data_9CVI
# 
_entry.id   9CVI 
# 
_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   9CVI         pdb_00009cvi 10.2210/pdb9cvi/pdb 
WWPDB D_1000286172 ?            ?                   
# 
_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                        9CVI 
_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           Y 
# 
_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'                              48735.438 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 '4-methyl-6-{3-[(methylamino)methyl]phenyl}pyridin-2-amine' 227.305   1  ?          ?     ? ? 
5 non-polymer syn 'ACETATE ION'                                               59.044    1  ?          ?     ? ? 
6 non-polymer syn 'ZINC ION'                                                  65.409    1  ?          ?     ? ? 
7 water       nat water                                                       18.015    30 ?          ?     ? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        'BNOS,Constitutive NOS,NC-NOS,NOS type I,Neuronal NOS,N-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
DMRKTSSLWKDQALVEINIAVLYSFQSDKVTIVDHHSATESFIKHMENEYRCRGGCPADWVWIVPPMSGSITPVFFQEML
NYRLTPSFEYQPDPWNTHVWKG
;
_entity_poly.pdbx_seq_one_letter_code_can   
;CPRFLKVKNWETDVVLTDTLHLKSTLETGCTEHICMGSIMLPSQHTRKPEDVATKDQLFPLAKEFLDQYYSSIKRFGSKA
HMDRLEEVNKEIESTSTYQLKDTELIYGAKHAWRNASRCVGRIQWSKLQVFDARDCTTAHGMFNYICNHVKYATNKGNLR
SAITIFPQRTDGKHDFRVWNSQLIRYAGYKQPDGSTLGDPANVQFTEICIQQGWKAPRGRFDVLPLLLQANGNDPELFQI
PPELVLEVPIRHPKFDWFKDLGLKWYGLPAVSNMLLEIGGLEFSACPFSGWYMGTEIGVRDYCDNSRYNILEEVAKKMDL
DMRKTSSLWKDQALVEINIAVLYSFQSDKVTIVDHHSATESFIKHMENEYRCRGGCPADWVWIVPPMSGSITPVFFQEML
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 '4-methyl-6-{3-[(methylamino)methyl]phenyl}pyridin-2-amine' KMI 
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 PHE 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 
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 
KMI non-polymer         . '4-methyl-6-{3-[(methylamino)methyl]phenyl}pyridin-2-amine' ?    'C14 H17 N3'       227.305 
LEU 'L-peptide linking' y LEUCINE                                                     ?    'C6 H13 N O2'      131.173 
LYS 'L-peptide linking' y LYSINE                                                      ?    'C6 H15 N2 O2 1'   147.195 
MET 'L-peptide linking' y METHIONINE                                                  ?    'C5 H11 N O2 S'    149.211 
PHE 'L-peptide linking' y PHENYLALANINE                                               ?    'C9 H11 N O2'      165.189 
PRO 'L-peptide linking' y PROLINE                                                     ?    'C5 H9 N O2'       115.130 
SER 'L-peptide linking' y SERINE                                                      ?    'C3 H7 N O3'       105.093 
THR 'L-peptide linking' y THREONINE                                                   ?    'C4 H9 N O3'       119.119 
TRP 'L-peptide linking' y TRYPTOPHAN                                                  ?    'C11 H12 N2 O2'    204.225 
TYR 'L-peptide linking' y TYROSINE                                                    ?    'C9 H11 N O3'      181.189 
VAL 'L-peptide linking' y VALINE                                                      ?    'C5 H11 N O2'      117.146 
ZN  non-polymer         . 'ZINC ION'                                                  ?    'Zn 2'             65.409  
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   CYS 1   297 ?   ?   ?   A . n 
A 1 2   PRO 2   298 ?   ?   ?   A . n 
A 1 3   ARG 3   299 299 ARG ARG A . n 
A 1 4   PHE 4   300 300 PHE PHE A . n 
A 1 5   LEU 5   301 301 LEU LEU A . n 
A 1 6   LYS 6   302 302 LYS LYS A . n 
A 1 7   VAL 7   303 303 VAL VAL A . n 
A 1 8   LYS 8   304 304 LYS LYS A . n 
A 1 9   ASN 9   305 305 ASN ASN A . n 
A 1 10  TRP 10  306 306 TRP TRP A . n 
A 1 11  GLU 11  307 307 GLU GLU A . n 
A 1 12  THR 12  308 308 THR THR A . n 
A 1 13  ASP 13  309 309 ASP ASP A . n 
A 1 14  VAL 14  310 310 VAL VAL A . n 
A 1 15  VAL 15  311 311 VAL VAL A . n 
A 1 16  LEU 16  312 312 LEU LEU A . n 
A 1 17  THR 17  313 313 THR THR A . n 
A 1 18  ASP 18  314 314 ASP ASP A . n 
A 1 19  THR 19  315 315 THR THR A . n 
A 1 20  LEU 20  316 316 LEU LEU A . n 
A 1 21  HIS 21  317 317 HIS HIS A . n 
A 1 22  LEU 22  318 318 LEU LEU A . n 
A 1 23  LYS 23  319 319 LYS LYS A . n 
A 1 24  SER 24  320 320 SER SER A . n 
A 1 25  THR 25  321 321 THR THR A . n 
A 1 26  LEU 26  322 322 LEU LEU A . n 
A 1 27  GLU 27  323 323 GLU GLU A . n 
A 1 28  THR 28  324 324 THR THR A . n 
A 1 29  GLY 29  325 325 GLY GLY A . n 
A 1 30  CYS 30  326 326 CYS CYS A . n 
A 1 31  THR 31  327 327 THR THR A . n 
A 1 32  GLU 32  328 328 GLU GLU A . n 
A 1 33  HIS 33  329 329 HIS HIS A . n 
A 1 34  ILE 34  330 330 ILE ILE A . n 
A 1 35  CYS 35  331 331 CYS CYS A . n 
A 1 36  MET 36  332 332 MET MET A . n 
A 1 37  GLY 37  333 333 GLY GLY A . n 
A 1 38  SER 38  334 334 SER SER A . n 
A 1 39  ILE 39  335 335 ILE ILE A . n 
A 1 40  MET 40  336 336 MET MET A . n 
A 1 41  LEU 41  337 337 LEU LEU A . n 
A 1 42  PRO 42  338 338 PRO PRO A . n 
A 1 43  SER 43  339 339 SER SER A . n 
A 1 44  GLN 44  340 ?   ?   ?   A . n 
A 1 45  HIS 45  341 ?   ?   ?   A . n 
A 1 46  THR 46  342 ?   ?   ?   A . n 
A 1 47  ARG 47  343 ?   ?   ?   A . n 
A 1 48  LYS 48  344 ?   ?   ?   A . n 
A 1 49  PRO 49  345 ?   ?   ?   A . n 
A 1 50  GLU 50  346 ?   ?   ?   A . n 
A 1 51  ASP 51  347 ?   ?   ?   A . n 
A 1 52  VAL 52  348 348 VAL VAL A . n 
A 1 53  ALA 53  349 349 ALA ALA A . n 
A 1 54  THR 54  350 350 THR THR A . n 
A 1 55  LYS 55  351 351 LYS LYS A . n 
A 1 56  ASP 56  352 352 ASP ASP A . n 
A 1 57  GLN 57  353 353 GLN GLN A . n 
A 1 58  LEU 58  354 354 LEU LEU A . n 
A 1 59  PHE 59  355 355 PHE PHE A . n 
A 1 60  PRO 60  356 356 PRO PRO A . n 
A 1 61  LEU 61  357 357 LEU LEU A . n 
A 1 62  ALA 62  358 358 ALA ALA A . n 
A 1 63  LYS 63  359 359 LYS LYS A . n 
A 1 64  GLU 64  360 360 GLU GLU A . n 
A 1 65  PHE 65  361 361 PHE PHE A . n 
A 1 66  LEU 66  362 362 LEU LEU A . n 
A 1 67  ASP 67  363 363 ASP ASP A . n 
A 1 68  GLN 68  364 364 GLN GLN A . n 
A 1 69  TYR 69  365 365 TYR TYR A . n 
A 1 70  TYR 70  366 366 TYR TYR A . n 
A 1 71  SER 71  367 367 SER SER A . n 
A 1 72  SER 72  368 368 SER SER A . n 
A 1 73  ILE 73  369 369 ILE ILE A . n 
A 1 74  LYS 74  370 370 LYS LYS A . n 
A 1 75  ARG 75  371 371 ARG ARG A . n 
A 1 76  PHE 76  372 372 PHE PHE A . n 
A 1 77  GLY 77  373 373 GLY GLY A . n 
A 1 78  SER 78  374 374 SER SER A . n 
A 1 79  LYS 79  375 375 LYS LYS A . n 
A 1 80  ALA 80  376 376 ALA ALA A . n 
A 1 81  HIS 81  377 377 HIS HIS A . n 
A 1 82  MET 82  378 378 MET MET A . n 
A 1 83  ASP 83  379 379 ASP ASP A . n 
A 1 84  ARG 84  380 380 ARG ARG A . n 
A 1 85  LEU 85  381 381 LEU LEU A . n 
A 1 86  GLU 86  382 382 GLU GLU A . n 
A 1 87  GLU 87  383 383 GLU GLU A . n 
A 1 88  VAL 88  384 384 VAL VAL A . n 
A 1 89  ASN 89  385 385 ASN ASN A . n 
A 1 90  LYS 90  386 386 LYS LYS A . n 
A 1 91  GLU 91  387 387 GLU GLU A . n 
A 1 92  ILE 92  388 388 ILE ILE A . n 
A 1 93  GLU 93  389 389 GLU GLU A . n 
A 1 94  SER 94  390 390 SER SER A . n 
A 1 95  THR 95  391 391 THR THR A . n 
A 1 96  SER 96  392 392 SER SER A . n 
A 1 97  THR 97  393 393 THR THR A . n 
A 1 98  TYR 98  394 394 TYR TYR A . n 
A 1 99  GLN 99  395 395 GLN GLN A . n 
A 1 100 LEU 100 396 396 LEU LEU A . n 
A 1 101 LYS 101 397 397 LYS LYS A . n 
A 1 102 ASP 102 398 398 ASP ASP A . n 
A 1 103 THR 103 399 399 THR THR A . n 
A 1 104 GLU 104 400 400 GLU GLU A . n 
A 1 105 LEU 105 401 401 LEU LEU A . n 
A 1 106 ILE 106 402 402 ILE ILE A . n 
A 1 107 TYR 107 403 403 TYR TYR A . n 
A 1 108 GLY 108 404 404 GLY GLY A . n 
A 1 109 ALA 109 405 405 ALA ALA A . n 
A 1 110 LYS 110 406 406 LYS LYS A . n 
A 1 111 HIS 111 407 407 HIS HIS A . n 
A 1 112 ALA 112 408 408 ALA ALA A . n 
A 1 113 TRP 113 409 409 TRP TRP A . n 
A 1 114 ARG 114 410 410 ARG ARG A . n 
A 1 115 ASN 115 411 411 ASN ASN A . n 
A 1 116 ALA 116 412 412 ALA ALA A . n 
A 1 117 SER 117 413 413 SER SER A . n 
A 1 118 ARG 118 414 414 ARG ARG A . n 
A 1 119 CYS 119 415 415 CYS CYS A . n 
A 1 120 VAL 120 416 416 VAL VAL A . n 
A 1 121 GLY 121 417 417 GLY GLY A . n 
A 1 122 ARG 122 418 418 ARG ARG A . n 
A 1 123 ILE 123 419 419 ILE ILE A . n 
A 1 124 GLN 124 420 420 GLN GLN A . n 
A 1 125 TRP 125 421 421 TRP TRP A . n 
A 1 126 SER 126 422 422 SER SER A . n 
A 1 127 LYS 127 423 423 LYS LYS A . n 
A 1 128 LEU 128 424 424 LEU LEU A . n 
A 1 129 GLN 129 425 425 GLN GLN A . n 
A 1 130 VAL 130 426 426 VAL VAL A . n 
A 1 131 PHE 131 427 427 PHE PHE A . n 
A 1 132 ASP 132 428 428 ASP ASP A . n 
A 1 133 ALA 133 429 429 ALA ALA A . n 
A 1 134 ARG 134 430 430 ARG ARG A . n 
A 1 135 ASP 135 431 431 ASP ASP A . n 
A 1 136 CYS 136 432 432 CYS CYS A . n 
A 1 137 THR 137 433 433 THR THR A . n 
A 1 138 THR 138 434 434 THR THR A . n 
A 1 139 ALA 139 435 435 ALA ALA A . n 
A 1 140 HIS 140 436 436 HIS HIS A . n 
A 1 141 GLY 141 437 437 GLY GLY A . n 
A 1 142 MET 142 438 438 MET MET A . n 
A 1 143 PHE 143 439 439 PHE PHE A . n 
A 1 144 ASN 144 440 440 ASN ASN A . n 
A 1 145 TYR 145 441 441 TYR TYR A . n 
A 1 146 ILE 146 442 442 ILE ILE A . n 
A 1 147 CYS 147 443 443 CYS CYS A . n 
A 1 148 ASN 148 444 444 ASN ASN A . n 
A 1 149 HIS 149 445 445 HIS HIS A . n 
A 1 150 VAL 150 446 446 VAL VAL A . n 
A 1 151 LYS 151 447 447 LYS LYS A . n 
A 1 152 TYR 152 448 448 TYR TYR A . n 
A 1 153 ALA 153 449 449 ALA ALA A . n 
A 1 154 THR 154 450 450 THR THR A . n 
A 1 155 ASN 155 451 451 ASN ASN A . n 
A 1 156 LYS 156 452 452 LYS LYS A . n 
A 1 157 GLY 157 453 453 GLY GLY A . n 
A 1 158 ASN 158 454 454 ASN ASN A . n 
A 1 159 LEU 159 455 455 LEU LEU A . n 
A 1 160 ARG 160 456 456 ARG ARG A . n 
A 1 161 SER 161 457 457 SER SER A . n 
A 1 162 ALA 162 458 458 ALA ALA A . n 
A 1 163 ILE 163 459 459 ILE ILE A . n 
A 1 164 THR 164 460 460 THR THR A . n 
A 1 165 ILE 165 461 461 ILE ILE A . n 
A 1 166 PHE 166 462 462 PHE PHE A . n 
A 1 167 PRO 167 463 463 PRO PRO A . n 
A 1 168 GLN 168 464 464 GLN GLN A . n 
A 1 169 ARG 169 465 465 ARG ARG A . n 
A 1 170 THR 170 466 466 THR THR A . n 
A 1 171 ASP 171 467 467 ASP ASP A . n 
A 1 172 GLY 172 468 468 GLY GLY A . n 
A 1 173 LYS 173 469 469 LYS LYS A . n 
A 1 174 HIS 174 470 470 HIS HIS A . n 
A 1 175 ASP 175 471 471 ASP ASP A . n 
A 1 176 PHE 176 472 472 PHE PHE A . n 
A 1 177 ARG 177 473 473 ARG ARG A . n 
A 1 178 VAL 178 474 474 VAL VAL A . n 
A 1 179 TRP 179 475 475 TRP TRP A . n 
A 1 180 ASN 180 476 476 ASN ASN A . n 
A 1 181 SER 181 477 477 SER SER A . n 
A 1 182 GLN 182 478 478 GLN GLN A . n 
A 1 183 LEU 183 479 479 LEU LEU A . n 
A 1 184 ILE 184 480 480 ILE ILE A . n 
A 1 185 ARG 185 481 481 ARG ARG A . n 
A 1 186 TYR 186 482 482 TYR TYR A . n 
A 1 187 ALA 187 483 483 ALA ALA A . n 
A 1 188 GLY 188 484 484 GLY GLY A . n 
A 1 189 TYR 189 485 485 TYR TYR A . n 
A 1 190 LYS 190 486 486 LYS LYS A . n 
A 1 191 GLN 191 487 487 GLN GLN A . n 
A 1 192 PRO 192 488 488 PRO PRO A . n 
A 1 193 ASP 193 489 489 ASP ASP A . n 
A 1 194 GLY 194 490 490 GLY GLY A . n 
A 1 195 SER 195 491 491 SER SER A . n 
A 1 196 THR 196 492 492 THR THR A . n 
A 1 197 LEU 197 493 493 LEU LEU A . n 
A 1 198 GLY 198 494 494 GLY GLY A . n 
A 1 199 ASP 199 495 495 ASP ASP A . n 
A 1 200 PRO 200 496 496 PRO PRO A . n 
A 1 201 ALA 201 497 497 ALA ALA A . n 
A 1 202 ASN 202 498 498 ASN ASN A . n 
A 1 203 VAL 203 499 499 VAL VAL A . n 
A 1 204 GLN 204 500 500 GLN GLN A . n 
A 1 205 PHE 205 501 501 PHE PHE A . n 
A 1 206 THR 206 502 502 THR THR A . n 
A 1 207 GLU 207 503 503 GLU GLU A . n 
A 1 208 ILE 208 504 504 ILE ILE A . n 
A 1 209 CYS 209 505 505 CYS CYS A . n 
A 1 210 ILE 210 506 506 ILE ILE A . n 
A 1 211 GLN 211 507 507 GLN GLN A . n 
A 1 212 GLN 212 508 508 GLN GLN A . n 
A 1 213 GLY 213 509 509 GLY GLY A . n 
A 1 214 TRP 214 510 510 TRP TRP A . n 
A 1 215 LYS 215 511 511 LYS LYS A . n 
A 1 216 ALA 216 512 512 ALA ALA A . n 
A 1 217 PRO 217 513 513 PRO PRO A . n 
A 1 218 ARG 218 514 514 ARG ARG A . n 
A 1 219 GLY 219 515 515 GLY GLY A . n 
A 1 220 ARG 220 516 516 ARG ARG A . n 
A 1 221 PHE 221 517 517 PHE PHE A . n 
A 1 222 ASP 222 518 518 ASP ASP A . n 
A 1 223 VAL 223 519 519 VAL VAL A . n 
A 1 224 LEU 224 520 520 LEU LEU A . n 
A 1 225 PRO 225 521 521 PRO PRO A . n 
A 1 226 LEU 226 522 522 LEU LEU A . n 
A 1 227 LEU 227 523 523 LEU LEU A . n 
A 1 228 LEU 228 524 524 LEU LEU A . n 
A 1 229 GLN 229 525 525 GLN GLN A . n 
A 1 230 ALA 230 526 526 ALA ALA A . n 
A 1 231 ASN 231 527 527 ASN ASN A . n 
A 1 232 GLY 232 528 528 GLY GLY A . n 
A 1 233 ASN 233 529 529 ASN ASN A . n 
A 1 234 ASP 234 530 530 ASP ASP A . n 
A 1 235 PRO 235 531 531 PRO PRO A . n 
A 1 236 GLU 236 532 532 GLU GLU A . n 
A 1 237 LEU 237 533 533 LEU LEU A . n 
A 1 238 PHE 238 534 534 PHE PHE A . n 
A 1 239 GLN 239 535 535 GLN GLN A . n 
A 1 240 ILE 240 536 536 ILE ILE A . n 
A 1 241 PRO 241 537 537 PRO PRO A . n 
A 1 242 PRO 242 538 538 PRO PRO A . n 
A 1 243 GLU 243 539 539 GLU GLU A . n 
A 1 244 LEU 244 540 540 LEU LEU A . n 
A 1 245 VAL 245 541 541 VAL VAL A . n 
A 1 246 LEU 246 542 542 LEU LEU A . n 
A 1 247 GLU 247 543 543 GLU GLU A . n 
A 1 248 VAL 248 544 544 VAL VAL A . n 
A 1 249 PRO 249 545 545 PRO PRO A . n 
A 1 250 ILE 250 546 546 ILE ILE A . n 
A 1 251 ARG 251 547 547 ARG ARG A . n 
A 1 252 HIS 252 548 548 HIS HIS A . n 
A 1 253 PRO 253 549 549 PRO PRO A . n 
A 1 254 LYS 254 550 550 LYS LYS A . n 
A 1 255 PHE 255 551 551 PHE PHE A . n 
A 1 256 ASP 256 552 552 ASP ASP A . n 
A 1 257 TRP 257 553 553 TRP TRP A . n 
A 1 258 PHE 258 554 554 PHE PHE A . n 
A 1 259 LYS 259 555 555 LYS LYS A . n 
A 1 260 ASP 260 556 556 ASP ASP A . n 
A 1 261 LEU 261 557 557 LEU LEU A . n 
A 1 262 GLY 262 558 558 GLY GLY A . n 
A 1 263 LEU 263 559 559 LEU LEU A . n 
A 1 264 LYS 264 560 560 LYS LYS A . n 
A 1 265 TRP 265 561 561 TRP TRP A . n 
A 1 266 TYR 266 562 562 TYR TYR A . n 
A 1 267 GLY 267 563 563 GLY GLY A . n 
A 1 268 LEU 268 564 564 LEU LEU A . n 
A 1 269 PRO 269 565 565 PRO PRO A . n 
A 1 270 ALA 270 566 566 ALA ALA A . n 
A 1 271 VAL 271 567 567 VAL VAL A . n 
A 1 272 SER 272 568 568 SER SER A . n 
A 1 273 ASN 273 569 569 ASN ASN A . n 
A 1 274 MET 274 570 570 MET MET A . n 
A 1 275 LEU 275 571 571 LEU LEU A . n 
A 1 276 LEU 276 572 572 LEU LEU A . n 
A 1 277 GLU 277 573 573 GLU GLU A . n 
A 1 278 ILE 278 574 574 ILE ILE A . n 
A 1 279 GLY 279 575 575 GLY GLY A . n 
A 1 280 GLY 280 576 576 GLY GLY A . n 
A 1 281 LEU 281 577 577 LEU LEU A . n 
A 1 282 GLU 282 578 578 GLU GLU A . n 
A 1 283 PHE 283 579 579 PHE PHE A . n 
A 1 284 SER 284 580 580 SER SER A . n 
A 1 285 ALA 285 581 581 ALA ALA A . n 
A 1 286 CYS 286 582 582 CYS CYS A . n 
A 1 287 PRO 287 583 583 PRO PRO A . n 
A 1 288 PHE 288 584 584 PHE PHE A . n 
A 1 289 SER 289 585 585 SER SER A . n 
A 1 290 GLY 290 586 586 GLY GLY A . n 
A 1 291 TRP 291 587 587 TRP TRP A . n 
A 1 292 TYR 292 588 588 TYR TYR A . n 
A 1 293 MET 293 589 589 MET MET A . n 
A 1 294 GLY 294 590 590 GLY GLY A . n 
A 1 295 THR 295 591 591 THR THR A . n 
A 1 296 GLU 296 592 592 GLU GLU A . n 
A 1 297 ILE 297 593 593 ILE ILE A . n 
A 1 298 GLY 298 594 594 GLY GLY A . n 
A 1 299 VAL 299 595 595 VAL VAL A . n 
A 1 300 ARG 300 596 596 ARG ARG A . n 
A 1 301 ASP 301 597 597 ASP ASP A . n 
A 1 302 TYR 302 598 598 TYR TYR A . n 
A 1 303 CYS 303 599 599 CYS CYS A . n 
A 1 304 ASP 304 600 600 ASP ASP A . n 
A 1 305 ASN 305 601 601 ASN ASN A . n 
A 1 306 SER 306 602 602 SER SER A . n 
A 1 307 ARG 307 603 603 ARG ARG A . n 
A 1 308 TYR 308 604 604 TYR TYR A . n 
A 1 309 ASN 309 605 605 ASN ASN A . n 
A 1 310 ILE 310 606 606 ILE ILE A . n 
A 1 311 LEU 311 607 607 LEU LEU A . n 
A 1 312 GLU 312 608 608 GLU GLU A . n 
A 1 313 GLU 313 609 609 GLU GLU A . n 
A 1 314 VAL 314 610 610 VAL VAL A . n 
A 1 315 ALA 315 611 611 ALA ALA A . n 
A 1 316 LYS 316 612 612 LYS LYS A . n 
A 1 317 LYS 317 613 613 LYS LYS A . n 
A 1 318 MET 318 614 614 MET MET A . n 
A 1 319 ASP 319 615 615 ASP ASP A . n 
A 1 320 LEU 320 616 616 LEU LEU A . n 
A 1 321 ASP 321 617 617 ASP ASP A . n 
A 1 322 MET 322 618 618 MET MET A . n 
A 1 323 ARG 323 619 619 ARG ARG A . n 
A 1 324 LYS 324 620 620 LYS LYS A . n 
A 1 325 THR 325 621 621 THR THR A . n 
A 1 326 SER 326 622 622 SER SER A . n 
A 1 327 SER 327 623 623 SER SER A . n 
A 1 328 LEU 328 624 624 LEU LEU A . n 
A 1 329 TRP 329 625 625 TRP TRP A . n 
A 1 330 LYS 330 626 626 LYS LYS A . n 
A 1 331 ASP 331 627 627 ASP ASP A . n 
A 1 332 GLN 332 628 628 GLN GLN A . n 
A 1 333 ALA 333 629 629 ALA ALA A . n 
A 1 334 LEU 334 630 630 LEU LEU A . n 
A 1 335 VAL 335 631 631 VAL VAL A . n 
A 1 336 GLU 336 632 632 GLU GLU A . n 
A 1 337 ILE 337 633 633 ILE ILE A . n 
A 1 338 ASN 338 634 634 ASN ASN A . n 
A 1 339 ILE 339 635 635 ILE ILE A . n 
A 1 340 ALA 340 636 636 ALA ALA A . n 
A 1 341 VAL 341 637 637 VAL VAL A . n 
A 1 342 LEU 342 638 638 LEU LEU A . n 
A 1 343 TYR 343 639 639 TYR TYR A . n 
A 1 344 SER 344 640 640 SER SER A . n 
A 1 345 PHE 345 641 641 PHE PHE A . n 
A 1 346 GLN 346 642 642 GLN GLN A . n 
A 1 347 SER 347 643 643 SER SER A . n 
A 1 348 ASP 348 644 644 ASP ASP A . n 
A 1 349 LYS 349 645 645 LYS LYS A . n 
A 1 350 VAL 350 646 646 VAL VAL A . n 
A 1 351 THR 351 647 647 THR THR A . n 
A 1 352 ILE 352 648 648 ILE ILE A . n 
A 1 353 VAL 353 649 649 VAL VAL A . n 
A 1 354 ASP 354 650 650 ASP ASP A . n 
A 1 355 HIS 355 651 651 HIS HIS A . n 
A 1 356 HIS 356 652 652 HIS HIS A . n 
A 1 357 SER 357 653 653 SER SER A . n 
A 1 358 ALA 358 654 654 ALA ALA A . n 
A 1 359 THR 359 655 655 THR THR A . n 
A 1 360 GLU 360 656 656 GLU GLU A . n 
A 1 361 SER 361 657 657 SER SER A . n 
A 1 362 PHE 362 658 658 PHE PHE A . n 
A 1 363 ILE 363 659 659 ILE ILE A . n 
A 1 364 LYS 364 660 660 LYS LYS A . n 
A 1 365 HIS 365 661 661 HIS HIS A . n 
A 1 366 MET 366 662 662 MET MET A . n 
A 1 367 GLU 367 663 663 GLU GLU A . n 
A 1 368 ASN 368 664 664 ASN ASN A . n 
A 1 369 GLU 369 665 665 GLU GLU A . n 
A 1 370 TYR 370 666 666 TYR TYR A . n 
A 1 371 ARG 371 667 667 ARG ARG A . n 
A 1 372 CYS 372 668 668 CYS CYS A . n 
A 1 373 ARG 373 669 669 ARG ARG A . n 
A 1 374 GLY 374 670 670 GLY GLY A . n 
A 1 375 GLY 375 671 671 GLY GLY A . n 
A 1 376 CYS 376 672 672 CYS CYS A . n 
A 1 377 PRO 377 673 673 PRO PRO A . n 
A 1 378 ALA 378 674 674 ALA ALA A . n 
A 1 379 ASP 379 675 675 ASP ASP A . n 
A 1 380 TRP 380 676 676 TRP TRP A . n 
A 1 381 VAL 381 677 677 VAL VAL A . n 
A 1 382 TRP 382 678 678 TRP TRP A . n 
A 1 383 ILE 383 679 679 ILE ILE A . n 
A 1 384 VAL 384 680 680 VAL VAL A . n 
A 1 385 PRO 385 681 681 PRO PRO A . n 
A 1 386 PRO 386 682 682 PRO PRO A . n 
A 1 387 MET 387 683 683 MET MET A . n 
A 1 388 SER 388 684 684 SER SER A . n 
A 1 389 GLY 389 685 685 GLY GLY A . n 
A 1 390 SER 390 686 686 SER SER A . n 
A 1 391 ILE 391 687 687 ILE ILE A . n 
A 1 392 THR 392 688 688 THR THR A . n 
A 1 393 PRO 393 689 689 PRO PRO A . n 
A 1 394 VAL 394 690 690 VAL VAL A . n 
A 1 395 PHE 395 691 691 PHE PHE A . n 
A 1 396 PHE 396 692 692 PHE PHE A . n 
A 1 397 GLN 397 693 693 GLN GLN A . n 
A 1 398 GLU 398 694 694 GLU GLU A . n 
A 1 399 MET 399 695 695 MET MET A . n 
A 1 400 LEU 400 696 696 LEU LEU A . n 
A 1 401 ASN 401 697 697 ASN ASN A . n 
A 1 402 TYR 402 698 698 TYR TYR A . n 
A 1 403 ARG 403 699 699 ARG ARG A . n 
A 1 404 LEU 404 700 700 LEU LEU A . n 
A 1 405 THR 405 701 701 THR THR A . n 
A 1 406 PRO 406 702 702 PRO PRO A . n 
A 1 407 SER 407 703 703 SER SER A . n 
A 1 408 PHE 408 704 704 PHE PHE A . n 
A 1 409 GLU 409 705 705 GLU GLU A . n 
A 1 410 TYR 410 706 706 TYR TYR A . n 
A 1 411 GLN 411 707 707 GLN GLN A . n 
A 1 412 PRO 412 708 708 PRO PRO A . n 
A 1 413 ASP 413 709 709 ASP ASP A . n 
A 1 414 PRO 414 710 710 PRO PRO A . n 
A 1 415 TRP 415 711 711 TRP TRP A . n 
A 1 416 ASN 416 712 712 ASN ASN A . n 
A 1 417 THR 417 713 713 THR THR A . n 
A 1 418 HIS 418 714 714 HIS HIS A . n 
A 1 419 VAL 419 715 715 VAL VAL A . n 
A 1 420 TRP 420 716 716 TRP TRP A . n 
A 1 421 LYS 421 717 ?   ?   ?   A . n 
A 1 422 GLY 422 718 ?   ?   ?   A . n 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        KMI 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   KMI 
_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 KMI 1  803 800 KMI 5V1 A . 
E 5 ACT 1  804 860 ACT ACT A . 
F 6 ZN  1  805 900 ZN  ZN  A . 
G 7 HOH 1  901 20  HOH HOH A . 
G 7 HOH 2  902 23  HOH HOH A . 
G 7 HOH 3  903 24  HOH HOH A . 
G 7 HOH 4  904 30  HOH HOH A . 
G 7 HOH 5  905 8   HOH HOH A . 
G 7 HOH 6  906 27  HOH HOH A . 
G 7 HOH 7  907 1   HOH HOH A . 
G 7 HOH 8  908 9   HOH HOH A . 
G 7 HOH 9  909 2   HOH HOH A . 
G 7 HOH 10 910 10  HOH HOH A . 
G 7 HOH 11 911 6   HOH HOH A . 
G 7 HOH 12 912 3   HOH HOH A . 
G 7 HOH 13 913 11  HOH HOH A . 
G 7 HOH 14 914 16  HOH HOH A . 
G 7 HOH 15 915 12  HOH HOH A . 
G 7 HOH 16 916 18  HOH HOH A . 
G 7 HOH 17 917 28  HOH HOH A . 
G 7 HOH 18 918 4   HOH HOH A . 
G 7 HOH 19 919 22  HOH HOH A . 
G 7 HOH 20 920 26  HOH HOH A . 
G 7 HOH 21 921 14  HOH HOH A . 
G 7 HOH 22 922 17  HOH HOH A . 
G 7 HOH 23 923 7   HOH HOH A . 
G 7 HOH 24 924 5   HOH HOH A . 
G 7 HOH 25 925 21  HOH HOH A . 
G 7 HOH 26 926 25  HOH HOH A . 
G 7 HOH 27 927 29  HOH HOH A . 
G 7 HOH 28 928 15  HOH HOH A . 
G 7 HOH 29 929 19  HOH HOH A . 
G 7 HOH 30 930 13  HOH HOH A . 
# 
loop_
_software.citation_id 
_software.classification 
_software.compiler_name 
_software.compiler_version 
_software.contact_author 
_software.contact_author_email 
_software.date 
_software.description 
_software.dependencies 
_software.hardware 
_software.language 
_software.location 
_software.mods 
_software.name 
_software.os 
_software.os_version 
_software.type 
_software.version 
_software.pdbx_ordinal 
? refinement       ? ? ? ? ? ? ? ? ? ? ? PHENIX  ? ? ? '(1.11.1_2575: ???)' 1 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? Aimless ? ? ? .                    2 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? XDS     ? ? ? .                    3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? REFMAC  ? ? ? .                    4 
# 
_cell.angle_alpha                  90.00 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   90.00 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.00 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     9CVI 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     48.545 
_cell.length_a_esd                 ? 
_cell.length_b                     114.161 
_cell.length_b_esd                 ? 
_cell.length_c                     163.961 
_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                         9CVI 
_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                   9CVI 
_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         2021-10-08 
_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                                       9CVI 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              2.03 
_reflns.d_resolution_low                               46.84 
_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                                     29446 
_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                           98.4 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                5.5 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          5.9 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               1.04 
_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                                0.157 
_reflns.pdbx_Rpim_I_all                                0.068 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       163416 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.996 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              0.141 
_reflns.pdbx_Rmerge_I_all                              ? 
_reflns.pdbx_Rsym_value                                ? 
_reflns.pdbx_CC_split_method                           ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_1                 ? 
_reflns.pdbx_aniso_diffraction_limit_2                 ? 
_reflns.pdbx_aniso_diffraction_limit_3                 ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_1               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_2               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_3               ? 
_reflns.pdbx_orthogonalization_convention              ? 
_reflns.pdbx_percent_possible_ellipsoidal              ? 
_reflns.pdbx_percent_possible_spherical                ? 
_reflns.pdbx_percent_possible_ellipsoidal_anomalous    ? 
_reflns.pdbx_percent_possible_spherical_anomalous      ? 
_reflns.pdbx_redundancy_anomalous                      ? 
_reflns.pdbx_CC_half_anomalous                         ? 
_reflns.pdbx_absDiff_over_sigma_anomalous              ? 
_reflns.pdbx_percent_possible_anomalous                ? 
_reflns.pdbx_observed_signal_threshold                 ? 
_reflns.pdbx_signal_type                               ? 
_reflns.pdbx_signal_details                            ? 
_reflns.pdbx_signal_software_id                        ? 
# 
_reflns_shell.d_res_high                                    2.03 
_reflns_shell.d_res_low                                     2.08 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           ? 
_reflns_shell.number_measured_all                           12502 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             2158 
_reflns_shell.percent_possible_obs                          98.9 
_reflns_shell.Rmerge_F_all                                  ? 
_reflns_shell.Rmerge_F_obs                                  ? 
_reflns_shell.meanI_over_sigI_gt                            ? 
_reflns_shell.meanI_over_uI_all                             ? 
_reflns_shell.meanI_over_uI_gt                              ? 
_reflns_shell.number_measured_gt                            ? 
_reflns_shell.number_unique_gt                              ? 
_reflns_shell.percent_possible_gt                           ? 
_reflns_shell.Rmerge_F_gt                                   ? 
_reflns_shell.Rmerge_I_gt                                   ? 
_reflns_shell.pdbx_redundancy                               5.8 
_reflns_shell.pdbx_chi_squared                              1.02 
_reflns_shell.pdbx_netI_over_sigmaI_all                     ? 
_reflns_shell.pdbx_netI_over_sigmaI_obs                     0.5 
_reflns_shell.pdbx_Rrim_I_all                               5.194 
_reflns_shell.pdbx_Rpim_I_all                               2.128 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.344 
_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                                  4.729 
_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                                 9CVI 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.ls_abs_structure_details                 ? 
_refine.ls_abs_structure_Flack                   ? 
_refine.ls_abs_structure_Flack_esd               ? 
_refine.ls_abs_structure_Rogers                  ? 
_refine.ls_abs_structure_Rogers_esd              ? 
_refine.ls_d_res_high                            2.030 
_refine.ls_d_res_low                             46.84 
_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                     27504 
_refine.ls_number_reflns_R_free                  2599 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    91.11 
_refine.ls_percent_reflns_R_free                 5.01 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.2371 
_refine.ls_R_factor_R_free                       0.2973 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.2338 
_refine.ls_R_Fsqd_factor_obs                     ? 
_refine.ls_R_I_factor_obs                        ? 
_refine.ls_redundancy_reflns_all                 ? 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.ls_restrained_S_all                      ? 
_refine.ls_restrained_S_obs                      ? 
_refine.ls_shift_over_esd_max                    ? 
_refine.ls_shift_over_esd_mean                   ? 
_refine.ls_structure_factor_coef                 ? 
_refine.ls_weighting_details                     ? 
_refine.ls_weighting_scheme                      ? 
_refine.ls_wR_factor_all                         ? 
_refine.ls_wR_factor_obs                         ? 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_wR_factor_R_work                      ? 
_refine.occupancy_max                            ? 
_refine.occupancy_min                            ? 
_refine.solvent_model_details                    'FLAT BULK SOLVENT MODEL' 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.pdbx_R_complete                          ? 
_refine.ls_R_factor_gt                           ? 
_refine.ls_goodness_of_fit_gt                    ? 
_refine.ls_goodness_of_fit_ref                   ? 
_refine.ls_shift_over_su_max                     ? 
_refine.ls_shift_over_su_max_lt                  ? 
_refine.ls_shift_over_su_mean                    ? 
_refine.ls_shift_over_su_mean_lt                 ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          0.00 
_refine.pdbx_ls_sigma_Fsqd                       ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_ls_cross_valid_method               'FREE R-VALUE' 
_refine.pdbx_method_to_determine_struct          'FOURIER SYNTHESIS' 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_stereochemistry_target_values       ML 
_refine.pdbx_R_Free_selection_details            random 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.pdbx_solvent_vdw_probe_radii             1.11 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             0.90 
_refine.pdbx_real_space_R                        ? 
_refine.pdbx_density_correlation                 ? 
_refine.pdbx_pd_number_of_powder_patterns        ? 
_refine.pdbx_pd_number_of_points                 ? 
_refine.pdbx_pd_meas_number_of_points            ? 
_refine.pdbx_pd_proc_ls_prof_R_factor            ? 
_refine.pdbx_pd_proc_ls_prof_wR_factor           ? 
_refine.pdbx_pd_Marquardt_correlation_coeff      ? 
_refine.pdbx_pd_Fsqrd_R_factor                   ? 
_refine.pdbx_pd_ls_matrix_band_width             ? 
_refine.pdbx_overall_phase_error                 44.37 
_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                            0.29 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.overall_SU_R_free                        ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.pdbx_average_fsc_overall                 ? 
_refine.pdbx_average_fsc_work                    ? 
_refine.pdbx_average_fsc_free                    ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.details                          ? 
_refine_hist.d_res_high                       2.030 
_refine_hist.d_res_low                        46.84 
_refine_hist.number_atoms_solvent             30 
_refine_hist.number_atoms_total               3445 
_refine_hist.number_reflns_all                ? 
_refine_hist.number_reflns_obs                ? 
_refine_hist.number_reflns_R_free             ? 
_refine_hist.number_reflns_R_work             ? 
_refine_hist.R_factor_all                     ? 
_refine_hist.R_factor_obs                     ? 
_refine_hist.R_factor_R_free                  ? 
_refine_hist.R_factor_R_work                  ? 
_refine_hist.pdbx_number_residues_total       ? 
_refine_hist.pdbx_B_iso_mean_ligand           ? 
_refine_hist.pdbx_B_iso_mean_solvent          ? 
_refine_hist.pdbx_number_atoms_protein        3333 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         82 
_refine_hist.pdbx_number_atoms_lipid          ? 
_refine_hist.pdbx_number_atoms_carb           ? 
_refine_hist.pdbx_pseudo_atom_details         ? 
# 
loop_
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.criterion 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.number 
_refine_ls_restr.rejects 
_refine_ls_restr.type 
_refine_ls_restr.weight 
_refine_ls_restr.pdbx_restraint_function 
'X-RAY DIFFRACTION' ? 0.008  ? 3526 ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 1.081  ? 4798 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 18.882 ? 2052 ? f_dihedral_angle_d ? ? 
'X-RAY DIFFRACTION' ? 0.050  ? 498  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.006  ? 606  ? f_plane_restr      ? ? 
# 
loop_
_refine_ls_shell.pdbx_refine_id 
_refine_ls_shell.d_res_high 
_refine_ls_shell.d_res_low 
_refine_ls_shell.number_reflns_all 
_refine_ls_shell.number_reflns_obs 
_refine_ls_shell.number_reflns_R_free 
_refine_ls_shell.number_reflns_R_work 
_refine_ls_shell.percent_reflns_obs 
_refine_ls_shell.percent_reflns_R_free 
_refine_ls_shell.R_factor_all 
_refine_ls_shell.R_factor_obs 
_refine_ls_shell.R_factor_R_free_error 
_refine_ls_shell.R_factor_R_work 
_refine_ls_shell.redundancy_reflns_all 
_refine_ls_shell.redundancy_reflns_obs 
_refine_ls_shell.wR_factor_all 
_refine_ls_shell.wR_factor_obs 
_refine_ls_shell.wR_factor_R_free 
_refine_ls_shell.wR_factor_R_work 
_refine_ls_shell.pdbx_R_complete 
_refine_ls_shell.pdbx_total_number_of_bins_used 
_refine_ls_shell.pdbx_phase_error 
_refine_ls_shell.pdbx_fsc_work 
_refine_ls_shell.pdbx_fsc_free 
_refine_ls_shell.R_factor_R_free 
'X-RAY DIFFRACTION' 2.0300 2.0669 . . 87  2242 77.00 . . . . 0.4526 . . . . . . . . . . . 0.4756 
'X-RAY DIFFRACTION' 2.0669 2.1067 . . 121 2171 77.00 . . . . 0.4244 . . . . . . . . . . . 0.4728 
'X-RAY DIFFRACTION' 2.1067 2.1497 . . 120 2313 81.00 . . . . 0.3969 . . . . . . . . . . . 0.3834 
'X-RAY DIFFRACTION' 2.1497 2.1964 . . 120 2315 81.00 . . . . 0.3736 . . . . . . . . . . . 0.4108 
'X-RAY DIFFRACTION' 2.1964 2.2475 . . 140 2373 84.00 . . . . 0.3694 . . . . . . . . . . . 0.4437 
'X-RAY DIFFRACTION' 2.2475 2.3037 . . 140 2447 85.00 . . . . 0.3437 . . . . . . . . . . . 0.3932 
'X-RAY DIFFRACTION' 2.3037 2.3660 . . 120 2473 89.00 . . . . 0.3303 . . . . . . . . . . . 0.3902 
'X-RAY DIFFRACTION' 2.3660 2.4357 . . 135 2621 91.00 . . . . 0.3344 . . . . . . . . . . . 0.4051 
'X-RAY DIFFRACTION' 2.4357 2.5143 . . 132 2696 96.00 . . . . 0.3279 . . . . . . . . . . . 0.4220 
'X-RAY DIFFRACTION' 2.5143 2.6041 . . 129 2775 97.00 . . . . 0.3275 . . . . . . . . . . . 0.3409 
'X-RAY DIFFRACTION' 2.6041 2.7084 . . 149 2815 98.00 . . . . 0.3209 . . . . . . . . . . . 0.3951 
'X-RAY DIFFRACTION' 2.7084 2.8316 . . 142 2786 98.00 . . . . 0.2946 . . . . . . . . . . . 0.3527 
'X-RAY DIFFRACTION' 2.8316 2.9809 . . 109 2830 98.00 . . . . 0.2866 . . . . . . . . . . . 0.4049 
'X-RAY DIFFRACTION' 2.9809 3.1676 . . 169 2758 98.00 . . . . 0.2813 . . . . . . . . . . . 0.3237 
'X-RAY DIFFRACTION' 3.1676 3.4121 . . 176 2764 98.00 . . . . 0.2839 . . . . . . . . . . . 0.3033 
'X-RAY DIFFRACTION' 3.4121 3.7554 . . 157 2741 97.00 . . . . 0.2418 . . . . . . . . . . . 0.2923 
'X-RAY DIFFRACTION' 3.7554 4.2984 . . 154 2684 95.00 . . . . 0.2079 . . . . . . . . . . . 0.2768 
'X-RAY DIFFRACTION' 4.2984 5.4143 . . 151 2695 94.00 . . . . 0.1668 . . . . . . . . . . . 0.2706 
'X-RAY DIFFRACTION' 5.4143 46.84  . . 148 2747 97.00 . . . . 0.1533 . . . . . . . . . . . 0.2171 
# 
_struct.entry_id                     9CVI 
_struct.title                        
;Structure of rat neuronal nitric oxide synthase R349A mutant heme domain bound with 4-methyl-6-(3-((methylamino)methyl)phenyl)pyridin-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        9CVI 
_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              9CVI 
_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 
# 
loop_
_struct_ref_seq_dif.align_id 
_struct_ref_seq_dif.pdbx_pdb_id_code 
_struct_ref_seq_dif.mon_id 
_struct_ref_seq_dif.pdbx_pdb_strand_id 
_struct_ref_seq_dif.seq_num 
_struct_ref_seq_dif.pdbx_pdb_ins_code 
_struct_ref_seq_dif.pdbx_seq_db_name 
_struct_ref_seq_dif.pdbx_seq_db_accession_code 
_struct_ref_seq_dif.db_mon_id 
_struct_ref_seq_dif.pdbx_seq_db_seq_num 
_struct_ref_seq_dif.details 
_struct_ref_seq_dif.pdbx_auth_seq_num 
_struct_ref_seq_dif.pdbx_ordinal 
1 9CVI ALA A 53  ? UNP P29476 ARG 349 'engineered mutation' 349 1 
1 9CVI PHE A 396 ? UNP P29476 HIS 692 'engineered mutation' 692 2 
# 
_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 ? ALA A 116 ? LYS A 397 ALA A 412 1 ? 16 
HELX_P HELX_P5  AA5 GLY A 121 ? TRP A 125 ? GLY A 417 TRP A 421 5 ? 5  
HELX_P HELX_P6  AA6 THR A 138 ? ASN A 155 ? THR A 434 ASN A 451 1 ? 18 
HELX_P HELX_P7  AA7 LYS A 156 ? ASN A 158 ? LYS A 452 ASN A 454 5 ? 3  
HELX_P HELX_P8  AA8 ASN A 202 ? GLN A 212 ? ASN A 498 GLN A 508 1 ? 11 
HELX_P HELX_P9  AA9 PRO A 241 ? VAL A 245 ? PRO A 537 VAL A 541 5 ? 5  
HELX_P HELX_P10 AB1 ASP A 256 ? LEU A 261 ? ASP A 552 LEU A 557 1 ? 6  
HELX_P HELX_P11 AB2 GLY A 294 ? VAL A 299 ? GLY A 590 VAL A 595 1 ? 6  
HELX_P HELX_P12 AB3 VAL A 299 ? ASP A 304 ? VAL A 595 ASP A 600 1 ? 6  
HELX_P HELX_P13 AB4 ILE A 310 ? MET A 318 ? ILE A 606 MET A 614 1 ? 9  
HELX_P HELX_P14 AB5 LYS A 324 ? SER A 327 ? LYS A 620 SER A 623 5 ? 4  
HELX_P HELX_P15 AB6 LEU A 328 ? ASP A 348 ? LEU A 624 ASP A 644 1 ? 21 
HELX_P HELX_P16 AB7 ASP A 354 ? CYS A 372 ? ASP A 650 CYS A 668 1 ? 19 
HELX_P HELX_P17 AB8 ASP A 379 ? VAL A 384 ? ASP A 675 VAL A 680 1 ? 6  
HELX_P HELX_P18 AB9 SER A 388 ? GLN A 397 ? SER A 684 GLN A 693 5 ? 10 
HELX_P HELX_P19 AC1 ASP A 413 ? THR A 417 ? ASP A 709 THR A 713 5 ? 5  
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_conn.id 
_struct_conn.conn_type_id 
_struct_conn.pdbx_leaving_atom_flag 
_struct_conn.pdbx_PDB_id 
_struct_conn.ptnr1_label_asym_id 
_struct_conn.ptnr1_label_comp_id 
_struct_conn.ptnr1_label_seq_id 
_struct_conn.ptnr1_label_atom_id 
_struct_conn.pdbx_ptnr1_label_alt_id 
_struct_conn.pdbx_ptnr1_PDB_ins_code 
_struct_conn.pdbx_ptnr1_standard_comp_id 
_struct_conn.ptnr1_symmetry 
_struct_conn.ptnr2_label_asym_id 
_struct_conn.ptnr2_label_comp_id 
_struct_conn.ptnr2_label_seq_id 
_struct_conn.ptnr2_label_atom_id 
_struct_conn.pdbx_ptnr2_label_alt_id 
_struct_conn.pdbx_ptnr2_PDB_ins_code 
_struct_conn.ptnr1_auth_asym_id 
_struct_conn.ptnr1_auth_comp_id 
_struct_conn.ptnr1_auth_seq_id 
_struct_conn.ptnr2_auth_asym_id 
_struct_conn.ptnr2_auth_comp_id 
_struct_conn.ptnr2_auth_seq_id 
_struct_conn.ptnr2_symmetry 
_struct_conn.pdbx_ptnr3_label_atom_id 
_struct_conn.pdbx_ptnr3_label_seq_id 
_struct_conn.pdbx_ptnr3_label_comp_id 
_struct_conn.pdbx_ptnr3_label_asym_id 
_struct_conn.pdbx_ptnr3_label_alt_id 
_struct_conn.pdbx_ptnr3_PDB_ins_code 
_struct_conn.details 
_struct_conn.pdbx_dist_value 
_struct_conn.pdbx_value_order 
_struct_conn.pdbx_role 
metalc1 metalc ? ? A CYS 30  SG ? ? ? 1_555 F ZN  . ZN ? ? A CYS 326 A ZN  805 1_555 ? ? ? ? ? ? ? 2.458 ? ? 
metalc2 metalc ? ? A CYS 30  SG ? ? ? 1_555 F ZN  . ZN ? ? A CYS 326 A ZN  805 3_455 ? ? ? ? ? ? ? 2.492 ? ? 
metalc3 metalc ? ? A CYS 35  SG ? ? ? 1_555 F ZN  . ZN ? ? A CYS 331 A ZN  805 1_555 ? ? ? ? ? ? ? 2.363 ? ? 
metalc4 metalc ? ? A CYS 35  SG ? ? ? 1_555 F ZN  . ZN ? ? A CYS 331 A ZN  805 3_455 ? ? ? ? ? ? ? 2.366 ? ? 
metalc5 metalc ? ? A CYS 119 SG ? ? ? 1_555 B HEM . FE ? ? A CYS 415 A HEM 801 1_555 ? ? ? ? ? ? ? 2.367 ? ? 
# 
_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_555 113.6 ? 
3  SG ? A CYS 30  ? A CYS 326 ? 1_555 ZN ? F ZN  . ? A ZN  805 ? 1_555 SG ? A CYS 35 ? A CYS 331 ? 1_555 113.6 ? 
4  SG ? A CYS 30  ? A CYS 326 ? 1_555 ZN ? F ZN  . ? A ZN  805 ? 1_555 SG ? A CYS 35 ? A CYS 331 ? 1_555 113.6 ? 
5  SG ? A CYS 30  ? A CYS 326 ? 1_555 ZN ? F ZN  . ? A ZN  805 ? 1_555 SG ? A CYS 35 ? A CYS 331 ? 1_555 113.6 ? 
6  SG ? A CYS 35  ? A CYS 331 ? 1_555 ZN ? F ZN  . ? A ZN  805 ? 1_555 SG ? A CYS 35 ? A CYS 331 ? 1_555 0.0   ? 
7  SG ? A CYS 119 ? A CYS 415 ? 1_555 FE ? B HEM . ? A HEM 801 ? 1_555 NA ? B HEM .  ? A HEM 801 ? 1_555 106.1 ? 
8  SG ? A CYS 119 ? A CYS 415 ? 1_555 FE ? B HEM . ? A HEM 801 ? 1_555 NB ? B HEM .  ? A HEM 801 ? 1_555 98.8  ? 
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 85.3  ? 
10 SG ? A CYS 119 ? A CYS 415 ? 1_555 FE ? B HEM . ? A HEM 801 ? 1_555 NC ? B HEM .  ? A HEM 801 ? 1_555 98.3  ? 
11 NA ? B HEM .   ? A HEM 801 ? 1_555 FE ? B HEM . ? A HEM 801 ? 1_555 NC ? B HEM .  ? A HEM 801 ? 1_555 155.0 ? 
12 NB ? B HEM .   ? A HEM 801 ? 1_555 FE ? B HEM . ? A HEM 801 ? 1_555 NC ? B HEM .  ? A HEM 801 ? 1_555 85.6  ? 
13 SG ? A CYS 119 ? A CYS 415 ? 1_555 FE ? B HEM . ? A HEM 801 ? 1_555 ND ? B HEM .  ? A HEM 801 ? 1_555 112.0 ? 
14 NA ? B HEM .   ? A HEM 801 ? 1_555 FE ? B HEM . ? A HEM 801 ? 1_555 ND ? B HEM .  ? A HEM 801 ? 1_555 88.4  ? 
15 NB ? B HEM .   ? A HEM 801 ? 1_555 FE ? B HEM . ? A HEM 801 ? 1_555 ND ? B HEM .  ? A HEM 801 ? 1_555 149.1 ? 
16 NC ? B HEM .   ? A HEM 801 ? 1_555 FE ? B HEM . ? A HEM 801 ? 1_555 ND ? B HEM .  ? A HEM 801 ? 1_555 87.6  ? 
# 
_struct_mon_prot_cis.pdbx_id                1 
_struct_mon_prot_cis.label_comp_id          THR 
_struct_mon_prot_cis.label_seq_id           405 
_struct_mon_prot_cis.label_asym_id          A 
_struct_mon_prot_cis.label_alt_id           . 
_struct_mon_prot_cis.pdbx_PDB_ins_code      ? 
_struct_mon_prot_cis.auth_comp_id           THR 
_struct_mon_prot_cis.auth_seq_id            701 
_struct_mon_prot_cis.auth_asym_id           A 
_struct_mon_prot_cis.pdbx_label_comp_id_2   PRO 
_struct_mon_prot_cis.pdbx_label_seq_id_2    406 
_struct_mon_prot_cis.pdbx_label_asym_id_2   A 
_struct_mon_prot_cis.pdbx_PDB_ins_code_2    ? 
_struct_mon_prot_cis.pdbx_auth_comp_id_2    PRO 
_struct_mon_prot_cis.pdbx_auth_seq_id_2     702 
_struct_mon_prot_cis.pdbx_auth_asym_id_2    A 
_struct_mon_prot_cis.pdbx_PDB_model_num     1 
_struct_mon_prot_cis.pdbx_omega_angle       3.45 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 2 ? 
AA2 ? 4 ? 
AA3 ? 3 ? 
AA4 ? 2 ? 
AA5 ? 2 ? 
AA6 ? 3 ? 
AA7 ? 2 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? anti-parallel 
AA2 1 2 ? parallel      
AA2 2 3 ? anti-parallel 
AA2 3 4 ? anti-parallel 
AA3 1 2 ? anti-parallel 
AA3 2 3 ? anti-parallel 
AA4 1 2 ? anti-parallel 
AA5 1 2 ? anti-parallel 
AA6 1 2 ? anti-parallel 
AA6 2 3 ? anti-parallel 
AA7 1 2 ? parallel      
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 LYS A 6   ? LYS A 8   ? LYS A 302 LYS A 304 
AA1 2 VAL A 15  ? THR A 17  ? VAL A 311 THR A 313 
AA2 1 GLN A 129 ? ASP A 132 ? GLN A 425 ASP A 428 
AA2 2 ALA A 162 ? ILE A 165 ? ALA A 458 ILE A 461 
AA2 3 PHE A 288 ? SER A 289 ? PHE A 584 SER A 585 
AA2 4 ALA A 270 ? VAL A 271 ? ALA A 566 VAL A 567 
AA3 1 ARG A 177 ? VAL A 178 ? ARG A 473 VAL A 474 
AA3 2 LEU A 226 ? GLN A 229 ? LEU A 522 GLN A 525 
AA3 3 GLU A 236 ? PHE A 238 ? GLU A 532 PHE A 534 
AA4 1 GLY A 188 ? LYS A 190 ? GLY A 484 LYS A 486 
AA4 2 THR A 196 ? GLY A 198 ? THR A 492 GLY A 494 
AA5 1 GLU A 247 ? PRO A 249 ? GLU A 543 PRO A 545 
AA5 2 LYS A 264 ? TYR A 266 ? LYS A 560 TYR A 562 
AA6 1 LEU A 281 ? PHE A 283 ? LEU A 577 PHE A 579 
AA6 2 MET A 274 ? ILE A 278 ? MET A 570 ILE A 574 
AA6 3 SER A 407 ? TYR A 410 ? SER A 703 TYR A 706 
AA7 1 TYR A 292 ? MET A 293 ? TYR A 588 MET A 589 
AA7 2 ILE A 352 ? VAL A 353 ? ILE A 648 VAL A 649 
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2 N VAL A 7   ? N VAL A 303 O LEU A 16  ? O LEU A 312 
AA2 1 2 N PHE A 131 ? N PHE A 427 O ILE A 165 ? O ILE A 461 
AA2 2 3 N ALA A 162 ? N ALA A 458 O SER A 289 ? O SER A 585 
AA2 3 4 O PHE A 288 ? O PHE A 584 N VAL A 271 ? N VAL A 567 
AA3 1 2 N ARG A 177 ? N ARG A 473 O GLN A 229 ? O GLN A 525 
AA3 2 3 N LEU A 226 ? N LEU A 522 O PHE A 238 ? O PHE A 534 
AA4 1 2 N TYR A 189 ? N TYR A 485 O LEU A 197 ? O LEU A 493 
AA5 1 2 N VAL A 248 ? N VAL A 544 O TRP A 265 ? O TRP A 561 
AA6 1 2 O LEU A 281 ? O LEU A 577 N ILE A 278 ? N ILE A 574 
AA6 2 3 N LEU A 275 ? N LEU A 571 O GLU A 409 ? O GLU A 705 
AA7 1 2 N TYR A 292 ? N TYR A 588 O VAL A 353 ? O VAL A 649 
# 
_pdbx_entry_details.entry_id                   9CVI 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.has_protein_modification   N 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1  1 THR A 321 ? ? -143.55 -54.64  
2  1 SER A 392 ? ? 76.70   -29.95  
3  1 THR A 393 ? ? -100.40 -163.09 
4  1 ALA A 412 ? ? -69.61  92.92   
5  1 THR A 466 ? ? -115.44 -89.95  
6  1 SER A 491 ? ? -69.03  -165.29 
7  1 PHE A 517 ? ? -112.58 64.43   
8  1 CYS A 582 ? ? -153.01 52.43   
9  1 ARG A 603 ? ? -117.60 -130.15 
10 1 ASP A 615 ? ? 52.32   78.29   
11 1 ASP A 617 ? ? -62.84  90.24   
12 1 ARG A 667 ? ? -81.73  -76.08  
13 1 ARG A 669 ? ? -152.15 -23.17  
14 1 THR A 713 ? ? -140.74 -21.17  
# 
_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         -23.4533 
_pdbx_refine_tls.origin_y         -4.9805 
_pdbx_refine_tls.origin_z         22.2786 
_pdbx_refine_tls.T[1][1]          0.2594 
_pdbx_refine_tls.T[1][1]_esd      ? 
_pdbx_refine_tls.T[1][2]          -0.0178 
_pdbx_refine_tls.T[1][2]_esd      ? 
_pdbx_refine_tls.T[1][3]          -0.0469 
_pdbx_refine_tls.T[1][3]_esd      ? 
_pdbx_refine_tls.T[2][2]          0.4272 
_pdbx_refine_tls.T[2][2]_esd      ? 
_pdbx_refine_tls.T[2][3]          -0.0104 
_pdbx_refine_tls.T[2][3]_esd      ? 
_pdbx_refine_tls.T[3][3]          0.4573 
_pdbx_refine_tls.T[3][3]_esd      ? 
_pdbx_refine_tls.L[1][1]          0.7491 
_pdbx_refine_tls.L[1][1]_esd      ? 
_pdbx_refine_tls.L[1][2]          -0.1850 
_pdbx_refine_tls.L[1][2]_esd      ? 
_pdbx_refine_tls.L[1][3]          0.2710 
_pdbx_refine_tls.L[1][3]_esd      ? 
_pdbx_refine_tls.L[2][2]          1.0566 
_pdbx_refine_tls.L[2][2]_esd      ? 
_pdbx_refine_tls.L[2][3]          -0.0602 
_pdbx_refine_tls.L[2][3]_esd      ? 
_pdbx_refine_tls.L[3][3]          7.6263 
_pdbx_refine_tls.L[3][3]_esd      ? 
_pdbx_refine_tls.S[1][1]          0.0117 
_pdbx_refine_tls.S[1][1]_esd      ? 
_pdbx_refine_tls.S[1][2]          0.1294 
_pdbx_refine_tls.S[1][2]_esd      ? 
_pdbx_refine_tls.S[1][3]          -0.0194 
_pdbx_refine_tls.S[1][3]_esd      ? 
_pdbx_refine_tls.S[2][1]          0.0988 
_pdbx_refine_tls.S[2][1]_esd      ? 
_pdbx_refine_tls.S[2][2]          -0.0726 
_pdbx_refine_tls.S[2][2]_esd      ? 
_pdbx_refine_tls.S[2][3]          -0.0256 
_pdbx_refine_tls.S[2][3]_esd      ? 
_pdbx_refine_tls.S[3][1]          -0.1122 
_pdbx_refine_tls.S[3][1]_esd      ? 
_pdbx_refine_tls.S[3][2]          0.3041 
_pdbx_refine_tls.S[3][2]_esd      ? 
_pdbx_refine_tls.S[3][3]          0.0557 
_pdbx_refine_tls.S[3][3]_esd      ? 
# 
_pdbx_refine_tls_group.id                  1 
_pdbx_refine_tls_group.pdbx_refine_id      'X-RAY DIFFRACTION' 
_pdbx_refine_tls_group.refine_tls_id       1 
_pdbx_refine_tls_group.beg_label_asym_id   ? 
_pdbx_refine_tls_group.beg_label_seq_id    ? 
_pdbx_refine_tls_group.beg_auth_asym_id    ? 
_pdbx_refine_tls_group.beg_auth_seq_id     ? 
_pdbx_refine_tls_group.beg_PDB_ins_code    ? 
_pdbx_refine_tls_group.end_label_asym_id   ? 
_pdbx_refine_tls_group.end_label_seq_id    ? 
_pdbx_refine_tls_group.end_auth_asym_id    ? 
_pdbx_refine_tls_group.end_auth_seq_id     ? 
_pdbx_refine_tls_group.end_PDB_ins_code    ? 
_pdbx_refine_tls_group.selection           ? 
