG  
1528 O OD1 . ASP A 193 ? 1.9724 2.7175 1.3034 -1.1000 -0.1010 0.1163  489 ASP A OD1 
1529 O OD2 . ASP A 193 ? 1.9869 2.6356 1.3113 -1.0807 -0.1107 0.1147  489 ASP A OD2 
1530 N N   . GLY A 194 ? 1.5794 2.6448 1.2078 -0.9256 -0.0931 0.1033  490 GLY A N   
1531 C CA  . GLY A 194 ? 1.5718 2.6341 1.2749 -0.8559 -0.0950 0.0970  490 GLY A CA  
1532 C C   . GLY A 194 ? 1.6532 2.5652 1.3476 -0.8299 -0.0990 0.0937  490 GLY A C   
1533 O O   . GLY A 194 ? 1.6652 2.5772 1.4247 -0.7687 -0.0982 0.0881  490 GLY A O   
1534 N N   . SER A 195 ? 1.7093 2.4933 1.3200 -0.8737 -0.1035 0.0969  491 SER A N   
1535 C CA  . SER A 195 ? 1.6906 2.3295 1.2830 -0.8492 -0.1079 0.0937  491 SER A CA  
1536 C C   . SER A 195 ? 1.6779 2.2973 1.2998 -0.8162 -0.1022 0.0913  491 SER A C   
1537 O O   . SER A 195 ? 1.6633 2.3824 1.3271 -0.8061 -0.0951 0.0915  491 SER A O   
1538 C CB  . SER A 195 ? 1.7407 2.2489 1.2239 -0.9025 -0.1138 0.0979  491 SER A CB  
1539 O OG  . SER A 195 ? 1.8024 2.3177 1.2191 -0.9594 -0.1109 0.1036  491 SER A OG  
1540 N N   . THR A 196 ? 1.6458 2.1364 1.2435 -0.7977 -0.1052 0.0887  492 THR A N   
1541 C CA  . THR A 196 ? 1.5100 1.9814 1.1430 -0.7607 -0.1002 0.0859  492 THR A CA  
1542 C C   . THR A 196 ? 1.5970 1.9263 1.1491 -0.7804 -0.1022 0.0876  492 THR A C   
1543 O O   . THR A 196 ? 1.6957 1.9113 1.1907 -0.7861 -0.1089 0.0869  492 THR A O   
1544 C CB  . THR A 196 ? 1.3374 1.8162 1.0488 -0.6965 -0.1014 0.0789  492 THR A CB  
1545 O OG1 . THR A 196 ? 1.2740 1.8838 1.0556 -0.6727 -0.0996 0.0771  492 THR A OG1 
1546 C CG2 . THR A 196 ? 1.1260 1.5808 0.8685 -0.6618 -0.0962 0.0763  492 THR A CG2 
1547 N N   . LEU A 197 ? 1.5383 1.8737 1.0827 -0.7875 -0.0964 0.0893  493 LEU A N   
1548 C CA  . LEU A 197 ? 1.4850 1.6925 0.9614 -0.7953 -0.0975 0.0902  493 LEU A CA  
1549 C C   . LEU A 197 ? 1.3363 1.5249 0.8727 -0.7392 -0.0942 0.0855  493 LEU A C   
1550 O O   . LEU A 197 ? 1.2569 1.5474 0.8792 -0.7066 -0.0883 0.0832  493 LEU A O   
1551 C CB  . LEU A 197 ? 1.5314 1.7520 0.9525 -0.8434 -0.0941 0.0950  493 LEU A CB  
1552 C CG  . LEU A 197 ? 1.6417 1.7299 0.9768 -0.8585 -0.0958 0.0961  493 LEU A CG  
1553 C CD1 . LEU A 197 ? 1.7191 1.6575 0.9653 -0.8645 -0.1045 0.0955  493 LEU A CD1 
1554 C CD2 . LEU A 197 ? 1.6712 1.7863 0.9482 -0.9149 -0.0938 0.1004  493 LEU A CD2 
1555 N N   . GLY A 198 ? 1.3171 1.3731 0.8025 -0.7266 -0.0982 0.0840  494 GLY A N   
1556 C CA  . GLY A 198 ? 1.4019 1.4321 0.9336 -0.6782 -0.0956 0.0800  494 GLY A CA  
1557 C C   . GLY A 198 ? 1.3212 1.3732 0.9207 -0.6339 -0.0986 0.0739  494 GLY A C   
1558 O O   . GLY A 198 ? 1.4626 1.4658 1.0349 -0.6350 -0.1054 0.0721  494 GLY A O   
1559 N N   . ASP A 199 ? 1.1126 1.2376 0.7971 -0.5950 -0.0938 0.0704  495 ASP A N   
1560 C CA  . ASP A 199 ? 0.9849 1.1267 0.7308 -0.5518 -0.0973 0.0637  495 ASP A CA  
1561 C C   . ASP A 199 ? 1.0720 1.3479 0.8917 -0.5391 -0.0949 0.0624  495 ASP A C   
1562 O O   . ASP A 199 ? 0.9895 1.3522 0.8598 -0.5236 -0.0877 0.0624  495 ASP A O   
1563 C CB  . ASP A 199 ? 0.9393 1.0519 0.7180 -0.5135 -0.0952 0.0598  495 ASP A CB  
1564 C CG  . ASP A 199 ? 1.0745 1.1671 0.8894 -0.4755 -0.1013 0.0526  495 ASP A CG  
1565 O OD1 . ASP A 199 ? 1.0230 1.1614 0.8648 -0.4706 -0.1051 0.0504  495 ASP A OD1 
1566 O OD2 . ASP A 199 ? 0.9756 1.0068 0.7888 -0.4513 -0.1027 0.0492  495 ASP A OD2 
1567 N N   . PRO A 200 ? 1.1153 1.4105 0.9394 -0.5416 -0.1006 0.0610  496 PRO A N   
1568 C CA  . PRO A 200 ? 1.0298 1.4510 0.9172 -0.5255 -0.0989 0.0599  496 PRO A CA  
1569 C C   . PRO A 200 ? 0.8547 1.3281 0.8182 -0.4707 -0.0968 0.0542  496 PRO A C   
1570 O O   . PRO A 200 ? 0.8532 1.4322 0.8644 -0.4504 -0.0928 0.0538  496 PRO A O   
1571 C CB  . PRO A 200 ? 1.1220 1.5270 0.9886 -0.5385 -0.1071 0.0593  496 PRO A CB  
1572 C CG  . PRO A 200 ? 1.1860 1.4683 0.9637 -0.5760 -0.1112 0.0622  496 PRO A CG  
1573 C CD  . PRO A 200 ? 1.1392 1.3410 0.9017 -0.5604 -0.1088 0.0608  496 PRO A CD  
1574 N N   . ALA A 201 ? 0.8297 1.2317 0.8000 -0.4452 -0.0994 0.0499  497 ALA A N   
1575 C CA  . ALA A 201 ? 0.8755 1.3213 0.9101 -0.3964 -0.0975 0.0449  497 ALA A CA  
1576 C C   . ALA A 201 ? 0.8893 1.4133 0.9562 -0.3840 -0.0876 0.0463  497 ALA A C   
1577 O O   . ALA A 201 ? 0.9507 1.5502 1.0683 -0.3451 -0.0848 0.0434  497 ALA A O   
1578 C CB  . ALA A 201 ? 0.7727 1.1263 0.7987 -0.3803 -0.1013 0.0410  497 ALA A CB  
1579 N N   . ASN A 202 ? 0.9223 1.4254 0.9537 -0.4151 -0.0823 0.0509  498 ASN A N   
1580 C CA  . ASN A 202 ? 0.9011 1.4580 0.9560 -0.4040 -0.0728 0.0519  498 ASN A CA  
1581 C C   . ASN A 202 ? 0.9021 1.5519 0.9554 -0.4235 -0.0667 0.0561  498 ASN A C   
1582 O O   . ASN A 202 ? 0.9112 1.6010 0.9714 -0.4226 -0.0585 0.0577  498 ASN A O   
1583 C CB  . ASN A 202 ? 0.9132 1.3851 0.9281 -0.4238 -0.0709 0.0543  498 ASN A CB  
1584 C CG  . ASN A 202 ? 0.8579 1.2363 0.8657 -0.4069 -0.0776 0.0502  498 ASN A CG  
1585 O OD1 . ASN A 202 ? 0.7598 1.1469 0.8094 -0.3578 -0.0767 0.0443  498 ASN A OD1 
1586 N ND2 . ASN A 202 ? 0.8944 1.1665 0.8357 -0.4345 -0.0817 0.0529  498 ASN A ND2 
1587 N N   . VAL A 203 ? 0.7313 1.4186 0.7731 -0.4422 -0.0706 0.0579  499 VAL A N   
1588 C CA  . VAL A 203 ? 0.7536 1.5287 0.7841 -0.4688 -0.0657 0.0623  499 VAL A CA  
1589 C C   . VAL A 203 ? 0.7728 1.6532 0.8544 -0.4275 -0.0575 0.0598  499 VAL A C   
1590 O O   . VAL A 203 ? 0.9522 1.8878 1.0249 -0.4432 -0.0505 0.0628  499 VAL A O   
1591 C CB  . VAL A 203 ? 0.8769 1.6828 0.8916 -0.4911 -0.0717 0.0640  499 VAL A CB  
1592 C CG1 . VAL A 203 ? 1.0145 1.9242 1.0191 -0.5181 -0.0667 0.0682  499 VAL A CG1 
1593 C CG2 . VAL A 203 ? 0.9449 1.6399 0.8976 -0.5329 -0.0793 0.0665  499 VAL A CG2 
1594 N N   . GLN A 204 ? 0.5970 1.5019 0.7263 -0.3728 -0.0586 0.0542  500 GLN A N   
1595 C CA  . GLN A 204 ? 0.7094 1.7011 0.8774 -0.3262 -0.0511 0.0511  500 GLN A CA  
1596 C C   . GLN A 204 ? 0.7620 1.7282 0.9350 -0.3162 -0.0438 0.0502  500 GLN A C   
1597 O O   . GLN A 204 ? 0.7765 1.8109 0.9558 -0.3076 -0.0356 0.0508  500 GLN A O   
1598 C CB  . GLN A 204 ? 0.8631 1.8710 1.0681 -0.2691 -0.0549 0.0454  500 GLN A CB  
1599 C CG  . GLN A 204 ? 0.9461 2.0587 1.1737 -0.2242 -0.0494 0.0432  500 GLN A CG  
1600 C CD  . GLN A 204 ? 0.9711 2.0727 1.2259 -0.1591 -0.0473 0.0369  500 GLN A CD  
1601 O OE1 . GLN A 204 ? 1.0668 2.1101 1.3263 -0.1522 -0.0449 0.0349  500 GLN A OE1 
1602 N NE2 . GLN A 204 ? 0.9210 2.0751 1.1876 -0.1105 -0.0481 0.0339  500 GLN A NE2 
1603 N N   . PHE A 205 ? 0.7461 1.6174 0.9145 -0.3173 -0.0468 0.0488  501 PHE A N   
1604 C CA  . PHE A 205 ? 0.6941 1.5389 0.8642 -0.3116 -0.0401 0.0483  501 PHE A CA  
1605 C C   . PHE A 205 ? 0.7845 1.6318 0.9151 -0.3608 -0.0352 0.0548  501 PHE A C   
1606 O O   . PHE A 205 ? 0.8148 1.7067 0.9525 -0.3531 -0.0266 0.0552  501 PHE A O   
1607 C CB  . PHE A 205 ? 0.5927 1.3374 0.7599 -0.3074 -0.0455 0.0458  501 PHE A CB  
1608 C CG  . PHE A 205 ? 0.7533 1.4709 0.9210 -0.3025 -0.0393 0.0454  501 PHE A CG  
1609 C CD1 . PHE A 205 ? 0.8138 1.5668 1.0161 -0.2527 -0.0329 0.0398  501 PHE A CD1 
1610 C CD2 . PHE A 205 ? 0.8607 1.5073 0.9844 -0.3443 -0.0394 0.0504  501 PHE A CD2 
1611 C CE1 . PHE A 205 ? 0.8188 1.5280 1.0095 -0.2410 -0.0260 0.0383  501 PHE A CE1 
1612 C CE2 . PHE A 205 ? 0.8848 1.4925 0.9993 -0.3310 -0.0329 0.0497  501 PHE A CE2 
1613 C CZ  . PHE A 205 ? 0.8321 1.4733 0.9820 -0.2798 -0.0262 0.0434  501 PHE A CZ  
1614 N N   . THR A 206 ? 0.8475 1.6420 0.9299 -0.4115 -0.0408 0.0597  502 THR A N   
1615 C CA  . THR A 206 ? 0.9015 1.6913 0.9345 -0.4623 -0.0375 0.0662  502 THR A CA  
1616 C C   . THR A 206 ? 0.9873 1.8983 1.0339 -0.4630 -0.0308 0.0673  502 THR A C   
1617 O O   . THR A 206 ? 0.9886 1.9219 1.0177 -0.4824 -0.0246 0.0703  502 THR A O   
1618 C CB  . THR A 206 ? 0.8780 1.5963 0.8499 -0.5130 -0.0456 0.0705  502 THR A CB  
1619 O OG1 . THR A 206 ? 0.9537 1.5529 0.9037 -0.5103 -0.0515 0.0693  502 THR A OG1 
1620 C CG2 . THR A 206 ? 0.8929 1.6052 0.8043 -0.5680 -0.0433 0.0769  502 THR A CG2 
1621 N N   . GLU A 207 ? 1.0323 2.0241 1.1075 -0.4409 -0.0324 0.0650  503 GLU A N   
1622 C CA  . GLU A 207 ? 1.1128 2.2263 1.1991 -0.4363 -0.0267 0.0656  503 GLU A CA  
1623 C C   . GLU A 207 ? 0.9997 2.1610 1.1236 -0.3853 -0.0180 0.0613  503 GLU A C   
1624 O O   . GLU A 207 ? 0.9891 2.2268 1.1088 -0.3905 -0.0118 0.0626  503 GLU A O   
1625 C CB  . GLU A 207 ? 1.1643 2.3496 1.2666 -0.4224 -0.0309 0.0642  503 GLU A CB  
1626 C CG  . GLU A 207 ? 1.2960 2.6113 1.3978 -0.4274 -0.0266 0.0657  503 GLU A CG  
1627 C CD  . GLU A 207 ? 1.4376 2.7638 1.4888 -0.4959 -0.0258 0.0720  503 GLU A CD  
1628 O OE1 . GLU A 207 ? 1.5076 2.7500 1.5137 -0.5471 -0.0315 0.0759  503 GLU A OE1 
1629 O OE2 . GLU A 207 ? 1.4468 2.8626 1.4979 -0.4981 -0.0201 0.0727  503 GLU A OE2 
1630 N N   . ILE A 208 ? 0.8834 1.9996 1.0395 -0.3371 -0.0179 0.0559  504 ILE A N   
1631 C CA  . ILE A 208 ? 0.7752 1.9218 0.9589 -0.2888 -0.0097 0.0514  504 ILE A CA  
1632 C C   . ILE A 208 ? 0.7481 1.8655 0.9107 -0.3180 -0.0035 0.0547  504 ILE A C   
1633 O O   . ILE A 208 ? 0.7390 1.9207 0.9061 -0.3055 0.0044  0.0543  504 ILE A O   
1634 C CB  . ILE A 208 ? 0.6377 1.7331 0.8521 -0.2363 -0.0120 0.0448  504 ILE A CB  
1635 C CG1 . ILE A 208 ? 0.5914 1.7311 0.8246 -0.1973 -0.0167 0.0412  504 ILE A CG1 
1636 C CG2 . ILE A 208 ? 0.5291 1.6304 0.7599 -0.1951 -0.0034 0.0402  504 ILE A CG2 
1637 C CD1 . ILE A 208 ? 0.6766 1.7497 0.9284 -0.1618 -0.0228 0.0360  504 ILE A CD1 
1638 N N   . CYS A 209 ? 0.7304 1.7492 0.8650 -0.3565 -0.0072 0.0583  505 CYS A N   
1639 C CA  . CYS A 209 ? 0.7831 1.7642 0.8899 -0.3859 -0.0018 0.0623  505 CYS A CA  
1640 C C   . CYS A 209 ? 0.9202 1.9656 0.9962 -0.4270 0.0014  0.0674  505 CYS A C   
1641 O O   . CYS A 209 ? 0.8988 1.9692 0.9700 -0.4294 0.0090  0.0685  505 CYS A O   
1642 C CB  . CYS A 209 ? 0.7625 1.6205 0.8314 -0.4206 -0.0081 0.0659  505 CYS A CB  
1643 S SG  . CYS A 209 ? 0.7883 1.5719 0.8901 -0.3770 -0.0126 0.0596  505 CYS A SG  
1644 N N   . ILE A 210 ? 0.9943 2.0700 1.0474 -0.4611 -0.0045 0.0703  506 ILE A N   
1645 C CA  . ILE A 210 ? 1.1049 2.2511 1.1269 -0.5032 -0.0026 0.0745  506 ILE A CA  
1646 C C   . ILE A 210 ? 1.0962 2.3711 1.1569 -0.4620 0.0040  0.0707  506 ILE A C   
1647 O O   . ILE A 210 ? 1.0099 2.3429 1.0574 -0.4792 0.0088  0.0726  506 ILE A O   
1648 C CB  . ILE A 210 ? 1.0877 2.2340 1.0702 -0.5530 -0.0110 0.0782  506 ILE A CB  
1649 C CG1 . ILE A 210 ? 1.0118 2.0208 0.9504 -0.5848 -0.0183 0.0809  506 ILE A CG1 
1650 C CG2 . ILE A 210 ? 1.2220 2.4314 1.1626 -0.6063 -0.0101 0.0825  506 ILE A CG2 
1651 C CD1 . ILE A 210 ? 1.1672 2.1664 1.0632 -0.6300 -0.0265 0.0839  506 ILE A CD1 
1652 N N   . GLN A 211 ? 1.0614 2.3790 1.1650 -0.4053 0.0038  0.0653  507 GLN A N   
1653 C CA  . GLN A 211 ? 1.0459 2.4717 1.1792 -0.3548 0.0096  0.0609  507 GLN A CA  
1654 C C   . GLN A 211 ? 0.9913 2.4084 1.1375 -0.3240 0.0184  0.0581  507 GLN A C   
1655 O O   . GLN A 211 ? 1.0205 2.5258 1.1766 -0.2945 0.0238  0.0557  507 GLN A O   
1656 C CB  . GLN A 211 ? 1.0542 2.5021 1.2203 -0.2967 0.0068  0.0553  507 GLN A CB  
1657 C CG  . GLN A 211 ? 1.1048 2.6161 1.2633 -0.3140 0.0006  0.0573  507 GLN A CG  
1658 C CD  . GLN A 211 ? 1.1212 2.7601 1.2927 -0.2719 0.0036  0.0544  507 GLN A CD  
1659 O OE1 . GLN A 211 ? 1.1213 2.7839 1.3110 -0.2136 0.0089  0.0494  507 GLN A OE1 
1660 N NE2 . GLN A 211 ? 1.1152 2.8360 1.2722 -0.3004 -0.0001 0.0575  507 GLN A NE2 
1661 N N   . GLN A 212 ? 0.9130 2.2277 1.0567 -0.3287 0.0198  0.0583  508 GLN A N   
1662 C CA  . GLN A 212 ? 0.8393 2.1377 0.9886 -0.3094 0.0286  0.0566  508 GLN A CA  
1663 C C   . GLN A 212 ? 0.8635 2.1281 0.9731 -0.3700 0.0308  0.0635  508 GLN A C   
1664 O O   . GLN A 212 ? 0.8535 2.0833 0.9611 -0.3634 0.0379  0.0634  508 GLN A O   
1665 C CB  . GLN A 212 ? 0.7418 1.9564 0.9131 -0.2711 0.0294  0.0517  508 GLN A CB  
1666 C CG  . GLN A 212 ? 0.8545 2.0888 1.0580 -0.2088 0.0269  0.0442  508 GLN A CG  
1667 C CD  . GLN A 212 ? 0.9751 2.2900 1.1914 -0.1530 0.0338  0.0386  508 GLN A CD  
1668 O OE1 . GLN A 212 ? 0.9484 2.2427 1.1724 -0.1138 0.0405  0.0333  508 GLN A OE1 
1669 N NE2 . GLN A 212 ? 1.0527 2.4592 1.2664 -0.1480 0.0319  0.0394  508 GLN A NE2 
1670 N N   . GLY A 213 ? 0.9475 2.2166 1.0199 -0.4292 0.0247  0.0692  509 GLY A N   
1671 C CA  . GLY A 213 ? 0.9791 2.2222 1.0040 -0.4878 0.0258  0.0754  509 GLY A CA  
1672 C C   . GLY A 213 ? 1.0335 2.1475 1.0090 -0.5360 0.0200  0.0806  509 GLY A C   
1673 O O   . GLY A 213 ? 0.9638 2.0376 0.8918 -0.5809 0.0209  0.0855  509 GLY A O   
1674 N N   . TRP A 214 ? 1.1631 2.2070 1.1428 -0.5272 0.0134  0.0796  510 TRP A N   
1675 C CA  . TRP A 214 ? 1.1987 2.1134 1.1231 -0.5685 0.0071  0.0843  510 TRP A CA  
1676 C C   . TRP A 214 ? 1.2655 2.1737 1.1257 -0.6339 0.0006  0.0891  510 TRP A C   
1677 O O   . TRP A 214 ? 1.2086 2.1927 1.0742 -0.6452 -0.0032 0.0884  510 TRP A O   
1678 C CB  . TRP A 214 ? 1.0953 1.9432 1.0361 -0.5450 0.0003  0.0817  510 TRP A CB  
1679 C CG  . TRP A 214 ? 1.0930 1.7990 0.9765 -0.5739 -0.0055 0.0858  510 TRP A CG  
1680 C CD1 . TRP A 214 ? 1.1162 1.7454 0.9703 -0.5794 -0.0018 0.0890  510 TRP A CD1 
1681 C CD2 . TRP A 214 ? 1.1837 1.8049 1.0255 -0.5972 -0.0161 0.0870  510 TRP A CD2 
1682 N NE1 . TRP A 214 ? 1.1626 1.6619 0.9565 -0.6015 -0.0099 0.0923  510 TRP A NE1 
1683 C CE2 . TRP A 214 ? 1.2167 1.7078 1.0016 -0.6123 -0.0188 0.0906  510 TRP A CE2 
1684 C CE3 . TRP A 214 ? 1.1952 1.8359 1.0384 -0.6047 -0.0233 0.0856  510 TRP A CE3 
1685 C CZ2 . TRP A 214 ? 1.2710 1.6490 0.9980 -0.6309 -0.0288 0.0919  510 TRP A CZ2 
1686 C CZ3 . TRP A 214 ? 1.2003 1.7315 0.9897 -0.6271 -0.0327 0.0871  510 TRP A CZ3 
1687 C CH2 . TRP A 214 ? 1.2758 1.6763 1.0068 -0.6382 -0.0355 0.0898  510 TRP A CH2 
1688 N N   . LYS A 215 ? 1.3516 2.1677 1.1458 -0.6770 -0.0010 0.0938  511 LYS A N   
1689 C CA  . LYS A 215 ? 1.4559 2.2403 1.1732 -0.7431 -0.0083 0.0976  511 LYS A CA  
1690 C C   . LYS A 215 ? 1.4502 2.1110 1.1201 -0.7572 -0.0180 0.0986  511 LYS A C   
1691 O O   . LYS A 215 ? 1.4577 1.9930 1.0836 -0.7591 -0.0201 0.1005  511 LYS A O   
1692 C CB  . LYS A 215 ? 1.5101 2.2578 1.1743 -0.7794 -0.0052 0.1011  511 LYS A CB  
1693 C CG  . LYS A 215 ? 1.5529 2.4246 1.2644 -0.7630 0.0047  0.0998  511 LYS A CG  
1694 C CD  . LYS A 215 ? 1.6143 2.6060 1.3194 -0.7986 0.0022  0.0994  511 LYS A CD  
1695 C CE  . LYS A 215 ? 1.5170 2.6305 1.2913 -0.7564 0.0032  0.0953  511 LYS A CE  
1696 N NZ  . LYS A 215 ? 1.5687 2.7802 1.3214 -0.7989 -0.0019 0.0960  511 LYS A NZ  
1697 N N   . ALA A 216 ? 1.4067 2.1037 1.0833 -0.7639 -0.0239 0.0973  512 ALA A N   
1698 C CA  . ALA A 216 ? 1.3668 1.9610 1.0128 -0.7654 -0.0324 0.0972  512 ALA A CA  
1699 C C   . ALA A 216 ? 1.4414 1.9274 0.9793 -0.8258 -0.0405 0.1006  512 ALA A C   
1700 O O   . ALA A 216 ? 1.5267 2.0611 1.0249 -0.8749 -0.0428 0.1021  512 ALA A O   
1701 C CB  . ALA A 216 ? 1.2888 1.9625 0.9803 -0.7497 -0.0352 0.0947  512 ALA A CB  
1702 N N   . PRO A 217 ? 1.4273 1.7661 0.9093 -0.8234 -0.0454 0.1012  513 PRO A N   
1703 C CA  . PRO A 217 ? 1.5835 1.8059 0.9519 -0.8748 -0.0545 0.1029  513 PRO A CA  
1704 C C   . PRO A 217 ? 1.8143 2.0192 1.1566 -0.8912 -0.0626 0.1023  513 PRO A C   
1705 O O   . PRO A 217 ? 1.9487 2.0242 1.2016 -0.9118 -0.0707 0.1024  513 PRO A O   
1706 C CB  . PRO A 217 ? 1.5743 1.6482 0.8965 -0.8515 -0.0563 0.1031  513 PRO A CB  
1707 C CG  . PRO A 217 ? 1.4287 1.5373 0.8445 -0.7893 -0.0506 0.1016  513 PRO A CG  
1708 C CD  . PRO A 217 ? 1.3456 1.6192 0.8558 -0.7755 -0.0419 0.1005  513 PRO A CD  
1709 N N   . ARG A 218 ? 1.8313 2.1637 1.2462 -0.8801 -0.0603 0.1014  514 ARG A N   
1710 C CA  . ARG A 218 ? 1.7674 2.1115 1.1784 -0.8891 -0.0662 0.1011  514 ARG A CA  
1711 C C   . ARG A 218 ? 1.7978 1.9864 1.1152 -0.9080 -0.0757 0.1014  514 ARG A C   
1712 O O   . ARG A 218 ? 2.0013 2.1535 1.2343 -0.9618 -0.0816 0.1035  514 ARG A O   
1713 C CB  . ARG A 218 ? 1.8198 2.2799 1.2223 -0.9358 -0.0661 0.1033  514 ARG A CB  
1714 C CG  . ARG A 218 ? 1.8349 2.3433 1.2557 -0.9378 -0.0700 0.1033  514 ARG A CG  
1715 C CD  . ARG A 218 ? 1.7690 2.4530 1.2716 -0.9222 -0.0641 0.1026  514 ARG A CD  
1716 N NE  . ARG A 218 ? 1.7316 2.4902 1.2940 -0.8896 -0.0556 0.1009  514 ARG A NE  
1717 C CZ  . ARG A 218 ? 1.6283 2.5149 1.2775 -0.8446 -0.0494 0.0982  514 ARG A CZ  
1718 N NH1 . ARG A 218 ? 1.5566 2.4993 1.2493 -0.8159 -0.0417 0.0966  514 ARG A NH1 
1719 N NH2 . ARG A 218 ? 1.6419 2.5958 1.3300 -0.8260 -0.0511 0.0968  514 ARG A NH2 
1720 N N   . GLY A 219 ? 1.6556 1.7506 0.9817 -0.8634 -0.0774 0.0991  515 GLY A N   
1721 C CA  . GLY A 219 ? 1.7405 1.6872 0.9809 -0.8682 -0.0863 0.0983  515 GLY A CA  
1722 C C   . GLY A 219 ? 1.7192 1.6471 1.0127 -0.8182 -0.0886 0.0950  515 GLY A C   
1723 O O   . GLY A 219 ? 1.5560 1.5934 0.9470 -0.7898 -0.0847 0.0932  515 GLY A O   
1724 N N   . ARG A 220 ? 1.8338 1.6215 1.0593 -0.8048 -0.0954 0.0932  516 ARG A N   
1725 C CA  . ARG A 220 ? 1.8155 1.5720 1.0820 -0.7565 -0.0984 0.0891  516 ARG A CA  
1726 C C   . ARG A 220 ? 1.8207 1.5842 1.1552 -0.7047 -0.0935 0.0866  516 ARG A C   
1727 O O   . ARG A 220 ? 1.8154 1.6918 1.2510 -0.6812 -0.0878 0.0850  516 ARG A O   
1728 C CB  . ARG A 220 ? 1.8815 1.4838 1.0428 -0.7567 -0.1073 0.0876  516 ARG A CB  
1729 C CG  . ARG A 220 ? 1.8142 1.4046 0.9996 -0.7310 -0.1121 0.0841  516 ARG A CG  
1730 C CD  . ARG A 220 ? 1.8571 1.4511 0.9891 -0.7779 -0.1169 0.0867  516 ARG A CD  
1731 N NE  . ARG A 220 ? 1.9511 1.4536 1.0374 -0.7610 -0.1242 0.0838  516 ARG A NE  
1732 C CZ  . ARG A 220 ? 1.8262 1.3821 0.9700 -0.7471 -0.1260 0.0817  516 ARG A CZ  
1733 N NH1 . ARG A 220 ? 1.6557 1.3545 0.9021 -0.7463 -0.1214 0.0819  516 ARG A NH1 
1734 N NH2 . ARG A 220 ? 1.8941 1.3593 0.9883 -0.7318 -0.1326 0.0789  516 ARG A NH2 
1735 N N   . PHE A 221 ? 1.7753 1.4142 1.0467 -0.6858 -0.0961 0.0859  517 PHE A N   
1736 C CA  . PHE A 221 ? 1.5288 1.1491 0.8465 -0.6359 -0.0932 0.0838  517 PHE A CA  
1737 C C   . PHE A 221 ? 1.6403 1.3016 0.9782 -0.6415 -0.0851 0.0875  517 PHE A C   
1738 O O   . PHE A 221 ? 1.6156 1.1895 0.9013 -0.6296 -0.0849 0.0892  517 PHE A O   
1739 C CB  . PHE A 221 ? 1.5248 0.9937 0.7603 -0.6066 -0.1002 0.0813  517 PHE A CB  
1740 C CG  . PHE A 221 ? 1.6573 1.0761 0.8559 -0.6048 -0.1079 0.0778  517 PHE A CG  
1741 C CD1 . PHE A 221 ? 1.7505 1.0652 0.8332 -0.6300 -0.1143 0.0782  517 PHE A CD1 
1742 C CD2 . PHE A 221 ? 1.3275 0.8018 0.6028 -0.5787 -0.1091 0.0735  517 PHE A CD2 
1743 C CE1 . PHE A 221 ? 1.7950 1.0624 0.8399 -0.6281 -0.1209 0.0754  517 PHE A CE1 
1744 C CE2 . PHE A 221 ? 1.5197 0.9468 0.7596 -0.5765 -0.1159 0.0704  517 PHE A CE2 
1745 C CZ  . PHE A 221 ? 1.4917 0.8169 0.6173 -0.6012 -0.1214 0.0719  517 PHE A CZ  
1746 N N   . ASP A 222 ? 1.6122 1.4109 1.0243 -0.6570 -0.0783 0.0887  518 ASP A N   
1747 C CA  . ASP A 222 ? 1.4616 1.3251 0.9108 -0.6577 -0.0692 0.0915  518 ASP A CA  
1748 C C   . ASP A 222 ? 1.3950 1.3142 0.9389 -0.6089 -0.0645 0.0883  518 ASP A C   
1749 O O   . ASP A 222 ? 1.1753 1.1888 0.7978 -0.5910 -0.0637 0.0841  518 ASP A O   
1750 C CB  . ASP A 222 ? 1.3794 1.3663 0.8557 -0.6938 -0.0644 0.0932  518 ASP A CB  
1751 C CG  . ASP A 222 ? 1.4645 1.4094 0.8509 -0.7475 -0.0707 0.0953  518 ASP A CG  
1752 O OD1 . ASP A 222 ? 1.6400 1.4512 0.9357 -0.7562 -0.0783 0.0951  518 ASP A OD1 
1753 O OD2 . ASP A 222 ? 1.3720 1.4182 0.7742 -0.7799 -0.0682 0.0967  518 ASP A OD2 
1754 N N   . VAL A 223 ? 1.4054 1.2625 0.9361 -0.5866 -0.0621 0.0901  519 VAL A N   
1755 C CA  . VAL A 223 ? 1.2702 1.1767 0.8837 -0.5398 -0.0585 0.0859  519 VAL A CA  
1756 C C   . VAL A 223 ? 1.1069 1.1589 0.8016 -0.5418 -0.0487 0.0854  519 VAL A C   
1757 O O   . VAL A 223 ? 1.0907 1.1770 0.7667 -0.5704 -0.0420 0.0904  519 VAL A O   
1758 C CB  . VAL A 223 ? 1.2495 1.0662 0.8272 -0.4966 -0.0585 0.0851  519 VAL A CB  