_pdbx_refine_tls_group.selection_details   '(chain A and resid 299:716)' 
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1  1 Y 1 A CYS 297 ? A CYS 1   
2  1 Y 1 A PRO 298 ? A PRO 2   
3  1 Y 1 A GLN 340 ? A GLN 44  
4  1 Y 1 A HIS 341 ? A HIS 45  
5  1 Y 1 A THR 342 ? A THR 46  
6  1 Y 1 A ARG 343 ? A ARG 47  
7  1 Y 1 A LYS 344 ? A LYS 48  
8  1 Y 1 A PRO 345 ? A PRO 49  
9  1 Y 1 A GLU 346 ? A GLU 50  
10 1 Y 1 A ASP 347 ? A ASP 51  
11 1 Y 1 A LYS 717 ? A LYS 421 
12 1 Y 1 A GLY 718 ? A GLY 422 
# 
loop_
_chem_comp_atom.comp_id 
_chem_comp_atom.atom_id 
_chem_comp_atom.type_symbol 
_chem_comp_atom.pdbx_aromatic_flag 
_chem_comp_atom.pdbx_stereo_config 
_chem_comp_atom.pdbx_ordinal 
ACT C    C  N N 1   
ACT O    O  N N 2   
ACT OXT  O  N N 3   
ACT CH3  C  N N 4   
ACT H1   H  N N 5   
ACT H2   H  N N 6   
ACT H3   H  N N 7   
ALA N    N  N N 8   
ALA CA   C  N S 9   
ALA C    C  N N 10  
ALA O    O  N N 11  
ALA CB   C  N N 12  
ALA OXT  O  N N 13  
ALA H    H  N N 14  
ALA H2   H  N N 15  
ALA HA   H  N N 16  
ALA HB1  H  N N 17  
ALA HB2  H  N N 18  
ALA HB3  H  N N 19  
ALA HXT  H  N N 20  
ARG N    N  N N 21  
ARG CA   C  N S 22  
ARG C    C  N N 23  
ARG O    O  N N 24  
ARG CB   C  N N 25  
ARG CG   C  N N 26  
ARG CD   C  N N 27  
ARG NE   N  N N 28  
ARG CZ   C  N N 29  
ARG NH1  N  N N 30  
ARG NH2  N  N N 31  
ARG OXT  O  N N 32  
ARG H    H  N N 33  
ARG H2   H  N N 34  
ARG HA   H  N N 35  
ARG HB2  H  N N 36  
ARG HB3  H  N N 37  
ARG HG2  H  N N 38  
ARG HG3  H  N N 39  
ARG HD2  H  N N 40  
ARG HD3  H  N N 41  
ARG HE   H  N N 42  
ARG HH11 H  N N 43  
ARG HH12 H  N N 44  
ARG HH21 H  N N 45  
ARG HH22 H  N N 46  
ARG HXT  H  N N 47  
ASN N    N  N N 48  
ASN CA   C  N S 49  
ASN C    C  N N 50  
ASN O    O  N N 51  
ASN CB   C  N N 52  
ASN CG   C  N N 53  
ASN OD1  O  N N 54  
ASN ND2  N  N N 55  
ASN OXT  O  N N 56  
ASN H    H  N N 57  
ASN H2   H  N N 58  
ASN HA   H  N N 59  
ASN HB2  H  N N 60  
ASN HB3  H  N N 61  
ASN HD21 H  N N 62  
ASN HD22 H  N N 63  
ASN HXT  H  N N 64  
ASP N    N  N N 65  
ASP CA   C  N S 66  
ASP C    C  N N 67  
ASP O    O  N N 68  
ASP CB   C  N N 69  
ASP CG   C  N N 70  
ASP OD1  O  N N 71  
ASP OD2  O  N N 72  
ASP OXT  O  N N 73  
ASP H    H  N N 74  
ASP H2   H  N N 75  
ASP HA   H  N N 76  
ASP HB2  H  N N 77  
ASP HB3  H  N N 78  
ASP HD2  H  N N 79  
ASP HXT  H  N N 80  
CYS N    N  N N 81  
CYS CA   C  N R 82  
CYS C    C  N N 83  
CYS O    O  N N 84  
CYS CB   C  N N 85  
CYS SG   S  N N 86  
CYS OXT  O  N N 87  
CYS H    H  N N 88  
CYS H2   H  N N 89  
CYS HA   H  N N 90  
CYS HB2  H  N N 91  
CYS HB3  H  N N 92  
CYS HG   H  N N 93  
CYS HXT  H  N N 94  
GLN N    N  N N 95  
GLN CA   C  N S 96  
GLN C    C  N N 97  
GLN O    O  N N 98  
GLN CB   C  N N 99  
GLN CG   C  N N 100 
GLN CD   C  N N 101 
GLN OE1  O  N N 102 
GLN NE2  N  N N 103 
GLN OXT  O  N N 104 
GLN H    H  N N 105 
GLN H2   H  N N 106 
GLN HA   H  N N 107 
GLN HB2  H  N N 108 
GLN HB3  H  N N 109 
GLN HG2  H  N N 110 
GLN HG3  H  N N 111 
GLN HE21 H  N N 112 
GLN HE22 H  N N 113 
GLN HXT  H  N N 114 
GLU N    N  N N 115 
GLU CA   C  N S 116 
GLU C    C  N N 117 
GLU O    O  N N 118 
GLU CB   C  N N 119 
GLU CG   C  N N 120 
GLU CD   C  N N 121 
GLU OE1  O  N N 122 
GLU OE2  O  N N 123 
GLU OXT  O  N N 124 
GLU H    H  N N 125 
GLU H2   H  N N 126 
GLU HA   H  N N 127 
GLU HB2  H  N N 128 
GLU HB3  H  N N 129 
GLU HG2  H  N N 130 
GLU HG3  H  N N 131 
GLU HE2  H  N N 132 
GLU HXT  H  N N 133 
GLY N    N  N N 134 
GLY CA   C  N N 135 
GLY C    C  N N 136 
GLY O    O  N N 137 
GLY OXT  O  N N 138 
GLY H    H  N N 139 
GLY H2   H  N N 140 
GLY HA2  H  N N 141 
GLY HA3  H  N N 142 
GLY HXT  H  N N 143 
H4B N1   N  Y N 144 
H4B C2   C  Y N 145 
H4B N2   N  N N 146 
H4B N3   N  Y N 147 
H4B C4   C  Y N 148 
H4B O4   O  N N 149 
H4B C4A  C  Y N 150 
H4B C8A  C  Y N 151 
H4B N5   N  N N 152 
H4B N8   N  N N 153 
H4B C6   C  N R 154 
H4B C7   C  N N 155 
H4B C9   C  N R 156 
H4B O9   O  N N 157 
H4B C10  C  N S 158 
H4B C11  C  N N 159 
H4B O10  O  N N 160 
H4B HN21 H  N N 161 
H4B HN22 H  N N 162 
H4B HN3  H  N N 163 
H4B HN5  H  N N 164 
H4B HN8  H  N N 165 
H4B H6   H  N N 166 
H4B H71  H  N N 167 
H4B H72  H  N N 168 
H4B H9   H  N N 169 
H4B HO9  H  N N 170 
H4B H10  H  N N 171 
H4B H111 H  N N 172 
H4B H112 H  N N 173 
H4B H113 H  N N 174 
H4B HO0  H  N N 175 
HEM CHA  C  N N 176 
HEM CHB  C  N N 177 
HEM CHC  C  N N 178 
HEM CHD  C  N N 179 
HEM C1A  C  Y N 180 
HEM C2A  C  Y N 181 
HEM C3A  C  Y N 182 
HEM C4A  C  Y N 183 
HEM CMA  C  N N 184 
HEM CAA  C  N N 185 
HEM CBA  C  N N 186 
HEM CGA  C  N N 187 
HEM O1A  O  N N 188 
HEM O2A  O  N N 189 
HEM C1B  C  N N 190 
HEM C2B  C  N N 191 
HEM C3B  C  N N 192 
HEM C4B  C  N N 193 
HEM CMB  C  N N 194 
HEM CAB  C  N N 195 
HEM CBB  C  N N 196 
HEM C1C  C  Y N 197 
HEM C2C  C  Y N 198 
HEM C3C  C  Y N 199 
HEM C4C  C  Y N 200 
HEM CMC  C  N N 201 
HEM CAC  C  N N 202 
HEM CBC  C  N N 203 
HEM C1D  C  N N 204 
HEM C2D  C  N N 205 
HEM C3D  C  N N 206 
HEM C4D  C  N N 207 
HEM CMD  C  N N 208 
HEM CAD  C  N N 209 
HEM CBD  C  N N 210 
HEM CGD  C  N N 211 
HEM O1D  O  N N 212 
HEM O2D  O  N N 213 
HEM NA   N  Y N 214 
HEM NB   N  N N 215 
HEM NC   N  Y N 216 
HEM ND   N  N N 217 
HEM FE   FE N N 218 
HEM HHB  H  N N 219 
HEM HHC  H  N N 220 
HEM HHD  H  N N 221 
HEM HMA  H  N N 222 
HEM HMAA H  N N 223 
HEM HMAB H  N N 224 
HEM HAA  H  N N 225 
HEM HAAA H  N N 226 
HEM HBA  H  N N 227 
HEM HBAA H  N N 228 
HEM HMB  H  N N 229 
HEM HMBA H  N N 230 
HEM HMBB H  N N 231 
HEM HAB  H  N N 232 
HEM HBB  H  N N 233 
HEM HBBA H  N N 234 
HEM HMC  H  N N 235 
HEM HMCA H  N N 236 
HEM HMCB H  N N 237 
HEM HAC  H  N N 238 
HEM HBC  H  N N 239 
HEM HBCA H  N N 240 
HEM HMD  H  N N 241 
HEM HMDA H  N N 242 
HEM HMDB H  N N 243 
HEM HAD  H  N N 244 
HEM HADA H  N N 245 
HEM HBD  H  N N 246 
HEM HBDA H  N N 247 
HEM H2A  H  N N 248 
HEM H2D  H  N N 249 
HEM HHA  H  N N 250 
HIS N    N  N N 251 
HIS CA   C  N S 252 
HIS C    C  N N 253 
HIS O    O  N N 254 
HIS CB   C  N N 255 
HIS CG   C  Y N 256 
HIS ND1  N  Y N 257 
HIS CD2  C  Y N 258 
HIS CE1  C  Y N 259 
HIS NE2  N  Y N 260 
HIS OXT  O  N N 261 
HIS H    H  N N 262 
HIS H2   H  N N 263 
HIS HA   H  N N 264 
HIS HB2  H  N N 265 
HIS HB3  H  N N 266 
HIS HD1  H  N N 267 
HIS HD2  H  N N 268 
HIS HE1  H  N N 269 
HIS HE2  H  N N 270 
HIS HXT  H  N N 271 
HOH O    O  N N 272 
HOH H1   H  N N 273 
HOH H2   H  N N 274 
ILE N    N  N N 275 
ILE CA   C  N S 276 
ILE C    C  N N 277 
ILE O    O  N N 278 
ILE CB   C  N S 279 
ILE CG1  C  N N 280 
ILE CG2  C  N N 281 
ILE CD1  C  N N 282 
ILE OXT  O  N N 283 
ILE H    H  N N 284 
ILE H2   H  N N 285 
ILE HA   H  N N 286 
ILE HB   H  N N 287 
ILE HG12 H  N N 288 
ILE HG13 H  N N 289 
ILE HG21 H  N N 290 
ILE HG22 H  N N 291 
ILE HG23 H  N N 292 
ILE HD11 H  N N 293 
ILE HD12 H  N N 294 
ILE HD13 H  N N 295 
ILE HXT  H  N N 296 
KMI C13  C  Y N 297 
KMI C11  C  Y N 298 
KMI C12  C  Y N 299 
KMI C14  C  Y N 300 
KMI C02  C  Y N 301 
KMI C03  C  Y N 302 
KMI C04  C  Y N 303 
KMI C05  C  Y N 304 
KMI C06  C  Y N 305 
KMI C07  C  N N 306 
KMI C15  C  Y N 307 
KMI C16  C  Y N 308 
KMI C17  C  N N 309 
KMI C19  C  N N 310 
KMI N01  N  Y N 311 
KMI N02  N  N N 312 
KMI N18  N  N N 313 
KMI H1   H  N N 314 
KMI H2   H  N N 315 
KMI H3   H  N N 316 
KMI H4   H  N N 317 
KMI H5   H  N N 318 
KMI H6   H  N N 319 
KMI H7   H  N N 320 
KMI H8   H  N N 321 
KMI H9   H  N N 322 
KMI H10  H  N N 323 
KMI H11  H  N N 324 
KMI H12  H  N N 325 
KMI H13  H  N N 326 
KMI H14  H  N N 327 
KMI H15  H  N N 328 
KMI H16  H  N N 329 
KMI H17  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 
ACT C   O    doub N N 1   
ACT C   OXT  sing N N 2   
ACT C   CH3  sing N N 3   
ACT CH3 H1   sing N N 4   
ACT CH3 H2   sing N N 5   
ACT CH3 H3   sing N N 6   
ALA N   CA   sing N N 7   
ALA N   H    sing N N 8   
ALA N   H2   sing N N 9   
ALA CA  C    sing N N 10  
ALA CA  CB   sing N N 11  
ALA CA  HA   sing N N 12  
ALA C   O    doub N N 13  
ALA C   OXT  sing N N 14  
ALA CB  HB1  sing N N 15  
ALA CB  HB2  sing N N 16  
ALA CB  HB3  sing N N 17  
ALA OXT HXT  sing N N 18  
ARG N   CA   sing N N 19  
ARG N   H    sing N N 20  
ARG N   H2   sing N N 21  
ARG CA  C    sing N N 22  
ARG CA  CB   sing N N 23  
ARG CA  HA   sing N N 24  
ARG C   O    doub N N 25  
ARG C   OXT  sing N N 26  
ARG CB  CG   sing N N 27  
ARG CB  HB2  sing N N 28  
ARG CB  HB3  sing N N 29  
ARG CG  CD   sing N N 30  
ARG CG  HG2  sing N N 31  
ARG CG  HG3  sing N N 32  
ARG CD  NE   sing N N 33  
ARG CD  HD2  sing N N 34  
ARG CD  HD3  sing N N 35  
ARG NE  CZ   sing N N 36  
ARG NE  HE   sing N N 37  
ARG CZ  NH1  sing N N 38  
ARG CZ  NH2  doub N N 39  
ARG NH1 HH11 sing N N 40  
ARG NH1 HH12 sing N N 41  
ARG NH2 HH21 sing N N 42  
ARG NH2 HH22 sing N N 43  
ARG OXT HXT  sing N N 44  
ASN N   CA   sing N N 45  
ASN N   H    sing N N 46  
ASN N   H2   sing N N 47  
ASN CA  C    sing N N 48  
ASN CA  CB   sing N N 49  
ASN CA  HA   sing N N 50  
ASN C   O    doub N N 51  
ASN C   OXT  sing N N 52  
ASN CB  CG   sing N N 53  
ASN CB  HB2  sing N N 54  
ASN CB  HB3  sing N N 55  
ASN CG  OD1  doub N N 56  
ASN CG  ND2  sing N N 57  
ASN ND2 HD21 sing N N 58  
ASN ND2 HD22 sing N N 59  
ASN OXT HXT  sing N N 60  
ASP N   CA   sing N N 61  
ASP N   H    sing N N 62  
ASP N   H2   sing N N 63  
ASP CA  C    sing N N 64  
ASP CA  CB   sing N N 65  
ASP CA  HA   sing N N 66  
ASP C   O    doub N N 67  
ASP C   OXT  sing N N 68  
ASP CB  CG   sing N N 69  
ASP CB  HB2  sing N N 70  
ASP CB  HB3  sing N N 71  
ASP CG  OD1  doub N N 72  
ASP CG  OD2  sing N N 73  
ASP OD2 HD2  sing N N 74  
ASP OXT HXT  sing N N 75  
CYS N   CA   sing N N 76  
CYS N   H    sing N N 77  
CYS N   H2   sing N N 78  
CYS CA  C    sing N N 79  
CYS CA  CB   sing N N 80  
CYS CA  HA   sing N N 81  
CYS C   O    doub N N 82  
CYS C   OXT  sing N N 83  
CYS CB  SG   sing N N 84  
CYS CB  HB2  sing N N 85  
CYS CB  HB3  sing N N 86  
CYS SG  HG   sing N N 87  
CYS OXT HXT  sing N N 88  
GLN N   CA   sing N N 89  
GLN N   H    sing N N 90  
GLN N   H2   sing N N 91  
GLN CA  C    sing N N 92  
GLN CA  CB   sing N N 93  
GLN CA  HA   sing N N 94  
GLN C   O    doub N N 95  
GLN C   OXT  sing N N 96  
GLN CB  CG   sing N N 97  
GLN CB  HB2  sing N N 98  
GLN CB  HB3  sing N N 99  
GLN CG  CD   sing N N 100 
GLN CG  HG2  sing N N 101 
GLN CG  HG3  sing N N 102 
GLN CD  OE1  doub N N 103 
GLN CD  NE2  sing N N 104 
GLN NE2 HE21 sing N N 105 
GLN NE2 HE22 sing N N 106 
GLN OXT HXT  sing N N 107 
GLU N   CA   sing N N 108 
GLU N   H    sing N N 109 
GLU N   H2   sing N N 110 
GLU CA  C    sing N N 111 
GLU CA  CB   sing N N 112 
GLU CA  HA   sing N N 113 
GLU C   O    doub N N 114 
GLU C   OXT  sing N N 115 
GLU CB  CG   sing N N 116 
GLU CB  HB2  sing N N 117 
GLU CB  HB3  sing N N 118 
GLU CG  CD   sing N N 119 
GLU CG  HG2  sing N N 120 
GLU CG  HG3  sing N N 121 
GLU CD  OE1  doub N N 122 
GLU CD  OE2  sing N N 123 
GLU OE2 HE2  sing N N 124 
GLU OXT HXT  sing N N 125 
GLY N   CA   sing N N 126 
GLY N   H    sing N N 127 
GLY N   H2   sing N N 128 
GLY CA  C    sing N N 129 
GLY CA  HA2  sing N N 130 
GLY CA  HA3  sing N N 131 
GLY C   O    doub N N 132 
GLY C   OXT  sing N N 133 
GLY OXT HXT  sing N N 134 
H4B N1  C2   doub Y N 135 
H4B N1  C8A  sing Y N 136 
H4B C2  N2   sing N N 137 
H4B C2  N3   sing Y N 138 
H4B N2  HN21 sing N N 139 
H4B N2  HN22 sing N N 140 
H4B N3  C4   sing Y N 141 
H4B N3  HN3  sing N N 142 
H4B C4  O4   doub N N 143 
H4B C4  C4A  sing Y N 144 
H4B C4A C8A  doub Y N 145 
H4B C4A N5   sing N N 146 
H4B C8A N8   sing N N 147 
H4B N5  C6   sing N N 148 
H4B N5  HN5  sing N N 149 
H4B N8  C7   sing N N 150 
H4B N8  HN8  sing N N 151 
H4B C6  C7   sing N N 152 
H4B C6  C9   sing N N 153 
H4B C6  H6   sing N N 154 
H4B C7  H71  sing N N 155 
H4B C7  H72  sing N N 156 
H4B C9  O9   sing N N 157 
H4B C9  C10  sing N N 158 
H4B C9  H9   sing N N 159 
H4B O9  HO9  sing N N 160 
H4B C10 C11  sing N N 161 
H4B C10 O10  sing N N 162 
H4B C10 H10  sing N N 163 
H4B C11 H111 sing N N 164 
H4B C11 H112 sing N N 165 
H4B C11 H113 sing N N 166 
H4B O10 HO0  sing N N 167 
HEM CHA C1A  sing N N 168 
HEM CHA C4D  doub N N 169 
HEM CHA HHA  sing N N 170 
HEM CHB C4A  sing N N 171 
HEM CHB C1B  doub N N 172 
HEM CHB HHB  sing N N 173 
HEM CHC C4B  sing N N 174 
HEM CHC C1C  doub N N 175 
HEM CHC HHC  sing N N 176 
HEM CHD C4C  doub N N 177 
HEM CHD C1D  sing N N 178 
HEM CHD HHD  sing N N 179 
HEM C1A C2A  doub Y N 180 
HEM C1A NA   sing Y N 181 
HEM C2A C3A  sing Y N 182 
HEM C2A CAA  sing N N 183 
HEM C3A C4A  doub Y N 184 
HEM C3A CMA  sing N N 185 
HEM C4A NA   sing Y N 186 
HEM CMA HMA  sing N N 187 
HEM CMA HMAA sing N N 188 
HEM CMA HMAB sing N N 189 
HEM CAA CBA  sing N N 190 
HEM CAA HAA  sing N N 191 
HEM CAA HAAA sing N N 192 
HEM CBA CGA  sing N N 193 
HEM CBA HBA  sing N N 194 
HEM CBA HBAA sing N N 195 
HEM CGA O1A  doub N N 196 
HEM CGA O2A  sing N N 197 
HEM C1B C2B  sing N N 198 
HEM C1B NB   sing N N 199 
HEM C2B C3B  doub N N 200 
HEM C2B CMB  sing N N 201 
HEM C3B C4B  sing N N 202 
HEM C3B CAB  sing N N 203 
HEM C4B NB   doub N N 204 
HEM CMB HMB  sing N N 205 
HEM CMB HMBA sing N N 206 
HEM CMB HMBB sing N N 207 
HEM CAB CBB  doub N N 208 
HEM CAB HAB  sing N N 209 
HEM CBB HBB  sing N N 210 
HEM CBB HBBA sing N N 211 
HEM C1C C2C  sing Y N 212 
HEM C1C NC   sing Y N 213 
HEM C2C C3C  doub Y N 214 
HEM C2C CMC  sing N N 215 
HEM C3C C4C  sing Y N 216 
HEM C3C CAC  sing N N 217 
HEM C4C NC   sing Y N 218 
HEM CMC HMC  sing N N 219 
HEM CMC HMCA sing N N 220 
HEM CMC HMCB sing N N 221 
HEM CAC CBC  doub N N 222 
HEM CAC HAC  sing N N 223 
HEM CBC HBC  sing N N 224 
HEM CBC HBCA sing N N 225 
HEM C1D C2D  sing N N 226 
HEM C1D ND   doub N N 227 
HEM C2D C3D  doub N N 228 
HEM C2D CMD  sing N N 229 
HEM C3D C4D  sing N N 230 
HEM C3D CAD  sing N N 231 
HEM C4D ND   sing N N 232 
HEM CMD HMD  sing N N 233 
HEM CMD HMDA sing N N 234 
HEM CMD HMDB sing N N 235 
HEM CAD CBD  sing N N 236 
HEM CAD HAD  sing N N 237 
HEM CAD HADA sing N N 238 
HEM CBD CGD  sing N N 239 
HEM CBD HBD  sing N N 240 
HEM CBD HBDA sing N N 241 
HEM CGD O1D  doub N N 242 
HEM CGD O2D  sing N N 243 
HEM O2A H2A  sing N N 244 
HEM O2D H2D  sing N N 245 
HEM FE  NA   sing N N 246 
HEM FE  NB   sing N N 247 
HEM FE  NC   sing N N 248 
HEM FE  ND   sing N N 249 
HIS N   CA   sing N N 250 
HIS N   H    sing N N 251 
HIS N   H2   sing N N 252 
HIS CA  C    sing N N 253 
HIS CA  CB   sing N N 254 
HIS CA  HA   sing N N 255 
HIS C   O    doub N N 256 
HIS C   OXT  sing N N 257 
HIS CB  CG   sing N N 258 
HIS CB  HB2  sing N N 259 
HIS CB  HB3  sing N N 260 
HIS CG  ND1  sing Y N 261 
HIS CG  CD2  doub Y N 262 
HIS ND1 CE1  doub Y N 263 
HIS ND1 HD1  sing N N 264 
HIS CD2 NE2  sing Y N 265 
HIS CD2 HD2  sing N N 266 
HIS CE1 NE2  sing Y N 267 
HIS CE1 HE1  sing N N 268 
HIS NE2 HE2  sing N N 269 
HIS OXT HXT  sing N N 270 
HOH O   H1   sing N N 271 
HOH O   H2   sing N N 272 
ILE N   CA   sing N N 273 
ILE N   H    sing N N 274 
ILE N   H2   sing N N 275 
ILE CA  C    sing N N 276 
ILE CA  CB   sing N N 277 
ILE CA  HA   sing N N 278 
ILE C   O    doub N N 279 
ILE C   OXT  sing N N 280 
ILE CB  CG1  sing N N 281 
ILE CB  CG2  sing N N 282 
ILE CB  HB   sing N N 283 
ILE CG1 CD1  sing N N 284 
ILE CG1 HG12 sing N N 285 
ILE CG1 HG13 sing N N 286 
ILE CG2 HG21 sing N N 287 
ILE CG2 HG22 sing N N 288 
ILE CG2 HG23 sing N N 289 
ILE CD1 HD11 sing N N 290 
ILE CD1 HD12 sing N N 291 
ILE CD1 HD13 sing N N 292 
ILE OXT HXT  sing N N 293 
KMI C07 C04  sing N N 294 
KMI C04 C05  doub Y N 295 
KMI C04 C03  sing Y N 296 
KMI C05 C06  sing Y N 297 
KMI C03 C02  doub Y N 298 
KMI C06 C11  sing N N 299 
KMI C06 N01  doub Y N 300 
KMI C02 N01  sing Y N 301 
KMI C02 N02  sing N N 302 
KMI C12 C11  doub Y N 303 
KMI C12 C13  sing Y N 304 
KMI C11 C16  sing Y N 305 
KMI C13 C14  doub Y N 306 
KMI C16 C15  doub Y N 307 
KMI C14 C15  sing Y N 308 
KMI C15 C17  sing N N 309 
KMI C17 N18  sing N N 310 
KMI N18 C19  sing N N 311 
KMI C13 H1   sing N N 312 
KMI C12 H2   sing N N 313 
KMI C14 H3   sing N N 314 
KMI C03 H4   sing N N 315 
KMI C05 H5   sing N N 316 
KMI C07 H6   sing N N 317 
KMI C07 H7   sing N N 318 
KMI C07 H8   sing N N 319 
KMI C16 H9   sing N N 320 
KMI C17 H10  sing N N 321 
KMI C17 H11  sing N N 322 
KMI C19 H12  sing N N 323 
KMI C19 H13  sing N N 324 
KMI C19 H14  sing N N 325 
KMI N02 H15  sing N N 326 
KMI N02 H16  sing N N 327 
KMI N18 H17  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                    9CVI 
_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]   0.020599 
_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]   0.008760 
_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]   0.006099 
_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  
FE 
N  
O  
S  
ZN 
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N  N   . ARG A 1 3   ? -38.760 -25.566 41.556 1.00 123.63 ? 299 ARG A N   1 
ATOM   2    C  CA  . ARG A 1 3   ? -38.266 -25.575 40.180 1.00 123.98 ? 299 ARG A CA  1 
ATOM   3    C  C   . ARG A 1 3   ? -38.922 -24.455 39.360 1.00 122.38 ? 299 ARG A C   1 
ATOM   4    O  O   . ARG A 1 3   ? -38.763 -24.373 38.142 1.00 125.36 ? 299 ARG A O   1 
ATOM   5    C  CB  . ARG A 1 3   ? -38.513 -26.956 39.539 1.00 130.67 ? 299 ARG A CB  1 
ATOM   6    C  CG  . ARG A 1 3   ? -37.722 -27.274 38.251 1.00 127.68 ? 299 ARG A CG  1 
ATOM   7    C  CD  . ARG A 1 3   ? -36.212 -27.498 38.463 1.00 127.16 ? 299 ARG A CD  1 
ATOM   8    N  NE  . ARG A 1 3   ? -35.555 -26.379 39.140 1.00 125.66 ? 299 ARG A NE  1 
ATOM   9    C  CZ  . ARG A 1 3   ? -35.012 -25.328 38.530 1.00 122.53 ? 299 ARG A CZ  1 
ATOM   10   N  NH1 . ARG A 1 3   ? -35.015 -25.245 37.206 1.00 125.78 ? 299 ARG A NH1 1 
ATOM   11   N  NH2 . ARG A 1 3   ? -34.455 -24.360 39.249 1.00 112.36 ? 299 ARG A NH2 1 
ATOM   12   N  N   . PHE A 1 4   ? -39.654 -23.584 40.055 1.00 116.88 ? 300 PHE A N   1 
ATOM   13   C  CA  . PHE A 1 4   ? -40.452 -22.528 39.439 1.00 110.76 ? 300 PHE A CA  1 
ATOM   14   C  C   . PHE A 1 4   ? -40.218 -21.229 40.217 1.00 110.44 ? 300 PHE A C   1 
ATOM   15   O  O   . PHE A 1 4   ? -41.124 -20.665 40.831 1.00 114.00 ? 300 PHE A O   1 
ATOM   16   C  CB  . PHE A 1 4   ? -41.930 -22.936 39.413 1.00 114.36 ? 300 PHE A CB  1 
ATOM   17   C  CG  . PHE A 1 4   ? -42.156 -24.416 39.148 1.00 120.47 ? 300 PHE A CG  1 
ATOM   18   C  CD1 . PHE A 1 4   ? -42.267 -25.324 40.206 1.00 117.46 ? 300 PHE A CD1 1 
ATOM   19   C  CD2 . PHE A 1 4   ? -42.257 -24.900 37.844 1.00 115.86 ? 300 PHE A CD2 1 
ATOM   20   C  CE1 . PHE A 1 4   ? -42.471 -26.678 39.964 1.00 117.56 ? 300 PHE A CE1 1 
ATOM   21   C  CE2 . PHE A 1 4   ? -42.461 -26.255 37.599 1.00 118.01 ? 300 PHE A CE2 1 
ATOM   22   C  CZ  . PHE A 1 4   ? -42.568 -27.142 38.661 1.00 121.21 ? 300 PHE A CZ  1 
ATOM   23   N  N   . LEU A 1 5   ? -38.973 -20.751 40.164 1.00 107.28 ? 301 LEU A N   1 
ATOM   24   C  CA  . LEU A 1 5   ? -38.428 -19.776 41.105 1.00 102.51 ? 301 LEU A CA  1 
ATOM   25   C  C   . LEU A 1 5   ? -39.076 -18.399 40.962 1.00 101.28 ? 301 LEU A C   1 
ATOM   26   O  O   . LEU A 1 5   ? -39.700 -18.065 39.951 1.00 98.43  ? 301 LEU A O   1 
ATOM   27   C  CB  . LEU A 1 5   ? -36.916 -19.652 40.916 1.00 99.62  ? 301 LEU A CB  1 
ATOM   28   C  CG  . LEU A 1 5   ? -36.182 -20.993 40.990 1.00 107.40 ? 301 LEU A CG  1 
ATOM   29   C  CD1 . LEU A 1 5   ? -34.886 -20.970 40.199 1.00 107.28 ? 301 LEU A CD1 1 
ATOM   30   C  CD2 . LEU A 1 5   ? -35.914 -21.349 42.432 1.00 107.42 ? 301 LEU A CD2 1 
ATOM   31   N  N   . LYS A 1 6   ? -38.889 -17.582 41.998 1.00 100.82 ? 302 LYS A N   1 
ATOM   32   C  CA  . LYS A 1 6   ? -39.568 -16.302 42.135 1.00 102.25 ? 302 LYS A CA  1 
ATOM   33   C  C   . LYS A 1 6   ? -38.551 -15.183 42.295 1.00 96.27  ? 302 LYS A C   1 
ATOM   34   O  O   . LYS A 1 6   ? -37.609 -15.302 43.087 1.00 84.70  ? 302 LYS A O   1 
ATOM   35   C  CB  . LYS A 1 6   ? -40.513 -16.316 43.337 1.00 106.72 ? 302 LYS A CB  1 
ATOM   36   C  CG  . LYS A 1 6   ? -41.565 -17.405 43.291 1.00 111.51 ? 302 LYS A CG  1 
ATOM   37   C  CD  . LYS A 1 6   ? -42.807 -16.955 42.545 1.00 115.29 ? 302 LYS A CD  1 
ATOM   38   C  CE  . LYS A 1 6   ? -43.847 -18.070 42.490 1.00 124.75 ? 302 LYS A CE  1 
ATOM   39   N  NZ  . LYS A 1 6   ? -44.139 -18.634 43.837 1.00 129.10 ? 302 LYS A NZ  1 
ATOM   40   N  N   . VAL A 1 7   ? -38.753 -14.096 41.553 1.00 97.90  ? 303 VAL A N   1 
ATOM   41   C  CA  . VAL A 1 7   ? -37.955 -12.884 41.685 1.00 93.03  ? 303 VAL A CA  1 
ATOM   42   C  C   . VAL A 1 7   ? -38.853 -11.773 42.208 1.00 92.40  ? 303 VAL A C   1 
ATOM   43   O  O   . VAL A 1 7   ? -39.970 -11.578 41.712 1.00 97.75  ? 303 VAL A O   1 
ATOM   44   C  CB  . VAL A 1 7   ? -37.303 -12.489 40.352 1.00 90.30  ? 303 VAL A CB  1 
ATOM   45   C  CG1 . VAL A 1 7   ? -36.375 -13.595 39.894 1.00 89.81  ? 303 VAL A CG1 1 
ATOM   46   C  CG2 . VAL A 1 7   ? -38.359 -12.199 39.298 1.00 90.94  ? 303 VAL A CG2 1 
ATOM   47   N  N   . LYS A 1 8   ? -38.371 -11.054 43.214 1.00 86.84  ? 304 LYS A N   1 
ATOM   48   C  CA  . LYS A 1 8   ? -39.135 -9.988  43.837 1.00 80.52  ? 304 LYS A CA  1 
ATOM   49   C  C   . LYS A 1 8   ? -38.569 -8.637  43.426 1.00 72.18  ? 304 LYS A C   1 
ATOM   50   O  O   . LYS A 1 8   ? -37.371 -8.503  43.160 1.00 71.74  ? 304 LYS A O   1 
ATOM   51   C  CB  . LYS A 1 8   ? -39.109 -10.119 45.360 1.00 81.73  ? 304 LYS A CB  1 
ATOM   52   C  CG  . LYS A 1 8   ? -40.177 -9.304  46.077 1.00 88.96  ? 304 LYS A CG  1 
ATOM   53   C  CD  . LYS A 1 8   ? -39.894 -9.182  47.559 1.00 82.85  ? 304 LYS A CD  1 
ATOM   54   C  CE  . LYS A 1 8   ? -40.902 -8.263  48.242 1.00 86.13  ? 304 LYS A CE  1 
ATOM   55   N  NZ  . LYS A 1 8   ? -40.592 -8.045  49.692 1.00 77.63  ? 304 LYS A NZ  1 
ATOM   56   N  N   . ASN A 1 9   ? -39.441 -7.640  43.352 1.00 65.85  ? 305 ASN A N   1 
ATOM   57   C  CA  . ASN A 1 9   ? -39.020 -6.249  43.273 1.00 72.27  ? 305 ASN A CA  1 
ATOM   58   C  C   . ASN A 1 9   ? -39.320 -5.611  44.621 1.00 84.69  ? 305 ASN A C   1 
ATOM   59   O  O   . ASN A 1 9   ? -40.427 -5.763  45.145 1.00 94.65  ? 305 ASN A O   1 
ATOM   60   C  CB  . ASN A 1 9   ? -39.728 -5.511  42.132 1.00 77.27  ? 305 ASN A CB  1 
ATOM   61   C  CG  . ASN A 1 9   ? -39.232 -4.087  41.963 1.00 80.00  ? 305 ASN A CG  1 
ATOM   62   O  OD1 . ASN A 1 9   ? -39.523 -3.227  42.787 1.00 83.09  ? 305 ASN A OD1 1 
ATOM   63   N  ND2 . ASN A 1 9   ? -38.483 -3.829  40.892 1.00 74.87  ? 305 ASN A ND2 1 
ATOM   64   N  N   . TRP A 1 10  ? -38.328 -4.935  45.203 1.00 85.21  ? 306 TRP A N   1 
ATOM   65   C  CA  . TRP A 1 10  ? -38.479 -4.418  46.559 1.00 87.82  ? 306 TRP A CA  1 
ATOM   66   C  C   . TRP A 1 10  ? -38.880 -2.950  46.613 1.00 92.78  ? 306 TRP A C   1 
ATOM   67   O  O   . TRP A 1 10  ? -39.311 -2.490  47.675 1.00 91.69  ? 306 TRP A O   1 
ATOM   68   C  CB  . TRP A 1 10  ? -37.187 -4.621  47.365 1.00 80.32  ? 306 TRP A CB  1 
ATOM   69   C  CG  . TRP A 1 10  ? -36.760 -6.054  47.420 1.00 77.44  ? 306 TRP A CG  1 
ATOM   70   C  CD1 . TRP A 1 10  ? -36.095 -6.740  46.458 1.00 74.19  ? 306 TRP A CD1 1 
ATOM   71   C  CD2 . TRP A 1 10  ? -36.976 -6.977  48.493 1.00 78.09  ? 306 TRP A CD2 1 
ATOM   72   N  NE1 . TRP A 1 10  ? -35.883 -8.035  46.857 1.00 68.86  ? 306 TRP A NE1 1 
ATOM   73   C  CE2 . TRP A 1 10  ? -36.414 -8.207  48.105 1.00 78.55  ? 306 TRP A CE2 1 
ATOM   74   C  CE3 . TRP A 1 10  ? -37.595 -6.887  49.737 1.00 72.19  ? 306 TRP A CE3 1 
ATOM   75   C  CZ2 . TRP A 1 10  ? -36.437 -9.336  48.926 1.00 76.22  ? 306 TRP A CZ2 1 
ATOM   76   C  CZ3 . TRP A 1 10  ? -37.623 -8.009  50.537 1.00 77.36  ? 306 TRP A CZ3 1 
ATOM   77   C  CH2 . TRP A 1 10  ? -37.055 -9.221  50.119 1.00 70.62  ? 306 TRP A CH2 1 
ATOM   78   N  N   . GLU A 1 11  ? -38.752 -2.200  45.510 1.00 91.13  ? 307 GLU A N   1 
ATOM   79   C  CA  . GLU A 1 11  ? -39.335 -0.860  45.490 1.00 91.99  ? 307 GLU A CA  1 
ATOM   80   C  C   . GLU A 1 11  ? -40.852 -0.931  45.345 1.00 99.23  ? 307 GLU A C   1 
ATOM   81   O  O   . GLU A 1 11  ? -41.561 -0.064  45.869 1.00 103.86 ? 307 GLU A O   1 
ATOM   82   C  CB  . GLU A 1 11  ? -38.725 -0.007  44.365 1.00 84.47  ? 307 GLU A CB  1 
ATOM   83   C  CG  . GLU A 1 11  ? -38.844 1.525   44.571 1.00 82.29  ? 307 GLU A CG  1 
ATOM   84   C  CD  . GLU A 1 11  ? -38.858 2.328   43.252 1.00 100.34 ? 307 GLU A CD  1 
ATOM   85   O  OE1 . GLU A 1 11  ? -39.670 3.274   43.143 1.00 108.47 ? 307 GLU A OE1 1 
ATOM   86   O  OE2 . GLU A 1 11  ? -38.073 2.018   42.324 1.00 99.95  ? 307 GLU A OE2 1 
ATOM   87   N  N   . THR A 1 12  ? -41.366 -1.975  44.672 1.00 97.06  ? 308 THR A N   1 
ATOM   88   C  CA  . THR A 1 12  ? -42.787 -2.097  44.355 1.00 93.55  ? 308 THR A CA  1 
ATOM   89   C  C   . THR A 1 12  ? -43.501 -3.245  45.067 1.00 99.15  ? 308 THR A C   1 
ATOM   90   O  O   . THR A 1 12  ? -44.739 -3.279  45.051 1.00 106.42 ? 308 THR A O   1 
ATOM   91   C  CB  . THR A 1 12  ? -42.983 -2.254  42.833 1.00 83.23  ? 308 THR A CB  1 
ATOM   92   O  OG1 . THR A 1 12  ? -42.397 -3.483  42.364 1.00 69.55  ? 308 THR A OG1 1 
ATOM   93   C  CG2 . THR A 1 12  ? -42.346 -1.085  42.097 1.00 77.61  ? 308 THR A CG2 1 
ATOM   94   N  N   . ASP A 1 13  ? -42.770 -4.169  45.696 1.00 97.34  ? 309 ASP A N   1 
ATOM   95   C  CA  . ASP A 1 13  ? -43.334 -5.375  46.310 1.00 100.18 ? 309 ASP A CA  1 
ATOM   96   C  C   . ASP A 1 13  ? -44.007 -6.279  45.285 1.00 103.41 ? 309 ASP A C   1 
ATOM   97   O  O   . ASP A 1 13  ? -44.855 -7.102  45.635 1.00 107.93 ? 309 ASP A O   1 
ATOM   98   C  CB  . ASP A 1 13  ? -44.320 -5.032  47.435 1.00 109.37 ? 309 ASP A CB  1 
ATOM   99   C  CG  . ASP A 1 13  ? -43.625 -4.729  48.752 1.00 108.94 ? 309 ASP A CG  1 
ATOM   100  O  OD1 . ASP A 1 13  ? -42.877 -5.599  49.245 1.00 107.60 ? 309 ASP A OD1 1 
ATOM   101  O  OD2 . ASP A 1 13  ? -43.823 -3.618  49.289 1.00 109.69 ? 309 ASP A OD2 1 
ATOM   102  N  N   . VAL A 1 14  ? -43.640 -6.133  44.031 1.00 103.33 ? 310 VAL A N   1 
ATOM   103  C  CA  . VAL A 1 14  ? -44.195 -6.918  42.936 1.00 103.85 ? 310 VAL A CA  1 
ATOM   104  C  C   . VAL A 1 14  ? -43.370 -8.183  42.765 1.00 101.83 ? 310 VAL A C   1 
ATOM   105  O  O   . VAL A 1 14  ? -42.143 -8.165  42.921 1.00 100.03 ? 310 VAL A O   1 
ATOM   106  C  CB  . VAL A 1 14  ? -44.217 -6.083  41.644 1.00 102.25 ? 310 VAL A CB  1 
ATOM   107  C  CG1 . VAL A 1 14  ? -44.417 -6.966  40.426 1.00 103.72 ? 310 VAL A CG1 1 
ATOM   108  C  CG2 . VAL A 1 14  ? -45.303 -5.025  41.728 1.00 103.95 ? 310 VAL A CG2 1 
ATOM   109  N  N   . VAL A 1 15  ? -44.042 -9.294  42.455 1.00 101.77 ? 311 VAL A N   1 
ATOM   110  C  CA  . VAL A 1 15  ? -43.376 -10.575 42.273 1.00 101.19 ? 311 VAL A CA  1 
ATOM   111  C  C   . VAL A 1 15  ? -43.763 -11.162 40.926 1.00 107.80 ? 311 VAL A C   1 
ATOM   112  O  O   . VAL A 1 15  ? -44.892 -10.996 40.454 1.00 114.66 ? 311 VAL A O   1 
ATOM   113  C  CB  . VAL A 1 15  ? -43.720 -11.576 43.391 1.00 101.59 ? 311 VAL A CB  1 
ATOM   114  C  CG1 . VAL A 1 15  ? -42.659 -12.671 43.461 1.00 99.08  ? 311 VAL A CG1 1 
ATOM   115  C  CG2 . VAL A 1 15  ? -43.883 -10.859 44.722 1.00 104.79 ? 311 VAL A CG2 1 
ATOM   116  N  N   . LEU A 1 16  ? -42.814 -11.867 40.315 1.00 108.59 ? 312 LEU A N   1 
ATOM   117  C  CA  . LEU A 1 16  ? -43.042 -12.613 39.087 1.00 107.57 ? 312 LEU A CA  1 
ATOM   118  C  C   . LEU A 1 16  ? -42.429 -14.000 39.229 1.00 105.40 ? 312 LEU A C   1 
ATOM   119  O  O   . LEU A 1 16  ? -41.530 -14.225 40.044 1.00 93.30  ? 312 LEU A O   1 
ATOM   120  C  CB  . LEU A 1 16  ? -42.459 -11.890 37.872 1.00 102.54 ? 312 LEU A CB  1 
ATOM   121  C  CG  . LEU A 1 16  ? -43.375 -10.864 37.198 1.00 107.32 ? 312 LEU A CG  1 
ATOM   122  C  CD1 . LEU A 1 16  ? -42.604 -10.042 36.167 1.00 95.31  ? 312 LEU A CD1 1 
ATOM   123  C  CD2 . LEU A 1 16  ? -44.575 -11.553 36.543 1.00 115.95 ? 312 LEU A CD2 1 
ATOM   124  N  N   . THR A 1 17  ? -42.927 -14.934 38.421 1.00 111.15 ? 313 THR A N   1 
ATOM   125  C  CA  . THR A 1 17  ? -42.524 -16.333 38.493 1.00 112.44 ? 313 THR A CA  1 
ATOM   126  C  C   . THR A 1 17  ? -41.731 -16.704 37.251 1.00 107.25 ? 313 THR A C   1 
ATOM   127  O  O   . THR A 1 17  ? -42.253 -16.636 36.133 1.00 113.31 ? 313 THR A O   1 
ATOM   128  C  CB  . THR A 1 17  ? -43.737 -17.249 38.623 1.00 123.08 ? 313 THR A CB  1 
ATOM   129  O  OG1 . THR A 1 17  ? -44.568 -16.796 39.697 1.00 128.07 ? 313 THR A OG1 1 
ATOM   130  C  CG2 . THR A 1 17  ? -43.282 -18.676 38.898 1.00 125.95 ? 313 THR A CG2 1 
ATOM   131  N  N   . ASP A 1 18  ? -40.485 -17.122 37.449 1.00 97.40  ? 314 ASP A N   1 
ATOM   132  C  CA  . ASP A 1 18  ? -39.626 -17.538 36.346 1.00 87.04  ? 314 ASP A CA  1 
ATOM   133  C  C   . ASP A 1 18  ? -39.736 -19.044 36.165 1.00 91.92  ? 314 ASP A C   1 
ATOM   134  O  O   . ASP A 1 18  ? -39.380 -19.813 37.065 1.00 95.62  ? 314 ASP A O   1 
ATOM   135  C  CB  . ASP A 1 18  ? -38.173 -17.142 36.602 1.00 76.23  ? 314 ASP A CB  1 
ATOM   136  C  CG  . ASP A 1 18  ? -37.357 -17.098 35.332 1.00 76.36  ? 314 ASP A CG  1 
ATOM   137  O  OD1 . ASP A 1 18  ? -37.176 -18.171 34.714 1.00 74.90  ? 314 ASP A OD1 1 
ATOM   138  O  OD2 . ASP A 1 18  ? -36.920 -15.991 34.939 1.00 74.75  ? 314 ASP A OD2 1 
ATOM   139  N  N   . THR A 1 19  ? -40.259 -19.464 35.021 1.00 92.27  ? 315 THR A N   1 
ATOM   140  C  CA  . THR A 1 19  ? -40.075 -20.831 34.564 1.00 93.75  ? 315 THR A CA  1 
ATOM   141  C  C   . THR A 1 19  ? -39.260 -20.917 33.290 1.00 86.50  ? 315 THR A C   1 
ATOM   142  O  O   . THR A 1 19  ? -38.846 -22.020 32.922 1.00 84.36  ? 315 THR A O   1 
ATOM   143  C  CB  . THR A 1 19  ? -41.420 -21.527 34.320 1.00 97.46  ? 315 THR A CB  1 
ATOM   144  O  OG1 . THR A 1 19  ? -42.342 -20.598 33.736 1.00 96.83  ? 315 THR A OG1 1 
ATOM   145  C  CG2 . THR A 1 19  ? -41.975 -22.087 35.617 1.00 98.30  ? 315 THR A CG2 1 
ATOM   146  N  N   . LEU A 1 20  ? -39.019 -19.790 32.610 1.00 77.93  ? 316 LEU A N   1 
ATOM   147  C  CA  . LEU A 1 20  ? -38.237 -19.808 31.381 1.00 83.29  ? 316 LEU A CA  1 
ATOM   148  C  C   . LEU A 1 20  ? -36.859 -20.407 31.611 1.00 83.98  ? 316 LEU A C   1 
ATOM   149  O  O   . LEU A 1 20  ? -36.266 -20.982 30.691 1.00 87.73  ? 316 LEU A O   1 
ATOM   150  C  CB  . LEU A 1 20  ? -38.114 -18.386 30.822 1.00 78.18  ? 316 LEU A CB  1 
ATOM   151  C  CG  . LEU A 1 20  ? -37.532 -18.225 29.421 1.00 72.42  ? 316 LEU A CG  1 
ATOM   152  C  CD1 . LEU A 1 20  ? -38.445 -18.878 28.377 1.00 70.18  ? 316 LEU A CD1 1 
ATOM   153  C  CD2 . LEU A 1 20  ? -37.294 -16.753 29.107 1.00 66.89  ? 316 LEU A CD2 1 
ATOM   154  N  N   . HIS A 1 21  ? -36.343 -20.296 32.838 1.00 69.96  ? 317 HIS A N   1 
ATOM   155  C  CA  . HIS A 1 21  ? -35.013 -20.803 33.144 1.00 66.99  ? 317 HIS A CA  1 
ATOM   156  C  C   . HIS A 1 21  ? -34.932 -22.318 33.029 1.00 72.83  ? 317 HIS A C   1 
ATOM   157  O  O   . HIS A 1 21  ? -33.826 -22.854 32.898 1.00 80.22  ? 317 HIS A O   1 
ATOM   158  C  CB  . HIS A 1 21  ? -34.591 -20.358 34.551 1.00 71.02  ? 317 HIS A CB  1 
ATOM   159  C  CG  . HIS A 1 21  ? -35.330 -21.049 35.649 1.00 75.51  ? 317 HIS A CG  1 
ATOM   160  N  ND1 . HIS A 1 21  ? -36.573 -20.639 36.085 1.00 83.32  ? 317 HIS A ND1 1 
ATOM   161  C  CD2 . HIS A 1 21  ? -35.005 -22.127 36.400 1.00 82.51  ? 317 HIS A CD2 1 
ATOM   162  C  CE1 . HIS A 1 21  ? -36.980 -21.434 37.059 1.00 85.23  ? 317 HIS A CE1 1 
ATOM   163  N  NE2 . HIS A 1 21  ? -36.047 -22.345 37.271 1.00 85.35  ? 317 HIS A NE2 1 
ATOM   164  N  N   . LEU A 1 22  ? -36.072 -23.017 33.091 1.00 73.32  ? 318 LEU A N   1 
ATOM   165  C  CA  . LEU A 1 22  ? -36.085 -24.453 32.822 1.00 89.69  ? 318 LEU A CA  1 
ATOM   166  C  C   . LEU A 1 22  ? -35.541 -24.767 31.432 1.00 89.95  ? 318 LEU A C   1 
ATOM   167  O  O   . LEU A 1 22  ? -34.927 -25.822 31.227 1.00 97.66  ? 318 LEU A O   1 
ATOM   168  C  CB  . LEU A 1 22  ? -37.508 -25.011 32.951 1.00 91.31  ? 318 LEU A CB  1 
ATOM   169  C  CG  . LEU A 1 22  ? -38.339 -24.826 34.219 1.00 87.72  ? 318 LEU A CG  1 
ATOM   170  C  CD1 . LEU A 1 22  ? -39.755 -25.383 34.040 1.00 84.71  ? 318 LEU A CD1 1 
ATOM   171  C  CD2 . LEU A 1 22  ? -37.643 -25.473 35.386 1.00 88.77  ? 318 LEU A CD2 1 
ATOM   172  N  N   . LYS A 1 23  ? -35.776 -23.880 30.462 1.00 85.84  ? 319 LYS A N   1 
ATOM   173  C  CA  . LYS A 1 23  ? -35.289 -24.092 29.104 1.00 87.18  ? 319 LYS A CA  1 
ATOM   174  C  C   . LYS A 1 23  ? -33.801 -23.804 28.972 1.00 91.81  ? 319 LYS A C   1 
ATOM   175  O  O   . LYS A 1 23  ? -33.235 -24.055 27.902 1.00 97.21  ? 319 LYS A O   1 
ATOM   176  C  CB  . LYS A 1 23  ? -36.078 -23.226 28.107 1.00 79.58  ? 319 LYS A CB  1 
ATOM   177  C  CG  . LYS A 1 23  ? -37.542 -23.637 27.887 1.00 84.06  ? 319 LYS A CG  1 
ATOM   178  C  CD  . LYS A 1 23  ? -37.677 -24.845 26.952 1.00 96.75  ? 319 LYS A CD  1 
ATOM   179  C  CE  . LYS A 1 23  ? -37.240 -24.534 25.507 1.00 96.17  ? 319 LYS A CE  1 
ATOM   180  N  NZ  . LYS A 1 23  ? -38.253 -23.773 24.717 1.00 91.63  ? 319 LYS A NZ  1 
ATOM   181  N  N   . SER A 1 24  ? -33.159 -23.297 30.025 1.00 88.08  ? 320 SER A N   1 
ATOM   182  C  CA  . SER A 1 24  ? -31.738 -22.988 29.959 1.00 94.21  ? 320 SER A CA  1 
ATOM   183  C  C   . SER A 1 24  ? -30.918 -24.249 29.729 1.00 101.84 ? 320 SER A C   1 
ATOM   184  O  O   . SER A 1 24  ? -31.369 -25.374 29.950 1.00 101.99 ? 320 SER A O   1 
ATOM   185  C  CB  . SER A 1 24  ? -31.252 -22.301 31.227 1.00 98.00  ? 320 SER A CB  1 
ATOM   186  O  OG  . SER A 1 24  ? -29.838 -22.192 31.193 1.00 101.15 ? 320 SER A OG  1 
ATOM   187  N  N   . THR A 1 25  ? -29.677 -24.038 29.305 1.00 107.46 ? 321 THR A N   1 
ATOM   188  C  CA  . THR A 1 25  ? -28.890 -25.121 28.744 1.00 115.23 ? 321 THR A CA  1 
ATOM   189  C  C   . THR A 1 25  ? -27.427 -24.983 29.148 1.00 106.89 ? 321 THR A C   1 
ATOM   190  O  O   . THR A 1 25  ? -26.850 -25.908 29.731 1.00 103.30 ? 321 THR A O   1 
ATOM   191  C  CB  . THR A 1 25  ? -29.074 -25.135 27.215 1.00 119.12 ? 321 THR A CB  1 
ATOM   192  O  OG1 . THR A 1 25  ? -28.045 -25.913 26.590 1.00 117.81 ? 321 THR A OG1 1 
ATOM   193  C  CG2 . THR A 1 25  ? -29.094 -23.703 26.647 1.00 114.35 ? 321 THR A CG2 1 
ATOM   194  N  N   . LEU A 1 26  ? -26.834 -23.825 28.867 1.00 103.45 ? 322 LEU A N   1 
ATOM   195  C  CA  . LEU A 1 26  ? -25.429 -23.588 29.148 1.00 104.20 ? 322 LEU A CA  1 
ATOM   196  C  C   . LEU A 1 26  ? -25.212 -23.309 30.635 1.00 97.54  ? 322 LEU A C   1 
ATOM   197  O  O   . LEU A 1 26  ? -26.127 -22.919 31.368 1.00 87.14  ? 322 LEU A O   1 
ATOM   198  C  CB  . LEU A 1 26  ? -24.909 -22.418 28.308 1.00 105.53 ? 322 LEU A CB  1 
ATOM   199  C  CG  . LEU A 1 26  ? -23.610 -22.600 27.512 1.00 111.78 ? 322 LEU A CG  1 
ATOM   200  C  CD1 . LEU A 1 26  ? -23.424 -21.443 26.535 1.00 114.69 ? 322 LEU A CD1 1 
ATOM   201  C  CD2 . LEU A 1 26  ? -22.389 -22.733 28.420 1.00 110.68 ? 322 LEU A CD2 1 
ATOM   202  N  N   . GLU A 1 27  ? -23.977 -23.517 31.073 1.00 96.82  ? 323 GLU A N   1 
ATOM   203  C  CA  . GLU A 1 27  ? -23.591 -23.288 32.453 1.00 98.09  ? 323 GLU A CA  1 
ATOM   204  C  C   . GLU A 1 27  ? -23.122 -21.845 32.645 1.00 93.61  ? 323 GLU A C   1 
ATOM   205  O  O   . GLU A 1 27  ? -22.768 -21.149 31.687 1.00 88.40  ? 323 GLU A O   1 
ATOM   206  C  CB  . GLU A 1 27  ? -22.512 -24.289 32.874 1.00 101.60 ? 323 GLU A CB  1 
ATOM   207  C  CG  . GLU A 1 27  ? -23.075 -25.690 33.099 1.00 110.35 ? 323 GLU A CG  1 
ATOM   208  C  CD  . GLU A 1 27  ? -22.006 -26.763 33.177 1.00 124.93 ? 323 GLU A CD  1 
ATOM   209  O  OE1 . GLU A 1 27  ? -21.146 -26.807 32.271 1.00 129.44 ? 323 GLU A OE1 1 
ATOM   210  O  OE2 . GLU A 1 27  ? -22.034 -27.564 34.140 1.00 130.16 ? 323 GLU A OE2 1 
ATOM   211  N  N   . THR A 1 28  ? -23.128 -21.405 33.916 1.00 82.72  ? 324 THR A N   1 
ATOM   212  C  CA  . THR A 1 28  ? -22.999 -19.997 34.284 1.00 72.60  ? 324 THR A CA  1 
ATOM   213  C  C   . THR A 1 28  ? -21.674 -19.617 34.937 1.00 73.95  ? 324 THR A C   1 
ATOM   214  O  O   . THR A 1 28  ? -21.364 -18.424 35.002 1.00 73.01  ? 324 THR A O   1 
ATOM   215  C  CB  . THR A 1 28  ? -24.122 -19.604 35.256 1.00 61.84  ? 324 THR A CB  1 
ATOM   216  O  OG1 . THR A 1 28  ? -23.988 -20.383 36.465 1.00 69.04  ? 324 THR A OG1 1 
ATOM   217  C  CG2 . THR A 1 28  ? -25.471 -19.903 34.647 1.00 67.58  ? 324 THR A CG2 1 
ATOM   218  N  N   . GLY A 1 29  ? -20.896 -20.584 35.432 1.00 78.30  ? 325 GLY A N   1 
ATOM   219  C  CA  . GLY A 1 29  ? -19.749 -20.329 36.278 1.00 79.83  ? 325 GLY A CA  1 
ATOM   220  C  C   . GLY A 1 29  ? -20.044 -20.514 37.755 1.00 81.15  ? 325 GLY A C   1 
ATOM   221  O  O   . GLY A 1 29  ? -19.132 -20.808 38.546 1.00 80.64  ? 325 GLY A O   1 
ATOM   222  N  N   . CYS A 1 30  ? -21.300 -20.353 38.141 1.00 79.49  ? 326 CYS A N   1 
ATOM   223  C  CA  . CYS A 1 30  ? -21.674 -20.526 39.525 1.00 75.73  ? 326 CYS A CA  1 
ATOM   224  C  C   . CYS A 1 30  ? -21.948 -21.997 39.794 1.00 76.84  ? 326 CYS A C   1 
ATOM   225  O  O   . CYS A 1 30  ? -22.487 -22.708 38.947 1.00 72.75  ? 326 CYS A O   1 
ATOM   226  C  CB  . CYS A 1 30  ? -22.898 -19.672 39.858 1.00 71.80  ? 326 CYS A CB  1 
ATOM   227  S  SG  . CYS A 1 30  ? -22.663 -17.903 39.547 1.00 63.58  ? 326 CYS A SG  1 
ATOM   228  N  N   . THR A 1 31  ? -21.521 -22.460 40.956 1.00 78.69  ? 327 THR A N   1 
ATOM   229  C  CA  . THR A 1 31  ? -21.839 -23.785 41.463 1.00 85.76  ? 327 THR A CA  1 
ATOM   230  C  C   . THR A 1 31  ? -22.816 -23.626 42.627 1.00 82.73  ? 327 THR A C   1 
ATOM   231  O  O   . THR A 1 31  ? -23.165 -22.509 43.014 1.00 82.64  ? 327 THR A O   1 
ATOM   232  C  CB  . THR A 1 31  ? -20.557 -24.514 41.868 1.00 88.26  ? 327 THR A CB  1 
ATOM   233  O  OG1 . THR A 1 31  ? -20.002 -23.887 43.029 1.00 82.66  ? 327 THR A OG1 1 
ATOM   234  C  CG2 . THR A 1 31  ? -19.540 -24.433 40.737 1.00 83.73  ? 327 THR A CG2 1 
ATOM   235  N  N   . GLU A 1 32  ? -23.278 -24.750 43.184 1.00 89.96  ? 328 GLU A N   1 
ATOM   236  C  CA  . GLU A 1 32  ? -24.180 -24.668 44.331 1.00 99.78  ? 328 GLU A CA  1 
ATOM   237  C  C   . GLU A 1 32  ? -23.525 -23.974 45.521 1.00 90.48  ? 328 GLU A C   1 
ATOM   238  O  O   . GLU A 1 32  ? -24.228 -23.536 46.436 1.00 86.61  ? 328 GLU A O   1 
ATOM   239  C  CB  . GLU A 1 32  ? -24.672 -26.065 44.740 1.00 116.42 ? 328 GLU A CB  1 
ATOM   240  C  CG  . GLU A 1 32  ? -25.673 -26.697 43.773 1.00 126.46 ? 328 GLU A CG  1 
ATOM   241  C  CD  . GLU A 1 32  ? -25.012 -27.595 42.744 1.00 133.55 ? 328 GLU A CD  1 
ATOM   242  O  OE1 . GLU A 1 32  ? -25.589 -28.657 42.417 1.00 138.77 ? 328 GLU A OE1 1 
ATOM   243  O  OE2 . GLU A 1 32  ? -23.911 -27.244 42.272 1.00 132.22 ? 328 GLU A OE2 1 
ATOM   244  N  N   . HIS A 1 33  ? -22.196 -23.838 45.508 1.00 82.12  ? 329 HIS A N   1 
ATOM   245  C  CA  . HIS A 1 33  ? -21.436 -23.332 46.637 1.00 80.49  ? 329 HIS A CA  1 
ATOM   246  C  C   . HIS A 1 33  ? -20.517 -22.174 46.252 1.00 84.62  ? 329 HIS A C   1 
ATOM   247  O  O   . HIS A 1 33  ? -19.634 -21.812 47.040 1.00 96.41  ? 329 HIS A O   1 
ATOM   248  C  CB  . HIS A 1 33  ? -20.632 -24.476 47.270 1.00 94.61  ? 329 HIS A CB  1 
ATOM   249  C  CG  . HIS A 1 33  ? -21.366 -25.788 47.306 1.00 106.83 ? 329 HIS A CG  1 
ATOM   250  N  ND1 . HIS A 1 33  ? -21.553 -26.571 46.184 1.00 108.73 ? 329 HIS A ND1 1 
ATOM   251  C  CD2 . HIS A 1 33  ? -21.957 -26.454 48.329 1.00 108.46 ? 329 HIS A CD2 1 
ATOM   252  C  CE1 . HIS A 1 33  ? -22.227 -27.659 46.512 1.00 111.72 ? 329 HIS A CE1 1 
ATOM   253  N  NE2 . HIS A 1 33  ? -22.485 -27.612 47.808 1.00 112.07 ? 329 HIS A NE2 1 
ATOM   254  N  N   . ILE A 1 34  ? -20.705 -21.570 45.078 1.00 73.43  ? 330 ILE A N   1 
ATOM   255  C  CA  . ILE A 1 34  ? -19.935 -20.390 44.698 1.00 72.34  ? 330 ILE A CA  1 
ATOM   256  C  C   . ILE A 1 34  ? -20.718 -19.606 43.659 1.00 67.53  ? 330 ILE A C   1 
ATOM   257  O  O   . ILE A 1 34  ? -21.396 -20.181 42.800 1.00 80.57  ? 330 ILE A O   1 
ATOM   258  C  CB  . ILE A 1 34  ? -18.520 -20.749 44.187 1.00 83.16  ? 330 ILE A CB  1 
ATOM   259  C  CG1 . ILE A 1 34  ? -17.602 -19.544 44.323 1.00 80.18  ? 330 ILE A CG1 1 
ATOM   260  C  CG2 . ILE A 1 34  ? -18.544 -21.158 42.715 1.00 96.11  ? 330 ILE A CG2 1 
ATOM   261  C  CD1 . ILE A 1 34  ? -16.161 -19.876 44.130 1.00 90.70  ? 330 ILE A CD1 1 
ATOM   262  N  N   . CYS A 1 35  ? -20.629 -18.280 43.751 1.00 60.02  ? 331 CYS A N   1 
ATOM   263  C  CA  . CYS A 1 35  ? -21.382 -17.375 42.898 1.00 66.60  ? 331 CYS A CA  1 
ATOM   264  C  C   . CYS A 1 35  ? -20.395 -16.510 42.133 1.00 66.61  ? 331 CYS A C   1 
ATOM   265  O  O   . CYS A 1 35  ? -19.592 -15.789 42.744 1.00 50.95  ? 331 CYS A O   1 
ATOM   266  C  CB  . CYS A 1 35  ? -22.349 -16.495 43.692 1.00 62.01  ? 331 CYS A CB  1 
ATOM   267  S  SG  . CYS A 1 35  ? -23.219 -15.309 42.588 1.00 57.60  ? 331 CYS A SG  1 
ATOM   268  N  N   . MET A 1 36  ? -20.454 -16.596 40.804 1.00 57.57  ? 332 MET A N   1 
ATOM   269  C  CA  . MET A 1 36  ? -19.549 -15.881 39.921 1.00 69.27  ? 332 MET A CA  1 
ATOM   270  C  C   . MET A 1 36  ? -20.210 -14.687 39.257 1.00 60.01  ? 332 MET A C   1 
ATOM   271  O  O   . MET A 1 36  ? -19.691 -14.181 38.260 1.00 53.55  ? 332 MET A O   1 
ATOM   272  C  CB  . MET A 1 36  ? -19.002 -16.825 38.850 1.00 88.34  ? 332 MET A CB  1 
ATOM   273  C  CG  . MET A 1 36  ? -18.155 -17.950 39.399 1.00 97.89  ? 332 MET A CG  1 
ATOM   274  S  SD  . MET A 1 36  ? -16.760 -18.248 38.307 1.00 103.40 ? 332 MET A SD  1 
ATOM   275  C  CE  . MET A 1 36  ? -15.674 -19.101 39.439 1.00 105.15 ? 332 MET A CE  1 
ATOM   276  N  N   . GLY A 1 37  ? -21.335 -14.219 39.783 1.00 60.34  ? 333 GLY A N   1 
ATOM   277  C  CA  . GLY A 1 37  ? -22.079 -13.156 39.130 1.00 67.26  ? 333 GLY A CA  1 
ATOM   278  C  C   . GLY A 1 37  ? -21.350 -11.866 38.785 1.00 62.65  ? 333 GLY A C   1 
ATOM   279  O  O   . GLY A 1 37  ? -21.943 -11.002 38.140 1.00 65.63  ? 333 GLY A O   1 
ATOM   280  N  N   . SER A 1 38  ? -20.094 -11.698 39.210 1.00 57.77  ? 334 SER A N   1 
ATOM   281  C  CA  . SER A 1 38  ? -19.360 -10.457 38.981 1.00 53.03  ? 334 SER A CA  1 
ATOM   282  C  C   . SER A 1 38  ? -18.042 -10.698 38.260 1.00 62.41  ? 334 SER A C   1 
ATOM   283  O  O   . SER A 1 38  ? -17.276 -9.742  38.049 1.00 61.06  ? 334 SER A O   1 
ATOM   284  C  CB  . SER A 1 38  ? -19.125 -9.692  40.292 1.00 55.13  ? 334 SER A CB  1 
ATOM   285  O  OG  . SER A 1 38  ? -18.235 -10.365 41.182 1.00 68.83  ? 334 SER A OG  1 
ATOM   286  N  N   . ILE A 1 39  ? -17.782 -11.938 37.847 1.00 65.63  ? 335 ILE A N   1 
ATOM   287  C  CA  . ILE A 1 39  ? -16.679 -12.244 36.947 1.00 67.32  ? 335 ILE A CA  1 
ATOM   288  C  C   . ILE A 1 39  ? -17.118 -11.919 35.524 1.00 74.46  ? 335 ILE A C   1 
ATOM   289  O  O   . ILE A 1 39  ? -18.165 -12.390 35.060 1.00 74.28  ? 335 ILE A O   1 
ATOM   290  C  CB  . ILE A 1 39  ? -16.260 -13.717 37.069 1.00 62.60  ? 335 ILE A CB  1 
ATOM   291  C  CG1 . ILE A 1 39  ? -16.294 -14.214 38.530 1.00 55.28  ? 335 ILE A CG1 1 
ATOM   292  C  CG2 . ILE A 1 39  ? -14.886 -13.911 36.482 1.00 66.09  ? 335 ILE A CG2 1 
ATOM   293  C  CD1 . ILE A 1 39  ? -15.446 -13.388 39.514 1.00 66.96  ? 335 ILE A CD1 1 
ATOM   294  N  N   . MET A 1 40  ? -16.304 -11.126 34.823 1.00 81.40  ? 336 MET A N   1 
ATOM   295  C  CA  . MET A 1 40  ? -16.723 -10.547 33.547 1.00 86.27  ? 336 MET A CA  1 
ATOM   296  C  C   . MET A 1 40  ? -16.948 -11.615 32.487 1.00 86.57  ? 336 MET A C   1 
ATOM   297  O  O   . MET A 1 40  ? -18.006 -11.655 31.846 1.00 91.91  ? 336 MET A O   1 
ATOM   298  C  CB  . MET A 1 40  ? -15.682 -9.540  33.064 1.00 87.60  ? 336 MET A CB  1 
ATOM   299  C  CG  . MET A 1 40  ? -15.768 -8.198  33.757 1.00 91.66  ? 336 MET A CG  1 
ATOM   300  S  SD  . MET A 1 40  ? -15.241 -6.849  32.681 1.00 99.94  ? 336 MET A SD  1 
ATOM   301  C  CE  . MET A 1 40  ? -16.050 -7.324  31.144 1.00 88.13  ? 336 MET A CE  1 
ATOM   302  N  N   . LEU A 1 41  ? -15.948 -12.467 32.266 1.00 90.88  ? 337 LEU A N   1 
ATOM   303  C  CA  . LEU A 1 41  ? -15.972 -13.486 31.219 1.00 92.73  ? 337 LEU A CA  1 
ATOM   304  C  C   . LEU A 1 41  ? -15.547 -14.811 31.835 1.00 100.99 ? 337 LEU A C   1 
ATOM   305  O  O   . LEU A 1 41  ? -14.347 -15.094 31.966 1.00 103.39 ? 337 LEU A O   1 
ATOM   306  C  CB  . LEU A 1 41  ? -15.054 -13.107 30.057 1.00 89.66  ? 337 LEU A CB  1 
ATOM   307  C  CG  . LEU A 1 41  ? -14.503 -11.673 30.027 1.00 88.58  ? 337 LEU A CG  1 
ATOM   308  C  CD1 . LEU A 1 41  ? -13.262 -11.572 29.142 1.00 95.12  ? 337 LEU A CD1 1 
ATOM   309  C  CD2 . LEU A 1 41  ? -15.559 -10.653 29.583 1.00 83.09  ? 337 LEU A CD2 1 
ATOM   310  N  N   . PRO A 1 42  ? -16.497 -15.632 32.263 1.00 108.22 ? 338 PRO A N   1 
ATOM   311  C  CA  . PRO A 1 42  ? -16.158 -16.996 32.676 1.00 114.11 ? 338 PRO A CA  1 
ATOM   312  C  C   . PRO A 1 42  ? -16.200 -17.960 31.499 1.00 115.24 ? 338 PRO A C   1 
ATOM   313  O  O   . PRO A 1 42  ? -16.928 -17.769 30.521 1.00 113.47 ? 338 PRO A O   1 
ATOM   314  C  CB  . PRO A 1 42  ? -17.247 -17.330 33.713 1.00 112.44 ? 338 PRO A CB  1 
ATOM   315  C  CG  . PRO A 1 42  ? -18.009 -16.027 33.950 1.00 107.27 ? 338 PRO A CG  1 
ATOM   316  C  CD  . PRO A 1 42  ? -17.857 -15.259 32.676 1.00 101.89 ? 338 PRO A CD  1 
ATOM   317  N  N   . SER A 1 43  ? -15.382 -19.006 31.597 1.00 120.75 ? 339 SER A N   1 
ATOM   318  C  CA  . SER A 1 43  ? -15.340 -20.041 30.562 1.00 117.24 ? 339 SER A CA  1 
ATOM   319  C  C   . SER A 1 43  ? -15.589 -21.411 31.182 1.00 114.52 ? 339 SER A C   1 
ATOM   320  O  O   . SER A 1 43  ? -16.694 -21.696 31.644 1.00 110.07 ? 339 SER A O   1 
ATOM   321  C  CB  . SER A 1 43  ? -13.995 -20.024 29.820 1.00 115.34 ? 339 SER A CB  1 
ATOM   322  O  OG  . SER A 1 43  ? -14.083 -20.667 28.557 1.00 107.92 ? 339 SER A OG  1 
ATOM   323  N  N   . VAL A 1 52  ? -13.521 -27.108 15.320 1.00 144.63 ? 348 VAL A N   1 
ATOM   324  C  CA  . VAL A 1 52  ? -14.735 -27.419 14.576 1.00 143.21 ? 348 VAL A CA  1 
ATOM   325  C  C   . VAL A 1 52  ? -15.720 -28.134 15.501 1.00 145.98 ? 348 VAL A C   1 
ATOM   326  O  O   . VAL A 1 52  ? -15.313 -28.827 16.436 1.00 149.96 ? 348 VAL A O   1 
ATOM   327  C  CB  . VAL A 1 52  ? -14.419 -28.265 13.303 1.00 143.06 ? 348 VAL A CB  1 
ATOM   328  C  CG1 . VAL A 1 52  ? -14.058 -29.707 13.666 1.00 147.29 ? 348 VAL A CG1 1 
ATOM   329  C  CG2 . VAL A 1 52  ? -15.577 -28.223 12.314 1.00 137.66 ? 348 VAL A CG2 1 
ATOM   330  N  N   . ALA A 1 53  ? -17.015 -27.944 15.250 1.00 140.38 ? 349 ALA A N   1 
ATOM   331  C  CA  . ALA A 1 53  ? -18.077 -28.621 15.987 1.00 137.16 ? 349 ALA A CA  1 
ATOM   332  C  C   . ALA A 1 53  ? -18.630 -29.766 15.145 1.00 136.62 ? 349 ALA A C   1 
ATOM   333  O  O   . ALA A 1 53  ? -18.961 -29.571 13.969 1.00 145.24 ? 349 ALA A O   1 
ATOM   334  C  CB  . ALA A 1 53  ? -19.194 -27.644 16.354 1.00 129.16 ? 349 ALA A CB  1 
ATOM   335  N  N   . THR A 1 54  ? -18.738 -30.953 15.748 1.00 126.38 ? 350 THR A N   1 
ATOM   336  C  CA  . THR A 1 54  ? -19.095 -32.161 15.012 1.00 124.72 ? 350 THR A CA  1 
ATOM   337  C  C   . THR A 1 54  ? -20.599 -32.224 14.734 1.00 118.69 ? 350 THR A C   1 
ATOM   338  O  O   . THR A 1 54  ? -21.398 -31.432 15.248 1.00 112.49 ? 350 THR A O   1 
ATOM   339  C  CB  . THR A 1 54  ? -18.667 -33.416 15.774 1.00 125.11 ? 350 THR A CB  1 
ATOM   340  O  OG1 . THR A 1 54  ? -19.773 -33.908 16.539 1.00 129.27 ? 350 THR A OG1 1 
ATOM   341  C  CG2 . THR A 1 54  ? -17.505 -33.110 16.712 1.00 120.25 ? 350 THR A CG2 1 
ATOM   342  N  N   . LYS A 1 55  ? -20.977 -33.205 13.906 1.00 124.78 ? 351 LYS A N   1 
ATOM   343  C  CA  . LYS A 1 55  ? -22.364 -33.388 13.495 1.00 130.67 ? 351 LYS A CA  1 
ATOM   344  C  C   . LYS A 1 55  ? -23.174 -34.149 14.530 1.00 140.64 ? 351 LYS A C   1 
ATOM   345  O  O   . LYS A 1 55  ? -24.401 -33.998 14.583 1.00 140.67 ? 351 LYS A O   1 
ATOM   346  C  CB  . LYS A 1 55  ? -22.413 -34.128 12.161 1.00 135.77 ? 351 LYS A CB  1 
ATOM   347  C  CG  . LYS A 1 55  ? -21.202 -35.005 11.942 1.00 139.71 ? 351 LYS A CG  1 
ATOM   348  C  CD  . LYS A 1 55  ? -21.588 -36.420 11.580 1.00 147.81 ? 351 LYS A CD  1 
ATOM   349  C  CE  . LYS A 1 55  ? -20.361 -37.318 11.572 1.00 155.62 ? 351 LYS A CE  1 
ATOM   350  N  NZ  . LYS A 1 55  ? -20.667 -38.711 11.135 1.00 161.34 ? 351 LYS A NZ  1 
ATOM   351  N  N   . ASP A 1 56  ? -22.509 -34.984 15.334 1.00 146.47 ? 352 ASP A N   1 
ATOM   352  C  CA  . ASP A 1 56  ? -23.182 -35.654 16.440 1.00 152.62 ? 352 ASP A CA  1 
ATOM   353  C  C   . ASP A 1 56  ? -23.791 -34.646 17.404 1.00 148.35 ? 352 ASP A C   1 
ATOM   354  O  O   . ASP A 1 56  ? -24.858 -34.897 17.977 1.00 155.45 ? 352 ASP A O   1 
ATOM   355  C  CB  . ASP A 1 56  ? -22.196 -36.565 17.176 1.00 158.65 ? 352 ASP A CB  1 
ATOM   356  C  CG  . ASP A 1 56  ? -21.399 -37.454 16.234 1.00 163.69 ? 352 ASP A CG  1 
ATOM   357  O  OD1 . ASP A 1 56  ? -21.915 -38.515 15.825 1.00 168.48 ? 352 ASP A OD1 1 
ATOM   358  O  OD2 . ASP A 1 56  ? -20.256 -37.082 15.891 1.00 162.93 ? 352 ASP A OD2 1 
ATOM   359  N  N   . GLN A 1 57  ? -23.132 -33.504 17.594 1.00 135.33 ? 353 GLN A N   1 
ATOM   360  C  CA  . GLN A 1 57  ? -23.633 -32.471 18.489 1.00 125.14 ? 353 GLN A CA  1 
ATOM   361  C  C   . GLN A 1 57  ? -24.454 -31.412 17.772 1.00 107.62 ? 353 GLN A C   1 
ATOM   362  O  O   . GLN A 1 57  ? -25.215 -30.689 18.431 1.00 102.06 ? 353 GLN A O   1 
ATOM   363  C  CB  . GLN A 1 57  ? -22.470 -31.783 19.214 1.00 130.72 ? 353 GLN A CB  1 
ATOM   364  C  CG  . GLN A 1 57  ? -21.118 -32.467 19.053 1.00 138.90 ? 353 GLN A CG  1 
ATOM   365  C  CD  . GLN A 1 57  ? -20.004 -31.488 18.716 1.00 139.08 ? 353 GLN A CD  1 
ATOM   366  O  OE1 . GLN A 1 57  ? -20.126 -30.691 17.786 1.00 138.80 ? 353 GLN A OE1 1 
ATOM   367  N  NE2 . GLN A 1 57  ? -18.914 -31.540 19.479 1.00 137.14 ? 353 GLN A NE2 1 
ATOM   368  N  N   . LEU A 1 58  ? -24.327 -31.309 16.444 1.00 100.26 ? 354 LEU A N   1 
ATOM   369  C  CA  . LEU A 1 58  ? -24.895 -30.184 15.718 1.00 95.14  ? 354 LEU A CA  1 
ATOM   370  C  C   . LEU A 1 58  ? -26.372 -30.357 15.396 1.00 103.17 ? 354 LEU A C   1 
ATOM   371  O  O   . LEU A 1 58  ? -27.057 -29.350 15.185 1.00 96.38  ? 354 LEU A O   1 
ATOM   372  C  CB  . LEU A 1 58  ? -24.118 -29.946 14.425 1.00 105.31 ? 354 LEU A CB  1 
ATOM   373  C  CG  . LEU A 1 58  ? -23.949 -28.490 13.983 1.00 102.89 ? 354 LEU A CG  1 
ATOM   374  C  CD1 . LEU A 1 58  ? -22.882 -27.806 14.808 1.00 98.63  ? 354 LEU A CD1 1 
ATOM   375  C  CD2 . LEU A 1 58  ? -23.605 -28.435 12.499 1.00 105.70 ? 354 LEU A CD2 1 
ATOM   376  N  N   . PHE A 1 59  ? -26.886 -31.597 15.332 1.00 111.07 ? 355 PHE A N   1 
ATOM   377  C  CA  . PHE A 1 59  ? -28.315 -31.716 15.050 1.00 120.46 ? 355 PHE A CA  1 
ATOM   378  C  C   . PHE A 1 59  ? -29.167 -31.491 16.300 1.00 124.16 ? 355 PHE A C   1 
ATOM   379  O  O   . PHE A 1 59  ? -30.226 -30.861 16.194 1.00 130.84 ? 355 PHE A O   1 
ATOM   380  C  CB  . PHE A 1 59  ? -28.685 -33.061 14.419 1.00 129.49 ? 355 PHE A CB  1 
ATOM   381  C  CG  . PHE A 1 59  ? -30.149 -33.164 14.082 1.00 134.11 ? 355 PHE A CG  1 
ATOM   382  C  CD1 . PHE A 1 59  ? -30.651 -32.560 12.937 1.00 137.48 ? 355 PHE A CD1 1 
ATOM   383  C  CD2 . PHE A 1 59  ? -31.031 -33.825 14.924 1.00 134.22 ? 355 PHE A CD2 1 
ATOM   384  C  CE1 . PHE A 1 59  ? -31.999 -32.629 12.630 1.00 140.34 ? 355 PHE A CE1 1 
ATOM   385  C  CE2 . PHE A 1 59  ? -32.381 -33.898 14.621 1.00 137.30 ? 355 PHE A CE2 1 
ATOM   386  C  CZ  . PHE A 1 59  ? -32.865 -33.302 13.473 1.00 141.52 ? 355 PHE A CZ  1 
ATOM   387  N  N   . PRO A 1 60  ? -28.790 -32.012 17.480 1.00 120.14 ? 356 PRO A N   1 
ATOM   388  C  CA  . PRO A 1 60  ? -29.488 -31.587 18.709 1.00 107.31 ? 356 PRO A CA  1 
ATOM   389  C  C   . PRO A 1 60  ? -29.706 -30.084 18.814 1.00 93.64  ? 356 PRO A C   1 
ATOM   390  O  O   . PRO A 1 60  ? -30.842 -29.650 19.045 1.00 91.29  ? 356 PRO A O   1 
ATOM   391  C  CB  . PRO A 1 60  ? -28.573 -32.113 19.827 1.00 110.25 ? 356 PRO A CB  1 
ATOM   392  C  CG  . PRO A 1 60  ? -27.527 -33.006 19.138 1.00 115.98 ? 356 PRO A CG  1 
ATOM   393  C  CD  . PRO A 1 60  ? -27.983 -33.218 17.733 1.00 120.09 ? 356 PRO A CD  1 
ATOM   394  N  N   . LEU A 1 61  ? -28.645 -29.281 18.649 1.00 84.03  ? 357 LEU A N   1 
ATOM   395  C  CA  . LEU A 1 61  ? -28.775 -27.821 18.614 1.00 72.42  ? 357 LEU A CA  1 
ATOM   396  C  C   . LEU A 1 61  ? -29.658 -27.343 17.457 1.00 87.88  ? 357 LEU A C   1 
ATOM   397  O  O   . LEU A 1 61  ? -30.435 -26.392 17.618 1.00 89.90  ? 357 LEU A O   1 
ATOM   398  C  CB  . LEU A 1 61  ? -27.394 -27.179 18.498 1.00 66.44  ? 357 LEU A CB  1 
ATOM   399  C  CG  . LEU A 1 61  ? -26.313 -27.701 19.448 1.00 83.02  ? 357 LEU A CG  1 
ATOM   400  C  CD1 . LEU A 1 61  ? -24.934 -27.549 18.837 1.00 95.17  ? 357 LEU A CD1 1 
ATOM   401  C  CD2 . LEU A 1 61  ? -26.372 -26.986 20.809 1.00 82.66  ? 357 LEU A CD2 1 
ATOM   402  N  N   . ALA A 1 62  ? -29.514 -27.947 16.267 1.00 81.32  ? 358 ALA A N   1 
ATOM   403  C  CA  . ALA A 1 62  ? -30.387 -27.593 15.150 1.00 79.88  ? 358 ALA A CA  1 
ATOM   404  C  C   . ALA A 1 62  ? -31.827 -28.004 15.433 1.00 87.36  ? 358 ALA A C   1 
ATOM   405  O  O   . ALA A 1 62  ? -32.769 -27.282 15.084 1.00 83.75  ? 358 ALA A O   1 
ATOM   406  C  CB  . ALA A 1 62  ? -29.891 -28.249 13.856 1.00 89.62  ? 358 ALA A CB  1 
ATOM   407  N  N   . LYS A 1 63  ? -32.009 -29.157 16.081 1.00 101.93 ? 359 LYS A N   1 
ATOM   408  C  CA  . LYS A 1 63  ? -33.340 -29.616 16.470 1.00 105.96 ? 359 LYS A CA  1 
ATOM   409  C  C   . LYS A 1 63  ? -33.979 -28.660 17.469 1.00 103.57 ? 359 LYS A C   1 
ATOM   410  O  O   . LYS A 1 63  ? -35.109 -28.200 17.272 1.00 108.34 ? 359 LYS A O   1 
ATOM   411  C  CB  . LYS A 1 63  ? -33.246 -31.025 17.055 1.00 104.19 ? 359 LYS A CB  1 
ATOM   412  C  CG  . LYS A 1 63  ? -34.573 -31.704 17.284 1.00 104.85 ? 359 LYS A CG  1 
ATOM   413  C  CD  . LYS A 1 63  ? -34.373 -33.035 17.981 1.00 110.34 ? 359 LYS A CD  1 
ATOM   414  C  CE  . LYS A 1 63  ? -35.604 -33.901 17.843 1.00 106.36 ? 359 LYS A CE  1 
ATOM   415  N  NZ  . LYS A 1 63  ? -36.829 -33.112 18.136 1.00 99.43  ? 359 LYS A NZ  1 
ATOM   416  N  N   . GLU A 1 64  ? -33.264 -28.343 18.549 1.00 96.15  ? 360 GLU A N   1 
ATOM   417  C  CA  . GLU A 1 64  ? -33.802 -27.446 19.565 1.00 90.48  ? 360 GLU A CA  1 
ATOM   418  C  C   . GLU A 1 64  ? -34.233 -26.112 18.954 1.00 86.88  ? 360 GLU A C   1 
ATOM   419  O  O   . GLU A 1 64  ? -35.362 -25.658 19.167 1.00 83.33  ? 360 GLU A O   1 
ATOM   420  C  CB  . GLU A 1 64  ? -32.760 -27.243 20.669 1.00 91.60  ? 360 GLU A CB  1 
ATOM   421  C  CG  . GLU A 1 64  ? -33.175 -26.303 21.784 1.00 95.03  ? 360 GLU A CG  1 
ATOM   422  C  CD  . GLU A 1 64  ? -31.982 -25.619 22.431 1.00 95.13  ? 360 GLU A CD  1 
ATOM   423  O  OE1 . GLU A 1 64  ? -30.873 -26.195 22.379 1.00 91.91  ? 360 GLU A OE1 1 
ATOM   424  O  OE2 . GLU A 1 64  ? -32.152 -24.504 22.975 1.00 92.58  ? 360 GLU A OE2 1 
ATOM   425  N  N   . PHE A 1 65  ? -33.353 -25.487 18.166 1.00 80.86  ? 361 PHE A N   1 
ATOM   426  C  CA  . PHE A 1 65  ? -33.666 -24.193 17.562 1.00 76.41  ? 361 PHE A CA  1 
ATOM   427  C  C   . PHE A 1 65  ? -34.937 -24.265 16.727 1.00 81.40  ? 361 PHE A C   1 
ATOM   428  O  O   . PHE A 1 65  ? -35.890 -23.509 16.955 1.00 73.76  ? 361 PHE A O   1 
ATOM   429  C  CB  . PHE A 1 65  ? -32.499 -23.715 16.694 1.00 76.50  ? 361 PHE A CB  1 
ATOM   430  C  CG  . PHE A 1 65  ? -32.790 -22.453 15.925 1.00 73.84  ? 361 PHE A CG  1 
ATOM   431  C  CD1 . PHE A 1 65  ? -32.696 -21.216 16.541 1.00 64.14  ? 361 PHE A CD1 1 
ATOM   432  C  CD2 . PHE A 1 65  ? -33.149 -22.504 14.585 1.00 74.72  ? 361 PHE A CD2 1 
ATOM   433  C  CE1 . PHE A 1 65  ? -32.959 -20.054 15.838 1.00 68.05  ? 361 PHE A CE1 1 
ATOM   434  C  CE2 . PHE A 1 65  ? -33.415 -21.338 13.874 1.00 74.65  ? 361 PHE A CE2 1 
ATOM   435  C  CZ  . PHE A 1 65  ? -33.316 -20.108 14.515 1.00 71.04  ? 361 PHE A CZ  1 
ATOM   436  N  N   . LEU A 1 66  ? -34.962 -25.177 15.744 1.00 85.39  ? 362 LEU A N   1 
ATOM   437  C  CA  . LEU A 1 66  ? -36.082 -25.239 14.815 1.00 87.97  ? 362 LEU A CA  1 
ATOM   438  C  C   . LEU A 1 66  ? -37.384 -25.574 15.524 1.00 94.51  ? 362 LEU A C   1 
ATOM   439  O  O   . LEU A 1 66  ? -38.458 -25.133 15.099 1.00 96.95  ? 362 LEU A O   1 
ATOM   440  C  CB  . LEU A 1 66  ? -35.795 -26.270 13.724 1.00 98.86  ? 362 LEU A CB  1 
ATOM   441  C  CG  . LEU A 1 66  ? -34.581 -26.016 12.829 1.00 99.48  ? 362 LEU A CG  1 
ATOM   442  C  CD1 . LEU A 1 66  ? -34.241 -27.283 12.079 1.00 106.42 ? 362 LEU A CD1 1 
ATOM   443  C  CD2 . LEU A 1 66  ? -34.857 -24.876 11.869 1.00 97.62  ? 362 LEU A CD2 1 
ATOM   444  N  N   . ASP A 1 67  ? -37.311 -26.356 16.600 1.00 100.46 ? 363 ASP A N   1 
ATOM   445  C  CA  . ASP A 1 67  ? -38.519 -26.718 17.330 1.00 112.30 ? 363 ASP A CA  1 
ATOM   446  C  C   . ASP A 1 67  ? -39.182 -25.495 17.954 1.00 111.61 ? 363 ASP A C   1 
ATOM   447  O  O   . ASP A 1 67  ? -40.404 -25.340 17.870 1.00 114.59 ? 363 ASP A O   1 
ATOM   448  C  CB  . ASP A 1 67  ? -38.186 -27.770 18.383 1.00 117.68 ? 363 ASP A CB  1 
ATOM   449  C  CG  . ASP A 1 67  ? -38.255 -29.181 17.836 1.00 126.09 ? 363 ASP A CG  1 
ATOM   450  O  OD1 . ASP A 1 67  ? -39.374 -29.723 17.741 1.00 133.20 ? 363 ASP A OD1 1 
ATOM   451  O  OD2 . ASP A 1 67  ? -37.200 -29.746 17.479 1.00 127.69 ? 363 ASP A OD2 1 
ATOM   452  N  N   . GLN A 1 68  ? -38.399 -24.604 18.567 1.00 109.74 ? 364 GLN A N   1 
ATOM   453  C  CA  . GLN A 1 68  ? -38.979 -23.388 19.127 1.00 109.20 ? 364 GLN A CA  1 
ATOM   454  C  C   . GLN A 1 68  ? -39.273 -22.346 18.057 1.00 107.16 ? 364 GLN A C   1 
ATOM   455  O  O   . GLN A 1 68  ? -40.055 -21.423 18.310 1.00 112.94 ? 364 GLN A O   1 
ATOM   456  C  CB  . GLN A 1 68  ? -38.057 -22.799 20.208 1.00 102.80 ? 364 GLN A CB  1 
ATOM   457  C  CG  . GLN A 1 68  ? -36.840 -22.053 19.676 1.00 100.98 ? 364 GLN A CG  1 
ATOM   458  C  CD  . GLN A 1 68  ? -35.631 -22.147 20.593 1.00 98.83  ? 364 GLN A CD  1 
ATOM   459  O  OE1 . GLN A 1 68  ? -35.507 -23.085 21.379 1.00 99.04  ? 364 GLN A OE1 1 
ATOM   460  N  NE2 . GLN A 1 68  ? -34.727 -21.172 20.488 1.00 94.70  ? 364 GLN A NE2 1 
ATOM   461  N  N   . TYR A 1 69  ? -38.680 -22.479 16.868 1.00 98.49  ? 365 TYR A N   1 
ATOM   462  C  CA  . TYR A 1 69  ? -38.942 -21.524 15.796 1.00 94.21  ? 365 TYR A CA  1 
ATOM   463  C  C   . TYR A 1 69  ? -40.284 -21.788 15.116 1.00 102.44 ? 365 TYR A C   1 
ATOM   464  O  O   . TYR A 1 69  ? -40.979 -20.843 14.718 1.00 96.85  ? 365 TYR A O   1 
ATOM   465  C  CB  . TYR A 1 69  ? -37.810 -21.552 14.766 1.00 86.92  ? 365 TYR A CB  1 
ATOM   466  C  CG  . TYR A 1 69  ? -38.215 -20.897 13.474 1.00 90.49  ? 365 TYR A CG  1 
ATOM   467  C  CD1 . TYR A 1 69  ? -38.475 -19.535 13.424 1.00 90.06  ? 365 TYR A CD1 1 
ATOM   468  C  CD2 . TYR A 1 69  ? -38.368 -21.640 12.307 1.00 90.62  ? 365 TYR A CD2 1 
ATOM   469  C  CE1 . TYR A 1 69  ? -38.860 -18.932 12.260 1.00 88.86  ? 365 TYR A CE1 1 
ATOM   470  C  CE2 . TYR A 1 69  ? -38.754 -21.040 11.137 1.00 90.48  ? 365 TYR A CE2 1 
ATOM   471  C  CZ  . TYR A 1 69  ? -38.997 -19.683 11.120 1.00 91.35  ? 365 TYR A CZ  1 
ATOM   472  O  OH  . TYR A 1 69  ? -39.387 -19.059 9.962  1.00 101.30 ? 365 TYR A OH  1 
ATOM   473  N  N   . TYR A 1 70  ? -40.651 -23.063 14.947 1.00 110.50 ? 366 TYR A N   1 
ATOM   474  C  CA  . TYR A 1 70  ? -41.997 -23.392 14.494 1.00 117.38 ? 366 TYR A CA  1 
ATOM   475  C  C   . TYR A 1 70  ? -43.000 -23.310 15.635 1.00 125.72 ? 366 TYR A C   1 
ATOM   476  O  O   . TYR A 1 70  ? -44.177 -23.010 15.402 1.00 132.14 ? 366 TYR A O   1 
ATOM   477  C  CB  . TYR A 1 70  ? -42.015 -24.778 13.840 1.00 119.07 ? 366 TYR A CB  1 
ATOM   478  C  CG  . TYR A 1 70  ? -41.411 -24.757 12.454 1.00 116.38 ? 366 TYR A CG  1 
ATOM   479  C  CD1 . TYR A 1 70  ? -40.123 -25.226 12.222 1.00 111.22 ? 366 TYR A CD1 1 
ATOM   480  C  CD2 . TYR A 1 70  ? -42.115 -24.223 11.385 1.00 116.39 ? 366 TYR A CD2 1 
ATOM   481  C  CE1 . TYR A 1 70  ? -39.566 -25.184 10.957 1.00 108.75 ? 366 TYR A CE1 1 
ATOM   482  C  CE2 . TYR A 1 70  ? -41.570 -24.176 10.123 1.00 116.70 ? 366 TYR A CE2 1 
ATOM   483  C  CZ  . TYR A 1 70  ? -40.298 -24.657 9.910  1.00 114.23 ? 366 TYR A CZ  1 
ATOM   484  O  OH  . TYR A 1 70  ? -39.768 -24.598 8.639  1.00 113.30 ? 366 TYR A OH  1 
ATOM   485  N  N   . SER A 1 71  ? -42.549 -23.539 16.871 1.00 124.27 ? 367 SER A N   1 
ATOM   486  C  CA  . SER A 1 71  ? -43.371 -23.319 18.052 1.00 123.42 ? 367 SER A CA  1 
ATOM   487  C  C   . SER A 1 71  ? -43.476 -21.845 18.412 1.00 120.25 ? 367 SER A C   1 
ATOM   488  O  O   . SER A 1 71  ? -43.999 -21.519 19.482 1.00 123.79 ? 367 SER A O   1 
ATOM   489  C  CB  . SER A 1 71  ? -42.821 -24.121 19.237 1.00 121.76 ? 367 SER A CB  1 
ATOM   490  O  OG  . SER A 1 71  ? -43.657 -24.010 20.379 1.00 122.34 ? 367 SER A OG  1 
ATOM   491  N  N   . SER A 1 72  ? -42.983 -20.954 17.553 1.00 110.18 ? 368 SER A N   1 
ATOM   492  C  CA  . SER A 1 72  ? -43.247 -19.528 17.665 1.00 108.27 ? 368 SER A CA  1 
ATOM   493  C  C   . SER A 1 72  ? -44.307 -19.063 16.679 1.00 116.94 ? 368 SER A C   1 
ATOM   494  O  O   . SER A 1 72  ? -45.101 -18.176 17.008 1.00 121.80 ? 368 SER A O   1 
ATOM   495  C  CB  . SER A 1 72  ? -41.961 -18.713 17.454 1.00 101.03 ? 368 SER A CB  1 
ATOM   496  O  OG  . SER A 1 72  ? -41.775 -18.337 16.091 1.00 104.74 ? 368 SER A OG  1 
ATOM   497  N  N   . ILE A 1 73  ? -44.347 -19.658 15.485 1.00 119.34 ? 369 ILE A N   1 
ATOM   498  C  CA  . ILE A 1 73  ? -45.261 -19.268 14.417 1.00 122.60 ? 369 ILE A CA  1 
ATOM   499  C  C   . ILE A 1 73  ? -46.477 -20.184 14.415 1.00 132.15 ? 369 ILE A C   1 
ATOM   500  O  O   . ILE A 1 73  ? -47.133 -20.360 13.382 1.00 135.79 ? 369 ILE A O   1 
ATOM   501  C  CB  . ILE A 1 73  ? -44.560 -19.290 13.047 1.00 121.44 ? 369 ILE A CB  1 
ATOM   502  C  CG1 . ILE A 1 73  ? -43.687 -20.541 12.912 1.00 122.65 ? 369 ILE A CG1 1 
ATOM   503  C  CG2 . ILE A 1 73  ? -43.736 -18.026 12.834 1.00 114.70 ? 369 ILE A CG2 1 
ATOM   504  C  CD1 . ILE A 1 73  ? -42.794 -20.527 11.697 1.00 118.97 ? 369 ILE A CD1 1 
ATOM   505  N  N   . LYS A 1 74  ? -46.773 -20.781 15.571 1.00 134.00 ? 370 LYS A N   1 
ATOM   506  C  CA  . LYS A 1 74  ? -47.982 -21.579 15.775 1.00 137.92 ? 370 LYS A CA  1 
ATOM   507  C  C   . LYS A 1 74  ? -48.139 -22.654 14.700 1.00 135.63 ? 370 LYS A C   1 
ATOM   508  O  O   . LYS A 1 74  ? -49.238 -22.921 14.207 1.00 140.55 ? 370 LYS A O   1 
ATOM   509  C  CB  . LYS A 1 74  ? -49.213 -20.675 15.858 1.00 141.16 ? 370 LYS A CB  1 
ATOM   510  C  CG  . LYS A 1 74  ? -49.219 -19.794 17.109 1.00 137.72 ? 370 LYS A CG  1 
ATOM   511  C  CD  . LYS A 1 74  ? -50.117 -18.580 16.952 1.00 134.06 ? 370 LYS A CD  1 
ATOM   512  C  CE  . LYS A 1 74  ? -49.796 -17.525 17.998 1.00 122.40 ? 370 LYS A CE  1 
ATOM   513  N  NZ  . LYS A 1 74  ? -50.477 -16.234 17.710 1.00 119.10 ? 370 LYS A NZ  1 
ATOM   514  N  N   . ARG A 1 75  ? -47.009 -23.264 14.320 1.00 129.40 ? 371 ARG A N   1 
ATOM   515  C  CA  . ARG A 1 75  ? -46.988 -24.456 13.479 1.00 128.39 ? 371 ARG A CA  1 
ATOM   516  C  C   . ARG A 1 75  ? -46.005 -25.485 14.028 1.00 138.47 ? 371 ARG A C   1 
ATOM   517  O  O   . ARG A 1 75  ? -45.371 -26.225 13.264 1.00 140.71 ? 371 ARG A O   1 
ATOM   518  C  CB  . ARG A 1 75  ? -46.661 -24.101 12.034 1.00 111.91 ? 371 ARG A CB  1 
ATOM   519  C  CG  . ARG A 1 75  ? -47.751 -23.285 11.384 1.00 112.42 ? 371 ARG A CG  1 
ATOM   520  C  CD  . ARG A 1 75  ? -47.174 -22.369 10.335 1.00 116.79 ? 371 ARG A CD  1 
ATOM   521  N  NE  . ARG A 1 75  ? -48.087 -22.178 9.215  1.00 122.58 ? 371 ARG A NE  1 
ATOM   522  C  CZ  . ARG A 1 75  ? -48.239 -23.045 8.222  1.00 129.55 ? 371 ARG A CZ  1 
ATOM   523  N  NH1 . ARG A 1 75  ? -49.090 -22.785 7.241  1.00 129.83 ? 371 ARG A NH1 1 
ATOM   524  N  NH2 . ARG A 1 75  ? -47.544 -24.175 8.212  1.00 136.11 ? 371 ARG A NH2 1 
ATOM   525  N  N   . PHE A 1 76  ? -45.861 -25.511 15.352 1.00 142.89 ? 372 PHE A N   1 
ATOM   526  C  CA  . PHE A 1 76  ? -45.111 -26.542 16.056 1.00 150.42 ? 372 PHE A CA  1 
ATOM   527  C  C   . PHE A 1 76  ? -45.611 -27.928 15.667 1.00 163.14 ? 372 PHE A C   1 
ATOM   528  O  O   . PHE A 1 76  ? -46.818 -28.173 15.594 1.00 171.12 ? 372 PHE A O   1 
ATOM   529  C  CB  . PHE A 1 76  ? -45.268 -26.304 17.566 1.00 147.57 ? 372 PHE A CB  1 
ATOM   530  C  CG  . PHE A 1 76  ? -44.590 -27.321 18.450 1.00 144.75 ? 372 PHE A CG  1 
ATOM   531  C  CD1 . PHE A 1 76  ? -43.446 -27.991 18.048 1.00 141.22 ? 372 PHE A CD1 1 
ATOM   532  C  CD2 . PHE A 1 76  ? -45.103 -27.584 19.711 1.00 147.47 ? 372 PHE A CD2 1 
ATOM   533  C  CE1 . PHE A 1 76  ? -42.843 -28.917 18.876 1.00 141.57 ? 372 PHE A CE1 1 
ATOM   534  C  CE2 . PHE A 1 76  ? -44.502 -28.501 20.545 1.00 149.33 ? 372 PHE A CE2 1 
ATOM   535  C  CZ  . PHE A 1 76  ? -43.369 -29.169 20.127 1.00 147.62 ? 372 PHE A CZ  1 
ATOM   536  N  N   . GLY A 1 77  ? -44.670 -28.833 15.393 1.00 162.82 ? 373 GLY A N   1 
ATOM   537  C  CA  . GLY A 1 77  ? -44.977 -30.232 15.172 1.00 165.49 ? 373 GLY A CA  1 
ATOM   538  C  C   . GLY A 1 77  ? -45.617 -30.571 13.845 1.00 160.85 ? 373 GLY A C   1 
ATOM   539  O  O   . GLY A 1 77  ? -45.764 -31.763 13.538 1.00 169.50 ? 373 GLY A O   1 
ATOM   540  N  N   . SER A 1 78  ? -46.003 -29.578 13.048 1.00 146.34 ? 374 SER A N   1 
ATOM   541  C  CA  . SER A 1 78  ? -46.616 -29.848 11.762 1.00 138.39 ? 374 SER A CA  1 
ATOM   542  C  C   . SER A 1 78  ? -45.621 -30.556 10.845 1.00 132.92 ? 374 SER A C   1 
ATOM   543  O  O   . SER A 1 78  ? -44.449 -30.752 11.180 1.00 124.81 ? 374 SER A O   1 
ATOM   544  C  CB  . SER A 1 78  ? -47.098 -28.547 11.118 1.00 133.99 ? 374 SER A CB  1 
ATOM   545  O  OG  . SER A 1 78  ? -46.034 -27.618 10.985 1.00 127.51 ? 374 SER A OG  1 
ATOM   546  N  N   . LYS A 1 79  ? -46.112 -30.956 9.668  1.00 134.12 ? 375 LYS A N   1 
ATOM   547  C  CA  . LYS A 1 79  ? -45.221 -31.536 8.668  1.00 133.03 ? 375 LYS A CA  1 
ATOM   548  C  C   . LYS A 1 79  ? -44.300 -30.471 8.081  1.00 120.17 ? 375 LYS A C   1 
ATOM   549  O  O   . LYS A 1 79  ? -43.128 -30.747 7.801  1.00 115.26 ? 375 LYS A O   1 
ATOM   550  C  CB  . LYS A 1 79  ? -46.032 -32.230 7.570  1.00 143.47 ? 375 LYS A CB  1 
ATOM   551  C  CG  . LYS A 1 79  ? -45.219 -33.119 6.618  1.00 144.64 ? 375 LYS A CG  1 
ATOM   552  C  CD  . LYS A 1 79  ? -44.866 -34.472 7.235  1.00 148.67 ? 375 LYS A CD  1 
ATOM   553  C  CE  . LYS A 1 79  ? -44.545 -35.500 6.150  1.00 150.36 ? 375 LYS A CE  1 
ATOM   554  N  NZ  . LYS A 1 79  ? -43.506 -35.021 5.194  1.00 142.52 ? 375 LYS A NZ  1 
ATOM   555  N  N   . ALA A 1 80  ? -44.807 -29.245 7.900  1.00 118.42 ? 376 ALA A N   1 
ATOM   556  C  CA  . ALA A 1 80  ? -43.932 -28.144 7.504  1.00 113.83 ? 376 ALA A CA  1 
ATOM   557  C  C   . ALA A 1 80  ? -42.771 -28.002 8.484  1.00 116.95 ? 376 ALA A C   1 
ATOM   558  O  O   . ALA A 1 80  ? -41.649 -27.663 8.089  1.00 118.68 ? 376 ALA A O   1 
ATOM   559  C  CB  . ALA A 1 80  ? -44.732 -26.843 7.398  1.00 109.39 ? 376 ALA A CB  1 
ATOM   560  N  N   . HIS A 1 81  ? -43.020 -28.289 9.764  1.00 117.58 ? 377 HIS A N   1 
ATOM   561  C  CA  . HIS A 1 81  ? -41.933 -28.452 10.725 1.00 117.78 ? 377 HIS A CA  1 
ATOM   562  C  C   . HIS A 1 81  ? -41.139 -29.726 10.443 1.00 121.52 ? 377 HIS A C   1 
ATOM   563  O  O   . HIS A 1 81  ? -39.918 -29.681 10.253 1.00 119.85 ? 377 HIS A O   1 
ATOM   564  C  CB  . HIS A 1 81  ? -42.495 -28.469 12.148 1.00 117.91 ? 377 HIS A CB  1 
ATOM   565  C  CG  . HIS A 1 81  ? -41.470 -28.752 13.205 1.00 120.79 ? 377 HIS A CG  1 
ATOM   566  N  ND1 . HIS A 1 81  ? -41.810 -29.082 14.499 1.00 121.42 ? 377 HIS A ND1 1 
ATOM   567  C  CD2 . HIS A 1 81  ? -40.116 -28.744 13.163 1.00 117.96 ? 377 HIS A CD2 1 
ATOM   568  C  CE1 . HIS A 1 81  ? -40.710 -29.276 15.204 1.00 121.23 ? 377 HIS A CE1 1 
ATOM   569  N  NE2 . HIS A 1 81  ? -39.669 -29.079 14.416 1.00 117.28 ? 377 HIS A NE2 1 
ATOM   570  N  N   . MET A 1 82  ? -41.821 -30.875 10.413 1.00 126.54 ? 378 MET A N   1 
ATOM   571  C  CA  . MET A 1 82  ? -41.134 -32.159 10.268 1.00 130.28 ? 378 MET A CA  1 
ATOM   572  C  C   . MET A 1 82  ? -40.302 -32.229 8.988  1.00 125.48 ? 378 MET A C   1 
ATOM   573  O  O   . MET A 1 82  ? -39.200 -32.793 8.992  1.00 127.18 ? 378 MET A O   1 
ATOM   574  C  CB  . MET A 1 82  ? -42.148 -33.304 10.304 1.00 139.61 ? 378 MET A CB  1 
ATOM   575  C  CG  . MET A 1 82  ? -42.867 -33.452 11.633 1.00 148.80 ? 378 MET A CG  1 
ATOM   576  S  SD  . MET A 1 82  ? -41.744 -33.790 13.007 1.00 153.51 ? 378 MET A SD  1 
ATOM   577  C  CE  . MET A 1 82  ? -42.386 -32.685 14.260 1.00 150.59 ? 378 MET A CE  1 
ATOM   578  N  N   . ASP A 1 83  ? -40.811 -31.682 7.878  1.00 118.70 ? 379 ASP A N   1 
ATOM   579  C  CA  . ASP A 1 83  ? -40.018 -31.686 6.648  1.00 118.46 ? 379 ASP A CA  1 
ATOM   580  C  C   . ASP A 1 83  ? -38.809 -30.771 6.768  1.00 114.46 ? 379 ASP A C   1 
ATOM   581  O  O   . ASP A 1 83  ? -37.775 -31.030 6.143  1.00 108.23 ? 379 ASP A O   1 
ATOM   582  C  CB  . ASP A 1 83  ? -40.860 -31.271 5.436  1.00 117.97 ? 379 ASP A CB  1 
ATOM   583  C  CG  . ASP A 1 83  ? -41.683 -32.415 4.860  1.00 123.87 ? 379 ASP A CG  1 
ATOM   584  O  OD1 . ASP A 1 83  ? -42.884 -32.192 4.607  1.00 127.06 ? 379 ASP A OD1 1 
ATOM   585  O  OD2 . ASP A 1 83  ? -41.144 -33.527 4.656  1.00 125.88 ? 379 ASP A OD2 1 
ATOM   586  N  N   . ARG A 1 84  ? -38.925 -29.697 7.557  1.00 113.12 ? 380 ARG A N   1 
ATOM   587  C  CA  . ARG A 1 84  ? -37.781 -28.834 7.821  1.00 111.59 ? 380 ARG A CA  1 
ATOM   588  C  C   . ARG A 1 84  ? -36.774 -29.528 8.728  1.00 113.16 ? 380 ARG A C   1 
ATOM   589  O  O   . ARG A 1 84  ? -35.559 -29.382 8.550  1.00 119.17 ? 380 ARG A O   1 
ATOM   590  C  CB  . ARG A 1 84  ? -38.254 -27.526 8.453  1.00 112.40 ? 380 ARG A CB  1 
ATOM   591  C  CG  . ARG A 1 84  ? -37.156 -26.526 8.691  1.00 104.96 ? 380 ARG A CG  1 
ATOM   592  C  CD  . ARG A 1 84  ? -36.943 -25.680 7.465  1.00 103.92 ? 380 ARG A CD  1 
ATOM   593  N  NE  . ARG A 1 84  ? -35.676 -24.968 7.546  1.00 102.43 ? 380 ARG A NE  1 
ATOM   594  C  CZ  . ARG A 1 84  ? -34.518 -25.516 7.211  1.00 93.19  ? 380 ARG A CZ  1 
ATOM   595  N  NH1 . ARG A 1 84  ? -34.505 -26.761 6.782  1.00 102.46 ? 380 ARG A NH1 1 
ATOM   596  N  NH2 . ARG A 1 84  ? -33.388 -24.828 7.303  1.00 81.78  ? 380 ARG A NH2 1 
ATOM   597  N  N   . LEU A 1 85  ? -37.262 -30.275 9.718  1.00 109.54 ? 381 LEU A N   1 
ATOM   598  C  CA  . LEU A 1 85  ? -36.365 -31.046 10.570 1.00 109.09 ? 381 LEU A CA  1 
ATOM   599  C  C   . LEU A 1 85  ? -35.670 -32.144 9.777  1.00 112.52 ? 381 LEU A C   1 
ATOM   600  O  O   . LEU A 1 85  ? -34.466 -32.371 9.939  1.00 110.36 ? 381 LEU A O   1 
ATOM   601  C  CB  . LEU A 1 85  ? -37.138 -31.646 11.738 1.00 110.75 ? 381 LEU A CB  1 
ATOM   602  C  CG  . LEU A 1 85  ? -36.275 -31.910 12.966 1.00 110.88 ? 381 LEU A CG  1 
ATOM   603  C  CD1 . LEU A 1 85  ? -36.140 -30.628 13.761 1.00 97.78  ? 381 LEU A CD1 1 
ATOM   604  C  CD2 . LEU A 1 85  ? -36.863 -33.030 13.803 1.00 123.27 ? 381 LEU A CD2 1 
ATOM   605  N  N   . GLU A 1 86  ? -36.420 -32.841 8.918  1.00 118.04 ? 382 GLU A N   1 
ATOM   606  C  CA  . GLU A 1 86  ? -35.830 -33.875 8.074  1.00 121.46 ? 382 GLU A CA  1 
ATOM   607  C  C   . GLU A 1 86  ? -34.838 -33.273 7.087  1.00 107.76 ? 382 GLU A C   1 
ATOM   608  O  O   . GLU A 1 86  ? -33.751 -33.822 6.868  1.00 116.50 ? 382 GLU A O   1 
ATOM   609  C  CB  . GLU A 1 86  ? -36.936 -34.633 7.339  1.00 139.24 ? 382 GLU A CB  1 
ATOM   610  C  CG  . GLU A 1 86  ? -36.473 -35.881 6.601  1.00 152.76 ? 382 GLU A CG  1 
ATOM   611  C  CD  . GLU A 1 86  ? -37.076 -37.146 7.181  1.00 162.01 ? 382 GLU A CD  1 
ATOM   612  O  OE1 . GLU A 1 86  ? -36.737 -38.249 6.697  1.00 166.80 ? 382 GLU A OE1 1 
ATOM   613  O  OE2 . GLU A 1 86  ? -37.891 -37.034 8.123  1.00 163.17 ? 382 GLU A OE2 1 
ATOM   614  N  N   . GLU A 1 87  ? -35.194 -32.137 6.488  1.00 89.94  ? 383 GLU A N   1 
ATOM   615  C  CA  . GLU A 1 87  ? -34.298 -31.443 5.569  1.00 88.67  ? 383 GLU A CA  1 
ATOM   616  C  C   . GLU A 1 87  ? -32.968 -31.073 6.233  1.00 97.51  ? 383 GLU A C   1 
ATOM   617  O  O   . GLU A 1 87  ? -31.894 -31.332 5.677  1.00 81.82  ? 383 GLU A O   1 
ATOM   618  C  CB  . GLU A 1 87  ? -35.000 -30.196 5.034  1.00 95.64  ? 383 GLU A CB  1 
ATOM   619  C  CG  . GLU A 1 87  ? -34.286 -29.512 3.907  1.00 101.95 ? 383 GLU A CG  1 
ATOM   620  C  CD  . GLU A 1 87  ? -35.080 -28.348 3.345  1.00 107.81 ? 383 GLU A CD  1 
ATOM   621  O  OE1 . GLU A 1 87  ? -35.708 -27.605 4.143  1.00 104.08 ? 383 GLU A OE1 1 
ATOM   622  O  OE2 . GLU A 1 87  ? -35.074 -28.185 2.100  1.00 108.77 ? 383 GLU A OE2 1 
ATOM   623  N  N   . VAL A 1 88  ? -33.014 -30.455 7.424  1.00 93.51  ? 384 VAL A N   1 
ATOM   624  C  CA  . VAL A 1 88  ? -31.769 -30.090 8.102  1.00 92.47  ? 384 VAL A CA  1 
ATOM   625  C  C   . VAL A 1 88  ? -31.008 -31.339 8.512  1.00 93.66  ? 384 VAL A C   1 
ATOM   626  O  O   . VAL A 1 88  ? -29.778 -31.401 8.391  1.00 91.18  ? 384 VAL A O   1 
ATOM   627  C  CB  . VAL A 1 88  ? -32.037 -29.184 9.319  1.00 93.82  ? 384 VAL A CB  1 
ATOM   628  C  CG1 . VAL A 1 88  ? -30.739 -28.942 10.089 1.00 93.55  ? 384 VAL A CG1 1 
ATOM   629  C  CG2 . VAL A 1 88  ? -32.611 -27.866 8.877  1.00 93.34  ? 384 VAL A CG2 1 
ATOM   630  N  N   . ASN A 1 89  ? -31.729 -32.342 9.024  1.00 101.70 ? 385 ASN A N   1 
ATOM   631  C  CA  . ASN A 1 89  ? -31.114 -33.610 9.402  1.00 109.92 ? 385 ASN A CA  1 
ATOM   632  C  C   . ASN A 1 89  ? -30.290 -34.172 8.250  1.00 106.41 ? 385 ASN A C   1 
ATOM   633  O  O   . ASN A 1 89  ? -29.105 -34.482 8.411  1.00 107.51 ? 385 ASN A O   1 
ATOM   634  C  CB  . ASN A 1 89  ? -32.201 -34.600 9.840  1.00 121.22 ? 385 ASN A CB  1 
ATOM   635  C  CG  . ASN A 1 89  ? -31.638 -35.856 10.486 1.00 128.39 ? 385 ASN A CG  1 
ATOM   636  O  OD1 . ASN A 1 89  ? -31.157 -35.820 11.619 1.00 128.77 ? 385 ASN A OD1 1 
ATOM   637  N  ND2 . ASN A 1 89  ? -31.721 -36.982 9.777  1.00 131.11 ? 385 ASN A ND2 1 
ATOM   638  N  N   . LYS A 1 90  ? -30.891 -34.267 7.061  1.00 101.74 ? 386 LYS A N   1 
ATOM   639  C  CA  . LYS A 1 90  ? -30.182 -34.880 5.946  1.00 108.87 ? 386 LYS A CA  1 
ATOM   640  C  C   . LYS A 1 90  ? -29.061 -33.986 5.417  1.00 109.93 ? 386 LYS A C   1 
ATOM   641  O  O   . LYS A 1 90  ? -28.020 -34.501 4.998  1.00 114.53 ? 386 LYS A O   1 
ATOM   642  C  CB  . LYS A 1 90  ? -31.177 -35.264 4.842  1.00 109.55 ? 386 LYS A CB  1 
ATOM   643  C  CG  . LYS A 1 90  ? -32.280 -36.207 5.340  1.00 120.21 ? 386 LYS A CG  1 
ATOM   644  C  CD  . LYS A 1 90  ? -32.970 -36.977 4.219  1.00 125.47 ? 386 LYS A CD  1 
ATOM   645  C  CE  . LYS A 1 90  ? -33.915 -38.032 4.787  1.00 131.12 ? 386 LYS A CE  1 
ATOM   646  N  NZ  . LYS A 1 90  ? -34.483 -38.937 3.740  1.00 132.50 ? 386 LYS A NZ  1 
ATOM   647  N  N   . GLU A 1 91  ? -29.229 -32.656 5.436  1.00 104.82 ? 387 GLU A N   1 
ATOM   648  C  CA  . GLU A 1 91  ? -28.115 -31.793 5.037  1.00 103.63 ? 387 GLU A CA  1 
ATOM   649  C  C   . GLU A 1 91  ? -26.971 -31.859 6.046  1.00 113.93 ? 387 GLU A C   1 
ATOM   650  O  O   . GLU A 1 91  ? -25.802 -31.702 5.669  1.00 108.83 ? 387 GLU A O   1 
ATOM   651  C  CB  . GLU A 1 91  ? -28.579 -30.342 4.850  1.00 98.07  ? 387 GLU A CB  1 
ATOM   652  C  CG  . GLU A 1 91  ? -27.462 -29.404 4.362  1.00 92.23  ? 387 GLU A CG  1 
ATOM   653  C  CD  . GLU A 1 91  ? -27.848 -27.930 4.348  1.00 89.56  ? 387 GLU A CD  1 
ATOM   654  O  OE1 . GLU A 1 91  ? -26.965 -27.090 4.046  1.00 81.36  ? 387 GLU A OE1 1 
ATOM   655  O  OE2 . GLU A 1 91  ? -29.023 -27.606 4.639  1.00 96.80  ? 387 GLU A OE2 1 
ATOM   656  N  N   . ILE A 1 92  ? -27.288 -32.088 7.326  1.00 121.65 ? 388 ILE A N   1 
ATOM   657  C  CA  . ILE A 1 92  ? -26.271 -32.364 8.340  1.00 123.22 ? 388 ILE A CA  1 
ATOM   658  C  C   . ILE A 1 92  ? -25.636 -33.742 8.131  1.00 126.11 ? 388 ILE A C   1 
ATOM   659  O  O   . ILE A 1 92  ? -24.507 -33.980 8.572  1.00 128.03 ? 388 ILE A O   1 
ATOM   660  C  CB  . ILE A 1 92  ? -26.888 -32.216 9.749  1.00 124.21 ? 388 ILE A CB  1 
ATOM   661  C  CG1 . ILE A 1 92  ? -27.206 -30.745 10.042 1.00 119.62 ? 388 ILE A CG1 1 
ATOM   662  C  CG2 . ILE A 1 92  ? -25.963 -32.749 10.839 1.00 129.84 ? 388 ILE A CG2 1 
ATOM   663  C  CD1 . ILE A 1 92  ? -27.733 -30.503 11.434 1.00 113.23 ? 388 ILE A CD1 1 
ATOM   664  N  N   . GLU A 1 93  ? -26.323 -34.664 7.455  1.00 131.12 ? 389 GLU A N   1 
ATOM   665  C  CA  . GLU A 1 93  ? -25.642 -35.870 6.994  1.00 126.78 ? 389 GLU A CA  1 
ATOM   666  C  C   . GLU A 1 93  ? -24.691 -35.534 5.850  1.00 120.07 ? 389 GLU A C   1 
ATOM   667  O  O   . GLU A 1 93  ? -23.480 -35.773 5.939  1.00 112.53 ? 389 GLU A O   1 
ATOM   668  C  CB  . GLU A 1 93  ? -26.662 -36.930 6.562  1.00 129.06 ? 389 GLU A CB  1 
ATOM   669  C  CG  . GLU A 1 93  ? -27.743 -37.263 7.595  1.00 135.14 ? 389 GLU A CG  1 
ATOM   670  C  CD  . GLU A 1 93  ? -27.249 -38.128 8.751  1.00 136.45 ? 389 GLU A CD  1 
ATOM   671  O  OE1 . GLU A 1 93  ? -26.101 -38.615 8.700  1.00 139.19 ? 389 GLU A OE1 1 
ATOM   672  O  OE2 . GLU A 1 93  ? -28.019 -38.327 9.714  1.00 135.40 ? 389 GLU A OE2 1 
ATOM   673  N  N   . SER A 1 94  ? -25.227 -34.927 4.786  1.00 125.21 ? 390 SER A N   1 
ATOM   674  C  CA  . SER A 1 94  ? -24.544 -34.673 3.518  1.00 122.71 ? 390 SER A CA  1 
ATOM   675  C  C   . SER A 1 94  ? -23.328 -33.766 3.663  1.00 116.37 ? 390 SER A C   1 
ATOM   676  O  O   . SER A 1 94  ? -22.188 -34.205 3.468  1.00 107.41 ? 390 SER A O   1 
ATOM   677  C  CB  . SER A 1 94  ? -25.533 -34.054 2.528  1.00 125.23 ? 390 SER A CB  1 
ATOM   678  O  OG  . SER A 1 94  ? -24.862 -33.423 1.450  1.00 133.11 ? 390 SER A OG  1 
ATOM   679  N  N   . THR A 1 95  ? -23.575 -32.493 3.989  1.00 120.32 ? 391 THR A N   1 
ATOM   680  C  CA  . THR A 1 95  ? -22.532 -31.492 4.171  1.00 117.80 ? 391 THR A CA  1 
ATOM   681  C  C   . THR A 1 95  ? -21.978 -31.442 5.588  1.00 114.00 ? 391 THR A C   1 
ATOM   682  O  O   . THR A 1 95  ? -20.949 -30.794 5.800  1.00 104.90 ? 391 THR A O   1 
ATOM   683  C  CB  . THR A 1 95  ? -23.063 -30.098 3.814  1.00 110.38 ? 391 THR A CB  1 
ATOM   684  O  OG1 . THR A 1 95  ? -24.026 -29.677 4.798  1.00 104.92 ? 391 THR A OG1 1 
ATOM   685  C  CG2 . THR A 1 95  ? -23.703 -30.108 2.438  1.00 98.46  ? 391 THR A CG2 1 
ATOM   686  N  N   . SER A 1 96  ? -22.642 -32.093 6.551  1.00 120.24 ? 392 SER A N   1 
ATOM   687  C  CA  . SER A 1 96  ? -22.280 -32.118 7.969  1.00 123.58 ? 392 SER A CA  1 
ATOM   688  C  C   . SER A 1 96  ? -22.658 -30.822 8.685  1.00 122.43 ? 392 SER A C   1 
ATOM   689  O  O   . SER A 1 96  ? -22.951 -30.848 9.885  1.00 132.72 ? 392 SER A O   1 
ATOM   690  C  CB  . SER A 1 96  ? -20.792 -32.436 8.169  1.00 127.39 ? 392 SER A CB  1 
ATOM   691  O  OG  . SER A 1 96  ? -19.968 -31.379 7.719  1.00 125.07 ? 392 SER A OG  1 
ATOM   692  N  N   . THR A 1 97  ? -22.663 -29.692 7.980  1.00 110.50 ? 393 THR A N   1 
ATOM   693  C  CA  . THR A 1 97  ? -23.168 -28.430 8.510  1.00 99.86  ? 393 THR A CA  1 
ATOM   694  C  C   . THR A 1 97  ? -24.585 -28.199 7.968  1.00 97.14  ? 393 THR A C   1 
ATOM   695  O  O   . THR A 1 97  ? -25.233 -29.137 7.495  1.00 91.18  ? 393 THR A O   1 
ATOM   696  C  CB  . THR A 1 97  ? -22.205 -27.286 8.154  1.00 87.92  ? 393 THR A CB  1 
ATOM   697  O  OG1 . THR A 1 97  ? -22.632 -26.082 8.807  1.00 95.06  ? 393 THR A OG1 1 
ATOM   698  C  CG2 . THR A 1 97  ? -22.195 -27.041 6.663  1.00 87.03  ? 393 THR A CG2 1 
ATOM   699  N  N   . TYR A 1 98  ? -25.085 -26.963 8.048  1.00 91.98  ? 394 TYR A N   1 
ATOM   700  C  CA  . TYR A 1 98  ? -26.329 -26.625 7.360  1.00 91.04  ? 394 TYR A CA  1 
ATOM   701  C  C   . TYR A 1 98  ? -26.455 -25.108 7.242  1.00 85.17  ? 394 TYR A C   1 
ATOM   702  O  O   . TYR A 1 98  ? -25.656 -24.350 7.791  1.00 76.42  ? 394 TYR A O   1 
ATOM   703  C  CB  . TYR A 1 98  ? -27.555 -27.246 8.055  1.00 91.72  ? 394 TYR A CB  1 
ATOM   704  C  CG  . TYR A 1 98  ? -27.926 -26.647 9.381  1.00 97.98  ? 394 TYR A CG  1 
ATOM   705  C  CD1 . TYR A 1 98  ? -28.972 -25.741 9.483  1.00 100.37 ? 394 TYR A CD1 1 
ATOM   706  C  CD2 . TYR A 1 98  ? -27.245 -26.998 10.547 1.00 97.84  ? 394 TYR A CD2 1 
ATOM   707  C  CE1 . TYR A 1 98  ? -29.320 -25.182 10.716 1.00 87.76  ? 394 TYR A CE1 1 
ATOM   708  C  CE2 . TYR A 1 98  ? -27.588 -26.450 11.768 1.00 89.19  ? 394 TYR A CE2 1 
ATOM   709  C  CZ  . TYR A 1 98  ? -28.629 -25.545 11.847 1.00 83.55  ? 394 TYR A CZ  1 
ATOM   710  O  OH  . TYR A 1 98  ? -28.975 -24.989 13.066 1.00 70.90  ? 394 TYR A OH  1 
ATOM   711  N  N   . GLN A 1 99  ? -27.469 -24.676 6.493  1.00 88.78  ? 395 GLN A N   1 
ATOM   712  C  CA  . GLN A 1 99  ? -27.741 -23.265 6.240  1.00 76.97  ? 395 GLN A CA  1 
ATOM   713  C  C   . GLN A 1 99  ? -29.133 -22.904 6.748  1.00 71.42  ? 395 GLN A C   1 
ATOM   714  O  O   . GLN A 1 99  ? -30.078 -23.688 6.616  1.00 65.77  ? 395 GLN A O   1 
ATOM   715  C  CB  . GLN A 1 99  ? -27.630 -22.934 4.723  1.00 67.37  ? 395 GLN A CB  1 
ATOM   716  C  CG  . GLN A 1 99  ? -26.269 -23.238 4.091  1.00 61.34  ? 395 GLN A CG  1 
ATOM   717  C  CD  . GLN A 1 99  ? -25.192 -22.245 4.473  1.00 75.83  ? 395 GLN A CD  1 
ATOM   718  O  OE1 . GLN A 1 99  ? -25.397 -21.034 4.420  1.00 87.49  ? 395 GLN A OE1 1 
ATOM   719  N  NE2 . GLN A 1 99  ? -24.032 -22.756 4.866  1.00 76.61  ? 395 GLN A NE2 1 
ATOM   720  N  N   . LEU A 1 100 ? -29.253 -21.717 7.337  1.00 59.14  ? 396 LEU A N   1 
ATOM   721  C  CA  . LEU A 1 100 ? -30.530 -21.215 7.835  1.00 62.70  ? 396 LEU A CA  1 
ATOM   722  C  C   . LEU A 1 100 ? -31.312 -20.534 6.715  1.00 68.34  ? 396 LEU A C   1 
ATOM   723  O  O   . LEU A 1 100 ? -30.728 -19.856 5.867  1.00 70.22  ? 396 LEU A O   1 
ATOM   724  C  CB  . LEU A 1 100 ? -30.308 -20.212 8.975  1.00 54.30  ? 396 LEU A CB  1 
ATOM   725  C  CG  . LEU A 1 100 ? -29.382 -20.677 10.096 1.00 64.91  ? 396 LEU A CG  1 
ATOM   726  C  CD1 . LEU A 1 100 ? -29.099 -19.566 11.070 1.00 66.06  ? 396 LEU A CD1 1 
ATOM   727  C  CD2 . LEU A 1 100 ? -30.034 -21.837 10.792 1.00 71.57  ? 396 LEU A CD2 1 
ATOM   728  N  N   . LYS A 1 101 ? -32.638 -20.705 6.734  1.00 70.18  ? 397 LYS A N   1 
ATOM   729  C  CA  . LYS A 1 101 ? -33.537 -19.858 5.954  1.00 73.38  ? 397 LYS A CA  1 
ATOM   730  C  C   . LYS A 1 101 ? -33.365 -18.393 6.348  1.00 74.17  ? 397 LYS A C   1 
ATOM   731  O  O   . LYS A 1 101 ? -32.911 -18.069 7.449  1.00 82.98  ? 397 LYS A O   1 
ATOM   732  C  CB  . LYS A 1 101 ? -34.997 -20.245 6.200  1.00 81.79  ? 397 LYS A CB  1 
ATOM   733  C  CG  . LYS A 1 101 ? -35.348 -21.684 5.912  1.00 94.32  ? 397 LYS A CG  1 
ATOM   734  C  CD  . LYS A 1 101 ? -35.445 -21.897 4.425  1.00 97.64  ? 397 LYS A CD  1 
ATOM   735  C  CE  . LYS A 1 101 ? -35.258 -23.344 4.050  1.00 103.05 ? 397 LYS A CE  1 
ATOM   736  N  NZ  . LYS A 1 101 ? -34.885 -23.422 2.612  1.00 104.28 ? 397 LYS A NZ  1 
ATOM   737  N  N   . ASP A 1 102 ? -33.789 -17.500 5.448  1.00 66.43  ? 398 ASP A N   1 
ATOM   738  C  CA  . ASP A 1 102 ? -33.865 -16.077 5.780  1.00 64.85  ? 398 ASP A CA  1 
ATOM   739  C  C   . ASP A 1 102 ? -34.700 -15.848 7.037  1.00 73.67  ? 398 ASP A C   1 
ATOM   740  O  O   . ASP A 1 102 ? -34.297 -15.102 7.935  1.00 67.35  ? 398 ASP A O   1 
ATOM   741  C  CB  . ASP A 1 102 ? -34.463 -15.282 4.614  1.00 80.18  ? 398 ASP A CB  1 
ATOM   742  C  CG  . ASP A 1 102 ? -33.728 -15.499 3.305  1.00 94.20  ? 398 ASP A CG  1 
ATOM   743  O  OD1 . ASP A 1 102 ? -32.966 -16.483 3.196  1.00 99.67  ? 398 ASP A OD1 1 
ATOM   744  O  OD2 . ASP A 1 102 ? -33.919 -14.680 2.374  1.00 99.42  ? 398 ASP A OD2 1 
ATOM   745  N  N   . THR A 1 103 ? -35.867 -16.486 7.120  1.00 79.78  ? 399 THR A N   1 
ATOM   746  C  CA  . THR A 1 103 ? -36.734 -16.297 8.276  1.00 77.74  ? 399 THR A CA  1 
ATOM   747  C  C   . THR A 1 103 ? -36.118 -16.873 9.551  1.00 80.00  ? 399 THR A C   1 
ATOM   748  O  O   . THR A 1 103 ? -36.307 -16.313 10.645 1.00 64.52  ? 399 THR A O   1 
ATOM   749  C  CB  . THR A 1 103 ? -38.100 -16.921 7.985  1.00 79.76  ? 399 THR A CB  1 
ATOM   750  O  OG1 . THR A 1 103 ? -37.930 -18.248 7.464  1.00 79.77  ? 399 THR A OG1 1 
ATOM   751  C  CG2 . THR A 1 103 ? -38.847 -16.092 6.953  1.00 70.59  ? 399 THR A CG2 1 
ATOM   752  N  N   . GLU A 1 104 ? -35.354 -17.966 9.425  1.00 83.39  ? 400 GLU A N   1 
ATOM   753  C  CA  . GLU A 1 104 ? -34.703 -18.576 10.583 1.00 84.02  ? 400 GLU A CA  1 
ATOM   754  C  C   . GLU A 1 104 ? -33.546 -17.726 11.091 1.00 78.21  ? 400 GLU A C   1 
ATOM   755  O  O   . GLU A 1 104 ? -33.246 -17.739 12.293 1.00 80.84  ? 400 GLU A O   1 
ATOM   756  C  CB  . GLU A 1 104 ? -34.219 -19.981 10.214 1.00 81.05  ? 400 GLU A CB  1 
ATOM   757  C  CG  . GLU A 1 104 ? -35.342 -20.897 9.762  1.00 82.78  ? 400 GLU A CG  1 
ATOM   758  C  CD  . GLU A 1 104 ? -34.857 -22.248 9.278  1.00 81.83  ? 400 GLU A CD  1 
ATOM   759  O  OE1 . GLU A 1 104 ? -35.694 -23.053 8.805  1.00 86.02  ? 400 GLU A OE1 1 
ATOM   760  O  OE2 . GLU A 1 104 ? -33.639 -22.504 9.367  1.00 82.69  ? 400 GLU A OE2 1 
ATOM   761  N  N   . LEU A 1 105 ? -32.901 -16.980 10.189 1.00 67.54  ? 401 LEU A N   1 
ATOM   762  C  CA  . LEU A 1 105 ? -31.815 -16.083 10.568 1.00 65.55  ? 401 LEU A CA  1 
ATOM   763  C  C   . LEU A 1 105 ? -32.349 -14.837 11.267 1.00 65.96  ? 401 LEU A C   1 
ATOM   764  O  O   . LEU A 1 105 ? -31.780 -14.393 12.269 1.00 74.27  ? 401 LEU A O   1 
ATOM   765  C  CB  . LEU A 1 105 ? -30.996 -15.701 9.324  1.00 67.37  ? 401 LEU A CB  1 
ATOM   766  C  CG  . LEU A 1 105 ? -29.610 -15.072 9.554  1.00 60.92  ? 401 LEU A CG  1 
ATOM   767  C  CD1 . LEU A 1 105 ? -28.586 -16.080 10.062 1.00 60.40  ? 401 LEU A CD1 1 
ATOM   768  C  CD2 . LEU A 1 105 ? -29.096 -14.377 8.308  1.00 56.27  ? 401 LEU A CD2 1 
ATOM   769  N  N   . ILE A 1 106 ? -33.459 -14.277 10.776 1.00 56.94  ? 402 ILE A N   1 
ATOM   770  C  CA  . ILE A 1 106 ? -34.029 -13.076 11.394 1.00 58.45  ? 402 ILE A CA  1 
ATOM   771  C  C   . ILE A 1 106 ? -34.604 -13.407 12.776 1.00 65.73  ? 402 ILE A C   1 
ATOM   772  O  O   . ILE A 1 106 ? -34.404 -12.660 13.749 1.00 58.68  ? 402 ILE A O   1 
ATOM   773  C  CB  . ILE A 1 106 ? -35.076 -12.442 10.448 1.00 66.74  ? 402 ILE A CB  1 
ATOM   774  C  CG1 . ILE A 1 106 ? -34.429 -12.102 9.090  1.00 48.12  ? 402 ILE A CG1 1 
ATOM   775  C  CG2 . ILE A 1 106 ? -35.677 -11.197 11.084 1.00 78.29  ? 402 ILE A CG2 1 
ATOM   776  C  CD1 . ILE A 1 106 ? -35.416 -11.937 7.827  1.00 48.91  ? 402 ILE A CD1 1 
ATOM   777  N  N   . TYR A 1 107 ? -35.293 -14.544 12.896 1.00 67.86  ? 403 TYR A N   1 
ATOM   778  C  CA  . TYR A 1 107 ? -35.724 -15.031 14.206 1.00 72.51  ? 403 TYR A CA  1 
ATOM   779  C  C   . TYR A 1 107 ? -34.528 -15.262 15.127 1.00 74.47  ? 403 TYR A C   1 
ATOM   780  O  O   . TYR A 1 107 ? -34.463 -14.725 16.241 1.00 73.80  ? 403 TYR A O   1 
ATOM   781  C  CB  . TYR A 1 107 ? -36.530 -16.324 14.039 1.00 74.12  ? 403 TYR A CB  1 
ATOM   782  C  CG  . TYR A 1 107 ? -36.942 -16.987 15.351 1.00 83.45  ? 403 TYR A CG  1 
ATOM   783  C  CD1 . TYR A 1 107 ? -38.234 -16.846 15.849 1.00 87.90  ? 403 TYR A CD1 1 
ATOM   784  C  CD2 . TYR A 1 107 ? -36.044 -17.765 16.086 1.00 83.84  ? 403 TYR A CD2 1 
ATOM   785  C  CE1 . TYR A 1 107 ? -38.615 -17.447 17.045 1.00 85.21  ? 403 TYR A CE1 1 
ATOM   786  C  CE2 . TYR A 1 107 ? -36.418 -18.363 17.284 1.00 83.77  ? 403 TYR A CE2 1 
ATOM   787  C  CZ  . TYR A 1 107 ? -37.704 -18.203 17.757 1.00 86.83  ? 403 TYR A CZ  1 
ATOM   788  O  OH  . TYR A 1 107 ? -38.079 -18.802 18.947 1.00 93.48  ? 403 TYR A OH  1 
ATOM   789  N  N   . GLY A 1 108 ? -33.575 -16.084 14.680 1.00 71.68  ? 404 GLY A N   1 
ATOM   790  C  CA  . GLY A 1 108 ? -32.426 -16.398 15.515 1.00 61.39  ? 404 GLY A CA  1 
ATOM   791  C  C   . GLY A 1 108 ? -31.667 -15.166 15.969 1.00 60.79  ? 404 GLY A C   1 
ATOM   792  O  O   . GLY A 1 108 ? -31.226 -15.087 17.110 1.00 54.29  ? 404 GLY A O   1 
ATOM   793  N  N   . ALA A 1 109 ? -31.509 -14.184 15.089 1.00 61.66  ? 405 ALA A N   1 
ATOM   794  C  CA  . ALA A 1 109 ? -30.777 -12.980 15.463 1.00 60.53  ? 405 ALA A CA  1 
ATOM   795  C  C   . ALA A 1 109 ? -31.552 -12.174 16.490 1.00 63.11  ? 405 ALA A C   1 
ATOM   796  O  O   . ALA A 1 109 ? -30.979 -11.664 17.460 1.00 60.45  ? 405 ALA A O   1 
ATOM   797  C  CB  . ALA A 1 109 ? -30.496 -12.130 14.218 1.00 44.53  ? 405 ALA A CB  1 
ATOM   798  N  N   . LYS A 1 110 ? -32.864 -12.035 16.289 1.00 62.59  ? 406 LYS A N   1 
ATOM   799  C  CA  . LYS A 1 110 ? -33.643 -11.211 17.206 1.00 60.64  ? 406 LYS A CA  1 
ATOM   800  C  C   . LYS A 1 110 ? -33.688 -11.831 18.590 1.00 63.72  ? 406 LYS A C   1 
ATOM   801  O  O   . LYS A 1 110 ? -33.787 -11.109 19.593 1.00 63.10  ? 406 LYS A O   1 
ATOM   802  C  CB  . LYS A 1 110 ? -35.060 -11.000 16.658 1.00 63.67  ? 406 LYS A CB  1 
ATOM   803  C  CG  . LYS A 1 110 ? -35.116 -10.126 15.413 1.00 75.47  ? 406 LYS A CG  1 
ATOM   804  C  CD  . LYS A 1 110 ? -36.549 -9.879  14.956 1.00 77.14  ? 406 LYS A CD  1 
ATOM   805  C  CE  . LYS A 1 110 ? -36.578 -8.962  13.747 1.00 72.41  ? 406 LYS A CE  1 
ATOM   806  N  NZ  . LYS A 1 110 ? -37.923 -8.359  13.538 1.00 71.31  ? 406 LYS A NZ  1 
ATOM   807  N  N   . HIS A 1 111 ? -33.577 -13.162 18.673 1.00 58.48  ? 407 HIS A N   1 
ATOM   808  C  CA  . HIS A 1 111 ? -33.619 -13.850 19.963 1.00 55.11  ? 407 HIS A CA  1 
ATOM   809  C  C   . HIS A 1 111 ? -32.265 -13.914 20.655 1.00 58.45  ? 407 HIS A C   1 
ATOM   810  O  O   . HIS A 1 111 ? -32.208 -13.945 21.902 1.00 55.13  ? 407 HIS A O   1 
ATOM   811  C  CB  . HIS A 1 111 ? -34.210 -15.240 19.766 1.00 58.06  ? 407 HIS A CB  1 
ATOM   812  C  CG  . HIS A 1 111 ? -35.687 -15.203 19.552 1.00 66.82  ? 407 HIS A CG  1 
ATOM   813  N  ND1 . HIS A 1 111 ? -36.587 -15.649 20.496 1.00 72.23  ? 407 HIS A ND1 1 
ATOM   814  C  CD2 . HIS A 1 111 ? -36.425 -14.683 18.546 1.00 68.20  ? 407 HIS A CD2 1 
ATOM   815  C  CE1 . HIS A 1 111 ? -37.817 -15.456 20.053 1.00 72.78  ? 407 HIS A CE1 1 
ATOM   816  N  NE2 . HIS A 1 111 ? -37.746 -14.870 18.873 1.00 70.94  ? 407 HIS A NE2 1 
ATOM   817  N  N   . ALA A 1 112 ? -31.171 -13.891 19.893 1.00 51.89  ? 408 ALA A N   1 
ATOM   818  C  CA  . ALA A 1 112 ? -29.871 -13.672 20.517 1.00 59.00  ? 408 ALA A CA  1 
ATOM   819  C  C   . ALA A 1 112 ? -29.867 -12.360 21.306 1.00 63.91  ? 408 ALA A C   1 
ATOM   820  O  O   . ALA A 1 112 ? -29.481 -12.325 22.482 1.00 63.67  ? 408 ALA A O   1 
ATOM   821  C  CB  . ALA A 1 112 ? -28.781 -13.684 19.451 1.00 62.91  ? 408 ALA A CB  1 
ATOM   822  N  N   . TRP A 1 113 ? -30.334 -11.275 20.677 1.00 50.68  ? 409 TRP A N   1 
ATOM   823  C  CA  . TRP A 1 113 ? -30.566 -10.030 21.398 1.00 50.12  ? 409 TRP A CA  1 
ATOM   824  C  C   . TRP A 1 113 ? -31.515 -10.238 22.577 1.00 62.34  ? 409 TRP A C   1 
ATOM   825  O  O   . TRP A 1 113 ? -31.246 -9.771  23.691 1.00 67.14  ? 409 TRP A O   1 
ATOM   826  C  CB  . TRP A 1 113 ? -31.120 -8.976  20.445 1.00 45.11  ? 409 TRP A CB  1 
ATOM   827  C  CG  . TRP A 1 113 ? -31.279 -7.636  21.069 1.00 48.49  ? 409 TRP A CG  1 
ATOM   828  C  CD1 . TRP A 1 113 ? -30.891 -7.265  22.335 1.00 55.63  ? 409 TRP A CD1 1 
ATOM   829  C  CD2 . TRP A 1 113 ? -31.850 -6.467  20.468 1.00 50.68  ? 409 TRP A CD2 1 
ATOM   830  N  NE1 . TRP A 1 113 ? -31.203 -5.944  22.558 1.00 52.28  ? 409 TRP A NE1 1 
ATOM   831  C  CE2 . TRP A 1 113 ? -31.793 -5.431  21.431 1.00 51.33  ? 409 TRP A CE2 1 
ATOM   832  C  CE3 . TRP A 1 113 ? -32.418 -6.197  19.219 1.00 51.64  ? 409 TRP A CE3 1 
ATOM   833  C  CZ2 . TRP A 1 113 ? -32.265 -4.145  21.177 1.00 50.54  ? 409 TRP A CZ2 1 
ATOM   834  C  CZ3 . TRP A 1 113 ? -32.898 -4.913  18.975 1.00 54.52  ? 409 TRP A CZ3 1 
ATOM   835  C  CH2 . TRP A 1 113 ? -32.813 -3.907  19.948 1.00 57.79  ? 409 TRP A CH2 1 
ATOM   836  N  N   . ARG A 1 114 ? -32.635 -10.937 22.350 1.00 58.63  ? 410 ARG A N   1 
ATOM   837  C  CA  . ARG A 1 114 ? -33.660 -11.076 23.383 1.00 65.18  ? 410 ARG A CA  1 
ATOM   838  C  C   . ARG A 1 114 ? -33.126 -11.803 24.614 1.00 68.90  ? 410 ARG A C   1 
ATOM   839  O  O   . ARG A 1 114 ? -33.548 -11.521 25.742 1.00 66.24  ? 410 ARG A O   1 
ATOM   840  C  CB  . ARG A 1 114 ? -34.874 -11.817 22.815 1.00 60.68  ? 410 ARG A CB  1 
ATOM   841  C  CG  . ARG A 1 114 ? -36.119 -11.804 23.698 1.00 65.95  ? 410 ARG A CG  1 
ATOM   842  C  CD  . ARG A 1 114 ? -37.240 -12.703 23.148 1.00 70.71  ? 410 ARG A CD  1 
ATOM   843  N  NE  . ARG A 1 114 ? -38.507 -12.487 23.856 1.00 74.16  ? 410 ARG A NE  1 
ATOM   844  C  CZ  . ARG A 1 114 ? -39.665 -13.060 23.529 1.00 72.12  ? 410 ARG A CZ  1 
ATOM   845  N  NH1 . ARG A 1 114 ? -40.765 -12.802 24.234 1.00 65.12  ? 410 ARG A NH1 1 
ATOM   846  N  NH2 . ARG A 1 114 ? -39.729 -13.888 22.496 1.00 68.14  ? 410 ARG A NH2 1 
ATOM   847  N  N   . ASN A 1 115 ? -32.191 -12.727 24.413 1.00 62.35  ? 411 ASN A N   1 
ATOM   848  C  CA  . ASN A 1 115 ? -31.621 -13.534 25.476 1.00 66.56  ? 411 ASN A CA  1 
ATOM   849  C  C   . ASN A 1 115 ? -30.386 -12.913 26.116 1.00 60.76  ? 411 ASN A C   1 
ATOM   850  O  O   . ASN A 1 115 ? -29.873 -13.469 27.096 1.00 51.52  ? 411 ASN A O   1 
ATOM   851  C  CB  . ASN A 1 115 ? -31.284 -14.914 24.925 1.00 47.29  ? 411 ASN A CB  1 
ATOM   852  C  CG  . ASN A 1 115 ? -32.510 -15.655 24.463 1.00 66.97  ? 411 ASN A CG  1 
ATOM   853  O  OD1 . ASN A 1 115 ? -33.556 -15.594 25.114 1.00 72.51  ? 411 ASN A OD1 1 
ATOM   854  N  ND2 . ASN A 1 115 ? -32.404 -16.348 23.326 1.00 70.22  ? 411 ASN A ND2 1 
ATOM   855  N  N   . ALA A 1 116 ? -29.907 -11.787 25.584 1.00 46.30  ? 412 ALA A N   1 
ATOM   856  C  CA  . ALA A 1 116 ? -28.720 -11.086 26.066 1.00 55.99  ? 412 ALA A CA  1 
ATOM   857  C  C   . ALA A 1 116 ? -28.982 -10.455 27.428 1.00 57.79  ? 412 ALA A C   1 
ATOM   858  O  O   . ALA A 1 116 ? -29.452 -9.320  27.519 1.00 63.46  ? 412 ALA A O   1 
ATOM   859  C  CB  . ALA A 1 116 ? -28.291 -10.017 25.059 1.00 40.20  ? 412 ALA A CB  1 
ATOM   860  N  N   . SER A 1 117 ? -28.655 -11.185 28.491 1.00 59.52  ? 413 SER A N   1 
ATOM   861  C  CA  . SER A 1 117 ? -29.047 -10.800 29.841 1.00 56.57  ? 413 SER A CA  1 
ATOM   862  C  C   . SER A 1 117 ? -28.390 -9.503  30.304 1.00 56.09  ? 413 SER A C   1 
ATOM   863  O  O   . SER A 1 117 ? -28.953 -8.806  31.155 1.00 52.20  ? 413 SER A O   1 
ATOM   864  C  CB  . SER A 1 117 ? -28.733 -11.957 30.798 1.00 52.40  ? 413 SER A CB  1 
ATOM   865  O  OG  . SER A 1 117 ? -27.468 -12.533 30.501 1.00 48.25  ? 413 SER A OG  1 
ATOM   866  N  N   . ARG A 1 118 ? -27.232 -9.160  29.749 1.00 50.61  ? 414 ARG A N   1 
ATOM   867  C  CA  . ARG A 1 118 ? -26.505 -7.941  30.071 1.00 46.97  ? 414 ARG A CA  1 
ATOM   868  C  C   . ARG A 1 118 ? -27.020 -6.691  29.342 1.00 47.94  ? 414 ARG A C   1 
ATOM   869  O  O   . ARG A 1 118 ? -26.469 -5.616  29.582 1.00 47.97  ? 414 ARG A O   1 
ATOM   870  C  CB  . ARG A 1 118 ? -25.011 -8.140  29.751 1.00 42.39  ? 414 ARG A CB  1 
ATOM   871  C  CG  . ARG A 1 118 ? -24.368 -9.312  30.502 1.00 42.52  ? 414 ARG A CG  1 
ATOM   872  C  CD  . ARG A 1 118 ? -22.825 -9.196  30.557 1.00 52.87  ? 414 ARG A CD  1 
ATOM   873  N  NE  . ARG A 1 118 ? -22.235 -10.022 31.618 1.00 50.79  ? 414 ARG A NE  1 
ATOM   874  C  CZ  . ARG A 1 118 ? -20.931 -10.276 31.750 1.00 57.83  ? 414 ARG A CZ  1 
ATOM   875  N  NH1 . ARG A 1 118 ? -20.051 -9.772  30.902 1.00 63.65  ? 414 ARG A NH1 1 
ATOM   876  N  NH2 . ARG A 1 118 ? -20.496 -11.022 32.758 1.00 69.63  ? 414 ARG A NH2 1 
ATOM   877  N  N   . CYS A 1 119 ? -28.051 -6.775  28.477 1.00 48.11  ? 415 CYS A N   1 
ATOM   878  C  CA  . CYS A 1 119 ? -28.534 -5.619  27.708 1.00 45.96  ? 415 CYS A CA  1 
ATOM   879  C  C   . CYS A 1 119 ? -29.788 -5.051  28.361 1.00 42.32  ? 415 CYS A C   1 
ATOM   880  O  O   . CYS A 1 119 ? -30.792 -5.758  28.503 1.00 46.59  ? 415 CYS A O   1 
ATOM   881  C  CB  . CYS A 1 119 ? -28.828 -5.987  26.239 1.00 43.40  ? 415 CYS A CB  1 
ATOM   882  S  SG  . CYS A 1 119 ? -29.652 -4.703  25.223 1.00 48.52  ? 415 CYS A SG  1 
ATOM   883  N  N   . VAL A 1 120 ? -29.736 -3.763  28.721 1.00 55.85  ? 416 VAL A N   1 
ATOM   884  C  CA  . VAL A 1 120 ? -30.880 -3.081  29.324 1.00 58.14  ? 416 VAL A CA  1 
ATOM   885  C  C   . VAL A 1 120 ? -31.875 -2.566  28.282 1.00 58.83  ? 416 VAL A C   1 
ATOM   886  O  O   . VAL A 1 120 ? -33.033 -2.292  28.623 1.00 53.65  ? 416 VAL A O   1 
ATOM   887  C  CB  . VAL A 1 120 ? -30.399 -1.923  30.218 1.00 58.93  ? 416 VAL A CB  1 
ATOM   888  C  CG1 . VAL A 1 120 ? -30.046 -0.690  29.369 1.00 55.53  ? 416 VAL A CG1 1 
ATOM   889  C  CG2 . VAL A 1 120 ? -31.448 -1.586  31.311 1.00 42.24  ? 416 VAL A CG2 1 
ATOM   890  N  N   . GLY A 1 121 ? -31.488 -2.468  27.010 1.00 52.75  ? 417 GLY A N   1 
ATOM   891  C  CA  . GLY A 1 121 ? -32.380 -1.875  26.024 1.00 52.94  ? 417 GLY A CA  1 
ATOM   892  C  C   . GLY A 1 121 ? -33.208 -2.880  25.250 1.00 56.59  ? 417 GLY A C   1 
ATOM   893  O  O   . GLY A 1 121 ? -33.734 -2.568  24.177 1.00 71.76  ? 417 GLY A O   1 
ATOM   894  N  N   . ARG A 1 122 ? -33.348 -4.091  25.797 1.00 48.86  ? 418 ARG A N   1 
ATOM   895  C  CA  . ARG A 1 122 ? -33.924 -5.212  25.060 1.00 52.50  ? 418 ARG A CA  1 
ATOM   896  C  C   . ARG A 1 122 ? -35.428 -5.097  24.851 1.00 63.41  ? 418 ARG A C   1 
ATOM   897  O  O   . ARG A 1 122 ? -36.003 -5.976  24.203 1.00 62.60  ? 418 ARG A O   1 
ATOM   898  C  CB  . ARG A 1 122 ? -33.645 -6.530  25.780 1.00 53.06  ? 418 ARG A CB  1 
ATOM   899  C  CG  . ARG A 1 122 ? -32.253 -7.098  25.582 1.00 62.02  ? 418 ARG A CG  1 
ATOM   900  C  CD  . ARG A 1 122 ? -32.136 -8.400  26.324 1.00 61.71  ? 418 ARG A CD  1 
ATOM   901  N  NE  . ARG A 1 122 ? -32.041 -8.191  27.760 1.00 61.60  ? 418 ARG A NE  1 
ATOM   902  C  CZ  . ARG A 1 122 ? -32.235 -9.141  28.663 1.00 58.54  ? 418 ARG A CZ  1 
ATOM   903  N  NH1 . ARG A 1 122 ? -32.553 -10.366 28.277 1.00 49.09  ? 418 ARG A NH1 1 
ATOM   904  N  NH2 . ARG A 1 122 ? -32.120 -8.862  29.947 1.00 68.56  ? 418 ARG A NH2 1 
ATOM   905  N  N   . ILE A 1 123 ? -36.084 -4.069  25.397 1.00 58.40  ? 419 ILE A N   1 
ATOM   906  C  CA  . ILE A 1 123 ? -37.501 -3.846  25.135 1.00 51.08  ? 419 ILE A CA  1 
ATOM   907  C  C   . ILE A 1 123 ? -37.710 -3.756  23.619 1.00 67.11  ? 419 ILE A C   1 
ATOM   908  O  O   . ILE A 1 123 ? -38.806 -4.018  23.106 1.00 69.32  ? 419 ILE A O   1 
ATOM   909  C  CB  . ILE A 1 123 ? -38.008 -2.573  25.842 1.00 59.22  ? 419 ILE A CB  1 
ATOM   910  C  CG1 . ILE A 1 123 ? -39.532 -2.610  25.940 1.00 71.18  ? 419 ILE A CG1 1 
ATOM   911  C  CG2 . ILE A 1 123 ? -37.551 -1.301  25.089 1.00 59.70  ? 419 ILE A CG2 1 
ATOM   912  C  CD1 . ILE A 1 123 ? -40.176 -1.244  26.068 1.00 81.56  ? 419 ILE A CD1 1 
ATOM   913  N  N   . GLN A 1 124 ? -36.646 -3.414  22.892 1.00 61.67  ? 420 GLN A N   1 
ATOM   914  C  CA  . GLN A 1 124 ? -36.676 -3.184  21.452 1.00 69.40  ? 420 GLN A CA  1 
ATOM   915  C  C   . GLN A 1 124 ? -36.307 -4.421  20.633 1.00 66.34  ? 420 GLN A C   1 
ATOM   916  O  O   . GLN A 1 124 ? -36.205 -4.326  19.402 1.00 49.91  ? 420 GLN A O   1 
ATOM   917  C  CB  . GLN A 1 124 ? -35.731 -2.033  21.103 1.00 70.81  ? 420 GLN A CB  1 
ATOM   918  C  CG  . GLN A 1 124 ? -36.244 -0.664  21.503 1.00 80.37  ? 420 GLN A CG  1 
ATOM   919  C  CD  . GLN A 1 124 ? -37.020 0.015   20.383 1.00 91.68  ? 420 GLN A CD  1 
ATOM   920  O  OE1 . GLN A 1 124 ? -37.467 -0.635  19.439 1.00 93.28  ? 420 GLN A OE1 1 
ATOM   921  N  NE2 . GLN A 1 124 ? -37.174 1.330   20.481 1.00 98.19  ? 420 GLN A NE2 1 
ATOM   922  N  N   . TRP A 1 125 ? -36.150 -5.581  21.281 1.00 68.15  ? 421 TRP A N   1 
ATOM   923  C  CA  . TRP A 1 125 ? -35.525 -6.735  20.639 1.00 63.57  ? 421 TRP A CA  1 
ATOM   924  C  C   . TRP A 1 125 ? -36.234 -7.133  19.354 1.00 68.87  ? 421 TRP A C   1 
ATOM   925  O  O   . TRP A 1 125 ? -35.586 -7.561  18.393 1.00 80.29  ? 421 TRP A O   1 
ATOM   926  C  CB  . TRP A 1 125 ? -35.497 -7.922  21.603 1.00 60.09  ? 421 TRP A CB  1 
ATOM   927  C  CG  . TRP A 1 125 ? -36.858 -8.525  21.775 1.00 65.43  ? 421 TRP A CG  1 
ATOM   928  C  CD1 . TRP A 1 125 ? -37.833 -8.121  22.635 1.00 61.83  ? 421 TRP A CD1 1 
ATOM   929  C  CD2 . TRP A 1 125 ? -37.412 -9.602  21.013 1.00 70.40  ? 421 TRP A CD2 1 
ATOM   930  N  NE1 . TRP A 1 125 ? -38.957 -8.897  22.473 1.00 60.21  ? 421 TRP A NE1 1 
ATOM   931  C  CE2 . TRP A 1 125 ? -38.720 -9.820  21.488 1.00 69.17  ? 421 TRP A CE2 1 
ATOM   932  C  CE3 . TRP A 1 125 ? -36.920 -10.415 19.991 1.00 60.68  ? 421 TRP A CE3 1 
ATOM   933  C  CZ2 . TRP A 1 125 ? -39.543 -10.814 20.974 1.00 74.94  ? 421 TRP A CZ2 1 
ATOM   934  C  CZ3 . TRP A 1 125 ? -37.745 -11.408 19.475 1.00 67.50  ? 421 TRP A CZ3 1 
ATOM   935  C  CH2 . TRP A 1 125 ? -39.040 -11.594 19.964 1.00 75.51  ? 421 TRP A CH2 1 
ATOM   936  N  N   . SER A 1 126 ? -37.562 -7.009  19.308 1.00 69.50  ? 422 SER A N   1 
ATOM   937  C  CA  . SER A 1 126 ? -38.280 -7.421  18.101 1.00 80.74  ? 422 SER A CA  1 
ATOM   938  C  C   . SER A 1 126 ? -38.003 -6.484  16.922 1.00 84.26  ? 422 SER A C   1 
ATOM   939  O  O   . SER A 1 126 ? -37.873 -6.940  15.778 1.00 92.49  ? 422 SER A O   1 
ATOM   940  C  CB  . SER A 1 126 ? -39.779 -7.507  18.385 1.00 91.58  ? 422 SER A CB  1 
ATOM   941  O  OG  . SER A 1 126 ? -40.468 -6.358  17.922 1.00 98.37  ? 422 SER A OG  1 
ATOM   942  N  N   . LYS A 1 127 ? -37.921 -5.172  17.172 1.00 79.64  ? 423 LYS A N   1 
ATOM   943  C  CA  . LYS A 1 127 ? -37.663 -4.179  16.123 1.00 71.32  ? 423 LYS A CA  1 
ATOM   944  C  C   . LYS A 1 127 ? -36.160 -4.152  15.847 1.00 73.20  ? 423 LYS A C   1 
ATOM   945  O  O   . LYS A 1 127 ? -35.410 -3.301  16.338 1.00 64.07  ? 423 LYS A O   1 
ATOM   946  C  CB  . LYS A 1 127 ? -38.182 -2.801  16.529 1.00 65.09  ? 423 LYS A CB  1 
ATOM   947  C  CG  . LYS A 1 127 ? -38.968 -2.070  15.448 1.00 78.93  ? 423 LYS A CG  1 
ATOM   948  C  CD  . LYS A 1 127 ? -38.880 -0.539  15.562 1.00 81.91  ? 423 LYS A CD  1 
ATOM   949  C  CE  . LYS A 1 127 ? -39.412 0.117   14.289 1.00 96.77  ? 423 LYS A CE  1 
ATOM   950  N  NZ  . LYS A 1 127 ? -39.323 1.605   14.293 1.00 101.79 ? 423 LYS A NZ  1 
ATOM   951  N  N   . LEU A 1 128 ? -35.718 -5.115  15.039 1.00 76.41  ? 424 LEU A N   1 
ATOM   952  C  CA  . LEU A 1 128 ? -34.327 -5.247  14.631 1.00 67.29  ? 424 LEU A CA  1 
ATOM   953  C  C   . LEU A 1 128 ? -34.286 -5.528  13.134 1.00 68.27  ? 424 LEU A C   1 
ATOM   954  O  O   . LEU A 1 128 ? -35.102 -6.296  12.615 1.00 57.34  ? 424 LEU A O   1 
ATOM   955  C  CB  . LEU A 1 128 ? -33.616 -6.372  15.411 1.00 58.82  ? 424 LEU A CB  1 
ATOM   956  C  CG  . LEU A 1 128 ? -32.170 -6.744  15.045 1.00 52.52  ? 424 LEU A CG  1 
ATOM   957  C  CD1 . LEU A 1 128 ? -31.248 -5.616  15.400 1.00 40.60  ? 424 LEU A CD1 1 
ATOM   958  C  CD2 . LEU A 1 128 ? -31.691 -8.042  15.713 1.00 54.92  ? 424 LEU A CD2 1 
ATOM   959  N  N   . GLN A 1 129 ? -33.331 -4.906  12.452 1.00 70.10  ? 425 GLN A N   1 
ATOM   960  C  CA  . GLN A 1 129 ? -33.178 -5.019  11.005 1.00 64.11  ? 425 GLN A CA  1 
ATOM   961  C  C   . GLN A 1 129 ? -31.996 -5.933  10.726 1.00 61.82  ? 425 GLN A C   1 
ATOM   962  O  O   . GLN A 1 129 ? -30.863 -5.638  11.120 1.00 67.68  ? 425 GLN A O   1 
ATOM   963  C  CB  . GLN A 1 129 ? -32.978 -3.642  10.369 1.00 68.44  ? 425 GLN A CB  1 
ATOM   964  C  CG  . GLN A 1 129 ? -32.548 -3.653  8.912  1.00 76.60  ? 425 GLN A CG  1 
ATOM   965  C  CD  . GLN A 1 129 ? -33.550 -4.348  8.024  1.00 78.80  ? 425 GLN A CD  1 
ATOM   966  O  OE1 . GLN A 1 129 ? -34.758 -4.119  8.129  1.00 78.24  ? 425 GLN A OE1 1 
ATOM   967  N  NE2 . GLN A 1 129 ? -33.058 -5.216  7.147  1.00 84.07  ? 425 GLN A NE2 1 
ATOM   968  N  N   . VAL A 1 130 ? -32.261 -7.049  10.075 1.00 55.10  ? 426 VAL A N   1 
ATOM   969  C  CA  . VAL A 1 130 ? -31.249 -8.058  9.817  1.00 54.38  ? 426 VAL A CA  1 
ATOM   970  C  C   . VAL A 1 130 ? -30.770 -7.878  8.390  1.00 52.20  ? 426 VAL A C   1 
ATOM   971  O  O   . VAL A 1 130 ? -31.584 -7.751  7.467  1.00 38.63  ? 426 VAL A O   1 
ATOM   972  C  CB  . VAL A 1 130 ? -31.804 -9.472  10.059 1.00 54.05  ? 426 VAL A CB  1 
ATOM   973  C  CG1 . VAL A 1 130 ? -30.689 -10.533 9.943  1.00 46.11  ? 426 VAL A CG1 1 
ATOM   974  C  CG2 . VAL A 1 130 ? -32.536 -9.510  11.430 1.00 44.37  ? 426 VAL A CG2 1 
ATOM   975  N  N   . PHE A 1 131 ? -29.455 -7.800  8.222  1.00 55.00  ? 427 PHE A N   1 
ATOM   976  C  CA  . PHE A 1 131 ? -28.815 -7.688  6.921  1.00 56.36  ? 427 PHE A CA  1 
ATOM   977  C  C   . PHE A 1 131 ? -28.095 -9.003  6.689  1.00 58.64  ? 427 PHE A C   1 
ATOM   978  O  O   . PHE A 1 131 ? -27.133 -9.324  7.395  1.00 49.62  ? 427 PHE A O   1 
ATOM   979  C  CB  . PHE A 1 131 ? -27.846 -6.510  6.851  1.00 48.16  ? 427 PHE A CB  1 
ATOM   980  C  CG  . PHE A 1 131 ? -28.522 -5.172  6.830  1.00 50.61  ? 427 PHE A CG  1 
ATOM   981  C  CD1 . PHE A 1 131 ? -29.254 -4.779  5.741  1.00 55.37  ? 427 PHE A CD1 1 
ATOM   982  C  CD2 . PHE A 1 131 ? -28.409 -4.299  7.912  1.00 49.10  ? 427 PHE A CD2 1 
ATOM   983  C  CE1 . PHE A 1 131 ? -29.877 -3.549  5.710  1.00 58.19  ? 427 PHE A CE1 1 
ATOM   984  C  CE2 . PHE A 1 131 ? -29.038 -3.067  7.892  1.00 48.54  ? 427 PHE A CE2 1 
ATOM   985  C  CZ  . PHE A 1 131 ? -29.766 -2.696  6.797  1.00 60.10  ? 427 PHE A CZ  1 
ATOM   986  N  N   . ASP A 1 132 ? -28.579 -9.766  5.717  1.00 58.87  ? 428 ASP A N   1 
ATOM   987  C  CA  . ASP A 1 132 ? -27.984 -11.047 5.363  1.00 46.28  ? 428 ASP A CA  1 
ATOM   988  C  C   . ASP A 1 132 ? -26.769 -10.759 4.494  1.00 51.16  ? 428 ASP A C   1 
ATOM   989  O  O   . ASP A 1 132 ? -26.901 -10.402 3.323  1.00 65.20  ? 428 ASP A O   1 
ATOM   990  C  CB  . ASP A 1 132 ? -29.010 -11.926 4.656  1.00 50.50  ? 428 ASP A CB  1 
ATOM   991  C  CG  . ASP A 1 132 ? -28.495 -13.340 4.405  1.00 54.23  ? 428 ASP A CG  1 
ATOM   992  O  OD1 . ASP A 1 132 ? -29.298 -14.213 4.015  1.00 54.89  ? 428 ASP A OD1 1 
ATOM   993  O  OD2 . ASP A 1 132 ? -27.282 -13.575 4.600  1.00 48.38  ? 428 ASP A OD2 1 
ATOM   994  N  N   . ALA A 1 133 ? -25.577 -10.859 5.083  1.00 59.38  ? 429 ALA A N   1 
ATOM   995  C  CA  . ALA A 1 133 ? -24.332 -10.785 4.331  1.00 49.19  ? 429 ALA A CA  1 
ATOM   996  C  C   . ALA A 1 133 ? -23.670 -12.144 4.200  1.00 54.76  ? 429 ALA A C   1 
ATOM   997  O  O   . ALA A 1 133 ? -22.446 -12.235 4.037  1.00 66.38  ? 429 ALA A O   1 
ATOM   998  C  CB  . ALA A 1 133 ? -23.363 -9.793  4.961  1.00 41.12  ? 429 ALA A CB  1 
ATOM   999  N  N   . ARG A 1 134 ? -24.461 -13.210 4.247  1.00 47.97  ? 430 ARG A N   1 
ATOM   1000 C  CA  . ARG A 1 134 ? -23.893 -14.541 4.102  1.00 57.55  ? 430 ARG A CA  1 
ATOM   1001 C  C   . ARG A 1 134 ? -23.393 -14.857 2.686  1.00 59.83  ? 430 ARG A C   1 
ATOM   1002 O  O   . ARG A 1 134 ? -22.663 -15.844 2.539  1.00 61.11  ? 430 ARG A O   1 
ATOM   1003 C  CB  . ARG A 1 134 ? -24.917 -15.584 4.547  1.00 63.67  ? 430 ARG A CB  1 
ATOM   1004 C  CG  . ARG A 1 134 ? -24.984 -15.825 6.033  1.00 63.65  ? 430 ARG A CG  1 
ATOM   1005 C  CD  . ARG A 1 134 ? -26.039 -16.884 6.336  1.00 71.70  ? 430 ARG A CD  1 
ATOM   1006 N  NE  . ARG A 1 134 ? -27.365 -16.483 5.860  1.00 68.87  ? 430 ARG A NE  1 
ATOM   1007 C  CZ  . ARG A 1 134 ? -28.413 -17.300 5.768  1.00 68.92  ? 430 ARG A CZ  1 
ATOM   1008 N  NH1 . ARG A 1 134 ? -28.304 -18.581 6.112  1.00 73.01  ? 430 ARG A NH1 1 
ATOM   1009 N  NH2 . ARG A 1 134 ? -29.578 -16.838 5.329  1.00 60.35  ? 430 ARG A NH2 1 
ATOM   1010 N  N   . ASP A 1 135 ? -23.747 -14.058 1.653  1.00 56.92  ? 431 ASP A N   1 
ATOM   1011 C  CA  . ASP A 1 135 ? -23.189 -14.200 0.303  1.00 67.01  ? 431 ASP A CA  1 
ATOM   1012 C  C   . ASP A 1 135 ? -21.855 -13.475 0.125  1.00 70.57  ? 431 ASP A C   1 
ATOM   1013 O  O   . ASP A 1 135 ? -21.307 -13.468 -0.986 1.00 67.96  ? 431 ASP A O   1 
ATOM   1014 C  CB  . ASP A 1 135 ? -24.191 -13.675 -0.761 1.00 63.69  ? 431 ASP A CB  1 
ATOM   1015 C  CG  . ASP A 1 135 ? -24.550 -12.192 -0.561 1.00 71.78  ? 431 ASP A CG  1 
ATOM   1016 O  OD1 . ASP A 1 135 ? -24.302 -11.392 -1.477 1.00 71.90  ? 431 ASP A OD1 1 