1759 C CG1 . VAL A 223 ? 1.0480 0.9113 0.7066 -0.4275 -0.0573 0.0750  519 VAL A CG1 
1760 C CG2 . VAL A 223 ? 1.4159 1.0824 0.8909 -0.4993 -0.0676 0.0876  519 VAL A CG2 
1761 N N   . LEU A 224 ? 1.0714 1.2059 0.8499 -0.4992 -0.0480 0.0773  520 LEU A N   
1762 C CA  . LEU A 224 ? 0.9624 1.2324 0.8133 -0.4920 -0.0394 0.0757  520 LEU A CA  
1763 C C   . LEU A 224 ? 0.9384 1.2170 0.8082 -0.4564 -0.0312 0.0738  520 LEU A C   
1764 O O   . LEU A 224 ? 1.0028 1.1974 0.8517 -0.4232 -0.0336 0.0709  520 LEU A O   
1765 C CB  . LEU A 224 ? 0.7021 1.0391 0.6227 -0.4535 -0.0422 0.0678  520 LEU A CB  
1766 C CG  . LEU A 224 ? 0.8076 1.1656 0.7204 -0.4800 -0.0490 0.0686  520 LEU A CG  
1767 C CD1 . LEU A 224 ? 0.6257 0.9803 0.5799 -0.4423 -0.0557 0.0614  520 LEU A CD1 
1768 C CD2 . LEU A 224 ? 0.7973 1.2721 0.7348 -0.4891 -0.0429 0.0699  520 LEU A CD2 
1769 N N   . PRO A 225 ? 0.9791 1.3633 0.8870 -0.4616 -0.0215 0.0749  521 PRO A N   
1770 C CA  . PRO A 225 ? 0.9749 1.3732 0.9054 -0.4227 -0.0137 0.0714  521 PRO A CA  
1771 C C   . PRO A 225 ? 0.9232 1.3541 0.9167 -0.3597 -0.0140 0.0605  521 PRO A C   
1772 O O   . PRO A 225 ? 0.9043 1.3887 0.9366 -0.3476 -0.0166 0.0568  521 PRO A O   
1773 C CB  . PRO A 225 ? 0.9452 1.4505 0.8883 -0.4547 -0.0028 0.0768  521 PRO A CB  
1774 C CG  . PRO A 225 ? 0.9525 1.5360 0.9179 -0.4725 -0.0058 0.0766  521 PRO A CG  
1775 C CD  . PRO A 225 ? 1.0065 1.4969 0.9296 -0.4943 -0.0176 0.0780  521 PRO A CD  
1776 N N   . LEU A 226 ? 0.8379 1.2307 0.8351 -0.3211 -0.0118 0.0555  522 LEU A N   
1777 C CA  . LEU A 226 ? 0.7622 1.1819 0.8095 -0.2665 -0.0107 0.0451  522 LEU A CA  
1778 C C   . LEU A 226 ? 0.7608 1.2923 0.8498 -0.2544 -0.0016 0.0431  522 LEU A C   
1779 O O   . LEU A 226 ? 0.8139 1.3931 0.8954 -0.2730 0.0068  0.0476  522 LEU A O   
1780 C CB  . LEU A 226 ? 0.7529 1.1114 0.7883 -0.2362 -0.0106 0.0403  522 LEU A CB  
1781 C CG  . LEU A 226 ? 0.7733 1.0300 0.7719 -0.2317 -0.0198 0.0402  522 LEU A CG  
1782 C CD1 . LEU A 226 ? 0.7623 0.9799 0.7462 -0.2081 -0.0189 0.0370  522 LEU A CD1 
1783 C CD2 . LEU A 226 ? 0.6510 0.8912 0.6749 -0.2067 -0.0266 0.0333  522 LEU A CD2 
1784 N N   . LEU A 227 ? 0.6900 1.2634 0.8183 -0.2213 -0.0029 0.0366  523 LEU A N   
1785 C CA  . LEU A 227 ? 0.6587 1.3304 0.8216 -0.1939 0.0050  0.0330  523 LEU A CA  
1786 C C   . LEU A 227 ? 0.6640 1.3018 0.8401 -0.1387 0.0058  0.0224  523 LEU A C   
1787 O O   . LEU A 227 ? 0.5985 1.2103 0.7865 -0.1138 0.0001  0.0171  523 LEU A O   
1788 C CB  . LEU A 227 ? 0.5676 1.3183 0.7554 -0.1992 0.0025  0.0346  523 LEU A CB  
1789 C CG  . LEU A 227 ? 0.6521 1.5311 0.8573 -0.2135 0.0106  0.0389  523 LEU A CG  
1790 C CD1 . LEU A 227 ? 0.6060 1.5612 0.8434 -0.1770 0.0087  0.0346  523 LEU A CD1 
1791 C CD2 . LEU A 227 ? 0.6310 1.5446 0.8347 -0.1987 0.0223  0.0377  523 LEU A CD2 
1792 N N   . LEU A 228 ? 0.5564 1.1929 0.7256 -0.1224 0.0129  0.0193  524 LEU A N   
1793 C CA  . LEU A 228 ? 0.5611 1.1454 0.7291 -0.0810 0.0127  0.0093  524 LEU A CA  
1794 C C   . LEU A 228 ? 0.5786 1.2227 0.7583 -0.0408 0.0212  0.0030  524 LEU A C   
1795 O O   . LEU A 228 ? 0.4567 1.1589 0.6349 -0.0441 0.0301  0.0054  524 LEU A O   
1796 C CB  . LEU A 228 ? 0.5230 1.0442 0.6653 -0.0918 0.0124  0.0095  524 LEU A CB  
1797 C CG  . LEU A 228 ? 0.5637 1.0235 0.6843 -0.1258 0.0041  0.0162  524 LEU A CG  
1798 C CD1 . LEU A 228 ? 0.6697 1.0683 0.7615 -0.1280 0.0028  0.0161  524 LEU A CD1 
1799 C CD2 . LEU A 228 ? 0.5008 0.9214 0.6313 -0.1156 -0.0046 0.0126  524 LEU A CD2 
1800 N N   . GLN A 229 ? 0.6217 1.2474 0.8066 -0.0022 0.0187  -0.0049 525 GLN A N   
1801 C CA  . GLN A 229 ? 0.6776 1.3337 0.8590 0.0452  0.0254  -0.0125 525 GLN A CA  
1802 C C   . GLN A 229 ? 0.6912 1.2627 0.8478 0.0673  0.0247  -0.0222 525 GLN A C   
1803 O O   . GLN A 229 ? 0.6567 1.1566 0.8067 0.0652  0.0171  -0.0258 525 GLN A O   
1804 C CB  . GLN A 229 ? 0.6409 1.3283 0.8328 0.0745  0.0227  -0.0143 525 GLN A CB  
1805 C CG  . GLN A 229 ? 0.6871 1.3439 0.8561 0.1302  0.0252  -0.0246 525 GLN A CG  
1806 C CD  . GLN A 229 ? 0.8842 1.5528 1.0549 0.1596  0.0207  -0.0256 525 GLN A CD  
1807 O OE1 . GLN A 229 ? 0.9281 1.6522 1.1239 0.1411  0.0167  -0.0186 525 GLN A OE1 
1808 N NE2 . GLN A 229 ? 1.0027 1.6131 1.1400 0.2043  0.0207  -0.0343 525 GLN A NE2 
1809 N N   . ALA A 230 ? 0.5977 1.1815 0.7390 0.0857  0.0327  -0.0266 526 ALA A N   
1810 C CA  . ALA A 230 ? 0.5429 1.0521 0.6560 0.1012  0.0321  -0.0361 526 ALA A CA  
1811 C C   . ALA A 230 ? 0.6658 1.1740 0.7536 0.1519  0.0379  -0.0456 526 ALA A C   
1812 O O   . ALA A 230 ? 0.6586 1.2386 0.7478 0.1743  0.0467  -0.0448 526 ALA A O   
1813 C CB  . ALA A 230 ? 0.5881 1.0966 0.6938 0.0789  0.0357  -0.0337 526 ALA A CB  
1814 N N   . ASN A 231 ? 0.7782 1.2047 0.8378 0.1695  0.0329  -0.0545 527 ASN A N   
1815 C CA  . ASN A 231 ? 0.8708 1.2626 0.8867 0.2171  0.0370  -0.0650 527 ASN A CA  
1816 C C   . ASN A 231 ? 0.8231 1.2863 0.8413 0.2586  0.0428  -0.0633 527 ASN A C   
1817 O O   . ASN A 231 ? 0.8428 1.3248 0.8328 0.3006  0.0507  -0.0689 527 ASN A O   
1818 C CB  . ASN A 231 ? 0.9807 1.3498 0.9671 0.2243  0.0425  -0.0720 527 ASN A CB  
1819 C CG  . ASN A 231 ? 1.0892 1.3810 1.0144 0.2639  0.0436  -0.0848 527 ASN A CG  
1820 O OD1 . ASN A 231 ? 1.1297 1.3462 1.0293 0.2640  0.0370  -0.0895 527 ASN A OD1 
1821 N ND2 . ASN A 231 ? 1.2213 1.5274 1.1164 0.2968  0.0523  -0.0905 527 ASN A ND2 
1822 N N   . GLY A 232 ? 0.7566 1.2627 0.8070 0.2490  0.0384  -0.0557 528 GLY A N   
1823 C CA  . GLY A 232 ? 0.6884 1.2701 0.7446 0.2872  0.0416  -0.0536 528 GLY A CA  
1824 C C   . GLY A 232 ? 0.7628 1.4723 0.8540 0.2809  0.0494  -0.0463 528 GLY A C   
1825 O O   . GLY A 232 ? 0.8196 1.6146 0.9283 0.3016  0.0504  -0.0425 528 GLY A O   
1826 N N   . ASN A 233 ? 0.7574 1.4868 0.8573 0.2515  0.0550  -0.0440 529 ASN A N   
1827 C CA  . ASN A 233 ? 0.7534 1.6045 0.8815 0.2386  0.0636  -0.0366 529 ASN A CA  
1828 C C   . ASN A 233 ? 0.7538 1.6680 0.9229 0.1930  0.0583  -0.0253 529 ASN A C   
1829 O O   . ASN A 233 ? 0.8019 1.6581 0.9780 0.1688  0.0482  -0.0231 529 ASN A O   
1830 C CB  . ASN A 233 ? 0.7172 1.5598 0.8392 0.2108  0.0699  -0.0357 529 ASN A CB  
1831 C CG  . ASN A 233 ? 0.7854 1.5576 0.8633 0.2499  0.0738  -0.0475 529 ASN A CG  
1832 O OD1 . ASN A 233 ? 0.8055 1.5962 0.8577 0.3055  0.0798  -0.0548 529 ASN A OD1 
1833 N ND2 . ASN A 233 ? 0.7565 1.4456 0.8201 0.2224  0.0699  -0.0497 529 ASN A ND2 
1834 N N   . ASP A 234 ? 0.7474 1.7846 0.9406 0.1801  0.0655  -0.0186 530 ASP A N   
1835 C CA  . ASP A 234 ? 0.8432 1.9408 1.0664 0.1313  0.0602  -0.0081 530 ASP A CA  
1836 C C   . ASP A 234 ? 0.8673 1.8997 1.0911 0.0668  0.0556  -0.0014 530 ASP A C   
1837 O O   . ASP A 234 ? 0.9610 1.9551 1.1685 0.0518  0.0601  -0.0015 530 ASP A O   
1838 C CB  . ASP A 234 ? 0.9076 2.1008 1.1263 0.1194  0.0625  -0.0019 530 ASP A CB  
1839 C CG  . ASP A 234 ? 0.9381 2.1698 1.1369 0.1842  0.0628  -0.0076 530 ASP A CG  
1840 O OD1 . ASP A 234 ? 0.9360 2.2456 1.1266 0.1878  0.0663  -0.0051 530 ASP A OD1 
1841 O OD2 . ASP A 234 ? 0.9411 2.1224 1.1273 0.2319  0.0589  -0.0144 530 ASP A OD2 
1842 N N   . PRO A 235 ? 0.7923 1.8027 1.0273 0.0310  0.0457  0.0042  531 PRO A N   
1843 C CA  . PRO A 235 ? 0.7435 1.6727 0.9667 -0.0214 0.0399  0.0096  531 PRO A CA  
1844 C C   . PRO A 235 ? 0.7363 1.7183 0.9555 -0.0751 0.0458  0.0194  531 PRO A C   
1845 O O   . PRO A 235 ? 0.7982 1.8909 1.0311 -0.0867 0.0519  0.0240  531 PRO A O   
1846 C CB  . PRO A 235 ? 0.7568 1.6571 0.9892 -0.0368 0.0285  0.0119  531 PRO A CB  
1847 C CG  . PRO A 235 ? 0.7649 1.7770 1.0208 -0.0203 0.0299  0.0132  531 PRO A CG  
1848 C CD  . PRO A 235 ? 0.7627 1.8170 1.0166 0.0400  0.0389  0.0055  531 PRO A CD  
1849 N N   . GLU A 236 ? 0.6989 1.5968 0.8931 -0.1083 0.0434  0.0229  532 GLU A N   
1850 C CA  . GLU A 236 ? 0.6334 1.5526 0.8084 -0.1593 0.0490  0.0324  532 GLU A CA  
1851 C C   . GLU A 236 ? 0.5509 1.3853 0.6981 -0.2089 0.0395  0.0398  532 GLU A C   
1852 O O   . GLU A 236 ? 0.5242 1.2635 0.6624 -0.1959 0.0304  0.0360  532 GLU A O   
1853 C CB  . GLU A 236 ? 0.6481 1.5421 0.8047 -0.1434 0.0570  0.0294  532 GLU A CB  
1854 C CG  . GLU A 236 ? 0.6224 1.5716 0.7945 -0.0853 0.0655  0.0198  532 GLU A CG  
1855 C CD  . GLU A 236 ? 0.6834 1.5618 0.8331 -0.0593 0.0679  0.0127  532 GLU A CD  
1856 O OE1 . GLU A 236 ? 0.6634 1.5053 0.7895 -0.0911 0.0694  0.0181  532 GLU A OE1 
1857 O OE2 . GLU A 236 ? 0.6773 1.5313 0.8272 -0.0083 0.0678  0.0017  532 GLU A OE2 
1858 N N   . LEU A 237 ? 0.6016 1.4705 0.7299 -0.2665 0.0420  0.0504  533 LEU A N   
1859 C CA  . LEU A 237 ? 0.6191 1.4038 0.7082 -0.3155 0.0332  0.0579  533 LEU A CA  
1860 C C   . LEU A 237 ? 0.7698 1.4507 0.8121 -0.3247 0.0325  0.0607  533 LEU A C   
1861 O O   . LEU A 237 ? 0.7955 1.4962 0.8253 -0.3279 0.0415  0.0627  533 LEU A O   
1862 C CB  . LEU A 237 ? 0.5805 1.4306 0.6539 -0.3777 0.0350  0.0678  533 LEU A CB  
1863 C CG  . LEU A 237 ? 0.6118 1.5176 0.7088 -0.3652 0.0277  0.0640  533 LEU A CG  
1864 C CD1 . LEU A 237 ? 0.6889 1.6343 0.7516 -0.4124 0.0251  0.0696  533 LEU A CD1 
1865 C CD2 . LEU A 237 ? 0.6677 1.5016 0.7689 -0.3628 0.0169  0.0623  533 LEU A CD2 
1866 N N   . PHE A 238 ? 0.7111 1.2837 0.7252 -0.3268 0.0216  0.0607  534 PHE A N   
1867 C CA  . PHE A 238 ? 0.8081 1.2782 0.7679 -0.3377 0.0186  0.0648  534 PHE A CA  
1868 C C   . PHE A 238 ? 0.9858 1.3662 0.9000 -0.3667 0.0079  0.0700  534 PHE A C   
1869 O O   . PHE A 238 ? 0.9375 1.3054 0.8723 -0.3520 0.0003  0.0654  534 PHE A O   
1870 C CB  . PHE A 238 ? 0.7163 1.1369 0.6873 -0.2845 0.0162  0.0554  534 PHE A CB  
1871 C CG  . PHE A 238 ? 0.7464 1.2401 0.7607 -0.2462 0.0247  0.0472  534 PHE A CG  
1872 C CD1 . PHE A 238 ? 0.6967 1.2351 0.7574 -0.2104 0.0241  0.0384  534 PHE A CD1 
1873 C CD2 . PHE A 238 ? 0.6739 1.1825 0.6746 -0.2436 0.0332  0.0481  534 PHE A CD2 
1874 C CE1 . PHE A 238 ? 0.7550 1.3461 0.8422 -0.1718 0.0316  0.0303  534 PHE A CE1 
1875 C CE2 . PHE A 238 ? 0.6644 1.2316 0.6965 -0.2056 0.0410  0.0396  534 PHE A CE2 
1876 C CZ  . PHE A 238 ? 0.5960 1.2014 0.6684 -0.1689 0.0403  0.0306  534 PHE A CZ  
1877 N N   . GLN A 239 ? 1.0828 1.3944 0.9285 -0.4063 0.0073  0.0795  535 GLN A N   
1878 C CA  . GLN A 239 ? 1.1430 1.3491 0.9265 -0.4310 -0.0029 0.0846  535 GLN A CA  
1879 C C   . GLN A 239 ? 1.1080 1.2072 0.8553 -0.3931 -0.0098 0.0820  535 GLN A C   
1880 O O   . GLN A 239 ? 1.0513 1.1203 0.7662 -0.3901 -0.0063 0.0853  535 GLN A O   
1881 C CB  . GLN A 239 ? 1.3007 1.4850 1.0151 -0.5015 -0.0002 0.0973  535 GLN A CB  
1882 C CG  . GLN A 239 ? 1.4517 1.4940 1.0751 -0.5219 -0.0101 0.1031  535 GLN A CG  
1883 C CD  . GLN A 239 ? 1.5674 1.5495 1.1013 -0.5762 -0.0062 0.1155  535 GLN A CD  
1884 O OE1 . GLN A 239 ? 1.6277 1.4775 1.0730 -0.5817 -0.0131 0.1205  535 GLN A OE1 
1885 N NE2 . GLN A 239 ? 1.6137 1.6919 1.1650 -0.6154 0.0054  0.1206  535 GLN A NE2 
1886 N N   . ILE A 240 ? 0.9842 1.0343 0.7379 -0.3631 -0.0193 0.0760  536 ILE A N   
1887 C CA  . ILE A 240 ? 0.9860 0.9394 0.7021 -0.3272 -0.0277 0.0733  536 ILE A CA  
1888 C C   . ILE A 240 ? 1.1372 0.9900 0.7544 -0.3575 -0.0301 0.0841  536 ILE A C   
1889 O O   . ILE A 240 ? 1.1219 0.9373 0.6879 -0.4046 -0.0318 0.0916  536 ILE A O   
1890 C CB  . ILE A 240 ? 0.9562 0.8787 0.6848 -0.3049 -0.0367 0.0673  536 ILE A CB  
1891 C CG1 . ILE A 240 ? 0.7656 0.7839 0.5798 -0.2890 -0.0338 0.0592  536 ILE A CG1 
1892 C CG2 . ILE A 240 ? 0.8086 0.6593 0.5140 -0.2579 -0.0444 0.0625  536 ILE A CG2 
1893 C CD1 . ILE A 240 ? 0.9738 0.9824 0.7918 -0.2992 -0.0400 0.0581  536 ILE A CD1 
1894 N N   . PRO A 241 ? 1.0560 0.8584 0.6372 -0.3337 -0.0310 0.0854  537 PRO A N   
1895 C CA  . PRO A 241 ? 1.2676 0.9554 0.7411 -0.3553 -0.0348 0.0958  537 PRO A CA  
1896 C C   . PRO A 241 ? 1.3604 0.9538 0.7747 -0.3578 -0.0448 0.0972  537 PRO A C   
1897 O O   . PRO A 241 ? 1.2715 0.8482 0.7073 -0.3107 -0.0522 0.0890  537 PRO A O   
1898 C CB  . PRO A 241 ? 1.1876 0.8431 0.6484 -0.3062 -0.0376 0.0930  537 PRO A CB  
1899 C CG  . PRO A 241 ? 1.1561 0.9249 0.7136 -0.2826 -0.0308 0.0838  537 PRO A CG  
1900 C CD  . PRO A 241 ? 0.9753 0.8190 0.6064 -0.2856 -0.0294 0.0771  537 PRO A CD  
1901 N N   . PRO A 242 ? 1.4589 0.9949 0.7990 -0.4151 -0.0449 0.1069  538 PRO A N   
1902 C CA  . PRO A 242 ? 1.5335 0.9744 0.8102 -0.4212 -0.0544 0.1076  538 PRO A CA  
1903 C C   . PRO A 242 ? 1.5711 0.9082 0.7929 -0.3613 -0.0643 0.1044  538 PRO A C   
1904 O O   . PRO A 242 ? 1.5484 0.8549 0.7698 -0.3352 -0.0715 0.0986  538 PRO A O   
1905 C CB  . PRO A 242 ? 1.6318 1.0041 0.8097 -0.4960 -0.0524 0.1203  538 PRO A CB  
1906 C CG  . PRO A 242 ? 1.5321 1.0229 0.7667 -0.5370 -0.0402 0.1239  538 PRO A CG  
1907 C CD  . PRO A 242 ? 1.4359 0.9969 0.7461 -0.4807 -0.0358 0.1172  538 PRO A CD  
1908 N N   . GLU A 243 ? 1.5380 0.8280 0.7154 -0.3353 -0.0647 0.1078  539 GLU A N   
1909 C CA  . GLU A 243 ? 1.4678 0.6740 0.5954 -0.2713 -0.0745 0.1045  539 GLU A CA  
1910 C C   . GLU A 243 ? 1.4691 0.7569 0.6951 -0.2130 -0.0775 0.0910  539 GLU A C   
1911 O O   . GLU A 243 ? 1.5552 0.7887 0.7490 -0.1628 -0.0861 0.0867  539 GLU A O   
1912 C CB  . GLU A 243 ? 1.6652 0.8242 0.7360 -0.2539 -0.0743 0.1106  539 GLU A CB  
1913 C CG  . GLU A 243 ? 1.5830 0.8594 0.7494 -0.2378 -0.0674 0.1055  539 GLU A CG  
1914 C CD  . GLU A 243 ? 1.6304 0.9541 0.8048 -0.2969 -0.0558 0.1133  539 GLU A CD  
1915 O OE1 . GLU A 243 ? 1.6314 0.9571 0.7896 -0.3566 -0.0511 0.1191  539 GLU A OE1 
1916 O OE2 . GLU A 243 ? 1.5622 0.9262 0.7583 -0.2835 -0.0512 0.1134  539 GLU A OE2 
1917 N N   . LEU A 244 ? 1.3340 0.7492 0.6730 -0.2189 -0.0706 0.0843  540 LEU A N   
1918 C CA  . LEU A 244 ? 1.2316 0.7225 0.6601 -0.1743 -0.0725 0.0720  540 LEU A CA  
1919 C C   . LEU A 244 ? 1.2395 0.7406 0.6937 -0.1829 -0.0747 0.0679  540 LEU A C   
1920 O O   . LEU A 244 ? 1.2280 0.7657 0.7337 -0.1441 -0.0778 0.0586  540 LEU A O   
1921 C CB  . LEU A 244 ? 1.1884 0.7968 0.7138 -0.1745 -0.0643 0.0664  540 LEU A CB  
1922 C CG  . LEU A 244 ? 1.1561 0.7757 0.6774 -0.1561 -0.0622 0.0669  540 LEU A CG  
1923 C CD1 . LEU A 244 ? 0.9716 0.7030 0.5916 -0.1459 -0.0558 0.0578  540 LEU A CD1 
1924 C CD2 . LEU A 244 ? 1.1949 0.7520 0.6685 -0.1048 -0.0722 0.0647  540 LEU A CD2 
1925 N N   . VAL A 245 ? 1.2239 0.6966 0.6421 -0.2350 -0.0733 0.0746  541 VAL A N   
1926 C CA  . VAL A 245 ? 1.2344 0.7136 0.6707 -0.2466 -0.0762 0.0712  541 VAL A CA  
1927 C C   . VAL A 245 ? 1.2655 0.6143 0.5967 -0.2369 -0.0851 0.0741  541 VAL A C   
1928 O O   . VAL A 245 ? 1.3019 0.5640 0.5412 -0.2786 -0.0866 0.0831  541 VAL A O   
1929 C CB  . VAL A 245 ? 1.2489 0.7849 0.7098 -0.3086 -0.0705 0.0758  541 VAL A CB  
1930 C CG1 . VAL A 245 ? 1.2623 0.7883 0.7239 -0.3231 -0.0754 0.0733  541 VAL A CG1 
1931 C CG2 . VAL A 245 ? 1.0768 0.7430 0.6414 -0.3047 -0.0620 0.0713  541 VAL A CG2 
1932 N N   . LEU A 246 ? 1.3608 0.6952 0.7012 -0.1823 -0.0908 0.0662  542 LEU A N   
1933 C CA  . LEU A 246 ? 1.4011 0.6163 0.6436 -0.1600 -0.0992 0.0670  542 LEU A CA  
1934 C C   . LEU A 246 ? 1.3778 0.5769 0.6137 -0.1903 -0.1013 0.0658  542 LEU A C   
1935 O O   . LEU A 246 ? 1.3436 0.6338 0.6701 -0.1889 -0.0989 0.0592  542 LEU A O   
1936 C CB  . LEU A 246 ? 1.4365 0.6597 0.6953 -0.0854 -0.1037 0.0586  542 LEU A CB  
1937 C CG  . LEU A 246 ? 1.5465 0.6728 0.7242 -0.0467 -0.1118 0.0562  542 LEU A CG  
1938 C CD1 . LEU A 246 ? 1.6595 0.6395 0.6956 -0.0471 -0.1171 0.0652  542 LEU A CD1 
1939 C CD2 . LEU A 246 ? 1.3827 0.5647 0.6085 0.0239  -0.1143 0.0462  542 LEU A CD2 
1940 N N   . GLU A 247 ? 1.5771 0.6535 0.6984 -0.2179 -0.1063 0.0722  543 GLU A N   
1941 C CA  . GLU A 247 ? 1.5571 0.6020 0.6532 -0.2534 -0.1096 0.0717  543 GLU A CA  
1942 C C   . GLU A 247 ? 1.7315 0.6327 0.7093 -0.2220 -0.1182 0.0709  543 GLU A C   
1943 O O   . GLU A 247 ? 1.7543 0.5719 0.6472 -0.1947 -0.1209 0.0705  543 GLU A O   
1944 C CB  . GLU A 247 ? 1.6409 0.6804 0.7056 -0.3379 -0.1069 0.0807  543 GLU A CB  
1945 C CG  . GLU A 247 ? 1.6045 0.7927 0.7832 -0.3680 -0.0981 0.0811  543 GLU A CG  
1946 C CD  . GLU A 247 ? 1.7598 0.9594 0.9068 -0.4471 -0.0949 0.0890  543 GLU A CD  
1947 O OE1 . GLU A 247 ? 1.7787 0.9458 0.8729 -0.4644 -0.0924 0.0932  543 GLU A OE1 
1948 O OE2 . GLU A 247 ? 1.7089 0.9764 0.8956 -0.4799 -0.0952 0.0857  543 GLU A OE2 
1949 N N   . VAL A 248 ? 1.6937 0.5889 0.6764 -0.2208 -0.1216 0.0651  544 VAL A N   
1950 C CA  . VAL A 248 ? 1.8504 0.6565 0.7489 -0.1812 -0.1276 0.0560  544 VAL A CA  
1951 C C   . VAL A 248 ? 1.8458 0.6195 0.6908 -0.2368 -0.1300 0.0533  544 VAL A C   
1952 O O   . VAL A 248 ? 1.7127 0.5528 0.6195 -0.2712 -0.1291 0.0540  544 VAL A O   
1953 C CB  . VAL A 248 ? 1.7577 0.5910 0.7054 -0.1220 -0.1296 0.0504  544 VAL A CB  
1954 C CG1 . VAL A 248 ? 1.9102 0.6570 0.7659 -0.0797 -0.1343 0.0404  544 VAL A CG1 
1955 C CG2 . VAL A 248 ? 1.5979 0.5217 0.6283 -0.0664 -0.1259 0.0471  544 VAL A CG2 
1956 N N   . PRO A 249 ? 1.9635 0.6382 0.6917 -0.2479 -0.1336 0.0502  545 PRO A N   
1957 C CA  . PRO A 249 ? 2.0376 0.6740 0.7026 -0.2969 -0.1375 0.0483  545 PRO A CA  
1958 C C   . PRO A 249 ? 2.0749 0.6722 0.7140 -0.2560 -0.1418 0.0412  545 PRO A C   
1959 O O   . PRO A 249 ? 2.1064 0.6456 0.7011 -0.1902 -0.1436 0.0345  545 PRO A O   
1960 C CB  . PRO A 249 ? 2.1229 0.6521 0.6599 -0.3140 -0.1406 0.0461  545 PRO A CB  
1961 C CG  . PRO A 249 ? 2.0884 0.6179 0.6395 -0.2814 -0.1371 0.0477  545 PRO A CG  
1962 C CD  . PRO A 249 ? 1.9981 0.5899 0.6417 -0.2187 -0.1348 0.0479  545 PRO A CD  
1963 N N   . ILE A 250 ? 2.1514 0.7892 0.8209 -0.2932 -0.1429 0.0425  546 ILE A N   
1964 C CA  . ILE A 250 ? 2.0560 0.6756 0.7200 -0.2591 -0.1459 0.0368  546 ILE A CA  
1965 C C   . ILE A 250 ? 2.2428 0.7446 0.7678 -0.2663 -0.1521 0.0332  546 ILE A C   
1966 O O   . ILE A 250 ? 2.1720 0.6549 0.6475 -0.3293 -0.1545 0.0374  546 ILE A O   
1967 C CB  . ILE A 250 ? 1.9891 0.7109 0.7554 -0.2926 -0.1444 0.0394  546 ILE A CB  
1968 C CG1 . ILE A 250 ? 1.7556 0.5886 0.6486 -0.2920 -0.1386 0.0425  546 ILE A CG1 
1969 C CG2 . ILE A 250 ? 1.9407 0.6465 0.7079 -0.2521 -0.1470 0.0329  546 ILE A CG2 
1970 C CD1 . ILE A 250 ? 1.7035 0.5337 0.6272 -0.2213 -0.1369 0.0387  546 ILE A CD1 
1971 N N   . ARG A 251 ? 2.3668 0.7926 0.8254 -0.2007 -0.1544 0.0254  547 ARG A N   
1972 C CA  . ARG A 251 ? 2.3781 0.6876 0.7010 -0.1956 -0.1602 0.0209  547 ARG A CA  
1973 C C   . ARG A 251 ? 2.4380 0.7476 0.7720 -0.1392 -0.1608 0.0153  547 ARG A C   
1974 O O   . ARG A 251 ? 2.2597 0.6482 0.6937 -0.0959 -0.1567 0.0130  547 ARG A O   
1975 C CB  . ARG A 251 ? 2.5195 0.7164 0.7174 -0.1679 -0.1625 0.0153  547 ARG A CB  
1976 C CG  . ARG A 251 ? 2.4373 0.6339 0.6482 -0.0821 -0.1597 0.0080  547 ARG A CG  
1977 C CD  . ARG A 251 ? 2.4165 0.6833 0.7122 -0.0842 -0.1549 0.0122  547 ARG A CD  
1978 N NE  . ARG A 251 ? 2.3604 0.6209 0.6525 -0.0053 -0.1530 0.0057  547 ARG A NE  
1979 C CZ  . ARG A 251 ? 2.4821 0.8042 0.8471 0.0094  -0.1492 0.0092  547 ARG A CZ  
1980 N NH1 . ARG A 251 ? 2.6006 0.9218 0.9578 0.0830  -0.1480 0.0032  547 ARG A NH1 
1981 N NH2 . ARG A 251 ? 2.3551 0.7451 0.7994 -0.0487 -0.1464 0.0192  547 ARG A NH2 
1982 N N   . HIS A 252 ? 2.4829 0.7036 0.7095 -0.1429 -0.1659 0.0134  548 HIS A N   
1983 C CA  . HIS A 252 ? 2.4496 0.6630 0.6738 -0.0892 -0.1662 0.0083  548 HIS A CA  
1984 C C   . HIS A 252 ? 2.7065 0.8288 0.8383 -0.0246 -0.1654 0.0018  548 HIS A C   
1985 O O   . HIS A 252 ? 2.7910 0.8241 0.8287 -0.0421 -0.1670 0.0028  548 HIS A O   
1986 C CB  . HIS A 252 ? 2.4135 0.6208 0.6258 -0.1356 -0.1695 0.0127  548 HIS A CB  
1987 C CG  . HIS A 252 ? 2.5777 0.8163 0.8302 -0.0907 -0.1688 0.0087  548 HIS A CG  
1988 N ND1 . HIS A 252 ? 2.6762 0.8472 0.8590 -0.0349 -0.1688 0.0033  548 HIS A ND1 
1989 C CD2 . HIS A 252 ? 2.4355 0.7791 0.8140 -0.0920 -0.1654 0.0085  548 HIS A CD2 
1990 C CE1 . HIS A 252 ? 2.5370 0.7587 0.7736 -0.0054 -0.1679 0.0005  548 HIS A CE1 
1991 N NE2 . HIS A 252 ? 2.4341 0.7609 0.7952 -0.0397 -0.1654 0.0030  548 HIS A NE2 
1992 N N   . PRO A 253 ? 2.6756 0.8216 0.8300 0.0504  -0.1630 -0.0048 549 PRO A N   
1993 C CA  . PRO A 253 ? 2.7140 0.7886 0.7859 0.1183  -0.1619 -0.0107 549 PRO A CA  
1994 C C   . PRO A 253 ? 2.8728 0.8488 0.8419 0.1135  -0.1650 -0.0100 549 PRO A C   
1995 O O   . PRO A 253 ? 3.0384 0.9407 0.9224 0.1638  -0.1649 -0.0140 549 PRO A O   
1996 C CB  . PRO A 253 ? 2.6980 0.8561 0.8424 0.1933  -0.1579 -0.0169 549 PRO A CB  
1997 C CG  . PRO A 253 ? 2.5450 0.7807 0.7777 0.1603  -0.1583 -0.0144 549 PRO A CG  
1998 C CD  . PRO A 253 ? 2.5128 0.7617 0.7726 0.0788  -0.1609 -0.0072 549 PRO A CD  
1999 N N   . LYS A 254 ? 2.8000 0.7733 0.7721 0.0572  -0.1679 -0.0051 550 LYS A N   
2000 C CA  . LYS A 254 ? 3.0035 0.8767 0.8716 0.0408  -0.1717 -0.0035 550 LYS A CA  
2001 C C   . LYS A 254 ? 3.0929 0.9213 0.9150 -0.0483 -0.1756 0.0038  550 LYS A C   
2002 O O   . LYS A 254 ? 3.3335 1.0556 1.0436 -0.0616 -0.1782 0.0044  550 LYS A O   
2003 C CB  . LYS A 254 ? 3.0437 0.9468 0.9424 0.0539  -0.1720 -0.0040 550 LYS A CB  
2004 C CG  . LYS A 254 ? 3.0249 1.0012 0.9913 0.1324  -0.1675 -0.0104 550 LYS A CG  
2005 C CD  . LYS A 254 ? 3.2149 1.1361 1.1084 0.2107  -0.1656 -0.0162 550 LYS A CD  
2006 C CE  . LYS A 254 ? 3.1284 1.1393 1.0941 0.2860  -0.1606 -0.0222 550 LYS A CE  
2007 N NZ  . LYS A 254 ? 3.2205 1.1950 1.1212 0.3649  -0.1587 -0.0273 550 LYS A NZ  
2008 N N   . PHE A 255 ? 2.8858 0.7961 0.7900 -0.1101 -0.1761 0.0093  551 PHE A N   
2009 C CA  . PHE A 255 ? 2.9367 0.8261 0.8069 -0.1976 -0.1796 0.0169  551 PHE A CA  
2010 C C   . PHE A 255 ? 2.9762 0.8546 0.8277 -0.2329 -0.1788 0.0191  551 PHE A C   
2011 O O   . PHE A 255 ? 2.8987 0.8675 0.8390 -0.2544 -0.1765 0.0214  551 PHE A O   
2012 C CB  . PHE A 255 ? 2.8413 0.8349 0.8101 -0.2444 -0.1802 0.0221  551 PHE A CB  
2013 C CG  . PHE A 255 ? 2.8848 0.8933 0.8769 -0.2113 -0.1809 0.0197  551 PHE A CG  
2014 C CD1 . PHE A 255 ? 2.8893 0.9636 0.9611 -0.1501 -0.1777 0.0143  551 PHE A CD1 
2015 C CD2 . PHE A 255 ? 2.9396 0.8976 0.8729 -0.2431 -0.1848 0.0229  551 PHE A CD2 
2016 C CE1 . PHE A 255 ? 2.8433 0.9340 0.9366 -0.1205 -0.1779 0.0118  551 PHE A CE1 
2017 C CE2 . PHE A 255 ? 2.8942 0.8659 0.8490 -0.2127 -0.1853 0.0207  551 PHE A CE2 
2018 C CZ  . PHE A 255 ? 2.8215 0.8599 0.8566 -0.1511 -0.1817 0.0150  551 PHE A CZ  
2019 N N   . ASP A 256 ? 3.2237 0.9882 0.9554 -0.2402 -0.1808 0.0185  552 ASP A N   
2020 C CA  . ASP A 256 ? 3.2722 1.0169 0.9758 -0.2745 -0.1801 0.0203  552 ASP A CA  
2021 C C   . ASP A 256 ? 3.2283 1.0312 0.9652 -0.3679 -0.1810 0.0284  552 ASP A C   
2022 O O   . ASP A 256 ? 3.2501 1.0678 0.9910 -0.4003 -0.1795 0.0304  552 ASP A O   
2023 C CB  . ASP A 256 ? 3.5263 1.1267 1.0837 -0.2610 -0.1826 0.0175  552 ASP A CB  
2024 C CG  . ASP A 256 ? 3.7333 1.2976 1.2689 -0.1743 -0.1801 0.0099  552 ASP A CG  
2025 O OD1 . ASP A 256 ? 3.8587 1.3373 1.3106 -0.1213 -0.1816 0.0056  552 ASP A OD1 
2026 O OD2 . ASP A 256 ? 3.7034 1.3293 1.3059 -0.1581 -0.1767 0.0085  552 ASP A OD2 
2027 N N   . TRP A 257 ? 3.1866 1.0278 0.9474 -0.4110 -0.1832 0.0333  553 TRP A N   
2028 C CA  . TRP A 257 ? 3.1077 1.0324 0.9186 -0.4941 -0.1832 0.0412  553 TRP A CA  
2029 C C   . TRP A 257 ? 2.9524 1.0173 0.9034 -0.4925 -0.1795 0.0429  553 TRP A C   
2030 O O   . TRP A 257 ? 2.8560 1.0052 0.8580 -0.5551 -0.1785 0.0493  553 TRP A O   
2031 C CB  . TRP A 257 ? 3.0599 0.9841 0.8498 -0.5390 -0.1868 0.0460  553 TRP A CB  
2032 C CG  . TRP A 257 ? 3.1307 1.0850 0.9730 -0.4917 -0.1873 0.0434  553 TRP A CG  
2033 C CD1 . TRP A 257 ? 3.2931 1.1599 1.0688 -0.4424 -0.1894 0.0388  553 TRP A CD1 
2034 C CD2 . TRP A 257 ? 2.9821 1.0624 0.9516 -0.4885 -0.1855 0.0452  553 TRP A CD2 
2035 N NE1 . TRP A 257 ? 3.1999 1.1325 1.0551 -0.4103 -0.1888 0.0373  553 TRP A NE1 
2036 C CE2 . TRP A 257 ? 3.0127 1.0730 0.9854 -0.4382 -0.1867 0.0411  553 TRP A CE2 
2037 C CE3 . TRP A 257 ? 2.7713 0.9786 0.8487 -0.5227 -0.1830 0.0499  553 TRP A CE3 
2038 C CZ2 . TRP A 257 ? 2.7636 0.9217 0.8414 -0.4232 -0.1859 0.0413  553 TRP A CZ2 
2039 C CZ3 . TRP A 257 ? 2.5791 0.8820 0.7590 -0.5063 -0.1824 0.0504  553 TRP A CZ3 
2040 C CH2 . TRP A 257 ? 2.6024 0.8778 0.7807 -0.4581 -0.1840 0.0460  553 TRP A CH2 
2041 N N   . PHE A 258 ? 2.7076 0.8011 0.7188 -0.4220 -0.1774 0.0374  554 PHE A N   
2042 C CA  . PHE A 258 ? 2.6749 0.8932 0.8130 -0.4180 -0.1745 0.0388  554 PHE A CA  
2043 C C   . PHE A 258 ? 2.6125 0.8695 0.7774 -0.4430 -0.1715 0.0410  554 PHE A C   
2044 O O   . PHE A 258 ? 2.5115 0.8860 0.7855 -0.4718 -0.1680 0.0456  554 PHE A O   
2045 C CB  . PHE A 258 ? 2.5283 0.7579 0.7115 -0.3356 -0.1730 0.0317  554 PHE A CB  
2046 C CG  . PHE A 258 ? 2.3429 0.7007 0.6716 -0.3329 -0.1694 0.0330  554 PHE A CG  
2047 C CD1 . PHE A 258 ? 2.4223 0.7994 0.7770 -0.3250 -0.1709 0.0321  554 PHE A CD1 
2048 C CD2 . PHE A 258 ? 2.2396 0.7004 0.6837 -0.3397 -0.1639 0.0348  554 PHE A CD2 
2049 C CE1 . PHE A 258 ? 2.2027 0.6967 0.6934 -0.3226 -0.1673 0.0316  554 PHE A CE1 
2050 C CE2 . PHE A 258 ? 2.1595 0.7367 0.7385 -0.3366 -0.1602 0.0350  554 PHE A CE2 
2051 C CZ  . PHE A 258 ? 2.1086 0.7016 0.7099 -0.3285 -0.1621 0.0327  554 PHE A CZ  
2052 N N   . LYS A 259 ? 2.6138 0.7826 0.6973 -0.4288 -0.1712 0.0377  555 LYS A N   
2053 C CA  . LYS A 259 ? 2.7493 0.9499 0.8533 -0.4533 -0.1683 0.0396  555 LYS A CA  
2054 C C   . LYS A 259 ? 2.8535 1.1083 0.9648 -0.5421 -0.1682 0.0476  555 LYS A C   
2055 O O   . LYS A 259 ? 2.7978 1.1414 0.9772 -0.5717 -0.1651 0.0513  555 LYS A O   
2056 C CB  . LYS A 259 ? 2.8272 0.9139 0.8325 -0.4205 -0.1683 0.0343  555 LYS A CB  
2057 C CG  . LYS A 259 ? 2.9745 0.9413 0.8766 -0.3747 -0.1712 0.0289  555 LYS A CG  
2058 C CD  . LYS A 259 ? 3.1919 1.0424 0.9792 -0.3665 -0.1719 0.0259  555 LYS A CD  
2059 C CE  . LYS A 259 ? 3.3963 1.1404 1.0955 -0.2961 -0.1737 0.0192  555 LYS A CE  
2060 N NZ  . LYS A 259 ? 3.3539 1.1532 1.1286 -0.2153 -0.1711 0.0137  555 LYS A NZ  
2061 N N   . ASP A 260 ? 2.9279 1.1349 0.9688 -0.5850 -0.1714 0.0504  556 ASP A N   
2062 C CA  . ASP A 260 ? 3.0241 1.2867 1.0659 -0.6696 -0.1713 0.0578  556 ASP A CA  
2063 C C   . ASP A 260 ? 2.8133 1.2284 0.9786 -0.6962 -0.1691 0.0636  556 ASP A C   
2064 O O   . ASP A 260 ? 2.7756 1.2716 0.9680 -0.7594 -0.1672 0.0696  556 ASP A O   
2065 C CB  . ASP A 260 ? 3.2688 1.4413 1.2023 -0.7069 -0.1757 0.0594  556 ASP A CB  
2066 C CG  . ASP A 260 ? 3.4580 1.4808 1.2583 -0.6942 -0.1778 0.0549  556 ASP A CG  
2067 O OD1 . ASP A 260 ? 3.5037 1.5140 1.2748 -0.7227 -0.1762 0.0554  556 ASP A OD1 
2068 O OD2 . ASP A 260 ? 3.5519 1.4700 1.2752 -0.6539 -0.1810 0.0507  556 ASP A OD2 
2069 N N   . LEU A 261 ? 2.6823 1.1414 0.9231 -0.6477 -0.1689 0.0616  557 LEU A N   
2070 C CA  . LEU A 261 ? 2.4871 1.1030 0.8811 -0.6585 -0.1634 0.0654  557 LEU A CA  
2071 C C   . LEU A 261 ? 2.6179 1.3301 1.0997 -0.6689 -0.1567 0.0675  557 LEU A C   
2072 O O   . LEU A 261 ? 2.6438 1.4876 1.2266 -0.6994 -0.1522 0.0720  557 LEU A O   
2073 C CB  . LEU A 261 ? 2.2528 0.8915 0.7238 -0.5948 -0.1627 0.0604  557 LEU A CB  
2074 C CG  . LEU A 261 ? 2.3240 0.9266 0.7572 -0.5958 -0.1676 0.0601  557 LEU A CG  
2075 C CD1 . LEU A 261 ? 2.1748 0.8087 0.6900 -0.5334 -0.1664 0.0540  557 LEU A CD1 
2076 C CD2 . LEU A 261 ? 2.3697 1.0564 0.8320 -0.6647 -0.1678 0.0673  557 LEU A CD2 
2077 N N   . GLY A 262 ? 2.6501 1.3000 1.0931 -0.6415 -0.1557 0.0642  558 GLY A N   
2078 C CA  . GLY A 262 ? 2.6332 1.3603 1.1432 -0.6540 -0.1494 0.0669  558 GLY A CA  
2079 C C   . GLY A 262 ? 2.5093 1.3599 1.1719 -0.6207 -0.1428 0.0675  558 GLY A C   
2080 O O   . GLY A 262 ? 2.4780 1.4441 1.2254 -0.6494 -0.1370 0.0719  558 GLY A O   
2081 N N   . LEU A 263 ? 2.3434 1.1716 1.0379 -0.5598 -0.1436 0.0625  559 LEU A N   
2082 C CA  . LEU A 263 ? 2.0838 1.0142 0.9114 -0.5259 -0.1384 0.0617  559 LEU A CA  
2083 C C   . LEU A 263 ? 1.9824 0.8801 0.8190 -0.4749 -0.1356 0.0595  559 LEU A C   
2084 O O   . LEU A 263 ? 1.9474 0.7326 0.6889 -0.4439 -0.1389 0.0560  559 LEU A O   
2085 C CB  . LEU A 263 ? 1.9944 0.9347 0.8596 -0.4948 -0.1411 0.0571  559 LEU A CB  
2086 C CG  . LEU A 263 ? 1.9117 0.8890 0.7743 -0.5407 -0.1441 0.0596  559 LEU A CG  
2087 C CD1 . LEU A 263 ? 1.9007 0.8761 0.7935 -0.5052 -0.1470 0.0542  559 LEU A CD1 
2088 C CD2 . LEU A 263 ? 1.7685 0.8853 0.7223 -0.5868 -0.1392 0.0648  559 LEU A CD2 
2089 N N   . LYS A 264 ? 1.8047 0.8038 0.7534 -0.4656 -0.1295 0.0615  560 LYS A N   
2090 C CA  . LYS A 264 ? 1.8754 0.8617 0.8501 -0.4167 -0.1266 0.0607  560 LYS A CA  
2091 C C   . LYS A 264 ? 1.7483 0.8479 0.8528 -0.4029 -0.1223 0.0602  560 LYS A C   
2092 O O   . LYS A 264 ? 1.6998 0.8948 0.8732 -0.4355 -0.1208 0.0605  560 LYS A O   
2093 C CB  . LYS A 264 ? 1.7313 0.7035 0.6731 -0.4369 -0.1230 0.0659  560 LYS A CB  
2094 C CG  . LYS A 264 ? 1.6529 0.7359 0.6554 -0.4965 -0.1173 0.0717  560 LYS A CG  
2095 C CD  . LYS A 264 ? 1.8825 0.9507 0.8520 -0.5139 -0.1132 0.0763  560 LYS A CD  
2096 C CE  . LYS A 264 ? 1.9069 1.0303 0.8633 -0.5831 -0.1112 0.0800  560 LYS A CE  
2097 N NZ  . LYS A 264 ? 1.7457 0.8937 0.7019 -0.6037 -0.1052 0.0845  560 LYS A NZ  
2098 N N   . TRP A 265 ? 1.6392 0.7280 0.7724 -0.3519 -0.1211 0.0587  561 TRP A N   
2099 C CA  . TRP A 265 ? 1.4116 0.6278 0.6725 -0.3311 -0.1157 0.0552  561 TRP A CA  
2100 C C   . TRP A 265 ? 1.4483 0.6845 0.7330 -0.2911 -0.1108 0.0556  561 TRP A C   
2101 O O   . TRP A 265 ? 1.5172 0.6556 0.7165 -0.2722 -0.1133 0.0588  561 TRP A O   
2102 C CB  . TRP A 265 ? 1.2724 0.5208 0.5848 -0.2875 -0.1175 0.0460  561 TRP A CB  
2103 C CG  . TRP A 265 ? 1.2333 0.6246 0.6721 -0.2866 -0.1121 0.0424  561 TRP A CG  
2104 C CD1 . TRP A 265 ? 1.2144 0.6820 0.7371 -0.2389 -0.1071 0.0364  561 TRP A CD1 
2105 C CD2 . TRP A 265 ? 1.2168 0.6886 0.7037 -0.3355 -0.1113 0.0446  561 TRP A CD2 
2106 N NE1 . TRP A 265 ? 1.1128 0.6890 0.7251 -0.2530 -0.1032 0.0350  561 TRP A NE1 
2107 C CE2 . TRP A 265 ? 1.1579 0.7436 0.7528 -0.3082 -0.1058 0.0399  561 TRP A CE2 
2108 C CE3 . TRP A 265 ? 1.2279 0.6882 0.6733 -0.4001 -0.1152 0.0500  561 TRP A CE3 
2109 C CZ2 . TRP A 265 ? 1.1053 0.7908 0.7659 -0.3352 -0.1042 0.0405  561 TRP A CZ2 
2110 C CZ3 . TRP A 265 ? 1.2001 0.7752 0.7195 -0.4299 -0.1137 0.0505  561 TRP A CZ3 
2111 C CH2 . TRP A 265 ? 1.0340 0.7188 0.6592 -0.3932 -0.1083 0.0457  561 TRP A CH2 
2112 N N   . TYR A 266 ? 1.2616 0.6220 0.6566 -0.2801 -0.1042 0.0527  562 TYR A N   
2113 C CA  . TYR A 266 ? 1.2259 0.6185 0.6548 -0.2410 -0.0998 0.0513  562 TYR A CA  
2114 C C   . TYR A 266 ? 1.3412 0.7428 0.8004 -0.1755 -0.1014 0.0424  562 TYR A C   
2115 O O   . TYR A 266 ? 1.1911 0.6233 0.6890 -0.1633 -0.1024 0.0366  562 TYR A O   
2116 C CB  . TYR A 266 ? 1.0593 0.5738 0.5831 -0.2585 -0.0920 0.0515  562 TYR A CB  
2117 C CG  . TYR A 266 ? 1.0775 0.6887 0.6889 -0.2633 -0.0900 0.0464  562 TYR A CG  
2118 C CD1 . TYR A 266 ? 1.0510 0.7245 0.7376 -0.2192 -0.0876 0.0382  562 TYR A CD1 
2119 C CD2 . TYR A 266 ? 0.9786 0.6211 0.5940 -0.3134 -0.0907 0.0501  562 TYR A CD2 
2120 C CE1 . TYR A 266 ? 1.0664 0.8167 0.8224 -0.2213 -0.0859 0.0343  562 TYR A CE1 
2121 C CE2 . TYR A 266 ? 1.0235 0.7542 0.7149 -0.3119 -0.0895 0.0458  562 TYR A CE2 
2122 C CZ  . TYR A 266 ? 1.0375 0.8155 0.7958 -0.2642 -0.0871 0.0381  562 TYR A CZ  
2123 O OH  . TYR A 266 ? 1.0019 0.8555 0.8256 -0.2600 -0.0860 0.0343  562 TYR A OH  
2124 N N   . GLY A 267 ? 1.1956 0.5738 0.6345 -0.1341 -0.1018 0.0415  563 GLY A N   
2125 C CA  . GLY A 267 ? 1.1386 0.5342 0.6021 -0.0742 -0.1035 0.0331  563 GLY A CA  
2126 C C   . GLY A 267 ? 1.1010 0.6168 0.6772 -0.0586 -0.0980 0.0259  563 GLY A C   
2127 O O   . GLY A 267 ? 1.1077 0.6525 0.7146 -0.0235 -0.0986 0.0186  563 GLY A O   
2128 N N   . LEU A 268 ? 1.0058 0.5895 0.6382 -0.0844 -0.0924 0.0278  564 LEU A N   
2129 C CA  . LEU A 268 ? 0.9110 0.5909 0.6325 -0.0667 -0.0875 0.0210  564 LEU A CA  
2130 C C   . LEU A 268 ? 0.9171 0.6618 0.7033 -0.0906 -0.0838 0.0190  564 LEU A C   
2131 O O   . LEU A 268 ? 0.8405 0.6130 0.6414 -0.1261 -0.0805 0.0236  564 LEU A O   
2132 C CB  . LEU A 268 ? 0.9037 0.6112 0.6381 -0.0705 -0.0839 0.0233  564 LEU A CB  
2133 C CG  . LEU A 268 ? 0.8653 0.6561 0.6750 -0.0497 -0.0798 0.0156  564 LEU A CG  
2134 C CD1 . LEU A 268 ? 0.9270 0.7214 0.7365 -0.0047 -0.0836 0.0087  564 LEU A CD1 
2135 C CD2 . LEU A 268 ? 0.8575 0.6760 0.6795 -0.0624 -0.0754 0.0182  564 LEU A CD2 
2136 N N   . PRO A 269 ? 0.8650 0.6375 0.6876 -0.0720 -0.0840 0.0126  565 PRO A N   
2137 C CA  . PRO A 269 ? 0.7075 0.5443 0.5927 -0.0876 -0.0803 0.0103  565 PRO A CA  
2138 C C   . PRO A 269 ? 0.7106 0.6135 0.6544 -0.0755 -0.0749 0.0056  565 PRO A C   
2139 O O   . PRO A 269 ? 0.6720 0.5890 0.6309 -0.0480 -0.0746 -0.0005 565 PRO A O   
2140 C CB  . PRO A 269 ? 0.7787 0.6057 0.6667 -0.0704 -0.0828 0.0056  565 PRO A CB  
2141 C CG  . PRO A 269 ? 0.9187 0.7155 0.7769 -0.0338 -0.0851 0.0020  565 PRO A CG  
2142 C CD  . PRO A 269 ? 0.9526 0.6958 0.7527 -0.0355 -0.0876 0.0076  565 PRO A CD  
2143 N N   . ALA A 270 ? 0.6498 0.5953 0.6228 -0.0962 -0.0707 0.0079  566 ALA A N   
2144 C CA  . ALA A 270 ? 0.5631 0.5571 0.5761 -0.0857 -0.0655 0.0038  566 ALA A CA  
2145 C C   . ALA A 270 ? 0.5890 0.6348 0.6427 -0.0966 -0.0614 0.0033  566 ALA A C   
2146 O O   . ALA A 270 ? 0.5560 0.6248 0.6096 -0.1172 -0.0591 0.0084  566 ALA A O   
2147 C CB  . ALA A 270 ? 0.5448 0.5288 0.5342 -0.0917 -0.0640 0.0077  566 ALA A CB  
2148 N N   . VAL A 271 ? 0.5432 0.6077 0.6268 -0.0824 -0.0607 -0.0024 567 VAL A N   
2149 C CA  . VAL A 271 ? 0.5455 0.6509 0.6595 -0.0851 -0.0578 -0.0030 567 VAL A CA  
2150 C C   . VAL A 271 ? 0.5564 0.6949 0.6889 -0.0768 -0.0521 -0.0057 567 VAL A C   
2151 O O   . VAL A 271 ? 0.6367 0.7679 0.7712 -0.0636 -0.0506 -0.0111 567 VAL A O   
2152 C CB  . VAL A 271 ? 0.5145 0.6171 0.6437 -0.0723 -0.0587 -0.0078 567 VAL A CB  
2153 C CG1 . VAL A 271 ? 0.5023 0.6399 0.6560 -0.0656 -0.0554 -0.0095 567 VAL A CG1 
2154 C CG2 . VAL A 271 ? 0.5399 0.6173 0.6515 -0.0819 -0.0639 -0.0045 567 VAL A CG2 
2155 N N   . SER A 272 ? 0.4967 0.6753 0.6404 -0.0840 -0.0491 -0.0025 568 SER A N   
2156 C CA  . SER A 272 ? 0.5067 0.7160 0.6616 -0.0735 -0.0431 -0.0050 568 SER A CA  
2157 C C   . SER A 272 ? 0.4605 0.7086 0.6347 -0.0573 -0.0398 -0.0074 568 SER A C   
2158 O O   . SER A 272 ? 0.5956 0.8626 0.7734 -0.0421 -0.0345 -0.0109 568 SER A O   
2159 C CB  . SER A 272 ? 0.6881 0.9154 0.8303 -0.0929 -0.0407 0.0014  568 SER A CB  
2160 O OG  . SER A 272 ? 0.6221 0.8729 0.7610 -0.1165 -0.0426 0.0082  568 SER A OG  
2161 N N   . ASN A 273 ? 0.5473 0.8046 0.7289 -0.0566 -0.0429 -0.0060 569 ASN A N   
2162 C CA  . ASN A 273 ? 0.5670 0.8642 0.7608 -0.0372 -0.0407 -0.0071 569 ASN A CA  
2163 C C   . ASN A 273 ? 0.6120 0.8750 0.8011 -0.0127 -0.0404 -0.0136 569 ASN A C   
2164 O O   . ASN A 273 ? 0.5524 0.8347 0.7412 0.0099  -0.0390 -0.0149 569 ASN A O   
2165 C CB  . ASN A 273 ? 0.6366 0.9734 0.8382 -0.0509 -0.0450 -0.0010 569 ASN A CB  
2166 C CG  . ASN A 273 ? 0.6187 0.9154 0.8141 -0.0607 -0.0515 -0.0003 569 ASN A CG  
2167 O OD1 . ASN A 273 ? 0.5156 0.7599 0.7017 -0.0592 -0.0523 -0.0037 569 ASN A OD1 
2168 N ND2 . ASN A 273 ? 0.5435 0.8710 0.7435 -0.0707 -0.0561 0.0038  569 ASN A ND2 
2169 N N   . MET A 274 ? 0.5307 0.7446 0.7115 -0.0163 -0.0417 -0.0177 570 MET A N   
2170 C CA  . MET A 274 ? 0.4950 0.6737 0.6658 -0.0025 -0.0414 -0.0232 570 MET A CA  
2171 C C   . MET A 274 ? 0.6205 0.7783 0.7763 0.0100  -0.0368 -0.0303 570 MET A C   
2172 O O   . MET A 274 ? 0.6202 0.7936 0.7766 0.0107  -0.0339 -0.0311 570 MET A O   
2173 C CB  . MET A 274 ? 0.5733 0.7209 0.7428 -0.0163 -0.0449 -0.0239 570 MET A CB  
2174 C CG  . MET A 274 ? 0.5536 0.7104 0.7288 -0.0246 -0.0497 -0.0181 570 MET A CG  
2175 S SD  . MET A 274 ? 0.5949 0.7154 0.7641 -0.0336 -0.0524 -0.0201 570 MET A SD  
2176 C CE  . MET A 274 ? 0.6286 0.7265 0.7882 -0.0213 -0.0500 -0.0242 570 MET A CE  
2177 N N   . LEU A 275 ? 0.6376 0.7551 0.7738 0.0173  -0.0361 -0.0354 571 LEU A N   
2178 C CA  . LEU A 275 ? 0.6230 0.7082 0.7320 0.0278  -0.0323 -0.0428 571 LEU A CA  
2179 C C   . LEU A 275 ? 0.6913 0.7381 0.7874 0.0091  -0.0331 -0.0482 571 LEU A C   
2180 O O   . LEU A 275 ? 0.7085 0.7369 0.8005 0.0017  -0.0347 -0.0475 571 LEU A O   
2181 C CB  . LEU A 275 ? 0.5488 0.6152 0.6304 0.0557  -0.0304 -0.0438 571 LEU A CB  
2182 C CG  . LEU A 275 ? 0.8038 0.8371 0.8467 0.0770  -0.0260 -0.0506 571 LEU A CG  
2183 C CD1 . LEU A 275 ? 1.0384 1.0777 1.0612 0.1151  -0.0248 -0.0490 571 LEU A CD1 
2184 C CD2 . LEU A 275 ? 0.7721 0.7349 0.7750 0.0633  -0.0255 -0.0579 571 LEU A CD2 
2185 N N   . LEU A 276 ? 0.5555 0.5965 0.6451 0.0001  -0.0320 -0.0537 572 LEU A N   
2186 C CA  . LEU A 276 ? 0.5467 0.5640 0.6229 -0.0204 -0.0327 -0.0600 572 LEU A CA  
2187 C C   . LEU A 276 ? 0.6969 0.6594 0.7259 -0.0188 -0.0298 -0.0669 572 LEU A C   
2188 O O   . LEU A 276 ? 0.8214 0.7683 0.8285 -0.0025 -0.0273 -0.0699 572 LEU A O   
2189 C CB  . LEU A 276 ? 0.5387 0.5822 0.6289 -0.0309 -0.0342 -0.0625 572 LEU A CB  
2190 C CG  . LEU A 276 ? 0.6714 0.7062 0.7472 -0.0519 -0.0353 -0.0706 572 LEU A CG  
2191 C CD1 . LEU A 276 ? 0.7320 0.7727 0.8149 -0.0677 -0.0368 -0.0703 572 LEU A CD1 
2192 C CD2 . LEU A 276 ? 0.5707 0.6380 0.6604 -0.0551 -0.0379 -0.0723 572 LEU A CD2 
2193 N N   . GLU A 277 ? 0.7503 0.6795 0.7573 -0.0361 -0.0299 -0.0694 573 GLU A N   
2194 C CA  . GLU A 277 ? 0.8349 0.6973 0.7836 -0.0425 -0.0275 -0.0760 573 GLU A CA  
2195 C C   . GLU A 277 ? 0.8437 0.7032 0.7813 -0.0805 -0.0282 -0.0828 573 GLU A C   
2196 O O   . GLU A 277 ? 0.8986 0.7904 0.8611 -0.1007 -0.0295 -0.0813 573 GLU A O   
2197 C CB  . GLU A 277 ? 1.0666 0.8823 0.9837 -0.0342 -0.0266 -0.0729 573 GLU A CB  
2198 C CG  . GLU A 277 ? 1.2576 1.0449 1.1467 0.0057  -0.0253 -0.0709 573 GLU A CG  
2199 C CD  . GLU A 277 ? 1.4050 1.1193 1.2359 0.0130  -0.0245 -0.0705 573 GLU A CD  
2200 O OE1 . GLU A 277 ? 1.4560 1.1217 1.2498 -0.0192 -0.0235 -0.0743 573 GLU A OE1 
2201 O OE2 . GLU A 277 ? 1.4405 1.1485 1.2602 0.0498  -0.0249 -0.0661 573 GLU A OE2 
2202 N N   . ILE A 278 ? 0.8147 0.6397 0.7131 -0.0900 -0.0275 -0.0906 574 ILE A N   
2203 C CA  . ILE A 278 ? 0.9267 0.7557 0.8110 -0.1296 -0.0289 -0.0982 574 ILE A CA  
2204 C C   . ILE A 278 ? 1.0686 0.8096 0.8736 -0.1425 -0.0270 -0.1059 574 ILE A C   
2205 O O   . ILE A 278 ? 1.1396 0.8476 0.9162 -0.1217 -0.0261 -0.1094 574 ILE A O   
2206 C CB  . ILE A 278 ? 0.8254 0.7152 0.7469 -0.1316 -0.0321 -0.1008 574 ILE A CB  
2207 C CG1 . ILE A 278 ? 0.7399 0.7010 0.7254 -0.1176 -0.0343 -0.0931 574 ILE A CG1 
2208 C CG2 . ILE A 278 ? 0.8576 0.7593 0.7621 -0.1728 -0.0344 -0.1093 574 ILE A CG2 
2209 C CD1 . ILE A 278 ? 0.7512 0.7615 0.7641 -0.1138 -0.0376 -0.0944 574 ILE A CD1 
2210 N N   . GLY A 279 ? 1.0930 0.7919 0.8559 -0.1769 -0.0260 -0.1084 575 GLY A N   
2211 C CA  . GLY A 279 ? 1.1629 0.7624 0.8351 -0.1956 -0.0245 -0.1158 575 GLY A CA  
2212 C C   . GLY A 279 ? 1.2385 0.7606 0.8597 -0.1501 -0.0223 -0.1153 575 GLY A C   
2213 O O   . GLY A 279 ? 1.4180 0.8777 0.9785 -0.1488 -0.0220 -0.1229 575 GLY A O   
2214 N N   . GLY A 280 ? 1.2483 0.7760 0.8901 -0.1107 -0.0211 -0.1068 576 GLY A N   
2215 C CA  . GLY A 280 ? 1.2999 0.7692 0.8964 -0.0607 -0.0193 -0.1060 576 GLY A CA  
2216 C C   . GLY A 280 ? 1.2134 0.7384 0.8520 -0.0216 -0.0189 -0.1054 576 GLY A C   
2217 O O   . GLY A 280 ? 1.3416 0.8507 0.9628 0.0266  -0.0171 -0.1028 576 GLY A O   
2218 N N   . LEU A 281 ? 1.0714 0.6650 0.7629 -0.0396 -0.0204 -0.1073 577 LEU A N   
2219 C CA  . LEU A 281 ? 1.1510 0.8007 0.8830 -0.0079 -0.0194 -0.1058 577 LEU A CA  
2220 C C   . LEU A 281 ? 1.0743 0.8062 0.8819 0.0088  -0.0201 -0.0953 577 LEU A C   