ATOM   1017 O  OD2 . ASP A 1 135 ? -25.042 -11.819 0.539  1.00 62.48  ? 431 ASP A OD2 1 
ATOM   1018 N  N   . CYS A 1 136 ? -21.334 -12.858 1.178  1.00 59.20  ? 432 CYS A N   1 
ATOM   1019 C  CA  . CYS A 1 136 ? -20.118 -12.057 1.099  1.00 67.08  ? 432 CYS A CA  1 
ATOM   1020 C  C   . CYS A 1 136 ? -18.893 -12.964 1.006  1.00 74.60  ? 432 CYS A C   1 
ATOM   1021 O  O   . CYS A 1 136 ? -18.876 -14.082 1.531  1.00 82.13  ? 432 CYS A O   1 
ATOM   1022 C  CB  . CYS A 1 136 ? -20.026 -11.128 2.326  1.00 59.23  ? 432 CYS A CB  1 
ATOM   1023 S  SG  . CYS A 1 136 ? -18.691 -9.875  2.333  1.00 61.84  ? 432 CYS A SG  1 
ATOM   1024 N  N   . THR A 1 137 ? -17.869 -12.484 0.289  1.00 65.24  ? 433 THR A N   1 
ATOM   1025 C  CA  . THR A 1 137 ? -16.672 -13.271 0.000  1.00 69.01  ? 433 THR A CA  1 
ATOM   1026 C  C   . THR A 1 137 ? -15.353 -12.541 0.246  1.00 71.74  ? 433 THR A C   1 
ATOM   1027 O  O   . THR A 1 137 ? -14.309 -13.200 0.303  1.00 71.43  ? 433 THR A O   1 
ATOM   1028 C  CB  . THR A 1 137 ? -16.663 -13.743 -1.467 1.00 79.42  ? 433 THR A CB  1 
ATOM   1029 O  OG1 . THR A 1 137 ? -16.071 -12.727 -2.286 1.00 79.52  ? 433 THR A OG1 1 
ATOM   1030 C  CG2 . THR A 1 137 ? -18.071 -14.031 -1.998 1.00 82.77  ? 433 THR A CG2 1 
ATOM   1031 N  N   . THR A 1 138 ? -15.360 -11.215 0.374  1.00 76.89  ? 434 THR A N   1 
ATOM   1032 C  CA  . THR A 1 138 ? -14.145 -10.414 0.330  1.00 69.06  ? 434 THR A CA  1 
ATOM   1033 C  C   . THR A 1 138 ? -14.192 -9.361  1.428  1.00 66.03  ? 434 THR A C   1 
ATOM   1034 O  O   . THR A 1 138 ? -15.265 -8.960  1.893  1.00 60.13  ? 434 THR A O   1 
ATOM   1035 C  CB  . THR A 1 138 ? -13.982 -9.721  -1.028 1.00 65.61  ? 434 THR A CB  1 
ATOM   1036 O  OG1 . THR A 1 138 ? -15.272 -9.281  -1.474 1.00 64.47  ? 434 THR A OG1 1 
ATOM   1037 C  CG2 . THR A 1 138 ? -13.363 -10.675 -2.091 1.00 63.83  ? 434 THR A CG2 1 
ATOM   1038 N  N   . ALA A 1 139 ? -13.003 -8.902  1.824  1.00 62.79  ? 435 ALA A N   1 
ATOM   1039 C  CA  . ALA A 1 139 ? -12.930 -7.809  2.781  1.00 69.15  ? 435 ALA A CA  1 
ATOM   1040 C  C   . ALA A 1 139 ? -13.512 -6.524  2.202  1.00 72.75  ? 435 ALA A C   1 
ATOM   1041 O  O   . ALA A 1 139 ? -13.983 -5.666  2.958  1.00 79.12  ? 435 ALA A O   1 
ATOM   1042 C  CB  . ALA A 1 139 ? -11.482 -7.602  3.226  1.00 76.56  ? 435 ALA A CB  1 
ATOM   1043 N  N   . HIS A 1 140 ? -13.503 -6.376  0.869  1.00 77.72  ? 436 HIS A N   1 
ATOM   1044 C  CA  . HIS A 1 140 ? -14.185 -5.239  0.257  1.00 71.95  ? 436 HIS A CA  1 
ATOM   1045 C  C   . HIS A 1 140 ? -15.697 -5.409  0.316  1.00 63.22  ? 436 HIS A C   1 
ATOM   1046 O  O   . HIS A 1 140 ? -16.425 -4.440  0.559  1.00 63.59  ? 436 HIS A O   1 
ATOM   1047 C  CB  . HIS A 1 140 ? -13.739 -5.052  -1.192 1.00 77.18  ? 436 HIS A CB  1 
ATOM   1048 C  CG  . HIS A 1 140 ? -12.456 -4.297  -1.351 1.00 79.24  ? 436 HIS A CG  1 
ATOM   1049 N  ND1 . HIS A 1 140 ? -12.407 -3.008  -1.842 1.00 75.94  ? 436 HIS A ND1 1 
ATOM   1050 C  CD2 . HIS A 1 140 ? -11.172 -4.661  -1.123 1.00 79.58  ? 436 HIS A CD2 1 
ATOM   1051 C  CE1 . HIS A 1 140 ? -11.148 -2.611  -1.914 1.00 75.72  ? 436 HIS A CE1 1 
ATOM   1052 N  NE2 . HIS A 1 140 ? -10.378 -3.598  -1.490 1.00 82.64  ? 436 HIS A NE2 1 
ATOM   1053 N  N   . GLY A 1 141 ? -16.191 -6.622  0.061  1.00 58.83  ? 437 GLY A N   1 
ATOM   1054 C  CA  . GLY A 1 141 ? -17.605 -6.881  0.273  1.00 62.97  ? 437 GLY A CA  1 
ATOM   1055 C  C   . GLY A 1 141 ? -18.022 -6.635  1.713  1.00 64.90  ? 437 GLY A C   1 
ATOM   1056 O  O   . GLY A 1 141 ? -19.089 -6.077  1.973  1.00 64.06  ? 437 GLY A O   1 
ATOM   1057 N  N   . MET A 1 142 ? -17.191 -7.053  2.668  1.00 63.10  ? 438 MET A N   1 
ATOM   1058 C  CA  . MET A 1 142 ? -17.485 -6.748  4.065  1.00 57.47  ? 438 MET A CA  1 
ATOM   1059 C  C   . MET A 1 142 ? -17.594 -5.247  4.262  1.00 59.68  ? 438 MET A C   1 
ATOM   1060 O  O   . MET A 1 142 ? -18.574 -4.752  4.828  1.00 56.20  ? 438 MET A O   1 
ATOM   1061 C  CB  . MET A 1 142 ? -16.412 -7.329  4.983  1.00 62.96  ? 438 MET A CB  1 
ATOM   1062 C  CG  . MET A 1 142 ? -16.427 -8.828  5.061  1.00 61.58  ? 438 MET A CG  1 
ATOM   1063 S  SD  . MET A 1 142 ? -15.046 -9.452  6.015  1.00 65.07  ? 438 MET A SD  1 
ATOM   1064 C  CE  . MET A 1 142 ? -15.492 -8.972  7.695  1.00 59.99  ? 438 MET A CE  1 
ATOM   1065 N  N   . PHE A 1 143 ? -16.635 -4.500  3.700  1.00 60.93  ? 439 PHE A N   1 
ATOM   1066 C  CA  . PHE A 1 143 ? -16.603 -3.055  3.884  1.00 59.22  ? 439 PHE A CA  1 
ATOM   1067 C  C   . PHE A 1 143 ? -17.842 -2.388  3.295  1.00 61.65  ? 439 PHE A C   1 
ATOM   1068 O  O   . PHE A 1 143 ? -18.376 -1.436  3.875  1.00 59.09  ? 439 PHE A O   1 
ATOM   1069 C  CB  . PHE A 1 143 ? -15.303 -2.517  3.292  1.00 48.39  ? 439 PHE A CB  1 
ATOM   1070 C  CG  . PHE A 1 143 ? -15.250 -1.033  3.169  1.00 65.69  ? 439 PHE A CG  1 
ATOM   1071 C  CD1 . PHE A 1 143 ? -15.081 -0.437  1.921  1.00 71.82  ? 439 PHE A CD1 1 
ATOM   1072 C  CD2 . PHE A 1 143 ? -15.362 -0.228  4.282  1.00 54.46  ? 439 PHE A CD2 1 
ATOM   1073 C  CE1 . PHE A 1 143 ? -15.029 0.936   1.799  1.00 72.59  ? 439 PHE A CE1 1 
ATOM   1074 C  CE2 . PHE A 1 143 ? -15.308 1.151   4.156  1.00 55.79  ? 439 PHE A CE2 1 
ATOM   1075 C  CZ  . PHE A 1 143 ? -15.148 1.729   2.927  1.00 71.39  ? 439 PHE A CZ  1 
ATOM   1076 N  N   . ASN A 1 144 ? -18.345 -2.913  2.173  1.00 66.15  ? 440 ASN A N   1 
ATOM   1077 C  CA  . ASN A 1 144 ? -19.591 -2.423  1.589  1.00 52.70  ? 440 ASN A CA  1 
ATOM   1078 C  C   . ASN A 1 144 ? -20.784 -2.686  2.511  1.00 62.88  ? 440 ASN A C   1 
ATOM   1079 O  O   . ASN A 1 144 ? -21.510 -1.757  2.879  1.00 76.21  ? 440 ASN A O   1 
ATOM   1080 C  CB  . ASN A 1 144 ? -19.799 -3.063  0.212  1.00 58.12  ? 440 ASN A CB  1 
ATOM   1081 C  CG  . ASN A 1 144 ? -20.872 -2.377  -0.589 1.00 56.10  ? 440 ASN A CG  1 
ATOM   1082 O  OD1 . ASN A 1 144 ? -20.784 -1.181  -0.879 1.00 62.78  ? 440 ASN A OD1 1 
ATOM   1083 N  ND2 . ASN A 1 144 ? -21.889 -3.132  -0.969 1.00 55.83  ? 440 ASN A ND2 1 
ATOM   1084 N  N   . TYR A 1 145 ? -20.998 -3.950  2.911  1.00 64.17  ? 441 TYR A N   1 
ATOM   1085 C  CA  . TYR A 1 145 ? -22.104 -4.271  3.821  1.00 65.80  ? 441 TYR A CA  1 
ATOM   1086 C  C   . TYR A 1 145 ? -22.066 -3.423  5.080  1.00 53.66  ? 441 TYR A C   1 
ATOM   1087 O  O   . TYR A 1 145 ? -23.107 -2.963  5.562  1.00 60.07  ? 441 TYR A O   1 
ATOM   1088 C  CB  . TYR A 1 145 ? -22.086 -5.747  4.223  1.00 54.51  ? 441 TYR A CB  1 
ATOM   1089 C  CG  . TYR A 1 145 ? -22.821 -6.651  3.265  1.00 49.28  ? 441 TYR A CG  1 
ATOM   1090 C  CD1 . TYR A 1 145 ? -22.122 -7.461  2.393  1.00 53.12  ? 441 TYR A CD1 1 
ATOM   1091 C  CD2 . TYR A 1 145 ? -24.215 -6.688  3.233  1.00 47.49  ? 441 TYR A CD2 1 
ATOM   1092 C  CE1 . TYR A 1 145 ? -22.772 -8.303  1.516  1.00 46.08  ? 441 TYR A CE1 1 
ATOM   1093 C  CE2 . TYR A 1 145 ? -24.879 -7.523  2.367  1.00 53.57  ? 441 TYR A CE2 1 
ATOM   1094 C  CZ  . TYR A 1 145 ? -24.154 -8.328  1.498  1.00 59.28  ? 441 TYR A CZ  1 
ATOM   1095 O  OH  . TYR A 1 145 ? -24.806 -9.159  0.593  1.00 58.86  ? 441 TYR A OH  1 
ATOM   1096 N  N   . ILE A 1 146 ? -20.869 -3.228  5.642  1.00 52.96  ? 442 ILE A N   1 
ATOM   1097 C  CA  . ILE A 1 146 ? -20.740 -2.488  6.896  1.00 49.24  ? 442 ILE A CA  1 
ATOM   1098 C  C   . ILE A 1 146 ? -21.046 -1.005  6.694  1.00 45.16  ? 442 ILE A C   1 
ATOM   1099 O  O   . ILE A 1 146 ? -21.665 -0.378  7.560  1.00 48.42  ? 442 ILE A O   1 
ATOM   1100 C  CB  . ILE A 1 146 ? -19.345 -2.717  7.511  1.00 58.35  ? 442 ILE A CB  1 
ATOM   1101 C  CG1 . ILE A 1 146 ? -19.206 -4.175  7.974  1.00 56.37  ? 442 ILE A CG1 1 
ATOM   1102 C  CG2 . ILE A 1 146 ? -19.101 -1.770  8.689  1.00 55.74  ? 442 ILE A CG2 1 
ATOM   1103 C  CD1 . ILE A 1 146 ? -17.893 -4.486  8.656  1.00 46.37  ? 442 ILE A CD1 1 
ATOM   1104 N  N   . CYS A 1 147 ? -20.666 -0.418  5.537  1.00 60.64  ? 443 CYS A N   1 
ATOM   1105 C  CA  . CYS A 1 147 ? -21.043 0.981   5.292  1.00 48.29  ? 443 CYS A CA  1 
ATOM   1106 C  C   . CYS A 1 147 ? -22.553 1.113   5.179  1.00 48.89  ? 443 CYS A C   1 
ATOM   1107 O  O   . CYS A 1 147 ? -23.150 2.056   5.711  1.00 59.87  ? 443 CYS A O   1 
ATOM   1108 C  CB  . CYS A 1 147 ? -20.394 1.548   4.022  1.00 47.76  ? 443 CYS A CB  1 
ATOM   1109 S  SG  . CYS A 1 147 ? -18.607 1.891   4.046  1.00 57.26  ? 443 CYS A SG  1 
ATOM   1110 N  N   . ASN A 1 148 ? -23.186 0.163   4.501  1.00 49.17  ? 444 ASN A N   1 
ATOM   1111 C  CA  . ASN A 1 148 ? -24.634 0.195   4.339  1.00 49.87  ? 444 ASN A CA  1 
ATOM   1112 C  C   . ASN A 1 148 ? -25.339 0.010   5.661  1.00 57.35  ? 444 ASN A C   1 
ATOM   1113 O  O   . ASN A 1 148 ? -26.472 0.484   5.835  1.00 49.20  ? 444 ASN A O   1 
ATOM   1114 C  CB  . ASN A 1 148 ? -25.074 -0.903  3.374  1.00 55.04  ? 444 ASN A CB  1 
ATOM   1115 C  CG  . ASN A 1 148 ? -24.872 -0.534  1.946  1.00 59.67  ? 444 ASN A CG  1 
ATOM   1116 O  OD1 . ASN A 1 148 ? -24.379 0.556   1.642  1.00 62.18  ? 444 ASN A OD1 1 
ATOM   1117 N  ND2 . ASN A 1 148 ? -25.256 -1.442  1.041  1.00 47.03  ? 444 ASN A ND2 1 
ATOM   1118 N  N   . HIS A 1 149 ? -24.705 -0.720  6.582  1.00 55.36  ? 445 HIS A N   1 
ATOM   1119 C  CA  . HIS A 1 149 ? -25.228 -0.836  7.932  1.00 55.86  ? 445 HIS A CA  1 
ATOM   1120 C  C   . HIS A 1 149 ? -25.135 0.506   8.653  1.00 54.05  ? 445 HIS A C   1 
ATOM   1121 O  O   . HIS A 1 149 ? -26.148 1.030   9.137  1.00 58.09  ? 445 HIS A O   1 
ATOM   1122 C  CB  . HIS A 1 149 ? -24.467 -1.950  8.672  1.00 66.87  ? 445 HIS A CB  1 
ATOM   1123 C  CG  . HIS A 1 149 ? -24.864 -2.147  10.108 1.00 52.11  ? 445 HIS A CG  1 
ATOM   1124 N  ND1 . HIS A 1 149 ? -24.962 -3.400  10.680 1.00 46.21  ? 445 HIS A ND1 1 
ATOM   1125 C  CD2 . HIS A 1 149 ? -25.150 -1.260  11.091 1.00 55.73  ? 445 HIS A CD2 1 
ATOM   1126 C  CE1 . HIS A 1 149 ? -25.312 -3.274  11.949 1.00 57.72  ? 445 HIS A CE1 1 
ATOM   1127 N  NE2 . HIS A 1 149 ? -25.420 -1.986  12.228 1.00 51.92  ? 445 HIS A NE2 1 
ATOM   1128 N  N   . VAL A 1 150 ? -23.927 1.083   8.724  1.00 42.74  ? 446 VAL A N   1 
ATOM   1129 C  CA  . VAL A 1 150 ? -23.716 2.401   9.336  1.00 48.82  ? 446 VAL A CA  1 
ATOM   1130 C  C   . VAL A 1 150 ? -24.754 3.393   8.842  1.00 55.93  ? 446 VAL A C   1 
ATOM   1131 O  O   . VAL A 1 150 ? -25.446 4.033   9.634  1.00 57.00  ? 446 VAL A O   1 
ATOM   1132 C  CB  . VAL A 1 150 ? -22.315 2.971   9.041  1.00 50.22  ? 446 VAL A CB  1 
ATOM   1133 C  CG1 . VAL A 1 150 ? -22.194 4.411   9.572  1.00 52.11  ? 446 VAL A CG1 1 
ATOM   1134 C  CG2 . VAL A 1 150 ? -21.221 2.088   9.611  1.00 54.60  ? 446 VAL A CG2 1 
ATOM   1135 N  N   . LYS A 1 151 ? -24.867 3.529   7.522  1.00 50.32  ? 447 LYS A N   1 
ATOM   1136 C  CA  . LYS A 1 151 ? -25.769 4.526   6.960  1.00 57.23  ? 447 LYS A CA  1 
ATOM   1137 C  C   . LYS A 1 151 ? -27.214 4.253   7.361  1.00 61.88  ? 447 LYS A C   1 
ATOM   1138 O  O   . LYS A 1 151 ? -27.914 5.151   7.842  1.00 69.24  ? 447 LYS A O   1 
ATOM   1139 C  CB  . LYS A 1 151 ? -25.630 4.553   5.439  1.00 56.64  ? 447 LYS A CB  1 
ATOM   1140 C  CG  . LYS A 1 151 ? -26.369 5.707   4.814  1.00 56.72  ? 447 LYS A CG  1 
ATOM   1141 C  CD  . LYS A 1 151 ? -25.951 5.895   3.350  1.00 54.18  ? 447 LYS A CD  1 
ATOM   1142 C  CE  . LYS A 1 151 ? -26.380 7.231   2.813  1.00 51.17  ? 447 LYS A CE  1 
ATOM   1143 N  NZ  . LYS A 1 151 ? -25.983 7.366   1.343  1.00 54.48  ? 447 LYS A NZ  1 
ATOM   1144 N  N   . TYR A 1 152 ? -27.684 3.017   7.156  1.00 61.57  ? 448 TYR A N   1 
ATOM   1145 C  CA  . TYR A 1 152 ? -29.038 2.659   7.575  1.00 67.42  ? 448 TYR A CA  1 
ATOM   1146 C  C   . TYR A 1 152 ? -29.222 2.846   9.083  1.00 60.93  ? 448 TYR A C   1 
ATOM   1147 O  O   . TYR A 1 152 ? -30.129 3.558   9.526  1.00 63.74  ? 448 TYR A O   1 
ATOM   1148 C  CB  . TYR A 1 152 ? -29.379 1.216   7.167  1.00 64.50  ? 448 TYR A CB  1 
ATOM   1149 C  CG  . TYR A 1 152 ? -30.724 0.773   7.740  1.00 64.55  ? 448 TYR A CG  1 
ATOM   1150 C  CD1 . TYR A 1 152 ? -31.906 1.011   7.053  1.00 68.56  ? 448 TYR A CD1 1 
ATOM   1151 C  CD2 . TYR A 1 152 ? -30.811 0.153   8.984  1.00 53.14  ? 448 TYR A CD2 1 
ATOM   1152 C  CE1 . TYR A 1 152 ? -33.132 0.640   7.578  1.00 62.03  ? 448 TYR A CE1 1 
ATOM   1153 C  CE2 . TYR A 1 152 ? -32.035 -0.218  9.516  1.00 50.57  ? 448 TYR A CE2 1 
ATOM   1154 C  CZ  . TYR A 1 152 ? -33.189 0.030   8.804  1.00 56.54  ? 448 TYR A CZ  1 
ATOM   1155 O  OH  . TYR A 1 152 ? -34.418 -0.328  9.291  1.00 63.15  ? 448 TYR A OH  1 
ATOM   1156 N  N   . ALA A 1 153 ? -28.393 2.188   9.897  1.00 61.57  ? 449 ALA A N   1 
ATOM   1157 C  CA  . ALA A 1 153 ? -28.618 2.237   11.341 1.00 51.38  ? 449 ALA A CA  1 
ATOM   1158 C  C   . ALA A 1 153 ? -28.597 3.665   11.889 1.00 61.59  ? 449 ALA A C   1 
ATOM   1159 O  O   . ALA A 1 153 ? -29.222 3.939   12.929 1.00 58.07  ? 449 ALA A O   1 
ATOM   1160 C  CB  . ALA A 1 153 ? -27.582 1.387   12.083 1.00 51.77  ? 449 ALA A CB  1 
ATOM   1161 N  N   . THR A 1 154 ? -27.908 4.579   11.202 1.00 54.22  ? 450 THR A N   1 
ATOM   1162 C  CA  . THR A 1 154 ? -27.793 5.955   11.669 1.00 52.18  ? 450 THR A CA  1 
ATOM   1163 C  C   . THR A 1 154 ? -29.022 6.778   11.286 1.00 63.30  ? 450 THR A C   1 
ATOM   1164 O  O   . THR A 1 154 ? -29.591 7.467   12.133 1.00 60.59  ? 450 THR A O   1 
ATOM   1165 C  CB  . THR A 1 154 ? -26.506 6.578   11.123 1.00 55.91  ? 450 THR A CB  1 
ATOM   1166 O  OG1 . THR A 1 154 ? -25.372 5.881   11.675 1.00 48.84  ? 450 THR A OG1 1 
ATOM   1167 C  CG2 . THR A 1 154 ? -26.423 8.025   11.498 1.00 61.66  ? 450 THR A CG2 1 
ATOM   1168 N  N   . ASN A 1 155 ? -29.459 6.717   10.022 1.00 65.84  ? 451 ASN A N   1 
ATOM   1169 C  CA  . ASN A 1 155 ? -30.744 7.312   9.621  1.00 66.32  ? 451 ASN A CA  1 
ATOM   1170 C  C   . ASN A 1 155 ? -30.846 8.785   10.037 1.00 64.43  ? 451 ASN A C   1 
ATOM   1171 O  O   . ASN A 1 155 ? -31.886 9.256   10.512 1.00 72.01  ? 451 ASN A O   1 
ATOM   1172 C  CB  . ASN A 1 155 ? -31.921 6.506   10.187 1.00 66.75  ? 451 ASN A CB  1 
ATOM   1173 C  CG  . ASN A 1 155 ? -33.263 6.942   9.621  1.00 72.02  ? 451 ASN A CG  1 
ATOM   1174 O  OD1 . ASN A 1 155 ? -33.318 7.586   8.583  1.00 74.20  ? 451 ASN A OD1 1 
ATOM   1175 N  ND2 . ASN A 1 155 ? -34.347 6.615   10.316 1.00 76.68  ? 451 ASN A ND2 1 
ATOM   1176 N  N   . LYS A 1 156 ? -29.755 9.524   9.847  1.00 53.07  ? 452 LYS A N   1 
ATOM   1177 C  CA  . LYS A 1 156 ? -29.724 10.981  9.944  1.00 69.10  ? 452 LYS A CA  1 
ATOM   1178 C  C   . LYS A 1 156 ? -29.718 11.426  11.393 1.00 61.19  ? 452 LYS A C   1 
ATOM   1179 O  O   . LYS A 1 156 ? -29.933 12.612  11.668 1.00 75.36  ? 452 LYS A O   1 
ATOM   1180 C  CB  . LYS A 1 156 ? -30.897 11.672  9.222  1.00 83.92  ? 452 LYS A CB  1 
ATOM   1181 C  CG  . LYS A 1 156 ? -31.034 11.416  7.726  1.00 95.61  ? 452 LYS A CG  1 
ATOM   1182 C  CD  . LYS A 1 156 ? -31.994 12.431  7.085  1.00 103.66 ? 452 LYS A CD  1 
ATOM   1183 C  CE  . LYS A 1 156 ? -33.266 12.648  7.920  1.00 112.29 ? 452 LYS A CE  1 
ATOM   1184 N  NZ  . LYS A 1 156 ? -34.284 11.570  7.748  1.00 114.53 ? 452 LYS A NZ  1 
ATOM   1185 N  N   . GLY A 1 157 ? -29.455 10.485  12.307 1.00 65.38  ? 453 GLY A N   1 
ATOM   1186 C  CA  . GLY A 1 157 ? -29.569 10.674  13.744 1.00 62.52  ? 453 GLY A CA  1 
ATOM   1187 C  C   . GLY A 1 157 ? -30.784 10.004  14.348 1.00 66.55  ? 453 GLY A C   1 
ATOM   1188 O  O   . GLY A 1 157 ? -30.810 9.762   15.567 1.00 65.50  ? 453 GLY A O   1 
ATOM   1189 N  N   . ASN A 1 158 ? -31.803 9.711   13.534 1.00 59.67  ? 454 ASN A N   1 
ATOM   1190 C  CA  . ASN A 1 158 ? -32.956 8.952   14.009 1.00 65.45  ? 454 ASN A CA  1 
ATOM   1191 C  C   . ASN A 1 158 ? -32.600 7.463   13.993 1.00 64.68  ? 454 ASN A C   1 
ATOM   1192 O  O   . ASN A 1 158 ? -33.079 6.685   13.163 1.00 61.22  ? 454 ASN A O   1 
ATOM   1193 C  CB  . ASN A 1 158 ? -34.179 9.249   13.162 1.00 63.99  ? 454 ASN A CB  1 
ATOM   1194 C  CG  . ASN A 1 158 ? -35.445 8.696   13.767 1.00 78.30  ? 454 ASN A CG  1 
ATOM   1195 O  OD1 . ASN A 1 158 ? -35.406 7.924   14.730 1.00 89.52  ? 454 ASN A OD1 1 
ATOM   1196 N  ND2 . ASN A 1 158 ? -36.581 9.089   13.213 1.00 80.81  ? 454 ASN A ND2 1 
ATOM   1197 N  N   . LEU A 1 159 ? -31.776 7.064   14.968 1.00 57.66  ? 455 LEU A N   1 
ATOM   1198 C  CA  . LEU A 1 159 ? -31.102 5.764   14.933 1.00 63.97  ? 455 LEU A CA  1 
ATOM   1199 C  C   . LEU A 1 159 ? -32.083 4.592   14.929 1.00 54.57  ? 455 LEU A C   1 
ATOM   1200 O  O   . LEU A 1 159 ? -33.153 4.630   15.544 1.00 61.48  ? 455 LEU A O   1 
ATOM   1201 C  CB  . LEU A 1 159 ? -30.129 5.623   16.116 1.00 58.72  ? 455 LEU A CB  1 
ATOM   1202 C  CG  . LEU A 1 159 ? -28.676 6.018   15.808 1.00 63.62  ? 455 LEU A CG  1 
ATOM   1203 C  CD1 . LEU A 1 159 ? -28.644 7.345   15.102 1.00 63.92  ? 455 LEU A CD1 1 
ATOM   1204 C  CD2 . LEU A 1 159 ? -27.830 6.119   17.044 1.00 73.87  ? 455 LEU A CD2 1 
ATOM   1205 N  N   . ARG A 1 160 ? -31.682 3.540   14.221 1.00 55.69  ? 456 ARG A N   1 
ATOM   1206 C  CA  . ARG A 1 160 ? -32.423 2.300   14.028 1.00 55.11  ? 456 ARG A CA  1 
ATOM   1207 C  C   . ARG A 1 160 ? -31.465 1.153   14.297 1.00 48.83  ? 456 ARG A C   1 
ATOM   1208 O  O   . ARG A 1 160 ? -30.279 1.241   13.967 1.00 57.83  ? 456 ARG A O   1 
ATOM   1209 C  CB  . ARG A 1 160 ? -32.986 2.180   12.579 1.00 62.86  ? 456 ARG A CB  1 
ATOM   1210 C  CG  . ARG A 1 160 ? -33.874 3.340   12.118 1.00 65.08  ? 456 ARG A CG  1 
ATOM   1211 C  CD  . ARG A 1 160 ? -34.350 3.231   10.616 1.00 55.49  ? 456 ARG A CD  1 
ATOM   1212 N  NE  . ARG A 1 160 ? -33.310 3.627   9.677  1.00 54.69  ? 456 ARG A NE  1 
ATOM   1213 C  CZ  . ARG A 1 160 ? -33.487 3.827   8.365  1.00 66.65  ? 456 ARG A CZ  1 
ATOM   1214 N  NH1 . ARG A 1 160 ? -34.683 3.680   7.788  1.00 54.48  ? 456 ARG A NH1 1 
ATOM   1215 N  NH2 . ARG A 1 160 ? -32.455 4.198   7.617  1.00 66.21  ? 456 ARG A NH2 1 
ATOM   1216 N  N   . SER A 1 161 ? -31.952 0.087   14.903 1.00 45.77  ? 457 SER A N   1 
ATOM   1217 C  CA  . SER A 1 161 ? -31.030 -0.961  15.316 1.00 60.76  ? 457 SER A CA  1 
ATOM   1218 C  C   . SER A 1 161 ? -30.922 -2.023  14.233 1.00 61.20  ? 457 SER A C   1 
ATOM   1219 O  O   . SER A 1 161 ? -31.866 -2.266  13.467 1.00 68.49  ? 457 SER A O   1 
ATOM   1220 C  CB  . SER A 1 161 ? -31.449 -1.585  16.659 1.00 66.38  ? 457 SER A CB  1 
ATOM   1221 O  OG  . SER A 1 161 ? -32.767 -2.099  16.604 1.00 77.44  ? 457 SER A OG  1 
ATOM   1222 N  N   . ALA A 1 162 ? -29.743 -2.636  14.151 1.00 53.90  ? 458 ALA A N   1 
ATOM   1223 C  CA  . ALA A 1 162 ? -29.442 -3.474  13.001 1.00 52.52  ? 458 ALA A CA  1 
ATOM   1224 C  C   . ALA A 1 162 ? -28.271 -4.386  13.310 1.00 50.92  ? 458 ALA A C   1 
ATOM   1225 O  O   . ALA A 1 162 ? -27.446 -4.105  14.175 1.00 60.49  ? 458 ALA A O   1 
ATOM   1226 C  CB  . ALA A 1 162 ? -29.129 -2.623  11.763 1.00 42.50  ? 458 ALA A CB  1 
ATOM   1227 N  N   . ILE A 1 163 ? -28.196 -5.469  12.552 1.00 55.07  ? 459 ILE A N   1 
ATOM   1228 C  CA  . ILE A 1 163 ? -27.088 -6.407  12.629 1.00 53.22  ? 459 ILE A CA  1 
ATOM   1229 C  C   . ILE A 1 163 ? -26.808 -6.885  11.213 1.00 49.40  ? 459 ILE A C   1 
ATOM   1230 O  O   . ILE A 1 163 ? -27.737 -7.060  10.414 1.00 56.54  ? 459 ILE A O   1 
ATOM   1231 C  CB  . ILE A 1 163 ? -27.400 -7.587  13.572 1.00 48.19  ? 459 ILE A CB  1 
ATOM   1232 C  CG1 . ILE A 1 163 ? -26.172 -8.477  13.769 1.00 41.68  ? 459 ILE A CG1 1 
ATOM   1233 C  CG2 . ILE A 1 163 ? -28.510 -8.455  12.987 1.00 36.27  ? 459 ILE A CG2 1 
ATOM   1234 C  CD1 . ILE A 1 163 ? -26.475 -9.623  14.721 1.00 47.29  ? 459 ILE A CD1 1 
ATOM   1235 N  N   . THR A 1 164 ? -25.526 -7.051  10.886 1.00 45.92  ? 460 THR A N   1 
ATOM   1236 C  CA  . THR A 1 164 ? -25.100 -7.607  9.609  1.00 51.37  ? 460 THR A CA  1 
ATOM   1237 C  C   . THR A 1 164 ? -24.412 -8.941  9.866  1.00 55.45  ? 460 THR A C   1 
ATOM   1238 O  O   . THR A 1 164 ? -23.431 -8.992  10.610 1.00 67.46  ? 460 THR A O   1 
ATOM   1239 C  CB  . THR A 1 164 ? -24.175 -6.635  8.871  1.00 56.02  ? 460 THR A CB  1 
ATOM   1240 O  OG1 . THR A 1 164 ? -24.846 -5.380  8.709  1.00 52.33  ? 460 THR A OG1 1 
ATOM   1241 C  CG2 . THR A 1 164 ? -23.853 -7.163  7.477  1.00 47.70  ? 460 THR A CG2 1 
ATOM   1242 N  N   . ILE A 1 165 ? -24.915 -10.013 9.234  1.00 59.13  ? 461 ILE A N   1 
ATOM   1243 C  CA  . ILE A 1 165 ? -24.507 -11.393 9.511  1.00 53.73  ? 461 ILE A CA  1 
ATOM   1244 C  C   . ILE A 1 165 ? -23.655 -11.904 8.354  1.00 60.61  ? 461 ILE A C   1 
ATOM   1245 O  O   . ILE A 1 165 ? -24.166 -12.167 7.257  1.00 56.05  ? 461 ILE A O   1 
ATOM   1246 C  CB  . ILE A 1 165 ? -25.719 -12.302 9.749  1.00 57.99  ? 461 ILE A CB  1 
ATOM   1247 C  CG1 . ILE A 1 165 ? -26.346 -11.997 11.105 1.00 60.81  ? 461 ILE A CG1 1 
ATOM   1248 C  CG2 . ILE A 1 165 ? -25.300 -13.743 9.731  1.00 60.46  ? 461 ILE A CG2 1 
ATOM   1249 C  CD1 . ILE A 1 165 ? -27.801 -12.351 11.172 1.00 67.74  ? 461 ILE A CD1 1 
ATOM   1250 N  N   . PHE A 1 166 ? -22.362 -12.063 8.597  1.00 60.10  ? 462 PHE A N   1 
ATOM   1251 C  CA  . PHE A 1 166 ? -21.436 -12.553 7.584  1.00 55.52  ? 462 PHE A CA  1 
ATOM   1252 C  C   . PHE A 1 166 ? -21.386 -14.079 7.618  1.00 63.34  ? 462 PHE A C   1 
ATOM   1253 O  O   . PHE A 1 166 ? -21.937 -14.709 8.533  1.00 56.09  ? 462 PHE A O   1 
ATOM   1254 C  CB  . PHE A 1 166 ? -20.067 -11.903 7.801  1.00 56.02  ? 462 PHE A CB  1 
ATOM   1255 C  CG  . PHE A 1 166 ? -20.030 -10.450 7.409  1.00 63.88  ? 462 PHE A CG  1 
ATOM   1256 C  CD1 . PHE A 1 166 ? -19.902 -10.081 6.075  1.00 65.73  ? 462 PHE A CD1 1 
ATOM   1257 C  CD2 . PHE A 1 166 ? -20.148 -9.450  8.365  1.00 60.95  ? 462 PHE A CD2 1 
ATOM   1258 C  CE1 . PHE A 1 166 ? -19.883 -8.738  5.700  1.00 71.22  ? 462 PHE A CE1 1 
ATOM   1259 C  CE2 . PHE A 1 166 ? -20.128 -8.102  7.994  1.00 52.70  ? 462 PHE A CE2 1 
ATOM   1260 C  CZ  . PHE A 1 166 ? -19.994 -7.743  6.678  1.00 63.37  ? 462 PHE A CZ  1 
ATOM   1261 N  N   . PRO A 1 167 ? -20.774 -14.716 6.608  1.00 68.00  ? 463 PRO A N   1 
ATOM   1262 C  CA  . PRO A 1 167 ? -20.842 -16.184 6.508  1.00 62.76  ? 463 PRO A CA  1 
ATOM   1263 C  C   . PRO A 1 167 ? -20.382 -16.881 7.789  1.00 76.60  ? 463 PRO A C   1 
ATOM   1264 O  O   . PRO A 1 167 ? -19.434 -16.454 8.455  1.00 82.63  ? 463 PRO A O   1 
ATOM   1265 C  CB  . PRO A 1 167 ? -19.919 -16.497 5.329  1.00 44.93  ? 463 PRO A CB  1 
ATOM   1266 C  CG  . PRO A 1 167 ? -19.980 -15.277 4.475  1.00 61.88  ? 463 PRO A CG  1 
ATOM   1267 C  CD  . PRO A 1 167 ? -20.110 -14.123 5.427  1.00 67.51  ? 463 PRO A CD  1 
ATOM   1268 N  N   . GLN A 1 168 ? -21.078 -17.960 8.135  1.00 73.35  ? 464 GLN A N   1 
ATOM   1269 C  CA  . GLN A 1 168 ? -20.827 -18.662 9.385  1.00 65.60  ? 464 GLN A CA  1 
ATOM   1270 C  C   . GLN A 1 168 ? -19.460 -19.334 9.366  1.00 65.10  ? 464 GLN A C   1 
ATOM   1271 O  O   . GLN A 1 168 ? -18.896 -19.632 8.308  1.00 73.19  ? 464 GLN A O   1 
ATOM   1272 C  CB  . GLN A 1 168 ? -21.900 -19.723 9.621  1.00 55.98  ? 464 GLN A CB  1 
ATOM   1273 C  CG  . GLN A 1 168 ? -22.050 -20.639 8.413  1.00 51.27  ? 464 GLN A CG  1 
ATOM   1274 C  CD  . GLN A 1 168 ? -23.389 -21.335 8.390  1.00 66.23  ? 464 GLN A CD  1 
ATOM   1275 O  OE1 . GLN A 1 168 ? -23.456 -22.556 8.469  1.00 80.56  ? 464 GLN A OE1 1 
ATOM   1276 N  NE2 . GLN A 1 168 ? -24.468 -20.561 8.282  1.00 68.07  ? 464 GLN A NE2 1 
ATOM   1277 N  N   . ARG A 1 169 ? -18.937 -19.614 10.557 1.00 59.61  ? 465 ARG A N   1 
ATOM   1278 C  CA  . ARG A 1 169 ? -17.724 -20.414 10.616 1.00 62.97  ? 465 ARG A CA  1 
ATOM   1279 C  C   . ARG A 1 169 ? -18.013 -21.788 10.024 1.00 75.89  ? 465 ARG A C   1 
ATOM   1280 O  O   . ARG A 1 169 ? -19.111 -22.330 10.187 1.00 88.07  ? 465 ARG A O   1 
ATOM   1281 C  CB  . ARG A 1 169 ? -17.207 -20.533 12.054 1.00 79.27  ? 465 ARG A CB  1 
ATOM   1282 C  CG  . ARG A 1 169 ? -15.882 -21.288 12.124 1.00 86.55  ? 465 ARG A CG  1 
ATOM   1283 C  CD  . ARG A 1 169 ? -15.413 -21.569 13.534 1.00 93.80  ? 465 ARG A CD  1 
ATOM   1284 N  NE  . ARG A 1 169 ? -14.800 -20.401 14.161 1.00 90.70  ? 465 ARG A NE  1 
ATOM   1285 C  CZ  . ARG A 1 169 ? -15.367 -19.693 15.128 1.00 92.58  ? 465 ARG A CZ  1 
ATOM   1286 N  NH1 . ARG A 1 169 ? -16.560 -20.046 15.588 1.00 88.62  ? 465 ARG A NH1 1 
ATOM   1287 N  NH2 . ARG A 1 169 ? -14.736 -18.643 15.638 1.00 96.86  ? 465 ARG A NH2 1 
ATOM   1288 N  N   . THR A 1 170 ? -17.042 -22.323 9.279  1.00 71.02  ? 466 THR A N   1 
ATOM   1289 C  CA  . THR A 1 170 ? -17.199 -23.626 8.655  1.00 77.87  ? 466 THR A CA  1 
ATOM   1290 C  C   . THR A 1 170 ? -16.167 -24.549 9.291  1.00 90.29  ? 466 THR A C   1 
ATOM   1291 O  O   . THR A 1 170 ? -16.461 -25.197 10.315 1.00 104.49 ? 466 THR A O   1 
ATOM   1292 C  CB  . THR A 1 170 ? -17.055 -23.529 7.127  1.00 80.45  ? 466 THR A CB  1 
ATOM   1293 O  OG1 . THR A 1 170 ? -15.865 -22.799 6.794  1.00 77.03  ? 466 THR A OG1 1 
ATOM   1294 C  CG2 . THR A 1 170 ? -18.293 -22.874 6.484  1.00 77.23  ? 466 THR A CG2 1 
ATOM   1295 N  N   . ASP A 1 171 ? -14.960 -24.638 8.741  1.00 91.71  ? 467 ASP A N   1 
ATOM   1296 C  CA  . ASP A 1 171 ? -13.931 -25.486 9.334  1.00 100.53 ? 467 ASP A CA  1 
ATOM   1297 C  C   . ASP A 1 171 ? -13.406 -24.888 10.629 1.00 105.93 ? 467 ASP A C   1 
ATOM   1298 O  O   . ASP A 1 171 ? -13.339 -25.570 11.654 1.00 112.44 ? 467 ASP A O   1 
ATOM   1299 C  CB  . ASP A 1 171 ? -12.788 -25.669 8.334  1.00 106.63 ? 467 ASP A CB  1 
ATOM   1300 C  CG  . ASP A 1 171 ? -12.258 -24.343 7.829  1.00 107.06 ? 467 ASP A CG  1 
ATOM   1301 O  OD1 . ASP A 1 171 ? -13.070 -23.399 7.671  1.00 104.44 ? 467 ASP A OD1 1 
ATOM   1302 O  OD2 . ASP A 1 171 ? -11.036 -24.234 7.610  1.00 108.25 ? 467 ASP A OD2 1 
ATOM   1303 N  N   . GLY A 1 172 ? -13.031 -23.612 10.597 1.00 104.62 ? 468 GLY A N   1 
ATOM   1304 C  CA  . GLY A 1 172 ? -12.370 -22.973 11.717 1.00 104.63 ? 468 GLY A CA  1 
ATOM   1305 C  C   . GLY A 1 172 ? -11.288 -22.015 11.260 1.00 105.52 ? 468 GLY A C   1 
ATOM   1306 O  O   . GLY A 1 172 ? -11.075 -20.977 11.891 1.00 102.04 ? 468 GLY A O   1 
ATOM   1307 N  N   . LYS A 1 173 ? -10.589 -22.353 10.171 1.00 111.00 ? 469 LYS A N   1 
ATOM   1308 C  CA  . LYS A 1 173 ? -9.609  -21.426 9.608  1.00 117.07 ? 469 LYS A CA  1 
ATOM   1309 C  C   . LYS A 1 173 ? -10.286 -20.337 8.796  1.00 112.84 ? 469 LYS A C   1 
ATOM   1310 O  O   . LYS A 1 173 ? -9.887  -19.170 8.852  1.00 116.23 ? 469 LYS A O   1 
ATOM   1311 C  CB  . LYS A 1 173 ? -8.608  -22.158 8.714  1.00 122.63 ? 469 LYS A CB  1 
ATOM   1312 C  CG  . LYS A 1 173 ? -7.782  -23.222 9.404  1.00 128.52 ? 469 LYS A CG  1 
ATOM   1313 C  CD  . LYS A 1 173 ? -8.430  -24.581 9.259  1.00 129.68 ? 469 LYS A CD  1 
ATOM   1314 C  CE  . LYS A 1 173 ? -7.541  -25.674 9.803  1.00 134.77 ? 469 LYS A CE  1 
ATOM   1315 N  NZ  . LYS A 1 173 ? -8.275  -26.961 9.920  1.00 139.49 ? 469 LYS A NZ  1 
ATOM   1316 N  N   . HIS A 1 174 ? -11.303 -20.710 8.035  1.00 100.01 ? 470 HIS A N   1 
ATOM   1317 C  CA  . HIS A 1 174 ? -12.007 -19.780 7.164  1.00 97.74  ? 470 HIS A CA  1 
ATOM   1318 C  C   . HIS A 1 174 ? -13.113 -19.137 7.976  1.00 103.16 ? 470 HIS A C   1 
ATOM   1319 O  O   . HIS A 1 174 ? -14.161 -19.738 8.231  1.00 105.67 ? 470 HIS A O   1 
ATOM   1320 C  CB  . HIS A 1 174 ? -12.501 -20.519 5.935  1.00 94.97  ? 470 HIS A CB  1 
ATOM   1321 C  CG  . HIS A 1 174 ? -11.403 -21.244 5.233  1.00 99.13  ? 470 HIS A CG  1 
ATOM   1322 N  ND1 . HIS A 1 174 ? -11.393 -22.612 5.075  1.00 103.76 ? 470 HIS A ND1 1 
ATOM   1323 C  CD2 . HIS A 1 174 ? -10.237 -20.795 4.713  1.00 103.18 ? 470 HIS A CD2 1 
ATOM   1324 C  CE1 . HIS A 1 174 ? -10.287 -22.971 4.448  1.00 109.70 ? 470 HIS A CE1 1 
ATOM   1325 N  NE2 . HIS A 1 174 ? -9.568  -21.887 4.218  1.00 108.93 ? 470 HIS A NE2 1 
ATOM   1326 N  N   . ASP A 1 175 ? -12.842 -17.915 8.414  1.00 103.39 ? 471 ASP A N   1 
ATOM   1327 C  CA  . ASP A 1 175 ? -13.649 -17.210 9.394  1.00 94.79  ? 471 ASP A CA  1 
ATOM   1328 C  C   . ASP A 1 175 ? -13.709 -15.752 8.996  1.00 89.77  ? 471 ASP A C   1 
ATOM   1329 O  O   . ASP A 1 175 ? -12.673 -15.139 8.723  1.00 98.57  ? 471 ASP A O   1 
ATOM   1330 C  CB  . ASP A 1 175 ? -13.056 -17.334 10.798 1.00 93.87  ? 471 ASP A CB  1 
ATOM   1331 C  CG  . ASP A 1 175 ? -13.478 -18.595 11.487 1.00 96.88  ? 471 ASP A CG  1 
ATOM   1332 O  OD1 . ASP A 1 175 ? -13.262 -19.685 10.923 1.00 107.61 ? 471 ASP A OD1 1 
ATOM   1333 O  OD2 . ASP A 1 175 ? -14.040 -18.496 12.586 1.00 98.30  ? 471 ASP A OD2 1 
ATOM   1334 N  N   . PHE A 1 176 ? -14.912 -15.208 8.951  1.00 81.08  ? 472 PHE A N   1 
ATOM   1335 C  CA  . PHE A 1 176 ? -15.089 -13.782 8.749  1.00 78.59  ? 472 PHE A CA  1 
ATOM   1336 C  C   . PHE A 1 176 ? -15.038 -13.099 10.110 1.00 71.69  ? 472 PHE A C   1 
ATOM   1337 O  O   . PHE A 1 176 ? -15.742 -13.512 11.034 1.00 73.60  ? 472 PHE A O   1 
ATOM   1338 C  CB  . PHE A 1 176 ? -16.409 -13.508 8.029  1.00 74.27  ? 472 PHE A CB  1 
ATOM   1339 C  CG  . PHE A 1 176 ? -16.388 -13.890 6.573  1.00 67.81  ? 472 PHE A CG  1 
ATOM   1340 C  CD1 . PHE A 1 176 ? -16.424 -15.224 6.185  1.00 59.34  ? 472 PHE A CD1 1 
ATOM   1341 C  CD2 . PHE A 1 176 ? -16.316 -12.917 5.601  1.00 58.72  ? 472 PHE A CD2 1 
ATOM   1342 C  CE1 . PHE A 1 176 ? -16.398 -15.564 4.862  1.00 72.44  ? 472 PHE A CE1 1 
ATOM   1343 C  CE2 . PHE A 1 176 ? -16.272 -13.257 4.285  1.00 69.21  ? 472 PHE A CE2 1 
ATOM   1344 C  CZ  . PHE A 1 176 ? -16.319 -14.581 3.909  1.00 66.57  ? 472 PHE A CZ  1 
ATOM   1345 N  N   . ARG A 1 177 ? -14.173 -12.091 10.242 1.00 64.84  ? 473 ARG A N   1 
ATOM   1346 C  CA  . ARG A 1 177 ? -13.993 -11.373 11.499 1.00 67.52  ? 473 ARG A CA  1 
ATOM   1347 C  C   . ARG A 1 177 ? -13.822 -9.884  11.237 1.00 72.13  ? 473 ARG A C   1 
ATOM   1348 O  O   . ARG A 1 177 ? -12.986 -9.491  10.417 1.00 79.49  ? 473 ARG A O   1 
ATOM   1349 C  CB  . ARG A 1 177 ? -12.777 -11.912 12.258 1.00 72.83  ? 473 ARG A CB  1 
ATOM   1350 C  CG  . ARG A 1 177 ? -12.973 -13.300 12.833 1.00 72.80  ? 473 ARG A CG  1 
ATOM   1351 C  CD  . ARG A 1 177 ? -13.978 -13.243 13.959 1.00 75.71  ? 473 ARG A CD  1 
ATOM   1352 N  NE  . ARG A 1 177 ? -13.520 -12.350 15.016 1.00 85.09  ? 473 ARG A NE  1 
ATOM   1353 C  CZ  . ARG A 1 177 ? -12.914 -12.747 16.134 1.00 81.14  ? 473 ARG A CZ  1 
ATOM   1354 N  NH1 . ARG A 1 177 ? -12.694 -14.036 16.365 1.00 84.13  ? 473 ARG A NH1 1 
ATOM   1355 N  NH2 . ARG A 1 177 ? -12.537 -11.846 17.027 1.00 77.57  ? 473 ARG A NH2 1 
ATOM   1356 N  N   . VAL A 1 178 ? -14.614 -9.065  11.928 1.00 65.29  ? 474 VAL A N   1 
ATOM   1357 C  CA  . VAL A 1 178 ? -14.335 -7.637  12.070 1.00 56.12  ? 474 VAL A CA  1 
ATOM   1358 C  C   . VAL A 1 178 ? -13.362 -7.494  13.231 1.00 75.56  ? 474 VAL A C   1 
ATOM   1359 O  O   . VAL A 1 178 ? -13.731 -7.724  14.388 1.00 71.90  ? 474 VAL A O   1 
ATOM   1360 C  CB  . VAL A 1 178 ? -15.610 -6.824  12.324 1.00 60.82  ? 474 VAL A CB  1 
ATOM   1361 C  CG1 . VAL A 1 178 ? -15.301 -5.324  12.276 1.00 65.19  ? 474 VAL A CG1 1 
ATOM   1362 C  CG2 . VAL A 1 178 ? -16.714 -7.202  11.334 1.00 70.36  ? 474 VAL A CG2 1 
ATOM   1363 N  N   . TRP A 1 179 ? -12.113 -7.127  12.934 1.00 77.19  ? 475 TRP A N   1 
ATOM   1364 C  CA  . TRP A 1 179 ? -11.129 -7.056  14.013 1.00 75.33  ? 475 TRP A CA  1 
ATOM   1365 C  C   . TRP A 1 179 ? -11.386 -5.902  14.975 1.00 71.60  ? 475 TRP A C   1 
ATOM   1366 O  O   . TRP A 1 179 ? -10.960 -5.976  16.135 1.00 68.98  ? 475 TRP A O   1 
ATOM   1367 C  CB  . TRP A 1 179 ? -9.716  -6.971  13.442 1.00 72.31  ? 475 TRP A CB  1 
ATOM   1368 C  CG  . TRP A 1 179 ? -9.225  -8.293  12.960 1.00 71.01  ? 475 TRP A CG  1 
ATOM   1369 C  CD1 . TRP A 1 179 ? -9.979  -9.306  12.444 1.00 82.96  ? 475 TRP A CD1 1 
ATOM   1370 C  CD2 . TRP A 1 179 ? -7.875  -8.760  12.966 1.00 74.41  ? 475 TRP A CD2 1 
ATOM   1371 N  NE1 . TRP A 1 179 ? -9.178  -10.371 12.109 1.00 93.36  ? 475 TRP A NE1 1 
ATOM   1372 C  CE2 . TRP A 1 179 ? -7.881  -10.060 12.421 1.00 91.82  ? 475 TRP A CE2 1 
ATOM   1373 C  CE3 . TRP A 1 179 ? -6.659  -8.199  13.361 1.00 74.95  ? 475 TRP A CE3 1 
ATOM   1374 C  CZ2 . TRP A 1 179 ? -6.720  -10.812 12.274 1.00 97.92  ? 475 TRP A CZ2 1 
ATOM   1375 C  CZ3 . TRP A 1 179 ? -5.508  -8.949  13.215 1.00 87.96  ? 475 TRP A CZ3 1 
ATOM   1376 C  CH2 . TRP A 1 179 ? -5.547  -10.241 12.676 1.00 96.73  ? 475 TRP A CH2 1 
ATOM   1377 N  N   . ASN A 1 180 ? -12.079 -4.853  14.538 1.00 65.56  ? 476 ASN A N   1 
ATOM   1378 C  CA  . ASN A 1 180 ? -12.463 -3.786  15.452 1.00 65.57  ? 476 ASN A CA  1 
ATOM   1379 C  C   . ASN A 1 180 ? -13.393 -4.324  16.530 1.00 68.63  ? 476 ASN A C   1 
ATOM   1380 O  O   . ASN A 1 180 ? -14.193 -5.234  16.284 1.00 55.40  ? 476 ASN A O   1 
ATOM   1381 C  CB  . ASN A 1 180 ? -13.157 -2.663  14.689 1.00 67.21  ? 476 ASN A CB  1 
ATOM   1382 C  CG  . ASN A 1 180 ? -12.283 -2.089  13.608 1.00 70.76  ? 476 ASN A CG  1 
ATOM   1383 O  OD1 . ASN A 1 180 ? -11.950 -2.779  12.649 1.00 81.50  ? 476 ASN A OD1 1 
ATOM   1384 N  ND2 . ASN A 1 180 ? -11.890 -0.826  13.760 1.00 67.57  ? 476 ASN A ND2 1 
ATOM   1385 N  N   . SER A 1 181 ? -13.279 -3.754  17.745 1.00 60.11  ? 477 SER A N   1 
ATOM   1386 C  CA  . SER A 1 181 ? -14.198 -4.126  18.815 1.00 52.23  ? 477 SER A CA  1 
ATOM   1387 C  C   . SER A 1 181 ? -15.571 -3.498  18.598 1.00 61.13  ? 477 SER A C   1 
ATOM   1388 O  O   . SER A 1 181 ? -16.602 -4.165  18.758 1.00 54.26  ? 477 SER A O   1 
ATOM   1389 C  CB  . SER A 1 181 ? -13.625 -3.723  20.180 1.00 68.33  ? 477 SER A CB  1 
ATOM   1390 O  OG  . SER A 1 181 ? -13.076 -2.411  20.174 1.00 75.31  ? 477 SER A OG  1 
ATOM   1391 N  N   . GLN A 1 182 ? -15.607 -2.219  18.231 1.00 67.31  ? 478 GLN A N   1 
ATOM   1392 C  CA  . GLN A 1 182 ? -16.808 -1.595  17.693 1.00 57.70  ? 478 GLN A CA  1 
ATOM   1393 C  C   . GLN A 1 182 ? -16.485 -1.020  16.325 1.00 46.63  ? 478 GLN A C   1 
ATOM   1394 O  O   . GLN A 1 182 ? -15.340 -0.658  16.038 1.00 54.48  ? 478 GLN A O   1 
ATOM   1395 C  CB  . GLN A 1 182 ? -17.336 -0.457  18.566 1.00 56.01  ? 478 GLN A CB  1 
ATOM   1396 C  CG  . GLN A 1 182 ? -17.372 -0.707  20.046 1.00 47.18  ? 478 GLN A CG  1 
ATOM   1397 C  CD  . GLN A 1 182 ? -17.651 0.579   20.821 1.00 55.58  ? 478 GLN A CD  1 
ATOM   1398 O  OE1 . GLN A 1 182 ? -17.925 1.633   20.239 1.00 50.70  ? 478 GLN A OE1 1 
ATOM   1399 N  NE2 . GLN A 1 182 ? -17.574 0.501   22.126 1.00 46.77  ? 478 GLN A NE2 1 
ATOM   1400 N  N   . LEU A 1 183 ? -17.509 -0.866  15.496 1.00 41.90  ? 479 LEU A N   1 
ATOM   1401 C  CA  . LEU A 1 183 ? -17.234 -0.375  14.138 1.00 49.22  ? 479 LEU A CA  1 
ATOM   1402 C  C   . LEU A 1 183 ? -16.643 1.026   14.172 1.00 53.32  ? 479 LEU A C   1 
ATOM   1403 O  O   . LEU A 1 183 ? -15.790 1.379   13.348 1.00 56.80  ? 479 LEU A O   1 
ATOM   1404 C  CB  . LEU A 1 183 ? -18.505 -0.365  13.296 1.00 47.80  ? 479 LEU A CB  1 
ATOM   1405 C  CG  . LEU A 1 183 ? -19.292 -1.642  13.062 1.00 54.84  ? 479 LEU A CG  1 
ATOM   1406 C  CD1 . LEU A 1 183 ? -20.448 -1.292  12.110 1.00 38.06  ? 479 LEU A CD1 1 
ATOM   1407 C  CD2 . LEU A 1 183 ? -18.357 -2.676  12.491 1.00 69.68  ? 479 LEU A CD2 1 
ATOM   1408 N  N   . ILE A 1 184 ? -17.096 1.848   15.112 1.00 55.74  ? 480 ILE A N   1 
ATOM   1409 C  CA  . ILE A 1 184 ? -16.646 3.224   15.230 1.00 46.68  ? 480 ILE A CA  1 
ATOM   1410 C  C   . ILE A 1 184 ? -16.087 3.434   16.618 1.00 54.87  ? 480 ILE A C   1 
ATOM   1411 O  O   . ILE A 1 184 ? -16.823 3.338   17.605 1.00 60.66  ? 480 ILE A O   1 
ATOM   1412 C  CB  . ILE A 1 184 ? -17.765 4.225   14.921 1.00 48.55  ? 480 ILE A CB  1 
ATOM   1413 C  CG1 . ILE A 1 184 ? -18.022 4.224   13.410 1.00 57.55  ? 480 ILE A CG1 1 
ATOM   1414 C  CG2 . ILE A 1 184 ? -17.370 5.635   15.365 1.00 47.34  ? 480 ILE A CG2 1 
ATOM   1415 C  CD1 . ILE A 1 184 ? -19.375 4.747   13.030 1.00 65.89  ? 480 ILE A CD1 1 
ATOM   1416 N  N   . ARG A 1 185 ? -14.779 3.680   16.694 1.00 63.09  ? 481 ARG A N   1 
ATOM   1417 C  CA  . ARG A 1 185 ? -14.075 4.008   17.920 1.00 62.58  ? 481 ARG A CA  1 
ATOM   1418 C  C   . ARG A 1 185 ? -12.966 5.007   17.614 1.00 65.97  ? 481 ARG A C   1 
ATOM   1419 O  O   . ARG A 1 185 ? -12.387 4.997   16.528 1.00 75.69  ? 481 ARG A O   1 
ATOM   1420 C  CB  . ARG A 1 185 ? -13.489 2.761   18.585 1.00 66.73  ? 481 ARG A CB  1 
ATOM   1421 C  CG  . ARG A 1 185 ? -14.521 1.773   19.079 1.00 63.97  ? 481 ARG A CG  1 
ATOM   1422 C  CD  . ARG A 1 185 ? -13.963 0.910   20.202 1.00 61.05  ? 481 ARG A CD  1 
ATOM   1423 N  NE  . ARG A 1 185 ? -13.891 1.661   21.448 1.00 66.00  ? 481 ARG A NE  1 
ATOM   1424 C  CZ  . ARG A 1 185 ? -13.672 1.111   22.637 1.00 65.07  ? 481 ARG A CZ  1 
ATOM   1425 N  NH1 . ARG A 1 185 ? -13.498 -0.201  22.743 1.00 57.52  ? 481 ARG A NH1 1 
ATOM   1426 N  NH2 . ARG A 1 185 ? -13.616 1.880   23.720 1.00 59.59  ? 481 ARG A NH2 1 
ATOM   1427 N  N   . TYR A 1 186 ? -12.664 5.857   18.598 1.00 54.68  ? 482 TYR A N   1 
ATOM   1428 C  CA  . TYR A 1 186 ? -11.589 6.837   18.497 1.00 62.04  ? 482 TYR A CA  1 
ATOM   1429 C  C   . TYR A 1 186 ? -10.225 6.193   18.716 1.00 74.33  ? 482 TYR A C   1 
ATOM   1430 O  O   . TYR A 1 186 ? -10.065 5.294   19.549 1.00 84.99  ? 482 TYR A O   1 
ATOM   1431 C  CB  . TYR A 1 186 ? -11.814 7.981   19.509 1.00 72.50  ? 482 TYR A CB  1 
ATOM   1432 C  CG  . TYR A 1 186 ? -13.101 8.716   19.178 1.00 77.79  ? 482 TYR A CG  1 
ATOM   1433 C  CD1 . TYR A 1 186 ? -14.199 8.660   20.016 1.00 72.22  ? 482 TYR A CD1 1 
ATOM   1434 C  CD2 . TYR A 1 186 ? -13.242 9.389   17.968 1.00 65.28  ? 482 TYR A CD2 1 
ATOM   1435 C  CE1 . TYR A 1 186 ? -15.388 9.299   19.686 1.00 75.55  ? 482 TYR A CE1 1 
ATOM   1436 C  CE2 . TYR A 1 186 ? -14.428 10.038  17.633 1.00 70.79  ? 482 TYR A CE2 1 
ATOM   1437 C  CZ  . TYR A 1 186 ? -15.502 9.977   18.488 1.00 76.27  ? 482 TYR A CZ  1 
ATOM   1438 O  OH  . TYR A 1 186 ? -16.687 10.603  18.151 1.00 75.51  ? 482 TYR A OH  1 
ATOM   1439 N  N   . ALA A 1 187 ? -9.234  6.693   17.982 1.00 81.84  ? 483 ALA A N   1 
ATOM   1440 C  CA  . ALA A 1 187 ? -7.893  6.132   18.006 1.00 88.85  ? 483 ALA A CA  1 
ATOM   1441 C  C   . ALA A 1 187 ? -7.257  6.301   19.380 1.00 103.09 ? 483 ALA A C   1 
ATOM   1442 O  O   . ALA A 1 187 ? -7.686  7.115   20.204 1.00 100.94 ? 483 ALA A O   1 
ATOM   1443 C  CB  . ALA A 1 187 ? -7.018  6.792   16.940 1.00 91.96  ? 483 ALA A CB  1 
ATOM   1444 N  N   . GLY A 1 188 ? -6.219  5.506   19.622 1.00 106.94 ? 484 GLY A N   1 
ATOM   1445 C  CA  . GLY A 1 188 ? -5.504  5.559   20.878 1.00 112.38 ? 484 GLY A CA  1 
ATOM   1446 C  C   . GLY A 1 188 ? -4.003  5.515   20.708 1.00 117.17 ? 484 GLY A C   1 
ATOM   1447 O  O   . GLY A 1 188 ? -3.436  4.488   20.325 1.00 121.93 ? 484 GLY A O   1 
ATOM   1448 N  N   . TYR A 1 189 ? -3.345  6.630   20.991 1.00 116.76 ? 485 TYR A N   1 
ATOM   1449 C  CA  . TYR A 1 189 ? -1.900  6.728   20.883 1.00 113.02 ? 485 TYR A CA  1 
ATOM   1450 C  C   . TYR A 1 189 ? -1.323  7.009   22.258 1.00 115.43 ? 485 TYR A C   1 
ATOM   1451 O  O   . TYR A 1 189 ? -1.764  7.939   22.943 1.00 105.85 ? 485 TYR A O   1 
ATOM   1452 C  CB  . TYR A 1 189 ? -1.480  7.837   19.915 1.00 113.61 ? 485 TYR A CB  1 
ATOM   1453 C  CG  . TYR A 1 189 ? -2.347  7.973   18.688 1.00 102.06 ? 485 TYR A CG  1 
ATOM   1454 C  CD1 . TYR A 1 189 ? -3.398  8.882   18.654 1.00 99.04  ? 485 TYR A CD1 1 
ATOM   1455 C  CD2 . TYR A 1 189 ? -2.103  7.208   17.556 1.00 107.54 ? 485 TYR A CD2 1 
ATOM   1456 C  CE1 . TYR A 1 189 ? -4.188  9.021   17.521 1.00 103.40 ? 485 TYR A CE1 1 
ATOM   1457 C  CE2 . TYR A 1 189 ? -2.885  7.337   16.423 1.00 103.45 ? 485 TYR A CE2 1 
ATOM   1458 C  CZ  . TYR A 1 189 ? -3.923  8.244   16.406 1.00 104.83 ? 485 TYR A CZ  1 
ATOM   1459 O  OH  . TYR A 1 189 ? -4.699  8.368   15.274 1.00 110.91 ? 485 TYR A OH  1 
ATOM   1460 N  N   . LYS A 1 190 ? -0.353  6.201   22.664 1.00 122.21 ? 486 LYS A N   1 
ATOM   1461 C  CA  . LYS A 1 190 ? 0.456   6.562   23.811 1.00 131.08 ? 486 LYS A CA  1 
ATOM   1462 C  C   . LYS A 1 190 ? 1.492   7.591   23.373 1.00 138.56 ? 486 LYS A C   1 
ATOM   1463 O  O   . LYS A 1 190 ? 1.944   7.598   22.225 1.00 138.13 ? 486 LYS A O   1 
ATOM   1464 C  CB  . LYS A 1 190 ? 1.120   5.325   24.420 1.00 133.12 ? 486 LYS A CB  1 
ATOM   1465 C  CG  . LYS A 1 190 ? 2.582   5.140   24.060 1.00 138.25 ? 486 LYS A CG  1 
ATOM   1466 C  CD  . LYS A 1 190 ? 3.080   3.752   24.440 1.00 135.89 ? 486 LYS A CD  1 
ATOM   1467 C  CE  . LYS A 1 190 ? 2.428   2.681   23.574 1.00 129.63 ? 486 LYS A CE  1 
ATOM   1468 N  NZ  . LYS A 1 190 ? 3.040   1.335   23.772 1.00 127.84 ? 486 LYS A NZ  1 
ATOM   1469 N  N   . GLN A 1 191 ? 1.836   8.482   24.283 1.00 145.89 ? 487 GLN A N   1 
ATOM   1470 C  CA  . GLN A 1 191 ? 2.696   9.604   23.947 1.00 152.19 ? 487 GLN A CA  1 
ATOM   1471 C  C   . GLN A 1 191 ? 4.145   9.305   24.298 1.00 157.42 ? 487 GLN A C   1 
ATOM   1472 O  O   . GLN A 1 191 ? 4.433   8.396   25.083 1.00 159.42 ? 487 GLN A O   1 
ATOM   1473 C  CB  . GLN A 1 191 ? 2.229   10.864  24.684 1.00 153.80 ? 487 GLN A CB  1 
ATOM   1474 C  CG  . GLN A 1 191 ? 0.873   11.390  24.229 1.00 149.65 ? 487 GLN A CG  1 
ATOM   1475 C  CD  . GLN A 1 191 ? 0.908   12.030  22.844 1.00 152.16 ? 487 GLN A CD  1 
ATOM   1476 O  OE1 . GLN A 1 191 ? 1.285   11.399  21.854 1.00 150.99 ? 487 GLN A OE1 1 
ATOM   1477 N  NE2 . GLN A 1 191 ? 0.505   13.293  22.773 1.00 153.69 ? 487 GLN A NE2 1 
ATOM   1478 N  N   . PRO A 1 192 ? 5.095   10.044  23.712 1.00 160.31 ? 488 PRO A N   1 
ATOM   1479 C  CA  . PRO A 1 192 ? 6.496   9.884   24.132 1.00 164.98 ? 488 PRO A CA  1 
ATOM   1480 C  C   . PRO A 1 192 ? 6.720   10.179  25.606 1.00 170.93 ? 488 PRO A C   1 
ATOM   1481 O  O   . PRO A 1 192 ? 7.652   9.627   26.206 1.00 175.68 ? 488 PRO A O   1 
ATOM   1482 C  CB  . PRO A 1 192 ? 7.248   10.876  23.229 1.00 166.62 ? 488 PRO A CB  1 
ATOM   1483 C  CG  . PRO A 1 192 ? 6.195   11.793  22.676 1.00 165.50 ? 488 PRO A CG  1 
ATOM   1484 C  CD  . PRO A 1 192 ? 4.968   10.955  22.562 1.00 161.18 ? 488 PRO A CD  1 
ATOM   1485 N  N   . ASP A 1 193 ? 5.883   11.023  26.217 1.00 167.89 ? 489 ASP A N   1 
ATOM   1486 C  CA  . ASP A 1 193 ? 5.988   11.353  27.634 1.00 166.51 ? 489 ASP A CA  1 
ATOM   1487 C  C   . ASP A 1 193 ? 5.215   10.387  28.528 1.00 155.08 ? 489 ASP A C   1 
ATOM   1488 O  O   . ASP A 1 193 ? 4.768   10.775  29.617 1.00 149.37 ? 489 ASP A O   1 
ATOM   1489 C  CB  . ASP A 1 193 ? 5.526   12.793  27.875 1.00 171.17 ? 489 ASP A CB  1 
ATOM   1490 C  CG  . ASP A 1 193 ? 4.331   13.182  27.018 1.00 168.58 ? 489 ASP A CG  1 
ATOM   1491 O  OD1 . ASP A 1 193 ? 4.382   12.975  25.784 1.00 168.47 ? 489 ASP A OD1 1 
ATOM   1492 O  OD2 . ASP A 1 193 ? 3.342   13.701  27.578 1.00 165.93 ? 489 ASP A OD2 1 
ATOM   1493 N  N   . GLY A 1 194 ? 5.042   9.141   28.098 1.00 149.87 ? 490 GLY A N   1 
ATOM   1494 C  CA  . GLY A 1 194 ? 4.373   8.150   28.918 1.00 143.95 ? 490 GLY A CA  1 
ATOM   1495 C  C   . GLY A 1 194 ? 2.857   8.202   28.889 1.00 137.80 ? 490 GLY A C   1 
ATOM   1496 O  O   . GLY A 1 194 ? 2.196   7.159   28.947 1.00 131.35 ? 490 GLY A O   1 
ATOM   1497 N  N   . SER A 1 195 ? 2.290   9.405   28.797 1.00 140.62 ? 491 SER A N   1 
ATOM   1498 C  CA  . SER A 1 195 ? 0.841   9.579   28.832 1.00 140.19 ? 491 SER A CA  1 
ATOM   1499 C  C   . SER A 1 195 ? 0.172   9.023   27.578 1.00 143.44 ? 491 SER A C   1 
ATOM   1500 O  O   . SER A 1 195 ? 0.791   8.276   26.812 1.00 144.79 ? 491 SER A O   1 
ATOM   1501 C  CB  . SER A 1 195 ? 0.489   11.056  29.015 1.00 140.90 ? 491 SER A CB  1 
ATOM   1502 O  OG  . SER A 1 195 ? 1.088   11.849  28.005 1.00 144.49 ? 491 SER A OG  1 
ATOM   1503 N  N   . THR A 1 196 ? -1.092  9.385   27.352 1.00 138.83 ? 492 THR A N   1 
ATOM   1504 C  CA  . THR A 1 196 ? -1.878  8.771   26.287 1.00 132.89 ? 492 THR A CA  1 
ATOM   1505 C  C   . THR A 1 196 ? -2.847  9.784   25.687 1.00 130.37 ? 492 THR A C   1 
ATOM   1506 O  O   . THR A 1 196 ? -3.527  10.507  26.422 1.00 130.28 ? 492 THR A O   1 
ATOM   1507 C  CB  . THR A 1 196 ? -2.642  7.552   26.825 1.00 125.16 ? 492 THR A CB  1 
ATOM   1508 O  OG1 . THR A 1 196 ? -1.732  6.677   27.509 1.00 123.67 ? 492 THR A OG1 1 
ATOM   1509 C  CG2 . THR A 1 196 ? -3.314  6.791   25.692 1.00 119.31 ? 492 THR A CG2 1 
ATOM   1510 N  N   . LEU A 1 197 ? -2.911  9.826   24.355 1.00 127.59 ? 493 LEU A N   1 
ATOM   1511 C  CA  . LEU A 1 197 ? -3.842  10.678  23.622 1.00 122.93 ? 493 LEU A CA  1 
ATOM   1512 C  C   . LEU A 1 197 ? -4.912  9.827   22.949 1.00 107.32 ? 493 LEU A C   1 
ATOM   1513 O  O   . LEU A 1 197 ? -4.618  8.756   22.406 1.00 102.18 ? 493 LEU A O   1 
ATOM   1514 C  CB  . LEU A 1 197 ? -3.109  11.524  22.568 1.00 128.96 ? 493 LEU A CB  1 
ATOM   1515 C  CG  . LEU A 1 197 ? -3.921  12.470  21.674 1.00 128.26 ? 493 LEU A CG  1 
ATOM   1516 C  CD1 . LEU A 1 197 ? -4.923  13.296  22.469 1.00 126.95 ? 493 LEU A CD1 1 
ATOM   1517 C  CD2 . LEU A 1 197 ? -2.996  13.391  20.882 1.00 135.91 ? 493 LEU A CD2 1 
ATOM   1518 N  N   . GLY A 1 198 ? -6.152  10.308  22.989 1.00 100.66 ? 494 GLY A N   1 
ATOM   1519 C  CA  . GLY A 1 198 ? -7.258  9.604   22.359 1.00 98.78  ? 494 GLY A CA  1 
ATOM   1520 C  C   . GLY A 1 198 ? -7.931  8.662   23.331 1.00 96.70  ? 494 GLY A C   1 
ATOM   1521 O  O   . GLY A 1 198 ? -8.264  9.051   24.449 1.00 108.24 ? 494 GLY A O   1 
ATOM   1522 N  N   . ASP A 1 199 ? -8.129  7.417   22.909 1.00 88.77  ? 495 ASP A N   1 
ATOM   1523 C  CA  . ASP A 1 199 ? -8.715  6.411   23.781 1.00 83.80  ? 495 ASP A CA  1 
ATOM   1524 C  C   . ASP A 1 199 ? -7.638  5.418   24.186 1.00 88.32  ? 495 ASP A C   1 
ATOM   1525 O  O   . ASP A 1 199 ? -7.079  4.737   23.311 1.00 83.30  ? 495 ASP A O   1 
ATOM   1526 C  CB  . ASP A 1 199 ? -9.871  5.695   23.084 1.00 75.23  ? 495 ASP A CB  1 
ATOM   1527 C  CG  . ASP A 1 199 ? -10.812 5.014   24.059 1.00 86.86  ? 495 ASP A CG  1 
ATOM   1528 O  OD1 . ASP A 1 199 ? -10.380 4.675   25.187 1.00 88.33  ? 495 ASP A OD1 1 
ATOM   1529 O  OD2 . ASP A 1 199 ? -11.994 4.817   23.698 1.00 82.04  ? 495 ASP A OD2 1 
ATOM   1530 N  N   . PRO A 1 200 ? -7.299  5.321   25.479 1.00 93.46  ? 496 PRO A N   1 
ATOM   1531 C  CA  . PRO A 1 200 ? -6.281  4.342   25.899 1.00 91.56  ? 496 PRO A CA  1 
ATOM   1532 C  C   . PRO A 1 200 ? -6.687  2.896   25.667 1.00 83.62  ? 496 PRO A C   1 
ATOM   1533 O  O   . PRO A 1 200 ? -5.810  2.044   25.484 1.00 77.60  ? 496 PRO A O   1 
ATOM   1534 C  CB  . PRO A 1 200 ? -6.102  4.641   27.395 1.00 94.26  ? 496 PRO A CB  1 
ATOM   1535 C  CG  . PRO A 1 200 ? -6.576  6.045   27.568 1.00 95.70  ? 496 PRO A CG  1 
ATOM   1536 C  CD  . PRO A 1 200 ? -7.691  6.218   26.579 1.00 90.53  ? 496 PRO A CD  1 
ATOM   1537 N  N   . ALA A 1 201 ? -7.988  2.589   25.679 1.00 84.01  ? 497 ALA A N   1 
ATOM   1538 C  CA  . ALA A 1 201 ? -8.434  1.218   25.447 1.00 80.50  ? 497 ALA A CA  1 
ATOM   1539 C  C   . ALA A 1 201 ? -7.984  0.691   24.088 1.00 92.55  ? 497 ALA A C   1 
ATOM   1540 O  O   . ALA A 1 201 ? -7.793  -0.520  23.924 1.00 97.81  ? 497 ALA A O   1 
ATOM   1541 C  CB  . ALA A 1 201 ? -9.959  1.140   25.560 1.00 65.60  ? 497 ALA A CB  1 
ATOM   1542 N  N   . ASN A 1 202 ? -7.804  1.574   23.106 1.00 95.72  ? 498 ASN A N   1 
ATOM   1543 C  CA  . ASN A 1 202 ? -7.558  1.166   21.730 1.00 91.77  ? 498 ASN A CA  1 
ATOM   1544 C  C   . ASN A 1 202 ? -6.085  1.200   21.339 1.00 98.74  ? 498 ASN A C   1 
ATOM   1545 O  O   . ASN A 1 202 ? -5.772  0.917   20.180 1.00 106.95 ? 498 ASN A O   1 
ATOM   1546 C  CB  . ASN A 1 202 ? -8.352  2.057   20.765 1.00 84.62  ? 498 ASN A CB  1 
ATOM   1547 C  CG  . ASN A 1 202 ? -9.853  2.023   21.019 1.00 77.77  ? 498 ASN A CG  1 
ATOM   1548 O  OD1 . ASN A 1 202 ? -10.436 0.963   21.269 1.00 81.96  ? 498 ASN A OD1 1 
ATOM   1549 N  ND2 . ASN A 1 202 ? -10.489 3.194   20.949 1.00 64.79  ? 498 ASN A ND2 1 
ATOM   1550 N  N   . VAL A 1 203 ? -5.175  1.534   22.261 1.00 98.25  ? 499 VAL A N   1 
ATOM   1551 C  CA  . VAL A 1 203 ? -3.786  1.777   21.870 1.00 103.20 ? 499 VAL A CA  1 
ATOM   1552 C  C   . VAL A 1 203 ? -3.146  0.511   21.312 1.00 107.75 ? 499 VAL A C   1 
ATOM   1553 O  O   . VAL A 1 203 ? -2.326  0.571   20.388 1.00 112.70 ? 499 VAL A O   1 
ATOM   1554 C  CB  . VAL A 1 203 ? -2.979  2.348   23.049 1.00 105.29 ? 499 VAL A CB  1 
ATOM   1555 C  CG1 . VAL A 1 203 ? -1.559  2.681   22.610 1.00 109.32 ? 499 VAL A CG1 1 
ATOM   1556 C  CG2 . VAL A 1 203 ? -3.656  3.587   23.580 1.00 109.12 ? 499 VAL A CG2 1 
ATOM   1557 N  N   . GLN A 1 204 ? -3.503  -0.652  21.857 1.00 109.71 ? 500 GLN A N   1 
ATOM   1558 C  CA  . GLN A 1 204 ? -3.029  -1.898  21.263 1.00 114.67 ? 500 GLN A CA  1 
ATOM   1559 C  C   . GLN A 1 204 ? -3.578  -2.058  19.850 1.00 113.02 ? 500 GLN A C   1 
ATOM   1560 O  O   . GLN A 1 204 ? -2.833  -2.363  18.910 1.00 115.91 ? 500 GLN A O   1 
ATOM   1561 C  CB  . GLN A 1 204 ? -3.419  -3.085  22.146 1.00 117.63 ? 500 GLN A CB  1 
ATOM   1562 C  CG  . GLN A 1 204 ? -2.412  -4.232  22.132 1.00 124.89 ? 500 GLN A CG  1 
ATOM   1563 C  CD  . GLN A 1 204 ? -2.475  -5.053  20.858 1.00 130.50 ? 500 GLN A CD  1 
ATOM   1564 O  OE1 . GLN A 1 204 ? -3.556  -5.424  20.402 1.00 129.24 ? 500 GLN A OE1 1 
ATOM   1565 N  NE2 . GLN A 1 204 ? -1.312  -5.338  20.274 1.00 135.66 ? 500 GLN A NE2 1 
ATOM   1566 N  N   . PHE A 1 205 ? -4.884  -1.829  19.681 1.00 104.27 ? 501 PHE A N   1 
ATOM   1567 C  CA  . PHE A 1 205 ? -5.497  -1.895  18.356 1.00 100.88 ? 501 PHE A CA  1 
ATOM   1568 C  C   . PHE A 1 205 ? -4.877  -0.874  17.410 1.00 97.12  ? 501 PHE A C   1 
ATOM   1569 O  O   . PHE A 1 205 ? -4.445  -1.218  16.304 1.00 90.73  ? 501 PHE A O   1 
ATOM   1570 C  CB  . PHE A 1 205 ? -7.007  -1.675  18.468 1.00 98.37  ? 501 PHE A CB  1 
ATOM   1571 C  CG  . PHE A 1 205 ? -7.746  -1.852  17.171 1.00 104.76 ? 501 PHE A CG  1 
ATOM   1572 C  CD1 . PHE A 1 205 ? -8.058  -3.122  16.704 1.00 107.97 ? 501 PHE A CD1 1 
ATOM   1573 C  CD2 . PHE A 1 205 ? -8.135  -0.754  16.417 1.00 106.95 ? 501 PHE A CD2 1 
ATOM   1574 C  CE1 . PHE A 1 205 ? -8.741  -3.296  15.499 1.00 105.18 ? 501 PHE A CE1 1 
ATOM   1575 C  CE2 . PHE A 1 205 ? -8.825  -0.924  15.216 1.00 105.99 ? 501 PHE A CE2 1 
ATOM   1576 C  CZ  . PHE A 1 205 ? -9.125  -2.197  14.760 1.00 101.85 ? 501 PHE A CZ  1 
ATOM   1577 N  N   . THR A 1 206 ? -4.827  0.393   17.839 1.00 98.17  ? 502 THR A N   1 
ATOM   1578 C  CA  . THR A 1 206 ? -4.271  1.465   17.017 1.00 101.02 ? 502 THR A CA  1 
ATOM   1579 C  C   . THR A 1 206 ? -2.872  1.124   16.520 1.00 102.61 ? 502 THR A C   1 
ATOM   1580 O  O   . THR A 1 206 ? -2.507  1.459   15.387 1.00 98.77  ? 502 THR A O   1 
ATOM   1581 C  CB  . THR A 1 206 ? -4.241  2.775   17.813 1.00 96.21  ? 502 THR A CB  1 
ATOM   1582 O  OG1 . THR A 1 206 ? -5.573  3.143   18.201 1.00 89.40  ? 502 THR A OG1 1 
ATOM   1583 C  CG2 . THR A 1 206 ? -3.611  3.908   16.991 1.00 88.47  ? 502 THR A CG2 1 
ATOM   1584 N  N   . GLU A 1 207 ? -2.068  0.467   17.360 1.00 106.01 ? 503 GLU A N   1 
ATOM   1585 C  CA  . GLU A 1 207 ? -0.741  0.050   16.924 1.00 111.33 ? 503 GLU A CA  1 
ATOM   1586 C  C   . GLU A 1 207 ? -0.836  -0.969  15.798 1.00 116.89 ? 503 GLU A C   1 
ATOM   1587 O  O   . GLU A 1 207 ? -0.114  -0.872  14.799 1.00 126.76 ? 503 GLU A O   1 
ATOM   1588 C  CB  . GLU A 1 207 ? 0.052   -0.515  18.100 1.00 108.58 ? 503 GLU A CB  1 
ATOM   1589 C  CG  . GLU A 1 207 ? 1.117   0.432   18.608 1.00 117.28 ? 503 GLU A CG  1 
ATOM   1590 C  CD  . GLU A 1 207 ? 1.236   0.402   20.119 1.00 122.61 ? 503 GLU A CD  1 
ATOM   1591 O  OE1 . GLU A 1 207 ? 0.994   -0.673  20.712 1.00 120.89 ? 503 GLU A OE1 1 
ATOM   1592 O  OE2 . GLU A 1 207 ? 1.559   1.456   20.711 1.00 124.20 ? 503 GLU A OE2 1 
ATOM   1593 N  N   . ILE A 1 208 ? -1.735  -1.951  15.937 1.00 112.28 ? 504 ILE A N   1 
ATOM   1594 C  CA  . ILE A 1 208 ? -1.928  -2.939  14.874 1.00 114.62 ? 504 ILE A CA  1 
ATOM   1595 C  C   . ILE A 1 208 ? -2.419  -2.273  13.595 1.00 107.42 ? 504 ILE A C   1 
ATOM   1596 O  O   . ILE A 1 208 ? -2.129  -2.745  12.491 1.00 111.19 ? 504 ILE A O   1 
ATOM   1597 C  CB  . ILE A 1 208 ? -2.896  -4.047  15.334 1.00 106.90 ? 504 ILE A CB  1 
ATOM   1598 C  CG1 . ILE A 1 208 ? -2.478  -4.589  16.694 1.00 106.39 ? 504 ILE A CG1 1 
ATOM   1599 C  CG2 . ILE A 1 208 ? -2.932  -5.183  14.319 1.00 103.75 ? 504 ILE A CG2 1 
ATOM   1600 C  CD1 . ILE A 1 208 ? -3.355  -5.710  17.190 1.00 107.09 ? 504 ILE A CD1 1 
ATOM   1601 N  N   . CYS A 1 209 ? -3.175  -1.177  13.720 1.00 107.92 ? 505 CYS A N   1 
ATOM   1602 C  CA  . CYS A 1 209 ? -3.654  -0.453  12.546 1.00 106.23 ? 505 CYS A CA  1 
ATOM   1603 C  C   . CYS A 1 209 ? -2.512  0.260   11.840 1.00 116.53 ? 505 CYS A C   1 
ATOM   1604 O  O   . CYS A 1 209 ? -2.316  0.091   10.630 1.00 120.71 ? 505 CYS A O   1 
ATOM   1605 C  CB  . CYS A 1 209 ? -4.738  0.551   12.940 1.00 101.76 ? 505 CYS A CB  1 
ATOM   1606 S  SG  . CYS A 1 209 ? -6.416  -0.107  12.931 1.00 98.89  ? 505 CYS A SG  1 
ATOM   1607 N  N   . ILE A 1 210 ? -1.754  1.081   12.575 1.00 117.38 ? 506 ILE A N   1 
ATOM   1608 C  CA  . ILE A 1 210 ? -0.564  1.684   11.982 1.00 123.44 ? 506 ILE A CA  1 
ATOM   1609 C  C   . ILE A 1 210 ? 0.388   0.597   11.504 1.00 129.45 ? 506 ILE A C   1 
ATOM   1610 O  O   . ILE A 1 210 ? 1.083   0.765   10.492 1.00 126.40 ? 506 ILE A O   1 
ATOM   1611 C  CB  . ILE A 1 210 ? 0.122   2.641   12.977 1.00 117.16 ? 506 ILE A CB  1 
ATOM   1612 C  CG1 . ILE A 1 210 ? -0.902  3.570   13.627 1.00 112.32 ? 506 ILE A CG1 1 
ATOM   1613 C  CG2 . ILE A 1 210 ? 1.175   3.476   12.259 1.00 121.84 ? 506 ILE A CG2 1 
ATOM   1614 C  CD1 . ILE A 1 210 ? -0.336  4.397   14.771 1.00 115.93 ? 506 ILE A CD1 1 
ATOM   1615 N  N   . GLN A 1 211 ? 0.415   -0.542  12.206 1.00 135.29 ? 507 GLN A N   1 
ATOM   1616 C  CA  . GLN A 1 211 ? 1.237   -1.674  11.786 1.00 140.66 ? 507 GLN A CA  1 
ATOM   1617 C  C   . GLN A 1 211 ? 0.869   -2.131  10.377 1.00 138.36 ? 507 GLN A C   1 
ATOM   1618 O  O   . GLN A 1 211 ? 1.748   -2.349  9.535  1.00 141.26 ? 507 GLN A O   1 