2221 O O   . LEU A 281 ? 0.9976 0.7653 0.8451 -0.0138 -0.0226 -0.0909 577 LEU A O   
2222 C CB  . LEU A 281 ? 1.1229 0.8055 0.8727 -0.0337 -0.0212 -0.1118 577 LEU A CB  
2223 C CG  . LEU A 281 ? 1.1640 0.7738 0.8408 -0.0575 -0.0217 -0.1232 577 LEU A CG  
2224 C CD1 . LEU A 281 ? 1.0770 0.7417 0.7864 -0.0827 -0.0249 -0.1278 577 LEU A CD1 
2225 C CD2 . LEU A 281 ? 1.1620 0.6949 0.7674 -0.0189 -0.0179 -0.1280 577 LEU A CD2 
2226 N N   . GLU A 282 ? 1.0281 0.7907 0.8514 0.0479  -0.0178 -0.0916 578 GLU A N   
2227 C CA  . GLU A 282 ? 0.9893 0.8231 0.8723 0.0624  -0.0186 -0.0818 578 GLU A CA  
2228 C C   . GLU A 282 ? 0.8146 0.7185 0.7457 0.0632  -0.0179 -0.0793 578 GLU A C   
2229 O O   . GLU A 282 ? 0.8658 0.7741 0.7820 0.0847  -0.0143 -0.0821 578 GLU A O   
2230 C CB  . GLU A 282 ? 1.0303 0.8530 0.8909 0.1047  -0.0168 -0.0783 578 GLU A CB  
2231 C CG  . GLU A 282 ? 1.1935 0.9386 0.9989 0.1066  -0.0178 -0.0795 578 GLU A CG  
2232 C CD  . GLU A 282 ? 1.2684 1.0177 1.0615 0.1506  -0.0178 -0.0742 578 GLU A CD  
2233 O OE1 . GLU A 282 ? 1.2651 1.0524 1.0625 0.1882  -0.0153 -0.0737 578 GLU A OE1 
2234 O OE2 . GLU A 282 ? 1.1939 0.9147 0.9732 0.1483  -0.0202 -0.0706 578 GLU A OE2 
2235 N N   . PHE A 283 ? 0.7161 0.6700 0.6983 0.0412  -0.0210 -0.0738 579 PHE A N   
2236 C CA  . PHE A 283 ? 0.7001 0.7119 0.7213 0.0383  -0.0209 -0.0700 579 PHE A CA  
2237 C C   . PHE A 283 ? 0.6466 0.7083 0.7035 0.0474  -0.0213 -0.0602 579 PHE A C   
2238 O O   . PHE A 283 ? 0.6366 0.7127 0.7183 0.0318  -0.0250 -0.0552 579 PHE A O   
2239 C CB  . PHE A 283 ? 0.6343 0.6573 0.6739 0.0090  -0.0249 -0.0715 579 PHE A CB  
2240 C CG  . PHE A 283 ? 0.6814 0.6676 0.6875 -0.0051 -0.0254 -0.0813 579 PHE A CG  
2241 C CD1 . PHE A 283 ? 0.6320 0.5837 0.6164 -0.0267 -0.0274 -0.0862 579 PHE A CD1 
2242 C CD2 . PHE A 283 ? 0.7832 0.7705 0.7759 0.0001  -0.0237 -0.0859 579 PHE A CD2 
2243 C CE1 . PHE A 283 ? 0.7598 0.6797 0.7084 -0.0468 -0.0284 -0.0958 579 PHE A CE1 
2244 C CE2 . PHE A 283 ? 0.8864 0.8394 0.8442 -0.0163 -0.0251 -0.0957 579 PHE A CE2 
2245 C CZ  . PHE A 283 ? 0.9384 0.8581 0.8735 -0.0415 -0.0277 -0.1007 579 PHE A CZ  
2246 N N   . SER A 284 ? 0.7164 0.8076 0.7727 0.0724  -0.0173 -0.0580 580 SER A N   
2247 C CA  . SER A 284 ? 0.5942 0.7406 0.6790 0.0803  -0.0175 -0.0495 580 SER A CA  
2248 C C   . SER A 284 ? 0.6227 0.8162 0.7429 0.0558  -0.0190 -0.0424 580 SER A C   
2249 O O   . SER A 284 ? 0.6653 0.8997 0.8071 0.0503  -0.0206 -0.0351 580 SER A O   
2250 C CB  . SER A 284 ? 0.6272 0.8013 0.6978 0.1158  -0.0122 -0.0503 580 SER A CB  
2251 O OG  . SER A 284 ? 0.6974 0.8787 0.7588 0.1200  -0.0073 -0.0542 580 SER A OG  
2252 N N   . ALA A 285 ? 0.7120 0.8978 0.8325 0.0406  -0.0189 -0.0443 581 ALA A N   
2253 C CA  . ALA A 285 ? 0.5990 0.8136 0.7392 0.0192  -0.0206 -0.0375 581 ALA A CA  
2254 C C   . ALA A 285 ? 0.6778 0.8592 0.8143 0.0035  -0.0251 -0.0405 581 ALA A C   
2255 O O   . ALA A 285 ? 0.6149 0.7814 0.7383 0.0047  -0.0242 -0.0465 581 ALA A O   
2256 C CB  . ALA A 285 ? 0.4883 0.7400 0.6282 0.0228  -0.0149 -0.0355 581 ALA A CB  
2257 N N   . CYS A 286 ? 0.5984 0.7723 0.7443 -0.0094 -0.0301 -0.0368 582 CYS A N   
2258 C CA  . CYS A 286 ? 0.5500 0.7017 0.6926 -0.0183 -0.0345 -0.0403 582 CYS A CA  
2259 C C   . CYS A 286 ? 0.5712 0.7230 0.7191 -0.0288 -0.0392 -0.0337 582 CYS A C   
2260 O O   . CYS A 286 ? 0.5286 0.6673 0.6780 -0.0310 -0.0427 -0.0352 582 CYS A O   
2261 C CB  . CYS A 286 ? 0.5395 0.6668 0.6759 -0.0171 -0.0351 -0.0469 582 CYS A CB  
2262 S SG  . CYS A 286 ? 0.5658 0.6899 0.7085 -0.0127 -0.0355 -0.0425 582 CYS A SG  
2263 N N   . PRO A 287 ? 0.5586 0.7207 0.7027 -0.0361 -0.0392 -0.0264 583 PRO A N   
2264 C CA  . PRO A 287 ? 0.4250 0.5725 0.5609 -0.0466 -0.0439 -0.0199 583 PRO A CA  
2265 C C   . PRO A 287 ? 0.5108 0.6358 0.6375 -0.0407 -0.0488 -0.0233 583 PRO A C   
2266 O O   . PRO A 287 ? 0.4833 0.6105 0.6069 -0.0339 -0.0493 -0.0282 583 PRO A O   
2267 C CB  . PRO A 287 ? 0.4734 0.6268 0.5945 -0.0592 -0.0425 -0.0125 583 PRO A CB  
2268 C CG  . PRO A 287 ? 0.6570 0.8246 0.7789 -0.0511 -0.0381 -0.0166 583 PRO A CG  
2269 C CD  . PRO A 287 ? 0.6354 0.8152 0.7738 -0.0372 -0.0350 -0.0243 583 PRO A CD  
2270 N N   . PHE A 288 ? 0.4785 0.5876 0.6009 -0.0418 -0.0525 -0.0213 584 PHE A N   
2271 C CA  . PHE A 288 ? 0.4706 0.5682 0.5855 -0.0315 -0.0566 -0.0248 584 PHE A CA  
2272 C C   . PHE A 288 ? 0.5983 0.6642 0.6869 -0.0321 -0.0609 -0.0187 584 PHE A C   
2273 O O   . PHE A 288 ? 0.5599 0.6161 0.6451 -0.0447 -0.0610 -0.0138 584 PHE A O   
2274 C CB  . PHE A 288 ? 0.5504 0.6606 0.6841 -0.0287 -0.0554 -0.0315 584 PHE A CB  
2275 C CG  . PHE A 288 ? 0.6974 0.8030 0.8398 -0.0347 -0.0541 -0.0292 584 PHE A CG  
2276 C CD1 . PHE A 288 ? 0.5819 0.6720 0.7163 -0.0346 -0.0572 -0.0263 584 PHE A CD1 
2277 C CD2 . PHE A 288 ? 0.6617 0.7765 0.8157 -0.0369 -0.0502 -0.0305 584 PHE A CD2 
2278 C CE1 . PHE A 288 ? 0.5103 0.5983 0.6521 -0.0399 -0.0567 -0.0243 584 PHE A CE1 
2279 C CE2 . PHE A 288 ? 0.5446 0.6574 0.7038 -0.0383 -0.0499 -0.0283 584 PHE A CE2 
2280 C CZ  . PHE A 288 ? 0.5639 0.6653 0.7192 -0.0415 -0.0533 -0.0252 584 PHE A CZ  
2281 N N   . SER A 289 ? 0.7168 0.7657 0.7816 -0.0173 -0.0651 -0.0193 585 SER A N   
2282 C CA  . SER A 289 ? 0.7731 0.7770 0.7978 -0.0134 -0.0696 -0.0140 585 SER A CA  
2283 C C   . SER A 289 ? 0.6974 0.7000 0.7120 0.0124  -0.0731 -0.0187 585 SER A C   
2284 O O   . SER A 289 ? 0.6137 0.6540 0.6470 0.0264  -0.0729 -0.0251 585 SER A O   
2285 C CB  . SER A 289 ? 0.7672 0.7357 0.7508 -0.0175 -0.0715 -0.0074 585 SER A CB  
2286 O OG  . SER A 289 ? 0.6828 0.6622 0.6613 0.0014  -0.0729 -0.0105 585 SER A OG  
2287 N N   . GLY A 290 ? 0.6424 0.6048 0.6251 0.0176  -0.0762 -0.0158 586 GLY A N   
2288 C CA  . GLY A 290 ? 0.7182 0.6714 0.6763 0.0487  -0.0798 -0.0192 586 GLY A CA  
2289 C C   . GLY A 290 ? 0.8637 0.7405 0.7525 0.0588  -0.0849 -0.0133 586 GLY A C   
2290 O O   . GLY A 290 ? 0.8375 0.6732 0.6875 0.0541  -0.0871 -0.0078 586 GLY A O   
2291 N N   . TRP A 291 ? 0.7301 0.5813 0.5960 0.0719  -0.0867 -0.0146 587 TRP A N   
2292 C CA  . TRP A 291 ? 0.8053 0.5691 0.5956 0.0767  -0.0917 -0.0095 587 TRP A CA  
2293 C C   . TRP A 291 ? 0.8629 0.6102 0.6549 0.0584  -0.0912 -0.0092 587 TRP A C   
2294 O O   . TRP A 291 ? 0.7941 0.5976 0.6417 0.0528  -0.0873 -0.0134 587 TRP A O   
2295 C CB  . TRP A 291 ? 0.8400 0.5738 0.5766 0.1261  -0.0961 -0.0121 587 TRP A CB  
2296 C CG  . TRP A 291 ? 0.9827 0.7831 0.7559 0.1570  -0.0941 -0.0203 587 TRP A CG  
2297 C CD1 . TRP A 291 ? 0.9374 0.7369 0.7075 0.1678  -0.0930 -0.0237 587 TRP A CD1 
2298 C CD2 . TRP A 291 ? 0.9566 0.8396 0.7730 0.1782  -0.0927 -0.0264 587 TRP A CD2 
2299 N NE1 . TRP A 291 ? 0.9536 0.8341 0.7637 0.1937  -0.0901 -0.0312 587 TRP A NE1 
2300 C CE2 . TRP A 291 ? 1.0254 0.9598 0.8643 0.1987  -0.0902 -0.0331 587 TRP A CE2 
2301 C CE3 . TRP A 291 ? 1.0225 0.9439 0.8593 0.1794  -0.0933 -0.0271 587 TRP A CE3 
2302 C CZ2 . TRP A 291 ? 1.0124 1.0399 0.8939 0.2161  -0.0883 -0.0402 587 TRP A CZ2 
2303 C CZ3 . TRP A 291 ? 0.9864 0.9956 0.8641 0.1981  -0.0925 -0.0346 587 TRP A CZ3 
2304 C CH2 . TRP A 291 ? 1.0634 1.1272 0.9633 0.2143  -0.0899 -0.0410 587 TRP A CH2 
2305 N N   . TYR A 292 ? 0.9857 0.6510 0.7107 0.0468  -0.0956 -0.0041 588 TYR A N   
2306 C CA  . TYR A 292 ? 1.0368 0.6841 0.7592 0.0227  -0.0963 -0.0033 588 TYR A CA  
2307 C C   . TYR A 292 ? 0.9780 0.6139 0.6834 0.0559  -0.0971 -0.0090 588 TYR A C   
2308 O O   . TYR A 292 ? 0.9784 0.5785 0.6340 0.0964  -0.0995 -0.0114 588 TYR A O   
2309 C CB  . TYR A 292 ? 1.0933 0.6566 0.7447 -0.0105 -0.1012 0.0040  588 TYR A CB  
2310 C CG  . TYR A 292 ? 1.0627 0.6613 0.7494 -0.0602 -0.0992 0.0094  588 TYR A CG  
2311 C CD1 . TYR A 292 ? 0.9477 0.5277 0.6098 -0.0817 -0.0990 0.0155  588 TYR A CD1 
2312 C CD2 . TYR A 292 ? 0.9737 0.6272 0.7151 -0.0833 -0.0974 0.0085  588 TYR A CD2 
2313 C CE1 . TYR A 292 ? 0.9624 0.5845 0.6555 -0.1252 -0.0965 0.0203  588 TYR A CE1 
2314 C CE2 . TYR A 292 ? 0.9973 0.6919 0.7686 -0.1228 -0.0959 0.0131  588 TYR A CE2 
2315 C CZ  . TYR A 292 ? 0.9637 0.6473 0.7130 -0.1435 -0.0950 0.0187  588 TYR A CZ  
2316 O OH  . TYR A 292 ? 0.9113 0.6478 0.6918 -0.1807 -0.0926 0.0231  588 TYR A OH  
2317 N N   . MET A 293 ? 0.8759 0.5448 0.6205 0.0417  -0.0949 -0.0112 589 MET A N   
2318 C CA  . MET A 293 ? 1.0022 0.6312 0.7080 0.0584  -0.0969 -0.0142 589 MET A CA  
2319 C C   . MET A 293 ? 1.1002 0.6420 0.7381 0.0274  -0.1031 -0.0089 589 MET A C   
2320 O O   . MET A 293 ? 1.1655 0.7173 0.8216 -0.0165 -0.1040 -0.0039 589 MET A O   
2321 C CB  . MET A 293 ? 0.9148 0.6099 0.6837 0.0544  -0.0922 -0.0183 589 MET A CB  
2322 C CG  . MET A 293 ? 0.9327 0.6039 0.6695 0.0811  -0.0923 -0.0229 589 MET A CG  
2323 S SD  . MET A 293 ? 0.8297 0.5847 0.6406 0.0779  -0.0852 -0.0274 589 MET A SD  
2324 C CE  . MET A 293 ? 0.8599 0.6148 0.6983 0.0276  -0.0876 -0.0219 589 MET A CE  
2325 N N   . GLY A 294 ? 1.0885 0.5446 0.6422 0.0507  -0.1075 -0.0102 590 GLY A N   
2326 C CA  . GLY A 294 ? 1.0346 0.3908 0.5050 0.0187  -0.1143 -0.0054 590 GLY A CA  
2327 C C   . GLY A 294 ? 1.1026 0.4827 0.6046 -0.0320 -0.1157 -0.0031 590 GLY A C   
2328 O O   . GLY A 294 ? 1.1850 0.5294 0.6546 -0.0788 -0.1198 0.0027  590 GLY A O   
2329 N N   . THR A 295 ? 1.0490 0.4940 0.6127 -0.0245 -0.1123 -0.0075 591 THR A N   
2330 C CA  . THR A 295 ? 1.0891 0.5478 0.6697 -0.0641 -0.1152 -0.0059 591 THR A CA  
2331 C C   . THR A 295 ? 1.0471 0.5732 0.6875 -0.1056 -0.1143 -0.0007 591 THR A C   
2332 O O   . THR A 295 ? 0.9644 0.4925 0.6000 -0.1463 -0.1189 0.0024  591 THR A O   
2333 C CB  . THR A 295 ? 0.9871 0.4918 0.6111 -0.0418 -0.1117 -0.0115 591 THR A CB  
2334 O OG1 . THR A 295 ? 0.8978 0.4868 0.5978 -0.0189 -0.1039 -0.0140 591 THR A OG1 
2335 C CG2 . THR A 295 ? 1.0568 0.4903 0.6098 -0.0047 -0.1132 -0.0166 591 THR A CG2 
2336 N N   . GLU A 296 ? 0.9405 0.5254 0.6349 -0.0954 -0.1088 -0.0001 592 GLU A N   
2337 C CA  . GLU A 296 ? 0.8690 0.5136 0.6110 -0.1300 -0.1075 0.0046  592 GLU A CA  
2338 C C   . GLU A 296 ? 0.9157 0.5100 0.5983 -0.1737 -0.1130 0.0110  592 GLU A C   
2339 O O   . GLU A 296 ? 1.1109 0.7418 0.8105 -0.2134 -0.1154 0.0145  592 GLU A O   
2340 C CB  . GLU A 296 ? 0.9162 0.6137 0.7081 -0.1105 -0.1011 0.0038  592 GLU A CB  
2341 C CG  . GLU A 296 ? 0.8533 0.6012 0.6985 -0.0752 -0.0955 -0.0025 592 GLU A CG  
2342 C CD  . GLU A 296 ? 0.9158 0.7012 0.7931 -0.0587 -0.0906 -0.0038 592 GLU A CD  
2343 O OE1 . GLU A 296 ? 0.6740 0.5094 0.5953 -0.0742 -0.0876 -0.0021 592 GLU A OE1 
2344 O OE2 . GLU A 296 ? 0.8930 0.6585 0.7478 -0.0292 -0.0901 -0.0067 592 GLU A OE2 
2345 N N   . ILE A 297 ? 1.0326 0.5423 0.6396 -0.1674 -0.1152 0.0126  593 ILE A N   
2346 C CA  . ILE A 297 ? 1.0857 0.5284 0.6177 -0.2133 -0.1204 0.0190  593 ILE A CA  
2347 C C   . ILE A 297 ? 1.2482 0.6245 0.7160 -0.2384 -0.1280 0.0185  593 ILE A C   
2348 O O   . ILE A 297 ? 1.1810 0.5697 0.6395 -0.2920 -0.1321 0.0224  593 ILE A O   
2349 C CB  . ILE A 297 ? 1.2126 0.5705 0.6705 -0.1952 -0.1208 0.0213  593 ILE A CB  
2350 C CG1 . ILE A 297 ? 1.1285 0.5501 0.6465 -0.1672 -0.1141 0.0210  593 ILE A CG1 
2351 C CG2 . ILE A 297 ? 1.3513 0.6385 0.7283 -0.2501 -0.1253 0.0288  593 ILE A CG2 
2352 C CD1 . ILE A 297 ? 1.0930 0.4355 0.5418 -0.1297 -0.1154 0.0210  593 ILE A CD1 
2353 N N   . GLY A 298 ? 1.3463 0.6499 0.7619 -0.2005 -0.1301 0.0134  594 GLY A N   
2354 C CA  . GLY A 298 ? 1.4452 0.6549 0.7721 -0.2221 -0.1379 0.0126  594 GLY A CA  
2355 C C   . GLY A 298 ? 1.3206 0.5864 0.6924 -0.2462 -0.1407 0.0105  594 GLY A C   
2356 O O   . GLY A 298 ? 1.4975 0.7130 0.8104 -0.2894 -0.1482 0.0118  594 GLY A O   
2357 N N   . VAL A 299 ? 1.2744 0.6416 0.7449 -0.2204 -0.1352 0.0074  595 VAL A N   
2358 C CA  . VAL A 299 ? 1.2938 0.7114 0.8036 -0.2363 -0.1380 0.0056  595 VAL A CA  
2359 C C   . VAL A 299 ? 1.1409 0.6621 0.7239 -0.2726 -0.1377 0.0102  595 VAL A C   
2360 O O   . VAL A 299 ? 1.1485 0.6839 0.7194 -0.3180 -0.1444 0.0127  595 VAL A O   
2361 C CB  . VAL A 299 ? 1.1672 0.6204 0.7255 -0.1859 -0.1327 -0.0006 595 VAL A CB  
2362 C CG1 . VAL A 299 ? 1.0719 0.5602 0.6547 -0.2032 -0.1367 -0.0018 595 VAL A CG1 
2363 C CG2 . VAL A 299 ? 1.1333 0.5004 0.6236 -0.1425 -0.1320 -0.0057 595 VAL A CG2 
2364 N N   . ARG A 300 ? 1.0629 0.6594 0.7191 -0.2514 -0.1301 0.0109  596 ARG A N   
2365 C CA  . ARG A 300 ? 1.0261 0.7256 0.7537 -0.2727 -0.1286 0.0142  596 ARG A CA  
2366 C C   . ARG A 300 ? 1.1464 0.8550 0.8530 -0.3181 -0.1300 0.0206  596 ARG A C   
2367 O O   . ARG A 300 ? 1.0625 0.8102 0.7684 -0.3623 -0.1353 0.0239  596 ARG A O   
2368 C CB  . ARG A 300 ? 0.8885 0.6545 0.6927 -0.2313 -0.1198 0.0117  596 ARG A CB  
2369 C CG  . ARG A 300 ? 0.8088 0.5690 0.6317 -0.1907 -0.1169 0.0058  596 ARG A CG  
2370 C CD  . ARG A 300 ? 0.8322 0.6083 0.6606 -0.2022 -0.1223 0.0051  596 ARG A CD  
2371 N NE  . ARG A 300 ? 0.7422 0.6019 0.6217 -0.2206 -0.1236 0.0085  596 ARG A NE  
2372 C CZ  . ARG A 300 ? 0.7236 0.6481 0.6642 -0.1985 -0.1174 0.0081  596 ARG A CZ  
2373 N NH1 . ARG A 300 ? 0.7645 0.6819 0.7248 -0.1647 -0.1099 0.0045  596 ARG A NH1 
2374 N NH2 . ARG A 300 ? 0.6566 0.6537 0.6341 -0.2098 -0.1191 0.0111  596 ARG A NH2 
2375 N N   . ASP A 301 ? 0.8744 0.5531 0.5630 -0.3091 -0.1254 0.0224  597 ASP A N   
2376 C CA  . ASP A 301 ? 0.9650 0.6502 0.6297 -0.3534 -0.1254 0.0290  597 ASP A CA  
2377 C C   . ASP A 301 ? 1.0238 0.6451 0.6056 -0.4096 -0.1341 0.0324  597 ASP A C   
2378 O O   . ASP A 301 ? 1.0815 0.7670 0.6739 -0.4471 -0.1324 0.0381  597 ASP A O   
2379 C CB  . ASP A 301 ? 0.9858 0.6238 0.6250 -0.3322 -0.1202 0.0303  597 ASP A CB  
2380 C CG  . ASP A 301 ? 0.9105 0.6259 0.6319 -0.2921 -0.1119 0.0277  597 ASP A CG  
2381 O OD1 . ASP A 301 ? 0.9829 0.7934 0.7751 -0.2941 -0.1092 0.0274  597 ASP A OD1 
2382 O OD2 . ASP A 301 ? 0.9972 0.6771 0.7081 -0.2573 -0.1085 0.0258  597 ASP A OD2 
2383 N N   . TYR A 302 ? 1.1614 0.6709 0.6631 -0.3992 -0.1384 0.0300  598 TYR A N   
2384 C CA  . TYR A 302 ? 1.2975 0.7497 0.7151 -0.4319 -0.1404 0.0352  598 TYR A CA  
2385 C C   . TYR A 302 ? 1.3907 0.8813 0.8188 -0.4519 -0.1447 0.0348  598 TYR A C   
2386 O O   . TYR A 302 ? 1.4003 0.8955 0.7876 -0.4936 -0.1456 0.0410  598 TYR A O   
2387 C CB  . TYR A 302 ? 1.4794 0.7938 0.7967 -0.4056 -0.1426 0.0334  598 TYR A CB  
2388 C CG  . TYR A 302 ? 1.6292 0.8903 0.9006 -0.4010 -0.1393 0.0372  598 TYR A CG  
2389 C CD1 . TYR A 302 ? 1.6694 0.8223 0.8684 -0.3583 -0.1404 0.0343  598 TYR A CD1 
2390 C CD2 . TYR A 302 ? 1.5615 0.8841 0.8593 -0.4359 -0.1349 0.0437  598 TYR A CD2 
2391 C CE1 . TYR A 302 ? 1.6929 0.7955 0.8454 -0.3509 -0.1380 0.0379  598 TYR A CE1 
2392 C CE2 . TYR A 302 ? 1.6896 0.9609 0.9422 -0.4326 -0.1320 0.0473  598 TYR A CE2 
2393 C CZ  . TYR A 302 ? 1.6802 0.8393 0.8596 -0.3903 -0.1341 0.0444  598 TYR A CZ  
2394 O OH  . TYR A 302 ? 1.4759 0.5819 0.6060 -0.3834 -0.1320 0.0479  598 TYR A OH  
2395 N N   . CYS A 303 ? 1.2990 0.8157 0.7756 -0.4248 -0.1478 0.0279  599 CYS A N   
2396 C CA  . CYS A 303 ? 1.2733 0.7970 0.7390 -0.4382 -0.1530 0.0270  599 CYS A CA  
2397 C C   . CYS A 303 ? 1.2061 0.8476 0.7639 -0.4382 -0.1548 0.0251  599 CYS A C   
2398 O O   . CYS A 303 ? 1.2355 0.8907 0.7865 -0.4511 -0.1596 0.0248  599 CYS A O   
2399 C CB  . CYS A 303 ? 1.3890 0.8098 0.7978 -0.4046 -0.1566 0.0204  599 CYS A CB  
2400 S SG  . CYS A 303 ? 1.5305 0.8046 0.8120 -0.3964 -0.1559 0.0229  599 CYS A SG  
2401 N N   . ASP A 304 ? 1.1187 0.8433 0.7569 -0.4227 -0.1516 0.0240  600 ASP A N   
2402 C CA  . ASP A 304 ? 1.1597 1.0040 0.8759 -0.4243 -0.1529 0.0245  600 ASP A CA  
2403 C C   . ASP A 304 ? 1.2157 1.1141 0.9188 -0.4654 -0.1521 0.0315  600 ASP A C   
2404 O O   . ASP A 304 ? 1.3148 1.1986 0.9799 -0.4932 -0.1477 0.0372  600 ASP A O   
2405 C CB  . ASP A 304 ? 1.1919 1.1158 0.9848 -0.3980 -0.1464 0.0246  600 ASP A CB  
2406 C CG  . ASP A 304 ? 1.1501 1.0720 0.9862 -0.3374 -0.1401 0.0197  600 ASP A CG  
2407 O OD1 . ASP A 304 ? 1.0783 0.9323 0.8828 -0.3190 -0.1418 0.0156  600 ASP A OD1 
2408 O OD2 . ASP A 304 ? 1.0303 1.0184 0.9281 -0.3097 -0.1332 0.0198  600 ASP A OD2 
2409 N N   . ASN A 305 ? 1.1806 1.1407 0.9107 -0.4700 -0.1568 0.0311  601 ASN A N   
2410 C CA  . ASN A 305 ? 1.1308 1.1535 0.8514 -0.5083 -0.1563 0.0374  601 ASN A CA  
2411 C C   . ASN A 305 ? 1.0384 1.1541 0.8009 -0.5159 -0.1486 0.0421  601 ASN A C   
2412 O O   . ASN A 305 ? 1.1336 1.2666 0.8616 -0.5548 -0.1453 0.0484  601 ASN A O   
2413 C CB  . ASN A 305 ? 0.9900 1.0773 0.7439 -0.5034 -0.1629 0.0355  601 ASN A CB  
2414 C CG  . ASN A 305 ? 1.2984 1.3027 0.9869 -0.5200 -0.1697 0.0342  601 ASN A CG  
2415 O OD1 . ASN A 305 ? 1.4983 1.4184 1.1091 -0.5486 -0.1689 0.0376  601 ASN A OD1 
2416 N ND2 . ASN A 305 ? 1.2166 1.2406 0.9302 -0.5011 -0.1768 0.0296  601 ASN A ND2 
2417 N N   . SER A 306 ? 1.0499 1.2253 0.8819 -0.4797 -0.1456 0.0391  602 SER A N   
2418 C CA  . SER A 306 ? 1.0024 1.2692 0.8768 -0.4786 -0.1377 0.0426  602 SER A CA  
2419 C C   . SER A 306 ? 1.0355 1.2530 0.8930 -0.4792 -0.1313 0.0438  602 SER A C   
2420 O O   . SER A 306 ? 1.0054 1.2928 0.9013 -0.4716 -0.1243 0.0456  602 SER A O   
2421 C CB  . SER A 306 ? 0.9513 1.3141 0.9051 -0.4354 -0.1377 0.0393  602 SER A CB  
2422 O OG  . SER A 306 ? 0.9665 1.2842 0.9422 -0.4000 -0.1400 0.0341  602 SER A OG  
2423 N N   . ARG A 307 ? 1.0112 1.1096 0.8091 -0.4846 -0.1335 0.0426  603 ARG A N   
2424 C CA  . ARG A 307 ? 1.1159 1.1600 0.8828 -0.4900 -0.1283 0.0448  603 ARG A CA  
2425 C C   . ARG A 307 ? 1.1898 1.1596 0.8655 -0.5333 -0.1286 0.0506  603 ARG A C   
2426 O O   . ARG A 307 ? 1.3202 1.3385 0.9809 -0.5681 -0.1284 0.0554  603 ARG A O   
2427 C CB  . ARG A 307 ? 1.0106 0.9768 0.7769 -0.4548 -0.1302 0.0389  603 ARG A CB  
2428 C CG  . ARG A 307 ? 1.0051 1.0409 0.8539 -0.4161 -0.1306 0.0338  603 ARG A CG  
2429 C CD  . ARG A 307 ? 0.9135 1.0334 0.8163 -0.4052 -0.1222 0.0360  603 ARG A CD  
2430 N NE  . ARG A 307 ? 0.8922 0.9520 0.7603 -0.4086 -0.1168 0.0381  603 ARG A NE  
2431 C CZ  . ARG A 307 ? 0.8992 0.8952 0.7618 -0.3671 -0.1125 0.0346  603 ARG A CZ  
2432 N NH1 . ARG A 307 ? 0.7419 0.7289 0.6324 -0.3239 -0.1121 0.0289  603 ARG A NH1 
2433 N NH2 . ARG A 307 ? 0.9901 0.9346 0.8175 -0.3698 -0.1087 0.0369  603 ARG A NH2 
2434 N N   . TYR A 308 ? 1.2206 1.0719 0.8290 -0.5305 -0.1296 0.0502  604 TYR A N   
2435 C CA  . TYR A 308 ? 1.2839 1.0572 0.7953 -0.5696 -0.1301 0.0562  604 TYR A CA  
2436 C C   . TYR A 308 ? 1.4615 1.1910 0.9156 -0.5922 -0.1366 0.0570  604 TYR A C   
2437 O O   . TYR A 308 ? 1.5648 1.2864 0.9598 -0.6376 -0.1369 0.0632  604 TYR A O   
2438 C CB  . TYR A 308 ? 1.3973 1.0519 0.8457 -0.5526 -0.1299 0.0554  604 TYR A CB  
2439 C CG  . TYR A 308 ? 1.3621 1.0455 0.8249 -0.5586 -0.1231 0.0591  604 TYR A CG  
2440 C CD1 . TYR A 308 ? 1.2737 1.0177 0.8177 -0.5267 -0.1187 0.0559  604 TYR A CD1 
2441 C CD2 . TYR A 308 ? 1.5619 1.2115 0.9530 -0.5982 -0.1213 0.0656  604 TYR A CD2 
2442 C CE1 . TYR A 308 ? 1.3425 1.1131 0.8985 -0.5322 -0.1122 0.0594  604 TYR A CE1 
2443 C CE2 . TYR A 308 ? 1.5663 1.2427 0.9688 -0.6045 -0.1150 0.0688  604 TYR A CE2 
2444 C CZ  . TYR A 308 ? 1.5004 1.2377 0.9869 -0.5705 -0.1102 0.0660  604 TYR A CZ  
2445 O OH  . TYR A 308 ? 1.5401 1.3045 1.0380 -0.5758 -0.1035 0.0693  604 TYR A OH  
2446 N N   . ASN A 309 ? 1.3029 1.0027 0.7688 -0.5635 -0.1418 0.0509  605 ASN A N   
2447 C CA  . ASN A 309 ? 1.4065 1.0934 0.8403 -0.5823 -0.1477 0.0512  605 ASN A CA  
2448 C C   . ASN A 309 ? 1.6148 1.1852 0.9280 -0.6133 -0.1505 0.0558  605 ASN A C   
2449 O O   . ASN A 309 ? 1.7841 1.3711 1.0554 -0.6609 -0.1514 0.0621  605 ASN A O   
2450 C CB  . ASN A 309 ? 1.3299 1.1488 0.8219 -0.6083 -0.1466 0.0546  605 ASN A CB  