ATOM   1619 C  CB  . GLN A 1 211 ? 1.088   -2.823  12.786 1.00 141.02 ? 507 GLN A CB  1 
ATOM   1620 C  CG  . GLN A 1 211 ? 2.393   -3.498  13.161 1.00 147.57 ? 507 GLN A CG  1 
ATOM   1621 C  CD  . GLN A 1 211 ? 2.395   -4.977  12.835 1.00 149.04 ? 507 GLN A CD  1 
ATOM   1622 O  OE1 . GLN A 1 211 ? 1.341   -5.613  12.781 1.00 144.78 ? 507 GLN A OE1 1 
ATOM   1623 N  NE2 . GLN A 1 211 ? 3.582   -5.532  12.608 1.00 154.17 ? 507 GLN A NE2 1 
ATOM   1624 N  N   . GLN A 1 212 ? -0.431  -2.279  10.101 1.00 131.69 ? 508 GLN A N   1 
ATOM   1625 C  CA  . GLN A 1 212 ? -0.913  -2.641  8.772  1.00 129.09 ? 508 GLN A CA  1 
ATOM   1626 C  C   . GLN A 1 212 ? -0.937  -1.463  7.811  1.00 124.11 ? 508 GLN A C   1 
ATOM   1627 O  O   . GLN A 1 212 ? -1.625  -1.525  6.783  1.00 116.62 ? 508 GLN A O   1 
ATOM   1628 C  CB  . GLN A 1 212 ? -2.312  -3.263  8.855  1.00 127.44 ? 508 GLN A CB  1 
ATOM   1629 C  CG  . GLN A 1 212 ? -2.400  -4.541  9.676  1.00 130.42 ? 508 GLN A CG  1 
ATOM   1630 C  CD  . GLN A 1 212 ? -1.689  -5.724  9.037  1.00 134.74 ? 508 GLN A CD  1 
ATOM   1631 O  OE1 . GLN A 1 212 ? -1.524  -6.765  9.668  1.00 134.93 ? 508 GLN A OE1 1 
ATOM   1632 N  NE2 . GLN A 1 212 ? -1.272  -5.573  7.782  1.00 136.33 ? 508 GLN A NE2 1 
ATOM   1633 N  N   . GLY A 1 213 ? -0.213  -0.396  8.130  1.00 125.12 ? 509 GLY A N   1 
ATOM   1634 C  CA  . GLY A 1 213 ? -0.143  0.754   7.256  1.00 122.23 ? 509 GLY A CA  1 
ATOM   1635 C  C   . GLY A 1 213 ? -1.270  1.745   7.420  1.00 116.89 ? 509 GLY A C   1 
ATOM   1636 O  O   . GLY A 1 213 ? -1.811  2.229   6.421  1.00 114.99 ? 509 GLY A O   1 
ATOM   1637 N  N   . TRP A 1 214 ? -1.657  2.057   8.650  1.00 121.76 ? 510 TRP A N   1 
ATOM   1638 C  CA  . TRP A 1 214 ? -2.582  3.160   8.839  1.00 119.73 ? 510 TRP A CA  1 
ATOM   1639 C  C   . TRP A 1 214 ? -1.798  4.450   9.016  1.00 121.98 ? 510 TRP A C   1 
ATOM   1640 O  O   . TRP A 1 214 ? -0.687  4.467   9.553  1.00 119.23 ? 510 TRP A O   1 
ATOM   1641 C  CB  . TRP A 1 214 ? -3.521  2.946   10.028 1.00 115.38 ? 510 TRP A CB  1 
ATOM   1642 C  CG  . TRP A 1 214 ? -4.655  3.941   10.032 1.00 114.43 ? 510 TRP A CG  1 
ATOM   1643 C  CD1 . TRP A 1 214 ? -5.495  4.215   8.998  1.00 114.18 ? 510 TRP A CD1 1 
ATOM   1644 C  CD2 . TRP A 1 214 ? -5.060  4.797   11.114 1.00 115.62 ? 510 TRP A CD2 1 
ATOM   1645 N  NE1 . TRP A 1 214 ? -6.401  5.181   9.361  1.00 113.45 ? 510 TRP A NE1 1 
ATOM   1646 C  CE2 . TRP A 1 214 ? -6.155  5.558   10.654 1.00 112.39 ? 510 TRP A CE2 1 
ATOM   1647 C  CE3 . TRP A 1 214 ? -4.605  4.993   12.422 1.00 116.74 ? 510 TRP A CE3 1 
ATOM   1648 C  CZ2 . TRP A 1 214 ? -6.803  6.498   11.454 1.00 108.20 ? 510 TRP A CZ2 1 
ATOM   1649 C  CZ3 . TRP A 1 214 ? -5.251  5.925   13.217 1.00 115.68 ? 510 TRP A CZ3 1 
ATOM   1650 C  CH2 . TRP A 1 214 ? -6.339  6.665   12.729 1.00 113.27 ? 510 TRP A CH2 1 
ATOM   1651 N  N   . LYS A 1 215 ? -2.388  5.529   8.537  1.00 124.02 ? 511 LYS A N   1 
ATOM   1652 C  CA  . LYS A 1 215 ? -1.752  6.836   8.483  1.00 129.95 ? 511 LYS A CA  1 
ATOM   1653 C  C   . LYS A 1 215 ? -2.471  7.702   9.510  1.00 119.20 ? 511 LYS A C   1 
ATOM   1654 O  O   . LYS A 1 215 ? -3.454  8.377   9.207  1.00 118.11 ? 511 LYS A O   1 
ATOM   1655 C  CB  . LYS A 1 215 ? -1.839  7.386   7.066  1.00 140.02 ? 511 LYS A CB  1 
ATOM   1656 C  CG  . LYS A 1 215 ? -2.544  6.420   6.104  1.00 142.36 ? 511 LYS A CG  1 
ATOM   1657 C  CD  . LYS A 1 215 ? -1.586  5.743   5.116  1.00 148.68 ? 511 LYS A CD  1 
ATOM   1658 C  CE  . LYS A 1 215 ? -0.469  4.970   5.811  1.00 151.05 ? 511 LYS A CE  1 
ATOM   1659 N  NZ  . LYS A 1 215 ? 0.318   4.149   4.846  1.00 152.54 ? 511 LYS A NZ  1 
ATOM   1660 N  N   . ALA A 1 216 ? -1.977  7.667   10.732 1.00 116.30 ? 512 ALA A N   1 
ATOM   1661 C  CA  . ALA A 1 216 ? -2.726  8.203   11.860 1.00 101.41 ? 512 ALA A CA  1 
ATOM   1662 C  C   . ALA A 1 216 ? -2.696  9.727   11.846 1.00 100.97 ? 512 ALA A C   1 
ATOM   1663 O  O   . ALA A 1 216 ? -1.616  10.319  11.758 1.00 105.64 ? 512 ALA A O   1 
ATOM   1664 C  CB  . ALA A 1 216 ? -2.156  7.677   13.164 1.00 98.63  ? 512 ALA A CB  1 
ATOM   1665 N  N   . PRO A 1 217 ? -3.853  10.394  11.921 1.00 99.83  ? 513 PRO A N   1 
ATOM   1666 C  CA  . PRO A 1 217 ? -3.836  11.852  12.125 1.00 111.69 ? 513 PRO A CA  1 
ATOM   1667 C  C   . PRO A 1 217 ? -3.301  12.262  13.486 1.00 124.32 ? 513 PRO A C   1 
ATOM   1668 O  O   . PRO A 1 217 ? -2.928  13.430  13.649 1.00 136.07 ? 513 PRO A O   1 
ATOM   1669 C  CB  . PRO A 1 217 ? -5.307  12.258  11.949 1.00 106.37 ? 513 PRO A CB  1 
ATOM   1670 C  CG  . PRO A 1 217 ? -6.096  11.000  12.101 1.00 91.79  ? 513 PRO A CG  1 
ATOM   1671 C  CD  . PRO A 1 217 ? -5.213  9.862   11.715 1.00 89.93  ? 513 PRO A CD  1 
ATOM   1672 N  N   . ARG A 1 218 ? -3.263  11.339  14.459 1.00 124.71 ? 514 ARG A N   1 
ATOM   1673 C  CA  . ARG A 1 218 ? -2.651  11.538  15.785 1.00 127.75 ? 514 ARG A CA  1 
ATOM   1674 C  C   . ARG A 1 218 ? -3.276  12.704  16.556 1.00 132.34 ? 514 ARG A C   1 
ATOM   1675 O  O   . ARG A 1 218 ? -2.581  13.549  17.126 1.00 136.39 ? 514 ARG A O   1 
ATOM   1676 C  CB  . ARG A 1 218 ? -1.130  11.695  15.688 1.00 130.19 ? 514 ARG A CB  1 
ATOM   1677 C  CG  . ARG A 1 218 ? -0.402  10.358  15.595 1.00 130.66 ? 514 ARG A CG  1 
ATOM   1678 C  CD  . ARG A 1 218 ? 0.986   10.393  16.229 1.00 139.72 ? 514 ARG A CD  1 
ATOM   1679 N  NE  . ARG A 1 218 ? 1.221   9.238   17.098 1.00 140.34 ? 514 ARG A NE  1 
ATOM   1680 C  CZ  . ARG A 1 218 ? 1.428   7.996   16.663 1.00 137.67 ? 514 ARG A CZ  1 
ATOM   1681 N  NH1 . ARG A 1 218 ? 1.630   7.011   17.528 1.00 138.67 ? 514 ARG A NH1 1 
ATOM   1682 N  NH2 . ARG A 1 218 ? 1.426   7.734   15.364 1.00 132.70 ? 514 ARG A NH2 1 
ATOM   1683 N  N   . GLY A 1 219 ? -4.609  12.718  16.603 1.00 128.93 ? 515 GLY A N   1 
ATOM   1684 C  CA  . GLY A 1 219 ? -5.353  13.614  17.448 1.00 127.42 ? 515 GLY A CA  1 
ATOM   1685 C  C   . GLY A 1 219 ? -6.050  12.889  18.581 1.00 120.62 ? 515 GLY A C   1 
ATOM   1686 O  O   . GLY A 1 219 ? -5.652  11.794  19.000 1.00 121.52 ? 515 GLY A O   1 
ATOM   1687 N  N   . ARG A 1 220 ? -7.121  13.506  19.079 1.00 116.28 ? 516 ARG A N   1 
ATOM   1688 C  CA  . ARG A 1 220 ? -7.895  12.922  20.172 1.00 113.37 ? 516 ARG A CA  1 
ATOM   1689 C  C   . ARG A 1 220 ? -8.996  12.004  19.658 1.00 107.41 ? 516 ARG A C   1 
ATOM   1690 O  O   . ARG A 1 220 ? -9.084  10.839  20.062 1.00 102.62 ? 516 ARG A O   1 
ATOM   1691 C  CB  . ARG A 1 220 ? -8.510  14.023  21.037 1.00 114.45 ? 516 ARG A CB  1 
ATOM   1692 C  CG  . ARG A 1 220 ? -9.178  13.500  22.304 1.00 112.18 ? 516 ARG A CG  1 
ATOM   1693 C  CD  . ARG A 1 220 ? -8.333  13.808  23.540 1.00 112.18 ? 516 ARG A CD  1 
ATOM   1694 N  NE  . ARG A 1 220 ? -9.004  14.731  24.456 1.00 115.71 ? 516 ARG A NE  1 
ATOM   1695 C  CZ  . ARG A 1 220 ? -9.302  14.457  25.725 1.00 115.33 ? 516 ARG A CZ  1 
ATOM   1696 N  NH1 . ARG A 1 220 ? -8.976  13.284  26.254 1.00 117.61 ? 516 ARG A NH1 1 
ATOM   1697 N  NH2 . ARG A 1 220 ? -9.914  15.367  26.475 1.00 108.42 ? 516 ARG A NH2 1 
ATOM   1698 N  N   . PHE A 1 221 ? -9.848  12.529  18.784 1.00 101.61 ? 517 PHE A N   1 
ATOM   1699 C  CA  . PHE A 1 221 ? -11.052 11.844  18.346 1.00 92.66  ? 517 PHE A CA  1 
ATOM   1700 C  C   . PHE A 1 221 ? -10.921 11.475  16.869 1.00 103.82 ? 517 PHE A C   1 
ATOM   1701 O  O   . PHE A 1 221 ? -11.670 11.936  15.997 1.00 106.28 ? 517 PHE A O   1 
ATOM   1702 C  CB  . PHE A 1 221 ? -12.295 12.719  18.623 1.00 82.82  ? 517 PHE A CB  1 
ATOM   1703 C  CG  . PHE A 1 221 ? -12.530 13.038  20.094 1.00 87.67  ? 517 PHE A CG  1 
ATOM   1704 C  CD1 . PHE A 1 221 ? -12.414 14.339  20.557 1.00 93.25  ? 517 PHE A CD1 1 
ATOM   1705 C  CD2 . PHE A 1 221 ? -12.878 12.045  21.008 1.00 76.50  ? 517 PHE A CD2 1 
ATOM   1706 C  CE1 . PHE A 1 221 ? -12.641 14.637  21.884 1.00 86.94  ? 517 PHE A CE1 1 
ATOM   1707 C  CE2 . PHE A 1 221 ? -13.123 12.351  22.321 1.00 79.83  ? 517 PHE A CE2 1 
ATOM   1708 C  CZ  . PHE A 1 221 ? -12.990 13.642  22.764 1.00 81.33  ? 517 PHE A CZ  1 
ATOM   1709 N  N   . ASP A 1 222 ? -9.956  10.600  16.594 1.00 103.02 ? 518 ASP A N   1 
ATOM   1710 C  CA  . ASP A 1 222 ? -9.724  10.085  15.250 1.00 88.78  ? 518 ASP A CA  1 
ATOM   1711 C  C   . ASP A 1 222 ? -10.484 8.775   15.076 1.00 88.35  ? 518 ASP A C   1 
ATOM   1712 O  O   . ASP A 1 222 ? -10.186 7.789   15.757 1.00 93.81  ? 518 ASP A O   1 
ATOM   1713 C  CB  . ASP A 1 222 ? -8.232  9.859   15.006 1.00 87.55  ? 518 ASP A CB  1 
ATOM   1714 C  CG  . ASP A 1 222 ? -7.391  11.090  15.285 1.00 100.70 ? 518 ASP A CG  1 
ATOM   1715 O  OD1 . ASP A 1 222 ? -7.963  12.164  15.569 1.00 107.57 ? 518 ASP A OD1 1 
ATOM   1716 O  OD2 . ASP A 1 222 ? -6.146  10.981  15.225 1.00 105.33 ? 518 ASP A OD2 1 
ATOM   1717 N  N   . VAL A 1 223 ? -11.456 8.759   14.161 1.00 87.91  ? 519 VAL A N   1 
ATOM   1718 C  CA  . VAL A 1 223 ? -12.142 7.516   13.825 1.00 87.81  ? 519 VAL A CA  1 
ATOM   1719 C  C   . VAL A 1 223 ? -11.136 6.523   13.261 1.00 89.64  ? 519 VAL A C   1 
ATOM   1720 O  O   . VAL A 1 223 ? -10.404 6.827   12.311 1.00 87.72  ? 519 VAL A O   1 
ATOM   1721 C  CB  . VAL A 1 223 ? -13.282 7.775   12.825 1.00 80.24  ? 519 VAL A CB  1 
ATOM   1722 C  CG1 . VAL A 1 223 ? -13.955 6.461   12.425 1.00 65.36  ? 519 VAL A CG1 1 
ATOM   1723 C  CG2 . VAL A 1 223 ? -14.306 8.734   13.411 1.00 85.27  ? 519 VAL A CG2 1 
ATOM   1724 N  N   . LEU A 1 224 ? -11.090 5.330   13.849 1.00 85.71  ? 520 LEU A N   1 
ATOM   1725 C  CA  . LEU A 1 224 ? -10.208 4.282   13.365 1.00 81.11  ? 520 LEU A CA  1 
ATOM   1726 C  C   . LEU A 1 224 ? -10.721 3.740   12.035 1.00 84.63  ? 520 LEU A C   1 
ATOM   1727 O  O   . LEU A 1 224 ? -11.898 3.895   11.701 1.00 86.77  ? 520 LEU A O   1 
ATOM   1728 C  CB  . LEU A 1 224 ? -10.115 3.150   14.391 1.00 72.77  ? 520 LEU A CB  1 
ATOM   1729 C  CG  . LEU A 1 224 ? -9.408  3.493   15.709 1.00 74.05  ? 520 LEU A CG  1 
ATOM   1730 C  CD1 . LEU A 1 224 ? -10.094 2.805   16.888 1.00 73.79  ? 520 LEU A CD1 1 
ATOM   1731 C  CD2 . LEU A 1 224 ? -7.925  3.130   15.671 1.00 78.08  ? 520 LEU A CD2 1 
ATOM   1732 N  N   . PRO A 1 225 ? -9.857  3.120   11.244 1.00 85.79  ? 521 PRO A N   1 
ATOM   1733 C  CA  . PRO A 1 225 ? -10.335 2.402   10.063 1.00 90.59  ? 521 PRO A CA  1 
ATOM   1734 C  C   . PRO A 1 225 ? -10.831 1.027   10.479 1.00 86.01  ? 521 PRO A C   1 
ATOM   1735 O  O   . PRO A 1 225 ? -10.683 0.607   11.624 1.00 90.80  ? 521 PRO A O   1 
ATOM   1736 C  CB  . PRO A 1 225 ? -9.095  2.311   9.169  1.00 93.60  ? 521 PRO A CB  1 
ATOM   1737 C  CG  . PRO A 1 225 ? -7.961  2.281   10.142 1.00 97.50  ? 521 PRO A CG  1 
ATOM   1738 C  CD  . PRO A 1 225 ? -8.387  3.087   11.347 1.00 94.20  ? 521 PRO A CD  1 
ATOM   1739 N  N   . LEU A 1 226 ? -11.427 0.330   9.522  1.00 82.03  ? 522 LEU A N   1 
ATOM   1740 C  CA  . LEU A 1 226 ? -11.896 -1.025  9.749  1.00 76.87  ? 522 LEU A CA  1 
ATOM   1741 C  C   . LEU A 1 226 ? -10.817 -2.018  9.345  1.00 78.85  ? 522 LEU A C   1 
ATOM   1742 O  O   . LEU A 1 226 ? -10.173 -1.861  8.308  1.00 91.81  ? 522 LEU A O   1 
ATOM   1743 C  CB  . LEU A 1 226 ? -13.175 -1.288  8.956  1.00 68.46  ? 522 LEU A CB  1 
ATOM   1744 C  CG  . LEU A 1 226 ? -14.396 -0.433  9.297  1.00 63.78  ? 522 LEU A CG  1 
ATOM   1745 C  CD1 . LEU A 1 226 ? -15.477 -0.662  8.236  1.00 70.88  ? 522 LEU A CD1 1 
ATOM   1746 C  CD2 . LEU A 1 226 ? -14.908 -0.760  10.702 1.00 59.62  ? 522 LEU A CD2 1 
ATOM   1747 N  N   . LEU A 1 227 ? -10.608 -3.026  10.180 1.00 69.89  ? 523 LEU A N   1 
ATOM   1748 C  CA  . LEU A 1 227 ? -9.754  -4.161  9.842  1.00 81.12  ? 523 LEU A CA  1 
ATOM   1749 C  C   . LEU A 1 227 ? -10.682 -5.358  9.689  1.00 82.81  ? 523 LEU A C   1 
ATOM   1750 O  O   . LEU A 1 227 ? -11.127 -5.936  10.684 1.00 85.52  ? 523 LEU A O   1 
ATOM   1751 C  CB  . LEU A 1 227 ? -8.682  -4.415  10.898 1.00 86.82  ? 523 LEU A CB  1 
ATOM   1752 C  CG  . LEU A 1 227 ? -7.226  -4.421  10.403 1.00 95.66  ? 523 LEU A CG  1 
ATOM   1753 C  CD1 . LEU A 1 227 ? -6.389  -5.426  11.182 1.00 101.67 ? 523 LEU A CD1 1 
ATOM   1754 C  CD2 . LEU A 1 227 ? -7.118  -4.684  8.921  1.00 97.54  ? 523 LEU A CD2 1 
ATOM   1755 N  N   . LEU A 1 228 ? -10.975 -5.715  8.444  1.00 73.62  ? 524 LEU A N   1 
ATOM   1756 C  CA  . LEU A 1 228 ? -11.958 -6.739  8.115  1.00 77.03  ? 524 LEU A CA  1 
ATOM   1757 C  C   . LEU A 1 228 ? -11.240 -7.967  7.572  1.00 83.96  ? 524 LEU A C   1 
ATOM   1758 O  O   . LEU A 1 228 ? -10.490 -7.869  6.594  1.00 76.81  ? 524 LEU A O   1 
ATOM   1759 C  CB  . LEU A 1 228 ? -12.963 -6.209  7.091  1.00 68.15  ? 524 LEU A CB  1 
ATOM   1760 C  CG  . LEU A 1 228 ? -13.505 -4.830  7.461  1.00 67.68  ? 524 LEU A CG  1 
ATOM   1761 C  CD1 . LEU A 1 228 ? -14.155 -4.138  6.276  1.00 64.66  ? 524 LEU A CD1 1 
ATOM   1762 C  CD2 . LEU A 1 228 ? -14.481 -4.947  8.600  1.00 68.61  ? 524 LEU A CD2 1 
ATOM   1763 N  N   . GLN A 1 229 ? -11.472 -9.112  8.210  1.00 86.85  ? 525 GLN A N   1 
ATOM   1764 C  CA  . GLN A 1 229 ? -10.905 -10.390 7.800  1.00 89.74  ? 525 GLN A CA  1 
ATOM   1765 C  C   . GLN A 1 229 ? -12.001 -11.222 7.140  1.00 81.98  ? 525 GLN A C   1 
ATOM   1766 O  O   . GLN A 1 229 ? -13.054 -11.470 7.743  1.00 67.92  ? 525 GLN A O   1 
ATOM   1767 C  CB  . GLN A 1 229 ? -10.303 -11.114 9.006  1.00 95.48  ? 525 GLN A CB  1 
ATOM   1768 C  CG  . GLN A 1 229 ? -10.256 -12.633 8.922  1.00 95.36  ? 525 GLN A CG  1 
ATOM   1769 C  CD  . GLN A 1 229 ? -9.837  -13.263 10.238 1.00 91.38  ? 525 GLN A CD  1 
ATOM   1770 O  OE1 . GLN A 1 229 ? -9.317  -12.583 11.126 1.00 89.49  ? 525 GLN A OE1 1 
ATOM   1771 N  NE2 . GLN A 1 229 ? -10.070 -14.563 10.375 1.00 91.92  ? 525 GLN A NE2 1 
ATOM   1772 N  N   . ALA A 1 230 ? -11.761 -11.632 5.900  1.00 83.32  ? 526 ALA A N   1 
ATOM   1773 C  CA  . ALA A 1 230 ? -12.741 -12.351 5.094  1.00 84.11  ? 526 ALA A CA  1 
ATOM   1774 C  C   . ALA A 1 230 ? -12.227 -13.756 4.816  1.00 85.36  ? 526 ALA A C   1 
ATOM   1775 O  O   . ALA A 1 230 ? -11.084 -13.923 4.388  1.00 88.46  ? 526 ALA A O   1 
ATOM   1776 C  CB  . ALA A 1 230 ? -13.013 -11.617 3.782  1.00 85.11  ? 526 ALA A CB  1 
ATOM   1777 N  N   . ASN A 1 231 ? -13.066 -14.758 5.078  1.00 83.89  ? 527 ASN A N   1 
ATOM   1778 C  CA  . ASN A 1 231 ? -12.744 -16.162 4.817  1.00 84.97  ? 527 ASN A CA  1 
ATOM   1779 C  C   . ASN A 1 231 ? -11.366 -16.533 5.361  1.00 90.24  ? 527 ASN A C   1 
ATOM   1780 O  O   . ASN A 1 231 ? -10.522 -17.097 4.664  1.00 95.59  ? 527 ASN A O   1 
ATOM   1781 C  CB  . ASN A 1 231 ? -12.838 -16.474 3.323  1.00 94.79  ? 527 ASN A CB  1 
ATOM   1782 C  CG  . ASN A 1 231 ? -13.034 -17.950 3.055  1.00 97.21  ? 527 ASN A CG  1 
ATOM   1783 O  OD1 . ASN A 1 231 ? -13.647 -18.657 3.860  1.00 96.16  ? 527 ASN A OD1 1 
ATOM   1784 N  ND2 . ASN A 1 231 ? -12.518 -18.425 1.923  1.00 98.07  ? 527 ASN A ND2 1 
ATOM   1785 N  N   . GLY A 1 232 ? -11.139 -16.210 6.628  1.00 90.73  ? 528 GLY A N   1 
ATOM   1786 C  CA  . GLY A 1 232 ? -9.873  -16.533 7.252  1.00 95.42  ? 528 GLY A CA  1 
ATOM   1787 C  C   . GLY A 1 232 ? -8.668  -15.798 6.695  1.00 99.36  ? 528 GLY A C   1 
ATOM   1788 O  O   . GLY A 1 232 ? -7.544  -16.027 7.151  1.00 108.56 ? 528 GLY A O   1 
ATOM   1789 N  N   . ASN A 1 233 ? -8.871  -14.903 5.731  1.00 95.91  ? 529 ASN A N   1 
ATOM   1790 C  CA  . ASN A 1 233 ? -7.737  -14.221 5.130  1.00 98.17  ? 529 ASN A CA  1 
ATOM   1791 C  C   . ASN A 1 233 ? -7.194  -13.117 6.036  1.00 104.41 ? 529 ASN A C   1 
ATOM   1792 O  O   . ASN A 1 233 ? -7.860  -12.635 6.958  1.00 106.33 ? 529 ASN A O   1 
ATOM   1793 C  CB  . ASN A 1 233 ? -8.114  -13.630 3.772  1.00 96.71  ? 529 ASN A CB  1 
ATOM   1794 C  CG  . ASN A 1 233 ? -7.992  -14.632 2.654  1.00 96.61  ? 529 ASN A CG  1 
ATOM   1795 O  OD1 . ASN A 1 233 ? -6.959  -14.705 1.987  1.00 104.68 ? 529 ASN A OD1 1 
ATOM   1796 N  ND2 . ASN A 1 233 ? -9.044  -15.420 2.443  1.00 86.62  ? 529 ASN A ND2 1 
ATOM   1797 N  N   . ASP A 1 234 ? -5.953  -12.727 5.758  1.00 110.82 ? 530 ASP A N   1 
ATOM   1798 C  CA  . ASP A 1 234 ? -5.339  -11.620 6.476  1.00 111.23 ? 530 ASP A CA  1 
ATOM   1799 C  C   . ASP A 1 234 ? -6.141  -10.345 6.219  1.00 100.06 ? 530 ASP A C   1 
ATOM   1800 O  O   . ASP A 1 234 ? -6.469  -10.046 5.059  1.00 114.59 ? 530 ASP A O   1 
ATOM   1801 C  CB  . ASP A 1 234 ? -3.879  -11.435 6.049  1.00 121.26 ? 530 ASP A CB  1 
ATOM   1802 C  CG  . ASP A 1 234 ? -3.022  -12.673 6.315  1.00 129.63 ? 530 ASP A CG  1 
ATOM   1803 O  OD1 . ASP A 1 234 ? -1.897  -12.754 5.772  1.00 133.70 ? 530 ASP A OD1 1 
ATOM   1804 O  OD2 . ASP A 1 234 ? -3.472  -13.570 7.060  1.00 132.04 ? 530 ASP A OD2 1 
ATOM   1805 N  N   . PRO A 1 235 ? -6.470  -9.576  7.249  1.00 77.98  ? 531 PRO A N   1 
ATOM   1806 C  CA  . PRO A 1 235 ? -7.437  -8.491  7.090  1.00 71.19  ? 531 PRO A CA  1 
ATOM   1807 C  C   . PRO A 1 235 ? -6.828  -7.270  6.422  1.00 77.23  ? 531 PRO A C   1 
ATOM   1808 O  O   . PRO A 1 235 ? -5.611  -7.111  6.328  1.00 88.19  ? 531 PRO A O   1 
ATOM   1809 C  CB  . PRO A 1 235 ? -7.837  -8.178  8.536  1.00 70.67  ? 531 PRO A CB  1 
ATOM   1810 C  CG  . PRO A 1 235 ? -6.612  -8.465  9.287  1.00 65.40  ? 531 PRO A CG  1 
ATOM   1811 C  CD  . PRO A 1 235 ? -5.993  -9.671  8.641  1.00 73.47  ? 531 PRO A CD  1 
ATOM   1812 N  N   . GLU A 1 236 ? -7.713  -6.390  5.962  1.00 77.24  ? 532 GLU A N   1 
ATOM   1813 C  CA  . GLU A 1 236 ? -7.318  -5.241  5.164  1.00 76.45  ? 532 GLU A CA  1 
ATOM   1814 C  C   . GLU A 1 236 ? -7.992  -3.982  5.684  1.00 77.06  ? 532 GLU A C   1 
ATOM   1815 O  O   . GLU A 1 236 ? -9.140  -4.020  6.135  1.00 78.88  ? 532 GLU A O   1 
ATOM   1816 C  CB  . GLU A 1 236 ? -7.674  -5.462  3.690  1.00 73.78  ? 532 GLU A CB  1 
ATOM   1817 C  CG  . GLU A 1 236 ? -7.253  -6.819  3.158  1.00 75.25  ? 532 GLU A CG  1 
ATOM   1818 C  CD  . GLU A 1 236 ? -8.065  -7.229  1.944  1.00 78.05  ? 532 GLU A CD  1 
ATOM   1819 O  OE1 . GLU A 1 236 ? -8.245  -6.381  1.041  1.00 73.98  ? 532 GLU A OE1 1 
ATOM   1820 O  OE2 . GLU A 1 236 ? -8.536  -8.389  1.913  1.00 78.51  ? 532 GLU A OE2 1 
ATOM   1821 N  N   . LEU A 1 237 ? -7.277  -2.864  5.602  1.00 80.60  ? 533 LEU A N   1 
ATOM   1822 C  CA  . LEU A 1 237 ? -7.712  -1.611  6.206  1.00 87.42  ? 533 LEU A CA  1 
ATOM   1823 C  C   . LEU A 1 237 ? -8.621  -0.828  5.267  1.00 85.02  ? 533 LEU A C   1 
ATOM   1824 O  O   . LEU A 1 237 ? -8.249  -0.551  4.126  1.00 81.90  ? 533 LEU A O   1 
ATOM   1825 C  CB  . LEU A 1 237 ? -6.499  -0.756  6.584  1.00 93.06  ? 533 LEU A CB  1 
ATOM   1826 C  CG  . LEU A 1 237 ? -5.893  -1.078  7.954  1.00 89.32  ? 533 LEU A CG  1 
ATOM   1827 C  CD1 . LEU A 1 237 ? -4.733  -0.153  8.296  1.00 94.53  ? 533 LEU A CD1 1 
ATOM   1828 C  CD2 . LEU A 1 237 ? -6.967  -0.995  9.006  1.00 83.53  ? 533 LEU A CD2 1 
ATOM   1829 N  N   . PHE A 1 238 ? -9.798  -0.443  5.762  1.00 84.86  ? 534 PHE A N   1 
ATOM   1830 C  CA  . PHE A 1 238 ? -10.697 0.438   5.026  1.00 76.73  ? 534 PHE A CA  1 
ATOM   1831 C  C   . PHE A 1 238 ? -11.228 1.518   5.957  1.00 79.08  ? 534 PHE A C   1 
ATOM   1832 O  O   . PHE A 1 238 ? -11.630 1.229   7.085  1.00 65.75  ? 534 PHE A O   1 
ATOM   1833 C  CB  . PHE A 1 238 ? -11.885 -0.310  4.433  1.00 64.27  ? 534 PHE A CB  1 
ATOM   1834 C  CG  . PHE A 1 238 ? -11.521 -1.568  3.728  1.00 69.31  ? 534 PHE A CG  1 
ATOM   1835 C  CD1 . PHE A 1 238 ? -11.490 -2.771  4.411  1.00 76.20  ? 534 PHE A CD1 1 
ATOM   1836 C  CD2 . PHE A 1 238 ? -11.232 -1.558  2.370  1.00 76.99  ? 534 PHE A CD2 1 
ATOM   1837 C  CE1 . PHE A 1 238 ? -11.163 -3.942  3.757  1.00 76.18  ? 534 PHE A CE1 1 
ATOM   1838 C  CE2 . PHE A 1 238 ? -10.898 -2.727  1.714  1.00 73.64  ? 534 PHE A CE2 1 
ATOM   1839 C  CZ  . PHE A 1 238 ? -10.874 -3.927  2.406  1.00 63.24  ? 534 PHE A CZ  1 
ATOM   1840 N  N   . GLN A 1 239 ? -11.268 2.755   5.467  1.00 84.98  ? 535 GLN A N   1 
ATOM   1841 C  CA  . GLN A 1 239 ? -11.722 3.901   6.250  1.00 82.65  ? 535 GLN A CA  1 
ATOM   1842 C  C   . GLN A 1 239 ? -13.158 4.243   5.857  1.00 79.05  ? 535 GLN A C   1 
ATOM   1843 O  O   . GLN A 1 239 ? -13.413 4.676   4.728  1.00 80.62  ? 535 GLN A O   1 
ATOM   1844 C  CB  . GLN A 1 239 ? -10.784 5.090   6.040  1.00 92.45  ? 535 GLN A CB  1 
ATOM   1845 C  CG  . GLN A 1 239 ? -11.383 6.455   6.350  1.00 101.39 ? 535 GLN A CG  1 
ATOM   1846 C  CD  . GLN A 1 239 ? -11.570 7.313   5.100  1.00 113.79 ? 535 GLN A CD  1 
ATOM   1847 O  OE1 . GLN A 1 239 ? -12.697 7.586   4.684  1.00 119.11 ? 535 GLN A OE1 1 
ATOM   1848 N  NE2 . GLN A 1 239 ? -10.461 7.746   4.503  1.00 114.36 ? 535 GLN A NE2 1 
ATOM   1849 N  N   . ILE A 1 240 ? -14.090 4.041   6.786  1.00 76.25  ? 536 ILE A N   1 
ATOM   1850 C  CA  . ILE A 1 240 ? -15.493 4.421   6.627  1.00 73.86  ? 536 ILE A CA  1 
ATOM   1851 C  C   . ILE A 1 240 ? -15.524 5.857   6.124  1.00 74.35  ? 536 ILE A C   1 
ATOM   1852 O  O   . ILE A 1 240 ? -14.791 6.709   6.649  1.00 70.19  ? 536 ILE A O   1 
ATOM   1853 C  CB  . ILE A 1 240 ? -16.276 4.290   7.948  1.00 73.55  ? 536 ILE A CB  1 
ATOM   1854 C  CG1 . ILE A 1 240 ? -15.852 3.037   8.710  1.00 79.74  ? 536 ILE A CG1 1 
ATOM   1855 C  CG2 . ILE A 1 240 ? -17.777 4.261   7.690  1.00 64.63  ? 536 ILE A CG2 1 
ATOM   1856 C  CD1 . ILE A 1 240 ? -14.863 3.298   9.823  1.00 86.28  ? 536 ILE A CD1 1 
ATOM   1857 N  N   . PRO A 1 241 ? -16.305 6.173   5.101  1.00 74.08  ? 537 PRO A N   1 
ATOM   1858 C  CA  . PRO A 1 241 ? -16.363 7.559   4.633  1.00 73.52  ? 537 PRO A CA  1 
ATOM   1859 C  C   . PRO A 1 241 ? -16.808 8.462   5.768  1.00 68.46  ? 537 PRO A C   1 
ATOM   1860 O  O   . PRO A 1 241 ? -17.783 8.145   6.467  1.00 58.95  ? 537 PRO A O   1 
ATOM   1861 C  CB  . PRO A 1 241 ? -17.400 7.514   3.503  1.00 72.53  ? 537 PRO A CB  1 
ATOM   1862 C  CG  . PRO A 1 241 ? -17.424 6.068   3.078  1.00 74.23  ? 537 PRO A CG  1 
ATOM   1863 C  CD  . PRO A 1 241 ? -17.206 5.291   4.344  1.00 75.58  ? 537 PRO A CD  1 
ATOM   1864 N  N   . PRO A 1 242 ? -16.083 9.551   6.034  1.00 75.76  ? 538 PRO A N   1 
ATOM   1865 C  CA  . PRO A 1 242 ? -16.395 10.356  7.224  1.00 78.45  ? 538 PRO A CA  1 
ATOM   1866 C  C   . PRO A 1 242 ? -17.785 10.949  7.185  1.00 77.78  ? 538 PRO A C   1 
ATOM   1867 O  O   . PRO A 1 242 ? -18.377 11.178  8.245  1.00 83.54  ? 538 PRO A O   1 
ATOM   1868 C  CB  . PRO A 1 242 ? -15.314 11.442  7.205  1.00 83.64  ? 538 PRO A CB  1 
ATOM   1869 C  CG  . PRO A 1 242 ? -14.202 10.845  6.401  1.00 86.03  ? 538 PRO A CG  1 
ATOM   1870 C  CD  . PRO A 1 242 ? -14.885 10.049  5.338  1.00 83.65  ? 538 PRO A CD  1 
ATOM   1871 N  N   . GLU A 1 243 ? -18.345 11.167  5.997  1.00 74.94  ? 539 GLU A N   1 
ATOM   1872 C  CA  . GLU A 1 243 ? -19.713 11.663  5.901  1.00 70.54  ? 539 GLU A CA  1 
ATOM   1873 C  C   . GLU A 1 243 ? -20.725 10.686  6.492  1.00 69.26  ? 539 GLU A C   1 
ATOM   1874 O  O   . GLU A 1 243 ? -21.846 11.105  6.814  1.00 65.46  ? 539 GLU A O   1 
ATOM   1875 C  CB  . GLU A 1 243 ? -20.067 11.977  4.439  1.00 80.24  ? 539 GLU A CB  1 
ATOM   1876 C  CG  . GLU A 1 243 ? -20.109 10.773  3.506  1.00 81.05  ? 539 GLU A CG  1 
ATOM   1877 C  CD  . GLU A 1 243 ? -18.808 10.558  2.749  1.00 87.25  ? 539 GLU A CD  1 
ATOM   1878 O  OE1 . GLU A 1 243 ? -17.736 10.775  3.356  1.00 87.92  ? 539 GLU A OE1 1 
ATOM   1879 O  OE2 . GLU A 1 243 ? -18.861 10.176  1.549  1.00 84.82  ? 539 GLU A OE2 1 
ATOM   1880 N  N   . LEU A 1 244 ? -20.353 9.399   6.635  1.00 64.27  ? 540 LEU A N   1 
ATOM   1881 C  CA  . LEU A 1 244 ? -21.179 8.355   7.236  1.00 62.24  ? 540 LEU A CA  1 
ATOM   1882 C  C   . LEU A 1 244 ? -21.040 8.252   8.746  1.00 63.26  ? 540 LEU A C   1 
ATOM   1883 O  O   . LEU A 1 244 ? -21.852 7.558   9.370  1.00 53.27  ? 540 LEU A O   1 
ATOM   1884 C  CB  . LEU A 1 244 ? -20.831 6.983   6.655  1.00 57.73  ? 540 LEU A CB  1 
ATOM   1885 C  CG  . LEU A 1 244 ? -21.292 6.755   5.226  1.00 63.31  ? 540 LEU A CG  1 
ATOM   1886 C  CD1 . LEU A 1 244 ? -20.970 5.316   4.790  1.00 61.95  ? 540 LEU A CD1 1 
ATOM   1887 C  CD2 . LEU A 1 244 ? -22.790 7.098   5.105  1.00 56.49  ? 540 LEU A CD2 1 
ATOM   1888 N  N   . VAL A 1 245 ? -20.019 8.873   9.336  1.00 71.26  ? 541 VAL A N   1 
ATOM   1889 C  CA  . VAL A 1 245 ? -19.755 8.796   10.772 1.00 69.89  ? 541 VAL A CA  1 
ATOM   1890 C  C   . VAL A 1 245 ? -20.360 10.035  11.414 1.00 68.25  ? 541 VAL A C   1 
ATOM   1891 O  O   . VAL A 1 245 ? -19.786 11.129  11.343 1.00 67.40  ? 541 VAL A O   1 
ATOM   1892 C  CB  . VAL A 1 245 ? -18.258 8.684   11.072 1.00 70.52  ? 541 VAL A CB  1 
ATOM   1893 C  CG1 . VAL A 1 245 ? -18.034 8.509   12.588 1.00 70.84  ? 541 VAL A CG1 1 
ATOM   1894 C  CG2 . VAL A 1 245 ? -17.659 7.512   10.313 1.00 74.87  ? 541 VAL A CG2 1 
ATOM   1895 N  N   . LEU A 1 246 ? -21.499 9.851   12.088 1.00 70.93  ? 542 LEU A N   1 
ATOM   1896 C  CA  . LEU A 1 246 ? -22.220 10.946  12.723 1.00 64.46  ? 542 LEU A CA  1 
ATOM   1897 C  C   . LEU A 1 246 ? -21.696 11.168  14.135 1.00 68.43  ? 542 LEU A C   1 
ATOM   1898 O  O   . LEU A 1 246 ? -21.744 10.261  14.975 1.00 62.74  ? 542 LEU A O   1 
ATOM   1899 C  CB  . LEU A 1 246 ? -23.727 10.670  12.755 1.00 64.03  ? 542 LEU A CB  1 
ATOM   1900 C  CG  . LEU A 1 246 ? -24.499 11.579  13.742 1.00 73.07  ? 542 LEU A CG  1 
ATOM   1901 C  CD1 . LEU A 1 246 ? -24.471 13.051  13.306 1.00 77.52  ? 542 LEU A CD1 1 
ATOM   1902 C  CD2 . LEU A 1 246 ? -25.937 11.116  13.922 1.00 71.07  ? 542 LEU A CD2 1 
ATOM   1903 N  N   . GLU A 1 247 ? -21.248 12.389  14.405 1.00 70.13  ? 543 GLU A N   1 
ATOM   1904 C  CA  . GLU A 1 247 ? -20.600 12.738  15.658 1.00 71.79  ? 543 GLU A CA  1 
ATOM   1905 C  C   . GLU A 1 247 ? -21.331 13.906  16.307 1.00 74.91  ? 543 GLU A C   1 
ATOM   1906 O  O   . GLU A 1 247 ? -21.881 14.779  15.620 1.00 83.25  ? 543 GLU A O   1 
ATOM   1907 C  CB  . GLU A 1 247 ? -19.116 13.079  15.424 1.00 69.84  ? 543 GLU A CB  1 
ATOM   1908 C  CG  . GLU A 1 247 ? -18.258 11.893  14.972 1.00 60.44  ? 543 GLU A CG  1 
ATOM   1909 C  CD  . GLU A 1 247 ? -16.825 12.311  14.717 1.00 76.64  ? 543 GLU A CD  1 
ATOM   1910 O  OE1 . GLU A 1 247 ? -16.583 12.977  13.686 1.00 90.88  ? 543 GLU A OE1 1 
ATOM   1911 O  OE2 . GLU A 1 247 ? -15.946 12.000  15.547 1.00 80.66  ? 543 GLU A OE2 1 
ATOM   1912 N  N   . VAL A 1 248 ? -21.336 13.903  17.633 1.00 81.78  ? 544 VAL A N   1 
ATOM   1913 C  CA  . VAL A 1 248 ? -22.043 14.890  18.446 1.00 81.02  ? 544 VAL A CA  1 
ATOM   1914 C  C   . VAL A 1 248 ? -21.018 15.699  19.233 1.00 70.91  ? 544 VAL A C   1 
ATOM   1915 O  O   . VAL A 1 248 ? -20.294 15.126  20.056 1.00 72.47  ? 544 VAL A O   1 
ATOM   1916 C  CB  . VAL A 1 248 ? -23.045 14.223  19.400 1.00 79.68  ? 544 VAL A CB  1 
ATOM   1917 C  CG1 . VAL A 1 248 ? -23.627 15.256  20.375 1.00 77.25  ? 544 VAL A CG1 1 
ATOM   1918 C  CG2 . VAL A 1 248 ? -24.151 13.520  18.605 1.00 71.20  ? 544 VAL A CG2 1 
ATOM   1919 N  N   . PRO A 1 249 ? -20.916 17.008  19.011 1.00 71.33  ? 545 PRO A N   1 
ATOM   1920 C  CA  . PRO A 1 249 ? -20.098 17.846  19.892 1.00 82.88  ? 545 PRO A CA  1 
ATOM   1921 C  C   . PRO A 1 249 ? -20.809 18.052  21.221 1.00 82.09  ? 545 PRO A C   1 
ATOM   1922 O  O   . PRO A 1 249 ? -22.025 18.265  21.260 1.00 75.50  ? 545 PRO A O   1 
ATOM   1923 C  CB  . PRO A 1 249 ? -19.960 19.159  19.099 1.00 84.33  ? 545 PRO A CB  1 
ATOM   1924 C  CG  . PRO A 1 249 ? -21.165 19.200  18.252 1.00 80.41  ? 545 PRO A CG  1 
ATOM   1925 C  CD  . PRO A 1 249 ? -21.475 17.777  17.879 1.00 77.83  ? 545 PRO A CD  1 
ATOM   1926 N  N   . ILE A 1 250 ? -20.048 17.936  22.315 1.00 87.23  ? 546 ILE A N   1 
ATOM   1927 C  CA  . ILE A 1 250 ? -20.585 17.869  23.673 1.00 71.77  ? 546 ILE A CA  1 
ATOM   1928 C  C   . ILE A 1 250 ? -20.542 19.256  24.302 1.00 79.48  ? 546 ILE A C   1 
ATOM   1929 O  O   . ILE A 1 250 ? -19.472 19.742  24.697 1.00 82.20  ? 546 ILE A O   1 
ATOM   1930 C  CB  . ILE A 1 250 ? -19.817 16.862  24.542 1.00 68.47  ? 546 ILE A CB  1 
ATOM   1931 C  CG1 . ILE A 1 250 ? -19.763 15.491  23.868 1.00 62.28  ? 546 ILE A CG1 1 
ATOM   1932 C  CG2 . ILE A 1 250 ? -20.472 16.745  25.912 1.00 69.35  ? 546 ILE A CG2 1 
ATOM   1933 C  CD1 . ILE A 1 250 ? -21.129 14.902  23.561 1.00 65.18  ? 546 ILE A CD1 1 
ATOM   1934 N  N   . ARG A 1 251 ? -21.713 19.890  24.434 1.00 86.77  ? 547 ARG A N   1 
ATOM   1935 C  CA  . ARG A 1 251 ? -21.849 21.111  25.219 1.00 91.32  ? 547 ARG A CA  1 
ATOM   1936 C  C   . ARG A 1 251 ? -22.764 20.883  26.418 1.00 96.37  ? 547 ARG A C   1 
ATOM   1937 O  O   . ARG A 1 251 ? -23.591 19.964  26.447 1.00 91.75  ? 547 ARG A O   1 
ATOM   1938 C  CB  . ARG A 1 251 ? -22.377 22.307  24.387 1.00 89.61  ? 547 ARG A CB  1 
ATOM   1939 C  CG  . ARG A 1 251 ? -23.809 22.197  23.854 1.00 93.19  ? 547 ARG A CG  1 
ATOM   1940 C  CD  . ARG A 1 251 ? -23.794 21.455  22.524 1.00 92.79  ? 547 ARG A CD  1 
ATOM   1941 N  NE  . ARG A 1 251 ? -25.071 21.386  21.824 1.00 88.82  ? 547 ARG A NE  1 
ATOM   1942 C  CZ  . ARG A 1 251 ? -25.241 20.663  20.725 1.00 96.22  ? 547 ARG A CZ  1 
ATOM   1943 N  NH1 . ARG A 1 251 ? -26.413 20.634  20.106 1.00 100.43 ? 547 ARG A NH1 1 
ATOM   1944 N  NH2 . ARG A 1 251 ? -24.221 19.961  20.248 1.00 97.66  ? 547 ARG A NH2 1 
ATOM   1945 N  N   . HIS A 1 252 ? -22.600 21.752  27.421 1.00 93.26  ? 548 HIS A N   1 
ATOM   1946 C  CA  . HIS A 1 252 ? -23.416 21.814  28.623 1.00 97.18  ? 548 HIS A CA  1 
ATOM   1947 C  C   . HIS A 1 252 ? -24.452 22.921  28.493 1.00 108.31 ? 548 HIS A C   1 
ATOM   1948 O  O   . HIS A 1 252 ? -24.148 23.986  27.947 1.00 110.83 ? 548 HIS A O   1 
ATOM   1949 C  CB  . HIS A 1 252 ? -22.554 22.074  29.853 1.00 90.26  ? 548 HIS A CB  1 
ATOM   1950 C  CG  . HIS A 1 252 ? -23.167 21.557  31.107 1.00 93.47  ? 548 HIS A CG  1 
ATOM   1951 N  ND1 . HIS A 1 252 ? -23.949 22.336  31.931 1.00 97.67  ? 548 HIS A ND1 1 
ATOM   1952 C  CD2 . HIS A 1 252 ? -23.164 20.316  31.647 1.00 86.61  ? 548 HIS A CD2 1 
ATOM   1953 C  CE1 . HIS A 1 252 ? -24.390 21.600  32.932 1.00 91.06  ? 548 HIS A CE1 1 
ATOM   1954 N  NE2 . HIS A 1 252 ? -23.931 20.370  32.780 1.00 86.00  ? 548 HIS A NE2 1 
ATOM   1955 N  N   . PRO A 1 253 ? -25.685 22.733  28.973 1.00 106.34 ? 549 PRO A N   1 
ATOM   1956 C  CA  . PRO A 1 253 ? -26.707 23.772  28.790 1.00 102.56 ? 549 PRO A CA  1 
ATOM   1957 C  C   . PRO A 1 253 ? -26.612 24.909  29.795 1.00 106.50 ? 549 PRO A C   1 
ATOM   1958 O  O   . PRO A 1 253 ? -27.445 25.822  29.748 1.00 112.97 ? 549 PRO A O   1 
ATOM   1959 C  CB  . PRO A 1 253 ? -28.033 23.000  28.942 1.00 85.52  ? 549 PRO A CB  1 
ATOM   1960 C  CG  . PRO A 1 253 ? -27.643 21.571  29.414 1.00 84.12  ? 549 PRO A CG  1 
ATOM   1961 C  CD  . PRO A 1 253 ? -26.188 21.598  29.758 1.00 80.16  ? 549 PRO A CD  1 
ATOM   1962 N  N   . LYS A 1 254 ? -25.631 24.883  30.694 1.00 96.72  ? 550 LYS A N   1 
ATOM   1963 C  CA  . LYS A 1 254 ? -25.323 26.022  31.546 1.00 109.83 ? 550 LYS A CA  1 
ATOM   1964 C  C   . LYS A 1 254 ? -23.920 26.568  31.329 1.00 116.53 ? 550 LYS A C   1 
ATOM   1965 O  O   . LYS A 1 254 ? -23.743 27.788  31.253 1.00 118.60 ? 550 LYS A O   1 
ATOM   1966 C  CB  . LYS A 1 254 ? -25.485 25.643  33.023 1.00 120.55 ? 550 LYS A CB  1 
ATOM   1967 C  CG  . LYS A 1 254 ? -26.720 24.809  33.351 1.00 121.83 ? 550 LYS A CG  1 
ATOM   1968 C  CD  . LYS A 1 254 ? -28.027 25.580  33.161 1.00 128.99 ? 550 LYS A CD  1 
ATOM   1969 C  CE  . LYS A 1 254 ? -29.189 24.851  33.847 1.00 125.78 ? 550 LYS A CE  1 
ATOM   1970 N  NZ  . LYS A 1 254 ? -30.532 25.408  33.496 1.00 130.95 ? 550 LYS A NZ  1 
ATOM   1971 N  N   . PHE A 1 255 ? -22.923 25.698  31.198 1.00 114.37 ? 551 PHE A N   1 
ATOM   1972 C  CA  . PHE A 1 255 ? -21.517 26.072  31.324 1.00 118.66 ? 551 PHE A CA  1 
ATOM   1973 C  C   . PHE A 1 255 ? -20.897 26.269  29.941 1.00 125.27 ? 551 PHE A C   1 
ATOM   1974 O  O   . PHE A 1 255 ? -20.691 25.298  29.203 1.00 115.79 ? 551 PHE A O   1 
ATOM   1975 C  CB  . PHE A 1 255 ? -20.767 25.000  32.112 1.00 109.62 ? 551 PHE A CB  1 
ATOM   1976 C  CG  . PHE A 1 255 ? -21.417 24.636  33.430 1.00 113.20 ? 551 PHE A CG  1 
ATOM   1977 C  CD1 . PHE A 1 255 ? -21.477 23.314  33.845 1.00 110.65 ? 551 PHE A CD1 1 
ATOM   1978 C  CD2 . PHE A 1 255 ? -21.951 25.615  34.261 1.00 116.11 ? 551 PHE A CD2 1 
ATOM   1979 C  CE1 . PHE A 1 255 ? -22.068 22.972  35.066 1.00 109.13 ? 551 PHE A CE1 1 
ATOM   1980 C  CE2 . PHE A 1 255 ? -22.544 25.282  35.473 1.00 119.16 ? 551 PHE A CE2 1 
ATOM   1981 C  CZ  . PHE A 1 255 ? -22.600 23.963  35.877 1.00 110.53 ? 551 PHE A CZ  1 
ATOM   1982 N  N   . ASP A 1 256 ? -20.581 27.528  29.604 1.00 133.21 ? 552 ASP A N   1 
ATOM   1983 C  CA  . ASP A 1 256 ? -20.004 27.839  28.297 1.00 132.21 ? 552 ASP A CA  1 
ATOM   1984 C  C   . ASP A 1 256 ? -18.566 27.353  28.176 1.00 125.42 ? 552 ASP A C   1 
ATOM   1985 O  O   . ASP A 1 256 ? -18.110 27.053  27.067 1.00 128.53 ? 552 ASP A O   1 
ATOM   1986 C  CB  . ASP A 1 256 ? -20.056 29.345  28.037 1.00 153.26 ? 552 ASP A CB  1 
ATOM   1987 C  CG  . ASP A 1 256 ? -20.985 29.710  26.896 1.00 166.58 ? 552 ASP A CG  1 
ATOM   1988 O  OD1 . ASP A 1 256 ? -22.000 30.392  27.149 1.00 172.66 ? 552 ASP A OD1 1 
ATOM   1989 O  OD2 . ASP A 1 256 ? -20.704 29.308  25.747 1.00 167.49 ? 552 ASP A OD2 1 
ATOM   1990 N  N   . TRP A 1 257 ? -17.826 27.300  29.289 1.00 128.05 ? 553 TRP A N   1 
ATOM   1991 C  CA  . TRP A 1 257 ? -16.492 26.711  29.259 1.00 122.27 ? 553 TRP A CA  1 
ATOM   1992 C  C   . TRP A 1 257 ? -16.513 25.251  28.840 1.00 112.03 ? 553 TRP A C   1 
ATOM   1993 O  O   . TRP A 1 257 ? -15.466 24.723  28.453 1.00 110.95 ? 553 TRP A O   1 
ATOM   1994 C  CB  . TRP A 1 257 ? -15.811 26.829  30.627 1.00 120.14 ? 553 TRP A CB  1 
ATOM   1995 C  CG  . TRP A 1 257 ? -16.640 26.326  31.789 1.00 122.63 ? 553 TRP A CG  1 
ATOM   1996 C  CD1 . TRP A 1 257 ? -17.404 27.081  32.628 1.00 125.06 ? 553 TRP A CD1 1 
ATOM   1997 C  CD2 . TRP A 1 257 ? -16.787 24.963  32.235 1.00 112.81 ? 553 TRP A CD2 1 
ATOM   1998 N  NE1 . TRP A 1 257 ? -18.014 26.282  33.561 1.00 124.30 ? 553 TRP A NE1 1 
ATOM   1999 C  CE2 . TRP A 1 257 ? -17.652 24.979  33.343 1.00 116.70 ? 553 TRP A CE2 1 
ATOM   2000 C  CE3 . TRP A 1 257 ? -16.274 23.737  31.802 1.00 102.44 ? 553 TRP A CE3 1 
ATOM   2001 C  CZ2 . TRP A 1 257 ? -18.013 23.818  34.028 1.00 108.22 ? 553 TRP A CZ2 1 
ATOM   2002 C  CZ3 . TRP A 1 257 ? -16.634 22.588  32.482 1.00 100.18 ? 553 TRP A CZ3 1 
ATOM   2003 C  CH2 . TRP A 1 257 ? -17.498 22.634  33.578 1.00 95.16  ? 553 TRP A CH2 1 
ATOM   2004 N  N   . PHE A 1 258 ? -17.672 24.591  28.912 1.00 99.78  ? 554 PHE A N   1 
ATOM   2005 C  CA  . PHE A 1 258 ? -17.751 23.183  28.539 1.00 104.57 ? 554 PHE A CA  1 
ATOM   2006 C  C   . PHE A 1 258 ? -17.451 22.962  27.062 1.00 103.98 ? 554 PHE A C   1 
ATOM   2007 O  O   . PHE A 1 258 ? -16.895 21.919  26.702 1.00 102.94 ? 554 PHE A O   1 
ATOM   2008 C  CB  . PHE A 1 258 ? -19.129 22.622  28.880 1.00 106.40 ? 554 PHE A CB  1 
ATOM   2009 C  CG  . PHE A 1 258 ? -19.122 21.163  29.145 1.00 99.23  ? 554 PHE A CG  1 
ATOM   2010 C  CD1 . PHE A 1 258 ? -18.889 20.693  30.428 1.00 97.93  ? 554 PHE A CD1 1 
ATOM   2011 C  CD2 . PHE A 1 258 ? -19.324 20.251  28.125 1.00 97.01  ? 554 PHE A CD2 1 
ATOM   2012 C  CE1 . PHE A 1 258 ? -18.866 19.344  30.698 1.00 89.35  ? 554 PHE A CE1 1 
ATOM   2013 C  CE2 . PHE A 1 258 ? -19.301 18.885  28.387 1.00 93.54  ? 554 PHE A CE2 1 
ATOM   2014 C  CZ  . PHE A 1 258 ? -19.074 18.434  29.683 1.00 91.28  ? 554 PHE A CZ  1 
ATOM   2015 N  N   . LYS A 1 259 ? -17.823 23.911  26.195 1.00 104.49 ? 555 LYS A N   1 
ATOM   2016 C  CA  . LYS A 1 259 ? -17.457 23.826  24.782 1.00 115.64 ? 555 LYS A CA  1 
ATOM   2017 C  C   . LYS A 1 259 ? -15.953 23.710  24.616 1.00 118.46 ? 555 LYS A C   1 
ATOM   2018 O  O   . LYS A 1 259 ? -15.465 22.964  23.757 1.00 104.92 ? 555 LYS A O   1 
ATOM   2019 C  CB  . LYS A 1 259 ? -17.943 25.064  24.025 1.00 124.83 ? 555 LYS A CB  1 
ATOM   2020 C  CG  . LYS A 1 259 ? -19.432 25.290  24.040 1.00 127.77 ? 555 LYS A CG  1 
ATOM   2021 C  CD  . LYS A 1 259 ? -19.769 26.766  23.863 1.00 135.94 ? 555 LYS A CD  1 
ATOM   2022 C  CE  . LYS A 1 259 ? -21.271 26.928  23.823 1.00 135.92 ? 555 LYS A CE  1 
ATOM   2023 N  NZ  . LYS A 1 259 ? -21.913 25.847  24.634 1.00 127.40 ? 555 LYS A NZ  1 
ATOM   2024 N  N   . ASP A 1 260 ? -15.201 24.473  25.414 1.00 117.94 ? 556 ASP A N   1 
ATOM   2025 C  CA  . ASP A 1 260 ? -13.757 24.536  25.248 1.00 124.69 ? 556 ASP A CA  1 
ATOM   2026 C  C   . ASP A 1 260 ? -13.087 23.241  25.674 1.00 116.89 ? 556 ASP A C   1 
ATOM   2027 O  O   . ASP A 1 260 ? -11.919 23.020  25.341 1.00 125.69 ? 556 ASP A O   1 
ATOM   2028 C  CB  . ASP A 1 260 ? -13.195 25.733  26.025 1.00 133.29 ? 556 ASP A CB  1 
ATOM   2029 C  CG  . ASP A 1 260 ? -13.913 27.038  25.686 1.00 135.28 ? 556 ASP A CG  1 
ATOM   2030 O  OD1 . ASP A 1 260 ? -14.465 27.138  24.569 1.00 135.63 ? 556 ASP A OD1 1 
ATOM   2031 O  OD2 . ASP A 1 260 ? -13.932 27.956  26.534 1.00 138.67 ? 556 ASP A OD2 1 
ATOM   2032 N  N   . LEU A 1 261 ? -13.804 22.374  26.387 1.00 108.03 ? 557 LEU A N   1 
ATOM   2033 C  CA  . LEU A 1 261 ? -13.287 21.035  26.620 1.00 114.69 ? 557 LEU A CA  1 
ATOM   2034 C  C   . LEU A 1 261 ? -13.126 20.283  25.306 1.00 121.57 ? 557 LEU A C   1 
ATOM   2035 O  O   . LEU A 1 261 ? -12.335 19.339  25.233 1.00 127.14 ? 557 LEU A O   1 
ATOM   2036 C  CB  . LEU A 1 261 ? -14.193 20.272  27.600 1.00 106.02 ? 557 LEU A CB  1 
ATOM   2037 C  CG  . LEU A 1 261 ? -14.162 20.744  29.060 1.00 109.15 ? 557 LEU A CG  1 
ATOM   2038 C  CD1 . LEU A 1 261 ? -15.137 19.971  29.988 1.00 93.81  ? 557 LEU A CD1 1 
ATOM   2039 C  CD2 . LEU A 1 261 ? -12.744 20.649  29.599 1.00 120.57 ? 557 LEU A CD2 1 
ATOM   2040 N  N   . GLY A 1 262 ? -13.835 20.708  24.263 1.00 125.25 ? 558 GLY A N   1 
ATOM   2041 C  CA  . GLY A 1 262 ? -13.612 20.191  22.924 1.00 126.15 ? 558 GLY A CA  1 
ATOM   2042 C  C   . GLY A 1 262 ? -13.890 18.717  22.778 1.00 118.69 ? 558 GLY A C   1 
ATOM   2043 O  O   . GLY A 1 262 ? -13.232 18.044  21.980 1.00 120.10 ? 558 GLY A O   1 
ATOM   2044 N  N   . LEU A 1 263 ? -14.842 18.190  23.537 1.00 110.04 ? 559 LEU A N   1 
ATOM   2045 C  CA  . LEU A 1 263 ? -15.161 16.777  23.480 1.00 99.70  ? 559 LEU A CA  1 
ATOM   2046 C  C   . LEU A 1 263 ? -16.261 16.527  22.463 1.00 96.53  ? 559 LEU A C   1 
ATOM   2047 O  O   . LEU A 1 263 ? -17.072 17.405  22.160 1.00 98.21  ? 559 LEU A O   1 
ATOM   2048 C  CB  . LEU A 1 263 ? -15.606 16.264  24.845 1.00 90.15  ? 559 LEU A CB  1 
ATOM   2049 C  CG  . LEU A 1 263 ? -14.684 16.538  26.030 1.00 96.96  ? 559 LEU A CG  1 
ATOM   2050 C  CD1 . LEU A 1 263 ? -15.531 16.513  27.271 1.00 87.76  ? 559 LEU A CD1 1 
ATOM   2051 C  CD2 . LEU A 1 263 ? -13.567 15.509  26.128 1.00 104.58 ? 559 LEU A CD2 1 
ATOM   2052 N  N   . LYS A 1 264 ? -16.279 15.306  21.942 1.00 91.75  ? 560 LYS A N   1 
ATOM   2053 C  CA  . LYS A 1 264 ? -17.347 14.859  21.065 1.00 84.85  ? 560 LYS A CA  1 
ATOM   2054 C  C   . LYS A 1 264 ? -17.476 13.362  21.231 1.00 74.67  ? 560 LYS A C   1 
ATOM   2055 O  O   . LYS A 1 264 ? -16.614 12.710  21.823 1.00 76.16  ? 560 LYS A O   1 
ATOM   2056 C  CB  . LYS A 1 264 ? -17.092 15.215  19.594 1.00 87.04  ? 560 LYS A CB  1 
ATOM   2057 C  CG  . LYS A 1 264 ? -15.745 14.774  19.034 1.00 92.76  ? 560 LYS A CG  1 
ATOM   2058 C  CD  . LYS A 1 264 ? -15.680 15.063  17.537 1.00 99.36  ? 560 LYS A CD  1 
ATOM   2059 C  CE  . LYS A 1 264 ? -14.251 15.126  16.991 1.00 100.82 ? 560 LYS A CE  1 
ATOM   2060 N  NZ  . LYS A 1 264 ? -14.216 15.232  15.496 1.00 91.89  ? 560 LYS A NZ  1 
ATOM   2061 N  N   . TRP A 1 265 ? -18.574 12.824  20.717 1.00 66.19  ? 561 TRP A N   1 
ATOM   2062 C  CA  . TRP A 1 265 ? -18.738 11.384  20.647 1.00 67.19  ? 561 TRP A CA  1 
ATOM   2063 C  C   . TRP A 1 265 ? -19.499 11.046  19.373 1.00 69.12  ? 561 TRP A C   1 
ATOM   2064 O  O   . TRP A 1 265 ? -20.164 11.899  18.773 1.00 70.79  ? 561 TRP A O   1 
ATOM   2065 C  CB  . TRP A 1 265 ? -19.458 10.820  21.888 1.00 60.56  ? 561 TRP A CB  1 
ATOM   2066 C  CG  . TRP A 1 265 ? -19.155 9.356   22.118 1.00 53.56  ? 561 TRP A CG  1 
ATOM   2067 C  CD1 . TRP A 1 265 ? -20.008 8.297   21.966 1.00 58.32  ? 561 TRP A CD1 1 
ATOM   2068 C  CD2 . TRP A 1 265 ? -17.898 8.803   22.511 1.00 64.39  ? 561 TRP A CD2 1 
ATOM   2069 N  NE1 . TRP A 1 265 ? -19.362 7.116   22.269 1.00 67.85  ? 561 TRP A NE1 1 
ATOM   2070 C  CE2 . TRP A 1 265 ? -18.062 7.401   22.601 1.00 71.50  ? 561 TRP A CE2 1 
ATOM   2071 C  CE3 . TRP A 1 265 ? -16.646 9.358   22.807 1.00 64.84  ? 561 TRP A CE3 1 
ATOM   2072 C  CZ2 . TRP A 1 265 ? -17.017 6.549   22.966 1.00 65.81  ? 561 TRP A CZ2 1 
ATOM   2073 C  CZ3 . TRP A 1 265 ? -15.615 8.517   23.159 1.00 67.89  ? 561 TRP A CZ3 1 
ATOM   2074 C  CH2 . TRP A 1 265 ? -15.806 7.124   23.246 1.00 59.09  ? 561 TRP A CH2 1 
ATOM   2075 N  N   . TYR A 1 266 ? -19.366 9.792   18.951 1.00 61.69  ? 562 TYR A N   1 
ATOM   2076 C  CA  . TYR A 1 266 ? -20.082 9.291   17.789 1.00 60.46  ? 562 TYR A CA  1 
ATOM   2077 C  C   . TYR A 1 266 ? -21.446 8.750   18.204 1.00 62.92  ? 562 TYR A C   1 
ATOM   2078 O  O   . TYR A 1 266 ? -21.624 8.225   19.312 1.00 68.28  ? 562 TYR A O   1 
ATOM   2079 C  CB  . TYR A 1 266 ? -19.269 8.195   17.100 1.00 46.10  ? 562 TYR A CB  1 
ATOM   2080 C  CG  . TYR A 1 266 ? -18.833 7.068   18.026 1.00 53.58  ? 562 TYR A CG  1 
ATOM   2081 C  CD1 . TYR A 1 266 ? -19.666 5.984   18.276 1.00 61.31  ? 562 TYR A CD1 1 
ATOM   2082 C  CD2 . TYR A 1 266 ? -17.580 7.078   18.635 1.00 46.40  ? 562 TYR A CD2 1 
ATOM   2083 C  CE1 . TYR A 1 266 ? -19.270 4.950   19.105 1.00 62.42  ? 562 TYR A CE1 1 
ATOM   2084 C  CE2 . TYR A 1 266 ? -17.183 6.028   19.488 1.00 47.38  ? 562 TYR A CE2 1 
ATOM   2085 C  CZ  . TYR A 1 266 ? -18.026 4.980   19.717 1.00 55.01  ? 562 TYR A CZ  1 
ATOM   2086 O  OH  . TYR A 1 266 ? -17.624 3.951   20.569 1.00 67.61  ? 562 TYR A OH  1 
ATOM   2087 N  N   . GLY A 1 267 ? -22.420 8.893   17.304 1.00 54.08  ? 563 GLY A N   1 
ATOM   2088 C  CA  . GLY A 1 267 ? -23.787 8.527   17.625 1.00 56.71  ? 563 GLY A CA  1 
ATOM   2089 C  C   . GLY A 1 267 ? -24.059 7.031   17.680 1.00 67.90  ? 563 GLY A C   1 
ATOM   2090 O  O   . GLY A 1 267 ? -25.022 6.621   18.337 1.00 76.20  ? 563 GLY A O   1 
ATOM   2091 N  N   . LEU A 1 268 ? -23.232 6.207   17.022 1.00 51.86  ? 564 LEU A N   1 
ATOM   2092 C  CA  . LEU A 1 268 ? -23.621 4.825   16.732 1.00 56.59  ? 564 LEU A CA  1 
ATOM   2093 C  C   . LEU A 1 268 ? -22.838 3.812   17.560 1.00 60.65  ? 564 LEU A C   1 
ATOM   2094 O  O   . LEU A 1 268 ? -21.652 3.564   17.274 1.00 54.00  ? 564 LEU A O   1 
ATOM   2095 C  CB  . LEU A 1 268 ? -23.457 4.522   15.241 1.00 53.77  ? 564 LEU A CB  1 
ATOM   2096 C  CG  . LEU A 1 268 ? -24.074 3.221   14.707 1.00 53.55  ? 564 LEU A CG  1 
ATOM   2097 C  CD1 . LEU A 1 268 ? -25.586 3.289   14.507 1.00 59.08  ? 564 LEU A CD1 1 
ATOM   2098 C  CD2 . LEU A 1 268 ? -23.400 2.821   13.434 1.00 46.02  ? 564 LEU A CD2 1 
ATOM   2099 N  N   . PRO A 1 269 ? -23.454 3.188   18.574 1.00 59.06  ? 565 PRO A N   1 
ATOM   2100 C  CA  . PRO A 1 269 ? -22.800 2.077   19.281 1.00 47.72  ? 565 PRO A CA  1 
ATOM   2101 C  C   . PRO A 1 269 ? -23.006 0.790   18.490 1.00 40.77  ? 565 PRO A C   1 
ATOM   2102 O  O   . PRO A 1 269 ? -24.143 0.353   18.275 1.00 47.14  ? 565 PRO A O   1 
ATOM   2103 C  CB  . PRO A 1 269 ? -23.526 2.049   20.630 1.00 57.36  ? 565 PRO A CB  1 
ATOM   2104 C  CG  . PRO A 1 269 ? -24.918 2.515   20.271 1.00 60.68  ? 565 PRO A CG  1 
ATOM   2105 C  CD  . PRO A 1 269 ? -24.803 3.455   19.093 1.00 61.63  ? 565 PRO A CD  1 
ATOM   2106 N  N   . ALA A 1 270 ? -21.902 0.220   17.969 1.00 41.50  ? 566 ALA A N   1 
ATOM   2107 C  CA  . ALA A 1 270 ? -21.982 -0.921  17.028 1.00 44.54  ? 566 ALA A CA  1 
ATOM   2108 C  C   . ALA A 1 270 ? -20.875 -1.919  17.376 1.00 48.74  ? 566 ALA A C   1 
ATOM   2109 O  O   . ALA A 1 270 ? -19.735 -1.787  16.919 1.00 52.57  ? 566 ALA A O   1 
ATOM   2110 C  CB  . ALA A 1 270 ? -21.891 -0.458  15.554 1.00 36.55  ? 566 ALA A CB  1 
ATOM   2111 N  N   . VAL A 1 271 ? -21.220 -2.920  18.179 1.00 43.94  ? 567 VAL A N   1 
ATOM   2112 C  CA  . VAL A 1 271 ? -20.247 -3.905  18.629 1.00 45.45  ? 567 VAL A CA  1 
ATOM   2113 C  C   . VAL A 1 271 ? -20.019 -4.913  17.521 1.00 43.82  ? 567 VAL A C   1 
ATOM   2114 O  O   . VAL A 1 271 ? -20.968 -5.429  16.919 1.00 70.14  ? 567 VAL A O   1 
ATOM   2115 C  CB  . VAL A 1 271 ? -20.719 -4.584  19.925 1.00 44.58  ? 567 VAL A CB  1 
ATOM   2116 C  CG1 . VAL A 1 271 ? -20.038 -5.967  20.104 1.00 50.69  ? 567 VAL A CG1 1 
ATOM   2117 C  CG2 . VAL A 1 271 ? -20.424 -3.680  21.103 1.00 43.05  ? 567 VAL A CG2 1 
ATOM   2118 N  N   . SER A 1 272 ? -18.754 -5.179  17.237 1.00 49.99  ? 568 SER A N   1 
ATOM   2119 C  CA  . SER A 1 272 ? -18.367 -5.958  16.085 1.00 60.67  ? 568 SER A CA  1 
ATOM   2120 C  C   . SER A 1 272 ? -17.597 -7.221  16.431 1.00 62.78  ? 568 SER A C   1 
ATOM   2121 O  O   . SER A 1 272 ? -17.250 -7.978  15.511 1.00 63.65  ? 568 SER A O   1 
ATOM   2122 C  CB  . SER A 1 272 ? -17.528 -5.080  15.148 1.00 64.96  ? 568 SER A CB  1 
ATOM   2123 O  OG  . SER A 1 272 ? -16.633 -4.266  15.891 1.00 59.93  ? 568 SER A OG  1 
ATOM   2124 N  N   . ASN A 1 273 ? -17.309 -7.473  17.715 1.00 58.40  ? 569 ASN A N   1 
ATOM   2125 C  CA  . ASN A 1 273 ? -16.341 -8.494  18.096 1.00 57.90  ? 569 ASN A CA  1 
ATOM   2126 C  C   . ASN A 1 273 ? -16.966 -9.707  18.759 1.00 59.80  ? 569 ASN A C   1 
ATOM   2127 O  O   . ASN A 1 273 ? -16.235 -10.534 19.304 1.00 73.03  ? 569 ASN A O   1 
ATOM   2128 C  CB  . ASN A 1 273 ? -15.255 -7.915  19.013 1.00 65.88  ? 569 ASN A CB  1 
ATOM   2129 C  CG  . ASN A 1 273 ? -15.807 -7.285  20.309 1.00 55.47  ? 569 ASN A CG  1 
ATOM   2130 O  OD1 . ASN A 1 273 ? -16.984 -7.417  20.659 1.00 52.85  ? 569 ASN A OD1 1 
ATOM   2131 N  ND2 . ASN A 1 273 ? -14.934 -6.585  21.015 1.00 59.91  ? 569 ASN A ND2 1 
ATOM   2132 N  N   . MET A 1 274 ? -18.281 -9.857  18.704 1.00 50.99  ? 570 MET A N   1 
ATOM   2133 C  CA  . MET A 1 274 ? -18.957 -10.965 19.356 1.00 54.89  ? 570 MET A CA  1 
ATOM   2134 C  C   . MET A 1 274 ? -19.449 -11.983 18.338 1.00 55.51  ? 570 MET A C   1 
ATOM   2135 O  O   . MET A 1 274 ? -19.443 -11.744 17.126 1.00 62.93  ? 570 MET A O   1 
ATOM   2136 C  CB  . MET A 1 274 ? -20.106 -10.445 20.212 1.00 65.10  ? 570 MET A CB  1 
ATOM   2137 C  CG  . MET A 1 274 ? -19.605 -9.538  21.321 1.00 67.48  ? 570 MET A CG  1 
ATOM   2138 S  SD  . MET A 1 274 ? -20.929 -9.182  22.439 1.00 51.54  ? 570 MET A SD  1 
ATOM   2139 C  CE  . MET A 1 274 ? -20.987 -10.775 23.295 1.00 43.66  ? 570 MET A CE  1 
ATOM   2140 N  N   . LEU A 1 275 ? -19.863 -13.142 18.856 1.00 47.23  ? 571 LEU A N   1 
ATOM   2141 C  CA  . LEU A 1 275 ? -20.211 -14.307 18.049 1.00 54.80  ? 571 LEU A CA  1 
ATOM   2142 C  C   . LEU A 1 275 ? -21.706 -14.579 18.180 1.00 60.39  ? 571 LEU A C   1 
ATOM   2143 O  O   . LEU A 1 275 ? -22.223 -14.641 19.292 1.00 56.22  ? 571 LEU A O   1 
ATOM   2144 C  CB  . LEU A 1 275 ? -19.398 -15.524 18.495 1.00 60.60  ? 571 LEU A CB  1 
ATOM   2145 C  CG  . LEU A 1 275 ? -19.291 -16.667 17.481 1.00 70.19  ? 571 LEU A CG  1 
ATOM   2146 C  CD1 . LEU A 1 275 ? -17.932 -17.349 17.591 1.00 71.65  ? 571 LEU A CD1 1 
ATOM   2147 C  CD2 . LEU A 1 275 ? -20.434 -17.666 17.655 1.00 73.02  ? 571 LEU A CD2 1 
ATOM   2148 N  N   . LEU A 1 276 ? -22.395 -14.759 17.054 1.00 58.74  ? 572 LEU A N   1 
ATOM   2149 C  CA  . LEU A 1 276 ? -23.835 -15.026 17.039 1.00 52.71  ? 572 LEU A CA  1 
ATOM   2150 C  C   . LEU A 1 276 ? -24.070 -16.525 16.863 1.00 61.19  ? 572 LEU A C   1 
ATOM   2151 O  O   . LEU A 1 276 ? -23.849 -17.068 15.774 1.00 68.74  ? 572 LEU A O   1 
ATOM   2152 C  CB  . LEU A 1 276 ? -24.507 -14.244 15.906 1.00 51.29  ? 572 LEU A CB  1 
ATOM   2153 C  CG  . LEU A 1 276 ? -25.953 -14.555 15.512 1.00 53.82  ? 572 LEU A CG  1 
ATOM   2154 C  CD1 . LEU A 1 276 ? -26.891 -14.485 16.695 1.00 47.89  ? 572 LEU A CD1 1 
ATOM   2155 C  CD2 . LEU A 1 276 ? -26.405 -13.582 14.444 1.00 54.27  ? 572 LEU A CD2 1 
ATOM   2156 N  N   . GLU A 1 277 ? -24.543 -17.191 17.910 1.00 67.05  ? 573 GLU A N   1 
ATOM   2157 C  CA  . GLU A 1 277 ? -24.863 -18.611 17.824 1.00 66.55  ? 573 GLU A CA  1 
ATOM   2158 C  C   . GLU A 1 277 ? -26.348 -18.787 17.511 1.00 63.13  ? 573 GLU A C   1 
ATOM   2159 O  O   . GLU A 1 277 ? -27.209 -18.268 18.231 1.00 54.52  ? 573 GLU A O   1 
ATOM   2160 C  CB  . GLU A 1 277 ? -24.504 -19.344 19.114 1.00 74.10  ? 573 GLU A CB  1 
ATOM   2161 C  CG  . GLU A 1 277 ? -23.593 -20.533 18.882 1.00 84.28  ? 573 GLU A CG  1 
ATOM   2162 C  CD  . GLU A 1 277 ? -23.744 -21.599 19.947 1.00 94.81  ? 573 GLU A CD  1 
ATOM   2163 O  OE1 . GLU A 1 277 ? -24.891 -22.043 20.172 1.00 97.08  ? 573 GLU A OE1 1 
ATOM   2164 O  OE2 . GLU A 1 277 ? -22.718 -21.992 20.545 1.00 96.43  ? 573 GLU A OE2 1 
ATOM   2165 N  N   . ILE A 1 278 ? -26.645 -19.486 16.414 1.00 64.53  ? 574 ILE A N   1 
ATOM   2166 C  CA  . ILE A 1 278 ? -28.010 -19.816 16.025 1.00 59.08  ? 574 ILE A CA  1 
ATOM   2167 C  C   . ILE A 1 278 ? -28.028 -21.277 15.638 1.00 64.31  ? 574 ILE A C   1 
ATOM   2168 O  O   . ILE A 1 278 ? -27.272 -21.685 14.749 1.00 72.85  ? 574 ILE A O   1 
ATOM   2169 C  CB  . ILE A 1 278 ? -28.517 -18.973 14.846 1.00 69.60  ? 574 ILE A CB  1 
ATOM   2170 C  CG1 . ILE A 1 278 ? -28.464 -17.481 15.156 1.00 66.63  ? 574 ILE A CG1 1 
ATOM   2171 C  CG2 . ILE A 1 278 ? -29.922 -19.386 14.497 1.00 73.59  ? 574 ILE A CG2 1 
ATOM   2172 C  CD1 . ILE A 1 278 ? -28.790 -16.631 13.947 1.00 55.25  ? 574 ILE A CD1 1 
ATOM   2173 N  N   . GLY A 1 279 ? -28.887 -22.059 16.286 1.00 64.53  ? 575 GLY A N   1 
ATOM   2174 C  CA  . GLY A 1 279 ? -29.021 -23.460 15.898 1.00 67.00  ? 575 GLY A CA  1 
ATOM   2175 C  C   . GLY A 1 279 ? -27.694 -24.165 15.751 1.00 69.53  ? 575 GLY A C   1 
ATOM   2176 O  O   . GLY A 1 279 ? -27.504 -24.965 14.825 1.00 78.72  ? 575 GLY A O   1 
ATOM   2177 N  N   . GLY A 1 280 ? -26.748 -23.852 16.629 1.00 68.90  ? 576 GLY A N   1 
ATOM   2178 C  CA  . GLY A 1 280 ? -25.449 -24.469 16.588 1.00 74.22  ? 576 GLY A CA  1 
ATOM   2179 C  C   . GLY A 1 280 ? -24.524 -23.931 15.530 1.00 71.86  ? 576 GLY A C   1 
ATOM   2180 O  O   . GLY A 1 280 ? -23.389 -24.410 15.422 1.00 81.63  ? 576 GLY A O   1 
ATOM   2181 N  N   . LEU A 1 281 ? -24.961 -22.958 14.743 1.00 70.73  ? 577 LEU A N   1 
ATOM   2182 C  CA  . LEU A 1 281 ? -24.071 -22.317 13.797 1.00 70.94  ? 577 LEU A CA  1 
ATOM   2183 C  C   . LEU A 1 281 ? -23.481 -21.072 14.436 1.00 67.26  ? 577 LEU A C   1 
ATOM   2184 O  O   . LEU A 1 281 ? -24.122 -20.399 15.251 1.00 71.88  ? 577 LEU A O   1 
ATOM   2185 C  CB  . LEU A 1 281 ? -24.800 -21.979 12.490 1.00 66.72  ? 577 LEU A CB  1 
ATOM   2186 C  CG  . LEU A 1 281 ? -25.444 -23.164 11.773 1.00 64.74  ? 577 LEU A CG  1 
ATOM   2187 C  CD1 . LEU A 1 281 ? -26.288 -22.722 10.568 1.00 64.17  ? 577 LEU A CD1 1 
ATOM   2188 C  CD2 . LEU A 1 281 ? -24.378 -24.147 11.357 1.00 80.57  ? 577 LEU A CD2 1 
ATOM   2189 N  N   . GLU A 1 282 ? -22.235 -20.787 14.073 1.00 62.81  ? 578 GLU A N   1 
ATOM   2190 C  CA  . GLU A 1 282 ? -21.439 -19.744 14.702 1.00 61.29  ? 578 GLU A CA  1 
ATOM   2191 C  C   . GLU A 1 282 ? -21.074 -18.702 13.659 1.00 62.82  ? 578 GLU A C   1 
ATOM   2192 O  O   . GLU A 1 282 ? -20.343 -19.004 12.708 1.00 62.62  ? 578 GLU A O   1 
ATOM   2193 C  CB  . GLU A 1 282 ? -20.177 -20.334 15.330 1.00 63.47  ? 578 GLU A CB  1 
ATOM   2194 C  CG  . GLU A 1 282 ? -20.396 -21.636 16.053 1.00 73.21  ? 578 GLU A CG  1 
ATOM   2195 C  CD  . GLU A 1 282 ? -19.220 -21.981 16.934 1.00 86.05  ? 578 GLU A CD  1 
ATOM   2196 O  OE1 . GLU A 1 282 ? -18.095 -22.054 16.387 1.00 86.08  ? 578 GLU A OE1 1 
ATOM   2197 O  OE2 . GLU A 1 282 ? -19.425 -22.160 18.159 1.00 84.47  ? 578 GLU A OE2 1 
ATOM   2198 N  N   . PHE A 1 283 ? -21.576 -17.486 13.838 1.00 60.86  ? 579 PHE A N   1 
ATOM   2199 C  CA  . PHE A 1 283 ? -21.290 -16.378 12.932 1.00 52.47  ? 579 PHE A CA  1 
ATOM   2200 C  C   . PHE A 1 283 ? -20.246 -15.506 13.618 1.00 50.30  ? 579 PHE A C   1 
ATOM   2201 O  O   . PHE A 1 283 ? -20.553 -14.774 14.559 1.00 61.50  ? 579 PHE A O   1 
ATOM   2202 C  CB  . PHE A 1 283 ? -22.564 -15.614 12.588 1.00 60.17  ? 579 PHE A CB  1 
ATOM   2203 C  CG  . PHE A 1 283 ? -23.595 -16.461 11.870 1.00 64.93  ? 579 PHE A CG  1 
ATOM   2204 C  CD1 . PHE A 1 283 ? -24.607 -17.097 12.573 1.00 65.23  ? 579 PHE A CD1 1 
ATOM   2205 C  CD2 . PHE A 1 283 ? -23.527 -16.653 10.500 1.00 68.71  ? 579 PHE A CD2 1 
ATOM   2206 C  CE1 . PHE A 1 283 ? -25.552 -17.884 11.918 1.00 64.25  ? 579 PHE A CE1 1 
ATOM   2207 C  CE2 . PHE A 1 283 ? -24.467 -17.443 9.830  1.00 66.89  ? 579 PHE A CE2 1 
ATOM   2208 C  CZ  . PHE A 1 283 ? -25.477 -18.061 10.541 1.00 71.39  ? 579 PHE A CZ  1 
ATOM   2209 N  N   . SER A 1 284 ? -18.992 -15.611 13.168 1.00 53.25  ? 580 SER A N   1 
ATOM   2210 C  CA  . SER A 1 284 ? -17.896 -14.918 13.849 1.00 46.83  ? 580 SER A CA  1 
ATOM   2211 C  C   . SER A 1 284 ? -17.907 -13.409 13.621 1.00 55.36  ? 580 SER A C   1 
ATOM   2212 O  O   . SER A 1 284 ? -17.188 -12.675 14.316 1.00 50.26  ? 580 SER A O   1 
ATOM   2213 C  CB  . SER A 1 284 ? -16.574 -15.502 13.359 1.00 43.57  ? 580 SER A CB  1 
ATOM   2214 O  OG  . SER A 1 284 ? -16.751 -16.006 12.057 1.00 67.26  ? 580 SER A OG  1 
ATOM   2215 N  N   . ALA A 1 285 ? -18.672 -12.943 12.631 1.00 53.14  ? 581 ALA A N   1 
ATOM   2216 C  CA  . ALA A 1 285 ? -18.741 -11.542 12.244 1.00 51.03  ? 581 ALA A CA  1 
ATOM   2217 C  C   . ALA A 1 285 ? -20.210 -11.173 12.232 1.00 50.68  ? 581 ALA A C   1 
ATOM   2218 O  O   . ALA A 1 285 ? -20.961 -11.651 11.385 1.00 54.54  ? 581 ALA A O   1 
ATOM   2219 C  CB  . ALA A 1 285 ? -18.109 -11.319 10.875 1.00 46.02  ? 581 ALA A CB  1 
ATOM   2220 N  N   . CYS A 1 286 ? -20.626 -10.348 13.162 1.00 55.82  ? 582 CYS A N   1 
ATOM   2221 C  CA  . CYS A 1 286 ? -22.048 -10.060 13.234 1.00 44.31  ? 582 CYS A CA  1 