2451 C CG  . ASN A 309 ? 1.3358 1.1592 0.8152 -0.6200 -0.1531 0.0538  605 ASN A CG  
2452 O OD1 . ASN A 309 ? 1.2674 1.0232 0.7301 -0.5951 -0.1581 0.0483  605 ASN A OD1 
2453 N ND2 . ASN A 309 ? 1.3194 1.2228 0.8028 -0.6585 -0.1528 0.0592  605 ASN A ND2 
2454 N N   . ILE A 310 ? 1.5825 1.0336 0.8349 -0.5839 -0.1521 0.0523  606 ILE A N   
2455 C CA  . ILE A 310 ? 1.7400 1.0667 0.8678 -0.6032 -0.1548 0.0561  606 ILE A CA  
2456 C C   . ILE A 310 ? 1.7235 0.9599 0.7869 -0.5889 -0.1610 0.0528  606 ILE A C   
2457 O O   . ILE A 310 ? 1.9086 1.0288 0.8599 -0.5955 -0.1639 0.0549  606 ILE A O   
2458 C CB  . ILE A 310 ? 1.7661 1.0161 0.8529 -0.5780 -0.1520 0.0552  606 ILE A CB  
2459 C CG1 . ILE A 310 ? 1.7575 0.9675 0.8713 -0.5142 -0.1523 0.0467  606 ILE A CG1 
2460 C CG2 . ILE A 310 ? 1.4786 0.8145 0.6235 -0.5946 -0.1457 0.0589  606 ILE A CG2 
2461 C CD1 . ILE A 310 ? 1.5370 0.6594 0.5965 -0.4830 -0.1505 0.0456  606 ILE A CD1 
2462 N N   . LEU A 311 ? 1.6774 0.9611 0.8040 -0.5673 -0.1633 0.0473  607 LEU A N   
2463 C CA  . LEU A 311 ? 1.7227 0.9269 0.7890 -0.5556 -0.1688 0.0443  607 LEU A CA  
2464 C C   . LEU A 311 ? 1.7416 0.9049 0.7190 -0.6092 -0.1726 0.0520  607 LEU A C   
2465 O O   . LEU A 311 ? 1.8626 0.9106 0.7392 -0.6041 -0.1764 0.0522  607 LEU A O   
2466 C CB  . LEU A 311 ? 1.4640 0.7396 0.6149 -0.5332 -0.1710 0.0377  607 LEU A CB  
2467 C CG  . LEU A 311 ? 1.4349 0.7221 0.6505 -0.4760 -0.1687 0.0286  607 LEU A CG  
2468 C CD1 . LEU A 311 ? 1.3864 0.7559 0.6850 -0.4633 -0.1717 0.0229  607 LEU A CD1 
2469 C CD2 . LEU A 311 ? 1.5040 0.6662 0.6407 -0.4329 -0.1689 0.0239  607 LEU A CD2 
2470 N N   . GLU A 312 ? 1.7984 1.0548 0.8067 -0.6599 -0.1713 0.0585  608 GLU A N   
2471 C CA  . GLU A 312 ? 2.1290 1.3538 1.0493 -0.7192 -0.1741 0.0669  608 GLU A CA  
2472 C C   . GLU A 312 ? 2.2002 1.2870 0.9894 -0.7299 -0.1752 0.0704  608 GLU A C   
2473 O O   . GLU A 312 ? 2.1997 1.1759 0.8867 -0.7336 -0.1801 0.0715  608 GLU A O   
2474 C CB  . GLU A 312 ? 2.2385 1.5911 1.2115 -0.7677 -0.1703 0.0731  608 GLU A CB  
2475 C CG  . GLU A 312 ? 2.2026 1.6967 1.2893 -0.7636 -0.1701 0.0707  608 GLU A CG  
2476 C CD  . GLU A 312 ? 2.3619 1.8660 1.4191 -0.7973 -0.1754 0.0735  608 GLU A CD  
2477 O OE1 . GLU A 312 ? 2.4763 1.8664 1.4489 -0.7967 -0.1804 0.0731  608 GLU A OE1 
2478 O OE2 . GLU A 312 ? 2.3500 1.9774 1.4660 -0.8228 -0.1745 0.0761  608 GLU A OE2 
2479 N N   . GLU A 313 ? 2.2246 1.3153 1.0118 -0.7337 -0.1709 0.0722  609 GLU A N   
2480 C CA  . GLU A 313 ? 2.4782 1.4471 1.1355 -0.7527 -0.1726 0.0758  609 GLU A CA  
2481 C C   . GLU A 313 ? 2.5173 1.3492 1.0997 -0.6970 -0.1756 0.0700  609 GLU A C   
2482 O O   . GLU A 313 ? 2.8207 1.5276 1.2700 -0.7092 -0.1797 0.0723  609 GLU A O   
2483 C CB  . GLU A 313 ? 2.6855 1.6978 1.3633 -0.7692 -0.1673 0.0782  609 GLU A CB  
2484 C CG  . GLU A 313 ? 2.8172 1.9200 1.5008 -0.8387 -0.1652 0.0859  609 GLU A CG  
2485 C CD  . GLU A 313 ? 3.0122 2.0187 1.5508 -0.8965 -0.1700 0.0921  609 GLU A CD  
2486 O OE1 . GLU A 313 ? 3.0627 1.9972 1.5337 -0.9032 -0.1755 0.0931  609 GLU A OE1 
2487 O OE2 . GLU A 313 ? 3.0571 2.0582 1.5451 -0.9370 -0.1684 0.0959  609 GLU A OE2 
2488 N N   . VAL A 314 ? 2.2792 1.1314 0.9380 -0.6349 -0.1736 0.0622  610 VAL A N   
2489 C CA  . VAL A 314 ? 2.2789 1.0127 0.8687 -0.5767 -0.1757 0.0561  610 VAL A CA  
2490 C C   . VAL A 314 ? 2.3282 0.9869 0.8443 -0.5741 -0.1812 0.0559  610 VAL A C   
2491 O O   . VAL A 314 ? 2.3297 0.8592 0.7197 -0.5617 -0.1849 0.0562  610 VAL A O   
2492 C CB  . VAL A 314 ? 2.1774 0.9610 0.8686 -0.5135 -0.1715 0.0478  610 VAL A CB  
2493 C CG1 . VAL A 314 ? 2.2456 0.9219 0.8695 -0.4493 -0.1732 0.0410  610 VAL A CG1 
2494 C CG2 . VAL A 314 ? 2.0418 0.8760 0.7844 -0.5139 -0.1663 0.0488  610 VAL A CG2 
2495 N N   . ALA A 315 ? 2.1575 0.8946 0.7473 -0.5844 -0.1822 0.0552  611 ALA A N   
2496 C CA  . ALA A 315 ? 2.3115 0.9845 0.8362 -0.5862 -0.1874 0.0555  611 ALA A CA  
2497 C C   . ALA A 315 ? 2.4998 1.0945 0.8985 -0.6455 -0.1916 0.0648  611 ALA A C   
2498 O O   . ALA A 315 ? 2.5771 1.0571 0.8657 -0.6377 -0.1961 0.0658  611 ALA A O   
2499 C CB  . ALA A 315 ? 2.1743 0.9563 0.8045 -0.5935 -0.1879 0.0531  611 ALA A CB  
2500 N N   . LYS A 316 ? 2.4943 1.1488 0.9024 -0.7050 -0.1899 0.0716  612 LYS A N   
2501 C CA  . LYS A 316 ? 2.6246 1.2056 0.9064 -0.7673 -0.1935 0.0804  612 LYS A CA  
2502 C C   . LYS A 316 ? 2.8186 1.2414 0.9664 -0.7419 -0.1959 0.0780  612 LYS A C   
2503 O O   . LYS A 316 ? 2.9401 1.2590 0.9953 -0.7402 -0.1998 0.0766  612 LYS A O   
2504 C CB  . LYS A 316 ? 2.4770 1.1550 0.7966 -0.8268 -0.1898 0.0864  612 LYS A CB  
2505 C CG  . LYS A 316 ? 2.3834 1.1995 0.7899 -0.8720 -0.1887 0.0905  612 LYS A CG  
2506 C CD  . LYS A 316 ? 2.4603 1.3256 0.8342 -0.9461 -0.1869 0.0989  612 LYS A CD  
2507 C CE  . LYS A 316 ? 2.7203 1.4398 0.9225 -0.9881 -0.1917 0.1043  612 LYS A CE  
2508 N NZ  . LYS A 316 ? 2.6928 1.4602 0.8612 -1.0675 -0.1905 0.1106  612 LYS A NZ  
2509 N N   . LYS A 317 ? 2.7366 1.1478 0.8917 -0.7148 -0.1926 0.0743  613 LYS A N   
2510 C CA  . LYS A 317 ? 2.9063 1.1833 0.9577 -0.6840 -0.1933 0.0685  613 LYS A CA  
2511 C C   . LYS A 317 ? 3.0148 1.2039 1.0274 -0.6134 -0.1951 0.0612  613 LYS A C   
2512 O O   . LYS A 317 ? 3.2054 1.2713 1.1109 -0.5921 -0.1967 0.0574  613 LYS A O   
2513 C CB  . LYS A 317 ? 2.7271 1.0215 0.8074 -0.6627 -0.1892 0.0656  613 LYS A CB  
2514 C CG  . LYS A 317 ? 2.8140 1.1248 0.8660 -0.7267 -0.1878 0.0705  613 LYS A CG  
2515 C CD  . LYS A 317 ? 2.7244 1.1908 0.8902 -0.7648 -0.1842 0.0765  613 LYS A CD  
2516 C CE  . LYS A 317 ? 2.8552 1.3453 0.9902 -0.8316 -0.1825 0.0813  613 LYS A CE  
2517 N NZ  . LYS A 317 ? 2.7761 1.4212 1.0234 -0.8572 -0.1777 0.0861  613 LYS A NZ  
2518 N N   . MET A 318 ? 2.9372 1.1878 1.0317 -0.5753 -0.1947 0.0590  614 MET A N   
2519 C CA  . MET A 318 ? 2.9046 1.0842 0.9651 -0.5119 -0.1960 0.0524  614 MET A CA  
2520 C C   . MET A 318 ? 2.9453 1.0663 0.9353 -0.5399 -0.2006 0.0552  614 MET A C   
2521 O O   . MET A 318 ? 3.1468 1.1848 1.0792 -0.4916 -0.2018 0.0500  614 MET A O   
2522 C CB  . MET A 318 ? 2.6176 0.8825 0.7861 -0.4643 -0.1941 0.0487  614 MET A CB  
2523 C CG  . MET A 318 ? 2.6448 0.9533 0.8822 -0.4193 -0.1888 0.0428  614 MET A CG  
2524 S SD  . MET A 318 ? 2.3518 0.7705 0.7432 -0.3603 -0.1836 0.0331  614 MET A SD  
2525 C CE  . MET A 318 ? 2.4354 0.7570 0.7431 -0.2997 -0.1861 0.0280  614 MET A CE  
2526 N N   . ASP A 319 ? 2.9969 1.1622 0.9886 -0.6158 -0.2028 0.0634  615 ASP A N   
2527 C CA  . ASP A 319 ? 3.1562 1.2839 1.0934 -0.6502 -0.2074 0.0672  615 ASP A CA  
2528 C C   . ASP A 319 ? 2.9988 1.1615 0.9950 -0.6089 -0.2083 0.0643  615 ASP A C   
2529 O O   . ASP A 319 ? 3.0093 1.0902 0.9572 -0.5531 -0.2091 0.0580  615 ASP A O   
2530 C CB  . ASP A 319 ? 3.3840 1.3582 1.1766 -0.6460 -0.2104 0.0651  615 ASP A CB  
2531 C CG  . ASP A 319 ? 3.5103 1.4482 1.2308 -0.7136 -0.2152 0.0717  615 ASP A CG  
2532 O OD1 . ASP A 319 ? 3.4957 1.5011 1.2350 -0.7859 -0.2154 0.0790  615 ASP A OD1 
2533 O OD2 . ASP A 319 ? 3.6052 1.4486 1.2477 -0.6943 -0.2187 0.0698  615 ASP A OD2 
2534 N N   . LEU A 320 ? 2.8541 1.1401 0.9527 -0.6347 -0.2081 0.0688  616 LEU A N   
2535 C CA  . LEU A 320 ? 2.7124 1.0573 0.9021 -0.5932 -0.2076 0.0617  616 LEU A CA  
2536 C C   . LEU A 320 ? 2.7273 1.1363 0.9521 -0.6443 -0.2108 0.0656  616 LEU A C   
2537 O O   . LEU A 320 ? 2.7859 1.2533 1.0207 -0.7102 -0.2113 0.0729  616 LEU A O   
2538 C CB  . LEU A 320 ? 2.3858 0.8488 0.7223 -0.5556 -0.2018 0.0533  616 LEU A CB  
2539 C CG  . LEU A 320 ? 2.4435 0.8578 0.7673 -0.4901 -0.1981 0.0469  616 LEU A CG  
2540 C CD1 . LEU A 320 ? 2.3802 0.9141 0.8512 -0.4574 -0.1925 0.0390  616 LEU A CD1 
2541 C CD2 . LEU A 320 ? 2.4747 0.7776 0.7107 -0.4312 -0.1998 0.0427  616 LEU A CD2 
2542 N N   . ASP A 321 ? 2.6543 1.0573 0.8985 -0.6118 -0.2128 0.0600  617 ASP A N   
2543 C CA  . ASP A 321 ? 2.6020 1.0768 0.8958 -0.6493 -0.2162 0.0610  617 ASP A CA  
2544 C C   . ASP A 321 ? 2.3787 1.0183 0.8224 -0.6649 -0.2133 0.0579  617 ASP A C   
2545 O O   . ASP A 321 ? 2.1699 0.8804 0.7134 -0.6239 -0.2121 0.0486  617 ASP A O   
2546 C CB  . ASP A 321 ? 2.6873 1.1237 0.9782 -0.6011 -0.2183 0.0537  617 ASP A CB  
2547 C CG  . ASP A 321 ? 2.8109 1.2842 1.1129 -0.6433 -0.2235 0.0557  617 ASP A CG  
2548 O OD1 . ASP A 321 ? 2.8083 1.2465 1.0993 -0.6107 -0.2257 0.0503  617 ASP A OD1 
2549 O OD2 . ASP A 321 ? 2.8516 1.3910 1.1710 -0.7083 -0.2252 0.0627  617 ASP A OD2 
2550 N N   . MET A 322 ? 2.4777 1.1793 0.9336 -0.7226 -0.2122 0.0655  618 MET A N   
2551 C CA  . MET A 322 ? 2.4471 1.3043 1.0379 -0.7326 -0.2089 0.0633  618 MET A CA  
2552 C C   . MET A 322 ? 2.5065 1.4714 1.1591 -0.7717 -0.2123 0.0646  618 MET A C   
2553 O O   . MET A 322 ? 2.4314 1.5313 1.1978 -0.7729 -0.2103 0.0621  618 MET A O   
2554 C CB  . MET A 322 ? 2.4092 1.2915 0.9903 -0.7668 -0.2046 0.0700  618 MET A CB  
2555 C CG  . MET A 322 ? 2.3657 1.2061 0.9499 -0.7185 -0.2001 0.0657  618 MET A CG  
2556 S SD  . MET A 322 ? 2.3946 1.2825 0.9847 -0.7574 -0.1950 0.0723  618 MET A SD  
2557 C CE  . MET A 322 ? 2.2636 1.3506 1.0121 -0.7762 -0.1918 0.0714  618 MET A CE  
2558 N N   . ARG A 323 ? 2.5944 1.5042 1.1734 -0.8012 -0.2177 0.0683  619 ARG A N   
2559 C CA  . ARG A 323 ? 2.5918 1.6065 1.2289 -0.8360 -0.2216 0.0688  619 ARG A CA  
2560 C C   . ARG A 323 ? 2.5054 1.5878 1.2448 -0.7857 -0.2238 0.0574  619 ARG A C   
2561 O O   . ARG A 323 ? 2.4769 1.6896 1.3089 -0.7978 -0.2257 0.0554  619 ARG A O   
2562 C CB  . ARG A 323 ? 2.7897 1.7207 1.3152 -0.8822 -0.2270 0.0757  619 ARG A CB  
2563 C CG  . ARG A 323 ? 2.9203 1.7954 1.3388 -0.9455 -0.2257 0.0879  619 ARG A CG  
2564 C CD  . ARG A 323 ? 3.1025 1.8145 1.3702 -0.9595 -0.2303 0.0931  619 ARG A CD  
2565 N NE  . ARG A 323 ? 3.1686 1.7630 1.3933 -0.8898 -0.2300 0.0869  619 ARG A NE  
2566 C CZ  . ARG A 323 ? 3.3595 1.7964 1.4472 -0.8818 -0.2330 0.0905  619 ARG A CZ  
2567 N NH1 . ARG A 323 ? 3.5138 1.8828 1.4893 -0.9434 -0.2370 0.1006  619 ARG A NH1 
2568 N NH2 . ARG A 323 ? 3.3899 1.7383 1.4489 -0.8114 -0.2319 0.0841  619 ARG A NH2 
2569 N N   . LYS A 324 ? 2.4634 1.4617 1.1835 -0.7281 -0.2238 0.0498  620 LYS A N   
2570 C CA  . LYS A 324 ? 2.3246 1.3677 1.1206 -0.6823 -0.2262 0.0389  620 LYS A CA  
2571 C C   . LYS A 324 ? 2.1495 1.2432 1.0327 -0.6316 -0.2211 0.0314  620 LYS A C   
2572 O O   . LYS A 324 ? 2.2019 1.2327 1.0532 -0.6069 -0.2159 0.0315  620 LYS A O   
2573 C CB  . LYS A 324 ? 2.3963 1.3174 1.1102 -0.6517 -0.2288 0.0349  620 LYS A CB  
2574 C CG  . LYS A 324 ? 2.4844 1.4022 1.1671 -0.6844 -0.2360 0.0363  620 LYS A CG  
2575 C CD  . LYS A 324 ? 2.5811 1.4894 1.1968 -0.7574 -0.2383 0.0484  620 LYS A CD  
2576 C CE  . LYS A 324 ? 2.4583 1.3749 1.0511 -0.7912 -0.2458 0.0491  620 LYS A CE  
2577 N NZ  . LYS A 324 ? 2.4878 1.4136 1.0232 -0.8677 -0.2477 0.0608  620 LYS A NZ  
2578 N N   . THR A 325 ? 1.9134 1.1205 0.9027 -0.6163 -0.2231 0.0251  621 THR A N   
2579 C CA  . THR A 325 ? 1.7794 1.0350 0.8505 -0.5695 -0.2190 0.0179  621 THR A CA  
2580 C C   . THR A 325 ? 1.8307 0.9921 0.8679 -0.5128 -0.2164 0.0096  621 THR A C   
2581 O O   . THR A 325 ? 1.5678 0.7126 0.6217 -0.4774 -0.2105 0.0062  621 THR A O   
2582 C CB  . THR A 325 ? 1.7846 1.1729 0.9616 -0.5654 -0.2232 0.0139  621 THR A CB  
2583 O OG1 . THR A 325 ? 1.6664 1.0794 0.9071 -0.5156 -0.2206 0.0059  621 THR A OG1 
2584 C CG2 . THR A 325 ? 1.9840 1.3745 1.1473 -0.5727 -0.2312 0.0110  621 THR A CG2 
2585 N N   . SER A 326 ? 1.9807 1.0827 0.9685 -0.5027 -0.2202 0.0061  622 SER A N   
2586 C CA  . SER A 326 ? 1.8727 0.8948 0.8259 -0.4473 -0.2173 -0.0023 622 SER A CA  
2587 C C   . SER A 326 ? 1.8930 0.7872 0.7411 -0.4289 -0.2130 0.0009  622 SER A C   
2588 O O   . SER A 326 ? 1.8185 0.6449 0.6284 -0.3788 -0.2098 -0.0055 622 SER A O   
2589 C CB  . SER A 326 ? 1.7932 0.8055 0.7302 -0.4466 -0.2231 -0.0063 622 SER A CB  
2590 O OG  . SER A 326 ? 1.8508 0.8593 0.7450 -0.5021 -0.2293 0.0018  622 SER A OG  
2591 N N   . SER A 327 ? 1.9603 0.8208 0.7558 -0.4656 -0.2128 0.0107  623 SER A N   
2592 C CA  . SER A 327 ? 2.0148 0.7541 0.7088 -0.4408 -0.2094 0.0135  623 SER A CA  
2593 C C   . SER A 327 ? 2.0347 0.7833 0.7657 -0.3955 -0.2026 0.0087  623 SER A C   
2594 O O   . SER A 327 ? 2.0854 0.7422 0.7358 -0.3711 -0.2000 0.0109  623 SER A O   
2595 C CB  . SER A 327 ? 2.2794 0.9647 0.8861 -0.4974 -0.2122 0.0259  623 SER A CB  
2596 O OG  . SER A 327 ? 2.2753 1.0383 0.9368 -0.5308 -0.2100 0.0304  623 SER A OG  
2597 N N   . LEU A 328 ? 1.8990 0.7534 0.7442 -0.3830 -0.2001 0.0024  624 LEU A N   
2598 C CA  . LEU A 328 ? 1.8316 0.7148 0.7277 -0.3498 -0.1939 -0.0015 624 LEU A CA  
2599 C C   . LEU A 328 ? 2.0678 0.8996 0.9059 -0.3646 -0.1919 0.0063  624 LEU A C   
2600 O O   . LEU A 328 ? 2.2406 1.0306 1.0592 -0.3218 -0.1871 0.0032  624 LEU A O   
2601 C CB  . LEU A 328 ? 1.7338 0.5811 0.6273 -0.2801 -0.1886 -0.0118 624 LEU A CB  
2602 C CG  . LEU A 328 ? 1.7196 0.6044 0.6522 -0.2687 -0.1906 -0.0192 624 LEU A CG  
2603 C CD1 . LEU A 328 ? 1.6814 0.5428 0.6139 -0.2008 -0.1837 -0.0298 624 LEU A CD1 
2604 C CD2 . LEU A 328 ? 1.5448 0.5501 0.5859 -0.2975 -0.1936 -0.0202 624 LEU A CD2 
2605 N N   . TRP A 329 ? 2.1033 0.9416 0.9121 -0.4249 -0.1954 0.0161  625 TRP A N   
2606 C CA  . TRP A 329 ? 2.1210 0.9180 0.8764 -0.4447 -0.1935 0.0235  625 TRP A CA  
2607 C C   . TRP A 329 ? 2.1257 1.0063 0.9727 -0.4363 -0.1885 0.0215  625 TRP A C   
2608 O O   . TRP A 329 ? 2.1869 1.0231 0.9982 -0.4233 -0.1853 0.0232  625 TRP A O   
2609 C CB  . TRP A 329 ? 2.1339 0.9263 0.8364 -0.5153 -0.1975 0.0344  625 TRP A CB  
2610 C CG  . TRP A 329 ? 2.0285 0.9549 0.8282 -0.5590 -0.1986 0.0366  625 TRP A CG  
2611 C CD1 . TRP A 329 ? 2.1569 1.1378 0.9906 -0.5791 -0.2031 0.0358  625 TRP A CD1 
2612 C CD2 . TRP A 329 ? 2.0072 1.0332 0.8797 -0.5845 -0.1951 0.0400  625 TRP A CD2 
2613 N NE1 . TRP A 329 ? 2.0818 1.1928 1.0044 -0.6126 -0.2028 0.0383  625 TRP A NE1 
2614 C CE2 . TRP A 329 ? 1.9625 1.1042 0.9107 -0.6160 -0.1975 0.0411  625 TRP A CE2 
2615 C CE3 . TRP A 329 ? 1.8123 0.8424 0.6921 -0.5815 -0.1901 0.0421  625 TRP A CE3 
2616 C CZ2 . TRP A 329 ? 1.8730 1.1359 0.9023 -0.6410 -0.1946 0.0443  625 TRP A CZ2 
2617 C CZ3 . TRP A 329 ? 1.7705 0.9177 0.7314 -0.6101 -0.1870 0.0455  625 TRP A CZ3 
2618 C CH2 . TRP A 329 ? 1.7946 1.0579 0.8287 -0.6379 -0.1890 0.0466  625 TRP A CH2 
2619 N N   . LYS A 330 ? 1.9573 0.9562 0.9178 -0.4423 -0.1882 0.0181  626 LYS A N   
2620 C CA  . LYS A 330 ? 1.7916 0.8687 0.8392 -0.4308 -0.1836 0.0162  626 LYS A CA  
2621 C C   . LYS A 330 ? 1.6607 0.6970 0.7142 -0.3679 -0.1790 0.0078  626 LYS A C   
2622 O O   . LYS A 330 ? 1.7383 0.7732 0.8022 -0.3545 -0.1748 0.0084  626 LYS A O   
2623 C CB  . LYS A 330 ? 1.6623 0.8698 0.8209 -0.4452 -0.1852 0.0142  626 LYS A CB  
2624 C CG  . LYS A 330 ? 1.5203 0.8035 0.6967 -0.5034 -0.1872 0.0230  626 LYS A CG  
2625 C CD  . LYS A 330 ? 1.4772 0.8943 0.7649 -0.5043 -0.1888 0.0205  626 LYS A CD  
2626 C CE  . LYS A 330 ? 1.5236 1.0325 0.8351 -0.5551 -0.1894 0.0288  626 LYS A CE  
2627 N NZ  . LYS A 330 ? 1.4337 1.0737 0.8472 -0.5481 -0.1916 0.0264  626 LYS A NZ  
2628 N N   . ASP A 331 ? 1.6115 0.6193 0.6592 -0.3281 -0.1794 -0.0002 627 ASP A N   
2629 C CA  . ASP A 331 ? 1.6121 0.5893 0.6640 -0.2651 -0.1740 -0.0087 627 ASP A CA  
2630 C C   . ASP A 331 ? 1.6735 0.5490 0.6287 -0.2404 -0.1718 -0.0060 627 ASP A C   
2631 O O   . ASP A 331 ? 1.7987 0.6714 0.7664 -0.2076 -0.1671 -0.0082 627 ASP A O   
2632 C CB  . ASP A 331 ? 1.6657 0.6327 0.7194 -0.2297 -0.1741 -0.0174 627 ASP A CB  
2633 C CG  . ASP A 331 ? 1.5810 0.6411 0.7187 -0.2536 -0.1779 -0.0200 627 ASP A CG  
2634 O OD1 . ASP A 331 ? 1.5429 0.6234 0.6734 -0.3002 -0.1839 -0.0140 627 ASP A OD1 
2635 O OD2 . ASP A 331 ? 1.4382 0.5521 0.6456 -0.2260 -0.1752 -0.0277 627 ASP A OD2 
2636 N N   . GLN A 332 ? 1.7943 0.5833 0.6472 -0.2549 -0.1758 -0.0009 628 GLN A N   
2637 C CA  . GLN A 332 ? 2.0256 0.7081 0.7715 -0.2264 -0.1751 0.0014  628 GLN A CA  
2638 C C   . GLN A 332 ? 1.9935 0.6738 0.7292 -0.2500 -0.1740 0.0074  628 GLN A C   
2639 O O   . GLN A 332 ? 1.9783 0.6065 0.6691 -0.2104 -0.1715 0.0060  628 GLN A O   
2640 C CB  . GLN A 332 ? 2.1720 0.7600 0.8046 -0.2451 -0.1806 0.0068  628 GLN A CB  
2641 C CG  . GLN A 332 ? 2.2016 0.6840 0.7315 -0.1870 -0.1799 0.0045  628 GLN A CG  
2642 C CD  . GLN A 332 ? 2.4604 0.8558 0.8883 -0.2013 -0.1854 0.0090  628 GLN A CD  
2643 O OE1 . GLN A 332 ? 2.7492 1.1369 1.1508 -0.2646 -0.1905 0.0167  628 GLN A OE1 
2644 N NE2 . GLN A 332 ? 2.4319 0.7666 0.8024 -0.1420 -0.1842 0.0048  628 GLN A NE2 
2645 N N   . ALA A 333 ? 1.9247 0.6673 0.7023 -0.3121 -0.1758 0.0140  629 ALA A N   
2646 C CA  . ALA A 333 ? 2.0101 0.7580 0.7813 -0.3369 -0.1740 0.0198  629 ALA A CA  
2647 C C   . ALA A 333 ? 1.8735 0.7031 0.7488 -0.3118 -0.1686 0.0153  629 ALA A C   
2648 O O   . ALA A 333 ? 1.8138 0.6299 0.6760 -0.3102 -0.1661 0.0180  629 ALA A O   
2649 C CB  . ALA A 333 ? 1.8437 0.6315 0.6128 -0.4121 -0.1768 0.0291  629 ALA A CB  
2650 N N   . LEU A 334 ? 1.7389 0.6462 0.7099 -0.2917 -0.1670 0.0085  630 LEU A N   
2651 C CA  . LEU A 334 ? 1.5802 0.5548 0.6412 -0.2642 -0.1621 0.0039  630 LEU A CA  
2652 C C   . LEU A 334 ? 1.6932 0.6065 0.7170 -0.1990 -0.1582 -0.0016 630 LEU A C   
2653 O O   . LEU A 334 ? 1.6630 0.5977 0.7198 -0.1820 -0.1544 -0.0018 630 LEU A O   
2654 C CB  . LEU A 334 ? 1.4764 0.5404 0.6350 -0.2605 -0.1624 -0.0023 630 LEU A CB  
2655 C CG  . LEU A 334 ? 1.4304 0.5653 0.6813 -0.2361 -0.1584 -0.0073 630 LEU A CG  
2656 C CD1 . LEU A 334 ? 1.3036 0.5210 0.6171 -0.2790 -0.1581 -0.0006 630 LEU A CD1 
2657 C CD2 . LEU A 334 ? 1.3588 0.5649 0.6830 -0.2072 -0.1552 -0.0127 630 LEU A CD2 
2658 N N   . VAL A 335 ? 1.6241 0.4676 0.5805 -0.1591 -0.1587 -0.0060 631 VAL A N   
2659 C CA  . VAL A 335 ? 1.7481 0.5482 0.6698 -0.0899 -0.1545 -0.0114 631 VAL A CA  
2660 C C   . VAL A 335 ? 1.8514 0.5795 0.6895 -0.0883 -0.1555 -0.0058 631 VAL A C   
2661 O O   . VAL A 335 ? 1.8302 0.5698 0.6863 -0.0557 -0.1518 -0.0072 631 VAL A O   
2662 C CB  . VAL A 335 ? 1.8522 0.6062 0.7222 -0.0452 -0.1542 -0.0173 631 VAL A CB  
2663 C CG1 . VAL A 335 ? 1.8987 0.6047 0.7106 0.0250  -0.1506 -0.0208 631 VAL A CG1 
2664 C CG2 . VAL A 335 ? 1.7149 0.5456 0.6739 -0.0332 -0.1514 -0.0252 631 VAL A CG2 
2665 N N   . GLU A 336 ? 1.8369 0.4887 0.5786 -0.1245 -0.1607 0.0005  632 GLU A N   
2666 C CA  . GLU A 336 ? 1.9699 0.5471 0.6224 -0.1311 -0.1623 0.0054  632 GLU A CA  
2667 C C   . GLU A 336 ? 1.9764 0.6127 0.6943 -0.1545 -0.1593 0.0087  632 GLU A C   
2668 O O   . GLU A 336 ? 1.9885 0.5897 0.6709 -0.1264 -0.1578 0.0083  632 GLU A O   
2669 C CB  . GLU A 336 ? 2.1179 0.6209 0.6702 -0.1861 -0.1684 0.0127  632 GLU A CB  
2670 C CG  . GLU A 336 ? 2.3095 0.7411 0.7821 -0.1694 -0.1721 0.0114  632 GLU A CG  
2671 C CD  . GLU A 336 ? 2.4856 0.8323 0.8687 -0.0966 -0.1717 0.0062  632 GLU A CD  
2672 O OE1 . GLU A 336 ? 2.3701 0.6962 0.7302 -0.0660 -0.1697 0.0043  632 GLU A OE1 
2673 O OE2 . GLU A 336 ? 2.5671 0.8711 0.9021 -0.0680 -0.1732 0.0041  632 GLU A OE2 
2674 N N   . ILE A 337 ? 1.9035 0.6313 0.7141 -0.2047 -0.1586 0.0120  633 ILE A N   
2675 C CA  . ILE A 337 ? 1.8782 0.6689 0.7531 -0.2290 -0.1555 0.0160  633 ILE A CA  
2676 C C   . ILE A 337 ? 1.8778 0.6985 0.8098 -0.1712 -0.1507 0.0105  633 ILE A C   
2677 O O   . ILE A 337 ? 1.8241 0.6386 0.7516 -0.1645 -0.1486 0.0132  633 ILE A O   
2678 C CB  . ILE A 337 ? 1.6599 0.5562 0.6273 -0.2857 -0.1554 0.0196  633 ILE A CB  
2679 C CG1 . ILE A 337 ? 1.7980 0.6763 0.7063 -0.3506 -0.1589 0.0280  633 ILE A CG1 
2680 C CG2 . ILE A 337 ? 1.6267 0.6101 0.6888 -0.2910 -0.1509 0.0208  633 ILE A CG2 
2681 C CD1 . ILE A 337 ? 1.6616 0.6335 0.6393 -0.3952 -0.1604 0.0301  633 ILE A CD1 