ATOM   2222 C  C   . CYS A 1 286 ? -22.307 -8.682  13.843 1.00 50.29  ? 582 CYS A C   1 
ATOM   2223 O  O   . CYS A 1 286 ? -23.138 -8.570  14.748 1.00 55.81  ? 582 CYS A O   1 
ATOM   2224 C  CB  . CYS A 1 286 ? -22.744 -11.139 14.054 1.00 58.85  ? 582 CYS A CB  1 
ATOM   2225 S  SG  . CYS A 1 286 ? -21.992 -11.332 15.688 1.00 49.08  ? 582 CYS A SG  1 
ATOM   2226 N  N   . PRO A 1 287 ? -21.685 -7.614  13.336 1.00 50.31  ? 583 PRO A N   1 
ATOM   2227 C  CA  . PRO A 1 287 ? -21.826 -6.298  13.972 1.00 33.20  ? 583 PRO A CA  1 
ATOM   2228 C  C   . PRO A 1 287 ? -23.274 -5.904  14.191 1.00 44.95  ? 583 PRO A C   1 
ATOM   2229 O  O   . PRO A 1 287 ? -24.108 -5.996  13.290 1.00 51.65  ? 583 PRO A O   1 
ATOM   2230 C  CB  . PRO A 1 287 ? -21.136 -5.355  12.982 1.00 35.52  ? 583 PRO A CB  1 
ATOM   2231 C  CG  . PRO A 1 287 ? -21.291 -6.065  11.651 1.00 37.45  ? 583 PRO A CG  1 
ATOM   2232 C  CD  . PRO A 1 287 ? -21.036 -7.502  12.017 1.00 40.32  ? 583 PRO A CD  1 
ATOM   2233 N  N   . PHE A 1 288 ? -23.566 -5.457  15.411 1.00 51.20  ? 584 PHE A N   1 
ATOM   2234 C  CA  . PHE A 1 288 ? -24.916 -5.105  15.803 1.00 50.96  ? 584 PHE A CA  1 
ATOM   2235 C  C   . PHE A 1 288 ? -24.891 -3.745  16.483 1.00 54.07  ? 584 PHE A C   1 
ATOM   2236 O  O   . PHE A 1 288 ? -23.941 -3.393  17.187 1.00 47.96  ? 584 PHE A O   1 
ATOM   2237 C  CB  . PHE A 1 288 ? -25.546 -6.192  16.706 1.00 53.78  ? 584 PHE A CB  1 
ATOM   2238 C  CG  . PHE A 1 288 ? -24.802 -6.455  17.993 1.00 57.47  ? 584 PHE A CG  1 
ATOM   2239 C  CD1 . PHE A 1 288 ? -24.804 -5.521  19.012 1.00 52.52  ? 584 PHE A CD1 1 
ATOM   2240 C  CD2 . PHE A 1 288 ? -24.175 -7.667  18.213 1.00 54.14  ? 584 PHE A CD2 1 
ATOM   2241 C  CE1 . PHE A 1 288 ? -24.154 -5.746  20.147 1.00 42.58  ? 584 PHE A CE1 1 
ATOM   2242 C  CE2 . PHE A 1 288 ? -23.529 -7.910  19.406 1.00 37.60  ? 584 PHE A CE2 1 
ATOM   2243 C  CZ  . PHE A 1 288 ? -23.526 -6.952  20.352 1.00 43.79  ? 584 PHE A CZ  1 
ATOM   2244 N  N   . SER A 1 289 ? -25.935 -2.967  16.244 1.00 55.30  ? 585 SER A N   1 
ATOM   2245 C  CA  . SER A 1 289 ? -25.896 -1.566  16.600 1.00 53.44  ? 585 SER A CA  1 
ATOM   2246 C  C   . SER A 1 289 ? -27.244 -1.170  17.171 1.00 49.51  ? 585 SER A C   1 
ATOM   2247 O  O   . SER A 1 289 ? -28.283 -1.690  16.754 1.00 40.41  ? 585 SER A O   1 
ATOM   2248 C  CB  . SER A 1 289 ? -25.518 -0.698  15.376 1.00 53.16  ? 585 SER A CB  1 
ATOM   2249 O  OG  . SER A 1 289 ? -26.589 -0.579  14.449 1.00 52.77  ? 585 SER A OG  1 
ATOM   2250 N  N   . GLY A 1 290 ? -27.217 -0.266  18.150 1.00 42.55  ? 586 GLY A N   1 
ATOM   2251 C  CA  . GLY A 1 290 ? -28.465 0.328   18.573 1.00 49.79  ? 586 GLY A CA  1 
ATOM   2252 C  C   . GLY A 1 290 ? -28.375 1.837   18.683 1.00 58.46  ? 586 GLY A C   1 
ATOM   2253 O  O   . GLY A 1 290 ? -28.164 2.539   17.688 1.00 55.47  ? 586 GLY A O   1 
ATOM   2254 N  N   . TRP A 1 291 ? -28.559 2.344   19.898 1.00 59.93  ? 587 TRP A N   1 
ATOM   2255 C  CA  . TRP A 1 291 ? -28.290 3.735   20.222 1.00 49.18  ? 587 TRP A CA  1 
ATOM   2256 C  C   . TRP A 1 291 ? -27.820 3.754   21.665 1.00 63.22  ? 587 TRP A C   1 
ATOM   2257 O  O   . TRP A 1 291 ? -28.040 2.801   22.413 1.00 67.56  ? 587 TRP A O   1 
ATOM   2258 C  CB  . TRP A 1 291 ? -29.514 4.634   20.004 1.00 56.44  ? 587 TRP A CB  1 
ATOM   2259 C  CG  . TRP A 1 291 ? -30.747 4.171   20.697 1.00 61.22  ? 587 TRP A CG  1 
ATOM   2260 C  CD1 . TRP A 1 291 ? -31.039 4.285   22.047 1.00 65.27  ? 587 TRP A CD1 1 
ATOM   2261 C  CD2 . TRP A 1 291 ? -31.873 3.526   20.099 1.00 59.70  ? 587 TRP A CD2 1 
ATOM   2262 N  NE1 . TRP A 1 291 ? -32.278 3.743   22.307 1.00 65.41  ? 587 TRP A NE1 1 
ATOM   2263 C  CE2 . TRP A 1 291 ? -32.811 3.273   21.130 1.00 70.44  ? 587 TRP A CE2 1 
ATOM   2264 C  CE3 . TRP A 1 291 ? -32.187 3.140   18.789 1.00 66.78  ? 587 TRP A CE3 1 
ATOM   2265 C  CZ2 . TRP A 1 291 ? -34.028 2.637   20.886 1.00 77.66  ? 587 TRP A CZ2 1 
ATOM   2266 C  CZ3 . TRP A 1 291 ? -33.393 2.522   18.550 1.00 62.22  ? 587 TRP A CZ3 1 
ATOM   2267 C  CH2 . TRP A 1 291 ? -34.300 2.273   19.588 1.00 72.14  ? 587 TRP A CH2 1 
ATOM   2268 N  N   . TYR A 1 292 ? -27.149 4.835   22.044 1.00 65.28  ? 588 TYR A N   1 
ATOM   2269 C  CA  . TYR A 1 292 ? -26.478 4.864   23.326 1.00 58.91  ? 588 TYR A CA  1 
ATOM   2270 C  C   . TYR A 1 292 ? -27.458 5.208   24.426 1.00 59.36  ? 588 TYR A C   1 
ATOM   2271 O  O   . TYR A 1 292 ? -28.334 6.064   24.255 1.00 59.34  ? 588 TYR A O   1 
ATOM   2272 C  CB  . TYR A 1 292 ? -25.350 5.887   23.345 1.00 57.37  ? 588 TYR A CB  1 
ATOM   2273 C  CG  . TYR A 1 292 ? -23.960 5.399   22.981 1.00 60.37  ? 588 TYR A CG  1 
ATOM   2274 C  CD1 . TYR A 1 292 ? -23.330 5.914   21.879 1.00 53.47  ? 588 TYR A CD1 1 
ATOM   2275 C  CD2 . TYR A 1 292 ? -23.258 4.481   23.760 1.00 58.01  ? 588 TYR A CD2 1 
ATOM   2276 C  CE1 . TYR A 1 292 ? -22.065 5.536   21.537 1.00 58.11  ? 588 TYR A CE1 1 
ATOM   2277 C  CE2 . TYR A 1 292 ? -21.952 4.090   23.409 1.00 56.84  ? 588 TYR A CE2 1 
ATOM   2278 C  CZ  . TYR A 1 292 ? -21.375 4.629   22.279 1.00 56.67  ? 588 TYR A CZ  1 
ATOM   2279 O  OH  . TYR A 1 292 ? -20.099 4.306   21.833 1.00 52.51  ? 588 TYR A OH  1 
ATOM   2280 N  N   . MET A 1 293 ? -27.310 4.514   25.547 1.00 55.96  ? 589 MET A N   1 
ATOM   2281 C  CA  . MET A 1 293 ? -27.715 5.056   26.840 1.00 53.88  ? 589 MET A CA  1 
ATOM   2282 C  C   . MET A 1 293 ? -26.663 6.054   27.305 1.00 47.53  ? 589 MET A C   1 
ATOM   2283 O  O   . MET A 1 293 ? -25.459 5.795   27.208 1.00 49.19  ? 589 MET A O   1 
ATOM   2284 C  CB  . MET A 1 293 ? -27.892 3.931   27.864 1.00 52.26  ? 589 MET A CB  1 
ATOM   2285 C  CG  . MET A 1 293 ? -28.329 4.392   29.257 1.00 60.48  ? 589 MET A CG  1 
ATOM   2286 S  SD  . MET A 1 293 ? -28.763 2.991   30.283 1.00 58.72  ? 589 MET A SD  1 
ATOM   2287 C  CE  . MET A 1 293 ? -27.145 2.404   30.846 1.00 51.87  ? 589 MET A CE  1 
ATOM   2288 N  N   . GLY A 1 294 ? -27.131 7.198   27.820 1.00 50.94  ? 590 GLY A N   1 
ATOM   2289 C  CA  . GLY A 1 294 ? -26.242 8.321   28.086 1.00 51.45  ? 590 GLY A CA  1 
ATOM   2290 C  C   . GLY A 1 294 ? -25.024 7.979   28.930 1.00 53.26  ? 590 GLY A C   1 
ATOM   2291 O  O   . GLY A 1 294 ? -23.929 8.521   28.706 1.00 45.59  ? 590 GLY A O   1 
ATOM   2292 N  N   . THR A 1 295 ? -25.193 7.078   29.910 1.00 50.73  ? 591 THR A N   1 
ATOM   2293 C  CA  . THR A 1 295 ? -24.131 6.818   30.877 1.00 60.23  ? 591 THR A CA  1 
ATOM   2294 C  C   . THR A 1 295 ? -22.947 6.083   30.265 1.00 61.30  ? 591 THR A C   1 
ATOM   2295 O  O   . THR A 1 295 ? -21.818 6.232   30.750 1.00 56.13  ? 591 THR A O   1 
ATOM   2296 C  CB  . THR A 1 295 ? -24.666 6.030   32.085 1.00 56.00  ? 591 THR A CB  1 
ATOM   2297 O  OG1 . THR A 1 295 ? -25.542 4.980   31.659 1.00 61.86  ? 591 THR A OG1 1 
ATOM   2298 C  CG2 . THR A 1 295 ? -25.398 6.976   33.064 1.00 44.00  ? 591 THR A CG2 1 
ATOM   2299 N  N   . GLU A 1 296 ? -23.160 5.285   29.218 1.00 55.51  ? 592 GLU A N   1 
ATOM   2300 C  CA  . GLU A 1 296 ? -22.021 4.616   28.608 1.00 55.56  ? 592 GLU A CA  1 
ATOM   2301 C  C   . GLU A 1 296 ? -20.953 5.626   28.214 1.00 57.60  ? 592 GLU A C   1 
ATOM   2302 O  O   . GLU A 1 296 ? -19.772 5.458   28.550 1.00 65.00  ? 592 GLU A O   1 
ATOM   2303 C  CB  . GLU A 1 296 ? -22.474 3.817   27.402 1.00 61.85  ? 592 GLU A CB  1 
ATOM   2304 C  CG  . GLU A 1 296 ? -23.522 2.788   27.682 1.00 56.06  ? 592 GLU A CG  1 
ATOM   2305 C  CD  . GLU A 1 296 ? -23.802 2.009   26.384 1.00 62.81  ? 592 GLU A CD  1 
ATOM   2306 O  OE1 . GLU A 1 296 ? -22.812 1.507   25.786 1.00 54.64  ? 592 GLU A OE1 1 
ATOM   2307 O  OE2 . GLU A 1 296 ? -24.979 1.963   25.949 1.00 49.21  ? 592 GLU A OE2 1 
ATOM   2308 N  N   . ILE A 1 297 ? -21.365 6.711   27.544 1.00 65.37  ? 593 ILE A N   1 
ATOM   2309 C  CA  . ILE A 1 297 ? -20.448 7.789   27.169 1.00 57.26  ? 593 ILE A CA  1 
ATOM   2310 C  C   . ILE A 1 297 ? -20.048 8.612   28.381 1.00 53.95  ? 593 ILE A C   1 
ATOM   2311 O  O   . ILE A 1 297 ? -18.857 8.816   28.660 1.00 57.51  ? 593 ILE A O   1 
ATOM   2312 C  CB  . ILE A 1 297 ? -21.084 8.717   26.111 1.00 50.43  ? 593 ILE A CB  1 
ATOM   2313 C  CG1 . ILE A 1 297 ? -21.605 7.929   24.925 1.00 63.41  ? 593 ILE A CG1 1 
ATOM   2314 C  CG2 . ILE A 1 297 ? -20.085 9.729   25.693 1.00 50.50  ? 593 ILE A CG2 1 
ATOM   2315 C  CD1 . ILE A 1 297 ? -22.603 8.698   24.081 1.00 66.32  ? 593 ILE A CD1 1 
ATOM   2316 N  N   . GLY A 1 298 ? -21.046 9.161   29.073 1.00 58.84  ? 594 GLY A N   1 
ATOM   2317 C  CA  . GLY A 1 298 ? -20.795 10.182  30.087 1.00 62.14  ? 594 GLY A CA  1 
ATOM   2318 C  C   . GLY A 1 298 ? -20.233 9.675   31.400 1.00 60.51  ? 594 GLY A C   1 
ATOM   2319 O  O   . GLY A 1 298 ? -19.729 10.480  32.188 1.00 69.11  ? 594 GLY A O   1 
ATOM   2320 N  N   . VAL A 1 299 ? -20.333 8.376   31.674 1.00 63.00  ? 595 VAL A N   1 
ATOM   2321 C  CA  . VAL A 1 299 ? -19.743 7.767   32.872 1.00 65.47  ? 595 VAL A CA  1 
ATOM   2322 C  C   . VAL A 1 299 ? -18.525 6.920   32.521 1.00 64.70  ? 595 VAL A C   1 
ATOM   2323 O  O   . VAL A 1 299 ? -17.424 7.163   33.016 1.00 63.25  ? 595 VAL A O   1 
ATOM   2324 C  CB  . VAL A 1 299 ? -20.786 6.941   33.654 1.00 61.58  ? 595 VAL A CB  1 
ATOM   2325 C  CG1 . VAL A 1 299 ? -20.208 6.464   35.011 1.00 55.69  ? 595 VAL A CG1 1 
ATOM   2326 C  CG2 . VAL A 1 299 ? -22.038 7.758   33.863 1.00 52.70  ? 595 VAL A CG2 1 
ATOM   2327 N  N   . ARG A 1 300 ? -18.696 5.938   31.637 1.00 66.01  ? 596 ARG A N   1 
ATOM   2328 C  CA  . ARG A 1 300 ? -17.634 4.974   31.390 1.00 53.90  ? 596 ARG A CA  1 
ATOM   2329 C  C   . ARG A 1 300 ? -16.578 5.525   30.433 1.00 75.79  ? 596 ARG A C   1 
ATOM   2330 O  O   . ARG A 1 300 ? -15.403 5.646   30.801 1.00 86.60  ? 596 ARG A O   1 
ATOM   2331 C  CB  . ARG A 1 300 ? -18.246 3.673   30.861 1.00 48.57  ? 596 ARG A CB  1 
ATOM   2332 C  CG  . ARG A 1 300 ? -19.304 3.086   31.756 1.00 51.65  ? 596 ARG A CG  1 
ATOM   2333 C  CD  . ARG A 1 300 ? -18.680 2.855   33.160 1.00 58.89  ? 596 ARG A CD  1 
ATOM   2334 N  NE  . ARG A 1 300 ? -17.461 2.048   33.054 1.00 60.02  ? 596 ARG A NE  1 
ATOM   2335 C  CZ  . ARG A 1 300 ? -17.465 0.753   32.736 1.00 54.93  ? 596 ARG A CZ  1 
ATOM   2336 N  NH1 . ARG A 1 300 ? -18.622 0.132   32.502 1.00 36.52  ? 596 ARG A NH1 1 
ATOM   2337 N  NH2 . ARG A 1 300 ? -16.320 0.079   32.634 1.00 45.66  ? 596 ARG A NH2 1 
ATOM   2338 N  N   . ASP A 1 301 ? -16.980 5.840   29.191 1.00 67.50  ? 597 ASP A N   1 
ATOM   2339 C  CA  . ASP A 1 301 ? -16.057 6.389   28.197 1.00 68.03  ? 597 ASP A CA  1 
ATOM   2340 C  C   . ASP A 1 301 ? -15.319 7.616   28.730 1.00 62.03  ? 597 ASP A C   1 
ATOM   2341 O  O   . ASP A 1 301 ? -14.092 7.731   28.608 1.00 68.67  ? 597 ASP A O   1 
ATOM   2342 C  CB  . ASP A 1 301 ? -16.816 6.755   26.909 1.00 68.56  ? 597 ASP A CB  1 
ATOM   2343 C  CG  . ASP A 1 301 ? -17.385 5.539   26.169 1.00 63.52  ? 597 ASP A CG  1 
ATOM   2344 O  OD1 . ASP A 1 301 ? -16.724 4.478   26.117 1.00 62.47  ? 597 ASP A OD1 1 
ATOM   2345 O  OD2 . ASP A 1 301 ? -18.509 5.656   25.635 1.00 62.49  ? 597 ASP A OD2 1 
ATOM   2346 N  N   . TYR A 1 302 ? -16.052 8.551   29.326 1.00 54.42  ? 598 TYR A N   1 
ATOM   2347 C  CA  . TYR A 1 302 ? -15.438 9.821   29.703 1.00 69.94  ? 598 TYR A CA  1 
ATOM   2348 C  C   . TYR A 1 302 ? -14.732 9.793   31.059 1.00 77.57  ? 598 TYR A C   1 
ATOM   2349 O  O   . TYR A 1 302 ? -13.809 10.592  31.276 1.00 83.27  ? 598 TYR A O   1 
ATOM   2350 C  CB  . TYR A 1 302 ? -16.492 10.935  29.698 1.00 81.34  ? 598 TYR A CB  1 
ATOM   2351 C  CG  . TYR A 1 302 ? -16.842 11.470  28.319 1.00 80.53  ? 598 TYR A CG  1 
ATOM   2352 C  CD1 . TYR A 1 302 ? -18.011 12.194  28.114 1.00 79.83  ? 598 TYR A CD1 1 
ATOM   2353 C  CD2 . TYR A 1 302 ? -16.012 11.242  27.228 1.00 85.25  ? 598 TYR A CD2 1 
ATOM   2354 C  CE1 . TYR A 1 302 ? -18.345 12.692  26.860 1.00 83.70  ? 598 TYR A CE1 1 
ATOM   2355 C  CE2 . TYR A 1 302 ? -16.333 11.741  25.958 1.00 84.80  ? 598 TYR A CE2 1 
ATOM   2356 C  CZ  . TYR A 1 302 ? -17.502 12.463  25.785 1.00 83.83  ? 598 TYR A CZ  1 
ATOM   2357 O  OH  . TYR A 1 302 ? -17.831 12.956  24.540 1.00 76.07  ? 598 TYR A OH  1 
ATOM   2358 N  N   . CYS A 1 303 ? -15.135 8.908   31.985 1.00 71.15  ? 599 CYS A N   1 
ATOM   2359 C  CA  . CYS A 1 303 ? -14.649 8.997   33.363 1.00 76.46  ? 599 CYS A CA  1 
ATOM   2360 C  C   . CYS A 1 303 ? -14.012 7.731   33.930 1.00 78.10  ? 599 CYS A C   1 
ATOM   2361 O  O   . CYS A 1 303 ? -13.484 7.792   35.051 1.00 81.23  ? 599 CYS A O   1 
ATOM   2362 C  CB  . CYS A 1 303 ? -15.786 9.429   34.304 1.00 76.46  ? 599 CYS A CB  1 
ATOM   2363 S  SG  . CYS A 1 303 ? -16.477 11.070  33.953 1.00 76.72  ? 599 CYS A SG  1 
ATOM   2364 N  N   . ASP A 1 304 ? -14.050 6.596   33.230 1.00 72.33  ? 600 ASP A N   1 
ATOM   2365 C  CA  . ASP A 1 304 ? -13.193 5.477   33.607 1.00 77.29  ? 600 ASP A CA  1 
ATOM   2366 C  C   . ASP A 1 304 ? -11.753 5.968   33.720 1.00 89.48  ? 600 ASP A C   1 
ATOM   2367 O  O   . ASP A 1 304 ? -11.301 6.795   32.922 1.00 98.66  ? 600 ASP A O   1 
ATOM   2368 C  CB  . ASP A 1 304 ? -13.281 4.338   32.573 1.00 78.31  ? 600 ASP A CB  1 
ATOM   2369 C  CG  . ASP A 1 304 ? -14.459 3.380   32.805 1.00 77.29  ? 600 ASP A CG  1 
ATOM   2370 O  OD1 . ASP A 1 304 ? -15.442 3.754   33.488 1.00 76.16  ? 600 ASP A OD1 1 
ATOM   2371 O  OD2 . ASP A 1 304 ? -14.390 2.231   32.303 1.00 67.80  ? 600 ASP A OD2 1 
ATOM   2372 N  N   . ASN A 1 305 ? -11.037 5.482   34.737 1.00 95.28  ? 601 ASN A N   1 
ATOM   2373 C  CA  . ASN A 1 305 ? -9.659  5.922   34.938 1.00 102.15 ? 601 ASN A CA  1 
ATOM   2374 C  C   . ASN A 1 305 ? -8.790  5.573   33.733 1.00 101.57 ? 601 ASN A C   1 
ATOM   2375 O  O   . ASN A 1 305 ? -8.007  6.404   33.255 1.00 111.52 ? 601 ASN A O   1 
ATOM   2376 C  CB  . ASN A 1 305 ? -9.085  5.306   36.216 1.00 110.74 ? 601 ASN A CB  1 
ATOM   2377 C  CG  . ASN A 1 305 ? -9.018  6.300   37.370 1.00 121.14 ? 601 ASN A CG  1 
ATOM   2378 O  OD1 . ASN A 1 305 ? -9.055  7.515   37.163 1.00 123.87 ? 601 ASN A OD1 1 
ATOM   2379 N  ND2 . ASN A 1 305 ? -8.905  5.785   38.593 1.00 123.43 ? 601 ASN A ND2 1 
ATOM   2380 N  N   . SER A 1 306 ? -8.924  4.347   33.222 1.00 95.38  ? 602 SER A N   1 
ATOM   2381 C  CA  . SER A 1 306 ? -8.160  3.883   32.070 1.00 98.85  ? 602 SER A CA  1 
ATOM   2382 C  C   . SER A 1 306 ? -8.787  4.278   30.732 1.00 98.93  ? 602 SER A C   1 
ATOM   2383 O  O   . SER A 1 306 ? -8.437  3.678   29.708 1.00 98.65  ? 602 SER A O   1 
ATOM   2384 C  CB  . SER A 1 306 ? -7.983  2.362   32.127 1.00 99.36  ? 602 SER A CB  1 
ATOM   2385 O  OG  . SER A 1 306 ? -8.375  1.844   33.390 1.00 103.84 ? 602 SER A OG  1 
ATOM   2386 N  N   . ARG A 1 307 ? -9.706  5.249   30.711 1.00 92.72  ? 603 ARG A N   1 
ATOM   2387 C  CA  . ARG A 1 307 ? -10.257 5.762   29.459 1.00 92.46  ? 603 ARG A CA  1 
ATOM   2388 C  C   . ARG A 1 307 ? -9.906  7.242   29.316 1.00 99.73  ? 603 ARG A C   1 
ATOM   2389 O  O   . ARG A 1 307 ? -8.740  7.610   29.488 1.00 110.54 ? 603 ARG A O   1 
ATOM   2390 C  CB  . ARG A 1 307 ? -11.769 5.519   29.390 1.00 78.83  ? 603 ARG A CB  1 
ATOM   2391 C  CG  . ARG A 1 307 ? -12.152 4.040   29.500 1.00 72.62  ? 603 ARG A CG  1 
ATOM   2392 C  CD  . ARG A 1 307 ? -11.735 3.218   28.295 1.00 73.23  ? 603 ARG A CD  1 
ATOM   2393 N  NE  . ARG A 1 307 ? -12.359 3.743   27.092 1.00 70.98  ? 603 ARG A NE  1 
ATOM   2394 C  CZ  . ARG A 1 307 ? -13.645 3.588   26.806 1.00 70.33  ? 603 ARG A CZ  1 
ATOM   2395 N  NH1 . ARG A 1 307 ? -14.433 2.926   27.640 1.00 64.09  ? 603 ARG A NH1 1 
ATOM   2396 N  NH2 . ARG A 1 307 ? -14.144 4.100   25.691 1.00 77.09  ? 603 ARG A NH2 1 
ATOM   2397 N  N   . TYR A 1 308 ? -10.886 8.105   29.017 1.00 96.35  ? 604 TYR A N   1 
ATOM   2398 C  CA  . TYR A 1 308 ? -10.565 9.514   28.764 1.00 91.67  ? 604 TYR A CA  1 
ATOM   2399 C  C   . TYR A 1 308 ? -10.262 10.290  30.044 1.00 89.12  ? 604 TYR A C   1 
ATOM   2400 O  O   . TYR A 1 308 ? -9.587  11.325  29.982 1.00 92.02  ? 604 TYR A O   1 
ATOM   2401 C  CB  . TYR A 1 308 ? -11.695 10.186  27.987 1.00 83.19  ? 604 TYR A CB  1 
ATOM   2402 C  CG  . TYR A 1 308 ? -11.531 10.039  26.492 1.00 88.92  ? 604 TYR A CG  1 
ATOM   2403 C  CD1 . TYR A 1 308 ? -11.711 8.810   25.869 1.00 88.65  ? 604 TYR A CD1 1 
ATOM   2404 C  CD2 . TYR A 1 308 ? -11.176 11.124  25.704 1.00 88.94  ? 604 TYR A CD2 1 
ATOM   2405 C  CE1 . TYR A 1 308 ? -11.551 8.666   24.503 1.00 80.81  ? 604 TYR A CE1 1 
ATOM   2406 C  CE2 . TYR A 1 308 ? -11.015 10.986  24.327 1.00 90.87  ? 604 TYR A CE2 1 
ATOM   2407 C  CZ  . TYR A 1 308 ? -11.204 9.756   23.739 1.00 91.92  ? 604 TYR A CZ  1 
ATOM   2408 O  OH  . TYR A 1 308 ? -11.051 9.608   22.375 1.00 99.20  ? 604 TYR A OH  1 
ATOM   2409 N  N   . ASN A 1 309 ? -10.745 9.821   31.187 1.00 79.57  ? 605 ASN A N   1 
ATOM   2410 C  CA  . ASN A 1 309 ? -10.327 10.324  32.499 1.00 84.38  ? 605 ASN A CA  1 
ATOM   2411 C  C   . ASN A 1 309 ? -10.375 11.856  32.546 1.00 91.66  ? 605 ASN A C   1 
ATOM   2412 O  O   . ASN A 1 309 ? -9.359  12.545  32.668 1.00 96.58  ? 605 ASN A O   1 
ATOM   2413 C  CB  . ASN A 1 309 ? -8.931  9.805   32.849 1.00 82.54  ? 605 ASN A CB  1 
ATOM   2414 C  CG  . ASN A 1 309 ? -8.520  10.175  34.240 1.00 86.16  ? 605 ASN A CG  1 
ATOM   2415 O  OD1 . ASN A 1 309 ? -9.381  10.402  35.090 1.00 85.34  ? 605 ASN A OD1 1 
ATOM   2416 N  ND2 . ASN A 1 309 ? -7.214  10.267  34.485 1.00 84.40  ? 605 ASN A ND2 1 
ATOM   2417 N  N   . ILE A 1 310 ? -11.595 12.378  32.409 1.00 90.68  ? 606 ILE A N   1 
ATOM   2418 C  CA  . ILE A 1 310 ? -11.831 13.815  32.299 1.00 91.22  ? 606 ILE A CA  1 
ATOM   2419 C  C   . ILE A 1 310 ? -12.361 14.438  33.582 1.00 87.98  ? 606 ILE A C   1 
ATOM   2420 O  O   . ILE A 1 310 ? -12.443 15.675  33.654 1.00 82.43  ? 606 ILE A O   1 
ATOM   2421 C  CB  . ILE A 1 310 ? -12.787 14.139  31.133 1.00 90.17  ? 606 ILE A CB  1 
ATOM   2422 C  CG1 . ILE A 1 310 ? -14.209 13.710  31.510 1.00 87.31  ? 606 ILE A CG1 1 
ATOM   2423 C  CG2 . ILE A 1 310 ? -12.332 13.449  29.868 1.00 76.81  ? 606 ILE A CG2 1 
ATOM   2424 C  CD1 . ILE A 1 310 ? -15.250 14.078  30.487 1.00 71.53  ? 606 ILE A CD1 1 
ATOM   2425 N  N   . LEU A 1 311 ? -12.733 13.639  34.585 1.00 77.69  ? 607 LEU A N   1 
ATOM   2426 C  CA  . LEU A 1 311 ? -13.218 14.205  35.843 1.00 84.29  ? 607 LEU A CA  1 
ATOM   2427 C  C   . LEU A 1 311 ? -12.263 15.258  36.383 1.00 98.07  ? 607 LEU A C   1 
ATOM   2428 O  O   . LEU A 1 311 ? -12.698 16.299  36.891 1.00 97.34  ? 607 LEU A O   1 
ATOM   2429 C  CB  . LEU A 1 311 ? -13.436 13.102  36.879 1.00 67.92  ? 607 LEU A CB  1 
ATOM   2430 C  CG  . LEU A 1 311 ? -14.800 12.390  36.896 1.00 71.98  ? 607 LEU A CG  1 
ATOM   2431 C  CD1 . LEU A 1 311 ? -14.765 11.110  37.721 1.00 74.14  ? 607 LEU A CD1 1 
ATOM   2432 C  CD2 . LEU A 1 311 ? -15.839 13.324  37.480 1.00 67.68  ? 607 LEU A CD2 1 
ATOM   2433 N  N   . GLU A 1 312 ? -10.956 15.009  36.259 1.00 113.88 ? 608 GLU A N   1 
ATOM   2434 C  CA  . GLU A 1 312 ? -9.942  15.966  36.691 1.00 125.03 ? 608 GLU A CA  1 
ATOM   2435 C  C   . GLU A 1 312 ? -10.231 17.367  36.164 1.00 124.16 ? 608 GLU A C   1 
ATOM   2436 O  O   . GLU A 1 312 ? -10.377 18.326  36.932 1.00 116.29 ? 608 GLU A O   1 
ATOM   2437 C  CB  . GLU A 1 312 ? -8.567  15.502  36.212 1.00 131.57 ? 608 GLU A CB  1 
ATOM   2438 C  CG  . GLU A 1 312 ? -8.135  14.158  36.743 1.00 131.25 ? 608 GLU A CG  1 
ATOM   2439 C  CD  . GLU A 1 312 ? -6.854  14.264  37.534 1.00 135.95 ? 608 GLU A CD  1 
ATOM   2440 O  OE1 . GLU A 1 312 ? -6.647  15.309  38.189 1.00 138.74 ? 608 GLU A OE1 1 
ATOM   2441 O  OE2 . GLU A 1 312 ? -6.048  13.312  37.492 1.00 136.60 ? 608 GLU A OE2 1 
ATOM   2442 N  N   . GLU A 1 313 ? -10.335 17.491  34.840 1.00 134.55 ? 609 GLU A N   1 
ATOM   2443 C  CA  . GLU A 1 313 ? -10.460 18.801  34.214 1.00 146.19 ? 609 GLU A CA  1 
ATOM   2444 C  C   . GLU A 1 313 ? -11.849 19.402  34.363 1.00 144.73 ? 609 GLU A C   1 
ATOM   2445 O  O   . GLU A 1 313 ? -11.975 20.625  34.472 1.00 154.11 ? 609 GLU A O   1 
ATOM   2446 C  CB  . GLU A 1 313 ? -10.092 18.707  32.738 1.00 156.19 ? 609 GLU A CB  1 
ATOM   2447 C  CG  . GLU A 1 313 ? -8.658  19.107  32.444 1.00 168.61 ? 609 GLU A CG  1 
ATOM   2448 C  CD  . GLU A 1 313 ? -8.393  20.581  32.719 1.00 178.92 ? 609 GLU A CD  1 
ATOM   2449 O  OE1 . GLU A 1 313 ? -8.365  20.991  33.901 1.00 179.88 ? 609 GLU A OE1 1 
ATOM   2450 O  OE2 . GLU A 1 313 ? -8.221  21.337  31.741 1.00 183.46 ? 609 GLU A OE2 1 
ATOM   2451 N  N   . VAL A 1 314 ? -12.897 18.581  34.356 1.00 119.56 ? 610 VAL A N   1 
ATOM   2452 C  CA  . VAL A 1 314 ? -14.247 19.116  34.513 1.00 107.79 ? 610 VAL A CA  1 
ATOM   2453 C  C   . VAL A 1 314 ? -14.397 19.755  35.887 1.00 106.85 ? 610 VAL A C   1 
ATOM   2454 O  O   . VAL A 1 314 ? -14.916 20.873  36.023 1.00 109.26 ? 610 VAL A O   1 
ATOM   2455 C  CB  . VAL A 1 314 ? -15.291 18.009  34.269 1.00 100.31 ? 610 VAL A CB  1 
ATOM   2456 C  CG1 . VAL A 1 314 ? -16.710 18.525  34.485 1.00 95.58  ? 610 VAL A CG1 1 
ATOM   2457 C  CG2 . VAL A 1 314 ? -15.142 17.477  32.865 1.00 101.54 ? 610 VAL A CG2 1 
ATOM   2458 N  N   . ALA A 1 315 ? -13.907 19.065  36.924 1.00 88.54  ? 611 ALA A N   1 
ATOM   2459 C  CA  . ALA A 1 315 ? -14.038 19.559  38.281 1.00 95.33  ? 611 ALA A CA  1 
ATOM   2460 C  C   . ALA A 1 315 ? -13.219 20.819  38.491 1.00 106.91 ? 611 ALA A C   1 
ATOM   2461 O  O   . ALA A 1 315 ? -13.607 21.681  39.287 1.00 108.79 ? 611 ALA A O   1 
ATOM   2462 C  CB  . ALA A 1 315 ? -13.620 18.467  39.264 1.00 82.77  ? 611 ALA A CB  1 
ATOM   2463 N  N   . LYS A 1 316 ? -12.086 20.938  37.795 1.00 110.84 ? 612 LYS A N   1 
ATOM   2464 C  CA  . LYS A 1 316 ? -11.331 22.186  37.796 1.00 116.20 ? 612 LYS A CA  1 
ATOM   2465 C  C   . LYS A 1 316 ? -12.214 23.354  37.370 1.00 115.35 ? 612 LYS A C   1 
ATOM   2466 O  O   . LYS A 1 316 ? -12.406 24.316  38.124 1.00 114.27 ? 612 LYS A O   1 
ATOM   2467 C  CB  . LYS A 1 316 ? -10.116 22.068  36.868 1.00 119.58 ? 612 LYS A CB  1 
ATOM   2468 C  CG  . LYS A 1 316 ? -8.853  21.544  37.541 1.00 116.34 ? 612 LYS A CG  1 
ATOM   2469 C  CD  . LYS A 1 316 ? -7.599  22.034  36.811 1.00 116.46 ? 612 LYS A CD  1 
ATOM   2470 C  CE  . LYS A 1 316 ? -7.644  23.541  36.586 1.00 121.81 ? 612 LYS A CE  1 
ATOM   2471 N  NZ  . LYS A 1 316 ? -6.411  24.098  35.957 1.00 128.99 ? 612 LYS A NZ  1 
ATOM   2472 N  N   . LYS A 1 317 ? -12.774 23.268  36.157 1.00 108.58 ? 613 LYS A N   1 
ATOM   2473 C  CA  . LYS A 1 317 ? -13.552 24.363  35.580 1.00 112.23 ? 613 LYS A CA  1 
ATOM   2474 C  C   . LYS A 1 317 ? -14.818 24.668  36.367 1.00 109.70 ? 613 LYS A C   1 
ATOM   2475 O  O   . LYS A 1 317 ? -15.362 25.771  36.242 1.00 112.48 ? 613 LYS A O   1 
ATOM   2476 C  CB  . LYS A 1 317 ? -13.929 24.043  34.127 1.00 110.29 ? 613 LYS A CB  1 
ATOM   2477 C  CG  . LYS A 1 317 ? -12.922 24.484  33.096 1.00 113.87 ? 613 LYS A CG  1 
ATOM   2478 C  CD  . LYS A 1 317 ? -11.852 23.433  32.921 1.00 114.11 ? 613 LYS A CD  1 
ATOM   2479 C  CE  . LYS A 1 317 ? -10.826 23.918  31.910 1.00 123.86 ? 613 LYS A CE  1 
ATOM   2480 N  NZ  . LYS A 1 317 ? -10.185 22.803  31.149 1.00 124.28 ? 613 LYS A NZ  1 
ATOM   2481 N  N   . MET A 1 318 ? -15.320 23.708  37.142 1.00 114.29 ? 614 MET A N   1 
ATOM   2482 C  CA  . MET A 1 318 ? -16.397 23.987  38.079 1.00 115.44 ? 614 MET A CA  1 
ATOM   2483 C  C   . MET A 1 318 ? -15.894 24.650  39.346 1.00 128.35 ? 614 MET A C   1 
ATOM   2484 O  O   . MET A 1 318 ? -16.716 25.113  40.143 1.00 134.74 ? 614 MET A O   1 
ATOM   2485 C  CB  . MET A 1 318 ? -17.141 22.695  38.434 1.00 100.75 ? 614 MET A CB  1 
ATOM   2486 C  CG  . MET A 1 318 ? -17.908 22.120  37.258 1.00 111.87 ? 614 MET A CG  1 
ATOM   2487 S  SD  . MET A 1 318 ? -18.633 20.514  37.606 1.00 102.46 ? 614 MET A SD  1 
ATOM   2488 C  CE  . MET A 1 318 ? -19.628 20.900  39.049 1.00 96.92  ? 614 MET A CE  1 
ATOM   2489 N  N   . ASP A 1 319 ? -14.573 24.719  39.531 1.00 136.84 ? 615 ASP A N   1 
ATOM   2490 C  CA  . ASP A 1 319 ? -13.951 25.163  40.776 1.00 143.74 ? 615 ASP A CA  1 
ATOM   2491 C  C   . ASP A 1 319 ? -14.525 24.371  41.943 1.00 136.63 ? 615 ASP A C   1 
ATOM   2492 O  O   . ASP A 1 319 ? -15.395 24.861  42.670 1.00 137.02 ? 615 ASP A O   1 
ATOM   2493 C  CB  . ASP A 1 319 ? -14.139 26.670  40.978 1.00 156.84 ? 615 ASP A CB  1 
ATOM   2494 C  CG  . ASP A 1 319 ? -12.864 27.359  41.449 1.00 168.79 ? 615 ASP A CG  1 
ATOM   2495 O  OD1 . ASP A 1 319 ? -11.813 27.176  40.795 1.00 172.31 ? 615 ASP A OD1 1 
ATOM   2496 O  OD2 . ASP A 1 319 ? -12.916 28.087  42.466 1.00 173.17 ? 615 ASP A OD2 1 
ATOM   2497 N  N   . LEU A 1 320 ? -14.054 23.139  42.113 1.00 130.28 ? 616 LEU A N   1 
ATOM   2498 C  CA  . LEU A 1 320 ? -14.583 22.220  43.108 1.00 121.28 ? 616 LEU A CA  1 
ATOM   2499 C  C   . LEU A 1 320 ? -13.552 21.955  44.195 1.00 121.76 ? 616 LEU A C   1 
ATOM   2500 O  O   . LEU A 1 320 ? -12.341 22.002  43.956 1.00 123.72 ? 616 LEU A O   1 
ATOM   2501 C  CB  . LEU A 1 320 ? -15.005 20.894  42.465 1.00 107.34 ? 616 LEU A CB  1 
ATOM   2502 C  CG  . LEU A 1 320 ? -16.311 20.910  41.670 1.00 93.12  ? 616 LEU A CG  1 
ATOM   2503 C  CD1 . LEU A 1 320 ? -16.692 19.499  41.226 1.00 84.23  ? 616 LEU A CD1 1 
ATOM   2504 C  CD2 . LEU A 1 320 ? -17.428 21.539  42.496 1.00 96.76  ? 616 LEU A CD2 1 
ATOM   2505 N  N   . ASP A 1 321 ? -14.057 21.684  45.400 1.00 117.02 ? 617 ASP A N   1 
ATOM   2506 C  CA  . ASP A 1 321 ? -13.229 21.298  46.532 1.00 114.79 ? 617 ASP A CA  1 
ATOM   2507 C  C   . ASP A 1 321 ? -12.533 19.982  46.216 1.00 110.81 ? 617 ASP A C   1 
ATOM   2508 O  O   . ASP A 1 321 ? -13.081 18.909  46.490 1.00 95.87  ? 617 ASP A O   1 
ATOM   2509 C  CB  . ASP A 1 321 ? -14.096 21.161  47.786 1.00 115.63 ? 617 ASP A CB  1 
ATOM   2510 C  CG  . ASP A 1 321 ? -13.285 21.153  49.076 1.00 122.22 ? 617 ASP A CG  1 
ATOM   2511 O  OD1 . ASP A 1 321 ? -13.903 21.279  50.151 1.00 117.16 ? 617 ASP A OD1 1 
ATOM   2512 O  OD2 . ASP A 1 321 ? -12.043 21.040  49.022 1.00 127.22 ? 617 ASP A OD2 1 
ATOM   2513 N  N   . MET A 1 322 ? -11.339 20.039  45.629 1.00 119.27 ? 618 MET A N   1 
ATOM   2514 C  CA  . MET A 1 322 ? -10.670 18.829  45.166 1.00 126.64 ? 618 MET A CA  1 
ATOM   2515 C  C   . MET A 1 322 ? -9.561  18.363  46.101 1.00 134.40 ? 618 MET A C   1 
ATOM   2516 O  O   . MET A 1 322 ? -8.873  17.385  45.792 1.00 137.25 ? 618 MET A O   1 
ATOM   2517 C  CB  . MET A 1 322 ? -10.127 19.028  43.751 1.00 124.90 ? 618 MET A CB  1 
ATOM   2518 C  CG  . MET A 1 322 ? -11.195 18.909  42.676 1.00 122.75 ? 618 MET A CG  1 
ATOM   2519 S  SD  . MET A 1 322 ? -10.554 18.999  40.992 1.00 120.03 ? 618 MET A SD  1 
ATOM   2520 C  CE  . MET A 1 322 ? -9.387  17.639  40.964 1.00 118.48 ? 618 MET A CE  1 
ATOM   2521 N  N   . ARG A 1 323 ? -9.375  19.028  47.239 1.00 139.74 ? 619 ARG A N   1 
ATOM   2522 C  CA  . ARG A 1 323 ? -8.452  18.508  48.239 1.00 139.92 ? 619 ARG A CA  1 
ATOM   2523 C  C   . ARG A 1 323 ? -9.033  17.280  48.928 1.00 137.25 ? 619 ARG A C   1 
ATOM   2524 O  O   . ARG A 1 323 ? -8.310  16.321  49.228 1.00 140.57 ? 619 ARG A O   1 
ATOM   2525 C  CB  . ARG A 1 323 ? -8.126  19.594  49.262 1.00 142.55 ? 619 ARG A CB  1 
ATOM   2526 C  CG  . ARG A 1 323 ? -7.421  20.799  48.682 1.00 150.55 ? 619 ARG A CG  1 
ATOM   2527 C  CD  . ARG A 1 323 ? -7.791  22.063  49.442 1.00 160.07 ? 619 ARG A CD  1 
ATOM   2528 N  NE  . ARG A 1 323 ? -9.221  22.347  49.346 1.00 162.74 ? 619 ARG A NE  1 
ATOM   2529 C  CZ  . ARG A 1 323 ? -9.769  23.534  49.592 1.00 169.98 ? 619 ARG A CZ  1 
ATOM   2530 N  NH1 . ARG A 1 323 ? -9.010  24.562  49.945 1.00 176.77 ? 619 ARG A NH1 1 
ATOM   2531 N  NH2 . ARG A 1 323 ? -11.080 23.695  49.475 1.00 169.07 ? 619 ARG A NH2 1 
ATOM   2532 N  N   . LYS A 1 324 ? -10.339 17.285  49.170 1.00 129.02 ? 620 LYS A N   1 
ATOM   2533 C  CA  . LYS A 1 324 ? -10.996 16.259  49.964 1.00 115.01 ? 620 LYS A CA  1 
ATOM   2534 C  C   . LYS A 1 324 ? -11.687 15.253  49.052 1.00 107.61 ? 620 LYS A C   1 
ATOM   2535 O  O   . LYS A 1 324 ? -12.453 15.635  48.162 1.00 105.72 ? 620 LYS A O   1 
ATOM   2536 C  CB  . LYS A 1 324 ? -12.012 16.885  50.924 1.00 111.22 ? 620 LYS A CB  1 
ATOM   2537 C  CG  . LYS A 1 324 ? -11.416 17.497  52.185 1.00 113.62 ? 620 LYS A CG  1 
ATOM   2538 C  CD  . LYS A 1 324 ? -10.846 18.898  51.992 1.00 119.49 ? 620 LYS A CD  1 
ATOM   2539 C  CE  . LYS A 1 324 ? -10.253 19.430  53.307 1.00 123.19 ? 620 LYS A CE  1 
ATOM   2540 N  NZ  . LYS A 1 324 ? -9.740  20.823  53.175 1.00 126.36 ? 620 LYS A NZ  1 
ATOM   2541 N  N   . THR A 1 325 ? -11.400 13.969  49.274 1.00 98.72  ? 621 THR A N   1 
ATOM   2542 C  CA  . THR A 1 325 ? -12.188 12.905  48.662 1.00 95.71  ? 621 THR A CA  1 
ATOM   2543 C  C   . THR A 1 325 ? -13.670 13.048  48.993 1.00 91.10  ? 621 THR A C   1 
ATOM   2544 O  O   . THR A 1 325 ? -14.533 12.776  48.152 1.00 79.66  ? 621 THR A O   1 
ATOM   2545 C  CB  . THR A 1 325 ? -11.678 11.545  49.140 1.00 105.01 ? 621 THR A CB  1 
ATOM   2546 O  OG1 . THR A 1 325 ? -12.743 10.592  49.081 1.00 103.88 ? 621 THR A OG1 1 
ATOM   2547 C  CG2 . THR A 1 325 ? -11.165 11.632  50.591 1.00 117.78 ? 621 THR A CG2 1 
ATOM   2548 N  N   . SER A 1 326 ? -13.979 13.483  50.217 1.00 101.12 ? 622 SER A N   1 
ATOM   2549 C  CA  . SER A 1 326 ? -15.327 13.484  50.774 1.00 97.99  ? 622 SER A CA  1 
ATOM   2550 C  C   . SER A 1 326 ? -16.168 14.692  50.366 1.00 92.00  ? 622 SER A C   1 
ATOM   2551 O  O   . SER A 1 326 ? -17.325 14.787  50.787 1.00 84.35  ? 622 SER A O   1 
ATOM   2552 C  CB  . SER A 1 326 ? -15.248 13.394  52.302 1.00 93.67  ? 622 SER A CB  1 
ATOM   2553 O  OG  . SER A 1 326 ? -13.957 13.761  52.760 1.00 95.39  ? 622 SER A OG  1 
ATOM   2554 N  N   . SER A 1 327 ? -15.641 15.610  49.555 1.00 93.40  ? 623 SER A N   1 
ATOM   2555 C  CA  . SER A 1 327 ? -16.490 16.674  49.039 1.00 86.24  ? 623 SER A CA  1 
ATOM   2556 C  C   . SER A 1 327 ? -17.440 16.175  47.963 1.00 81.95  ? 623 SER A C   1 
ATOM   2557 O  O   . SER A 1 327 ? -18.324 16.928  47.533 1.00 77.58  ? 623 SER A O   1 
ATOM   2558 C  CB  . SER A 1 327 ? -15.629 17.812  48.484 1.00 95.33  ? 623 SER A CB  1 
ATOM   2559 O  OG  . SER A 1 327 ? -14.733 17.343  47.493 1.00 99.35  ? 623 SER A OG  1 
ATOM   2560 N  N   . LEU A 1 328 ? -17.272 14.924  47.530 1.00 79.73  ? 624 LEU A N   1 
ATOM   2561 C  CA  . LEU A 1 328 ? -17.970 14.366  46.378 1.00 71.17  ? 624 LEU A CA  1 
ATOM   2562 C  C   . LEU A 1 328 ? -17.776 15.242  45.144 1.00 79.33  ? 624 LEU A C   1 
ATOM   2563 O  O   . LEU A 1 328 ? -18.657 15.333  44.281 1.00 87.14  ? 624 LEU A O   1 
ATOM   2564 C  CB  . LEU A 1 328 ? -19.453 14.124  46.680 1.00 72.02  ? 624 LEU A CB  1 
ATOM   2565 C  CG  . LEU A 1 328 ? -19.628 13.196  47.907 1.00 81.56  ? 624 LEU A CG  1 
ATOM   2566 C  CD1 . LEU A 1 328 ? -21.008 12.548  47.963 1.00 76.63  ? 624 LEU A CD1 1 
ATOM   2567 C  CD2 . LEU A 1 328 ? -18.556 12.125  47.915 1.00 75.51  ? 624 LEU A CD2 1 
ATOM   2568 N  N   . TRP A 1 329 ? -16.598 15.870  45.051 1.00 77.28  ? 625 TRP A N   1 
ATOM   2569 C  CA  . TRP A 1 329 ? -16.249 16.597  43.834 1.00 80.90  ? 625 TRP A CA  1 
ATOM   2570 C  C   . TRP A 1 329 ? -16.261 15.667  42.636 1.00 81.88  ? 625 TRP A C   1 
ATOM   2571 O  O   . TRP A 1 329 ? -16.724 16.046  41.554 1.00 84.43  ? 625 TRP A O   1 
ATOM   2572 C  CB  . TRP A 1 329 ? -14.883 17.285  43.976 1.00 89.45  ? 625 TRP A CB  1 
ATOM   2573 C  CG  . TRP A 1 329 ? -13.668 16.372  43.959 1.00 93.31  ? 625 TRP A CG  1 
ATOM   2574 C  CD1 . TRP A 1 329 ? -13.013 15.877  45.040 1.00 99.74  ? 625 TRP A CD1 1 
ATOM   2575 C  CD2 . TRP A 1 329 ? -12.971 15.861  42.804 1.00 99.03  ? 625 TRP A CD2 1 
ATOM   2576 N  NE1 . TRP A 1 329 ? -11.954 15.096  44.644 1.00 98.13  ? 625 TRP A NE1 1 
ATOM   2577 C  CE2 . TRP A 1 329 ? -11.906 15.068  43.277 1.00 98.35  ? 625 TRP A CE2 1 
ATOM   2578 C  CE3 . TRP A 1 329 ? -13.141 16.003  41.422 1.00 95.01  ? 625 TRP A CE3 1 
ATOM   2579 C  CZ2 . TRP A 1 329 ? -11.021 14.411  42.421 1.00 93.43  ? 625 TRP A CZ2 1 
ATOM   2580 C  CZ3 . TRP A 1 329 ? -12.253 15.352  40.566 1.00 99.33  ? 625 TRP A CZ3 1 
ATOM   2581 C  CH2 . TRP A 1 329 ? -11.207 14.571  41.071 1.00 99.80  ? 625 TRP A CH2 1 
ATOM   2582 N  N   . LYS A 1 330 ? -15.779 14.433  42.808 1.00 82.75  ? 626 LYS A N   1 
ATOM   2583 C  CA  . LYS A 1 330 ? -15.882 13.464  41.721 1.00 75.62  ? 626 LYS A CA  1 
ATOM   2584 C  C   . LYS A 1 330 ? -17.338 13.228  41.352 1.00 69.62  ? 626 LYS A C   1 
ATOM   2585 O  O   . LYS A 1 330 ? -17.716 13.354  40.192 1.00 70.01  ? 626 LYS A O   1 
ATOM   2586 C  CB  . LYS A 1 330 ? -15.186 12.154  42.086 1.00 74.90  ? 626 LYS A CB  1 
ATOM   2587 C  CG  . LYS A 1 330 ? -13.745 12.099  41.614 1.00 84.81  ? 626 LYS A CG  1 
ATOM   2588 C  CD  . LYS A 1 330 ? -13.138 10.727  41.827 1.00 91.21  ? 626 LYS A CD  1 
ATOM   2589 C  CE  . LYS A 1 330 ? -11.628 10.758  41.608 1.00 91.23  ? 626 LYS A CE  1 
ATOM   2590 N  NZ  . LYS A 1 330 ? -10.964 9.506   42.098 1.00 83.37  ? 626 LYS A NZ  1 
ATOM   2591 N  N   . ASP A 1 331 ? -18.185 12.930  42.335 1.00 75.07  ? 627 ASP A N   1 
ATOM   2592 C  CA  . ASP A 1 331 ? -19.599 12.719  42.040 1.00 69.76  ? 627 ASP A CA  1 
ATOM   2593 C  C   . ASP A 1 331 ? -20.214 13.918  41.332 1.00 62.39  ? 627 ASP A C   1 
ATOM   2594 O  O   . ASP A 1 331 ? -21.029 13.755  40.424 1.00 60.95  ? 627 ASP A O   1 
ATOM   2595 C  CB  . ASP A 1 331 ? -20.350 12.426  43.330 1.00 63.23  ? 627 ASP A CB  1 
ATOM   2596 C  CG  . ASP A 1 331 ? -19.699 11.316  44.117 1.00 61.87  ? 627 ASP A CG  1 
ATOM   2597 O  OD1 . ASP A 1 331 ? -18.526 11.481  44.531 1.00 66.33  ? 627 ASP A OD1 1 
ATOM   2598 O  OD2 . ASP A 1 331 ? -20.363 10.283  44.299 1.00 64.75  ? 627 ASP A OD2 1 
ATOM   2599 N  N   . GLN A 1 332 ? -19.840 15.130  41.741 1.00 75.69  ? 628 GLN A N   1 
ATOM   2600 C  CA  . GLN A 1 332 ? -20.507 16.321  41.235 1.00 83.79  ? 628 GLN A CA  1 
ATOM   2601 C  C   . GLN A 1 332 ? -20.179 16.563  39.764 1.00 82.48  ? 628 GLN A C   1 
ATOM   2602 O  O   . GLN A 1 332 ? -21.069 16.893  38.966 1.00 79.37  ? 628 GLN A O   1 
ATOM   2603 C  CB  . GLN A 1 332 ? -20.116 17.513  42.103 1.00 96.39  ? 628 GLN A CB  1 
ATOM   2604 C  CG  . GLN A 1 332 ? -21.208 18.508  42.253 1.00 103.77 ? 628 GLN A CG  1 
ATOM   2605 C  CD  . GLN A 1 332 ? -21.094 19.286  43.542 1.00 111.71 ? 628 GLN A CD  1 
ATOM   2606 O  OE1 . GLN A 1 332 ? -20.016 19.391  44.139 1.00 107.37 ? 628 GLN A OE1 1 
ATOM   2607 N  NE2 . GLN A 1 332 ? -22.214 19.827  43.991 1.00 117.85 ? 628 GLN A NE2 1 
ATOM   2608 N  N   . ALA A 1 333 ? -18.913 16.380  39.376 1.00 85.54  ? 629 ALA A N   1 
ATOM   2609 C  CA  . ALA A 1 333 ? -18.536 16.575  37.984 1.00 86.85  ? 629 ALA A CA  1 
ATOM   2610 C  C   . ALA A 1 333 ? -19.049 15.450  37.105 1.00 91.17  ? 629 ALA A C   1 
ATOM   2611 O  O   . ALA A 1 333 ? -19.172 15.629  35.884 1.00 96.33  ? 629 ALA A O   1 
ATOM   2612 C  CB  . ALA A 1 333 ? -17.020 16.684  37.846 1.00 85.94  ? 629 ALA A CB  1 
ATOM   2613 N  N   . LEU A 1 334 ? -19.353 14.299  37.708 1.00 73.54  ? 630 LEU A N   1 
ATOM   2614 C  CA  . LEU A 1 334 ? -19.873 13.176  36.944 1.00 74.38  ? 630 LEU A CA  1 
ATOM   2615 C  C   . LEU A 1 334 ? -21.314 13.426  36.503 1.00 67.70  ? 630 LEU A C   1 
ATOM   2616 O  O   . LEU A 1 334 ? -21.720 12.991  35.418 1.00 78.51  ? 630 LEU A O   1 
ATOM   2617 C  CB  . LEU A 1 334 ? -19.788 11.895  37.782 1.00 64.54  ? 630 LEU A CB  1 
ATOM   2618 C  CG  . LEU A 1 334 ? -20.306 10.667  37.037 1.00 63.90  ? 630 LEU A CG  1 
ATOM   2619 C  CD1 . LEU A 1 334 ? -19.273 10.201  36.043 1.00 58.12  ? 630 LEU A CD1 1 
ATOM   2620 C  CD2 . LEU A 1 334 ? -20.662 9.545   37.987 1.00 67.70  ? 630 LEU A CD2 1 
ATOM   2621 N  N   . VAL A 1 335 ? -22.117 14.093  37.345 1.00 65.96  ? 631 VAL A N   1 
ATOM   2622 C  CA  . VAL A 1 335 ? -23.500 14.368  36.962 1.00 71.57  ? 631 VAL A CA  1 
ATOM   2623 C  C   . VAL A 1 335 ? -23.549 15.426  35.860 1.00 71.63  ? 631 VAL A C   1 
ATOM   2624 O  O   . VAL A 1 335 ? -24.330 15.309  34.908 1.00 74.54  ? 631 VAL A O   1 
ATOM   2625 C  CB  . VAL A 1 335 ? -24.347 14.799  38.167 1.00 77.60  ? 631 VAL A CB  1 
ATOM   2626 C  CG1 . VAL A 1 335 ? -25.717 15.294  37.665 1.00 64.55  ? 631 VAL A CG1 1 
ATOM   2627 C  CG2 . VAL A 1 335 ? -24.493 13.652  39.184 1.00 80.60  ? 631 VAL A CG2 1 
ATOM   2628 N  N   . GLU A 1 336 ? -22.736 16.480  35.979 1.00 74.18  ? 632 GLU A N   1 
ATOM   2629 C  CA  . GLU A 1 336 ? -22.727 17.521  34.946 1.00 86.25  ? 632 GLU A CA  1 
ATOM   2630 C  C   . GLU A 1 336 ? -22.342 16.959  33.582 1.00 80.42  ? 632 GLU A C   1 
ATOM   2631 O  O   . GLU A 1 336 ? -22.860 17.405  32.553 1.00 78.35  ? 632 GLU A O   1 
ATOM   2632 C  CB  . GLU A 1 336 ? -21.769 18.652  35.322 1.00 92.28  ? 632 GLU A CB  1 
ATOM   2633 C  CG  . GLU A 1 336 ? -22.021 19.284  36.672 1.00 101.15 ? 632 GLU A CG  1 
ATOM   2634 C  CD  . GLU A 1 336 ? -23.319 20.057  36.727 1.00 109.89 ? 632 GLU A CD  1 
ATOM   2635 O  OE1 . GLU A 1 336 ? -24.017 20.151  35.684 1.00 108.28 ? 632 GLU A OE1 1 
ATOM   2636 O  OE2 . GLU A 1 336 ? -23.634 20.579  37.817 1.00 112.48 ? 632 GLU A OE2 1 
ATOM   2637 N  N   . ILE A 1 337 ? -21.418 15.994  33.558 1.00 83.75  ? 633 ILE A N   1 
ATOM   2638 C  CA  . ILE A 1 337 ? -20.938 15.440  32.298 1.00 78.71  ? 633 ILE A CA  1 
ATOM   2639 C  C   . ILE A 1 337 ? -22.038 14.643  31.609 1.00 79.34  ? 633 ILE A C   1 
ATOM   2640 O  O   . ILE A 1 337 ? -22.171 14.685  30.386 1.00 88.75  ? 633 ILE A O   1 
ATOM   2641 C  CB  . ILE A 1 337 ? -19.669 14.596  32.531 1.00 68.82  ? 633 ILE A CB  1 
ATOM   2642 C  CG1 . ILE A 1 337 ? -18.476 15.511  32.805 1.00 64.87  ? 633 ILE A CG1 1 
ATOM   2643 C  CG2 . ILE A 1 337 ? -19.350 13.748  31.302 1.00 69.63  ? 633 ILE A CG2 1 
ATOM   2644 C  CD1 . ILE A 1 337 ? -17.329 14.766  33.473 1.00 81.43  ? 633 ILE A CD1 1 
ATOM   2645 N  N   . ASN A 1 338 ? -22.857 13.921  32.368 1.00 79.87  ? 634 ASN A N   1 
ATOM   2646 C  CA  . ASN A 1 338 ? -23.938 13.184  31.724 1.00 72.38  ? 634 ASN A CA  1 
ATOM   2647 C  C   . ASN A 1 338 ? -25.130 14.074  31.387 1.00 72.34  ? 634 ASN A C   1 
ATOM   2648 O  O   . ASN A 1 338 ? -25.931 13.706  30.524 1.00 68.88  ? 634 ASN A O   1 
ATOM   2649 C  CB  . ASN A 1 338 ? -24.362 11.992  32.596 1.00 67.71  ? 634 ASN A CB  1 
ATOM   2650 C  CG  . ASN A 1 338 ? -23.261 10.931  32.702 1.00 60.05  ? 634 ASN A CG  1 
ATOM   2651 O  OD1 . ASN A 1 338 ? -23.240 9.935   31.970 1.00 66.53  ? 634 ASN A OD1 1 
ATOM   2652 N  ND2 . ASN A 1 338 ? -22.319 11.172  33.597 1.00 58.58  ? 634 ASN A ND2 1 
ATOM   2653 N  N   . ILE A 1 339 ? -25.280 15.217  32.064 1.00 80.29  ? 635 ILE A N   1 
ATOM   2654 C  CA  . ILE A 1 339 ? -26.221 16.231  31.600 1.00 73.78  ? 635 ILE A CA  1 
ATOM   2655 C  C   . ILE A 1 339 ? -25.769 16.775  30.250 1.00 76.90  ? 635 ILE A C   1 
ATOM   2656 O  O   . ILE A 1 339 ? -26.597 17.056  29.378 1.00 76.96  ? 635 ILE A O   1 
ATOM   2657 C  CB  . ILE A 1 339 ? -26.363 17.357  32.652 1.00 69.13  ? 635 ILE A CB  1 
ATOM   2658 C  CG1 . ILE A 1 339 ? -26.992 16.832  33.953 1.00 72.80  ? 635 ILE A CG1 1 
ATOM   2659 C  CG2 . ILE A 1 339 ? -27.149 18.548  32.105 1.00 76.44  ? 635 ILE A CG2 1 
ATOM   2660 C  CD1 . ILE A 1 339 ? -27.210 17.906  34.988 1.00 74.26  ? 635 ILE A CD1 1 
ATOM   2661 N  N   . ALA A 1 340 ? -24.449 16.879  30.041 1.00 75.80  ? 636 ALA A N   1 
ATOM   2662 C  CA  . ALA A 1 340 ? -23.882 17.415  28.804 1.00 79.49  ? 636 ALA A CA  1 
ATOM   2663 C  C   . ALA A 1 340 ? -23.939 16.416  27.653 1.00 75.70  ? 636 ALA A C   1 
ATOM   2664 O  O   . ALA A 1 340 ? -24.157 16.815  26.499 1.00 64.19  ? 636 ALA A O   1 
ATOM   2665 C  CB  . ALA A 1 340 ? -22.442 17.845  29.047 1.00 80.45  ? 636 ALA A CB  1 
ATOM   2666 N  N   . VAL A 1 341 ? -23.678 15.133  27.923 1.00 68.81  ? 637 VAL A N   1 
ATOM   2667 C  CA  . VAL A 1 341 ? -23.874 14.127  26.882 1.00 63.08  ? 637 VAL A CA  1 
ATOM   2668 C  C   . VAL A 1 341 ? -25.323 14.157  26.421 1.00 67.86  ? 637 VAL A C   1 
ATOM   2669 O  O   . VAL A 1 341 ? -25.615 14.406  25.248 1.00 69.84  ? 637 VAL A O   1 
ATOM   2670 C  CB  . VAL A 1 341 ? -23.469 12.724  27.375 1.00 57.45  ? 637 VAL A CB  1 
ATOM   2671 C  CG1 . VAL A 1 341 ? -23.653 11.701  26.217 1.00 59.64  ? 637 VAL A CG1 1 
ATOM   2672 C  CG2 . VAL A 1 341 ? -22.022 12.726  27.824 1.00 62.40  ? 637 VAL A CG2 1 
ATOM   2673 N  N   . LEU A 1 342 ? -26.252 13.946  27.358 1.00 74.56  ? 638 LEU A N   1 
ATOM   2674 C  CA  . LEU A 1 342 ? -27.673 13.898  27.017 1.00 62.86  ? 638 LEU A CA  1 
ATOM   2675 C  C   . LEU A 1 342 ? -28.092 15.128  26.221 1.00 69.27  ? 638 LEU A C   1 
ATOM   2676 O  O   . LEU A 1 342 ? -28.578 15.019  25.083 1.00 68.41  ? 638 LEU A O   1 
ATOM   2677 C  CB  . LEU A 1 342 ? -28.507 13.756  28.300 1.00 73.47  ? 638 LEU A CB  1 
ATOM   2678 C  CG  . LEU A 1 342 ? -28.399 12.402  28.997 1.00 70.04  ? 638 LEU A CG  1 
ATOM   2679 C  CD1 . LEU A 1 342 ? -29.185 12.384  30.306 1.00 71.01  ? 638 LEU A CD1 1 
ATOM   2680 C  CD2 . LEU A 1 342 ? -28.870 11.319  28.068 1.00 57.85  ? 638 LEU A CD2 1 
ATOM   2681 N  N   . TYR A 1 343 ? -27.864 16.315  26.796 1.00 72.86  ? 639 TYR A N   1 
ATOM   2682 C  CA  . TYR A 1 343 ? -28.259 17.560  26.149 1.00 90.54  ? 639 TYR A CA  1 
ATOM   2683 C  C   . TYR A 1 343 ? -27.728 17.649  24.727 1.00 93.46  ? 639 TYR A C   1 
ATOM   2684 O  O   . TYR A 1 343 ? -28.472 17.964  23.793 1.00 86.13  ? 639 TYR A O   1 
ATOM   2685 C  CB  . TYR A 1 343 ? -27.761 18.747  26.965 1.00 98.08  ? 639 TYR A CB  1 
ATOM   2686 C  CG  . TYR A 1 343 ? -28.031 20.088  26.322 1.00 83.76  ? 639 TYR A CG  1 
ATOM   2687 C  CD1 . TYR A 1 343 ? -29.317 20.619  26.297 1.00 80.87  ? 639 TYR A CD1 1 
ATOM   2688 C  CD2 . TYR A 1 343 ? -26.999 20.840  25.782 1.00 94.22  ? 639 TYR A CD2 1 
ATOM   2689 C  CE1 . TYR A 1 343 ? -29.573 21.863  25.739 1.00 85.08  ? 639 TYR A CE1 1 
ATOM   2690 C  CE2 . TYR A 1 343 ? -27.246 22.087  25.210 1.00 97.51  ? 639 TYR A CE2 1 
ATOM   2691 C  CZ  . TYR A 1 343 ? -28.534 22.586  25.199 1.00 101.20 ? 639 TYR A CZ  1 
ATOM   2692 O  OH  . TYR A 1 343 ? -28.792 23.817  24.644 1.00 118.96 ? 639 TYR A OH  1 
ATOM   2693 N  N   . SER A 1 344 ? -26.436 17.379  24.549 1.00 95.13  ? 640 SER A N   1 
ATOM   2694 C  CA  . SER A 1 344 ? -25.823 17.540  23.239 1.00 81.99  ? 640 SER A CA  1 
ATOM   2695 C  C   . SER A 1 344 ? -26.474 16.615  22.214 1.00 85.59  ? 640 SER A C   1 
ATOM   2696 O  O   . SER A 1 344 ? -26.840 17.057  21.121 1.00 84.96  ? 640 SER A O   1 
ATOM   2697 C  CB  . SER A 1 344 ? -24.317 17.298  23.347 1.00 83.01  ? 640 SER A CB  1 
ATOM   2698 O  OG  . SER A 1 344 ? -23.760 18.056  24.417 1.00 94.42  ? 640 SER A OG  1 
ATOM   2699 N  N   . PHE A 1 345 ? -26.668 15.332  22.568 1.00 67.68  ? 641 PHE A N   1 
ATOM   2700 C  CA  . PHE A 1 345 ? -27.228 14.365  21.616 1.00 63.30  ? 641 PHE A CA  1 
ATOM   2701 C  C   . PHE A 1 345 ? -28.647 14.739  21.194 1.00 73.35  ? 641 PHE A C   1 
ATOM   2702 O  O   . PHE A 1 345 ? -29.029 14.533  20.035 1.00 80.41  ? 641 PHE A O   1 
ATOM   2703 C  CB  . PHE A 1 345 ? -27.224 12.951  22.210 1.00 58.46  ? 641 PHE A CB  1 
ATOM   2704 C  CG  . PHE A 1 345 ? -25.996 12.141  21.878 1.00 57.08  ? 641 PHE A CG  1 
ATOM   2705 C  CD1 . PHE A 1 345 ? -24.741 12.535  22.330 1.00 68.44  ? 641 PHE A CD1 1 
ATOM   2706 C  CD2 . PHE A 1 345 ? -26.102 10.964  21.123 1.00 49.66  ? 641 PHE A CD2 1 
ATOM   2707 C  CE1 . PHE A 1 345 ? -23.608 11.780  22.040 1.00 65.88  ? 641 PHE A CE1 1 
ATOM   2708 C  CE2 . PHE A 1 345 ? -24.975 10.185  20.863 1.00 47.88  ? 641 PHE A CE2 1 
ATOM   2709 C  CZ  . PHE A 1 345 ? -23.721 10.607  21.300 1.00 52.63  ? 641 PHE A CZ  1 
ATOM   2710 N  N   . GLN A 1 346 ? -29.442 15.294  22.120 1.00 67.18  ? 642 GLN A N   1 
ATOM   2711 C  CA  . GLN A 1 346 ? -30.843 15.620  21.847 1.00 78.56  ? 642 GLN A CA  1 
ATOM   2712 C  C   . GLN A 1 346 ? -31.015 16.956  21.138 1.00 84.81  ? 642 GLN A C   1 
ATOM   2713 O  O   . GLN A 1 346 ? -31.971 17.116  20.375 1.00 84.49  ? 642 GLN A O   1 
ATOM   2714 C  CB  . GLN A 1 346 ? -31.656 15.651  23.145 1.00 85.39  ? 642 GLN A CB  1 
ATOM   2715 C  CG  . GLN A 1 346 ? -31.654 14.339  23.958 1.00 76.96  ? 642 GLN A CG  1 
ATOM   2716 C  CD  . GLN A 1 346 ? -31.751 14.572  25.476 1.00 77.65  ? 642 GLN A CD  1 
ATOM   2717 O  OE1 . GLN A 1 346 ? -31.455 15.660  25.966 1.00 75.78  ? 642 GLN A OE1 1 
ATOM   2718 N  NE2 . GLN A 1 346 ? -32.158 13.532  26.220 1.00 74.75  ? 642 GLN A NE2 1 
ATOM   2719 N  N   . SER A 1 347 ? -30.162 17.946  21.423 1.00 81.02  ? 643 SER A N   1 
ATOM   2720 C  CA  . SER A 1 347 ? -30.226 19.196  20.669 1.00 87.60  ? 643 SER A CA  1 
ATOM   2721 C  C   . SER A 1 347 ? -29.812 18.993  19.215 1.00 87.70  ? 643 SER A C   1 
ATOM   2722 O  O   . SER A 1 347 ? -30.095 19.849  18.363 1.00 90.59  ? 643 SER A O   1 
ATOM   2723 C  CB  . SER A 1 347 ? -29.342 20.266  21.312 1.00 87.48  ? 643 SER A CB  1 
ATOM   2724 O  OG  . SER A 1 347 ? -29.659 20.464  22.689 1.00 92.46  ? 643 SER A OG  1 
ATOM   2725 N  N   . ASP A 1 348 ? -29.145 17.881  18.915 1.00 84.17  ? 644 ASP A N   1 
ATOM   2726 C  CA  . ASP A 1 348 ? -28.792 17.514  17.552 1.00 77.10  ? 644 ASP A CA  1 
ATOM   2727 C  C   . ASP A 1 348 ? -29.741 16.484  16.954 1.00 85.14  ? 644 ASP A C   1 
ATOM   2728 O  O   . ASP A 1 348 ? -29.562 16.098  15.790 1.00 78.79  ? 644 ASP A O   1 
ATOM   2729 C  CB  . ASP A 1 348 ? -27.358 16.981  17.504 1.00 74.73  ? 644 ASP A CB  1 
ATOM   2730 C  CG  . ASP A 1 348 ? -26.315 18.081  17.624 1.00 80.30  ? 644 ASP A CG  1 
ATOM   2731 O  OD1 . ASP A 1 348 ? -26.692 19.277  17.630 1.00 82.05  ? 644 ASP A OD1 1 
ATOM   2732 O  OD2 . ASP A 1 348 ? -25.114 17.751  17.707 1.00 78.43  ? 644 ASP A OD2 1 
ATOM   2733 N  N   . LYS A 1 349 ? -30.731 16.023  17.725 1.00 76.97  ? 645 LYS A N   1 
ATOM   2734 C  CA  . LYS A 1 349 ? -31.760 15.102  17.246 1.00 85.75  ? 645 LYS A CA  1 
ATOM   2735 C  C   . LYS A 1 349 ? -31.191 13.716  16.975 1.00 82.32  ? 645 LYS A C   1 
ATOM   2736 O  O   . LYS A 1 349 ? -31.723 12.960  16.157 1.00 79.36  ? 645 LYS A O   1 
ATOM   2737 C  CB  . LYS A 1 349 ? -32.455 15.658  15.996 1.00 98.59  ? 645 LYS A CB  1 
ATOM   2738 C  CG  . LYS A 1 349 ? -33.957 15.476  15.981 1.00 110.34 ? 645 LYS A CG  1 
ATOM   2739 C  CD  . LYS A 1 349 ? -34.551 15.608  17.375 1.00 118.16 ? 645 LYS A CD  1 
ATOM   2740 C  CE  . LYS A 1 349 ? -36.054 15.828  17.301 1.00 126.68 ? 645 LYS A CE  1 
ATOM   2741 N  NZ  . LYS A 1 349 ? -36.696 15.016  16.223 1.00 124.80 ? 645 LYS A NZ  1 
ATOM   2742 N  N   . VAL A 1 350 ? -30.097 13.396  17.650 1.00 76.64  ? 646 VAL A N   1 
ATOM   2743 C  CA  . VAL A 1 350 ? -29.468 12.084  17.590 1.00 69.49  ? 646 VAL A CA  1 
ATOM   2744 C  C   . VAL A 1 350 ? -29.995 11.253  18.751 1.00 68.60  ? 646 VAL A C   1 
ATOM   2745 O  O   . VAL A 1 350 ? -29.972 11.704  19.905 1.00 73.17  ? 646 VAL A O   1 
ATOM   2746 C  CB  . VAL A 1 350 ? -27.936 12.208  17.657 1.00 65.13  ? 646 VAL A CB  1 
ATOM   2747 C  CG1 . VAL A 1 350 ? -27.266 10.849  17.500 1.00 57.86  ? 646 VAL A CG1 1 
ATOM   2748 C  CG2 . VAL A 1 350 ? -27.435 13.219  16.634 1.00 55.20  ? 646 VAL A CG2 1 
ATOM   2749 N  N   . THR A 1 351 ? -30.431 10.027  18.452 1.00 61.04  ? 647 THR A N   1 
ATOM   2750 C  CA  . THR A 1 351 ? -31.103 9.157   19.420 1.00 65.93  ? 647 THR A CA  1 
ATOM   2751 C  C   . THR A 1 351 ? -30.182 8.821   20.593 1.00 65.27  ? 647 THR A C   1 
ATOM   2752 O  O   . THR A 1 351 ? -29.130 8.196   20.408 1.00 71.29  ? 647 THR A O   1 
ATOM   2753 C  CB  . THR A 1 351 ? -31.563 7.858   18.748 1.00 68.32  ? 647 THR A CB  1 
ATOM   2754 O  OG1 . THR A 1 351 ? -32.186 8.130   17.486 1.00 69.53  ? 647 THR A OG1 1 
ATOM   2755 C  CG2 . THR A 1 351 ? -32.543 7.079   19.662 1.00 62.19  ? 647 THR A CG2 1 
ATOM   2756 N  N   . ILE A 1 352 ? -30.590 9.222   21.801 1.00 66.98  ? 648 ILE A N   1 
ATOM   2757 C  CA  . ILE A 1 352 ? -29.939 8.822   23.048 1.00 62.89  ? 648 ILE A CA  1 
ATOM   2758 C  C   . ILE A 1 352 ? -31.019 8.667   24.116 1.00 62.54  ? 648 ILE A C   1 
ATOM   2759 O  O   . ILE A 1 352 ? -32.066 9.318   24.064 1.00 60.33  ? 648 ILE A O   1 
ATOM   2760 C  CB  . ILE A 1 352 ? -28.859 9.837   23.498 1.00 58.07  ? 648 ILE A CB  1 
ATOM   2761 C  CG1 . ILE A 1 352 ? -27.865 9.180   24.458 1.00 56.36  ? 648 ILE A CG1 1 
ATOM   2762 C  CG2 . ILE A 1 352 ? -29.504 11.037  24.133 1.00 49.20  ? 648 ILE A CG2 1 
ATOM   2763 C  CD1 . ILE A 1 352 ? -26.569 9.939   24.572 1.00 57.71  ? 648 ILE A CD1 1 
ATOM   2764 N  N   . VAL A 1 353 ? -30.778 7.779   25.078 1.00 62.73  ? 649 VAL A N   1 
ATOM   2765 C  CA  . VAL A 1 353 ? -31.739 7.510   26.144 1.00 59.25  ? 649 VAL A CA  1 
ATOM   2766 C  C   . VAL A 1 353 ? -31.016 7.672   27.476 1.00 57.55  ? 649 VAL A C   1 
ATOM   2767 O  O   . VAL A 1 353 ? -29.824 7.368   27.594 1.00 50.68  ? 649 VAL A O   1 
ATOM   2768 C  CB  . VAL A 1 353 ? -32.378 6.103   26.001 1.00 68.80  ? 649 VAL A CB  1 
ATOM   2769 C  CG1 . VAL A 1 353 ? -31.452 5.018   26.504 1.00 66.42  ? 649 VAL A CG1 1 
ATOM   2770 C  CG2 . VAL A 1 353 ? -33.740 6.023   26.702 1.00 62.84  ? 649 VAL A CG2 1 
ATOM   2771 N  N   . ASP A 1 354 ? -31.716 8.204   28.463 1.00 63.25  ? 650 ASP A N   1 
ATOM   2772 C  CA  . ASP A 1 354 ? -31.081 8.453   29.740 1.00 58.83  ? 650 ASP A CA  1 
ATOM   2773 C  C   . ASP A 1 354 ? -31.284 7.228   30.637 1.00 66.65  ? 650 ASP A C   1 
ATOM   2774 O  O   . ASP A 1 354 ? -32.201 6.427   30.432 1.00 68.06  ? 650 ASP A O   1 
ATOM   2775 C  CB  . ASP A 1 354 ? -31.634 9.736   30.356 1.00 52.89  ? 650 ASP A CB  1 
ATOM   2776 C  CG  . ASP A 1 354 ? -33.071 9.597   30.819 1.00 74.05  ? 650 ASP A CG  1 
ATOM   2777 O  OD1 . ASP A 1 354 ? -33.981 10.243  30.266 1.00 82.78  ? 650 ASP A OD1 1 
ATOM   2778 O  OD2 . ASP A 1 354 ? -33.296 8.823   31.760 1.00 81.47  ? 650 ASP A OD2 1 
ATOM   2779 N  N   . HIS A 1 355 ? -30.383 7.057   31.605 1.00 66.98  ? 651 HIS A N   1 
ATOM   2780 C  CA  . HIS A 1 355 ? -30.391 5.832   32.412 1.00 58.88  ? 651 HIS A CA  1 
ATOM   2781 C  C   . HIS A 1 355 ? -31.684 5.650   33.214 1.00 58.47  ? 651 HIS A C   1 
ATOM   2782 O  O   . HIS A 1 355 ? -32.022 4.516   33.569 1.00 62.41  ? 651 HIS A O   1 
ATOM   2783 C  CB  . HIS A 1 355 ? -29.167 5.798   33.333 1.00 62.74  ? 651 HIS A CB  1 
ATOM   2784 C  CG  . HIS A 1 355 ? -28.996 7.029   34.176 1.00 53.54  ? 651 HIS A CG  1 
ATOM   2785 N  ND1 . HIS A 1 355 ? -28.694 8.261   33.638 1.00 53.13  ? 651 HIS A ND1 1 
ATOM   2786 C  CD2 . HIS A 1 355 ? -29.043 7.208   35.519 1.00 54.93  ? 651 HIS A CD2 1 
ATOM   2787 C  CE1 . HIS A 1 355 ? -28.586 9.153   34.608 1.00 68.89  ? 651 HIS A CE1 1 
ATOM   2788 N  NE2 . HIS A 1 355 ? -28.802 8.544   35.760 1.00 55.38  ? 651 HIS A NE2 1 
ATOM   2789 N  N   . HIS A 1 356 ? -32.423 6.729   33.489 1.00 68.71  ? 652 HIS A N   1 
ATOM   2790 C  CA  . HIS A 1 356 ? -33.731 6.613   34.133 1.00 70.55  ? 652 HIS A CA  1 
ATOM   2791 C  C   . HIS A 1 356 ? -34.765 5.998   33.199 1.00 68.82  ? 652 HIS A C   1 
ATOM   2792 O  O   . HIS A 1 356 ? -35.463 5.043   33.562 1.00 56.20  ? 652 HIS A O   1 
ATOM   2793 C  CB  . HIS A 1 356 ? -34.188 7.990   34.598 1.00 71.83  ? 652 HIS A CB  1 
ATOM   2794 C  CG  . HIS A 1 356 ? -33.245 8.612   35.573 1.00 79.27  ? 652 HIS A CG  1 
ATOM   2795 N  ND1 . HIS A 1 356 ? -33.252 8.291   36.910 1.00 75.22  ? 652 HIS A ND1 1 
ATOM   2796 C  CD2 . HIS A 1 356 ? -32.226 9.486   35.399 1.00 79.13  ? 652 HIS A CD2 1 
ATOM   2797 C  CE1 . HIS A 1 356 ? -32.296 8.961   37.523 1.00 80.37  ? 652 HIS A CE1 1 
ATOM   2798 N  NE2 . HIS A 1 356 ? -31.652 9.685   36.627 1.00 70.24  ? 652 HIS A NE2 1 
ATOM   2799 N  N   . SER A 1 357 ? -34.880 6.538   31.988 1.00 77.59  ? 653 SER A N   1 
ATOM   2800 C  CA  . SER A 1 357 ? -35.895 6.056   31.061 1.00 78.54  ? 653 SER A CA  1 
ATOM   2801 C  C   . SER A 1 357 ? -35.563 4.676   30.511 1.00 57.72  ? 653 SER A C   1 
ATOM   2802 O  O   . SER A 1 357 ? -36.472 3.943   30.107 1.00 66.74  ? 653 SER A O   1 
ATOM   2803 C  CB  . SER A 1 357 ? -36.077 7.047   29.916 1.00 78.61  ? 653 SER A CB  1 
ATOM   2804 O  OG  . SER A 1 357 ? -37.160 6.640   29.108 1.00 82.45  ? 653 SER A OG  1 
ATOM   2805 N  N   . ALA A 1 358 ? -34.279 4.309   30.471 1.00 52.64  ? 654 ALA A N   1 
ATOM   2806 C  CA  . ALA A 1 358 ? -33.901 2.982   29.979 1.00 56.20  ? 654 ALA A CA  1 
ATOM   2807 C  C   . ALA A 1 358 ? -34.102 1.905   31.044 1.00 59.74  ? 654 ALA A C   1 
ATOM   2808 O  O   . ALA A 1 358 ? -34.494 0.773   30.729 1.00 59.00  ? 654 ALA A O   1 
ATOM   2809 C  CB  . ALA A 1 358 ? -32.444 2.980   29.514 1.00 56.39  ? 654 ALA A CB  1 
ATOM   2810 N  N   . THR A 1 359 ? -33.815 2.213   32.304 1.00 47.23  ? 655 THR A N   1 
ATOM   2811 C  CA  . THR A 1 359 ? -34.073 1.203   33.319 1.00 53.73  ? 655 THR A CA  1 
ATOM   2812 C  C   . THR A 1 359 ? -35.564 1.015   33.519 1.00 58.83  ? 655 THR A C   1 
ATOM   2813 O  O   . THR A 1 359 ? -36.020 -0.107  33.770 1.00 57.91  ? 655 THR A O   1 
ATOM   2814 C  CB  . THR A 1 359 ? -33.388 1.582   34.610 1.00 54.25  ? 655 THR A CB  1 
ATOM   2815 O  OG1 . THR A 1 359 ? -33.795 2.905   34.985 1.00 58.03  ? 655 THR A OG1 1 
ATOM   2816 C  CG2 . THR A 1 359 ? -31.914 1.573   34.375 1.00 55.45  ? 655 THR A CG2 1 
ATOM   2817 N  N   . GLU A 1 360 ? -36.339 2.090   33.368 1.00 60.10  ? 656 GLU A N   1 
ATOM   2818 C  CA  . GLU A 1 360 ? -37.785 1.969   33.495 1.00 68.81  ? 656 GLU A CA  1 
ATOM   2819 C  C   . GLU A 1 360 ? -38.329 1.042   32.420 1.00 76.34  ? 656 GLU A C   1 
ATOM   2820 O  O   . GLU A 1 360 ? -39.122 0.138   32.701 1.00 89.07  ? 656 GLU A O   1 
ATOM   2821 C  CB  . GLU A 1 360 ? -38.440 3.349   33.409 1.00 69.57  ? 656 GLU A CB  1 
ATOM   2822 C  CG  . GLU A 1 360 ? -39.731 3.480   34.187 1.00 79.33  ? 656 GLU A CG  1 
ATOM   2823 C  CD  . GLU A 1 360 ? -40.818 4.204   33.419 1.00 96.53  ? 656 GLU A CD  1 
ATOM   2824 O  OE1 . GLU A 1 360 ? -41.772 3.527   32.973 1.00 109.67 ? 656 GLU A OE1 1 
ATOM   2825 O  OE2 . GLU A 1 360 ? -40.722 5.442   33.255 1.00 94.70  ? 656 GLU A OE2 1 
ATOM   2826 N  N   . SER A 1 361 ? -37.892 1.248   31.179 1.00 69.53  ? 657 SER A N   1 
ATOM   2827 C  CA  A SER A 1 361 ? -38.365 0.400   30.093 0.36 63.66  ? 657 SER A CA  1 
ATOM   2828 C  CA  B SER A 1 361 ? -38.330 0.404   30.070 0.64 64.01  ? 657 SER A CA  1 
ATOM   2829 C  C   . SER A 1 361 ? -37.954 -1.052  30.305 1.00 65.48  ? 657 SER A C   1 
ATOM   2830 O  O   . SER A 1 361 ? -38.714 -1.966  29.968 1.00 76.37  ? 657 SER A O   1 
ATOM   2831 C  CB  A SER A 1 361 ? -37.850 0.935   28.761 0.36 53.13  ? 657 SER A CB  1 
ATOM   2832 C  CB  B SER A 1 361 ? -37.697 0.896   28.776 0.64 52.91  ? 657 SER A CB  1 
ATOM   2833 O  OG  A SER A 1 361 ? -38.197 2.300   28.634 0.36 50.07  ? 657 SER A OG  1 
ATOM   2834 O  OG  B SER A 1 361 ? -36.355 0.429   28.705 0.64 48.25  ? 657 SER A OG  1 
ATOM   2835 N  N   . PHE A 1 362 ? -36.774 -1.285  30.881 1.00 63.04  ? 658 PHE A N   1 
ATOM   2836 C  CA  . PHE A 1 362 ? -36.340 -2.654  31.119 1.00 62.15  ? 658 PHE A CA  1 
ATOM   2837 C  C   . PHE A 1 362 ? -37.243 -3.365  32.121 1.00 61.20  ? 658 PHE A C   1 
ATOM   2838 O  O   . PHE A 1 362 ? -37.661 -4.503  31.885 1.00 71.28  ? 658 PHE A O   1 
ATOM   2839 C  CB  . PHE A 1 362 ? -34.888 -2.694  31.574 1.00 56.44  ? 658 PHE A CB  1 
ATOM   2840 C  CG  . PHE A 1 362 ? -34.354 -4.089  31.670 1.00 59.79  ? 658 PHE A CG  1 
ATOM   2841 C  CD1 . PHE A 1 362 ? -34.221 -4.866  30.528 1.00 57.95  ? 658 PHE A CD1 1 
ATOM   2842 C  CD2 . PHE A 1 362 ? -34.036 -4.649  32.904 1.00 68.61  ? 658 PHE A CD2 1 
ATOM   2843 C  CE1 . PHE A 1 362 ? -33.750 -6.164  30.606 1.00 59.56  ? 658 PHE A CE1 1 
ATOM   2844 C  CE2 . PHE A 1 362 ? -33.562 -5.947  32.989 1.00 66.61  ? 658 PHE A CE2 1 
ATOM   2845 C  CZ  . PHE A 1 362 ? -33.420 -6.712  31.834 1.00 61.14  ? 658 PHE A CZ  1 
ATOM   2846 N  N   . ILE A 1 363 ? -37.548 -2.723  33.256 1.00 67.51  ? 659 ILE A N   1 
ATOM   2847 C  CA  . ILE A 1 363 ? -38.576 -3.269  34.146 1.00 68.55  ? 659 ILE A CA  1 
ATOM   2848 C  C   . ILE A 1 363 ? -39.852 -3.521  33.355 1.00 76.29  ? 659 ILE A C   1 
ATOM   2849 O  O   . ILE A 1 363 ? -40.464 -4.593  33.435 1.00 79.10  ? 659 ILE A O   1 
ATOM   2850 C  CB  . ILE A 1 363 ? -38.832 -2.319  35.333 1.00 69.42  ? 659 ILE A CB  1 
ATOM   2851 C  CG1 . ILE A 1 363 ? -37.593 -2.196  36.221 1.00 50.79  ? 659 ILE A CG1 1 
ATOM   2852 C  CG2 . ILE A 1 363 ? -40.018 -2.802  36.157 1.00 70.88  ? 659 ILE A CG2 1 
ATOM   2853 C  CD1 . ILE A 1 363 ? -37.470 -3.299  37.244 1.00 65.24  ? 659 ILE A CD1 1 
ATOM   2854 N  N   . LYS A 1 364 ? -40.240 -2.538  32.542 1.00 81.43  ? 660 LYS A N   1 
ATOM   2855 C  CA  . LYS A 1 364 ? -41.401 -2.683  31.677 1.00 85.66  ? 660 LYS A CA  1 
ATOM   2856 C  C   . LYS A 1 364 ? -41.243 -3.882  30.750 1.00 81.12  ? 660 LYS A C   1 
ATOM   2857 O  O   . LYS A 1 364 ? -42.162 -4.697  30.611 1.00 76.54  ? 660 LYS A O   1 
ATOM   2858 C  CB  . LYS A 1 364 ? -41.603 -1.398  30.875 1.00 90.70  ? 660 LYS A CB  1 
ATOM   2859 C  CG  . LYS A 1 364 ? -42.972 -1.267  30.254 1.00 99.41  ? 660 LYS A CG  1 
ATOM   2860 C  CD  . LYS A 1 364 ? -44.024 -1.038  31.326 1.00 102.31 ? 660 LYS A CD  1 
ATOM   2861 C  CE  . LYS A 1 364 ? -45.364 -0.732  30.691 1.00 109.21 ? 660 LYS A CE  1 
ATOM   2862 N  NZ  . LYS A 1 364 ? -45.234 0.364   29.688 1.00 109.88 ? 660 LYS A NZ  1 
ATOM   2863 N  N   . HIS A 1 365 ? -40.080 -4.004  30.101 1.00 82.13  ? 661 HIS A N   1 
ATOM   2864 C  CA  . HIS A 1 365 ? -39.811 -5.179  29.269 1.00 82.32  ? 661 HIS A CA  1 
ATOM   2865 C  C   . HIS A 1 365 ? -39.848 -6.447  30.101 1.00 84.75  ? 661 HIS A C   1 
ATOM   2866 O  O   . HIS A 1 365 ? -40.423 -7.459  29.687 1.00 94.82  ? 661 HIS A O   1 
ATOM   2867 C  CB  . HIS A 1 365 ? -38.452 -5.044  28.573 1.00 75.60  ? 661 HIS A CB  1 
ATOM   2868 C  CG  . HIS A 1 365 ? -37.969 -6.299  27.894 1.00 72.76  ? 661 HIS A CG  1 
ATOM   2869 N  ND1 . HIS A 1 365 ? -36.657 -6.722  27.968 1.00 68.64  ? 661 HIS A ND1 1 
ATOM   2870 C  CD2 . HIS A 1 365 ? -38.602 -7.190  27.096 1.00 68.66  ? 661 HIS A CD2 1 
ATOM   2871 C  CE1 . HIS A 1 365 ? -36.506 -7.833  27.270 1.00 62.92  ? 661 HIS A CE1 1 
ATOM   2872 N  NE2 . HIS A 1 365 ? -37.670 -8.136  26.727 1.00 69.40  ? 661 HIS A NE2 1 
ATOM   2873 N  N   . MET A 1 366 ? -39.251 -6.404  31.285 1.00 76.51  ? 662 MET A N   1 
ATOM   2874 C  CA  . MET A 1 366 ? -39.202 -7.586  32.134 1.00 77.81  ? 662 MET A CA  1 
ATOM   2875 C  C   . MET A 1 366 ? -40.590 -8.142  32.444 1.00 70.53  ? 662 MET A C   1 
ATOM   2876 O  O   . MET A 1 366 ? -40.754 -9.366  32.512 1.00 69.60  ? 662 MET A O   1 
ATOM   2877 C  CB  . MET A 1 366 ? -38.460 -7.257  33.420 1.00 79.93  ? 662 MET A CB  1 
ATOM   2878 C  CG  . MET A 1 366 ? -37.352 -8.230  33.730 1.00 77.20  ? 662 MET A CG  1 
ATOM   2879 S  SD  . MET A 1 366 ? -36.371 -7.624  35.100 1.00 71.09  ? 662 MET A SD  1 
ATOM   2880 C  CE  . MET A 1 366 ? -35.748 -9.180  35.746 1.00 80.07  ? 662 MET A CE  1 
ATOM   2881 N  N   . GLU A 1 367 ? -41.603 -7.283  32.615 1.00 65.82  ? 663 GLU A N   1 
ATOM   2882 C  CA  . GLU A 1 367 ? -42.957 -7.783  32.852 1.00 75.85  ? 663 GLU A CA  1 
ATOM   2883 C  C   . GLU A 1 367 ? -43.421 -8.666  31.705 1.00 86.45  ? 663 GLU A C   1 
ATOM   2884 O  O   . GLU A 1 367 ? -43.808 -9.823  31.906 1.00 97.02  ? 663 GLU A O   1 
ATOM   2885 C  CB  . GLU A 1 367 ? -43.941 -6.631  33.027 1.00 85.56  ? 663 GLU A CB  1 
ATOM   2886 C  CG  . GLU A 1 367 ? -43.475 -5.499  33.901 1.00 95.97  ? 663 GLU A CG  1 
ATOM   2887 C  CD  . GLU A 1 367 ? -44.236 -4.231  33.584 1.00 104.55 ? 663 GLU A CD  1 
ATOM   2888 O  OE1 . GLU A 1 367 ? -44.670 -4.087  32.414 1.00 108.35 ? 663 GLU A OE1 1 
ATOM   2889 O  OE2 . GLU A 1 367 ? -44.411 -3.391  34.493 1.00 100.21 ? 663 GLU A OE2 1 
ATOM   2890 N  N   . ASN A 1 368 ? -43.403 -8.114  30.486 1.00 86.16  ? 664 ASN A N   1 
ATOM   2891 C  CA  . ASN A 1 368 ? -43.916 -8.811  29.311 1.00 77.61  ? 664 ASN A CA  1 
ATOM   2892 C  C   . ASN A 1 368 ? -43.211 -10.143 29.086 1.00 77.25  ? 664 ASN A C   1 
ATOM   2893 O  O   . ASN A 1 368 ? -43.855 -11.131 28.711 1.00 83.17  ? 664 ASN A O   1 
ATOM   2894 C  CB  . ASN A 1 368 ? -43.770 -7.899  28.093 1.00 77.13  ? 664 ASN A CB  1 
ATOM   2895 C  CG  . ASN A 1 368 ? -44.333 -6.507  28.339 1.00 80.42  ? 664 ASN A CG  1 
ATOM   2896 O  OD1 . ASN A 1 368 ? -45.436 -6.355  28.867 1.00 91.31  ? 664 ASN A OD1 1 
ATOM   2897 N  ND2 . ASN A 1 368 ? -43.568 -5.484  27.974 1.00 76.89  ? 664 ASN A ND2 1 
ATOM   2898 N  N   . GLU A 1 369 ? -41.895 -10.190 29.317 1.00 75.91  ? 665 GLU A N   1 
ATOM   2899 C  CA  . GLU A 1 369 ? -41.150 -11.442 29.227 1.00 76.99  ? 665 GLU A CA  1 
ATOM   2900 C  C   . GLU A 1 369 ? -41.662 -12.491 30.214 1.00 92.77  ? 665 GLU A C   1 
ATOM   2901 O  O   . GLU A 1 369 ? -41.798 -13.664 29.852 1.00 104.14 ? 665 GLU A O   1 
ATOM   2902 C  CB  . GLU A 1 369 ? -39.665 -11.181 29.461 1.00 76.67  ? 665 GLU A CB  1 
ATOM   2903 C  CG  . GLU A 1 369 ? -38.976 -10.482 28.331 1.00 81.02  ? 665 GLU A CG  1 
ATOM   2904 C  CD  . GLU A 1 369 ? -38.772 -11.396 27.156 1.00 83.25  ? 665 GLU A CD  1 
ATOM   2905 O  OE1 . GLU A 1 369 ? -38.002 -12.370 27.312 1.00 100.98 ? 665 GLU A OE1 1 
ATOM   2906 O  OE2 . GLU A 1 369 ? -39.401 -11.158 26.107 1.00 69.01  ? 665 GLU A OE2 1 
ATOM   2907 N  N   . TYR A 1 370 ? -41.921 -12.110 31.473 1.00 92.37  ? 666 TYR A N   1 
ATOM   2908 C  CA  . TYR A 1 370 ? -42.437 -13.096 32.426 1.00 92.18  ? 666 TYR A CA  1 
ATOM   2909 C  C   . TYR A 1 370 ? -43.865 -13.513 32.100 1.00 100.18 ? 666 TYR A C   1 
ATOM   2910 O  O   . TYR A 1 370 ? -44.269 -14.625 32.456 1.00 98.23  ? 666 TYR A O   1 
ATOM   2911 C  CB  . TYR A 1 370 ? -42.342 -12.574 33.868 1.00 79.07  ? 666 TYR A CB  1 
ATOM   2912 C  CG  . TYR A 1 370 ? -40.966 -12.787 34.477 1.00 71.48  ? 666 TYR A CG  1 
ATOM   2913 C  CD1 . TYR A 1 370 ? -39.973 -11.832 34.336 1.00 73.37  ? 666 TYR A CD1 1 
ATOM   2914 C  CD2 . TYR A 1 370 ? -40.649 -13.962 35.146 1.00 75.73  ? 666 TYR A CD2 1 
ATOM   2915 C  CE1 . TYR A 1 370 ? -38.705 -12.021 34.862 1.00 77.41  ? 666 TYR A CE1 1 
ATOM   2916 C  CE2 . TYR A 1 370 ? -39.378 -14.159 35.679 1.00 81.16  ? 666 TYR A CE2 1 
ATOM   2917 C  CZ  . TYR A 1 370 ? -38.408 -13.186 35.529 1.00 81.44  ? 666 TYR A CZ  1 
ATOM   2918 O  OH  . TYR A 1 370 ? -37.139 -13.363 36.045 1.00 76.38  ? 666 TYR A OH  1 
ATOM   2919 N  N   . ARG A 1 371 ? -44.619 -12.668 31.395 1.00 107.15 ? 667 ARG A N   1 
ATOM   2920 C  CA  . ARG A 1 371 ? -45.978 -13.003 30.988 1.00 119.09 ? 667 ARG A CA  1 
ATOM   2921 C  C   . ARG A 1 371 ? -45.993 -13.869 29.729 1.00 124.82 ? 667 ARG A C   1 
ATOM   2922 O  O   . ARG A 1 371 ? -46.201 -15.084 29.822 1.00 129.25 ? 667 ARG A O   1 
ATOM   2923 C  CB  . ARG A 1 371 ? -46.797 -11.724 30.784 1.00 124.70 ? 667 ARG A CB  1 
ATOM   2924 C  CG  . ARG A 1 371 ? -47.537 -11.262 32.040 1.00 130.93 ? 667 ARG A CG  1 
ATOM   2925 C  CD  . ARG A 1 371 ? -47.553 -9.740  32.215 1.00 133.40 ? 667 ARG A CD  1 
ATOM   2926 N  NE  . ARG A 1 371 ? -47.136 -9.018  31.014 1.00 133.55 ? 667 ARG A NE  1 
ATOM   2927 C  CZ  . ARG A 1 371 ? -47.940 -8.717  29.998 1.00 132.13 ? 667 ARG A CZ  1 
ATOM   2928 N  NH1 . ARG A 1 371 ? -49.213 -9.088  30.022 1.00 133.23 ? 667 ARG A NH1 1 
ATOM   2929 N  NH2 . ARG A 1 371 ? -47.463 -8.056  28.952 1.00 129.86 ? 667 ARG A NH2 1 
ATOM   2930 N  N   . CYS A 1 372 ? -45.753 -13.274 28.551 1.00 123.06 ? 668 CYS A N   1 
ATOM   2931 C  CA  A CYS A 1 372 ? -45.851 -13.979 27.276 0.47 124.69 ? 668 CYS A CA  1 
ATOM   2932 C  CA  B CYS A 1 372 ? -45.863 -13.996 27.287 0.53 124.76 ? 668 CYS A CA  1 
ATOM   2933 C  C   . CYS A 1 372 ? -44.630 -14.849 26.965 1.00 120.01 ? 668 CYS A C   1 
ATOM   2934 O  O   . CYS A 1 372 ? -44.450 -15.239 25.802 1.00 125.04 ? 668 CYS A O   1 
ATOM   2935 C  CB  A CYS A 1 372 ? -46.081 -12.980 26.136 0.47 124.91 ? 668 CYS A CB  1 
ATOM   2936 C  CB  B CYS A 1 372 ? -46.147 -13.018 26.138 0.53 125.17 ? 668 CYS A CB  1 
ATOM   2937 S  SG  A CYS A 1 372 ? -47.822 -12.688 25.707 0.47 128.79 ? 668 CYS A SG  1 
ATOM   2938 S  SG  B CYS A 1 372 ? -44.705 -12.179 25.418 0.53 120.49 ? 668 CYS A SG  1 
ATOM   2939 N  N   . ARG A 1 373 ? -43.790 -15.166 27.954 1.00 107.40 ? 669 ARG A N   1 
ATOM   2940 C  CA  . ARG A 1 373 ? -42.630 -16.023 27.711 1.00 98.63  ? 669 ARG A CA  1 
ATOM   2941 C  C   . ARG A 1 373 ? -42.229 -16.792 28.966 1.00 95.27  ? 669 ARG A C   1 
ATOM   2942 O  O   . ARG A 1 373 ? -41.583 -17.841 28.879 1.00 90.26  ? 669 ARG A O   1 
ATOM   2943 C  CB  . ARG A 1 373 ? -41.441 -15.205 27.198 1.00 91.68  ? 669 ARG A CB  1 
ATOM   2944 C  CG  . ARG A 1 373 ? -40.335 -16.047 26.554 1.00 89.14  ? 669 ARG A CG  1 
ATOM   2945 C  CD  . ARG A 1 373 ? -39.015 -15.275 26.385 1.00 83.50  ? 669 ARG A CD  1 
ATOM   2946 N  NE  . ARG A 1 373 ? -38.051 -16.037 25.585 1.00 86.19  ? 669 ARG A NE  1 
ATOM   2947 C  CZ  . ARG A 1 373 ? -36.766 -15.720 25.434 1.00 77.47  ? 669 ARG A CZ  1 
ATOM   2948 N  NH1 . ARG A 1 373 ? -36.270 -14.647 26.032 1.00 65.15  ? 669 ARG A NH1 1 
ATOM   2949 N  NH2 . ARG A 1 373 ? -35.978 -16.478 24.679 1.00 70.61  ? 669 ARG A NH2 1 
ATOM   2950 N  N   . GLY A 1 374 ? -42.602 -16.279 30.136 1.00 102.80 ? 670 GLY A N   1 
ATOM   2951 C  CA  . GLY A 1 374 ? -42.332 -16.959 31.391 1.00 104.08 ? 670 GLY A CA  1 
ATOM   2952 C  C   . GLY A 1 374 ? -40.971 -16.715 32.006 1.00 99.02  ? 670 GLY A C   1 
ATOM   2953 O  O   . GLY A 1 374 ? -40.499 -17.566 32.771 1.00 102.95 ? 670 GLY A O   1 
ATOM   2954 N  N   . GLY A 1 375 ? -40.333 -15.588 31.721 1.00 81.03  ? 671 GLY A N   1 
ATOM   2955 C  CA  . GLY A 1 375 ? -39.008 -15.326 32.244 1.00 52.45  ? 671 GLY A CA  1 
ATOM   2956 C  C   . GLY A 1 375 ? -38.242 -14.328 31.408 1.00 67.60  ? 671 GLY A C   1 
ATOM   2957 O  O   . GLY A 1 375 ? -38.573 -14.042 30.252 1.00 82.16  ? 671 GLY A O   1 
ATOM   2958 N  N   . CYS A 1 376 ? -37.170 -13.803 32.014 1.00 71.15  ? 672 CYS A N   1 
ATOM   2959 C  CA  . CYS A 1 376 ? -36.282 -12.847 31.355 1.00 65.31  ? 672 CYS A CA  1 
ATOM   2960 C  C   . CYS A 1 376 ? -34.895 -12.985 31.963 1.00 68.07  ? 672 CYS A C   1 
ATOM   2961 O  O   . CYS A 1 376 ? -34.621 -12.412 33.023 1.00 69.48  ? 672 CYS A O   1 
ATOM   2962 C  CB  . CYS A 1 376 ? -36.791 -11.415 31.495 1.00 63.22  ? 672 CYS A CB  1 
ATOM   2963 S  SG  . CYS A 1 376 ? -35.850 -10.175 30.559 1.00 65.41  ? 672 CYS A SG  1 
ATOM   2964 N  N   . PRO A 1 377 ? -33.987 -13.717 31.319 1.00 71.82  ? 673 PRO A N   1 
ATOM   2965 C  CA  . PRO A 1 377 ? -32.601 -13.756 31.808 1.00 66.15  ? 673 PRO A CA  1 
ATOM   2966 C  C   . PRO A 1 377 ? -32.051 -12.346 31.925 1.00 59.62  ? 673 PRO A C   1 
ATOM   2967 O  O   . PRO A 1 377 ? -32.189 -11.534 31.003 1.00 49.31  ? 673 PRO A O   1 
ATOM   2968 C  CB  . PRO A 1 377 ? -31.864 -14.555 30.728 1.00 74.27  ? 673 PRO A CB  1 
ATOM   2969 C  CG  . PRO A 1 377 ? -32.732 -14.442 29.494 1.00 65.40  ? 673 PRO A CG  1 
ATOM   2970 C  CD  . PRO A 1 377 ? -34.138 -14.361 29.997 1.00 71.91  ? 673 PRO A CD  1 
ATOM   2971 N  N   . ALA A 1 378 ? -31.436 -12.038 33.070 1.00 47.88  ? 674 ALA A N   1 
ATOM   2972 C  CA  . ALA A 1 378 ? -31.016 -10.662 33.334 1.00 54.89  ? 674 ALA A CA  1 
ATOM   2973 C  C   . ALA A 1 378 ? -29.815 -10.633 34.271 1.00 56.86  ? 674 ALA A C   1 
ATOM   2974 O  O   . ALA A 1 378 ? -29.803 -11.332 35.288 1.00 51.65  ? 674 ALA A O   1 
ATOM   2975 C  CB  . ALA A 1 378 ? -32.173 -9.845  33.925 1.00 55.88  ? 674 ALA A CB  1 
ATOM   2976 N  N   . ASP A 1 379 ? -28.814 -9.818  33.945 1.00 47.63  ? 675 ASP A N   1 
ATOM   2977 C  CA  . ASP A 1 379 ? -27.603 -9.723  34.755 1.00 43.80  ? 675 ASP A CA  1 
ATOM   2978 C  C   . ASP A 1 379 ? -27.622 -8.374  35.463 1.00 49.92  ? 675 ASP A C   1 
ATOM   2979 O  O   . ASP A 1 379 ? -27.367 -7.331  34.846 1.00 46.51  ? 675 ASP A O   1 
ATOM   2980 C  CB  . ASP A 1 379 ? -26.343 -9.892  33.905 1.00 41.19  ? 675 ASP A CB  1 
ATOM   2981 C  CG  . ASP A 1 379 ? -25.064 -9.930  34.733 1.00 51.52  ? 675 ASP A CG  1 
ATOM   2982 O  OD1 . ASP A 1 379 ? -24.080 -10.570 34.306 1.00 49.92  ? 675 ASP A OD1 1 
ATOM   2983 O  OD2 . ASP A 1 379 ? -25.027 -9.322  35.826 1.00 58.91  ? 675 ASP A OD2 1 
ATOM   2984 N  N   . TRP A 1 380 ? -27.929 -8.418  36.761 1.00 45.21  ? 676 TRP A N   1 
ATOM   2985 C  CA  . TRP A 1 380 ? -27.989 -7.221  37.599 1.00 41.40  ? 676 TRP A CA  1 
ATOM   2986 C  C   . TRP A 1 380 ? -26.674 -6.448  37.587 1.00 43.65  ? 676 TRP A C   1 
ATOM   2987 O  O   . TRP A 1 380 ? -26.670 -5.210  37.599 1.00 53.12  ? 676 TRP A O   1 
ATOM   2988 C  CB  . TRP A 1 380 ? -28.335 -7.659  39.027 1.00 39.09  ? 676 TRP A CB  1 
ATOM   2989 C  CG  . TRP A 1 380 ? -28.788 -6.558  39.999 1.00 51.99  ? 676 TRP A CG  1 
ATOM   2990 C  CD1 . TRP A 1 380 ? -30.069 -6.320  40.413 1.00 35.93  ? 676 TRP A CD1 1 
ATOM   2991 C  CD2 . TRP A 1 380 ? -27.959 -5.599  40.679 1.00 52.39  ? 676 TRP A CD2 1 
ATOM   2992 N  NE1 . TRP A 1 380 ? -30.090 -5.275  41.289 1.00 41.67  ? 676 TRP A NE1 1 
ATOM   2993 C  CE2 . TRP A 1 380 ? -28.811 -4.821  41.490 1.00 48.72  ? 676 TRP A CE2 1 
ATOM   2994 C  CE3 . TRP A 1 380 ? -26.580 -5.335  40.698 1.00 34.46  ? 676 TRP A CE3 1 
ATOM   2995 C  CZ2 . TRP A 1 380 ? -28.339 -3.758  42.281 1.00 48.36  ? 676 TRP A CZ2 1 
ATOM   2996 C  CZ3 . TRP A 1 380 ? -26.114 -4.272  41.470 1.00 46.35  ? 676 TRP A CZ3 1 
ATOM   2997 C  CH2 . TRP A 1 380 ? -26.991 -3.505  42.258 1.00 47.85  ? 676 TRP A CH2 1 
ATOM   2998 N  N   . VAL A 1 381 ? -25.540 -7.153  37.609 1.00 45.79  ? 677 VAL A N   1 
ATOM   2999 C  CA  . VAL A 1 381 ? -24.263 -6.448  37.671 1.00 33.23  ? 677 VAL A CA  1 
ATOM   3000 C  C   . VAL A 1 381 ? -24.130 -5.506  36.495 1.00 45.60  ? 677 VAL A C   1 
ATOM   3001 O  O   . VAL A 1 381 ? -23.572 -4.408  36.617 1.00 37.04  ? 677 VAL A O   1 
ATOM   3002 C  CB  . VAL A 1 381 ? -23.104 -7.456  37.733 1.00 46.25  ? 677 VAL A CB  1 
ATOM   3003 C  CG1 . VAL A 1 381 ? -21.802 -6.728  37.727 1.00 45.21  ? 677 VAL A CG1 1 
ATOM   3004 C  CG2 . VAL A 1 381 ? -23.195 -8.310  39.015 1.00 46.88  ? 677 VAL A CG2 1 
ATOM   3005 N  N   . TRP A 1 382 ? -24.685 -5.901  35.347 1.00 51.30  ? 678 TRP A N   1 
ATOM   3006 C  CA  . TRP A 1 382 ? -24.620 -5.136  34.113 1.00 41.19  ? 678 TRP A CA  1 
ATOM   3007 C  C   . TRP A 1 382 ? -25.865 -4.292  33.863 1.00 51.93  ? 678 TRP A C   1 
ATOM   3008 O  O   . TRP A 1 382 ? -25.776 -3.265  33.171 1.00 50.47  ? 678 TRP A O   1 
ATOM   3009 C  CB  . TRP A 1 382 ? -24.397 -6.107  32.921 1.00 43.99  ? 678 TRP A CB  1 
ATOM   3010 C  CG  . TRP A 1 382 ? -22.926 -6.427  32.679 1.00 50.15  ? 678 TRP A CG  1 
ATOM   3011 C  CD1 . TRP A 1 382 ? -22.089 -7.126  33.510 1.00 57.61  ? 678 TRP A CD1 1 
ATOM   3012 C  CD2 . TRP A 1 382 ? -22.126 -6.033  31.546 1.00 51.62  ? 678 TRP A CD2 1 
ATOM   3013 N  NE1 . TRP A 1 382 ? -20.823 -7.193  32.962 1.00 56.85  ? 678 TRP A NE1 1 
ATOM   3014 C  CE2 . TRP A 1 382 ? -20.821 -6.529  31.760 1.00 60.21  ? 678 TRP A CE2 1 
ATOM   3015 C  CE3 . TRP A 1 382 ? -22.386 -5.312  30.386 1.00 55.11  ? 678 TRP A CE3 1 
ATOM   3016 C  CZ2 . TRP A 1 382 ? -19.784 -6.337  30.839 1.00 59.51  ? 678 TRP A CZ2 1 
ATOM   3017 C  CZ3 . TRP A 1 382 ? -21.347 -5.116  29.474 1.00 65.34  ? 678 TRP A CZ3 1 
ATOM   3018 C  CH2 . TRP A 1 382 ? -20.064 -5.618  29.715 1.00 61.09  ? 678 TRP A CH2 1 
ATOM   3019 N  N   . ILE A 1 383 ? -27.028 -4.681  34.402 1.00 37.48  ? 679 ILE A N   1 
ATOM   3020 C  CA  . ILE A 1 383 ? -28.240 -3.913  34.105 1.00 44.38  ? 679 ILE A CA  1 
ATOM   3021 C  C   . ILE A 1 383 ? -28.237 -2.577  34.852 1.00 53.42  ? 679 ILE A C   1 
ATOM   3022 O  O   . ILE A 1 383 ? -28.618 -1.540  34.288 1.00 52.58  ? 679 ILE A O   1 
ATOM   3023 C  CB  . ILE A 1 383 ? -29.496 -4.752  34.409 1.00 40.40  ? 679 ILE A CB  1 
ATOM   3024 C  CG1 . ILE A 1 383 ? -29.586 -5.964  33.486 1.00 51.47  ? 679 ILE A CG1 1 
ATOM   3025 C  CG2 . ILE A 1 383 ? -30.761 -3.923  34.307 1.00 51.33  ? 679 ILE A CG2 1 
ATOM   3026 C  CD1 . ILE A 1 383 ? -29.673 -5.613  31.972 1.00 59.60  ? 679 ILE A CD1 1 
ATOM   3027 N  N   . VAL A 1 384 ? -27.811 -2.572  36.118 1.00 48.30  ? 680 VAL A N   1 
ATOM   3028 C  CA  . VAL A 1 384 ? -27.783 -1.359  36.953 1.00 41.05  ? 680 VAL A CA  1 
ATOM   3029 C  C   . VAL A 1 384 ? -26.846 -0.330  36.336 1.00 45.47  ? 680 VAL A C   1 
ATOM   3030 O  O   . VAL A 1 384 ? -25.657 -0.628  36.142 1.00 56.43  ? 680 VAL A O   1 
ATOM   3031 C  CB  . VAL A 1 384 ? -27.330 -1.681  38.384 1.00 42.55  ? 680 VAL A CB  1 
ATOM   3032 C  CG1 . VAL A 1 384 ? -27.307 -0.415  39.225 1.00 46.23  ? 680 VAL A CG1 1 
ATOM   3033 C  CG2 . VAL A 1 384 ? -28.261 -2.673  38.978 1.00 50.50  ? 680 VAL A CG2 1 
ATOM   3034 N  N   . PRO A 1 385 ? -27.307 0.882   36.031 1.00 49.16  ? 681 PRO A N   1 
ATOM   3035 C  CA  . PRO A 1 385 ? -26.418 1.855   35.399 1.00 46.06  ? 681 PRO A CA  1 
ATOM   3036 C  C   . PRO A 1 385 ? -25.257 2.188   36.313 1.00 63.25  ? 681 PRO A C   1 
ATOM   3037 O  O   . PRO A 1 385 ? -25.381 2.123   37.555 1.00 65.21  ? 681 PRO A O   1 
ATOM   3038 C  CB  . PRO A 1 385 ? -27.324 3.074   35.177 1.00 49.81  ? 681 PRO A CB  1 
ATOM   3039 C  CG  . PRO A 1 385 ? -28.693 2.510   35.139 1.00 50.24  ? 681 PRO A CG  1 
ATOM   3040 C  CD  . PRO A 1 385 ? -28.685 1.383   36.145 1.00 51.73  ? 681 PRO A CD  1 
ATOM   3041 N  N   . PRO A 1 386 ? -24.118 2.580   35.744 1.00 50.88  ? 682 PRO A N   1 
ATOM   3042 C  CA  . PRO A 1 386 ? -22.899 2.798   36.538 1.00 51.11  ? 682 PRO A CA  1 
ATOM   3043 C  C   . PRO A 1 386 ? -22.853 4.119   37.294 1.00 60.78  ? 682 PRO A C   1 
ATOM   3044 O  O   . PRO A 1 386 ? -21.779 4.517   37.763 1.00 56.80  ? 682 PRO A O   1 
ATOM   3045 C  CB  . PRO A 1 386 ? -21.813 2.754   35.461 1.00 53.82  ? 682 PRO A CB  1 
ATOM   3046 C  CG  . PRO A 1 386 ? -22.502 3.318   34.246 1.00 45.96  ? 682 PRO A CG  1 
ATOM   3047 C  CD  . PRO A 1 386 ? -23.978 3.099   34.382 1.00 42.36  ? 682 PRO A CD  1 
ATOM   3048 N  N   . MET A 1 387 ? -23.979 4.817   37.402 1.00 61.81  ? 683 MET A N   1 
ATOM   3049 C  CA  . MET A 1 387 ? -24.119 5.911   38.345 1.00 52.72  ? 683 MET A CA  1 
ATOM   3050 C  C   . MET A 1 387 ? -25.555 5.903   38.845 1.00 58.08  ? 683 MET A C   1 
ATOM   3051 O  O   . MET A 1 387 ? -26.450 5.357   38.201 1.00 58.23  ? 683 MET A O   1 
ATOM   3052 C  CB  . MET A 1 387 ? -23.762 7.275   37.723 1.00 59.84  ? 683 MET A CB  1 
ATOM   3053 C  CG  . MET A 1 387 ? -24.785 7.833   36.756 1.00 56.74  ? 683 MET A CG  1 
ATOM   3054 S  SD  . MET A 1 387 ? -24.289 9.401   36.000 1.00 77.22  ? 683 MET A SD  1 
ATOM   3055 C  CE  . MET A 1 387 ? -24.717 10.541  37.286 1.00 61.53  ? 683 MET A CE  1 
ATOM   3056 N  N   . SER A 1 388 ? -25.766 6.530   40.005 1.00 56.49  ? 684 SER A N   1 
ATOM   3057 C  CA  . SER A 1 388 ? -27.111 6.733   40.552 1.00 53.42  ? 684 SER A CA  1 
ATOM   3058 C  C   . SER A 1 388 ? -27.915 5.431   40.580 1.00 58.11  ? 684 SER A C   1 
ATOM   3059 O  O   . SER A 1 388 ? -29.130 5.425   40.358 1.00 63.22  ? 684 SER A O   1 
ATOM   3060 C  CB  . SER A 1 388 ? -27.849 7.824   39.784 1.00 53.31  ? 684 SER A CB  1 
ATOM   3061 O  OG  . SER A 1 388 ? -27.056 9.003   39.707 1.00 61.55  ? 684 SER A OG  1 
ATOM   3062 N  N   . GLY A 1 389 ? -27.225 4.323   40.867 1.00 55.98  ? 685 GLY A N   1 
ATOM   3063 C  CA  . GLY A 1 389 ? -27.841 3.013   40.775 1.00 56.30  ? 685 GLY A CA  1 
ATOM   3064 C  C   . GLY A 1 389 ? -29.193 2.907   41.454 1.00 59.91  ? 685 GLY A C   1 
ATOM   3065 O  O   . GLY A 1 389 ? -30.150 2.386   40.875 1.00 56.26  ? 685 GLY A O   1 
ATOM   3066 N  N   . SER A 1 390 ? -29.298 3.376   42.698 1.00 56.15  ? 686 SER A N   1 
ATOM   3067 C  CA  . SER A 1 390 ? -30.505 3.087   43.469 1.00 60.30  ? 686 SER A CA  1 
ATOM   3068 C  C   . SER A 1 390 ? -31.638 4.102   43.282 1.00 67.11  ? 686 SER A C   1 
ATOM   3069 O  O   . SER A 1 390 ? -32.738 3.872   43.800 1.00 74.96  ? 686 SER A O   1 
ATOM   3070 C  CB  . SER A 1 390 ? -30.164 2.924   44.957 1.00 68.50  ? 686 SER A CB  1 
ATOM   3071 O  OG  . SER A 1 390 ? -29.454 4.025   45.491 1.00 65.02  ? 686 SER A OG  1 
ATOM   3072 N  N   . ILE A 1 391 ? -31.432 5.202   42.544 1.00 72.38  ? 687 ILE A N   1 
ATOM   3073 C  CA  . ILE A 1 391 ? -32.554 6.065   42.192 1.00 66.66  ? 687 ILE A CA  1 
ATOM   3074 C  C   . ILE A 1 391 ? -33.182 5.679   40.859 1.00 66.40  ? 687 ILE A C   1 
ATOM   3075 O  O   . ILE A 1 391 ? -34.131 6.343   40.424 1.00 73.56  ? 687 ILE A O   1 
ATOM   3076 C  CB  . ILE A 1 391 ? -32.162 7.560   42.171 1.00 74.51  ? 687 ILE A CB  1 
ATOM   3077 C  CG1 . ILE A 1 391 ? -31.249 7.888   40.992 1.00 71.41  ? 687 ILE A CG1 1 
ATOM   3078 C  CG2 . ILE A 1 391 ? -31.548 7.981   43.523 1.00 79.73  ? 687 ILE A CG2 1 
ATOM   3079 C  CD1 . ILE A 1 391 ? -30.901 9.355   40.900 1.00 69.88  ? 687 ILE A CD1 1 
ATOM   3080 N  N   . THR A 1 392 ? -32.678 4.564   40.179 1.00 59.94  ? 688 THR A N   1 
ATOM   3081 C  CA  . THR A 1 392 ? -33.333 3.878   39.067 1.00 68.27  ? 688 THR A CA  1 
ATOM   3082 C  C   . THR A 1 392 ? -34.039 2.619   39.561 1.00 68.30  ? 688 THR A C   1 
ATOM   3083 O  O   . THR A 1 392 ? -33.618 2.009   40.548 1.00 65.11  ? 688 THR A O   1 
ATOM   3084 C  CB  . THR A 1 392 ? -32.340 3.473   37.972 1.00 60.99  ? 688 THR A CB  1 
ATOM   3085 O  OG1 . THR A 1 392 ? -31.491 2.429   38.464 1.00 53.66  ? 688 THR A OG1 1 
ATOM   3086 C  CG2 . THR A 1 392 ? -31.508 4.680   37.470 1.00 59.79  ? 688 THR A CG2 1 
ATOM   3087 N  N   . PRO A 1 393 ? -35.119 2.197   38.900 1.00 67.59  ? 689 PRO A N   1 
ATOM   3088 C  CA  . PRO A 1 393 ? -35.907 1.076   39.433 1.00 70.17  ? 689 PRO A CA  1 
ATOM   3089 C  C   . PRO A 1 393 ? -35.222 -0.275  39.341 1.00 67.61  ? 689 PRO A C   1 
ATOM   3090 O  O   . PRO A 1 393 ? -35.620 -1.187  40.081 1.00 75.40  ? 689 PRO A O   1 
ATOM   3091 C  CB  . PRO A 1 393 ? -37.179 1.105   38.576 1.00 80.53  ? 689 PRO A CB  1 
ATOM   3092 C  CG  . PRO A 1 393 ? -36.731 1.711   37.290 1.00 77.55  ? 689 PRO A CG  1 
ATOM   3093 C  CD  . PRO A 1 393 ? -35.750 2.781   37.704 1.00 71.79  ? 689 PRO A CD  1 
ATOM   3094 N  N   . VAL A 1 394 ? -34.229 -0.457  38.462 1.00 56.99  ? 690 VAL A N   1 
ATOM   3095 C  CA  . VAL A 1 394 ? -33.616 -1.780  38.350 1.00 58.58  ? 690 VAL A CA  1 
ATOM   3096 C  C   . VAL A 1 394 ? -32.722 -2.100  39.558 1.00 66.18  ? 690 VAL A C   1 
ATOM   3097 O  O   . VAL A 1 394 ? -32.348 -3.268  39.767 1.00 53.49  ? 690 VAL A O   1 
ATOM   3098 C  CB  . VAL A 1 394 ? -32.841 -1.939  37.023 1.00 59.29  ? 690 VAL A CB  1 
ATOM   3099 C  CG1 . VAL A 1 394 ? -33.779 -1.819  35.824 1.00 48.78  ? 690 VAL A CG1 1 
ATOM   3100 C  CG2 . VAL A 1 394 ? -31.704 -0.941  36.916 1.00 69.21  ? 690 VAL A CG2 1 
ATOM   3101 N  N   . PHE A 1 395 ? -32.384 -1.105  40.384 1.00 61.65  ? 691 PHE A N   1 
ATOM   3102 C  CA  . PHE A 1 395 ? -31.575 -1.411  41.556 1.00 43.32  ? 691 PHE A CA  1 
ATOM   3103 C  C   . PHE A 1 395 ? -32.319 -2.355  42.488 1.00 61.13  ? 691 PHE A C   1 
ATOM   3104 O  O   . PHE A 1 395 ? -31.712 -3.223  43.129 1.00 66.68  ? 691 PHE A O   1 
ATOM   3105 C  CB  . PHE A 1 395 ? -31.206 -0.123  42.289 1.00 58.79  ? 691 PHE A CB  1 
ATOM   3106 C  CG  . PHE A 1 395 ? -30.362 -0.340  43.509 1.00 51.87  ? 691 PHE A CG  1 
ATOM   3107 C  CD1 . PHE A 1 395 ? -28.978 -0.300  43.421 1.00 53.90  ? 691 PHE A CD1 1 
ATOM   3108 C  CD2 . PHE A 1 395 ? -30.941 -0.601  44.741 1.00 57.90  ? 691 PHE A CD2 1 
ATOM   3109 C  CE1 . PHE A 1 395 ? -28.181 -0.521  44.541 1.00 49.68  ? 691 PHE A CE1 1 
ATOM   3110 C  CE2 . PHE A 1 395 ? -30.157 -0.812  45.857 1.00 58.70  ? 691 PHE A CE2 1 
ATOM   3111 C  CZ  . PHE A 1 395 ? -28.779 -0.764  45.755 1.00 57.80  ? 691 PHE A CZ  1 
ATOM   3112 N  N   . PHE A 1 396 ? -33.642 -2.208  42.555 1.00 59.13  ? 692 PHE A N   1 
ATOM   3113 C  CA  . PHE A 1 396 ? -34.497 -2.941  43.471 1.00 63.91  ? 692 PHE A CA  1 
ATOM   3114 C  C   . PHE A 1 396 ? -35.124 -4.182  42.846 1.00 63.05  ? 692 PHE A C   1 
ATOM   3115 O  O   . PHE A 1 396 ? -35.958 -4.831  43.486 1.00 65.54  ? 692 PHE A O   1 
ATOM   3116 C  CB  . PHE A 1 396 ? -35.595 -2.009  43.988 1.00 76.05  ? 692 PHE A CB  1 
ATOM   3117 C  CG  . PHE A 1 396 ? -35.083 -0.699  44.527 1.00 69.95  ? 692 PHE A CG  1 
ATOM   3118 C  CD1 . PHE A 1 396 ? -34.582 -0.610  45.823 1.00 77.50  ? 692 PHE A CD1 1 
ATOM   3119 C  CD2 . PHE A 1 396 ? -35.118 0.448   43.740 1.00 55.11  ? 692 PHE A CD2 1 
ATOM   3120 C  CE1 . PHE A 1 396 ? -34.121 0.606   46.329 1.00 71.46  ? 692 PHE A CE1 1 
ATOM   3121 C  CE2 . PHE A 1 396 ? -34.661 1.679   44.230 1.00 62.95  ? 692 PHE A CE2 1 
ATOM   3122 C  CZ  . PHE A 1 396 ? -34.150 1.754   45.525 1.00 60.75  ? 692 PHE A CZ  1 
ATOM   3123 N  N   . GLN A 1 397 ? -34.751 -4.520  41.619 1.00 64.70  ? 693 GLN A N   1 
ATOM   3124 C  CA  . GLN A 1 397 ? -35.330 -5.651  40.910 1.00 67.57  ? 693 GLN A CA  1 
ATOM   3125 C  C   . GLN A 1 397 ? -34.389 -6.842  41.013 1.00 55.55  ? 693 GLN A C   1 
ATOM   3126 O  O   . GLN A 1 397 ? -33.253 -6.784  40.528 1.00 47.27  ? 693 GLN A O   1 
ATOM   3127 C  CB  . GLN A 1 397 ? -35.607 -5.293  39.447 1.00 65.62  ? 693 GLN A CB  1 
ATOM   3128 C  CG  . GLN A 1 397 ? -36.251 -6.419  38.647 1.00 72.82  ? 693 GLN A CG  1 
ATOM   3129 C  CD  . GLN A 1 397 ? -37.641 -6.800  39.152 1.00 73.33  ? 693 GLN A CD  1 
ATOM   3130 O  OE1 . GLN A 1 397 ? -38.559 -5.968  39.190 1.00 62.05  ? 693 GLN A OE1 1 
ATOM   3131 N  NE2 . GLN A 1 397 ? -37.802 -8.069  39.536 1.00 78.68  ? 693 GLN A NE2 1 
ATOM   3132 N  N   . GLU A 1 398 ? -34.848 -7.895  41.684 1.00 63.09  ? 694 GLU A N   1 
ATOM   3133 C  CA  . GLU A 1 398 ? -34.149 -9.171  41.641 1.00 68.71  ? 694 GLU A CA  1 
ATOM   3134 C  C   . GLU A 1 398 ? -34.207 -9.746  40.231 1.00 68.51  ? 694 GLU A C   1 
ATOM   3135 O  O   . GLU A 1 398 ? -35.285 -9.859  39.634 1.00 70.35  ? 694 GLU A O   1 
ATOM   3136 C  CB  . GLU A 1 398 ? -34.769 -10.156 42.634 1.00 64.60  ? 694 GLU A CB  1 
ATOM   3137 C  CG  . GLU A 1 398 ? -34.650 -9.728  44.092 1.00 65.30  ? 694 GLU A CG  1 
ATOM   3138 C  CD  . GLU A 1 398 ? -35.370 -10.669 45.039 1.00 69.30  ? 694 GLU A CD  1 
ATOM   3139 O  OE1 . GLU A 1 398 ? -35.421 -10.345 46.241 1.00 72.81  ? 694 GLU A OE1 1 
ATOM   3140 O  OE2 . GLU A 1 398 ? -35.879 -11.726 44.595 1.00 71.98  ? 694 GLU A OE2 1 
ATOM   3141 N  N   . MET A 1 399 ? -33.047 -10.125 39.703 1.00 64.43  ? 695 MET A N   1 
ATOM   3142 C  CA  . MET A 1 399 ? -32.956 -10.740 38.391 1.00 66.65  ? 695 MET A CA  1 
ATOM   3143 C  C   . MET A 1 399 ? -32.329 -12.121 38.515 1.00 66.56  ? 695 MET A C   1 
ATOM   3144 O  O   . MET A 1 399 ? -31.452 -12.355 39.355 1.00 70.05  ? 695 MET A O   1 
ATOM   3145 C  CB  . MET A 1 399 ? -32.146 -9.862  37.406 1.00 53.28  ? 695 MET A CB  1 
ATOM   3146 C  CG  . MET A 1 399 ? -32.716 -8.451  37.244 1.00 51.14  ? 695 MET A CG  1 
ATOM   3147 S  SD  . MET A 1 399 ? -31.547 -7.251  36.625 1.00 53.95  ? 695 MET A SD  1 
ATOM   3148 C  CE  . MET A 1 399 ? -32.325 -5.694  37.044 1.00 51.90  ? 695 MET A CE  1 
ATOM   3149 N  N   . LEU A 1 400 ? -32.837 -13.040 37.700 1.00 66.61  ? 696 LEU A N   1 
ATOM   3150 C  CA  . LEU A 1 400 ? -32.298 -14.381 37.524 1.00 65.96  ? 696 LEU A CA  1 
ATOM   3151 C  C   . LEU A 1 400 ? -31.455 -14.379 36.260 1.00 67.12  ? 696 LEU A C   1 
ATOM   3152 O  O   . LEU A 1 400 ? -31.955 -14.020 35.199 1.00 58.33  ? 696 LEU A O   1 
ATOM   3153 C  CB  . LEU A 1 400 ? -33.428 -15.401 37.399 1.00 66.88  ? 696 LEU A CB  1 
ATOM   3154 C  CG  . LEU A 1 400 ? -33.860 -15.978 38.730 1.00 75.16  ? 696 LEU A CG  1 
ATOM   3155 C  CD1 . LEU A 1 400 ? -34.958 -16.997 38.512 1.00 82.16  ? 696 LEU A CD1 1 
ATOM   3156 C  CD2 . LEU A 1 400 ? -32.639 -16.607 39.351 1.00 74.69  ? 696 LEU A CD2 1 
ATOM   3157 N  N   . ASN A 1 401 ? -30.181 -14.745 36.375 1.00 67.31  ? 697 ASN A N   1 
ATOM   3158 C  CA  . ASN A 1 401 ? -29.304 -14.857 35.219 1.00 53.07  ? 697 ASN A CA  1 
ATOM   3159 C  C   . ASN A 1 401 ? -29.206 -16.317 34.803 1.00 59.07  ? 697 ASN A C   1 
ATOM   3160 O  O   . ASN A 1 401 ? -28.976 -17.198 35.638 1.00 52.59  ? 697 ASN A O   1 
ATOM   3161 C  CB  . ASN A 1 401 ? -27.903 -14.302 35.495 1.00 54.43  ? 697 ASN A CB  1 
ATOM   3162 C  CG  . ASN A 1 401 ? -27.180 -13.885 34.218 1.00 56.86  ? 697 ASN A CG  1 
ATOM   3163 O  OD1 . ASN A 1 401 ? -27.790 -13.821 33.155 1.00 50.90  ? 697 ASN A OD1 1 
ATOM   3164 N  ND2 . ASN A 1 401 ? -25.879 -13.602 34.318 1.00 53.62  ? 697 ASN A ND2 1 
ATOM   3165 N  N   . TYR A 1 402 ? -29.384 -16.559 33.507 1.00 60.51  ? 698 TYR A N   1 
ATOM   3166 C  CA  . TYR A 1 402 ? -29.237 -17.884 32.945 1.00 56.08  ? 698 TYR A CA  1 
ATOM   3167 C  C   . TYR A 1 402 ? -29.028 -17.724 31.440 1.00 60.00  ? 698 TYR A C   1 
ATOM   3168 O  O   . TYR A 1 402 ? -29.310 -16.666 30.856 1.00 54.44  ? 698 TYR A O   1 
ATOM   3169 C  CB  . TYR A 1 402 ? -30.442 -18.776 33.285 1.00 61.40  ? 698 TYR A CB  1 
ATOM   3170 C  CG  . TYR A 1 402 ? -31.813 -18.160 33.057 1.00 70.77  ? 698 TYR A CG  1 
ATOM   3171 C  CD1 . TYR A 1 402 ? -32.418 -18.194 31.803 1.00 70.74  ? 698 TYR A CD1 1 
ATOM   3172 C  CD2 . TYR A 1 402 ? -32.515 -17.562 34.107 1.00 75.64  ? 698 TYR A CD2 1 
ATOM   3173 C  CE1 . TYR A 1 402 ? -33.680 -17.643 31.594 1.00 71.43  ? 698 TYR A CE1 1 
ATOM   3174 C  CE2 . TYR A 1 402 ? -33.777 -17.011 33.910 1.00 77.49  ? 698 TYR A CE2 1 
ATOM   3175 C  CZ  . TYR A 1 402 ? -34.356 -17.059 32.649 1.00 77.23  ? 698 TYR A CZ  1 
ATOM   3176 O  OH  . TYR A 1 402 ? -35.607 -16.516 32.437 1.00 73.38  ? 698 TYR A OH  1 
ATOM   3177 N  N   . ARG A 1 403 ? -28.487 -18.772 30.829 1.00 62.52  ? 699 ARG A N   1 
ATOM   3178 C  CA  . ARG A 1 403 ? -27.996 -18.726 29.454 1.00 75.61  ? 699 ARG A CA  1 
ATOM   3179 C  C   . ARG A 1 403 ? -28.979 -19.448 28.536 1.00 76.00  ? 699 ARG A C   1 
ATOM   3180 O  O   . ARG A 1 403 ? -29.063 -20.679 28.547 1.00 71.16  ? 699 ARG A O   1 
ATOM   3181 C  CB  . ARG A 1 403 ? -26.598 -19.337 29.375 1.00 84.57  ? 699 ARG A CB  1 
ATOM   3182 C  CG  . ARG A 1 403 ? -25.619 -18.726 30.371 1.00 85.03  ? 699 ARG A CG  1 
ATOM   3183 C  CD  . ARG A 1 403 ? -24.442 -18.050 29.681 1.00 94.71  ? 699 ARG A CD  1 
ATOM   3184 N  NE  . ARG A 1 403 ? -23.384 -19.006 29.368 1.00 107.67 ? 699 ARG A NE  1 
ATOM   3185 C  CZ  . ARG A 1 403 ? -22.244 -18.690 28.761 1.00 109.61 ? 699 ARG A CZ  1 
ATOM   3186 N  NH1 . ARG A 1 403 ? -22.008 -17.436 28.396 1.00 103.34 ? 699 ARG A NH1 1 
ATOM   3187 N  NH2 . ARG A 1 403 ? -21.339 -19.633 28.518 1.00 113.05 ? 699 ARG A NH2 1 
ATOM   3188 N  N   . LEU A 1 404 ? -29.731 -18.676 27.756 1.00 74.62  ? 700 LEU A N   1 
ATOM   3189 C  CA  . LEU A 1 404 ? -30.608 -19.209 26.727 1.00 73.54  ? 700 LEU A CA  1 
ATOM   3190 C  C   . LEU A 1 404 ? -29.969 -19.012 25.365 1.00 75.40  ? 700 LEU A C   1 
ATOM   3191 O  O   . LEU A 1 404 ? -28.994 -18.280 25.206 1.00 72.21  ? 700 LEU A O   1 
ATOM   3192 C  CB  . LEU A 1 404 ? -31.982 -18.539 26.757 1.00 75.07  ? 700 LEU A CB  1 
ATOM   3193 C  CG  . LEU A 1 404 ? -32.735 -18.610 28.080 1.00 70.82  ? 700 LEU A CG  1 
ATOM   3194 C  CD1 . LEU A 1 404 ? -34.079 -17.914 27.941 1.00 71.79  ? 700 LEU A CD1 1 
ATOM   3195 C  CD2 . LEU A 1 404 ? -32.920 -20.049 28.496 1.00 75.91  ? 700 LEU A CD2 1 
ATOM   3196 N  N   . THR A 1 405 ? -30.543 -19.677 24.368 1.00 79.03  ? 701 THR A N   1 
ATOM   3197 C  CA  . THR A 1 405 ? -29.980 -19.684 23.037 1.00 69.06  ? 701 THR A CA  1 
ATOM   3198 C  C   . THR A 1 405 ? -31.130 -19.599 22.040 1.00 66.96  ? 701 THR A C   1 
ATOM   3199 O  O   . THR A 1 405 ? -32.206 -20.158 22.299 1.00 65.73  ? 701 THR A O   1 
ATOM   3200 C  CB  . THR A 1 405 ? -29.143 -20.955 22.814 1.00 74.42  ? 701 THR A CB  1 
ATOM   3201 O  OG1 . THR A 1 405 ? -28.472 -20.882 21.563 1.00 62.45  ? 701 THR A OG1 1 
ATOM   3202 C  CG2 . THR A 1 405 ? -30.006 -22.202 22.840 1.00 83.07  ? 701 THR A CG2 1 
ATOM   3203 N  N   . PRO A 1 406 ? -30.959 -18.889 20.900 1.00 59.41  ? 702 PRO A N   1 
ATOM   3204 C  CA  . PRO A 1 406 ? -29.790 -18.180 20.352 1.00 50.74  ? 702 PRO A CA  1 
ATOM   3205 C  C   . PRO A 1 406 ? -29.205 -17.106 21.256 1.00 58.57  ? 702 PRO A C   1 
ATOM   3206 O  O   . PRO A 1 406 ? -29.876 -16.598 22.177 1.00 55.45  ? 702 PRO A O   1 
ATOM   3207 C  CB  . PRO A 1 406 ? -30.336 -17.540 19.054 1.00 56.15  ? 702 PRO A CB  1 
ATOM   3208 C  CG  . PRO A 1 406 ? -31.460 -18.401 18.649 1.00 47.56  ? 702 PRO A CG  1 
ATOM   3209 C  CD  . PRO A 1 406 ? -32.088 -18.885 19.948 1.00 54.24  ? 702 PRO A CD  1 
ATOM   3210 N  N   . SER A 1 407 ? -27.937 -16.785 21.004 1.00 53.10  ? 703 SER A N   1 
ATOM   3211 C  CA  . SER A 1 407 ? -27.190 -15.994 21.961 1.00 57.71  ? 703 SER A CA  1 
ATOM   3212 C  C   . SER A 1 407 ? -25.998 -15.328 21.295 1.00 58.64  ? 703 SER A C   1 
ATOM   3213 O  O   . SER A 1 407 ? -25.455 -15.826 20.302 1.00 60.26  ? 703 SER A O   1 
ATOM   3214 C  CB  . SER A 1 407 ? -26.713 -16.856 23.140 1.00 59.54  ? 703 SER A CB  1 
ATOM   3215 O  OG  . SER A 1 407 ? -25.526 -17.561 22.813 1.00 70.45  ? 703 SER A OG  1 
ATOM   3216 N  N   . PHE A 1 408 ? -25.607 -14.192 21.876 1.00 50.63  ? 704 PHE A N   1 
ATOM   3217 C  CA  . PHE A 1 408 ? -24.354 -13.508 21.590 1.00 52.39  ? 704 PHE A CA  1 
ATOM   3218 C  C   . PHE A 1 408 ? -23.301 -13.965 22.594 1.00 58.13  ? 704 PHE A C   1 
ATOM   3219 O  O   . PHE A 1 408 ? -23.583 -14.058 23.789 1.00 71.00  ? 704 PHE A O   1 
ATOM   3220 C  CB  . PHE A 1 408 ? -24.538 -11.989 21.669 1.00 52.45  ? 704 PHE A CB  1 
ATOM   3221 C  CG  . PHE A 1 408 ? -25.316 -11.411 20.509 1.00 50.37  ? 704 PHE A CG  1 
ATOM   3222 C  CD1 . PHE A 1 408 ? -26.641 -11.009 20.663 1.00 48.24  ? 704 PHE A CD1 1 
ATOM   3223 C  CD2 . PHE A 1 408 ? -24.726 -11.297 19.276 1.00 52.19  ? 704 PHE A CD2 1 
ATOM   3224 C  CE1 . PHE A 1 408 ? -27.350 -10.496 19.615 1.00 54.99  ? 704 PHE A CE1 1 
ATOM   3225 C  CE2 . PHE A 1 408 ? -25.432 -10.783 18.207 1.00 44.70  ? 704 PHE A CE2 1 
ATOM   3226 C  CZ  . PHE A 1 408 ? -26.744 -10.382 18.370 1.00 53.51  ? 704 PHE A CZ  1 
ATOM   3227 N  N   . GLU A 1 409 ? -22.096 -14.253 22.108 1.00 52.05  ? 705 GLU A N   1 
ATOM   3228 C  CA  . GLU A 1 409 ? -21.003 -14.716 22.948 1.00 50.95  ? 705 GLU A CA  1 
ATOM   3229 C  C   . GLU A 1 409 ? -19.751 -13.914 22.648 1.00 62.23  ? 705 GLU A C   1 
ATOM   3230 O  O   . GLU A 1 409 ? -19.563 -13.407 21.539 1.00 66.46  ? 705 GLU A O   1 
ATOM   3231 C  CB  . GLU A 1 409 ? -20.669 -16.199 22.722 1.00 59.34  ? 705 GLU A CB  1 
ATOM   3232 C  CG  . GLU A 1 409 ? -21.839 -17.183 22.813 1.00 75.85  ? 705 GLU A CG  1 
ATOM   3233 C  CD  . GLU A 1 409 ? -22.313 -17.436 24.233 1.00 86.12  ? 705 GLU A CD  1 
ATOM   3234 O  OE1 . GLU A 1 409 ? -21.774 -16.822 25.186 1.00 86.37  ? 705 GLU A OE1 1 
ATOM   3235 O  OE2 . GLU A 1 409 ? -23.238 -18.262 24.388 1.00 93.77  ? 705 GLU A OE2 1 
ATOM   3236 N  N   . TYR A 1 410 ? -18.895 -13.804 23.648 1.00 59.65  ? 706 TYR A N   1 
ATOM   3237 C  CA  . TYR A 1 410 ? -17.572 -13.269 23.403 1.00 58.94  ? 706 TYR A CA  1 
ATOM   3238 C  C   . TYR A 1 410 ? -16.744 -14.284 22.644 1.00 65.06  ? 706 TYR A C   1 
ATOM   3239 O  O   . TYR A 1 410 ? -16.978 -15.498 22.712 1.00 66.01  ? 706 TYR A O   1 
ATOM   3240 C  CB  . TYR A 1 410 ? -16.842 -12.952 24.707 1.00 76.19  ? 706 TYR A CB  1 
ATOM   3241 C  CG  . TYR A 1 410 ? -17.536 -12.033 25.670 1.00 79.46  ? 706 TYR A CG  1 
ATOM   3242 C  CD1 . TYR A 1 410 ? -18.288 -12.549 26.727 1.00 86.47  ? 706 TYR A CD1 1 
ATOM   3243 C  CD2 . TYR A 1 410 ? -17.382 -10.653 25.578 1.00 80.60  ? 706 TYR A CD2 1 
ATOM   3244 C  CE1 . TYR A 1 410 ? -18.895 -11.714 27.647 1.00 83.72  ? 706 TYR A CE1 1 
ATOM   3245 C  CE2 . TYR A 1 410 ? -17.983 -9.810  26.494 1.00 86.66  ? 706 TYR A CE2 1 
ATOM   3246 C  CZ  . TYR A 1 410 ? -18.739 -10.348 27.524 1.00 83.46  ? 706 TYR A CZ  1 
ATOM   3247 O  OH  . TYR A 1 410 ? -19.342 -9.509  28.428 1.00 74.97  ? 706 TYR A OH  1 
ATOM   3248 N  N   . GLN A 1 411 ? -15.734 -13.777 21.954 1.00 69.21  ? 707 GLN A N   1 
ATOM   3249 C  CA  . GLN A 1 411 ? -14.791 -14.597 21.216 1.00 71.77  ? 707 GLN A CA  1 
ATOM   3250 C  C   . GLN A 1 411 ? -13.403 -13.994 21.368 1.00 73.80  ? 707 GLN A C   1 
ATOM   3251 O  O   . GLN A 1 411 ? -13.269 -12.794 21.625 1.00 80.45  ? 707 GLN A O   1 
ATOM   3252 C  CB  . GLN A 1 411 ? -15.175 -14.676 19.733 1.00 79.06  ? 707 GLN A CB  1 
ATOM   3253 C  CG  . GLN A 1 411 ? -14.940 -13.386 18.973 1.00 78.31  ? 707 GLN A CG  1 
ATOM   3254 C  CD  . GLN A 1 411 ? -15.713 -13.345 17.685 1.00 82.83  ? 707 GLN A CD  1 
ATOM   3255 O  OE1 . GLN A 1 411 ? -16.007 -14.386 17.100 1.00 89.54  ? 707 GLN A OE1 1 
ATOM   3256 N  NE2 . GLN A 1 411 ? -16.065 -12.141 17.240 1.00 76.59  ? 707 GLN A NE2 1 
ATOM   3257 N  N   . PRO A 1 412 ? -12.355 -14.802 21.199 1.00 74.09  ? 708 PRO A N   1 
ATOM   3258 C  CA  . PRO A 1 412 ? -10.986 -14.268 21.258 1.00 79.78  ? 708 PRO A CA  1 
ATOM   3259 C  C   . PRO A 1 412 ? -10.771 -13.131 20.270 1.00 87.20  ? 708 PRO A C   1 
ATOM   3260 O  O   . PRO A 1 412 ? -11.447 -13.037 19.244 1.00 87.01  ? 708 PRO A O   1 
ATOM   3261 C  CB  . PRO A 1 412 ? -10.116 -15.476 20.886 1.00 87.34  ? 708 PRO A CB  1 
ATOM   3262 C  CG  . PRO A 1 412 ? -10.965 -16.670 21.144 1.00 91.59  ? 708 PRO A CG  1 
ATOM   3263 C  CD  . PRO A 1 412 ? -12.384 -16.253 20.945 1.00 85.23  ? 708 PRO A CD  1 
ATOM   3264 N  N   . ASP A 1 413 ? -9.812  -12.268 20.591 1.00 93.31  ? 709 ASP A N   1 
ATOM   3265 C  CA  . ASP A 1 413 ? -9.313  -11.324 19.604 1.00 96.12  ? 709 ASP A CA  1 
ATOM   3266 C  C   . ASP A 1 413 ? -8.552  -12.084 18.523 1.00 97.74  ? 709 ASP A C   1 
ATOM   3267 O  O   . ASP A 1 413 ? -7.847  -13.052 18.824 1.00 102.81 ? 709 ASP A O   1 
ATOM   3268 C  CB  . ASP A 1 413 ? -8.399  -10.290 20.255 1.00 104.04 ? 709 ASP A CB  1 
ATOM   3269 C  CG  . ASP A 1 413 ? -9.126  -9.421  21.262 1.00 107.68 ? 709 ASP A CG  1 
ATOM   3270 O  OD1 . ASP A 1 413 ? -10.310 -9.097  21.026 1.00 104.92 ? 709 ASP A OD1 1 
ATOM   3271 O  OD2 . ASP A 1 413 ? -8.511  -9.062  22.289 1.00 110.93 ? 709 ASP A OD2 1 
ATOM   3272 N  N   . PRO A 1 414 ? -8.669  -11.675 17.262 1.00 93.03  ? 710 PRO A N   1 
ATOM   3273 C  CA  . PRO A 1 414 ? -8.120  -12.496 16.179 1.00 92.97  ? 710 PRO A CA  1 
ATOM   3274 C  C   . PRO A 1 414 ? -6.611  -12.382 16.052 1.00 99.10  ? 710 PRO A C   1 
ATOM   3275 O  O   . PRO A 1 414 ? -5.962  -13.324 15.589 1.00 102.55 ? 710 PRO A O   1 
ATOM   3276 C  CB  . PRO A 1 414 ? -8.831  -11.953 14.933 1.00 85.75  ? 710 PRO A CB  1 
ATOM   3277 C  CG  . PRO A 1 414 ? -9.921  -11.051 15.443 1.00 77.02  ? 710 PRO A CG  1 
ATOM   3278 C  CD  . PRO A 1 414 ? -9.427  -10.530 16.740 1.00 88.55  ? 710 PRO A CD  1 
ATOM   3279 N  N   . TRP A 1 415 ? -6.033  -11.247 16.451 1.00 98.55  ? 711 TRP A N   1 
ATOM   3280 C  CA  . TRP A 1 415 ? -4.578  -11.144 16.420 1.00 109.02 ? 711 TRP A CA  1 
ATOM   3281 C  C   . TRP A 1 415 ? -3.912  -11.987 17.499 1.00 118.08 ? 711 TRP A C   1 
ATOM   3282 O  O   . TRP A 1 415 ? -2.677  -12.008 17.575 1.00 123.03 ? 711 TRP A O   1 
ATOM   3283 C  CB  . TRP A 1 415 ? -4.143  -9.681  16.546 1.00 107.29 ? 711 TRP A CB  1 
ATOM   3284 C  CG  . TRP A 1 415 ? -4.540  -9.043  17.832 1.00 106.39 ? 711 TRP A CG  1 
ATOM   3285 C  CD1 . TRP A 1 415 ? -3.796  -8.969  18.973 1.00 111.88 ? 711 TRP A CD1 1 
ATOM   3286 C  CD2 . TRP A 1 415 ? -5.782  -8.389  18.119 1.00 101.60 ? 711 TRP A CD2 1 
ATOM   3287 N  NE1 . TRP A 1 415 ? -4.498  -8.312  19.956 1.00 108.42 ? 711 TRP A NE1 1 
ATOM   3288 C  CE2 . TRP A 1 415 ? -5.720  -7.944  19.456 1.00 104.13 ? 711 TRP A CE2 1 
ATOM   3289 C  CE3 . TRP A 1 415 ? -6.939  -8.137  17.378 1.00 96.88  ? 711 TRP A CE3 1 
ATOM   3290 C  CZ2 . TRP A 1 415 ? -6.769  -7.260  20.064 1.00 98.85  ? 711 TRP A CZ2 1 
ATOM   3291 C  CZ3 . TRP A 1 415 ? -7.980  -7.459  17.981 1.00 90.65  ? 711 TRP A CZ3 1 
ATOM   3292 C  CH2 . TRP A 1 415 ? -7.888  -7.025  19.311 1.00 97.00  ? 711 TRP A CH2 1 
ATOM   3293 N  N   . ASN A 1 416 ? -4.700  -12.677 18.328 1.00 121.05 ? 712 ASN A N   1 
ATOM   3294 C  CA  . ASN A 1 416 ? -4.193  -13.607 19.328 1.00 122.07 ? 712 ASN A CA  1 
ATOM   3295 C  C   . ASN A 1 416 ? -4.644  -15.042 19.065 1.00 118.43 ? 712 ASN A C   1 
ATOM   3296 O  O   . ASN A 1 416 ? -4.468  -15.904 19.933 1.00 121.65 ? 712 ASN A O   1 
ATOM   3297 C  CB  . ASN A 1 416 ? -4.623  -13.158 20.727 1.00 126.90 ? 712 ASN A CB  1 
ATOM   3298 C  CG  . ASN A 1 416 ? -4.050  -11.800 21.105 1.00 132.64 ? 712 ASN A CG  1 
ATOM   3299 O  OD1 . ASN A 1 416 ? -3.041  -11.364 20.544 1.00 138.07 ? 712 ASN A OD1 1 
ATOM   3300 N  ND2 . ASN A 1 416 ? -4.687  -11.127 22.064 1.00 126.72 ? 712 ASN A ND2 1 
ATOM   3301 N  N   . THR A 1 417 ? -5.227  -15.314 17.895 1.00 115.42 ? 713 THR A N   1 
ATOM   3302 C  CA  . THR A 1 417 ? -5.605  -16.667 17.480 1.00 115.91 ? 713 THR A CA  1 
ATOM   3303 C  C   . THR A 1 417 ? -5.351  -16.948 16.009 1.00 125.04 ? 713 THR A C   1 
ATOM   3304 O  O   . THR A 1 417 ? -5.250  -18.123 15.634 1.00 133.23 ? 713 THR A O   1 
ATOM   3305 C  CB  . THR A 1 417 ? -7.090  -16.934 17.769 1.00 111.69 ? 713 THR A CB  1 
ATOM   3306 O  OG1 . THR A 1 417 ? -7.884  -15.850 17.263 1.00 107.10 ? 713 THR A OG1 1 
ATOM   3307 C  CG2 . THR A 1 417 ? -7.343  -17.113 19.270 1.00 112.37 ? 713 THR A CG2 1 
ATOM   3308 N  N   . HIS A 1 418 ? -5.244  -15.926 15.165 1.00 123.18 ? 714 HIS A N   1 
ATOM   3309 C  CA  . HIS A 1 418 ? -5.130  -16.125 13.729 1.00 124.17 ? 714 HIS A CA  1 
ATOM   3310 C  C   . HIS A 1 418 ? -3.803  -16.789 13.388 1.00 132.20 ? 714 HIS A C   1 
ATOM   3311 O  O   . HIS A 1 418 ? -2.740  -16.340 13.828 1.00 133.50 ? 714 HIS A O   1 
ATOM   3312 C  CB  . HIS A 1 418 ? -5.253  -14.782 13.010 1.00 117.90 ? 714 HIS A CB  1 
ATOM   3313 C  CG  . HIS A 1 418 ? -5.548  -14.893 11.546 1.00 113.80 ? 714 HIS A CG  1 
ATOM   3314 N  ND1 . HIS A 1 418 ? -5.217  -13.901 10.647 1.00 112.80 ? 714 HIS A ND1 1 
ATOM   3315 C  CD2 . HIS A 1 418 ? -6.158  -15.864 10.827 1.00 111.76 ? 714 HIS A CD2 1 
ATOM   3316 C  CE1 . HIS A 1 418 ? -5.600  -14.261 9.435  1.00 113.50 ? 714 HIS A CE1 1 
ATOM   3317 N  NE2 . HIS A 1 418 ? -6.174  -15.448 9.517  1.00 114.21 ? 714 HIS A NE2 1 
ATOM   3318 N  N   . VAL A 1 419 ? -3.874  -17.875 12.623 1.00 134.70 ? 715 VAL A N   1 
ATOM   3319 C  CA  . VAL A 1 419 ? -2.701  -18.402 11.940 1.00 139.22 ? 715 VAL A CA  1 
ATOM   3320 C  C   . VAL A 1 419 ? -2.419  -17.454 10.779 1.00 142.67 ? 715 VAL A C   1 
ATOM   3321 O  O   . VAL A 1 419 ? -3.052  -17.542 9.721  1.00 142.94 ? 715 VAL A O   1 
ATOM   3322 C  CB  . VAL A 1 419 ? -2.926  -19.852 11.473 1.00 136.28 ? 715 VAL A CB  1 
ATOM   3323 C  CG1 . VAL A 1 419 ? -1.775  -20.315 10.612 1.00 138.83 ? 715 VAL A CG1 1 
ATOM   3324 C  CG2 . VAL A 1 419 ? -3.096  -20.779 12.676 1.00 134.49 ? 715 VAL A CG2 1 
ATOM   3325 N  N   . TRP A 1 420 ? -1.476  -16.534 10.976 1.00 144.98 ? 716 TRP A N   1 
ATOM   3326 C  CA  . TRP A 1 420 ? -1.354  -15.336 10.138 1.00 146.58 ? 716 TRP A CA  1 
ATOM   3327 C  C   . TRP A 1 420 ? -0.703  -15.554 8.765  1.00 146.10 ? 716 TRP A C   1 
ATOM   3328 O  O   . TRP A 1 420 ? -0.556  -16.674 8.281  1.00 147.46 ? 716 TRP A O   1 
ATOM   3329 C  CB  . TRP A 1 420 ? -0.573  -14.268 10.905 1.00 152.81 ? 716 TRP A CB  1 
ATOM   3330 C  CG  . TRP A 1 420 ? -1.165  -12.894 10.800 1.00 155.43 ? 716 TRP A CG  1 
ATOM   3331 C  CD1 . TRP A 1 420 ? -2.404  -12.562 10.325 1.00 151.51 ? 716 TRP A CD1 1 
ATOM   3332 C  CD2 . TRP A 1 420 ? -0.538  -11.663 11.176 1.00 158.64 ? 716 TRP A CD2 1 
ATOM   3333 N  NE1 . TRP A 1 420 ? -2.585  -11.200 10.385 1.00 149.42 ? 716 TRP A NE1 1 
ATOM   3334 C  CE2 . TRP A 1 420 ? -1.453  -10.626 10.902 1.00 153.56 ? 716 TRP A CE2 1 
ATOM   3335 C  CE3 . TRP A 1 420 ? 0.711   -11.336 11.716 1.00 162.37 ? 716 TRP A CE3 1 
ATOM   3336 C  CZ2 . TRP A 1 420 ? -1.159  -9.288  11.153 1.00 152.18 ? 716 TRP A CZ2 1 
ATOM   3337 C  CZ3 . TRP A 1 420 ? 1.001   -10.006 11.963 1.00 162.06 ? 716 TRP A CZ3 1 
ATOM   3338 C  CH2 . TRP A 1 420 ? 0.070   -8.999  11.681 1.00 157.23 ? 716 TRP A CH2 1 
HETATM 3339 C  CHA . HEM B 2 .   ? -24.841 -4.356  26.128 1.00 61.40  ? 801 HEM A CHA 1 
HETATM 3340 C  CHB . HEM B 2 .   ? -28.164 -0.830  25.819 1.00 66.37  ? 801 HEM A CHB 1 
HETATM 3341 C  CHC . HEM B 2 .   ? -29.172 -2.437  21.290 1.00 46.25  ? 801 HEM A CHC 1 
HETATM 3342 C  CHD . HEM B 2 .   ? -27.118 -6.643  22.449 1.00 53.34  ? 801 HEM A CHD 1 
HETATM 3343 C  C1A . HEM B 2 .   ? -25.526 -3.177  26.377 1.00 65.58  ? 801 HEM A C1A 1 
HETATM 3344 C  C2A . HEM B 2 .   ? -25.197 -2.160  27.361 1.00 65.36  ? 801 HEM A C2A 1 
HETATM 3345 C  C3A . HEM B 2 .   ? -26.106 -1.170  27.283 1.00 66.56  ? 801 HEM A C3A 1 
HETATM 3346 C  C4A . HEM B 2 .   ? -27.062 -1.535  26.251 1.00 62.79  ? 801 HEM A C4A 1 
HETATM 3347 C  CMA . HEM B 2 .   ? -26.109 0.102   28.185 1.00 63.14  ? 801 HEM A CMA 1 
HETATM 3348 C  CAA . HEM B 2 .   ? -23.972 -2.207  28.310 1.00 56.66  ? 801 HEM A CAA 1 
HETATM 3349 C  CBA . HEM B 2 .   ? -22.742 -1.964  27.422 1.00 50.98  ? 801 HEM A CBA 1 
HETATM 3350 C  CGA . HEM B 2 .   ? -21.507 -1.898  28.279 1.00 60.97  ? 801 HEM A CGA 1 
HETATM 3351 O  O1A . HEM B 2 .   ? -21.671 -1.679  29.491 1.00 58.91  ? 801 HEM A O1A 1 
HETATM 3352 O  O2A . HEM B 2 .   ? -20.371 -2.063  27.777 1.00 68.63  ? 801 HEM A O2A 1 
HETATM 3353 C  C1B . HEM B 2 .   ? -28.690 -0.917  24.538 1.00 66.92  ? 801 HEM A C1B 1 
HETATM 3354 C  C2B . HEM B 2 .   ? -29.568 0.056   23.901 1.00 61.23  ? 801 HEM A C2B 1 
HETATM 3355 C  C3B . HEM B 2 .   ? -29.853 -0.399  22.681 1.00 61.37  ? 801 HEM A C3B 1 
HETATM 3356 C  C4B . HEM B 2 .   ? -29.160 -1.663  22.451 1.00 56.75  ? 801 HEM A C4B 1 
HETATM 3357 C  CMB . HEM B 2 .   ? -30.124 1.363   24.532 1.00 55.12  ? 801 HEM A CMB 1 
HETATM 3358 C  CAB . HEM B 2 .   ? -30.768 0.344   21.695 1.00 66.92  ? 801 HEM A CAB 1 
HETATM 3359 C  CBB . HEM B 2 .   ? -31.975 -0.167  21.438 1.00 70.89  ? 801 HEM A CBB 1 
HETATM 3360 C  C1C . HEM B 2 .   ? -28.662 -3.713  21.174 1.00 40.32  ? 801 HEM A C1C 1 
HETATM 3361 C  C2C . HEM B 2 .   ? -28.666 -4.545  19.982 1.00 46.35  ? 801 HEM A C2C 1 
HETATM 3362 C  C3C . HEM B 2 .   ? -28.089 -5.733  20.275 1.00 42.80  ? 801 HEM A C3C 1 
HETATM 3363 C  C4C . HEM B 2 .   ? -27.729 -5.676  21.690 1.00 51.55  ? 801 HEM A C4C 1 
HETATM 3364 C  CMC . HEM B 2 .   ? -29.242 -4.005  18.652 1.00 52.18  ? 801 HEM A CMC 1 
HETATM 3365 C  CAC . HEM B 2 .   ? -27.818 -6.997  19.421 1.00 47.32  ? 801 HEM A CAC 1 
HETATM 3366 C  CBC . HEM B 2 .   ? -28.345 -7.257  18.205 1.00 57.06  ? 801 HEM A CBC 1 
HETATM 3367 C  C1D . HEM B 2 .   ? -26.289 -6.375  23.519 1.00 65.33  ? 801 HEM A C1D 1 
HETATM 3368 C  C2D . HEM B 2 .   ? -25.359 -7.311  24.095 1.00 61.14  ? 801 HEM A C2D 1 
HETATM 3369 C  C3D . HEM B 2 .   ? -24.714 -6.682  25.088 1.00 45.77  ? 801 HEM A C3D 1 
HETATM 3370 C  C4D . HEM B 2 .   ? -25.224 -5.329  25.204 1.00 57.44  ? 801 HEM A C4D 1 
HETATM 3371 C  CMD . HEM B 2 .   ? -25.165 -8.763  23.586 1.00 63.38  ? 801 HEM A CMD 1 
HETATM 3372 C  CAD . HEM B 2 .   ? -23.642 -7.269  26.033 1.00 53.91  ? 801 HEM A CAD 1 
HETATM 3373 C  CBD . HEM B 2 .   ? -22.330 -7.423  25.281 1.00 60.92  ? 801 HEM A CBD 1 
HETATM 3374 C  CGD . HEM B 2 .   ? -21.232 -7.514  26.306 1.00 60.73  ? 801 HEM A CGD 1 
HETATM 3375 O  O1D . HEM B 2 .   ? -21.322 -8.336  27.259 1.00 63.64  ? 801 HEM A O1D 1 
HETATM 3376 O  O2D . HEM B 2 .   ? -20.248 -6.755  26.164 1.00 56.05  ? 801 HEM A O2D 1 
HETATM 3377 N  NA  . HEM B 2 .   ? -26.675 -2.756  25.727 1.00 65.28  ? 801 HEM A NA  1 
HETATM 3378 N  NB  . HEM B 2 .   ? -28.453 -1.939  23.612 1.00 60.25  ? 801 HEM A NB  1 
HETATM 3379 N  NC  . HEM B 2 .   ? -28.097 -4.444  22.200 1.00 51.93  ? 801 HEM A NC  1 
HETATM 3380 N  ND  . HEM B 2 .   ? -26.177 -5.176  24.222 1.00 62.42  ? 801 HEM A ND  1 
HETATM 3381 FE FE  . HEM B 2 .   ? -27.696 -3.837  24.209 1.00 53.99  ? 801 HEM A FE  1 
HETATM 3382 N  N1  . H4B C 3 .   ? -21.746 -3.327  33.872 1.00 66.91  ? 802 H4B A N1  1 
HETATM 3383 C  C2  . H4B C 3 .   ? -21.760 -2.799  32.620 1.00 62.33  ? 802 H4B A C2  1 
HETATM 3384 N  N2  . H4B C 3 .   ? -22.946 -2.400  32.104 1.00 57.07  ? 802 H4B A N2  1 
HETATM 3385 N  N3  . H4B C 3 .   ? -20.611 -2.685  31.901 1.00 58.05  ? 802 H4B A N3  1 
HETATM 3386 C  C4  . H4B C 3 .   ? -19.426 -3.088  32.433 1.00 63.56  ? 802 H4B A C4  1 
HETATM 3387 O  O4  . H4B C 3 .   ? -18.372 -2.977  31.749 1.00 58.50  ? 802 H4B A O4  1 
HETATM 3388 C  C4A . H4B C 3 .   ? -19.410 -3.641  33.716 1.00 59.77  ? 802 H4B A C4A 1 
HETATM 3389 C  C8A . H4B C 3 .   ? -20.594 -3.744  34.440 1.00 61.38  ? 802 H4B A C8A 1 
HETATM 3390 N  N5  . H4B C 3 .   ? -18.263 -4.073  34.292 1.00 66.68  ? 802 H4B A N5  1 
HETATM 3391 N  N8  . H4B C 3 .   ? -20.627 -4.264  35.705 1.00 56.93  ? 802 H4B A N8  1 
HETATM 3392 C  C6  . H4B C 3 .   ? -18.349 -5.034  35.399 1.00 59.57  ? 802 H4B A C6  1 
HETATM 3393 C  C7  . H4B C 3 .   ? -19.415 -4.645  36.420 1.00 53.62  ? 802 H4B A C7  1 
HETATM 3394 C  C9  . H4B C 3 .   ? -17.006 -5.215  36.095 1.00 54.27  ? 802 H4B A C9  1 
HETATM 3395 O  O9  . H4B C 3 .   ? -16.599 -3.899  36.503 1.00 61.30  ? 802 H4B A O9  1 
HETATM 3396 C  C10 . H4B C 3 .   ? -17.082 -6.137  37.319 1.00 62.55  ? 802 H4B A C10 1 
HETATM 3397 C  C11 . H4B C 3 .   ? -15.699 -6.417  37.910 1.00 62.26  ? 802 H4B A C11 1 
HETATM 3398 O  O10 . H4B C 3 .   ? -17.719 -7.390  37.030 1.00 61.17  ? 802 H4B A O10 1 
HETATM 3399 C  C13 . KMI D 4 .   ? -19.973 -0.332  23.789 1.00 67.00  ? 803 KMI A C13 1 
HETATM 3400 C  C11 . KMI D 4 .   ? -22.178 -1.258  23.604 1.00 53.19  ? 803 KMI A C11 1 
HETATM 3401 C  C12 . KMI D 4 .   ? -21.305 -0.186  23.445 1.00 59.34  ? 803 KMI A C12 1 
HETATM 3402 C  C14 . KMI D 4 .   ? -19.526 -1.557  24.264 1.00 65.59  ? 803 KMI A C14 1 
HETATM 3403 C  C02 . KMI D 4 .   ? -25.574 0.202   23.289 1.00 52.60  ? 803 KMI A C02 1 
HETATM 3404 C  C03 . KMI D 4 .   ? -26.082 -0.519  22.212 1.00 46.72  ? 803 KMI A C03 1 
HETATM 3405 C  C04 . KMI D 4 .   ? -25.307 -1.488  21.588 1.00 54.37  ? 803 KMI A C04 1 
HETATM 3406 C  C05 . KMI D 4 .   ? -24.028 -1.734  22.053 1.00 57.13  ? 803 KMI A C05 1 
HETATM 3407 C  C06 . KMI D 4 .   ? -23.572 -1.011  23.162 1.00 58.08  ? 803 KMI A C06 1 
HETATM 3408 C  C07 . KMI D 4 .   ? -25.843 -2.281  20.443 1.00 53.41  ? 803 KMI A C07 1 
HETATM 3409 C  C15 . KMI D 4 .   ? -20.384 -2.648  24.402 1.00 60.08  ? 803 KMI A C15 1 
HETATM 3410 C  C16 . KMI D 4 .   ? -21.735 -2.500  24.065 1.00 52.93  ? 803 KMI A C16 1 
HETATM 3411 C  C17 . KMI D 4 .   ? -19.788 -3.935  24.941 1.00 60.27  ? 803 KMI A C17 1 
HETATM 3412 C  C19 . KMI D 4 .   ? -18.111 -4.681  26.629 1.00 63.63  ? 803 KMI A C19 1 
HETATM 3413 N  N01 . KMI D 4 .   ? -24.314 -0.036  23.731 1.00 51.19  ? 803 KMI A N01 1 
HETATM 3414 N  N02 . KMI D 4 .   ? -26.339 1.163   23.878 1.00 48.76  ? 803 KMI A N02 1 
HETATM 3415 N  N18 . KMI D 4 .   ? -18.672 -3.559  25.847 1.00 72.81  ? 803 KMI A N18 1 
HETATM 3416 C  C   . ACT E 5 .   ? -34.541 1.883   25.509 1.00 112.66 ? 804 ACT A C   1 
HETATM 3417 O  O   . ACT E 5 .   ? -33.995 2.976   25.241 1.00 115.19 ? 804 ACT A O   1 
HETATM 3418 O  OXT . ACT E 5 .   ? -35.025 1.651   26.636 1.00 113.46 ? 804 ACT A OXT 1 
HETATM 3419 C  CH3 . ACT E 5 .   ? -34.590 0.802   24.466 1.00 107.52 ? 804 ACT A CH3 1 
HETATM 3420 ZN ZN  . ZN  F 6 .   ? -24.255 -16.698 40.981 0.50 57.61  ? 805 ZN  A ZN  1 
HETATM 3421 O  O   . HOH G 7 .   ? -24.979 -4.273  6.240  1.00 74.25  ? 901 HOH A O   1 
HETATM 3422 O  O   . HOH G 7 .   ? -34.225 -1.771  13.323 1.00 64.73  ? 902 HOH A O   1 
HETATM 3423 O  O   . HOH G 7 .   ? -16.655 -19.445 7.377  1.00 69.45  ? 903 HOH A O   1 
HETATM 3424 O  O   . HOH G 7 .   ? -19.638 -8.540  34.614 1.00 52.37  ? 904 HOH A O   1 
HETATM 3425 O  O   . HOH G 7 .   ? -34.896 -12.396 36.009 1.00 55.38  ? 905 HOH A O   1 
HETATM 3426 O  O   . HOH G 7 .   ? -35.634 -10.796 26.890 1.00 70.56  ? 906 HOH A O   1 
HETATM 3427 O  O   . HOH G 7 .   ? -29.484 -15.551 28.437 1.00 48.12  ? 907 HOH A O   1 