2682 N N   . ASN A 338 ? 1.8159 0.6694 0.7984 -0.1284 -0.1489 0.0029  634 ASN A N   
2683 C CA  . ASN A 338 ? 1.6796 0.5694 0.7167 -0.0739 -0.1443 -0.0021 634 ASN A CA  
2684 C C   . ASN A 338 ? 1.7486 0.5692 0.7062 -0.0105 -0.1433 -0.0047 634 ASN A C   
2685 O O   . ASN A 338 ? 1.6412 0.4831 0.6232 0.0242  -0.1404 -0.0050 634 ASN A O   
2686 C CB  . ASN A 338 ? 1.6159 0.5847 0.7407 -0.0524 -0.1414 -0.0093 634 ASN A CB  
2687 C CG  . ASN A 338 ? 1.4530 0.5388 0.6867 -0.1009 -0.1393 -0.0057 634 ASN A CG  
2688 O OD1 . ASN A 338 ? 1.3937 0.5779 0.7188 -0.0911 -0.1329 -0.0046 634 ASN A OD1 
2689 N ND2 . ASN A 338 ? 1.4438 0.5166 0.6615 -0.1530 -0.1454 -0.0040 634 ASN A ND2 
2690 N N   . ILE A 339 ? 1.8741 0.6152 0.7345 0.0065  -0.1460 -0.0065 635 ILE A N   
2691 C CA  . ILE A 339 ? 1.8714 0.5451 0.6439 0.0625  -0.1460 -0.0090 635 ILE A CA  
2692 C C   . ILE A 339 ? 1.9418 0.5769 0.6715 0.0391  -0.1474 -0.0034 635 ILE A C   
2693 O O   . ILE A 339 ? 1.9625 0.5888 0.6740 0.0857  -0.1457 -0.0056 635 ILE A O   
2694 C CB  . ILE A 339 ? 1.9751 0.5600 0.6373 0.0772  -0.1497 -0.0110 635 ILE A CB  
2695 C CG1 . ILE A 339 ? 1.8895 0.5144 0.5913 0.1121  -0.1471 -0.0173 635 ILE A CG1 
2696 C CG2 . ILE A 339 ? 2.0259 0.5318 0.5810 0.1293  -0.1507 -0.0136 635 ILE A CG2 
2697 C CD1 . ILE A 339 ? 2.0583 0.5985 0.6496 0.1435  -0.1499 -0.0192 635 ILE A CD1 
2698 N N   . ALA A 340 ? 1.9180 0.5389 0.6344 -0.0339 -0.1503 0.0038  636 ALA A N   
2699 C CA  . ALA A 340 ? 2.0951 0.6765 0.7628 -0.0644 -0.1514 0.0092  636 ALA A CA  
2700 C C   . ALA A 340 ? 1.8915 0.5495 0.6517 -0.0621 -0.1470 0.0119  636 ALA A C   
2701 O O   . ALA A 340 ? 1.9196 0.5458 0.6426 -0.0425 -0.1464 0.0126  636 ALA A O   
2702 C CB  . ALA A 340 ? 2.0389 0.6000 0.6705 -0.1445 -0.1550 0.0162  636 ALA A CB  
2703 N N   . VAL A 341 ? 1.8440 0.5997 0.7201 -0.0811 -0.1443 0.0131  637 VAL A N   
2704 C CA  . VAL A 341 ? 1.7099 0.5355 0.6706 -0.0770 -0.1405 0.0161  637 VAL A CA  
2705 C C   . VAL A 341 ? 1.8670 0.6881 0.8249 0.0013  -0.1388 0.0116  637 VAL A C   
2706 O O   . VAL A 341 ? 1.8561 0.6644 0.7961 0.0165  -0.1381 0.0149  637 VAL A O   
2707 C CB  . VAL A 341 ? 1.6656 0.5942 0.7442 -0.1040 -0.1385 0.0154  637 VAL A CB  
2708 C CG1 . VAL A 341 ? 1.7005 0.7407 0.8792 -0.0940 -0.1315 0.0172  637 VAL A CG1 
2709 C CG2 . VAL A 341 ? 1.6969 0.6496 0.7835 -0.1780 -0.1404 0.0199  637 VAL A CG2 
2710 N N   . LEU A 342 ? 1.7622 0.6014 0.7368 0.0530  -0.1379 0.0040  638 LEU A N   
2711 C CA  . LEU A 342 ? 1.7468 0.6034 0.7210 0.1314  -0.1360 -0.0013 638 LEU A CA  
2712 C C   . LEU A 342 ? 1.9341 0.7115 0.8037 0.1582  -0.1378 -0.0019 638 LEU A C   
2713 O O   . LEU A 342 ? 1.8684 0.6642 0.7469 0.1858  -0.1369 -0.0004 638 LEU A O   
2714 C CB  . LEU A 342 ? 1.7130 0.5912 0.6957 0.1761  -0.1343 -0.0100 638 LEU A CB  
2715 C CG  . LEU A 342 ? 1.5127 0.5157 0.6230 0.1580  -0.1289 -0.0129 638 LEU A CG  
2716 C CD1 . LEU A 342 ? 1.4950 0.5196 0.6092 0.2041  -0.1263 -0.0213 638 LEU A CD1 
2717 C CD2 . LEU A 342 ? 1.3509 0.4739 0.5641 0.1652  -0.1232 -0.0122 638 LEU A CD2 
2718 N N   . TYR A 343 ? 2.1218 0.8078 0.8862 0.1513  -0.1408 -0.0047 639 TYR A N   
2719 C CA  . TYR A 343 ? 2.2687 0.8671 0.9189 0.1813  -0.1429 -0.0079 639 TYR A CA  
2720 C C   . TYR A 343 ? 2.1758 0.7544 0.8138 0.1497  -0.1434 -0.0020 639 TYR A C   
2721 O O   . TYR A 343 ? 2.2073 0.7678 0.8092 0.1932  -0.1430 -0.0051 639 TYR A O   
2722 C CB  . TYR A 343 ? 2.4400 0.9331 0.9721 0.1629  -0.1473 -0.0099 639 TYR A CB  
2723 C CG  . TYR A 343 ? 2.4738 0.8566 0.8704 0.1814  -0.1505 -0.0134 639 TYR A CG  
2724 C CD1 . TYR A 343 ? 2.3441 0.7029 0.6822 0.2603  -0.1497 -0.0221 639 TYR A CD1 
2725 C CD2 . TYR A 343 ? 2.5668 0.8723 0.8899 0.1199  -0.1541 -0.0088 639 TYR A CD2 
2726 C CE1 . TYR A 343 ? 2.5098 0.7737 0.7402 0.2780  -0.1510 -0.0242 639 TYR A CE1 
2727 C CE2 . TYR A 343 ? 2.7059 0.9089 0.9105 0.1356  -0.1560 -0.0120 639 TYR A CE2 
2728 C CZ  . TYR A 343 ? 2.7213 0.9040 0.8874 0.2155  -0.1540 -0.0189 639 TYR A CZ  
2729 O OH  . TYR A 343 ? 2.8720 0.9577 0.9337 0.2326  -0.1549 -0.0204 639 TYR A OH  
2730 N N   . SER A 344 ? 2.1600 0.7473 0.8271 0.0739  -0.1439 0.0063  640 SER A N   
2731 C CA  . SER A 344 ? 2.0801 0.6500 0.7316 0.0380  -0.1437 0.0126  640 SER A CA  
2732 C C   . SER A 344 ? 1.9404 0.5851 0.6736 0.0735  -0.1405 0.0154  640 SER A C   
2733 O O   . SER A 344 ? 1.9421 0.5554 0.6328 0.0956  -0.1406 0.0153  640 SER A O   
2734 C CB  . SER A 344 ? 2.0066 0.5984 0.6871 -0.0496 -0.1437 0.0209  640 SER A CB  
2735 O OG  . SER A 344 ? 2.2390 0.7763 0.8527 -0.0816 -0.1475 0.0191  640 SER A OG  
2736 N N   . PHE A 345 ? 1.7760 0.5184 0.6227 0.0800  -0.1381 0.0178  641 PHE A N   
2737 C CA  . PHE A 345 ? 1.6870 0.5062 0.6116 0.1134  -0.1364 0.0217  641 PHE A CA  
2738 C C   . PHE A 345 ? 1.8288 0.6480 0.7210 0.1951  -0.1370 0.0138  641 PHE A C   
2739 O O   . PHE A 345 ? 1.8715 0.7030 0.7623 0.2179  -0.1373 0.0162  641 PHE A O   
2740 C CB  . PHE A 345 ? 1.5196 0.4786 0.5826 0.1054  -0.1311 0.0174  641 PHE A CB  
2741 C CG  . PHE A 345 ? 1.5283 0.5635 0.6744 0.0355  -0.1266 0.0219  641 PHE A CG  
2742 C CD1 . PHE A 345 ? 1.6211 0.6110 0.7353 -0.0287 -0.1284 0.0267  641 PHE A CD1 
2743 C CD2 . PHE A 345 ? 1.4465 0.6057 0.7031 0.0364  -0.1206 0.0204  641 PHE A CD2 
2744 C CE1 . PHE A 345 ? 1.5489 0.6225 0.7411 -0.0866 -0.1242 0.0304  641 PHE A CE1 
2745 C CE2 . PHE A 345 ? 1.2244 0.4559 0.5543 -0.0190 -0.1162 0.0238  641 PHE A CE2 
2746 C CZ  . PHE A 345 ? 1.3024 0.4952 0.6013 -0.0786 -0.1178 0.0290  641 PHE A CZ  
2747 N N   . GLN A 346 ? 1.8602 0.6737 0.7271 0.2401  -0.1368 0.0038  642 GLN A N   
2748 C CA  . GLN A 346 ? 1.8233 0.6572 0.6658 0.3188  -0.1361 -0.0055 642 GLN A CA  
2749 C C   . GLN A 346 ? 1.9584 0.6976 0.6881 0.3339  -0.1377 -0.0088 642 GLN A C   
2750 O O   . GLN A 346 ? 1.9651 0.7335 0.6912 0.3852  -0.1371 -0.0129 642 GLN A O   
2751 C CB  . GLN A 346 ? 1.9711 0.8150 0.7998 0.3576  -0.1345 -0.0149 642 GLN A CB  
2752 C CG  . GLN A 346 ? 1.8549 0.8019 0.7960 0.3564  -0.1321 -0.0145 642 GLN A CG  
2753 C CD  . GLN A 346 ? 2.0659 1.0037 0.9825 0.3775  -0.1304 -0.0221 642 GLN A CD  
2754 O OE1 . GLN A 346 ? 2.2561 1.1203 1.1244 0.3374  -0.1323 -0.0207 642 GLN A OE1 
2755 N NE2 . GLN A 346 ? 2.0880 1.1077 1.0375 0.4384  -0.1268 -0.0299 642 GLN A NE2 
2756 N N   . SER A 347 ? 2.0377 0.6653 0.6714 0.2897  -0.1400 -0.0082 643 SER A N   
2757 C CA  . SER A 347 ? 2.1925 0.7164 0.7055 0.3024  -0.1419 -0.0129 643 SER A CA  
2758 C C   . SER A 347 ? 2.2237 0.7498 0.7512 0.2788  -0.1417 -0.0059 643 SER A C   
2759 O O   . SER A 347 ? 2.4072 0.8633 0.8477 0.3024  -0.1426 -0.0110 643 SER A O   
2760 C CB  . SER A 347 ? 2.3031 0.7088 0.7047 0.2569  -0.1454 -0.0142 643 SER A CB  
2761 O OG  . SER A 347 ? 2.5541 0.9360 0.9111 0.2915  -0.1463 -0.0214 643 SER A OG  
2762 N N   . ASP A 348 ? 2.1898 0.7914 0.8192 0.2343  -0.1403 0.0055  644 ASP A N   
2763 C CA  . ASP A 348 ? 2.2116 0.8324 0.8667 0.2160  -0.1396 0.0139  644 ASP A CA  
2764 C C   . ASP A 348 ? 2.0940 0.8271 0.8440 0.2671  -0.1390 0.0158  644 ASP A C   
2765 O O   . ASP A 348 ? 2.0575 0.8214 0.8400 0.2545  -0.1390 0.0242  644 ASP A O   
2766 C CB  . ASP A 348 ? 2.1454 0.7789 0.8419 0.1301  -0.1381 0.0263  644 ASP A CB  
2767 C CG  . ASP A 348 ? 2.2200 0.7568 0.8233 0.0702  -0.1395 0.0246  644 ASP A CG  
2768 O OD1 . ASP A 348 ? 2.2914 0.7291 0.7805 0.0921  -0.1422 0.0153  644 ASP A OD1 
2769 O OD2 . ASP A 348 ? 2.1192 0.6839 0.7615 0.0003  -0.1380 0.0323  644 ASP A OD2 
2770 N N   . LYS A 349 ? 2.1747 0.9761 0.9690 0.3219  -0.1387 0.0081  645 LYS A N   
2771 C CA  . LYS A 349 ? 2.1746 1.1010 1.0641 0.3677  -0.1390 0.0078  645 LYS A CA  
2772 C C   . LYS A 349 ? 1.9795 0.9893 0.9755 0.3243  -0.1397 0.0196  645 LYS A C   
2773 O O   . LYS A 349 ? 1.8497 0.9695 0.9277 0.3379  -0.1376 0.0166  645 LYS A O   
2774 C CB  . LYS A 349 ? 2.2859 1.2159 1.1432 0.4120  -0.1398 0.0040  645 LYS A CB  
2775 C CG  . LYS A 349 ? 2.3789 1.3902 1.2557 0.4887  -0.1386 -0.0088 645 LYS A CG  
2776 C CD  . LYS A 349 ? 2.5281 1.4841 1.3304 0.5206  -0.1362 -0.0203 645 LYS A CD  
2777 C CE  . LYS A 349 ? 2.6207 1.6287 1.4015 0.5982  -0.1341 -0.0333 645 LYS A CE  
2778 N NZ  . LYS A 349 ? 2.5330 1.7060 1.4334 0.6229  -0.1328 -0.0349 645 LYS A NZ  
2779 N N   . VAL A 350 ? 1.7901 0.7895 0.8113 0.2578  -0.1358 0.0221  646 VAL A N   
2780 C CA  . VAL A 350 ? 1.4871 0.6092 0.6375 0.2064  -0.1285 0.0206  646 VAL A CA  
2781 C C   . VAL A 350 ? 1.5070 0.7222 0.7396 0.2238  -0.1251 0.0111  646 VAL A C   
2782 O O   . VAL A 350 ? 1.5717 0.7371 0.7630 0.2340  -0.1268 0.0085  646 VAL A O   
2783 C CB  . VAL A 350 ? 1.4444 0.5223 0.5826 0.1287  -0.1262 0.0281  646 VAL A CB  
2784 C CG1 . VAL A 350 ? 1.2956 0.5031 0.5635 0.0854  -0.1188 0.0263  646 VAL A CG1 
2785 C CG2 . VAL A 350 ? 1.4862 0.4578 0.5258 0.1060  -0.1291 0.0383  646 VAL A CG2 
2786 N N   . THR A 351 ? 1.3941 0.7391 0.7372 0.2245  -0.1202 0.0059  647 THR A N   
2787 C CA  . THR A 351 ? 1.2962 0.7338 0.7124 0.2451  -0.1168 -0.0031 647 THR A CA  
2788 C C   . THR A 351 ? 1.2409 0.6787 0.6878 0.2005  -0.1134 -0.0032 647 THR A C   
2789 O O   . THR A 351 ? 1.1983 0.6565 0.6883 0.1469  -0.1102 0.0007  647 THR A O   
2790 C CB  . THR A 351 ? 1.2524 0.8189 0.7698 0.2468  -0.1126 -0.0081 647 THR A CB  
2791 O OG1 . THR A 351 ? 1.3555 0.9264 0.8435 0.2878  -0.1170 -0.0082 647 THR A OG1 
2792 C CG2 . THR A 351 ? 1.0802 0.7397 0.6646 0.2641  -0.1087 -0.0171 647 THR A CG2 
2793 N N   . ILE A 352 ? 1.2681 0.6870 0.6911 0.2261  -0.1141 -0.0078 648 ILE A N   
2794 C CA  . ILE A 352 ? 1.1287 0.5549 0.5814 0.1915  -0.1114 -0.0090 648 ILE A CA  
2795 C C   . ILE A 352 ? 1.2182 0.6871 0.6867 0.2350  -0.1094 -0.0172 648 ILE A C   
2796 O O   . ILE A 352 ? 1.2607 0.7146 0.6817 0.2922  -0.1118 -0.0208 648 ILE A O   
2797 C CB  . ILE A 352 ? 1.2925 0.5966 0.6560 0.1580  -0.1162 -0.0027 648 ILE A CB  
2798 C CG1 . ILE A 352 ? 1.1908 0.5198 0.5993 0.1103  -0.1141 -0.0028 648 ILE A CG1 
2799 C CG2 . ILE A 352 ? 1.3530 0.5528 0.6065 0.2049  -0.1216 -0.0046 648 ILE A CG2 
2800 C CD1 . ILE A 352 ? 1.2465 0.4893 0.5929 0.0553  -0.1183 0.0047  648 ILE A CD1 
2801 N N   . VAL A 353 ? 1.1675 0.6954 0.7025 0.2098  -0.1047 -0.0202 649 VAL A N   
2802 C CA  . VAL A 353 ? 1.0959 0.6668 0.6480 0.2419  -0.1014 -0.0274 649 VAL A CA  
2803 C C   . VAL A 353 ? 1.2360 0.7510 0.7623 0.2153  -0.1024 -0.0264 649 VAL A C   
2804 O O   . VAL A 353 ? 1.1152 0.6222 0.6651 0.1630  -0.1028 -0.0218 649 VAL A O   
2805 C CB  . VAL A 353 ? 1.0426 0.7444 0.6990 0.2367  -0.0943 -0.0323 649 VAL A CB  
2806 C CG1 . VAL A 353 ? 0.9479 0.6823 0.6702 0.1801  -0.0909 -0.0296 649 VAL A CG1 
2807 C CG2 . VAL A 353 ? 1.0135 0.7715 0.6825 0.2751  -0.0902 -0.0399 649 VAL A CG2 
2808 N N   . ASP A 354 ? 1.3199 0.7944 0.7910 0.2532  -0.1033 -0.0309 650 ASP A N   
2809 C CA  . ASP A 354 ? 1.2509 0.6766 0.6957 0.2329  -0.1043 -0.0313 650 ASP A CA  
2810 C C   . ASP A 354 ? 1.2217 0.7500 0.7591 0.2186  -0.0971 -0.0350 650 ASP A C   
2811 O O   . ASP A 354 ? 1.2570 0.8831 0.8602 0.2351  -0.0912 -0.0387 650 ASP A O   
2812 C CB  . ASP A 354 ? 1.3710 0.7087 0.7141 0.2828  -0.1077 -0.0353 650 ASP A CB  
2813 C CG  . ASP A 354 ? 1.3659 0.7829 0.7347 0.3412  -0.1017 -0.0434 650 ASP A CG  
2814 O OD1 . ASP A 354 ? 1.4036 0.8199 0.7329 0.3980  -0.1027 -0.0462 650 ASP A OD1 
2815 O OD2 . ASP A 354 ? 1.2079 0.6922 0.6346 0.3310  -0.0959 -0.0469 650 ASP A OD2 
2816 N N   . HIS A 355 ? 1.1230 0.6268 0.6610 0.1851  -0.0981 -0.0339 651 HIS A N   
2817 C CA  . HIS A 355 ? 0.9998 0.5918 0.6213 0.1661  -0.0917 -0.0359 651 HIS A CA  
2818 C C   . HIS A 355 ? 1.1590 0.8022 0.7917 0.2080  -0.0853 -0.0431 651 HIS A C   
2819 O O   . HIS A 355 ? 1.1609 0.8888 0.8644 0.1965  -0.0785 -0.0449 651 HIS A O   
2820 C CB  . HIS A 355 ? 1.0727 0.6304 0.6914 0.1213  -0.0953 -0.0325 651 HIS A CB  
2821 C CG  . HIS A 355 ? 1.0615 0.5176 0.5886 0.1280  -0.1014 -0.0335 651 HIS A CG  
2822 N ND1 . HIS A 355 ? 1.1306 0.4848 0.5705 0.1243  -0.1088 -0.0305 651 HIS A ND1 
2823 C CD2 . HIS A 355 ? 1.1445 0.5779 0.6464 0.1355  -0.1013 -0.0372 651 HIS A CD2 
2824 C CE1 . HIS A 355 ? 1.3490 0.6175 0.7103 0.1286  -0.1134 -0.0328 651 HIS A CE1 
2825 N NE2 . HIS A 355 ? 1.1846 0.5015 0.5835 0.1375  -0.1090 -0.0371 651 HIS A NE2 
2826 N N   . HIS A 356 ? 1.1205 0.7140 0.6801 0.2568  -0.0869 -0.0470 652 HIS A N   
2827 C CA  . HIS A 356 ? 1.0857 0.7425 0.6555 0.3028  -0.0799 -0.0542 652 HIS A CA  
2828 C C   . HIS A 356 ? 1.1163 0.8732 0.7373 0.3269  -0.0753 -0.0569 652 HIS A C   
2829 O O   . HIS A 356 ? 1.0069 0.8674 0.6930 0.3258  -0.0672 -0.0606 652 HIS A O   
2830 C CB  . HIS A 356 ? 1.2215 0.7904 0.6891 0.3529  -0.0834 -0.0580 652 HIS A CB  
2831 C CG  . HIS A 356 ? 1.3500 0.8138 0.7577 0.3258  -0.0891 -0.0561 652 HIS A CG  
2832 N ND1 . HIS A 356 ? 1.3171 0.8005 0.7501 0.3052  -0.0857 -0.0577 652 HIS A ND1 
2833 C CD2 . HIS A 356 ? 1.4050 0.7433 0.7258 0.3110  -0.0983 -0.0524 652 HIS A CD2 
2834 C CE1 . HIS A 356 ? 1.3990 0.7779 0.7660 0.2806  -0.0933 -0.0557 652 HIS A CE1 
2835 N NE2 . HIS A 356 ? 1.5197 0.8094 0.8175 0.2806  -0.1009 -0.0524 652 HIS A NE2 
2836 N N   . SER A 357 ? 1.0272 0.7547 0.6163 0.3458  -0.0805 -0.0550 653 SER A N   
2837 C CA  . SER A 357 ? 1.1365 0.9615 0.7708 0.3694  -0.0775 -0.0580 653 SER A CA  
2838 C C   . SER A 357 ? 0.8669 0.7754 0.5957 0.3182  -0.0730 -0.0562 653 SER A C   
2839 O O   . SER A 357 ? 0.8767 0.8915 0.6618 0.3226  -0.0669 -0.0607 653 SER A O   
2840 C CB  . SER A 357 ? 1.1230 0.8922 0.6985 0.4003  -0.0849 -0.0556 653 SER A CB  
2841 O OG  . SER A 357 ? 1.1955 1.0662 0.8084 0.4321  -0.0827 -0.0597 653 SER A OG  
2842 N N   . ALA A 358 ? 0.9272 0.7892 0.6695 0.2687  -0.0759 -0.0501 654 ALA A N   
2843 C CA  . ALA A 358 ? 0.8938 0.8215 0.7144 0.2248  -0.0720 -0.0485 654 ALA A CA  
2844 C C   . ALA A 358 ? 0.8695 0.8619 0.7407 0.2072  -0.0643 -0.0516 654 ALA A C   
2845 O O   . ALA A 358 ? 0.6706 0.7458 0.5969 0.1945  -0.0588 -0.0543 654 ALA A O   
2846 C CB  . ALA A 358 ? 0.8435 0.7103 0.6618 0.1817  -0.0766 -0.0415 654 ALA A CB  
2847 N N   . THR A 359 ? 0.7827 0.7348 0.6303 0.2041  -0.0638 -0.0513 655 THR A N   
2848 C CA  . THR A 359 ? 0.7293 0.7354 0.6199 0.1851  -0.0564 -0.0532 655 THR A CA  
2849 C C   . THR A 359 ? 0.6801 0.7700 0.5842 0.2154  -0.0489 -0.0598 655 THR A C   
2850 O O   . THR A 359 ? 0.7458 0.9056 0.6969 0.1931  -0.0414 -0.0615 655 THR A O   
2851 C CB  . THR A 359 ? 0.7709 0.7139 0.6316 0.1738  -0.0585 -0.0510 655 THR A CB  
2852 O OG1 . THR A 359 ? 0.8920 0.7735 0.6817 0.2120  -0.0622 -0.0533 655 THR A OG1 
2853 C CG2 . THR A 359 ? 0.7907 0.6830 0.6560 0.1341  -0.0647 -0.0445 655 THR A CG2 
2854 N N   . GLU A 360 ? 0.7854 0.8706 0.6446 0.2661  -0.0507 -0.0636 656 GLU A N   
2855 C CA  . GLU A 360 ? 0.8568 1.0421 0.7332 0.2981  -0.0438 -0.0702 656 GLU A CA  
2856 C C   . GLU A 360 ? 0.8156 1.0894 0.7473 0.2805  -0.0418 -0.0716 656 GLU A C   
2857 O O   . GLU A 360 ? 0.7069 1.0771 0.6830 0.2652  -0.0339 -0.0752 656 GLU A O   
2858 C CB  . GLU A 360 ? 0.9288 1.0884 0.7385 0.3644  -0.0471 -0.0740 656 GLU A CB  
2859 C CG  . GLU A 360 ? 0.9788 1.2591 0.8079 0.4042  -0.0411 -0.0810 656 GLU A CG  
2860 C CD  . GLU A 360 ? 1.1853 1.4400 0.9409 0.4797  -0.0439 -0.0853 656 GLU A CD  
2861 O OE1 . GLU A 360 ? 1.4025 1.7159 1.1514 0.5124  -0.0368 -0.0909 656 GLU A OE1 
2862 O OE2 . GLU A 360 ? 1.1576 1.3307 0.8566 0.5079  -0.0530 -0.0831 656 GLU A OE2 
2863 N N   . SER A 361 ? 0.9059 1.1466 0.8319 0.2784  -0.0489 -0.0687 657 SER A N   
2864 C CA  A SER A 361 ? 0.7696 1.0882 0.7438 0.2603  -0.0479 -0.0704 657 SER A CA  
2865 C CA  B SER A 361 ? 0.7675 1.0842 0.7417 0.2596  -0.0480 -0.0702 657 SER A CA  
2866 C C   . SER A 361 ? 0.7716 1.1227 0.7998 0.2024  -0.0419 -0.0694 657 SER A C   
2867 O O   . SER A 361 ? 0.6758 1.1133 0.7431 0.1842  -0.0375 -0.0732 657 SER A O   
2868 C CB  A SER A 361 ? 0.7559 1.0207 0.7103 0.2652  -0.0564 -0.0667 657 SER A CB  
2869 C CB  B SER A 361 ? 0.7497 1.0097 0.7058 0.2608  -0.0565 -0.0662 657 SER A CB  
2870 O OG  A SER A 361 ? 0.7752 1.0020 0.6685 0.3211  -0.0622 -0.0674 657 SER A OG  
2871 O OG  B SER A 361 ? 0.6069 0.8274 0.5891 0.2109  -0.0570 -0.0612 657 SER A OG  
2872 N N   . PHE A 362 ? 0.7596 1.0417 0.7849 0.1734  -0.0421 -0.0645 658 PHE A N   
2873 C CA  . PHE A 362 ? 0.6574 0.9558 0.7225 0.1243  -0.0372 -0.0629 658 PHE A CA  
2874 C C   . PHE A 362 ? 0.6420 1.0055 0.7243 0.1138  -0.0279 -0.0665 658 PHE A C   
2875 O O   . PHE A 362 ? 0.6468 1.0531 0.7591 0.0769  -0.0226 -0.0676 658 PHE A O   
2876 C CB  . PHE A 362 ? 0.5106 0.7246 0.5658 0.1018  -0.0409 -0.0566 658 PHE A CB  
2877 C CG  . PHE A 362 ? 0.6459 0.8667 0.7324 0.0594  -0.0369 -0.0547 658 PHE A CG  
2878 C CD1 . PHE A 362 ? 0.6003 0.8280 0.7084 0.0376  -0.0380 -0.0541 658 PHE A CD1 
2879 C CD2 . PHE A 362 ? 0.6886 0.9046 0.7763 0.0436  -0.0321 -0.0536 658 PHE A CD2 
2880 C CE1 . PHE A 362 ? 0.5799 0.8024 0.7046 0.0036  -0.0345 -0.0527 658 PHE A CE1 
2881 C CE2 . PHE A 362 ? 0.7622 0.9739 0.8674 0.0086  -0.0288 -0.0515 658 PHE A CE2 
2882 C CZ  . PHE A 362 ? 0.7172 0.9296 0.8385 -0.0101 -0.0301 -0.0512 658 PHE A CZ  
2883 N N   . ILE A 363 ? 0.7587 1.1252 0.8163 0.1438  -0.0254 -0.0684 659 ILE A N   
2884 C CA  . ILE A 363 ? 0.7921 1.2333 0.8645 0.1367  -0.0154 -0.0721 659 ILE A CA  
2885 C C   . ILE A 363 ? 0.7421 1.2947 0.8400 0.1413  -0.0116 -0.0781 659 ILE A C   
2886 O O   . ILE A 363 ? 0.8254 1.4450 0.9518 0.1033  -0.0042 -0.0800 659 ILE A O   
2887 C CB  . ILE A 363 ? 0.7429 1.1645 0.7789 0.1745  -0.0136 -0.0735 659 ILE A CB  
2888 C CG1 . ILE A 363 ? 0.7587 1.0732 0.7685 0.1640  -0.0186 -0.0679 659 ILE A CG1 
2889 C CG2 . ILE A 363 ? 0.8442 1.3534 0.8965 0.1672  -0.0019 -0.0773 659 ILE A CG2 
2890 C CD1 . ILE A 363 ? 0.7476 1.0561 0.7772 0.1205  -0.0131 -0.0646 659 ILE A CD1 
2891 N N   . LYS A 364 ? 0.7351 1.3078 0.8175 0.1868  -0.0170 -0.0810 660 LYS A N   
2892 C CA  . LYS A 364 ? 0.7627 1.4455 0.8698 0.1933  -0.0158 -0.0866 660 LYS A CA  
2893 C C   . LYS A 364 ? 0.6197 1.3172 0.7614 0.1393  -0.0163 -0.0858 660 LYS A C   
2894 O O   . LYS A 364 ? 0.6852 1.4751 0.8552 0.1085  -0.0105 -0.0899 660 LYS A O   
2895 C CB  . LYS A 364 ? 0.7593 1.4369 0.8361 0.2534  -0.0241 -0.0883 660 LYS A CB  
2896 C CG  . LYS A 364 ? 0.7479 1.5579 0.8431 0.2784  -0.0229 -0.0952 660 LYS A CG  
2897 C CD  . LYS A 364 ? 0.8836 1.7802 0.9741 0.3098  -0.0145 -0.1004 660 LYS A CD  
2898 C CE  . LYS A 364 ? 0.9079 1.9020 0.9913 0.3282  -0.0158 -0.1041 660 LYS A CE  
2899 N NZ  . LYS A 364 ? 0.8978 1.8496 0.9469 0.3716  -0.0266 -0.1033 660 LYS A NZ  
2900 N N   . HIS A 365 ? 0.6142 1.2203 0.7497 0.1257  -0.0231 -0.0808 661 HIS A N   
2901 C CA  . HIS A 365 ? 0.5847 1.1894 0.7450 0.0782  -0.0237 -0.0802 661 HIS A CA  
2902 C C   . HIS A 365 ? 0.6310 1.2446 0.8054 0.0270  -0.0154 -0.0798 661 HIS A C   
2903 O O   . HIS A 365 ? 0.5150 1.1745 0.7062 -0.0120 -0.0125 -0.0828 661 HIS A O   
2904 C CB  . HIS A 365 ? 0.6327 1.1370 0.7810 0.0758  -0.0310 -0.0744 661 HIS A CB  
2905 C CG  . HIS A 365 ? 0.6383 1.1264 0.8049 0.0307  -0.0307 -0.0735 661 HIS A CG  
2906 N ND1 . HIS A 365 ? 0.6177 1.1613 0.8009 0.0148  -0.0316 -0.0780 661 HIS A ND1 
2907 C CD2 . HIS A 365 ? 0.6149 1.0357 0.7806 0.0014  -0.0300 -0.0691 661 HIS A CD2 
2908 C CE1 . HIS A 365 ? 0.6558 1.1587 0.8435 -0.0225 -0.0311 -0.0766 661 HIS A CE1 
2909 N NE2 . HIS A 365 ? 0.5794 1.0096 0.7567 -0.0289 -0.0300 -0.0711 661 HIS A NE2 
2910 N N   . MET A 366 ? 0.5609 1.1247 0.7219 0.0247  -0.0119 -0.0760 662 MET A N   
2911 C CA  . MET A 366 ? 0.4754 1.0406 0.6409 -0.0211 -0.0039 -0.0749 662 MET A CA  
2912 C C   . MET A 366 ? 0.4773 1.1534 0.6565 -0.0392 0.0046  -0.0807 662 MET A C   
2913 O O   . MET A 366 ? 0.3978 1.0956 0.5821 -0.0890 0.0093  -0.0818 662 MET A O   
2914 C CB  . MET A 366 ? 0.5274 1.0292 0.6742 -0.0142 -0.0021 -0.0702 662 MET A CB  
2915 C CG  . MET A 366 ? 0.4790 0.8843 0.6171 -0.0328 -0.0066 -0.0639 662 MET A CG  
2916 S SD  . MET A 366 ? 0.7215 1.0631 0.8369 -0.0206 -0.0065 -0.0589 662 MET A SD  
2917 C CE  . MET A 366 ? 0.7689 1.0788 0.8798 -0.0691 -0.0009 -0.0550 662 MET A CE  
2918 N N   . GLU A 367 ? 0.7069 1.4543 0.8868 0.0007  0.0067  -0.0845 663 GLU A N   
2919 C CA  . GLU A 367 ? 0.8446 1.7176 1.0402 -0.0133 0.0152  -0.0902 663 GLU A CA  
2920 C C   . GLU A 367 ? 0.7971 1.7365 1.0127 -0.0462 0.0133  -0.0946 663 GLU A C   
2921 O O   . GLU A 367 ? 0.7575 1.7614 0.9812 -0.0972 0.0206  -0.0972 663 GLU A O   
2922 C CB  . GLU A 367 ? 0.9337 1.8770 1.1249 0.0487  0.0158  -0.0944 663 GLU A CB  
2923 C CG  . GLU A 367 ? 1.0111 1.9016 1.1764 0.0825  0.0186  -0.0918 663 GLU A CG  
2924 C CD  . GLU A 367 ? 1.0704 2.0227 1.2211 0.1513  0.0184  -0.0968 663 GLU A CD  
2925 O OE1 . GLU A 367 ? 1.0365 2.1000 1.2041 0.1680  0.0184  -0.1025 663 GLU A OE1 
2926 O OE2 . GLU A 367 ? 1.0806 1.9687 1.1985 0.1904  0.0175  -0.0954 663 GLU A OE2 
2927 N N   . ASN A 368 ? 0.8225 1.7457 1.0415 -0.0198 0.0035  -0.0954 664 ASN A N   
2928 C CA  . ASN A 368 ? 0.6863 1.6660 0.9215 -0.0493 0.0003  -0.0998 664 ASN A CA  
2929 C C   . ASN A 368 ? 0.7042 1.6199 0.9328 -0.1144 0.0023  -0.0978 664 ASN A C   
2930 O O   . ASN A 368 ? 0.6722 1.6201 0.8916 -0.1590 0.0058  -0.1001 664 ASN A O   
2931 C CB  . ASN A 368 ? 0.7113 1.6688 0.9453 -0.0052 -0.0109 -0.1000 664 ASN A CB  
2932 C CG  . ASN A 368 ? 0.7136 1.7175 0.9382 0.0642  -0.0137 -0.1018 664 ASN A CG  
2933 O OD1 . ASN A 368 ? 0.7371 1.8058 0.9509 0.0755  -0.0075 -0.1040 664 ASN A OD1 
2934 N ND2 . ASN A 368 ? 0.5393 1.4769 0.7462 0.1096  -0.0228 -0.0991 664 ASN A ND2 
2935 N N   . GLU A 369 ? 0.7045 1.4982 0.9165 -0.1153 0.0002  -0.0914 665 GLU A N   
2936 C CA  . GLU A 369 ? 0.5468 1.2679 0.7437 -0.1661 0.0013  -0.0893 665 GLU A CA  
2937 C C   . GLU A 369 ? 0.7914 1.5259 0.9733 -0.2164 0.0115  -0.0891 665 GLU A C   
2938 O O   . GLU A 369 ? 0.9208 1.6353 1.0845 -0.2684 0.0137  -0.0905 665 GLU A O   
2939 C CB  . GLU A 369 ? 0.5586 1.1598 0.7421 -0.1474 -0.0035 -0.0824 665 GLU A CB  
2940 C CG  . GLU A 369 ? 0.7745 1.3431 0.9640 -0.1165 -0.0128 -0.0816 665 GLU A CG  
2941 C CD  . GLU A 369 ? 0.7843 1.3167 0.9673 -0.1480 -0.0154 -0.0830 665 GLU A CD  
2942 O OE1 . GLU A 369 ? 0.9716 1.4235 1.1360 -0.1673 -0.0143 -0.0793 665 GLU A OE1 
2943 O OE2 . GLU A 369 ? 0.6027 1.1887 0.7958 -0.1512 -0.0187 -0.0881 665 GLU A OE2 
2944 N N   . TYR A 370 ? 0.9043 1.6634 1.0860 -0.2032 0.0180  -0.0873 666 TYR A N   
2945 C CA  . TYR A 370 ? 0.8690 1.6471 1.0335 -0.2541 0.0286  -0.0869 666 TYR A CA  
2946 C C   . TYR A 370 ? 0.9033 1.7826 1.0659 -0.2806 0.0328  -0.0921 666 TYR A C   
2947 O O   . TYR A 370 ? 0.9300 1.7919 1.0580 -0.3323 0.0385  -0.0913 666 TYR A O   
2948 C CB  . TYR A 370 ? 0.7861 1.5544 0.9451 -0.2308 0.0344  -0.0829 666 TYR A CB  
2949 C CG  . TYR A 370 ? 0.7524 1.3910 0.8881 -0.2246 0.0316  -0.0754 666 TYR A CG  
2950 C CD1 . TYR A 370 ? 0.6525 1.2249 0.7936 -0.1802 0.0219  -0.0726 666 TYR A CD1 
2951 C CD2 . TYR A 370 ? 0.8370 1.4217 0.9417 -0.2644 0.0382  -0.0711 666 TYR A CD2 
2952 C CE1 . TYR A 370 ? 0.6633 1.1327 0.7856 -0.1757 0.0187  -0.0661 666 TYR A CE1 
2953 C CE2 . TYR A 370 ? 0.8245 1.2993 0.9074 -0.2545 0.0346  -0.0643 666 TYR A CE2 
2954 C CZ  . TYR A 370 ? 0.7534 1.1775 0.8482 -0.2104 0.0247  -0.0621 666 TYR A CZ  
2955 O OH  . TYR A 370 ? 0.9216 1.2514 0.9971 -0.2021 0.0207  -0.0558 666 TYR A OH  
2956 N N   . ARG A 371 ? 0.9231 1.8835 1.1056 -0.2394 0.0286  -0.0963 667 ARG A N   
2957 C CA  . ARG A 371 ? 1.0040 2.0499 1.1744 -0.2532 0.0301  -0.1006 667 ARG A CA  
2958 C C   . ARG A 371 ? 0.9978 2.0179 1.1504 -0.2921 0.0264  -0.1025 667 ARG A C   
2959 O O   . ARG A 371 ? 1.0604 2.0723 1.1799 -0.3467 0.0315  -0.1028 667 ARG A O   
2960 C CB  . ARG A 371 ? 1.0820 2.2128 1.2719 -0.1900 0.0256  -0.1041 667 ARG A CB  
2961 C CG  . ARG A 371 ? 1.1981 2.4306 1.3766 -0.1967 0.0257  -0.1092 667 ARG A CG  
2962 C CD  . ARG A 371 ? 1.2716 2.5636 1.4613 -0.1284 0.0187  -0.1122 667 ARG A CD  
2963 N NE  . ARG A 371 ? 1.3684 2.6006 1.5702 -0.1015 0.0102  -0.1111 667 ARG A NE  
2964 C CZ  . ARG A 371 ? 1.4724 2.7048 1.6723 -0.1175 0.0053  -0.1132 667 ARG A CZ  
2965 N NH1 . ARG A 371 ? 1.5395 2.8279 1.7245 -0.1607 0.0083  -0.1166 667 ARG A NH1 
2966 N NH2 . ARG A 371 ? 1.4314 2.6086 1.6417 -0.0912 -0.0027 -0.1119 667 ARG A NH2 
2967 N N   . CYS A 372 ? 0.9073 1.9096 1.0763 -0.2653 0.0177  -0.1037 668 CYS A N   
2968 C CA  A CYS A 372 ? 0.9375 1.9252 1.0907 -0.2954 0.0142  -0.1062 668 CYS A CA  
2969 C CA  B CYS A 372 ? 0.9368 1.9242 1.0905 -0.2946 0.0140  -0.1062 668 CYS A CA  
2970 C C   . CYS A 372 ? 0.9187 1.7906 1.0536 -0.3272 0.0124  -0.1034 668 CYS A C   
2971 O O   . CYS A 372 ? 1.0121 1.8586 1.1324 -0.3469 0.0087  -0.1055 668 CYS A O   
2972 C CB  A CYS A 372 ? 0.9152 1.9494 1.0906 -0.2495 0.0056  -0.1093 668 CYS A CB  
2973 C CB  B CYS A 372 ? 0.9146 1.9461 1.0910 -0.2478 0.0054  -0.1092 668 CYS A CB  
2974 S SG  A CYS A 372 ? 0.9883 2.1420 1.1531 -0.2559 0.0064  -0.1153 668 CYS A SG  
2975 S SG  B CYS A 372 ? 0.8099 1.7732 1.0138 -0.1954 -0.0044 -0.1063 668 CYS A SG  
2976 N N   . ARG A 373 ? 0.7027 1.5033 0.8338 -0.3313 0.0148  -0.0991 669 ARG A N   
2977 C CA  . ARG A 373 ? 0.7153 1.4014 0.8199 -0.3582 0.0130  -0.0966 669 ARG A CA  
2978 C C   . ARG A 373 ? 0.9307 1.5495 0.9999 -0.3912 0.0205  -0.0920 669 ARG A C   
2979 O O   . ARG A 373 ? 1.0188 1.5409 1.0464 -0.4200 0.0205  -0.0902 669 ARG A O   
2980 C CB  . ARG A 373 ? 0.7360 1.3773 0.8692 -0.3197 0.0040  -0.0959 669 ARG A CB  
2981 C CG  . ARG A 373 ? 0.8436 1.3802 0.9485 -0.3397 -0.0001 -0.0956 669 ARG A CG  
2982 C CD  . ARG A 373 ? 0.7969 1.2647 0.9135 -0.2871 -0.0065 -0.0904 669 ARG A CD  
2983 N NE  . ARG A 373 ? 0.8639 1.2530 0.9555 -0.2968 -0.0104 -0.0910 669 ARG A NE  
2984 C CZ  . ARG A 373 ? 0.8570 1.1717 0.9461 -0.2651 -0.0143 -0.0861 669 ARG A CZ  
2985 N NH1 . ARG A 373 ? 0.7910 1.0952 0.8996 -0.2264 -0.0155 -0.0801 669 ARG A NH1 
2986 N NH2 . ARG A 373 ? 0.7352 0.9883 0.7992 -0.2731 -0.0168 -0.0877 669 ARG A NH2 
2987 N N   . GLY A 374 ? 0.9599 1.6211 1.0384 -0.3855 0.0269  -0.0900 670 GLY A N   
2988 C CA  . GLY A 374 ? 1.0461 1.6438 1.0884 -0.4159 0.0342  -0.0851 670 GLY A CA  
2989 C C   . GLY A 374 ? 1.0518 1.5775 1.1030 -0.3931 0.0322  -0.0804 670 GLY A C   
2990 O O   . GLY A 374 ? 1.1577 1.6095 1.1701 -0.4143 0.0371  -0.0752 670 GLY A O   
2991 N N   . GLY A 375 ? 0.8767 1.3962 0.9602 -0.3356 0.0243  -0.0794 671 GLY A N   
2992 C CA  . GLY A 375 ? 0.8574 1.2900 0.9357 -0.2983 0.0208  -0.0725 671 GLY A CA  
2993 C C   . GLY A 375 ? 0.7882 1.2057 0.8926 -0.2510 0.0110  -0.0724 671 GLY A C   
2994 O O   . GLY A 375 ? 0.7014 1.1690 0.8254 -0.2446 0.0069  -0.0772 671 GLY A O   
2995 N N   . CYS A 376 ? 0.6769 1.0257 0.7783 -0.2201 0.0071  -0.0665 672 CYS A N   
2996 C CA  . CYS A 376 ? 0.5840 0.9067 0.7026 -0.1802 -0.0018 -0.0648 672 CYS A CA  
2997 C C   . CYS A 376 ? 0.6871 0.9253 0.7909 -0.1663 -0.0050 -0.0580 672 CYS A C   
2998 O O   . CYS A 376 ? 0.6221 0.8533 0.7269 -0.1476 -0.0048 -0.0546 672 CYS A O   
2999 C CB  . CYS A 376 ? 0.6035 0.9862 0.7467 -0.1414 -0.0041 -0.0666 672 CYS A CB  
3000 S SG  . CYS A 376 ? 0.6323 0.9694 0.7836 -0.0974 -0.0146 -0.0633 672 CYS A SG  
3001 N N   . PRO A 377 ? 0.7193 0.8963 0.8077 -0.1725 -0.0082 -0.0561 673 PRO A N   
3002 C CA  . PRO A 377 ? 0.5658 0.6760 0.6418 -0.1559 -0.0119 -0.0497 673 PRO A CA  
3003 C C   . PRO A 377 ? 0.5606 0.6786 0.6596 -0.1210 -0.0182 -0.0470 673 PRO A C   
3004 O O   . PRO A 377 ? 0.5701 0.7123 0.6875 -0.1059 -0.0222 -0.0490 673 PRO A O   
3005 C CB  . PRO A 377 ? 0.7910 0.8526 0.8496 -0.1617 -0.0144 -0.0499 673 PRO A CB  
3006 C CG  . PRO A 377 ? 0.6790 0.7851 0.7542 -0.1684 -0.0152 -0.0560 673 PRO A CG  
3007 C CD  . PRO A 377 ? 0.7092 0.8837 0.7945 -0.1860 -0.0101 -0.0602 673 PRO A CD  
3008 N N   . ALA A 378 ? 0.7093 0.8021 0.8013 -0.1101 -0.0195 -0.0424 674 ALA A N   
3009 C CA  . ALA A 378 ? 0.6296 0.7247 0.7333 -0.0833 -0.0253 -0.0402 674 ALA A CA  
3010 C C   . ALA A 378 ? 0.5449 0.5957 0.6365 -0.0769 -0.0294 -0.0344 674 ALA A C   
3011 O O   . ALA A 378 ? 0.5761 0.6078 0.6505 -0.0870 -0.0260 -0.0323 674 ALA A O   
3012 C CB  . ALA A 378 ? 0.6169 0.7565 0.7252 -0.0729 -0.0221 -0.0435 674 ALA A CB  
3013 N N   . ASP A 379 ? 0.4755 0.5121 0.5733 -0.0622 -0.0369 -0.0316 675 ASP A N   
3014 C CA  . ASP A 379 ? 0.4648 0.4713 0.5544 -0.0570 -0.0426 -0.0262 675 ASP A CA  
3015 C C   . ASP A 379 ? 0.5682 0.5744 0.6529 -0.0466 -0.0464 -0.0257 675 ASP A C   
3016 O O   . ASP A 379 ? 0.5825 0.5891 0.6691 -0.0387 -0.0511 -0.0259 675 ASP A O   
3017 C CB  . ASP A 379 ? 0.5499 0.5489 0.6474 -0.0528 -0.0480 -0.0237 675 ASP A CB  
3018 C CG  . ASP A 379 ? 0.6799 0.6625 0.7705 -0.0478 -0.0539 -0.0184 675 ASP A CG  
3019 O OD1 . ASP A 379 ? 0.6933 0.6737 0.7855 -0.0429 -0.0561 -0.0164 675 ASP A OD1 
3020 O OD2 . ASP A 379 ? 0.6717 0.6470 0.7535 -0.0468 -0.0564 -0.0166 675 ASP A OD2 
3021 N N   . TRP A 380 ? 0.5200 0.5199 0.5914 -0.0472 -0.0439 -0.0253 676 TRP A N   
3022 C CA  . TRP A 380 ? 0.4497 0.4400 0.5070 -0.0363 -0.0474 -0.0255 676 TRP A CA  
3023 C C   . TRP A 380 ? 0.5072 0.4736 0.5584 -0.0349 -0.0576 -0.0218 676 TRP A C   
3024 O O   . TRP A 380 ? 0.5710 0.5223 0.6057 -0.0278 -0.0619 -0.0228 676 TRP A O   
3025 C CB  . TRP A 380 ? 0.4528 0.4354 0.4954 -0.0397 -0.0436 -0.0245 676 TRP A CB  
3026 C CG  . TRP A 380 ? 0.5355 0.5133 0.5592 -0.0271 -0.0437 -0.0267 676 TRP A CG  
3027 C CD1 . TRP A 380 ? 0.5158 0.5206 0.5344 -0.0188 -0.0356 -0.0311 676 TRP A CD1 
3028 C CD2 . TRP A 380 ? 0.5510 0.4954 0.5533 -0.0213 -0.0522 -0.0249 676 TRP A CD2 
3029 N NE1 . TRP A 380 ? 0.6553 0.6403 0.6482 -0.0031 -0.0382 -0.0324 676 TRP A NE1 
3030 C CE2 . TRP A 380 ? 0.7115 0.6541 0.6915 -0.0067 -0.0487 -0.0288 676 TRP A CE2 
3031 C CE3 . TRP A 380 ? 0.6163 0.5363 0.6138 -0.0284 -0.0625 -0.0208 676 TRP A CE3 
3032 C CZ2 . TRP A 380 ? 0.6474 0.5514 0.5945 0.0005  -0.0555 -0.0289 676 TRP A CZ2 
3033 C CZ3 . TRP A 380 ? 0.5678 0.4570 0.5359 -0.0266 -0.0697 -0.0207 676 TRP A CZ3 
3034 C CH2 . TRP A 380 ? 0.6343 0.5093 0.5748 -0.0125 -0.0664 -0.0249 676 TRP A CH2 
3035 N N   . VAL A 381 ? 0.6155 0.5765 0.6727 -0.0419 -0.0617 -0.0176 677 VAL A N   
3036 C CA  . VAL A 381 ? 0.5270 0.4797 0.5799 -0.0456 -0.0714 -0.0139 677 VAL A CA  
3037 C C   . VAL A 381 ? 0.6896 0.6443 0.7450 -0.0474 -0.0744 -0.0145 677 VAL A C   
3038 O O   . VAL A 381 ? 0.5665 0.5047 0.6039 -0.0540 -0.0814 -0.0130 677 VAL A O   
3039 C CB  . VAL A 381 ? 0.5384 0.5007 0.6009 -0.0469 -0.0745 -0.0097 677 VAL A CB  
3040 C CG1 . VAL A 381 ? 0.5280 0.5038 0.5942 -0.0534 -0.0838 -0.0063 677 VAL A CG1 
3041 C CG2 . VAL A 381 ? 0.5126 0.4613 0.5605 -0.0444 -0.0742 -0.0077 677 VAL A CG2 
3042 N N   . TRP A 382 ? 0.5881 0.5583 0.6592 -0.0439 -0.0691 -0.0168 678 TRP A N   
3043 C CA  . TRP A 382 ? 0.5711 0.5422 0.6425 -0.0441 -0.0710 -0.0172 678 TRP A CA  
3044 C C   . TRP A 382 ? 0.6035 0.5661 0.6598 -0.0316 -0.0684 -0.0214 678 TRP A C   
3045 O O   . TRP A 382 ? 0.5668 0.5112 0.6053 -0.0296 -0.0722 -0.0208 678 TRP A O   
3046 C CB  . TRP A 382 ? 0.6191 0.6133 0.7142 -0.0454 -0.0678 -0.0174 678 TRP A CB  
3047 C CG  . TRP A 382 ? 0.6200 0.6258 0.7243 -0.0519 -0.0721 -0.0130 678 TRP A CG  
3048 C CD1 . TRP A 382 ? 0.6032 0.6151 0.7095 -0.0516 -0.0747 -0.0101 678 TRP A CD1 
3049 C CD2 . TRP A 382 ? 0.5444 0.5640 0.6553 -0.0577 -0.0745 -0.0109 678 TRP A CD2 
3050 N NE1 . TRP A 382 ? 0.7004 0.7372 0.8169 -0.0542 -0.0785 -0.0068 678 TRP A NE1 
3051 C CE2 . TRP A 382 ? 0.6596 0.7025 0.7799 -0.0602 -0.0779 -0.0072 678 TRP A CE2 
3052 C CE3 . TRP A 382 ? 0.6096 0.6266 0.7172 -0.0597 -0.0740 -0.0116 678 TRP A CE3 
3053 C CZ2 . TRP A 382 ? 0.6606 0.7313 0.7901 -0.0667 -0.0799 -0.0044 678 TRP A CZ2 
3054 C CZ3 . TRP A 382 ? 0.7090 0.7444 0.8230 -0.0686 -0.0759 -0.0084 678 TRP A CZ3 
3055 C CH2 . TRP A 382 ? 0.7058 0.7713 0.8322 -0.0730 -0.0784 -0.0050 678 TRP A CH2 
3056 N N   . ILE A 383 ? 0.5565 0.5334 0.6152 -0.0223 -0.0620 -0.0253 679 ILE A N   
3057 C CA  . ILE A 383 ? 0.5347 0.5169 0.5797 -0.0040 -0.0595 -0.0297 679 ILE A CA  
3058 C C   . ILE A 383 ? 0.6926 0.6349 0.6975 0.0081  -0.0640 -0.0298 679 ILE A C   
3059 O O   . ILE A 383 ? 0.6675 0.5901 0.6448 0.0256  -0.0662 -0.0316 679 ILE A O   
3060 C CB  . ILE A 383 ? 0.5437 0.5686 0.6053 -0.0007 -0.0507 -0.0342 679 ILE A CB  
3061 C CG1 . ILE A 383 ? 0.4644 0.5176 0.5533 -0.0147 -0.0470 -0.0351 679 ILE A CG1 
3062 C CG2 . ILE A 383 ? 0.5321 0.5763 0.5786 0.0244  -0.0481 -0.0392 679 ILE A CG2 
3063 C CD1 . ILE A 383 ? 0.6782 0.7457 0.7734 -0.0072 -0.0487 -0.0370 679 ILE A CD1 
3064 N N   . VAL A 384 ? 0.5775 0.5013 0.5715 0.0009  -0.0659 -0.0282 680 VAL A N   
3065 C CA  . VAL A 384 ? 0.6775 0.5551 0.6249 0.0114  -0.0706 -0.0291 680 VAL A CA  
3066 C C   . VAL A 384 ? 0.7437 0.5763 0.6616 0.0008  -0.0795 -0.0259 680 VAL A C   
3067 O O   . VAL A 384 ? 0.6857 0.5224 0.6189 -0.0237 -0.0841 -0.0214 680 VAL A O   
3068 C CB  . VAL A 384 ? 0.6457 0.5125 0.5858 0.0032  -0.0716 -0.0281 680 VAL A CB  
3069 C CG1 . VAL A 384 ? 0.6472 0.4572 0.5311 0.0117  -0.0774 -0.0297 680 VAL A CG1 
3070 C CG2 . VAL A 384 ? 0.7054 0.6128 0.6670 0.0106  -0.0617 -0.0308 680 VAL A CG2 
3071 N N   . PRO A 385 ? 0.8354 0.6242 0.7058 0.0181  -0.0821 -0.0279 681 PRO A N   
3072 C CA  . PRO A 385 ? 0.8829 0.6176 0.7127 0.0025  -0.0903 -0.0243 681 PRO A CA  
3073 C C   . PRO A 385 ? 1.0024 0.7049 0.8096 -0.0268 -0.0980 -0.0212 681 PRO A C   
3074 O O   . PRO A 385 ? 0.8631 0.5648 0.6671 -0.0247 -0.0979 -0.0229 681 PRO A O   
3075 C CB  . PRO A 385 ? 0.9506 0.6314 0.7184 0.0345  -0.0911 -0.0280 681 PRO A CB  
3076 C CG  . PRO A 385 ? 0.9552 0.6909 0.7517 0.0687  -0.0823 -0.0334 681 PRO A CG  
3077 C CD  . PRO A 385 ? 0.7553 0.5395 0.5988 0.0544  -0.0776 -0.0336 681 PRO A CD  
3078 N N   . PRO A 386 ? 0.9219 0.6034 0.7129 -0.0568 -0.1047 -0.0166 682 PRO A N   
3079 C CA  . PRO A 386 ? 0.8349 0.5028 0.6098 -0.0907 -0.1128 -0.0135 682 PRO A CA  
3080 C C   . PRO A 386 ? 0.9284 0.5121 0.6227 -0.0957 -0.1197 -0.0155 682 PRO A C   
3081 O O   . PRO A 386 ? 0.9991 0.5648 0.6689 -0.1311 -0.1280 -0.0130 682 PRO A O   
3082 C CB  . PRO A 386 ? 0.8289 0.5174 0.6170 -0.1222 -0.1161 -0.0081 682 PRO A CB  
3083 C CG  . PRO A 386 ? 0.8697 0.5243 0.6316 -0.1064 -0.1132 -0.0085 682 PRO A CG  
3084 C CD  . PRO A 386 ? 0.8258 0.5014 0.6121 -0.0636 -0.1051 -0.0137 682 PRO A CD  
3085 N N   . MET A 387 ? 0.8857 0.4174 0.5331 -0.0613 -0.1169 -0.0201 683 MET A N   
3086 C CA  . MET A 387 ? 0.9251 0.3708 0.4898 -0.0567 -0.1224 -0.0234 683 MET A CA  
3087 C C   . MET A 387 ? 1.1876 0.6335 0.7453 -0.0049 -0.1147 -0.0298 683 MET A C   
3088 O O   . MET A 387 ? 1.0569 0.5561 0.6586 0.0232  -0.1067 -0.0312 683 MET A O   
3089 C CB  . MET A 387 ? 1.1436 0.4936 0.6202 -0.0702 -0.1293 -0.0218 683 MET A CB  
3090 C CG  . MET A 387 ? 1.2078 0.5364 0.6641 -0.0296 -0.1243 -0.0233 683 MET A CG  
3091 S SD  . MET A 387 ? 1.5256 0.7294 0.8676 -0.0428 -0.1320 -0.0202 683 MET A SD  
3092 C CE  . MET A 387 ? 1.5369 0.6291 0.7734 -0.0517 -0.1403 -0.0242 683 MET A CE  
3093 N N   . SER A 388 ? 1.1849 0.5783 0.6884 0.0056  -0.1172 -0.0339 684 SER A N   
3094 C CA  . SER A 388 ? 1.2347 0.6220 0.7161 0.0569  -0.1101 -0.0406 684 SER A CA  
3095 C C   . SER A 388 ? 1.1203 0.6125 0.6882 0.0752  -0.0990 -0.0418 684 SER A C   
3096 O O   . SER A 388 ? 1.1713 0.6893 0.7404 0.1174  -0.0913 -0.0463 684 SER A O   
3097 C CB  . SER A 388 ? 1.1877 0.5147 0.6032 0.0955  -0.1099 -0.0432 684 SER A CB  
3098 O OG  . SER A 388 ? 1.4064 0.6286 0.7365 0.0715  -0.1201 -0.0409 684 SER A OG  
3099 N N   . GLY A 389 ? 1.0367 0.5892 0.6712 0.0435  -0.0984 -0.0378 685 GLY A N   
3100 C CA  . GLY A 389 ? 0.9178 0.5593 0.6274 0.0519  -0.0884 -0.0379 685 GLY A CA  
3101 C C   . GLY A 389 ? 1.0498 0.7183 0.7561 0.0900  -0.0788 -0.0438 685 GLY A C   
3102 O O   . GLY A 389 ? 0.9060 0.6283 0.6425 0.1113  -0.0709 -0.0460 685 GLY A O   
3103 N N   . SER A 390 ? 1.0394 0.6763 0.7079 0.0984  -0.0792 -0.0467 686 SER A N   
3104 C CA  . SER A 390 ? 0.8968 0.5759 0.5715 0.1288  -0.0685 -0.0517 686 SER A CA  
3105 C C   . SER A 390 ? 0.9526 0.6120 0.5761 0.1786  -0.0651 -0.0581 686 SER A C   
3106 O O   . SER A 390 ? 1.0424 0.7503 0.6718 0.2081  -0.0553 -0.0628 686 SER A O   
3107 C CB  . SER A 390 ? 0.9737 0.6317 0.6293 0.1194  -0.0694 -0.0522 686 SER A CB  
3108 O OG  . SER A 390 ? 1.1143 0.6805 0.6956 0.1186  -0.0797 -0.0538 686 SER A OG  
3109 N N   . ILE A 391 ? 1.0058 0.5953 0.5739 0.1904  -0.0728 -0.0584 687 ILE A N   
3110 C CA  . ILE A 391 ? 1.0325 0.6054 0.5504 0.2447  -0.0701 -0.0641 687 ILE A CA  
3111 C C   . ILE A 391 ? 1.0179 0.6548 0.5806 0.2566  -0.0665 -0.0632 687 ILE A C   
3112 O O   . ILE A 391 ? 1.2144 0.8388 0.7357 0.3024  -0.0662 -0.0669 687 ILE A O   
3113 C CB  . ILE A 391 ? 1.3324 0.7771 0.7441 0.2582  -0.0804 -0.0655 687 ILE A CB  
3114 C CG1 . ILE A 391 ? 1.3765 0.7726 0.7776 0.2256  -0.0896 -0.0594 687 ILE A CG1 
3115 C CG2 . ILE A 391 ? 1.3829 0.7593 0.7410 0.2459  -0.0847 -0.0675 687 ILE A CG2 
3116 C CD1 . ILE A 391 ? 1.5355 0.8036 0.8220 0.2440  -0.0983 -0.0608 687 ILE A CD1 
3117 N N   . THR A 392 ? 1.0210 0.7257 0.6641 0.2185  -0.0642 -0.0586 688 THR A N   
3118 C CA  . THR A 392 ? 0.9641 0.7451 0.6621 0.2218  -0.0596 -0.0582 688 THR A CA  
3119 C C   . THR A 392 ? 0.8619 0.7443 0.6288 0.2104  -0.0488 -0.0595 688 THR A C   
3120 O O   . THR A 392 ? 0.8946 0.7812 0.6834 0.1809  -0.0470 -0.0571 688 THR A O   
3121 C CB  . THR A 392 ? 0.9917 0.7572 0.7161 0.1841  -0.0660 -0.0520 688 THR A CB  
3122 O OG1 . THR A 392 ? 0.8898 0.6798 0.6644 0.1403  -0.0654 -0.0478 688 THR A OG1 
3123 C CG2 . THR A 392 ? 1.0525 0.7137 0.7062 0.1805  -0.0767 -0.0493 688 THR A CG2 
3124 N N   . PRO A 393 ? 0.8957 0.8603 0.6941 0.2304  -0.0418 -0.0630 689 PRO A N   
3125 C CA  . PRO A 393 ? 0.8984 0.9579 0.7488 0.2182  -0.0306 -0.0650 689 PRO A CA  
3126 C C   . PRO A 393 ? 0.8701 0.9518 0.7753 0.1659  -0.0291 -0.0599 689 PRO A C   
3127 O O   . PRO A 393 ? 0.8620 0.9973 0.7962 0.1475  -0.0204 -0.0603 689 PRO A O   
3128 C CB  . PRO A 393 ? 0.9542 1.0961 0.8187 0.2506  -0.0257 -0.0701 689 PRO A CB  
3129 C CG  . PRO A 393 ? 1.0430 1.1372 0.8881 0.2609  -0.0352 -0.0682 689 PRO A CG  
3130 C CD  . PRO A 393 ? 0.9902 0.9667 0.7728 0.2649  -0.0441 -0.0654 689 PRO A CD  
3131 N N   . VAL A 394 ? 0.7631 0.8040 0.6780 0.1424  -0.0368 -0.0552 690 VAL A N   
3132 C CA  . VAL A 394 ? 0.6482 0.7081 0.6084 0.1003  -0.0353 -0.0509 690 VAL A CA  
3133 C C   . VAL A 394 ? 0.7101 0.7335 0.6647 0.0785  -0.0365 -0.0471 690 VAL A C   
3134 O O   . VAL A 394 ? 0.6277 0.6723 0.6109 0.0512  -0.0325 -0.0445 690 VAL A O   
3135 C CB  . VAL A 394 ? 0.5932 0.6292 0.5657 0.0858  -0.0424 -0.0474 690 VAL A CB  
3136 C CG1 . VAL A 394 ? 0.6316 0.7169 0.6198 0.1006  -0.0404 -0.0508 690 VAL A CG1 
3137 C CG2 . VAL A 394 ? 0.6819 0.6396 0.6113 0.0916  -0.0523 -0.0446 690 VAL A CG2 
3138 N N   . PHE A 395 ? 0.7562 0.7186 0.6680 0.0896  -0.0428 -0.0467 691 PHE A N   
3139 C CA  . PHE A 395 ? 0.7000 0.6332 0.6035 0.0717  -0.0446 -0.0437 691 PHE A CA  
3140 C C   . PHE A 395 ? 0.7079 0.6898 0.6281 0.0683  -0.0337 -0.0451 691 PHE A C   
3141 O O   . PHE A 395 ? 0.6042 0.5833 0.5375 0.0440  -0.0328 -0.0410 691 PHE A O   
3142 C CB  . PHE A 395 ? 0.7407 0.6056 0.5867 0.0871  -0.0520 -0.0450 691 PHE A CB  
3143 C CG  . PHE A 395 ? 0.8196 0.6541 0.6529 0.0691  -0.0556 -0.0424 691 PHE A CG  
3144 C CD1 . PHE A 395 ? 0.7320 0.5253 0.5580 0.0439  -0.0666 -0.0377 691 PHE A CD1 
3145 C CD2 . PHE A 395 ? 0.8157 0.6683 0.6423 0.0776  -0.0481 -0.0446 691 PHE A CD2 
3146 C CE1 . PHE A 395 ? 0.8848 0.6569 0.6983 0.0288  -0.0712 -0.0355 691 PHE A CE1 
3147 C CE2 . PHE A 395 ? 0.8040 0.6276 0.6160 0.0623  -0.0521 -0.0420 691 PHE A CE2 
3148 C CZ  . PHE A 395 ? 0.7942 0.5779 0.6001 0.0388  -0.0642 -0.0376 691 PHE A CZ  
3149 N N   . HIS A 396 ? 0.7547 0.7846 0.6717 0.0928  -0.0252 -0.0506 692 HIS A N   
3150 C CA  . HIS A 396 ? 0.6180 0.6975 0.5406 0.0922  -0.0138 -0.0526 692 HIS A CA  
3151 C C   . HIS A 396 ? 0.6946 0.8443 0.6588 0.0667  -0.0046 -0.0522 692 HIS A C   
3152 O O   . HIS A 396 ? 0.7061 0.9037 0.6756 0.0575  0.0060  -0.0533 692 HIS A O   
3153 C CB  . HIS A 396 ? 0.8142 0.9136 0.7052 0.1358  -0.0094 -0.0593 692 HIS A CB  
3154 C CG  . HIS A 396 ? 0.8796 0.8954 0.7154 0.1589  -0.0184 -0.0603 692 HIS A CG  
3155 N ND1 . HIS A 396 ? 0.8732 0.8401 0.6855 0.1468  -0.0212 -0.0582 692 HIS A ND1 
3156 C CD2 . HIS A 396 ? 0.8861 0.8508 0.6783 0.1901  -0.0259 -0.0631 692 HIS A CD2 
3157 C CE1 . HIS A 396 ? 0.9689 0.8605 0.7258 0.1672  -0.0300 -0.0602 692 HIS A CE1 
3158 N NE2 . HIS A 396 ? 0.9957 0.8794 0.7362 0.1932  -0.0328 -0.0630 692 HIS A NE2 
3159 N N   . GLN A 397 ? 0.6441 0.7972 0.6331 0.0518  -0.0085 -0.0506 693 GLN A N   
3160 C CA  . GLN A 397 ? 0.6157 0.8269 0.6365 0.0261  -0.0014 -0.0511 693 GLN A CA  
3161 C C   . GLN A 397 ? 0.5988 0.7711 0.6278 -0.0101 -0.0033 -0.0451 693 GLN A C   
3162 O O   . GLN A 397 ? 0.5843 0.7114 0.6164 -0.0131 -0.0123 -0.0419 693 GLN A O   
3163 C CB  . GLN A 397 ? 0.6258 0.8654 0.6625 0.0384  -0.0048 -0.0542 693 GLN A CB  
3164 C CG  . GLN A 397 ? 0.6344 0.9292 0.7003 0.0083  0.0008  -0.0554 693 GLN A CG  
3165 C CD  . GLN A 397 ? 0.6642 1.0489 0.7384 0.0045  0.0122  -0.0602 693 GLN A CD  
3166 O OE1 . GLN A 397 ? 0.7282 1.1667 0.8005 0.0386  0.0140  -0.0653 693 GLN A OE1 
3167 N NE2 . GLN A 397 ? 0.7017 1.1040 0.7805 -0.0367 0.0202  -0.0585 693 GLN A NE2 
3168 N N   . GLU A 398 ? 0.5800 0.7698 0.6076 -0.0362 0.0054  -0.0436 694 GLU A N   
3169 C CA  . GLU A 398 ? 0.6650 0.8196 0.6921 -0.0686 0.0050  -0.0387 694 GLU A CA  
3170 C C   . GLU A 398 ? 0.6957 0.8676 0.7417 -0.0823 0.0041  -0.0404 694 GLU A C   
3171 O O   . GLU A 398 ? 0.7378 0.9729 0.7978 -0.0863 0.0097  -0.0454 694 GLU A O   
3172 C CB  . GLU A 398 ? 0.6113 0.7786 0.6226 -0.0959 0.0157  -0.0369 694 GLU A CB  
3173 C CG  . GLU A 398 ? 0.7447 0.8882 0.7342 -0.0838 0.0164  -0.0346 694 GLU A CG  
3174 C CD  . GLU A 398 ? 0.7465 0.9108 0.7186 -0.1102 0.0285  -0.0331 694 GLU A CD  
3175 O OE1 . GLU A 398 ? 0.8521 0.9938 0.8034 -0.1036 0.0297  -0.0306 694 GLU A OE1 
3176 O OE2 . GLU A 398 ? 0.8281 1.0297 0.8034 -0.1407 0.0369  -0.0342 694 GLU A OE2 
3177 N N   . MET A 399 ? 0.7548 0.8756 0.8003 -0.0882 -0.0032 -0.0366 695 MET A N   
3178 C CA  . MET A 399 ? 0.7066 0.8330 0.7656 -0.0983 -0.0050 -0.0382 695 MET A CA  
3179 C C   . MET A 399 ? 0.7125 0.7886 0.7527 -0.1213 -0.0049 -0.0342 695 MET A C   
3180 O O   . MET A 399 ? 0.6998 0.7266 0.7264 -0.1135 -0.0102 -0.0291 695 MET A O   
3181 C CB  . MET A 399 ? 0.6033 0.7162 0.6762 -0.0742 -0.0148 -0.0382 695 MET A CB  
3182 C CG  . MET A 399 ? 0.5349 0.6728 0.6109 -0.0456 -0.0169 -0.0414 695 MET A CG  
3183 S SD  . MET A 399 ? 0.5847 0.6799 0.6599 -0.0266 -0.0288 -0.0389 695 MET A SD  
3184 C CE  . MET A 399 ? 0.6059 0.7056 0.6604 0.0067  -0.0304 -0.0422 695 MET A CE  
3185 N N   . LEU A 400 ? 0.5722 0.6590 0.6067 -0.1478 0.0003  -0.0367 696 LEU A N   
3186 C CA  . LEU A 400 ? 0.7107 0.7375 0.7150 -0.1668 0.0003  -0.0336 696 LEU A CA  
3187 C C   . LEU A 400 ? 0.8095 0.8169 0.8248 -0.1538 -0.0070 -0.0343 696 LEU A C   
3188 O O   . LEU A 400 ? 0.6815 0.7265 0.7167 -0.1566 -0.0070 -0.0391 696 LEU A O   
3189 C CB  . LEU A 400 ? 0.7332 0.7695 0.7130 -0.2079 0.0096  -0.0362 696 LEU A CB  
3190 C CG  . LEU A 400 ? 0.8176 0.8681 0.7764 -0.2310 0.0189  -0.0348 696 LEU A CG  
3191 C CD1 . LEU A 400 ? 0.8254 0.8919 0.7587 -0.2797 0.0278  -0.0379 696 LEU A CD1 
3192 C CD2 . LEU A 400 ? 0.7975 0.7755 0.7215 -0.2245 0.0172  -0.0275 696 LEU A CD2 
3193 N N   . ASN A 401 ? 0.8140 0.7692 0.8164 -0.1380 -0.0132 -0.0295 697 ASN A N   
3194 C CA  . ASN A 401 ? 0.6910 0.6292 0.6994 -0.1259 -0.0188 -0.0299 697 ASN A CA  
3195 C C   . ASN A 401 ? 0.8131 0.6997 0.7799 -0.1429 -0.0156 -0.0303 697 ASN A C   
3196 O O   . ASN A 401 ? 0.7201 0.5544 0.6465 -0.1465 -0.0143 -0.0264 697 ASN A O   
3197 C CB  . ASN A 401 ? 0.6968 0.6191 0.7141 -0.0980 -0.0274 -0.0250 697 ASN A CB  
3198 C CG  . ASN A 401 ? 0.6945 0.6276 0.7318 -0.0849 -0.0324 -0.0262 697 ASN A CG  
3199 O OD1 . ASN A 401 ? 0.6914 0.6455 0.7398 -0.0934 -0.0299 -0.0308 697 ASN A OD1 
3200 N ND2 . ASN A 401 ? 0.6566 0.5811 0.6982 -0.0653 -0.0392 -0.0221 697 ASN A ND2 
3201 N N   . TYR A 402 ? 0.8577 0.7530 0.8278 -0.1524 -0.0148 -0.0352 698 TYR A N   
3202 C CA  . TYR A 402 ? 0.8151 0.6510 0.7393 -0.1640 -0.0133 -0.0365 698 TYR A CA  
3203 C C   . TYR A 402 ? 0.8609 0.7133 0.8047 -0.1548 -0.0165 -0.0408 698 TYR A C   
3204 O O   . TYR A 402 ? 0.7300 0.6417 0.7190 -0.1482 -0.0186 -0.0431 698 TYR A O   
3205 C CB  . TYR A 402 ? 0.8870 0.7054 0.7709 -0.2072 -0.0053 -0.0392 698 TYR A CB  
3206 C CG  . TYR A 402 ? 0.9547 0.8536 0.8726 -0.2319 -0.0008 -0.0444 698 TYR A CG  
3207 C CD1 . TYR A 402 ? 0.8837 0.8148 0.8122 -0.2479 -0.0006 -0.0510 698 TYR A CD1 
3208 C CD2 . TYR A 402 ? 0.8336 0.7804 0.7710 -0.2366 0.0032  -0.0430 698 TYR A CD2 
3209 C CE1 . TYR A 402 ? 0.8624 0.8771 0.8215 -0.2665 0.0027  -0.0559 698 TYR A CE1 
3210 C CE2 . TYR A 402 ? 0.8943 0.9242 0.8610 -0.2531 0.0075  -0.0481 698 TYR A CE2 
3211 C CZ  . TYR A 402 ? 0.9101 0.9764 0.8883 -0.2675 0.0069  -0.0545 698 TYR A CZ  
3212 O OH  . TYR A 402 ? 0.8454 1.0041 0.8529 -0.2801 0.0102  -0.0598 698 TYR A OH  
3213 N N   . ARG A 403 ? 0.7541 0.5487 0.6583 -0.1506 -0.0172 -0.0417 699 ARG A N   
3214 C CA  . ARG A 403 ? 0.8440 0.6490 0.7634 -0.1358 -0.0204 -0.0450 699 ARG A CA  
3215 C C   . ARG A 403 ? 0.9077 0.6993 0.7999 -0.1677 -0.0167 -0.0522 699 ARG A C   
3216 O O   . ARG A 403 ? 1.0026 0.7257 0.8329 -0.1865 -0.0136 -0.0536 699 ARG A O   
3217 C CB  . ARG A 403 ? 0.9313 0.6911 0.8279 -0.1012 -0.0243 -0.0416 699 ARG A CB  
3218 C CG  . ARG A 403 ? 1.1334 0.9198 1.0602 -0.0743 -0.0291 -0.0350 699 ARG A CG  
3219 C CD  . ARG A 403 ? 1.2531 1.0721 1.2110 -0.0454 -0.0340 -0.0337 699 ARG A CD  
3220 N NE  . ARG A 403 ? 1.4602 1.2338 1.3778 -0.0196 -0.0349 -0.0332 699 ARG A NE  
3221 C CZ  . ARG A 403 ? 1.5215 1.3194 1.4542 0.0065  -0.0376 -0.0330 699 ARG A CZ  
3222 N NH1 . ARG A 403 ? 1.4798 1.3409 1.4650 0.0045  -0.0396 -0.0327 699 ARG A NH1 
3223 N NH2 . ARG A 403 ? 1.5587 1.3161 1.4488 0.0355  -0.0379 -0.0331 699 ARG A NH2 
3224 N N   . LEU A 404 ? 0.9426 0.7959 0.8749 -0.1751 -0.0175 -0.0567 700 LEU A N   
3225 C CA  . LEU A 404 ? 0.7888 0.6409 0.7006 -0.2047 -0.0156 -0.0641 700 LEU A CA  
3226 C C   . LEU A 404 ? 0.9278 0.7819 0.8516 -0.1833 -0.0195 -0.0669 700 LEU A C   
3227 O O   . LEU A 404 ? 0.7860 0.6642 0.7460 -0.1502 -0.0231 -0.0630 700 LEU A O   
3228 C CB  . LEU A 404 ? 0.8142 0.7456 0.7588 -0.2319 -0.0136 -0.0680 700 LEU A CB  
3229 C CG  . LEU A 404 ? 0.7733 0.7310 0.7189 -0.2526 -0.0088 -0.0660 700 LEU A CG  
3230 C CD1 . LEU A 404 ? 0.6725 0.7251 0.6554 -0.2697 -0.0076 -0.0710 700 LEU A CD1 
3231 C CD2 . LEU A 404 ? 0.9190 0.8058 0.7974 -0.2884 -0.0036 -0.0659 700 LEU A CD2 
3232 N N   . THR A 405 ? 0.8788 0.7066 0.7676 -0.2062 -0.0185 -0.0736 701 THR A N   
3233 C CA  . THR A 405 ? 0.8937 0.7248 0.7893 -0.1907 -0.0213 -0.0773 701 THR A CA  
3234 C C   . THR A 405 ? 0.9288 0.8132 0.8394 -0.2215 -0.0220 -0.0846 701 THR A C   
3235 O O   . THR A 405 ? 0.8334 0.7277 0.7251 -0.2615 -0.0194 -0.0881 701 THR A O   
3236 C CB  . THR A 405 ? 1.0026 0.7412 0.8309 -0.1822 -0.0204 -0.0795 701 THR A CB  
3237 O OG1 . THR A 405 ? 1.0103 0.7578 0.8515 -0.1566 -0.0227 -0.0818 701 THR A OG1 
3238 C CG2 . THR A 405 ? 1.0236 0.7067 0.7855 -0.2279 -0.0176 -0.0863 701 THR A CG2 
3239 N N   . PRO A 406 ? 0.8890 0.8158 0.8337 -0.2049 -0.0256 -0.0866 702 PRO A N   
3240 C CA  . PRO A 406 ? 0.8481 0.7801 0.8195 -0.1644 -0.0282 -0.0825 702 PRO A CA  
3241 C C   . PRO A 406 ? 0.8150 0.7745 0.8262 -0.1382 -0.0293 -0.0740 702 PRO A C   
3242 O O   . PRO A 406 ? 0.7844 0.7781 0.8158 -0.1471 -0.0290 -0.0722 702 PRO A O   
3243 C CB  . PRO A 406 ? 0.7768 0.7640 0.7765 -0.1671 -0.0314 -0.0868 702 PRO A CB  
3244 C CG  . PRO A 406 ? 0.8126 0.7974 0.7811 -0.2074 -0.0308 -0.0952 702 PRO A CG  
3245 C CD  . PRO A 406 ? 0.8152 0.7852 0.7627 -0.2341 -0.0272 -0.0944 702 PRO A CD  
3246 N N   . SER A 407 ? 0.7813 0.7296 0.8011 -0.1074 -0.0306 -0.0694 703 SER A N   
3247 C CA  . SER A 407 ? 0.7919 0.7572 0.8388 -0.0877 -0.0322 -0.0616 703 SER A CA  
3248 C C   . SER A 407 ? 0.7073 0.6905 0.7753 -0.0622 -0.0344 -0.0576 703 SER A C   
3249 O O   . SER A 407 ? 0.6715 0.6424 0.7263 -0.0530 -0.0335 -0.0602 703 SER A O   
3250 C CB  . SER A 407 ? 0.7785 0.6973 0.7959 -0.0833 -0.0306 -0.0584 703 SER A CB  
3251 O OG  . SER A 407 ? 0.9519 0.8339 0.9435 -0.0598 -0.0304 -0.0576 703 SER A OG  
3252 N N   . PHE A 408 ? 0.6460 0.6575 0.7428 -0.0531 -0.0371 -0.0513 704 PHE A N   
3253 C CA  . PHE A 408 ? 0.6221 0.6517 0.7353 -0.0352 -0.0390 -0.0458 704 PHE A CA  
3254 C C   . PHE A 408 ? 0.6462 0.6610 0.7501 -0.0217 -0.0395 -0.0414 704 PHE A C   
3255 O O   . PHE A 408 ? 0.6184 0.6252 0.7213 -0.0265 -0.0406 -0.0392 704 PHE A O   
3256 C CB  . PHE A 408 ? 0.4990 0.5610 0.6384 -0.0377 -0.0425 -0.0417 704 PHE A CB  
3257 C CG  . PHE A 408 ? 0.5896 0.6688 0.7353 -0.0433 -0.0431 -0.0451 704 PHE A CG  
3258 C CD1 . PHE A 408 ? 0.5290 0.6212 0.6786 -0.0512 -0.0441 -0.0479 704 PHE A CD1 
3259 C CD2 . PHE A 408 ? 0.6049 0.6925 0.7514 -0.0382 -0.0426 -0.0454 704 PHE A CD2 
3260 C CE1 . PHE A 408 ? 0.6162 0.7301 0.7698 -0.0517 -0.0457 -0.0512 704 PHE A CE1 
3261 C CE2 . PHE A 408 ? 0.5476 0.6499 0.6967 -0.0415 -0.0439 -0.0483 704 PHE A CE2 
3262 C CZ  . PHE A 408 ? 0.6089 0.7246 0.7614 -0.0471 -0.0460 -0.0511 704 PHE A CZ  
3263 N N   . GLU A 409 ? 0.5668 0.5823 0.6626 -0.0024 -0.0387 -0.0403 705 GLU A N   
3264 C CA  . GLU A 409 ? 0.6852 0.6974 0.7718 0.0169  -0.0401 -0.0361 705 GLU A CA  
3265 C C   . GLU A 409 ? 0.7193 0.7850 0.8327 0.0270  -0.0424 -0.0307 705 GLU A C   
3266 O O   . GLU A 409 ? 0.6195 0.7131 0.7493 0.0212  -0.0415 -0.0306 705 GLU A O   
3267 C CB  . GLU A 409 ? 0.6728 0.6383 0.7150 0.0364  -0.0371 -0.0400 705 GLU A CB  
3268 C CG  . GLU A 409 ? 0.8451 0.7514 0.8504 0.0179  -0.0345 -0.0457 705 GLU A CG  
3269 C CD  . GLU A 409 ? 1.0006 0.8842 0.9962 0.0056  -0.0354 -0.0431 705 GLU A CD  
3270 O OE1 . GLU A 409 ? 0.9046 0.8124 0.9194 0.0153  -0.0387 -0.0371 705 GLU A OE1 
3271 O OE2 . GLU A 409 ? 1.0823 0.9253 1.0486 -0.0166 -0.0327 -0.0472 705 GLU A OE2 
3272 N N   . TYR A 410 ? 0.5687 0.6510 0.6845 0.0390  -0.0455 -0.0259 706 TYR A N   
3273 C CA  . TYR A 410 ? 0.5258 0.6673 0.6622 0.0476  -0.0476 -0.0211 706 TYR A CA  
3274 C C   . TYR A 410 ? 0.6276 0.7792 0.7469 0.0793  -0.0441 -0.0233 706 TYR A C   
3275 O O   . TYR A 410 ? 0.7281 0.8285 0.8114 0.0979  -0.0415 -0.0278 706 TYR A O   
3276 C CB  . TYR A 410 ? 0.6669 0.8316 0.8122 0.0469  -0.0534 -0.0155 706 TYR A CB  
3277 C CG  . TYR A 410 ? 0.6404 0.8092 0.8028 0.0168  -0.0572 -0.0126 706 TYR A CG  
3278 C CD1 . TYR A 410 ? 0.8010 0.9334 0.9555 0.0078  -0.0591 -0.0129 706 TYR A CD1 
3279 C CD2 . TYR A 410 ? 0.7923 0.9961 0.9714 -0.0022 -0.0584 -0.0095 706 TYR A CD2 
3280 C CE1 . TYR A 410 ? 0.8094 0.9404 0.9718 -0.0141 -0.0624 -0.0109 706 TYR A CE1 
3281 C CE2 . TYR A 410 ? 0.8561 1.0490 1.0371 -0.0266 -0.0622 -0.0071 706 TYR A CE2 
3282 C CZ  . TYR A 410 ? 0.8360 0.9924 1.0085 -0.0301 -0.0643 -0.0081 706 TYR A CZ  
3283 O OH  . TYR A 410 ? 0.6846 0.8255 0.8517 -0.0493 -0.0679 -0.0064 706 TYR A OH  
3284 N N   . GLN A 411 ? 0.5599 0.7767 0.6997 0.0852  -0.0438 -0.0201 707 GLN A N   
3285 C CA  . GLN A 411 ? 0.5635 0.8037 0.6890 0.1199  -0.0399 -0.0222 707 GLN A CA  
3286 C C   . GLN A 411 ? 0.6174 0.9501 0.7711 0.1237  -0.0419 -0.0163 707 GLN A C   
3287 O O   . GLN A 411 ? 0.7129 1.0822 0.8943 0.0897  -0.0447 -0.0115 707 GLN A O   
3288 C CB  . GLN A 411 ? 0.6002 0.8241 0.7178 0.1183  -0.0339 -0.0274 707 GLN A CB  
3289 C CG  . GLN A 411 ? 0.6392 0.9049 0.7889 0.0871  -0.0333 -0.0241 707 GLN A CG  
3290 C CD  . GLN A 411 ? 0.7550 1.0059 0.8961 0.0861  -0.0279 -0.0289 707 GLN A CD  
3291 O OE1 . GLN A 411 ? 0.7526 0.9816 0.8664 0.1132  -0.0237 -0.0346 707 GLN A OE1 
3292 N NE2 . GLN A 411 ? 0.7507 1.0087 0.9090 0.0563  -0.0284 -0.0268 707 GLN A NE2 
3293 N N   . PRO A 412 ? 0.7208 1.0929 0.8633 0.1639  -0.0407 -0.0166 708 PRO A N   
3294 C CA  . PRO A 412 ? 0.7943 1.2732 0.9660 0.1663  -0.0424 -0.0112 708 PRO A CA  
3295 C C   . PRO A 412 ? 0.7653 1.2950 0.9643 0.1326  -0.0385 -0.0089 708 PRO A C   
3296 O O   . PRO A 412 ? 0.8302 1.3245 1.0213 0.1273  -0.0329 -0.0125 708 PRO A O   
3297 C CB  . PRO A 412 ? 0.8964 1.4016 1.0432 0.2248  -0.0395 -0.0142 708 PRO A CB  
3298 C CG  . PRO A 412 ? 0.9227 1.3212 1.0208 0.2506  -0.0403 -0.0189 708 PRO A CG  
3299 C CD  . PRO A 412 ? 0.8274 1.1455 0.9230 0.2100  -0.0387 -0.0217 708 PRO A CD  
3300 N N   . ASP A 413 ? 0.7539 1.3641 0.9804 0.1064  -0.0420 -0.0025 709 ASP A N   
3301 C CA  . ASP A 413 ? 0.8035 1.4676 1.0483 0.0732  -0.0379 0.0009  709 ASP A CA  
3302 C C   . ASP A 413 ? 0.8333 1.5534 1.0766 0.1073  -0.0295 -0.0019 709 ASP A C   
3303 O O   . ASP A 413 ? 0.8464 1.6144 1.0849 0.1523  -0.0291 -0.0035 709 ASP A O   
3304 C CB  . ASP A 413 ? 0.9032 1.6442 1.1692 0.0351  -0.0436 0.0082  709 ASP A CB  
3305 C CG  . ASP A 413 ? 0.8939 1.5721 1.1548 -0.0036 -0.0511 0.0107  709 ASP A CG  
3306 O OD1 . ASP A 413 ? 0.8698 1.4593 1.1170 -0.0113 -0.0502 0.0079  709 ASP A OD1 
3307 O OD2 . ASP A 413 ? 0.8503 1.5713 1.1191 -0.0253 -0.0581 0.0150  709 ASP A OD2 
3308 N N   . PRO A 414 ? 0.8302 1.5453 1.0734 0.0910  -0.0228 -0.0025 710 PRO A N   
3309 C CA  . PRO A 414 ? 0.8837 1.6344 1.1183 0.1287  -0.0139 -0.0068 710 PRO A CA  
3310 C C   . PRO A 414 ? 0.8482 1.7287 1.1012 0.1463  -0.0110 -0.0036 710 PRO A C   
3311 O O   . PRO A 414 ? 0.9447 1.8564 1.1843 0.1982  -0.0053 -0.0082 710 PRO A O   
3312 C CB  . PRO A 414 ? 0.8036 1.5275 1.0373 0.0962  -0.0085 -0.0065 710 PRO A CB  
3313 C CG  . PRO A 414 ? 0.8152 1.4634 1.0480 0.0546  -0.0151 -0.0042 710 PRO A CG  
3314 C CD  . PRO A 414 ? 0.8480 1.5197 1.0928 0.0414  -0.0232 0.0003  710 PRO A CD  
3315 N N   . TRP A 415 ? 0.6739 1.6331 0.9533 0.1050  -0.0149 0.0039  711 TRP A N   
3316 C CA  . TRP A 415 ? 0.7475 1.7948 1.0209 0.1094  -0.0109 0.0068  711 TRP A CA  
3317 C C   . TRP A 415 ? 0.7542 1.8237 1.0141 0.1572  -0.0149 0.0047  711 TRP A C   
3318 O O   . TRP A 415 ? 0.6915 1.8360 0.9408 0.1746  -0.0113 0.0054  711 TRP A O   
3319 C CB  . TRP A 415 ? 0.7731 1.8605 1.0542 0.0419  -0.0130 0.0149  711 TRP A CB  
3320 C CG  . TRP A 415 ? 0.7928 1.8396 1.0798 0.0074  -0.0234 0.0181  711 TRP A CG  
3321 C CD1 . TRP A 415 ? 0.8120 1.8831 1.0981 0.0100  -0.0304 0.0197  711 TRP A CD1 
3322 C CD2 . TRP A 415 ? 0.7971 1.7709 1.0873 -0.0339 -0.0284 0.0199  711 TRP A CD2 
3323 N NE1 . TRP A 415 ? 0.7169 1.7328 1.0057 -0.0273 -0.0393 0.0221  711 TRP A NE1 
3324 C CE2 . TRP A 415 ? 0.7273 1.6818 1.0168 -0.0539 -0.0384 0.0223  711 TRP A CE2 
3325 C CE3 . TRP A 415 ? 0.8263 1.7453 1.1143 -0.0542 -0.0255 0.0196  711 TRP A CE3 
3326 C CZ2 . TRP A 415 ? 0.6986 1.5816 0.9839 -0.0921 -0.0456 0.0241  711 TRP A CZ2 
3327 C CZ3 . TRP A 415 ? 0.7578 1.5822 1.0291 -0.0889 -0.0315 0.0212  711 TRP A CZ3 
3328 C CH2 . TRP A 415 ? 0.8050 1.6134 1.0752 -0.1065 -0.0412 0.0233  711 TRP A CH2 
3329 N N   . ASN A 416 ? 0.8157 1.8237 1.0719 0.1793  -0.0225 0.0023  712 ASN A N   
3330 C CA  . ASN A 416 ? 0.9271 1.9411 1.1612 0.2304  -0.0261 0.0002  712 ASN A CA  
3331 C C   . ASN A 416 ? 0.9336 1.8976 1.1303 0.2977  -0.0213 -0.0072 712 ASN A C   
3332 O O   . ASN A 416 ? 1.0315 1.9956 1.1960 0.3465  -0.0230 -0.0092 712 ASN A O   
3333 C CB  . ASN A 416 ? 0.9485 1.9154 1.1883 0.2213  -0.0371 0.0019  712 ASN A CB  
3334 C CG  . ASN A 416 ? 0.9447 1.9394 1.2111 0.1537  -0.0426 0.0084  712 ASN A CG  
3335 O OD1 . ASN A 416 ? 0.9750 2.0407 1.2475 0.1214  -0.0394 0.0123  712 ASN A OD1 
3336 N ND2 . ASN A 416 ? 0.9211 1.8550 1.1965 0.1316  -0.0512 0.0093  712 ASN A ND2 
3337 N N   . THR A 417 ? 0.7336 1.6495 0.9266 0.3011  -0.0154 -0.0116 713 THR A N   
3338 C CA  . THR A 417 ? 0.8784 1.7196 1.0261 0.3594  -0.0113 -0.0197 713 THR A CA  
3339 C C   . THR A 417 ? 0.9611 1.8202 1.0965 0.3726  -0.0008 -0.0236 713 THR A C   
3340 O O   . THR A 417 ? 1.1291 1.9335 1.2147 0.4248  0.0030  -0.0305 713 THR A O   
3341 C CB  . THR A 417 ? 0.8971 1.6056 1.0254 0.3444  -0.0147 -0.0232 713 THR A CB  
3342 O OG1 . THR A 417 ? 0.7908 1.4925 0.9555 0.2757  -0.0170 -0.0186 713 THR A OG1 
3343 C CG2 . THR A 417 ? 0.9485 1.5970 1.0475 0.3701  -0.0225 -0.0233 713 THR A CG2 
3344 N N   . HIS A 418 ? 0.9468 1.8729 1.1180 0.3261  0.0037  -0.0193 714 HIS A N   
3345 C CA  . HIS A 418 ? 0.8608 1.8011 1.0240 0.3320  0.0137  -0.0225 714 HIS A CA  
3346 C C   . HIS A 418 ? 1.0366 2.0443 1.1725 0.3706  0.0177  -0.0228 714 HIS A C   
3347 O O   . HIS A 418 ? 0.9921 2.0950 1.1463 0.3474  0.0169  -0.0164 714 HIS A O   
3348 C CB  . HIS A 418 ? 0.8070 1.7894 1.0112 0.2654  0.0164  -0.0165 714 HIS A CB  
3349 C CG  . HIS A 418 ? 0.8194 1.8220 1.0175 0.2656  0.0268  -0.0187 714 HIS A CG  
3350 N ND1 . HIS A 418 ? 0.8765 1.8215 1.0418 0.3118  0.0331  -0.0280 714 HIS A ND1 
3351 C CD2 . HIS A 418 ? 0.8283 1.8958 1.0430 0.2235  0.0320  -0.0129 714 HIS A CD2 
3352 C CE1 . HIS A 418 ? 0.8985 1.8787 1.0655 0.2999  0.0419  -0.0278 714 HIS A CE1 
3353 N NE2 . HIS A 418 ? 0.8226 1.8782 1.0200 0.2465  0.0414  -0.0183 714 HIS A NE2 
3354 N N   . VAL A 419 ? 1.2044 2.1604 1.2907 0.4287  0.0214  -0.0303 715 VAL A N   
3355 C CA  . VAL A 419 ? 1.2530 2.2703 1.3088 0.4683  0.0251  -0.0309 715 VAL A CA  
3356 C C   . VAL A 419 ? 1.2791 2.3744 1.3660 0.4297  0.0324  -0.0274 715 VAL A C   
3357 O O   . VAL A 419 ? 1.2265 2.2863 1.3026 0.4349  0.0394  -0.0320 715 VAL A O   
3358 C CB  . VAL A 419 ? 1.2368 2.1633 1.2231 0.5347  0.0269  -0.0396 715 VAL A CB  
3359 C CG1 . VAL A 419 ? 1.2508 2.2458 1.2068 0.5740  0.0302  -0.0396 715 VAL A CG1 
3360 C CG2 . VAL A 419 ? 1.1872 2.0357 1.1309 0.5721  0.0191  -0.0417 715 VAL A CG2 
3361 N N   . TRP A 420 ? 1.3546 2.5511 1.4753 0.3878  0.0309  -0.0194 716 TRP A N   
3362 C CA  . TRP A 420 ? 1.3979 2.6653 1.5455 0.3389  0.0365  -0.0143 716 TRP A CA  
3363 C C   . TRP A 420 ? 1.5957 2.9392 1.7191 0.3739  0.0411  -0.0151 716 TRP A C   
3364 O O   . TRP A 420 ? 1.6489 3.0231 1.7421 0.4257  0.0378  -0.0170 716 TRP A O   
3365 C CB  . TRP A 420 ? 1.3462 2.6771 1.5280 0.2755  0.0319  -0.0055 716 TRP A CB  
3366 C CG  . TRP A 420 ? 1.3266 2.6530 1.5346 0.2071  0.0350  -0.0003 716 TRP A CG  
3367 C CD1 . TRP A 420 ? 1.3551 2.6715 1.5621 0.1959  0.0431  -0.0012 716 TRP A CD1 
3368 C CD2 . TRP A 420 ? 1.2688 2.5918 1.4996 0.1413  0.0299  0.0068  716 TRP A CD2 
3369 N NE1 . TRP A 420 ? 1.3219 2.6289 1.5480 0.1274  0.0433  0.0054  716 TRP A NE1 
3370 C CE2 . TRP A 420 ? 1.2411 2.5480 1.4792 0.0930  0.0349  0.0103  716 TRP A CE2 
3371 C CE3 . TRP A 420 ? 1.2439 2.5710 1.4839 0.1191  0.0213  0.0104  716 TRP A CE3 
3372 C CZ2 . TRP A 420 ? 1.1827 2.4698 1.4305 0.0249  0.0310  0.0175  716 TRP A CZ2 
3373 C CZ3 . TRP A 420 ? 1.2493 2.5589 1.5017 0.0510  0.0176  0.0171  716 TRP A CZ3 
3374 C CH2 . TRP A 420 ? 1.2117 2.4979 1.4647 0.0051  0.0221  0.0206  716 TRP A CH2 
# 