HETATM 3428 O  O   . HOH G 7 .   ? -7.438  6.739   40.393 1.00 73.54  ? 908 HOH A O   1 
HETATM 3429 O  O   . HOH G 7 .   ? -16.955 -16.726 9.596  1.00 57.10  ? 909 HOH A O   1 
HETATM 3430 O  O   . HOH G 7 .   ? -21.541 -14.859 -3.156 1.00 62.38  ? 910 HOH A O   1 
HETATM 3431 O  O   . HOH G 7 .   ? -37.104 3.496   8.809  1.00 59.73  ? 911 HOH A O   1 
HETATM 3432 O  O   . HOH G 7 .   ? -21.073 24.165  26.813 1.00 68.11  ? 912 HOH A O   1 
HETATM 3433 O  O   . HOH G 7 .   ? -29.519 14.716  13.379 1.00 51.23  ? 913 HOH A O   1 
HETATM 3434 O  O   . HOH G 7 .   ? -24.853 -11.028 38.015 1.00 58.27  ? 914 HOH A O   1 
HETATM 3435 O  O   . HOH G 7 .   ? -21.348 0.462   32.983 1.00 51.28  ? 915 HOH A O   1 
HETATM 3436 O  O   . HOH G 7 .   ? -13.015 -19.854 32.820 1.00 64.63  ? 916 HOH A O   1 
HETATM 3437 O  O   . HOH G 7 .   ? -24.062 -2.183  38.242 1.00 52.93  ? 917 HOH A O   1 
HETATM 3438 O  O   . HOH G 7 .   ? -14.982 1.086   29.677 1.00 53.51  ? 918 HOH A O   1 
HETATM 3439 O  O   . HOH G 7 .   ? -25.937 -3.952  2.088  1.00 87.21  ? 919 HOH A O   1 
HETATM 3440 O  O   . HOH G 7 .   ? -29.369 16.741  29.661 1.00 64.47  ? 920 HOH A O   1 
HETATM 3441 O  O   . HOH G 7 .   ? -17.091 -6.320  23.254 1.00 69.89  ? 921 HOH A O   1 
HETATM 3442 O  O   . HOH G 7 .   ? -21.415 -10.078 35.517 1.00 57.71  ? 922 HOH A O   1 
HETATM 3443 O  O   . HOH G 7 .   ? -20.336 14.187  12.411 1.00 47.89  ? 923 HOH A O   1 
HETATM 3444 O  O   . HOH G 7 .   ? -28.510 -10.946 37.907 1.00 65.23  ? 924 HOH A O   1 
HETATM 3445 O  O   . HOH G 7 .   ? -27.642 -8.865  0.571  1.00 67.84  ? 925 HOH A O   1 
HETATM 3446 O  O   . HOH G 7 .   ? -8.867  -17.603 11.058 1.00 59.05  ? 926 HOH A O   1 
HETATM 3447 O  O   . HOH G 7 .   ? -22.905 -0.810  34.830 1.00 70.48  ? 927 HOH A O   1 
HETATM 3448 O  O   . HOH G 7 .   ? -37.556 4.341   40.187 1.00 74.23  ? 928 HOH A O   1 
HETATM 3449 O  O   . HOH G 7 .   ? -37.229 -8.051  10.345 1.00 73.81  ? 929 HOH A O   1 
HETATM 3450 O  O   . HOH G 7 .   ? -17.761 1.117   28.515 1.00 54.70  ? 930 HOH A O   1 
# 
loop_
_atom_site_anisotrop.id 
_atom_site_anisotrop.type_symbol 
_atom_site_anisotrop.pdbx_label_atom_id 
_atom_site_anisotrop.pdbx_label_alt_id 
_atom_site_anisotrop.pdbx_label_comp_id 
_atom_site_anisotrop.pdbx_label_asym_id 
_atom_site_anisotrop.pdbx_label_seq_id 
_atom_site_anisotrop.pdbx_PDB_ins_code 
_atom_site_anisotrop.U[1][1] 
_atom_site_anisotrop.U[2][2] 
_atom_site_anisotrop.U[3][3] 
_atom_site_anisotrop.U[1][2] 
_atom_site_anisotrop.U[1][3] 
_atom_site_anisotrop.U[2][3] 
_atom_site_anisotrop.pdbx_auth_seq_id 
_atom_site_anisotrop.pdbx_auth_comp_id 
_atom_site_anisotrop.pdbx_auth_asym_id 
_atom_site_anisotrop.pdbx_auth_atom_id 
1    N N   . ARG A 3   ? 1.9306 1.4841 1.2829 -0.6007 0.0568  0.0415  299 ARG A N   
2    C CA  . ARG A 3   ? 1.9385 1.4702 1.3019 -0.5828 0.0477  0.0354  299 ARG A CA  
3    C C   . ARG A 3   ? 1.8412 1.5066 1.3020 -0.5832 0.0508  0.0301  299 ARG A C   
4    O O   . ARG A 3   ? 1.8709 1.5414 1.3508 -0.5747 0.0441  0.0241  299 ARG A O   
5    C CB  . ARG A 3   ? 2.0800 1.5287 1.3562 -0.6107 0.0404  0.0317  299 ARG A CB  
6    C CG  . ARG A 3   ? 2.0699 1.4540 1.3274 -0.5853 0.0300  0.0266  299 ARG A CG  
7    C CD  . ARG A 3   ? 2.1137 1.3872 1.3307 -0.5330 0.0230  0.0290  299 ARG A CD  
8    N NE  . ARG A 3   ? 2.0608 1.3728 1.3411 -0.4978 0.0262  0.0332  299 ARG A NE  
9    C CZ  . ARG A 3   ? 1.9797 1.3419 1.3339 -0.4664 0.0238  0.0301  299 ARG A CZ  
10   N NH1 . ARG A 3   ? 2.0069 1.3877 1.3846 -0.4631 0.0182  0.0225  299 ARG A NH1 
11   N NH2 . ARG A 3   ? 1.8129 1.2292 1.2270 -0.4212 0.0248  0.0313  299 ARG A NH2 
12   N N   . PHE A 4   ? 1.7159 1.4895 1.2354 -0.5892 0.0610  0.0322  300 PHE A N   
13   C CA  . PHE A 4   ? 1.5639 1.4746 1.1701 -0.5862 0.0648  0.0271  300 PHE A CA  
14   C C   . PHE A 4   ? 1.5148 1.4952 1.1860 -0.5552 0.0737  0.0305  300 PHE A C   
15   O O   . PHE A 4   ? 1.5151 1.5941 1.2221 -0.5612 0.0831  0.0313  300 PHE A O   
16   C CB  . PHE A 4   ? 1.5866 1.5729 1.1858 -0.6290 0.0680  0.0247  300 PHE A CB  
17   C CG  . PHE A 4   ? 1.7245 1.6203 1.2326 -0.6691 0.0616  0.0240  300 PHE A CG  
18   C CD1 . PHE A 4   ? 1.7334 1.5616 1.1680 -0.6961 0.0640  0.0288  300 PHE A CD1 
19   C CD2 . PHE A 4   ? 1.6785 1.5542 1.1696 -0.6797 0.0532  0.0184  300 PHE A CD2 
20   C CE1 . PHE A 4   ? 1.7945 1.5347 1.1374 -0.7329 0.0579  0.0276  300 PHE A CE1 
21   C CE2 . PHE A 4   ? 1.7653 1.5537 1.1650 -0.7165 0.0478  0.0178  300 PHE A CE2 
22   C CZ  . PHE A 4   ? 1.8539 1.5736 1.1779 -0.7432 0.0501  0.0222  300 PHE A CZ  
23   N N   . LEU A 5   ? 1.4865 1.4168 1.1727 -0.4988 0.0656  0.0285  301 LEU A N   
24   C CA  . LEU A 5   ? 1.4067 1.3595 1.1289 -0.4502 0.0675  0.0295  301 LEU A CA  
25   C C   . LEU A 5   ? 1.3220 1.4011 1.1249 -0.4262 0.0726  0.0247  301 LEU A C   
26   O O   . LEU A 5   ? 1.2504 1.3983 1.0911 -0.4326 0.0719  0.0195  301 LEU A O   
27   C CB  . LEU A 5   ? 1.3981 1.2719 1.1150 -0.3983 0.0554  0.0276  301 LEU A CB  
28   C CG  . LEU A 5   ? 1.5681 1.3127 1.1999 -0.4096 0.0491  0.0317  301 LEU A CG  
29   C CD1 . LEU A 5   ? 1.5841 1.2743 1.2176 -0.3634 0.0362  0.0273  301 LEU A CD1 
30   C CD2 . LEU A 5   ? 1.6011 1.2939 1.1865 -0.4098 0.0532  0.0395  301 LEU A CD2 
31   N N   . LYS A 6   ? 1.3010 1.4047 1.1248 -0.3946 0.0770  0.0261  302 LYS A N   
32   C CA  . LYS A 6   ? 1.2629 1.4754 1.1468 -0.3697 0.0835  0.0224  302 LYS A CA  
33   C C   . LYS A 6   ? 1.1830 1.3786 1.0964 -0.3101 0.0763  0.0187  302 LYS A C   
34   O O   . LYS A 6   ? 1.0683 1.1944 0.9554 -0.2933 0.0725  0.0217  302 LYS A O   
35   C CB  . LYS A 6   ? 1.3043 1.5718 1.1787 -0.3926 0.0978  0.0274  302 LYS A CB  
36   C CG  . LYS A 6   ? 1.3681 1.6594 1.2094 -0.4598 0.1059  0.0321  302 LYS A CG  
37   C CD  . LYS A 6   ? 1.3572 1.7773 1.2459 -0.4743 0.1115  0.0278  302 LYS A CD  
38   C CE  . LYS A 6   ? 1.4850 1.9193 1.3356 -0.5318 0.1121  0.0292  302 LYS A CE  
39   N NZ  . LYS A 6   ? 1.5622 1.9742 1.3687 -0.5567 0.1199  0.0357  302 LYS A NZ  
40   N N   . VAL A 7   ? 1.1659 1.4245 1.1293 -0.2800 0.0741  0.0124  303 VAL A N   
41   C CA  . VAL A 7   ? 1.0986 1.3491 1.0870 -0.2286 0.0682  0.0087  303 VAL A CA  
42   C C   . VAL A 7   ? 1.0537 1.3881 1.0689 -0.2071 0.0773  0.0063  303 VAL A C   
43   O O   . VAL A 7   ? 1.0857 1.5042 1.1241 -0.2156 0.0835  0.0041  303 VAL A O   
44   C CB  . VAL A 7   ? 1.0606 1.2971 1.0734 -0.2072 0.0570  0.0037  303 VAL A CB  
45   C CG1 . VAL A 7   ? 1.0924 1.2460 1.0740 -0.2222 0.0486  0.0057  303 VAL A CG1 
46   C CG2 . VAL A 7   ? 1.0313 1.3479 1.0760 -0.2145 0.0597  -0.0004 303 VAL A CG2 
47   N N   . LYS A 8   ? 0.9927 1.3056 1.0011 -0.1777 0.0777  0.0064  304 LYS A N   
48   C CA  . LYS A 8   ? 0.8862 1.2646 0.9085 -0.1512 0.0862  0.0037  304 LYS A CA  
49   C C   . LYS A 8   ? 0.7791 1.1457 0.8179 -0.1037 0.0780  -0.0023 304 LYS A C   
50   O O   . LYS A 8   ? 0.7978 1.0963 0.8316 -0.0927 0.0666  -0.0030 304 LYS A O   
51   C CB  . LYS A 8   ? 0.9173 1.2773 0.9107 -0.1539 0.0935  0.0079  304 LYS A CB  
52   C CG  . LYS A 8   ? 0.9795 1.4198 0.9807 -0.1344 0.1060  0.0059  304 LYS A CG  
53   C CD  . LYS A 8   ? 0.9229 1.3308 0.8942 -0.1261 0.1108  0.0087  304 LYS A CD  
54   C CE  . LYS A 8   ? 0.9370 1.4226 0.9128 -0.0982 0.1231  0.0056  304 LYS A CE  
55   N NZ  . LYS A 8   ? 0.8518 1.3020 0.7958 -0.0863 0.1273  0.0074  304 LYS A NZ  
56   N N   . ASN A 9   ? 0.6712 1.1052 0.7256 -0.0756 0.0838  -0.0065 305 ASN A N   
57   C CA  . ASN A 9   ? 0.7599 1.1729 0.8132 -0.0288 0.0778  -0.0119 305 ASN A CA  
58   C C   . ASN A 9   ? 0.9224 1.3424 0.9530 -0.0061 0.0857  -0.0126 305 ASN A C   
59   O O   . ASN A 9   ? 1.0239 1.5160 1.0566 -0.0098 0.0985  -0.0116 305 ASN A O   
60   C CB  . ASN A 9   ? 0.7963 1.2667 0.8727 -0.0051 0.0772  -0.0166 305 ASN A CB  
61   C CG  . ASN A 9   ? 0.8485 1.2794 0.9118 0.0411  0.0699  -0.0216 305 ASN A CG  
62   O OD1 . ASN A 9   ? 0.8941 1.3275 0.9356 0.0723  0.0745  -0.0242 305 ASN A OD1 
63   N ND2 . ASN A 9   ? 0.7947 1.1848 0.8653 0.0447  0.0588  -0.0229 305 ASN A ND2 
64   N N   . TRP A 10  ? 0.9608 1.3089 0.9680 0.0149  0.0782  -0.0142 306 TRP A N   
65   C CA  . TRP A 10  ? 1.0056 1.3465 0.9845 0.0336  0.0845  -0.0150 306 TRP A CA  
66   C C   . TRP A 10  ? 1.0707 1.4209 1.0335 0.0829  0.0854  -0.0219 306 TRP A C   
67   O O   . TRP A 10  ? 1.0616 1.4224 0.9998 0.1033  0.0932  -0.0235 306 TRP A O   
68   C CB  . TRP A 10  ? 0.9471 1.2033 0.9015 0.0242  0.0757  -0.0127 306 TRP A CB  
69   C CG  . TRP A 10  ? 0.9162 1.1523 0.8740 -0.0167 0.0746  -0.0059 306 TRP A CG  
70   C CD1 . TRP A 10  ? 0.8792 1.0884 0.8513 -0.0360 0.0657  -0.0039 306 TRP A CD1 
71   C CD2 . TRP A 10  ? 0.9312 1.1661 0.8700 -0.0411 0.0826  0.0000  306 TRP A CD2 
72   N NE1 . TRP A 10  ? 0.8239 1.0097 0.7827 -0.0682 0.0673  0.0024  306 TRP A NE1 
73   C CE2 . TRP A 10  ? 0.9494 1.1484 0.8867 -0.0736 0.0775  0.0053  306 TRP A CE2 
74   C CE3 . TRP A 10  ? 0.8555 1.1134 0.7738 -0.0378 0.0940  0.0014  306 TRP A CE3 
75   C CZ2 . TRP A 10  ? 0.9359 1.1131 0.8469 -0.1031 0.0826  0.0123  306 TRP A CZ2 
76   C CZ3 . TRP A 10  ? 0.9325 1.1762 0.8305 -0.0700 0.0997  0.0086  306 TRP A CZ3 
77   C CH2 . TRP A 10  ? 0.8634 1.0639 0.7558 -0.1028 0.0937  0.0142  306 TRP A CH2 
78   N N   . GLU A 11  ? 1.0507 1.3917 1.0202 0.1043  0.0776  -0.0258 307 GLU A N   
79   C CA  . GLU A 11  ? 1.0660 1.4175 1.0119 0.1543  0.0796  -0.0321 307 GLU A CA  
80   C C   . GLU A 11  ? 1.1148 1.5764 1.0793 0.1695  0.0932  -0.0329 307 GLU A C   
81   O O   . GLU A 11  ? 1.1729 1.6610 1.1121 0.2124  0.1002  -0.0372 307 GLU A O   
82   C CB  . GLU A 11  ? 0.9900 1.2906 0.9288 0.1724  0.0670  -0.0353 307 GLU A CB  
83   C CG  . GLU A 11  ? 0.9935 1.2515 0.8818 0.2238  0.0647  -0.0417 307 GLU A CG  
84   C CD  . GLU A 11  ? 1.2291 1.4714 1.1118 0.2476  0.0570  -0.0444 307 GLU A CD  
85   O OE1 . GLU A 11  ? 1.3364 1.5949 1.1902 0.2953  0.0607  -0.0489 307 GLU A OE1 
86   O OE2 . GLU A 11  ? 1.2267 1.4406 1.1304 0.2214  0.0476  -0.0419 307 GLU A OE2 
87   N N   . THR A 12  ? 1.0513 1.5800 1.0565 0.1346  0.0970  -0.0291 308 THR A N   
88   C CA  . THR A 12  ? 0.9596 1.6065 0.9882 0.1423  0.1082  -0.0297 308 THR A CA  
89   C C   . THR A 12  ? 1.0016 1.7202 1.0454 0.1004  0.1212  -0.0243 308 THR A C   
90   O O   . THR A 12  ? 1.0513 1.8809 1.1111 0.1067  0.1324  -0.0246 308 THR A O   
91   C CB  . THR A 12  ? 0.8077 1.4871 0.8677 0.1352  0.1017  -0.0304 308 THR A CB  
92   O OG1 . THR A 12  ? 0.6360 1.2891 0.7174 0.0799  0.0966  -0.0255 308 THR A OG1 
93   C CG2 . THR A 12  ? 0.7661 1.3763 0.8063 0.1757  0.0898  -0.0350 308 THR A CG2 
94   N N   . ASP A 13  ? 1.0005 1.6615 1.0364 0.0584  0.1200  -0.0189 309 ASP A N   
95   C CA  . ASP A 13  ? 1.0184 1.7282 1.0596 0.0101  0.1311  -0.0125 309 ASP A CA  
96   C C   . ASP A 13  ? 1.0261 1.8046 1.0983 -0.0305 0.1326  -0.0100 309 ASP A C   
97   O O   . ASP A 13  ? 1.0580 1.9077 1.1352 -0.0687 0.1439  -0.0055 309 ASP A O   
98   C CB  . ASP A 13  ? 1.1137 1.8987 1.1430 0.0290  0.1469  -0.0127 309 ASP A CB  
99   C CG  . ASP A 13  ? 1.1461 1.8552 1.1378 0.0430  0.1474  -0.0122 309 ASP A CG  
100  O OD1 . ASP A 13  ? 1.1553 1.7990 1.1341 0.0051  0.1443  -0.0067 309 ASP A OD1 
101  O OD2 . ASP A 13  ? 1.1618 1.8736 1.1324 0.0938  0.1504  -0.0177 309 ASP A OD2 
102  N N   . VAL A 14  ? 1.0264 1.7838 1.1160 -0.0256 0.1214  -0.0128 310 VAL A N   
103  C CA  . VAL A 14  ? 1.0054 1.8190 1.1216 -0.0621 0.1204  -0.0116 310 VAL A CA  
104  C C   . VAL A 14  ? 1.0102 1.7440 1.1149 -0.1144 0.1141  -0.0066 310 VAL A C   
105  O O   . VAL A 14  ? 1.0272 1.6586 1.1149 -0.1073 0.1048  -0.0061 310 VAL A O   
106  C CB  . VAL A 14  ? 0.9734 1.8016 1.1098 -0.0262 0.1113  -0.0174 310 VAL A CB  
107  C CG1 . VAL A 14  ? 0.9762 1.8297 1.1350 -0.0671 0.1062  -0.0164 310 VAL A CG1 
108  C CG2 . VAL A 14  ? 0.9604 1.8853 1.1038 0.0234  0.1189  -0.0218 310 VAL A CG2 
109  N N   . VAL A 15  ? 0.9923 1.7729 1.1016 -0.1672 0.1187  -0.0029 311 VAL A N   
110  C CA  . VAL A 15  ? 1.0191 1.7198 1.1060 -0.2169 0.1132  0.0018  311 VAL A CA  
111  C C   . VAL A 15  ? 1.0871 1.8186 1.1900 -0.2473 0.1080  0.0002  311 VAL A C   
112  O O   . VAL A 15  ? 1.1295 1.9696 1.2575 -0.2535 0.1133  -0.0018 311 VAL A O   
113  C CB  . VAL A 15  ? 1.0359 1.7333 1.0909 -0.2633 0.1238  0.0091  311 VAL A CB  
114  C CG1 . VAL A 15  ? 1.0576 1.6335 1.0735 -0.2944 0.1159  0.0137  311 VAL A CG1 
115  C CG2 . VAL A 15  ? 1.0721 1.7899 1.1194 -0.2327 0.1333  0.0098  311 VAL A CG2 
116  N N   . LEU A 16  ? 1.1340 1.7718 1.2201 -0.2652 0.0974  0.0009  312 LEU A N   
117  C CA  . LEU A 16  ? 1.1177 1.7622 1.2072 -0.2996 0.0916  -0.0004 312 LEU A CA  
118  C C   . LEU A 16  ? 1.1390 1.6850 1.1807 -0.3459 0.0883  0.0045  312 LEU A C   
119  O O   . LEU A 16  ? 1.0241 1.4847 1.0364 -0.3376 0.0868  0.0080  312 LEU A O   
120  C CB  . LEU A 16  ? 1.0511 1.6783 1.1666 -0.2617 0.0800  -0.0063 312 LEU A CB  
121  C CG  . LEU A 16  ? 1.0629 1.7964 1.2185 -0.2311 0.0814  -0.0113 312 LEU A CG  
122  C CD1 . LEU A 16  ? 0.9183 1.6129 1.0901 -0.1891 0.0700  -0.0160 312 LEU A CD1 
123  C CD2 . LEU A 16  ? 1.1376 1.9635 1.3043 -0.2758 0.0849  -0.0116 312 LEU A CD2 
124  N N   . THR A 17  ? 1.2129 1.7686 1.2418 -0.3937 0.0865  0.0045  313 THR A N   
125  C CA  . THR A 17  ? 1.2807 1.7400 1.2513 -0.4417 0.0838  0.0090  313 THR A CA  
126  C C   . THR A 17  ? 1.2418 1.6296 1.2036 -0.4365 0.0707  0.0049  313 THR A C   
127  O O   . THR A 17  ? 1.2935 1.7334 1.2783 -0.4463 0.0670  0.0003  313 THR A O   
128  C CB  . THR A 17  ? 1.4137 1.9093 1.3534 -0.4931 0.0870  0.0105  313 THR A CB  
129  O OG1 . THR A 17  ? 1.4463 2.0209 1.3991 -0.4888 0.0974  0.0128  313 THR A OG1 
130  C CG2 . THR A 17  ? 1.5153 1.8911 1.3791 -0.5347 0.0835  0.0150  313 THR A CG2 
131  N N   . ASP A 18  ? 1.1671 1.4401 1.0937 -0.4202 0.0637  0.0066  314 ASP A N   
132  C CA  . ASP A 18  ? 1.0650 1.2651 0.9771 -0.4113 0.0519  0.0030  314 ASP A CA  
133  C C   . ASP A 18  ? 1.1761 1.2983 1.0180 -0.4648 0.0503  0.0057  314 ASP A C   
134  O O   . ASP A 18  ? 1.2678 1.3115 1.0536 -0.4799 0.0524  0.0115  314 ASP A O   
135  C CB  . ASP A 18  ? 0.9526 1.0794 0.8642 -0.3603 0.0447  0.0031  314 ASP A CB  
136  C CG  . ASP A 18  ? 0.9631 1.0545 0.8837 -0.3370 0.0338  -0.0020 314 ASP A CG  
137  O OD1 . ASP A 18  ? 0.9808 1.0085 0.8568 -0.3614 0.0290  -0.0025 314 ASP A OD1 
138  O OD2 . ASP A 18  ? 0.9159 1.0409 0.8833 -0.2954 0.0301  -0.0054 314 ASP A OD2 
139  N N   . THR A 19  ? 1.1755 1.3158 1.0143 -0.4944 0.0464  0.0015  315 THR A N   
140  C CA  . THR A 19  ? 1.2527 1.2925 1.0168 -0.5278 0.0403  0.0016  315 THR A CA  
141  C C   . THR A 19  ? 1.1781 1.1671 0.9413 -0.5081 0.0294  -0.0043 315 THR A C   
142  O O   . THR A 19  ? 1.2082 1.0948 0.9023 -0.5222 0.0234  -0.0046 315 THR A O   
143  C CB  . THR A 19  ? 1.2936 1.3771 1.0322 -0.5691 0.0417  0.0005  315 THR A CB  
144  O OG1 . THR A 19  ? 1.2199 1.4325 1.0269 -0.5597 0.0433  -0.0039 315 THR A OG1 
145  C CG2 . THR A 19  ? 1.3213 1.3960 1.0177 -0.5981 0.0492  0.0065  315 THR A CG2 
146  N N   . LEU A 20  ? 1.0251 1.0788 0.8571 -0.4632 0.0261  -0.0092 316 LEU A N   
147  C CA  . LEU A 20  ? 1.1060 1.1188 0.9401 -0.4368 0.0160  -0.0148 316 LEU A CA  
148  C C   . LEU A 20  ? 1.1708 1.0648 0.9552 -0.4085 0.0102  -0.0131 316 LEU A C   
149  O O   . LEU A 20  ? 1.2503 1.0803 1.0029 -0.4016 0.0026  -0.0168 316 LEU A O   
150  C CB  . LEU A 20  ? 0.9872 1.0836 0.8996 -0.3902 0.0144  -0.0186 316 LEU A CB  
151  C CG  . LEU A 20  ? 0.9147 0.9963 0.8406 -0.3668 0.0054  -0.0244 316 LEU A CG  
152  C CD1 . LEU A 20  ? 0.8847 0.9874 0.7944 -0.4109 0.0026  -0.0289 316 LEU A CD1 
153  C CD2 . LEU A 20  ? 0.7994 0.9492 0.7930 -0.3191 0.0046  -0.0263 316 LEU A CD2 
154  N N   . HIS A 21  ? 1.0059 0.8717 0.7805 -0.3900 0.0137  -0.0075 317 HIS A N   
155  C CA  . HIS A 21  ? 1.0166 0.7819 0.7468 -0.3573 0.0079  -0.0055 317 HIS A CA  
156  C C   . HIS A 21  ? 1.1600 0.8123 0.7949 -0.3881 0.0047  -0.0043 317 HIS A C   
157  O O   . HIS A 21  ? 1.2972 0.8626 0.8882 -0.3563 -0.0020 -0.0046 317 HIS A O   
158  C CB  . HIS A 21  ? 1.0646 0.8308 0.8031 -0.3349 0.0120  0.0002  317 HIS A CB  
159  C CG  . HIS A 21  ? 1.1448 0.8882 0.8361 -0.3771 0.0198  0.0065  317 HIS A CG  
160  N ND1 . HIS A 21  ? 1.2046 1.0347 0.9265 -0.4103 0.0295  0.0080  317 HIS A ND1 
161  C CD2 . HIS A 21  ? 1.2931 0.9371 0.9048 -0.3909 0.0197  0.0120  317 HIS A CD2 
162  C CE1 . HIS A 21  ? 1.2613 1.0498 0.9271 -0.4469 0.0356  0.0144  317 HIS A CE1 
163  N NE2 . HIS A 21  ? 1.3255 0.9959 0.9214 -0.4364 0.0296  0.0171  317 HIS A NE2 
164  N N   . LEU A 22  ? 1.1792 0.8304 0.7763 -0.4490 0.0094  -0.0030 318 LEU A N   
165  C CA  . LEU A 22  ? 1.4589 0.9939 0.9551 -0.4848 0.0055  -0.0027 318 LEU A CA  
166  C C   . LEU A 22  ? 1.4823 0.9734 0.9622 -0.4664 -0.0040 -0.0102 318 LEU A C   
167  O O   . LEU A 22  ? 1.6453 1.0231 1.0424 -0.4562 -0.0097 -0.0104 318 LEU A O   
168  C CB  . LEU A 22  ? 1.4705 1.0518 0.9472 -0.5359 0.0112  -0.0010 318 LEU A CB  
169  C CG  . LEU A 22  ? 1.4019 1.0410 0.8901 -0.5608 0.0213  0.0051  318 LEU A CG  
170  C CD1 . LEU A 22  ? 1.3529 1.0444 0.8214 -0.6110 0.0244  0.0043  318 LEU A CD1 
171  C CD2 . LEU A 22  ? 1.4716 1.0090 0.8924 -0.5520 0.0222  0.0118  318 LEU A CD2 
172  N N   . LYS A 23  ? 1.3735 0.9583 0.9299 -0.4536 -0.0057 -0.0161 319 LYS A N   
173  C CA  . LYS A 23  ? 1.4041 0.9575 0.9509 -0.4354 -0.0141 -0.0233 319 LYS A CA  
174  C C   . LYS A 23  ? 1.4721 0.9879 1.0284 -0.3666 -0.0193 -0.0241 319 LYS A C   
175  O O   . LYS A 23  ? 1.5572 1.0382 1.0980 -0.3452 -0.0259 -0.0296 319 LYS A O   
176  C CB  . LYS A 23  ? 1.2440 0.9126 0.8671 -0.4455 -0.0141 -0.0287 319 LYS A CB  
177  C CG  . LYS A 23  ? 1.2873 1.0064 0.9002 -0.5046 -0.0107 -0.0288 319 LYS A CG  
178  C CD  . LYS A 23  ? 1.4987 1.1412 1.0362 -0.5243 -0.0164 -0.0316 319 LYS A CD  
179  C CE  . LYS A 23  ? 1.4820 1.1291 1.0430 -0.5037 -0.0246 -0.0403 319 LYS A CE  
180  N NZ  . LYS A 23  ? 1.3598 1.1309 0.9906 -0.5175 -0.0240 -0.0436 319 LYS A NZ  
181  N N   . SER A 24  ? 1.4134 0.9397 0.9935 -0.3329 -0.0167 -0.0188 320 SER A N   
182  C CA  . SER A 24  ? 1.4939 0.9993 1.0863 -0.2708 -0.0218 -0.0191 320 SER A CA  
183  C C   . SER A 24  ? 1.6635 1.0444 1.1613 -0.2537 -0.0281 -0.0200 320 SER A C   
184  O O   . SER A 24  ? 1.7237 1.0159 1.1357 -0.2889 -0.0281 -0.0187 320 SER A O   
185  C CB  . SER A 24  ? 1.5207 1.0564 1.1466 -0.2446 -0.0186 -0.0131 320 SER A CB  
186  O OG  . SER A 24  ? 1.5691 1.0796 1.1945 -0.1895 -0.0246 -0.0131 320 SER A OG  
187  N N   . THR A 25  ? 1.7331 1.1073 1.2427 -0.1979 -0.0335 -0.0221 321 THR A N   
188  C CA  . THR A 25  ? 1.8938 1.1642 1.3204 -0.1719 -0.0400 -0.0251 321 THR A CA  
189  C C   . THR A 25  ? 1.7905 1.0521 1.2188 -0.1068 -0.0439 -0.0228 321 THR A C   
190  O O   . THR A 25  ? 1.8031 0.9715 1.1504 -0.0855 -0.0469 -0.0200 321 THR A O   
191  C CB  . THR A 25  ? 1.9355 1.2189 1.3717 -0.1766 -0.0432 -0.0332 321 THR A CB  
192  O OG1 . THR A 25  ? 1.9672 1.1698 1.3393 -0.1334 -0.0494 -0.0369 321 THR A OG1 
193  C CG2 . THR A 25  ? 1.7951 1.2064 1.3435 -0.1644 -0.0414 -0.0350 321 THR A CG2 
194  N N   . LEU A 26  ? 1.6852 1.0441 1.2013 -0.0763 -0.0442 -0.0236 322 LEU A N   
195  C CA  . LEU A 26  ? 1.6865 1.0587 1.2139 -0.0184 -0.0483 -0.0217 322 LEU A CA  
196  C C   . LEU A 26  ? 1.5959 0.9786 1.1316 -0.0127 -0.0468 -0.0146 322 LEU A C   
197  O O   . LEU A 26  ? 1.4476 0.8562 1.0071 -0.0505 -0.0414 -0.0114 322 LEU A O   
198  C CB  . LEU A 26  ? 1.6407 1.1137 1.2553 0.0033  -0.0489 -0.0245 322 LEU A CB  
199  C CG  . LEU A 26  ? 1.7229 1.1961 1.3280 0.0558  -0.0541 -0.0275 322 LEU A CG  
200  C CD1 . LEU A 26  ? 1.7000 1.2699 1.3878 0.0596  -0.0532 -0.0302 322 LEU A CD1 
201  C CD2 . LEU A 26  ? 1.7156 1.1852 1.3047 0.1022  -0.0579 -0.0230 322 LEU A CD2 
202  N N   . GLU A 27  ? 1.5991 0.9658 1.1138 0.0371  -0.0519 -0.0123 323 GLU A N   
203  C CA  . GLU A 27  ? 1.6109 0.9867 1.1294 0.0493  -0.0523 -0.0059 323 GLU A CA  
204  C C   . GLU A 27  ? 1.4838 0.9739 1.0991 0.0603  -0.0523 -0.0050 323 GLU A C   
205  O O   . GLU A 27  ? 1.3789 0.9324 1.0476 0.0708  -0.0533 -0.0087 323 GLU A O   
206  C CB  . GLU A 27  ? 1.7069 1.0072 1.1463 0.0987  -0.0588 -0.0036 323 GLU A CB  
207  C CG  . GLU A 27  ? 1.8994 1.0668 1.2267 0.0817  -0.0586 -0.0024 323 GLU A CG  
208  C CD  . GLU A 27  ? 2.1440 1.2233 1.3793 0.1389  -0.0659 -0.0018 323 GLU A CD  
209  O OE1 . GLU A 27  ? 2.1933 1.2920 1.4330 0.1830  -0.0702 -0.0066 323 GLU A OE1 
210  O OE2 . GLU A 27  ? 2.2665 1.2571 1.4217 0.1418  -0.0671 0.0035  323 GLU A OE2 
211  N N   . THR A 28  ? 1.3338 0.8440 0.9651 0.0558  -0.0512 0.0001  324 THR A N   
212  C CA  . THR A 28  ? 1.1469 0.7516 0.8599 0.0523  -0.0502 0.0011  324 THR A CA  
213  C C   . THR A 28  ? 1.1471 0.7880 0.8746 0.0916  -0.0571 0.0039  324 THR A C   
214  O O   . THR A 28  ? 1.0881 0.8064 0.8795 0.0905  -0.0580 0.0037  324 THR A O   
215  C CB  . THR A 28  ? 1.0042 0.6157 0.7299 0.0133  -0.0433 0.0040  324 THR A CB  
216  O OG1 . THR A 28  ? 1.1357 0.6852 0.8023 0.0184  -0.0441 0.0093  324 THR A OG1 
217  C CG2 . THR A 28  ? 1.0850 0.6800 0.8027 -0.0290 -0.0366 0.0014  324 THR A CG2 
218  N N   . GLY A 29  ? 1.2409 0.8275 0.9067 0.1255  -0.0624 0.0065  325 GLY A N   
219  C CA  . GLY A 29  ? 1.2464 0.8677 0.9191 0.1602  -0.0694 0.0099  325 GLY A CA  
220  C C   . GLY A 29  ? 1.2849 0.8706 0.9279 0.1509  -0.0688 0.0154  325 GLY A C   
221  O O   . GLY A 29  ? 1.2891 0.8696 0.9051 0.1850  -0.0756 0.0189  325 GLY A O   
222  N N   . CYS A 30  ? 1.2693 0.8353 0.9157 0.1065  -0.0607 0.0163  326 CYS A N   
223  C CA  . CYS A 30  ? 1.2424 0.7755 0.8596 0.0941  -0.0585 0.0217  326 CYS A CA  
224  C C   . CYS A 30  ? 1.3259 0.7472 0.8463 0.0955  -0.0579 0.0250  326 CYS A C   
225  O O   . CYS A 30  ? 1.3038 0.6727 0.7879 0.0806  -0.0550 0.0226  326 CYS A O   
226  C CB  . CYS A 30  ? 1.1655 0.7348 0.8277 0.0481  -0.0494 0.0214  326 CYS A CB  
227  S SG  . CYS A 30  ? 0.9917 0.6724 0.7515 0.0457  -0.0503 0.0174  326 CYS A SG  
228  N N   . THR A 31  ? 1.3790 0.7592 0.8515 0.1142  -0.0614 0.0307  327 THR A N   
229  C CA  . THR A 31  ? 1.5412 0.8052 0.9122 0.1115  -0.0604 0.0355  327 THR A CA  
230  C C   . THR A 31  ? 1.5088 0.7606 0.8739 0.0693  -0.0524 0.0407  327 THR A C   
231  O O   . THR A 31  ? 1.4565 0.7893 0.8943 0.0500  -0.0483 0.0399  327 THR A O   
232  C CB  . THR A 31  ? 1.6076 0.8284 0.9177 0.1718  -0.0711 0.0384  327 THR A CB  
233  O OG1 . THR A 31  ? 1.5095 0.7821 0.8491 0.1874  -0.0752 0.0423  327 THR A OG1 
234  C CG2 . THR A 31  ? 1.5276 0.7919 0.8618 0.2157  -0.0781 0.0329  327 THR A CG2 
235  N N   . GLU A 32  ? 1.6665 0.8128 0.9386 0.0545  -0.0497 0.0462  328 GLU A N   
236  C CA  . GLU A 32  ? 1.7983 0.9336 1.0591 0.0143  -0.0413 0.0521  328 GLU A CA  
237  C C   . GLU A 32  ? 1.6540 0.8381 0.9456 0.0398  -0.0453 0.0553  328 GLU A C   
238  O O   . GLU A 32  ? 1.5921 0.7983 0.9003 0.0095  -0.0378 0.0586  328 GLU A O   
239  C CB  . GLU A 32  ? 2.0922 1.0960 1.2354 -0.0064 -0.0384 0.0585  328 GLU A CB  
240  C CG  . GLU A 32  ? 2.2467 1.2023 1.3557 -0.0535 -0.0322 0.0559  328 GLU A CG  
241  C CD  . GLU A 32  ? 2.3839 1.2612 1.4292 -0.0208 -0.0405 0.0522  328 GLU A CD  
242  O OE1 . GLU A 32  ? 2.5105 1.2917 1.4704 -0.0505 -0.0383 0.0523  328 GLU A OE1 
243  O OE2 . GLU A 32  ? 2.3407 1.2610 1.4220 0.0341  -0.0490 0.0479  328 GLU A OE2 
244  N N   . HIS A 33  ? 1.5370 0.7452 0.8378 0.0944  -0.0569 0.0542  329 HIS A N   
245  C CA  . HIS A 33  ? 1.4982 0.7450 0.8152 0.1214  -0.0633 0.0573  329 HIS A CA  
246  C C   . HIS A 33  ? 1.4840 0.8423 0.8887 0.1468  -0.0708 0.0518  329 HIS A C   
247  O O   . HIS A 33  ? 1.6177 1.0127 1.0328 0.1753  -0.0793 0.0536  329 HIS A O   
248  C CB  . HIS A 33  ? 1.7385 0.8968 0.9592 0.1648  -0.0718 0.0634  329 HIS A CB  
249  C CG  . HIS A 33  ? 1.9717 0.9999 1.0877 0.1440  -0.0663 0.0683  329 HIS A CG  
250  N ND1 . HIS A 33  ? 2.0314 0.9969 1.1028 0.1419  -0.0656 0.0652  329 HIS A ND1 
251  C CD2 . HIS A 33  ? 2.0450 0.9898 1.0862 0.1209  -0.0612 0.0762  329 HIS A CD2 
252  C CE1 . HIS A 33  ? 2.1429 0.9885 1.1136 0.1163  -0.0609 0.0709  329 HIS A CE1 
253  N NE2 . HIS A 33  ? 2.1585 0.9903 1.1095 0.1023  -0.0578 0.0780  329 HIS A NE2 
254  N N   . ILE A 34  ? 1.3038 0.7172 0.7690 0.1341  -0.0683 0.0454  330 ILE A N   
255  C CA  . ILE A 34  ? 1.2287 0.7453 0.7745 0.1484  -0.0743 0.0407  330 ILE A CA  
256  C C   . ILE A 34  ? 1.1316 0.6949 0.7395 0.1148  -0.0668 0.0351  330 ILE A C   
257  O O   . ILE A 34  ? 1.3163 0.8401 0.9048 0.0985  -0.0611 0.0333  330 ILE A O   
258  C CB  . ILE A 34  ? 1.3626 0.8988 0.8981 0.2012  -0.0861 0.0396  330 ILE A CB  
259  C CG1 . ILE A 34  ? 1.2656 0.9087 0.8720 0.2120  -0.0937 0.0374  330 ILE A CG1 
260  C CG2 . ILE A 34  ? 1.5308 1.0558 1.0652 0.2073  -0.0844 0.0351  330 ILE A CG2 
261  C CD1 . ILE A 34  ? 1.3907 1.0691 0.9864 0.2642  -0.1057 0.0376  330 ILE A CD1 
262  N N   . CYS A 35  ? 0.9864 0.6302 0.6638 0.1042  -0.0673 0.0322  331 CYS A N   
263  C CA  . CYS A 35  ? 1.0353 0.7250 0.7700 0.0753  -0.0606 0.0273  331 CYS A CA  
264  C C   . CYS A 35  ? 0.9940 0.7556 0.7812 0.0923  -0.0681 0.0235  331 CYS A C   
265  O O   . CYS A 35  ? 0.7732 0.5803 0.5822 0.1027  -0.0753 0.0239  331 CYS A O   
266  C CB  . CYS A 35  ? 0.9614 0.6725 0.7220 0.0442  -0.0529 0.0273  331 CYS A CB  
267  S SG  . CYS A 35  ? 0.8641 0.6336 0.6908 0.0181  -0.0460 0.0211  331 CYS A SG  
268  N N   . MET A 36  ? 0.8707 0.6422 0.6744 0.0922  -0.0666 0.0199  332 MET A N   
269  C CA  . MET A 36  ? 0.9820 0.8193 0.8307 0.1057  -0.0725 0.0168  332 MET A CA  
270  C C   . MET A 36  ? 0.8323 0.7128 0.7348 0.0771  -0.0674 0.0131  332 MET A C   
271  O O   . MET A 36  ? 0.7252 0.6494 0.6600 0.0817  -0.0701 0.0105  332 MET A O   
272  C CB  . MET A 36  ? 1.2377 1.0566 1.0622 0.1323  -0.0751 0.0154  332 MET A CB  
273  C CG  . MET A 36  ? 1.3916 1.1702 1.1574 0.1716  -0.0819 0.0188  332 MET A CG  
274  S SD  . MET A 36  ? 1.4447 1.2690 1.2150 0.2171  -0.0897 0.0166  332 MET A SD  
275  C CE  . MET A 36  ? 1.4918 1.2974 1.2058 0.2660  -0.0996 0.0214  332 MET A CE  
276  N N   . GLY A 37  ? 0.8376 0.7078 0.7471 0.0500  -0.0600 0.0129  333 GLY A N   
277  C CA  . GLY A 37  ? 0.9000 0.8039 0.8515 0.0284  -0.0548 0.0093  333 GLY A CA  
278  C C   . GLY A 37  ? 0.8102 0.7688 0.8015 0.0293  -0.0604 0.0074  333 GLY A C   
279  O O   . GLY A 37  ? 0.8324 0.8105 0.8508 0.0148  -0.0566 0.0046  333 GLY A O   
280  N N   . SER A 38  ? 0.7397 0.7239 0.7315 0.0445  -0.0697 0.0091  334 SER A N   
281  C CA  . SER A 38  ? 0.6525 0.6873 0.6751 0.0376  -0.0756 0.0079  334 SER A CA  
282  C C   . SER A 38  ? 0.7538 0.8313 0.7862 0.0555  -0.0833 0.0086  334 SER A C   
283  O O   . SER A 38  ? 0.7131 0.8388 0.7681 0.0465  -0.0890 0.0085  334 SER A O   
284  C CB  . SER A 38  ? 0.6790 0.7195 0.6962 0.0294  -0.0801 0.0087  334 SER A CB  
285  O OG  . SER A 38  ? 0.8587 0.9023 0.8544 0.0479  -0.0876 0.0118  334 SER A OG  
286  N N   . ILE A 39  ? 0.8073 0.8675 0.8190 0.0798  -0.0833 0.0094  335 ILE A N   
287  C CA  . ILE A 39  ? 0.8117 0.9143 0.8317 0.1017  -0.0883 0.0094  335 ILE A CA  
288  C C   . ILE A 39  ? 0.8914 1.0026 0.9351 0.0900  -0.0828 0.0065  335 ILE A C   
289  O O   . ILE A 39  ? 0.9079 0.9735 0.9409 0.0835  -0.0756 0.0046  335 ILE A O   
290  C CB  . ILE A 39  ? 0.7770 0.8471 0.7544 0.1384  -0.0905 0.0109  335 ILE A CB  
291  C CG1 . ILE A 39  ? 0.7086 0.7416 0.6501 0.1472  -0.0934 0.0141  335 ILE A CG1 
292  C CG2 . ILE A 39  ? 0.7982 0.9296 0.7834 0.1683  -0.0976 0.0113  335 ILE A CG2 
293  C CD1 . ILE A 39  ? 0.8324 0.9203 0.7913 0.1444  -0.1021 0.0160  335 ILE A CD1 
294  N N   . MET A 40  ? 0.9490 1.1211 1.0228 0.0852  -0.0864 0.0064  336 MET A N   
295  C CA  . MET A 40  ? 0.9994 1.1818 1.0968 0.0696  -0.0815 0.0043  336 MET A CA  
296  C C   . MET A 40  ? 1.0152 1.1746 1.0997 0.0889  -0.0774 0.0021  336 MET A C   
297  O O   . MET A 40  ? 1.0935 1.2196 1.1789 0.0762  -0.0710 -0.0004 336 MET A O   
298  C CB  . MET A 40  ? 0.9841 1.2354 1.1089 0.0585  -0.0865 0.0057  336 MET A CB  
299  C CG  . MET A 40  ? 1.0304 1.2885 1.1638 0.0275  -0.0892 0.0066  336 MET A CG  
300  S SD  . MET A 40  ? 1.1122 1.4166 1.2686 -0.0007 -0.0905 0.0076  336 MET A SD  
301  C CE  . MET A 40  ? 0.9674 1.2494 1.1317 0.0089  -0.0817 0.0051  336 MET A CE  
302  N N   . LEU A 41  ? 1.0682 1.2471 1.1377 0.1211  -0.0814 0.0028  337 LEU A N   
303  C CA  . LEU A 41  ? 1.1062 1.2617 1.1553 0.1443  -0.0785 0.0002  337 LEU A CA  
304  C C   . LEU A 41  ? 1.2400 1.3572 1.2401 0.1814  -0.0819 0.0009  337 LEU A C   
305  O O   . LEU A 41  ? 1.2572 1.4194 1.2517 0.2133  -0.0879 0.0025  337 LEU A O   
306  C CB  . LEU A 41  ? 1.0360 1.2591 1.1114 0.1529  -0.0796 -0.0002 337 LEU A CB  
307  C CG  . LEU A 41  ? 0.9846 1.2787 1.1022 0.1257  -0.0820 0.0024  337 LEU A CG  
308  C CD1 . LEU A 41  ? 1.0354 1.4085 1.1703 0.1408  -0.0842 0.0035  337 LEU A CD1 
309  C CD2 . LEU A 41  ? 0.9155 1.1882 1.0532 0.0886  -0.0770 0.0013  337 LEU A CD2 
310  N N   . PRO A 42  ? 1.3720 1.4078 1.3320 0.1781  -0.0786 0.0002  338 PRO A N   
311  C CA  . PRO A 42  ? 1.4859 1.4656 1.3843 0.2144  -0.0815 0.0009  338 PRO A CA  
312  C C   . PRO A 42  ? 1.5259 1.4643 1.3885 0.2357  -0.0794 -0.0030 338 PRO A C   
313  O O   . PRO A 42  ? 1.5015 1.4306 1.3792 0.2132  -0.0742 -0.0064 338 PRO A O   
314  C CB  . PRO A 42  ? 1.4989 1.4063 1.3670 0.1912  -0.0782 0.0026  338 PRO A CB  
315  C CG  . PRO A 42  ? 1.4040 1.3467 1.3252 0.1485  -0.0742 0.0027  338 PRO A CG  
316  C CD  . PRO A 42  ? 1.3032 1.2993 1.2688 0.1403  -0.0727 -0.0002 338 PRO A CD  
317  N N   . SER A 43  ? 1.6216 1.5344 1.4319 0.2828  -0.0840 -0.0027 339 SER A N   
318  C CA  . SER A 43  ? 1.6113 1.4713 1.3718 0.3102  -0.0828 -0.0069 339 SER A CA  
319  C C   . SER A 43  ? 1.6447 1.3924 1.3141 0.3322  -0.0846 -0.0063 339 SER A C   
320  O O   . SER A 43  ? 1.6216 1.2962 1.2642 0.2972  -0.0809 -0.0056 339 SER A O   
321  C CB  . SER A 43  ? 1.5574 1.4936 1.3314 0.3554  -0.0863 -0.0081 339 SER A CB  
322  O OG  . SER A 43  ? 1.4851 1.3864 1.2290 0.3723  -0.0834 -0.0133 339 SER A OG  
323  N N   . VAL A 52  ? 2.2182 1.7524 1.5248 0.5861  -0.0655 -0.0805 348 VAL A N   
324  C CA  . VAL A 52  ? 2.2457 1.6810 1.5145 0.5504  -0.0661 -0.0885 348 VAL A CA  
325  C C   . VAL A 52  ? 2.3449 1.6539 1.5477 0.5163  -0.0708 -0.0883 348 VAL A C   
326  O O   . VAL A 52  ? 2.4256 1.6954 1.5766 0.5360  -0.0745 -0.0821 348 VAL A O   
327  C CB  . VAL A 52  ? 2.2803 1.6744 1.4811 0.5774  -0.0672 -0.0925 348 VAL A CB  
328  C CG1 . VAL A 52  ? 2.4067 1.6987 1.4911 0.6082  -0.0740 -0.0886 348 VAL A CG1 
329  C CG2 . VAL A 52  ? 2.2357 1.5687 1.4262 0.5357  -0.0666 -0.1021 348 VAL A CG2 
330  N N   . ALA A 53  ? 2.2929 1.5439 1.4969 0.4617  -0.0705 -0.0952 349 ALA A N   
331  C CA  . ALA A 53  ? 2.3113 1.4478 1.4525 0.4151  -0.0744 -0.0946 349 ALA A CA  
332  C C   . ALA A 53  ? 2.3729 1.4000 1.4180 0.3978  -0.0784 -0.0978 349 ALA A C   
333  O O   . ALA A 53  ? 2.4757 1.5111 1.5316 0.3854  -0.0774 -0.1057 349 ALA A O   
334  C CB  . ALA A 53  ? 2.1615 1.3554 1.3905 0.3406  -0.0722 -0.0906 349 ALA A CB  
335  N N   . THR A 54  ? 2.3094 1.2342 1.2582 0.3960  -0.0832 -0.0909 350 THR A N   
336  C CA  . THR A 54  ? 2.3588 1.1758 1.2040 0.3871  -0.0879 -0.0908 350 THR A CA  
337  C C   . THR A 54  ? 2.3046 1.0657 1.1394 0.3077  -0.0887 -0.0949 350 THR A C   
338  O O   . THR A 54  ? 2.1924 0.9906 1.0912 0.2588  -0.0861 -0.0974 350 THR A O   
339  C CB  . THR A 54  ? 2.4304 1.1555 1.1677 0.4139  -0.0930 -0.0813 350 THR A CB  
340  O OG1 . THR A 54  ? 2.5271 1.1668 1.2177 0.3529  -0.0945 -0.0772 350 THR A OG1 
341  C CG2 . THR A 54  ? 2.3352 1.1303 1.1036 0.4688  -0.0920 -0.0767 350 THR A CG2 
342  N N   . LYS A 55  ? 2.4389 1.1133 1.1890 0.2944  -0.0929 -0.0950 351 LYS A N   
343  C CA  . LYS A 55  ? 2.5341 1.1628 1.2679 0.2183  -0.0944 -0.0981 351 LYS A CA  
344  C C   . LYS A 55  ? 2.7083 1.2565 1.3788 0.1690  -0.0961 -0.0890 351 LYS A C   
345  O O   . LYS A 55  ? 2.7031 1.2510 1.3908 0.0970  -0.0955 -0.0901 351 LYS A O   
346  C CB  . LYS A 55  ? 2.6398 1.2113 1.3076 0.2239  -0.0982 -0.1010 351 LYS A CB  
347  C CG  . LYS A 55  ? 2.7322 1.2558 1.3204 0.2983  -0.1014 -0.0954 351 LYS A CG  
348  C CD  . LYS A 55  ? 2.9234 1.3129 1.3800 0.2834  -0.1077 -0.0895 351 LYS A CD  
349  C CE  . LYS A 55  ? 3.0692 1.4068 1.4369 0.3609  -0.1119 -0.0829 351 LYS A CE  
350  N NZ  . LYS A 55  ? 3.2351 1.4325 1.4625 0.3524  -0.1187 -0.0770 351 LYS A NZ  
351  N N   . ASP A 56  ? 2.8285 1.3138 1.4230 0.2065  -0.0983 -0.0799 352 ASP A N   
352  C CA  . ASP A 56  ? 2.9503 1.3642 1.4845 0.1639  -0.0990 -0.0710 352 ASP A CA  
353  C C   . ASP A 56  ? 2.8397 1.3289 1.4680 0.1218  -0.0939 -0.0715 352 ASP A C   
354  O O   . ASP A 56  ? 2.9456 1.4053 1.5554 0.0573  -0.0927 -0.0670 352 ASP A O   
355  C CB  . ASP A 56  ? 3.0792 1.4259 1.5228 0.2220  -0.1024 -0.0629 352 ASP A CB  
356  C CG  . ASP A 56  ? 3.1930 1.4782 1.5481 0.2773  -0.1077 -0.0626 352 ASP A CG  
357  O OD1 . ASP A 56  ? 3.3251 1.5022 1.5741 0.2523  -0.1120 -0.0587 352 ASP A OD1 
358  O OD2 . ASP A 56  ? 3.1506 1.4992 1.5408 0.3451  -0.1076 -0.0657 352 ASP A OD2 
359  N N   . GLN A 57  ? 2.6085 1.1979 1.3357 0.1567  -0.0906 -0.0762 353 GLN A N   
360  C CA  . GLN A 57  ? 2.4261 1.0868 1.2419 0.1223  -0.0863 -0.0765 353 GLN A CA  
361  C C   . GLN A 57  ? 2.1491 0.8865 1.0537 0.0770  -0.0842 -0.0861 353 GLN A C   
362  O O   . GLN A 57  ? 2.0428 0.8278 1.0073 0.0308  -0.0815 -0.0858 353 GLN A O   
363  C CB  . GLN A 57  ? 2.4565 1.1832 1.3270 0.1836  -0.0845 -0.0751 353 GLN A CB  
364  C CG  . GLN A 57  ? 2.5863 1.2912 1.4000 0.2616  -0.0876 -0.0721 353 GLN A CG  
365  C CD  . GLN A 57  ? 2.5230 1.3397 1.4219 0.3199  -0.0852 -0.0764 353 GLN A CD  
366  O OE1 . GLN A 57  ? 2.4768 1.3562 1.4409 0.3142  -0.0827 -0.0844 353 GLN A OE1 
367  N NE2 . GLN A 57  ? 2.4881 1.3365 1.3862 0.3745  -0.0859 -0.0709 353 GLN A NE2 
368  N N   . LEU A 58  ? 2.0487 0.8007 0.9601 0.0895  -0.0858 -0.0944 354 LEU A N   
369  C CA  . LEU A 58  ? 1.9273 0.7622 0.9255 0.0593  -0.0847 -0.1051 354 LEU A CA  
370  C C   . LEU A 58  ? 2.0337 0.8598 1.0265 -0.0219 -0.0863 -0.1059 354 LEU A C   
371  O O   . LEU A 58  ? 1.8889 0.8057 0.9674 -0.0584 -0.0852 -0.1097 354 LEU A O   
372  C CB  . LEU A 58  ? 2.0423 0.9061 1.0530 0.1082  -0.0852 -0.1139 354 LEU A CB  
373  C CG  . LEU A 58  ? 1.9126 0.9356 1.0609 0.1129  -0.0803 -0.1113 354 LEU A CG  
374  C CD1 . LEU A 58  ? 1.8110 0.9134 1.0230 0.1608  -0.0760 -0.1029 354 LEU A CD1 
375  C CD2 . LEU A 58  ? 1.9426 0.9830 1.0906 0.1374  -0.0810 -0.1192 354 LEU A CD2 
376  N N   . PHE A 59  ? 2.1935 0.9316 1.0952 -0.0502 -0.0886 -0.0991 355 PHE A N   
377  C CA  . PHE A 59  ? 2.3075 1.0570 1.2124 -0.1288 -0.0893 -0.0987 355 PHE A CA  
378  C C   . PHE A 59  ? 2.3344 1.1149 1.2681 -0.1799 -0.0854 -0.0910 355 PHE A C   
379  O O   . PHE A 59  ? 2.3724 1.2302 1.3686 -0.2345 -0.0843 -0.0929 355 PHE A O   
380  C CB  . PHE A 59  ? 2.4903 1.1414 1.2883 -0.1486 -0.0930 -0.0944 355 PHE A CB  
381  C CG  . PHE A 59  ? 2.5381 1.2146 1.3431 -0.2287 -0.0934 -0.0936 355 PHE A CG  
382  C CD1 . PHE A 59  ? 2.5403 1.2833 1.3998 -0.2495 -0.0959 -0.1031 355 PHE A CD1 
383  C CD2 . PHE A 59  ? 2.5653 1.2094 1.3249 -0.2823 -0.0912 -0.0834 355 PHE A CD2 
384  C CE1 . PHE A 59  ? 2.5599 1.3415 1.4310 -0.3202 -0.0964 -0.1017 355 PHE A CE1 
385  C CE2 . PHE A 59  ? 2.5879 1.2711 1.3578 -0.3542 -0.0908 -0.0820 355 PHE A CE2 
386  C CZ  . PHE A 59  ? 2.5983 1.3532 1.4258 -0.3721 -0.0935 -0.0909 355 PHE A CZ  
387  N N   . PRO A 60  ? 2.3162 1.0441 1.2045 -0.1646 -0.0833 -0.0817 356 PRO A N   
388  C CA  . PRO A 60  ? 2.1246 0.8978 1.0550 -0.2060 -0.0786 -0.0753 356 PRO A CA  
389  C C   . PRO A 60  ? 1.8713 0.7641 0.9226 -0.2150 -0.0763 -0.0814 356 PRO A C   
390  O O   . PRO A 60  ? 1.8026 0.7635 0.9025 -0.2725 -0.0736 -0.0795 356 PRO A O   
391  C CB  . PRO A 60  ? 2.2016 0.9093 1.0782 -0.1611 -0.0777 -0.0676 356 PRO A CB  
392  C CG  . PRO A 60  ? 2.3304 0.9530 1.1231 -0.1014 -0.0826 -0.0685 356 PRO A CG  
393  C CD  . PRO A 60  ? 2.3888 1.0056 1.1684 -0.1222 -0.0856 -0.0749 356 PRO A CD  
394  N N   . LEU A 61  ? 1.7234 0.6476 0.8218 -0.1581 -0.0773 -0.0881 357 LEU A N   
395  C CA  . LEU A 61  ? 1.4807 0.5570 0.7140 -0.1559 -0.0728 -0.0853 357 LEU A CA  
396  C C   . LEU A 61  ? 1.6380 0.7825 0.9186 -0.1926 -0.0744 -0.0912 357 LEU A C   
397  O O   . LEU A 61  ? 1.5988 0.8506 0.9663 -0.2221 -0.0711 -0.0880 357 LEU A O   
398  C CB  . LEU A 61  ? 1.3709 0.4983 0.6551 -0.0825 -0.0712 -0.0835 357 LEU A CB  
399  C CG  . LEU A 61  ? 1.6191 0.6834 0.8521 -0.0328 -0.0712 -0.0790 357 LEU A CG  
400  C CD1 . LEU A 61  ? 1.7627 0.8477 1.0057 0.0393  -0.0721 -0.0812 357 LEU A CD1 
401  C CD2 . LEU A 61  ? 1.5727 0.7001 0.8678 -0.0396 -0.0667 -0.0696 357 LEU A CD2 
402  N N   . ALA A 62  ? 1.5928 0.6796 0.8174 -0.1858 -0.0796 -0.0999 358 ALA A N   
403  C CA  . ALA A 62  ? 1.5436 0.6881 0.8034 -0.2228 -0.0824 -0.1058 358 ALA A CA  
404  C C   . ALA A 62  ? 1.6503 0.7858 0.8830 -0.3025 -0.0843 -0.1062 358 ALA A C   
405  O O   . ALA A 62  ? 1.5468 0.7848 0.8505 -0.3383 -0.0839 -0.1066 358 ALA A O   
406  C CB  . ALA A 62  ? 1.7126 0.7860 0.9066 -0.1982 -0.0880 -0.1155 358 ALA A CB  
407  N N   . LYS A 63  ? 1.8893 0.9419 1.0417 -0.3178 -0.0819 -0.0971 359 LYS A N   
408  C CA  . LYS A 63  ? 1.9376 1.0112 1.0773 -0.3834 -0.0788 -0.0889 359 LYS A CA  
409  C C   . LYS A 63  ? 1.8446 1.0215 1.0690 -0.4087 -0.0733 -0.0845 359 LYS A C   
410  O O   . LYS A 63  ? 1.8554 1.1276 1.1335 -0.4515 -0.0716 -0.0837 359 LYS A O   
411  C CB  . LYS A 63  ? 1.9925 0.9470 1.0193 -0.3893 -0.0776 -0.0797 359 LYS A CB  
412  C CG  . LYS A 63  ? 2.0118 0.9701 1.0018 -0.4578 -0.0749 -0.0720 359 LYS A CG  
413  C CD  . LYS A 63  ? 2.1623 0.9961 1.0339 -0.4610 -0.0742 -0.0628 359 LYS A CD  
414  C CE  . LYS A 63  ? 2.1383 0.9543 0.9486 -0.5288 -0.0733 -0.0569 359 LYS A CE  
415  N NZ  . LYS A 63  ? 1.9772 0.9261 0.8746 -0.5793 -0.0681 -0.0560 359 LYS A NZ  
416  N N   . GLU A 64  ? 1.7512 0.9145 0.9877 -0.3790 -0.0702 -0.0812 360 GLU A N   
417  C CA  . GLU A 64  ? 1.6235 0.8788 0.9355 -0.3992 -0.0645 -0.0764 360 GLU A CA  
418  C C   . GLU A 64  ? 1.4991 0.8847 0.9173 -0.4031 -0.0652 -0.0815 360 GLU A C   
419  O O   . GLU A 64  ? 1.4062 0.8852 0.8748 -0.4428 -0.0617 -0.0784 360 GLU A O   
420  C CB  . GLU A 64  ? 1.6525 0.8673 0.9606 -0.3576 -0.0626 -0.0733 360 GLU A CB  
421  C CG  . GLU A 64  ? 1.6356 0.9498 1.0253 -0.3657 -0.0551 -0.0652 360 GLU A CG  
422  C CD  . GLU A 64  ? 1.6141 0.9508 1.0497 -0.3010 -0.0523 -0.0602 360 GLU A CD  
423  O OE1 . GLU A 64  ? 1.6191 0.8730 1.0002 -0.2567 -0.0556 -0.0611 360 GLU A OE1 
424  O OE2 . GLU A 64  ? 1.5189 0.9570 1.0416 -0.2937 -0.0473 -0.0557 360 GLU A OE2 
425  N N   . PHE A 65  ? 1.3982 0.8134 0.8606 -0.3480 -0.0667 -0.0842 361 PHE A N   
426  C CA  . PHE A 65  ? 1.2648 0.8085 0.8301 -0.3369 -0.0654 -0.0845 361 PHE A CA  
427  C C   . PHE A 65  ? 1.3107 0.9014 0.8805 -0.3899 -0.0694 -0.0899 361 PHE A C   
428  O O   . PHE A 65  ? 1.1578 0.8531 0.7918 -0.4141 -0.0666 -0.0874 361 PHE A O   
429  C CB  . PHE A 65  ? 1.2553 0.8045 0.8467 -0.2767 -0.0669 -0.0869 361 PHE A CB  
430  C CG  . PHE A 65  ? 1.1536 0.8170 0.8351 -0.2661 -0.0665 -0.0874 361 PHE A CG  
431  C CD1 . PHE A 65  ? 0.9750 0.7248 0.7372 -0.2452 -0.0613 -0.0809 361 PHE A CD1 
432  C CD2 . PHE A 65  ? 1.1613 0.8383 0.8396 -0.2761 -0.0718 -0.0944 361 PHE A CD2 
433  C CE1 . PHE A 65  ? 0.9702 0.8119 0.8033 -0.2334 -0.0612 -0.0809 361 PHE A CE1 
434  C CE2 . PHE A 65  ? 1.1016 0.8781 0.8567 -0.2639 -0.0717 -0.0942 361 PHE A CE2 
435  C CZ  . PHE A 65  ? 1.0043 0.8603 0.8347 -0.2417 -0.0663 -0.0872 361 PHE A CZ  
436  N N   . LEU A 66  ? 1.4101 0.9257 0.9088 -0.4065 -0.0764 -0.0978 362 LEU A N   
437  C CA  . LEU A 66  ? 1.4230 0.9906 0.9289 -0.4505 -0.0806 -0.1022 362 LEU A CA  
438  C C   . LEU A 66  ? 1.4893 1.1052 0.9966 -0.4982 -0.0739 -0.0924 362 LEU A C   
439  O O   . LEU A 66  ? 1.4705 1.1874 1.0257 -0.5224 -0.0732 -0.0916 362 LEU A O   
440  C CB  . LEU A 66  ? 1.6194 1.0923 1.0445 -0.4486 -0.0864 -0.1078 362 LEU A CB  
441  C CG  . LEU A 66  ? 1.6418 1.0758 1.0621 -0.3948 -0.0913 -0.1168 362 LEU A CG  
442  C CD1 . LEU A 66  ? 1.8047 1.1175 1.1214 -0.3924 -0.0959 -0.1215 362 LEU A CD1 
443  C CD2 . LEU A 66  ? 1.5486 1.1014 1.0593 -0.3807 -0.0922 -0.1183 362 LEU A CD2 
444  N N   . ASP A 67  ? 1.6063 1.1529 1.0577 -0.5096 -0.0689 -0.0851 363 ASP A N   
445  C CA  . ASP A 67  ? 1.7448 1.3335 1.1886 -0.5562 -0.0622 -0.0763 363 ASP A CA  
446  C C   . ASP A 67  ? 1.6582 1.3830 1.1995 -0.5568 -0.0565 -0.0733 363 ASP A C   
447  O O   . ASP A 67  ? 1.6573 1.4715 1.2252 -0.5877 -0.0532 -0.0704 363 ASP A O   
448  C CB  . ASP A 67  ? 1.8773 1.3576 1.2365 -0.5641 -0.0585 -0.0691 363 ASP A CB  
449  C CG  . ASP A 67  ? 2.0568 1.4265 1.3074 -0.5862 -0.0619 -0.0680 363 ASP A CG  
450  O OD1 . ASP A 67  ? 2.1487 1.5413 1.3708 -0.6364 -0.0598 -0.0638 363 ASP A OD1 
451  O OD2 . ASP A 67  ? 2.1334 1.3946 1.3237 -0.5523 -0.0666 -0.0711 363 ASP A OD2 
452  N N   . GLN A 68  ? 1.6114 1.3549 1.2035 -0.5206 -0.0552 -0.0738 364 GLN A N   
453  C CA  . GLN A 68  ? 1.5327 1.4022 1.2143 -0.5148 -0.0498 -0.0706 364 GLN A CA  
454  C C   . GLN A 68  ? 1.4499 1.4184 1.2033 -0.4977 -0.0539 -0.0759 364 GLN A C   
455  O O   . GLN A 68  ? 1.4639 1.5446 1.2829 -0.4935 -0.0495 -0.0727 364 GLN A O   
456  C CB  . GLN A 68  ? 1.4489 1.3018 1.1552 -0.4845 -0.0468 -0.0682 364 GLN A CB  
457  C CG  . GLN A 68  ? 1.4166 1.2611 1.1590 -0.4247 -0.0500 -0.0710 364 GLN A CG  
458  C CD  . GLN A 68  ? 1.4191 1.1934 1.1427 -0.3839 -0.0468 -0.0659 364 GLN A CD  
459  O OE1 . GLN A 68  ? 1.4714 1.1629 1.1286 -0.4026 -0.0456 -0.0633 364 GLN A OE1 
460  N NE2 . GLN A 68  ? 1.3375 1.1448 1.1160 -0.3290 -0.0459 -0.0642 364 GLN A NE2 
461  N N   . TYR A 69  ? 1.3593 1.2867 1.0963 -0.4844 -0.0623 -0.0837 365 TYR A N   
462  C CA  . TYR A 69  ? 1.2546 1.2712 1.0537 -0.4677 -0.0668 -0.0885 365 TYR A CA  
463  C C   . TYR A 69  ? 1.3380 1.4177 1.1367 -0.4987 -0.0667 -0.0874 365 TYR A C   
464  O O   . TYR A 69  ? 1.2103 1.3981 1.0714 -0.4869 -0.0663 -0.0869 365 TYR A O   
465  C CB  . TYR A 69  ? 1.1890 1.1424 0.9712 -0.4319 -0.0733 -0.0949 365 TYR A CB  
466  C CG  . TYR A 69  ? 1.1956 1.2230 1.0196 -0.4238 -0.0788 -0.0997 365 TYR A CG  
467  C CD1 . TYR A 69  ? 1.1276 1.2615 1.0330 -0.3934 -0.0761 -0.0960 365 TYR A CD1 
468  C CD2 . TYR A 69  ? 1.2272 1.2134 1.0027 -0.4462 -0.0871 -0.1079 365 TYR A CD2 
469  C CE1 . TYR A 69  ? 1.0800 1.2779 1.0182 -0.3839 -0.0814 -0.0997 365 TYR A CE1 
470  C CE2 . TYR A 69  ? 1.1899 1.2453 1.0025 -0.4384 -0.0925 -0.1120 365 TYR A CE2 
471  C CZ  . TYR A 69  ? 1.1381 1.3002 1.0327 -0.4065 -0.0896 -0.1075 365 TYR A CZ  
472  O OH  . TYR A 69  ? 1.2311 1.4593 1.1585 -0.3956 -0.0952 -0.1110 365 TYR A OH  
473  N N   . TYR A 70  ? 1.4881 1.4986 1.2116 -0.5362 -0.0672 -0.0867 366 TYR A N   
474  C CA  . TYR A 70  ? 1.5570 1.6291 1.2738 -0.5734 -0.0659 -0.0845 366 TYR A CA  
475  C C   . TYR A 70  ? 1.6352 1.7749 1.3667 -0.5962 -0.0565 -0.0764 366 TYR A C   
476  O O   . TYR A 70  ? 1.6743 1.9129 1.4335 -0.6122 -0.0542 -0.0747 366 TYR A O   
477  C CB  . TYR A 70  ? 1.6423 1.6139 1.2678 -0.6074 -0.0701 -0.0864 366 TYR A CB  
478  C CG  . TYR A 70  ? 1.6223 1.5594 1.2401 -0.5881 -0.0796 -0.0954 366 TYR A CG  
479  C CD1 . TYR A 70  ? 1.6128 1.4323 1.1808 -0.5635 -0.0844 -0.1009 366 TYR A CD1 
480  C CD2 . TYR A 70  ? 1.5792 1.6043 1.2387 -0.5899 -0.0837 -0.0989 366 TYR A CD2 
481  C CE1 . TYR A 70  ? 1.5942 1.3848 1.1528 -0.5436 -0.0928 -0.1101 366 TYR A CE1 
482  C CE2 . TYR A 70  ? 1.5953 1.5914 1.2475 -0.5722 -0.0926 -0.1074 366 TYR A CE2 
483  C CZ  . TYR A 70  ? 1.6197 1.4990 1.2214 -0.5500 -0.0970 -0.1134 366 TYR A CZ  
484  O OH  . TYR A 70  ? 1.6201 1.4732 1.2114 -0.5308 -0.1055 -0.1227 366 TYR A OH  
485  N N   . SER A 71  ? 1.6396 1.7302 1.3520 -0.5954 -0.0511 -0.0717 367 SER A N   
486  C CA  . SER A 71  ? 1.6003 1.7571 1.3319 -0.6103 -0.0421 -0.0648 367 SER A CA  
487  C C   . SER A 71  ? 1.4945 1.7584 1.3162 -0.5702 -0.0388 -0.0642 367 SER A C   
488  O O   . SER A 71  ? 1.5153 1.8314 1.3568 -0.5728 -0.0312 -0.0591 367 SER A O   
489  C CB  . SER A 71  ? 1.6313 1.6906 1.3046 -0.6228 -0.0380 -0.0599 367 SER A CB  
490  O OG  . SER A 71  ? 1.6150 1.7346 1.2988 -0.6419 -0.0294 -0.0536 367 SER A OG  
491  N N   . SER A 72  ? 1.3406 1.6342 1.2115 -0.5325 -0.0444 -0.0692 368 SER A N   
492  C CA  . SER A 72  ? 1.2557 1.6538 1.2044 -0.4932 -0.0420 -0.0684 368 SER A CA  
493  C C   . SER A 72  ? 1.3247 1.8172 1.3012 -0.4913 -0.0441 -0.0702 368 SER A C   
494  O O   . SER A 72  ? 1.3398 1.9287 1.3595 -0.4726 -0.0395 -0.0676 368 SER A O   
495  C CB  . SER A 72  ? 1.1616 1.5323 1.1448 -0.4487 -0.0463 -0.0715 368 SER A CB  
496  O OG  . SER A 72  ? 1.1976 1.5839 1.1980 -0.4312 -0.0543 -0.0772 368 SER A OG  
497  N N   . ILE A 73  ? 1.3742 1.8382 1.3219 -0.5089 -0.0512 -0.0749 369 ILE A N   
498  C CA  . ILE A 73  ? 1.3806 1.9269 1.3506 -0.5070 -0.0544 -0.0771 369 ILE A CA  
499  C C   . ILE A 73  ? 1.5063 2.0798 1.4349 -0.5588 -0.0515 -0.0750 369 ILE A C   
500  O O   . ILE A 73  ? 1.5426 2.1524 1.4642 -0.5738 -0.0556 -0.0777 369 ILE A O   
501  C CB  . ILE A 73  ? 1.3814 1.8860 1.3467 -0.4940 -0.0644 -0.0839 369 ILE A CB  
502  C CG1 . ILE A 73  ? 1.4624 1.8386 1.3590 -0.5207 -0.0686 -0.0872 369 ILE A CG1 
503  C CG2 . ILE A 73  ? 1.2708 1.7960 1.2913 -0.4390 -0.0672 -0.0855 369 ILE A CG2 
504  C CD1 . ILE A 73  ? 1.4354 1.7608 1.3242 -0.5022 -0.0784 -0.0950 369 ILE A CD1 
505  N N   . LYS A 74  ? 1.5458 2.1018 1.4438 -0.5880 -0.0445 -0.0700 370 LYS A N   
506  C CA  . LYS A 74  ? 1.5968 2.1888 1.4548 -0.6395 -0.0405 -0.0669 370 LYS A CA  
507  C C   . LYS A 74  ? 1.6053 2.1434 1.4047 -0.6802 -0.0466 -0.0696 370 LYS A C   
508  O O   . LYS A 74  ? 1.6501 2.2529 1.4373 -0.7118 -0.0464 -0.0693 370 LYS A O   
509  C CB  . LYS A 74  ? 1.5743 2.3079 1.4811 -0.6269 -0.0363 -0.0655 370 LYS A CB  
510  C CG  . LYS A 74  ? 1.5013 2.2817 1.4496 -0.5947 -0.0291 -0.0620 370 LYS A CG  
511  C CD  . LYS A 74  ? 1.3943 2.3024 1.3972 -0.5583 -0.0272 -0.0624 370 LYS A CD  
512  C CE  . LYS A 74  ? 1.2243 2.1569 1.2695 -0.5121 -0.0221 -0.0600 370 LYS A CE  
513  N NZ  . LYS A 74  ? 1.1323 2.1691 1.2240 -0.4650 -0.0217 -0.0609 370 LYS A NZ  
514  N N   . ARG A 75  ? 1.5797 1.9974 1.3394 -0.6780 -0.0522 -0.0727 371 ARG A N   
515  C CA  . ARG A 75  ? 1.6190 1.9544 1.3050 -0.7169 -0.0577 -0.0748 371 ARG A CA  
516  C C   . ARG A 75  ? 1.8200 2.0091 1.4320 -0.7282 -0.0580 -0.0734 371 ARG A C   
517  O O   . ARG A 75  ? 1.9001 1.9893 1.4569 -0.7331 -0.0645 -0.0772 371 ARG A O   
518  C CB  . ARG A 75  ? 1.4018 1.7413 1.1089 -0.6942 -0.0668 -0.0821 371 ARG A CB  
519  C CG  . ARG A 75  ? 1.3448 1.8194 1.1073 -0.6883 -0.0670 -0.0829 371 ARG A CG  
520  C CD  . ARG A 75  ? 1.3765 1.8721 1.1889 -0.6411 -0.0746 -0.0892 371 ARG A CD  
521  N NE  . ARG A 75  ? 1.4191 1.9934 1.2450 -0.6499 -0.0786 -0.0917 371 ARG A NE  
522  C CZ  . ARG A 75  ? 1.5385 2.0691 1.3146 -0.6832 -0.0847 -0.0952 371 ARG A CZ  
523  N NH1 . ARG A 75  ? 1.5094 2.1206 1.3030 -0.6892 -0.0882 -0.0972 371 ARG A NH1 
524  N NH2 . ARG A 75  ? 1.6880 2.0911 1.3923 -0.7088 -0.0873 -0.0965 371 ARG A NH2 
525  N N   . PHE A 76  ? 1.8823 2.0567 1.4903 -0.7283 -0.0511 -0.0681 372 PHE A N   
526  C CA  . PHE A 76  ? 2.0481 2.0893 1.5777 -0.7416 -0.0501 -0.0650 372 PHE A CA  
527  C C   . PHE A 76  ? 2.2664 2.2341 1.6980 -0.7960 -0.0518 -0.0626 372 PHE A C   
528  O O   . PHE A 76  ? 2.3479 2.3846 1.7692 -0.8391 -0.0491 -0.0597 372 PHE A O   
529  C CB  . PHE A 76  ? 1.9983 2.0658 1.5431 -0.7421 -0.0415 -0.0587 372 PHE A CB  
530  C CG  . PHE A 76  ? 2.0328 1.9706 1.4963 -0.7548 -0.0397 -0.0544 372 PHE A CG  
531  C CD1 . PHE A 76  ? 2.0522 1.8570 1.4565 -0.7379 -0.0455 -0.0570 372 PHE A CD1 
532  C CD2 . PHE A 76  ? 2.0697 2.0202 1.5133 -0.7799 -0.0323 -0.0478 372 PHE A CD2 
533  C CE1 . PHE A 76  ? 2.1233 1.8082 1.4474 -0.7435 -0.0440 -0.0524 372 PHE A CE1 
534  C CE2 . PHE A 76  ? 2.1591 1.9902 1.5246 -0.7894 -0.0309 -0.0434 372 PHE A CE2 
535  C CZ  . PHE A 76  ? 2.2024 1.8995 1.5071 -0.7697 -0.0368 -0.0454 372 PHE A CZ  
536  N N   . GLY A 77  ? 2.3352 2.1614 1.6899 -0.7924 -0.0565 -0.0639 373 GLY A N   
537  C CA  . GLY A 77  ? 2.4378 2.1674 1.6829 -0.8404 -0.0580 -0.0603 373 GLY A CA  
538  C C   . GLY A 77  ? 2.3796 2.1277 1.6043 -0.8690 -0.0635 -0.0636 373 GLY A C   
539  O O   . GLY A 77  ? 2.5539 2.2073 1.6791 -0.9074 -0.0658 -0.0608 373 GLY A O   
540  N N   . SER A 78  ? 2.1291 1.9920 1.4390 -0.8515 -0.0660 -0.0691 374 SER A N   
541  C CA  . SER A 78  ? 2.0257 1.9123 1.3202 -0.8770 -0.0716 -0.0725 374 SER A CA  
542  C C   . SER A 78  ? 2.0232 1.7752 1.2519 -0.8623 -0.0798 -0.0777 374 SER A C   
543  O O   . SER A 78  ? 1.9638 1.6138 1.1647 -0.8271 -0.0811 -0.0791 374 SER A O   
544  C CB  . SER A 78  ? 1.8860 1.9184 1.2865 -0.8502 -0.0731 -0.0775 374 SER A CB  
545  O OG  . SER A 78  ? 1.7844 1.8142 1.2462 -0.7891 -0.0763 -0.0833 374 SER A OG  
546  N N   . LYS A 79  ? 2.0475 1.8008 1.2478 -0.8884 -0.0855 -0.0808 375 LYS A N   
547  C CA  . LYS A 79  ? 2.0922 1.7281 1.2343 -0.8702 -0.0939 -0.0869 375 LYS A CA  
548  C C   . LYS A 79  ? 1.8936 1.5589 1.1133 -0.8069 -0.0991 -0.0967 375 LYS A C   
549  O O   . LYS A 79  ? 1.8793 1.4386 1.0615 -0.7704 -0.1035 -0.1017 375 LYS A O   
550  C CB  . LYS A 79  ? 2.2430 1.8749 1.3333 -0.9174 -0.0987 -0.0876 375 LYS A CB  
551  C CG  . LYS A 79  ? 2.3348 1.8234 1.3374 -0.9078 -0.1068 -0.0924 375 LYS A CG  
552  C CD  . LYS A 79  ? 2.4796 1.8133 1.3561 -0.9304 -0.1049 -0.0846 375 LYS A CD  
553  C CE  . LYS A 79  ? 2.5766 1.7847 1.3514 -0.9395 -0.1126 -0.0871 375 LYS A CE  
554  N NZ  . LYS A 79  ? 2.4757 1.6577 1.2816 -0.8786 -0.1198 -0.0987 375 LYS A NZ  
555  N N   . ALA A 80  ? 1.7895 1.5976 1.1124 -0.7910 -0.0985 -0.0992 376 ALA A N   
556  C CA  . ALA A 80  ? 1.6964 1.5364 1.0923 -0.7320 -0.1028 -0.1072 376 ALA A CA  
557  C C   . ALA A 80  ? 1.7589 1.5309 1.1536 -0.6943 -0.0997 -0.1065 376 ALA A C   
558  O O   . ALA A 80  ? 1.7934 1.5194 1.1966 -0.6495 -0.1045 -0.1139 376 ALA A O   
559  C CB  . ALA A 80  ? 1.5513 1.5537 1.0512 -0.7200 -0.1012 -0.1070 376 ALA A CB  
560  N N   . HIS A 81  ? 1.7748 1.5386 1.1541 -0.7126 -0.0917 -0.0980 377 HIS A N   
561  C CA  . HIS A 81  ? 1.8146 1.4908 1.1695 -0.6836 -0.0889 -0.0964 377 HIS A CA  
562  C C   . HIS A 81  ? 1.9526 1.4681 1.1966 -0.6824 -0.0926 -0.0973 377 HIS A C   
563  O O   . HIS A 81  ? 1.9609 1.4025 1.1903 -0.6361 -0.0961 -0.1031 377 HIS A O   
564  C CB  . HIS A 81  ? 1.8022 1.5130 1.1648 -0.7060 -0.0796 -0.0868 377 HIS A CB  
565  C CG  . HIS A 81  ? 1.8811 1.4985 1.2099 -0.6810 -0.0766 -0.0839 377 HIS A CG  
566  N ND1 . HIS A 81  ? 1.8988 1.5087 1.2058 -0.7028 -0.0691 -0.0753 377 HIS A ND1 
567  C CD2 . HIS A 81  ? 1.8800 1.4106 1.1913 -0.6342 -0.0802 -0.0887 377 HIS A CD2 
568  C CE1 . HIS A 81  ? 1.9360 1.4563 1.2139 -0.6705 -0.0684 -0.0744 377 HIS A CE1 
569  N NE2 . HIS A 81  ? 1.9014 1.3736 1.1811 -0.6278 -0.0749 -0.0824 377 HIS A NE2 
570  N N   . MET A 82  ? 2.0631 1.5222 1.2225 -0.7315 -0.0917 -0.0914 378 MET A N   
571  C CA  . MET A 82  ? 2.2035 1.5019 1.2447 -0.7302 -0.0946 -0.0899 378 MET A CA  
572  C C   . MET A 82  ? 2.1689 1.4085 1.1904 -0.6933 -0.1029 -0.0999 378 MET A C   
573  O O   . MET A 82  ? 2.2516 1.3723 1.2082 -0.6554 -0.1049 -0.1014 378 MET A O   
574  C CB  . MET A 82  ? 2.3642 1.6228 1.3175 -0.7958 -0.0930 -0.0817 378 MET A CB  
575  C CG  . MET A 82  ? 2.4708 1.7636 1.4192 -0.8326 -0.0846 -0.0718 378 MET A CG  
576  S SD  . MET A 82  ? 2.5811 1.7668 1.4849 -0.7956 -0.0806 -0.0667 378 MET A SD  
577  C CE  . MET A 82  ? 2.4604 1.7909 1.4704 -0.8022 -0.0717 -0.0631 378 MET A CE  
578  N N   . ASP A 83  ? 2.0386 1.3604 1.1112 -0.7008 -0.1078 -0.1068 379 ASP A N   
579  C CA  . ASP A 83  ? 2.0576 1.3294 1.1137 -0.6642 -0.1156 -0.1172 379 ASP A CA  
580  C C   . ASP A 83  ? 1.9854 1.2662 1.0975 -0.5993 -0.1163 -0.1247 379 ASP A C   
581  O O   . ASP A 83  ? 1.9478 1.1461 1.0184 -0.5570 -0.1203 -0.1317 379 ASP A O   
582  C CB  . ASP A 83  ? 2.0071 1.3692 1.1058 -0.6869 -0.1211 -0.1229 379 ASP A CB  
583  C CG  . ASP A 83  ? 2.1279 1.4378 1.1409 -0.7415 -0.1234 -0.1190 379 ASP A CG  
584  O OD1 . ASP A 83  ? 2.1230 1.5332 1.1714 -0.7851 -0.1231 -0.1166 379 ASP A OD1 
585  O OD2 . ASP A 83  ? 2.2351 1.4055 1.1425 -0.7398 -0.1256 -0.1177 379 ASP A OD2 
586  N N   . ARG A 84  ? 1.9045 1.2860 1.1074 -0.5898 -0.1120 -0.1230 380 ARG A N   
587  C CA  . ARG A 84  ? 1.8674 1.2548 1.1177 -0.5334 -0.1121 -0.1288 380 ARG A CA  
588  C C   . ARG A 84  ? 1.9485 1.2190 1.1321 -0.5053 -0.1084 -0.1250 380 ARG A C   
589  O O   . ARG A 84  ? 2.0461 1.2639 1.2177 -0.4519 -0.1101 -0.1314 380 ARG A O   
590  C CB  . ARG A 84  ? 1.7958 1.3200 1.1549 -0.5342 -0.1086 -0.1263 380 ARG A CB  
591  C CG  . ARG A 84  ? 1.6786 1.2197 1.0897 -0.4825 -0.1091 -0.1318 380 ARG A CG  
592  C CD  . ARG A 84  ? 1.6307 1.2297 1.0881 -0.4597 -0.1161 -0.1415 380 ARG A CD  
593  N NE  . ARG A 84  ? 1.6042 1.1960 1.0918 -0.4004 -0.1141 -0.1435 380 ARG A NE  
594  C CZ  . ARG A 84  ? 1.5380 1.0334 0.9694 -0.3576 -0.1135 -0.1467 380 ARG A CZ  
595  N NH1 . ARG A 84  ? 1.7294 1.1084 1.0551 -0.3779 -0.1196 -0.1547 380 ARG A NH1 
596  N NH2 . ARG A 84  ? 1.3708 0.8879 0.8484 -0.2946 -0.1068 -0.1416 380 ARG A NH2 
597  N N   . LEU A 85  ? 1.9305 1.1632 1.0683 -0.5383 -0.1031 -0.1143 381 LEU A N   
598  C CA  . LEU A 85  ? 1.9884 1.1045 1.0520 -0.5117 -0.1003 -0.1092 381 LEU A CA  
599  C C   . LEU A 85  ? 2.1102 1.0956 1.0696 -0.4887 -0.1049 -0.1115 381 LEU A C   
600  O O   . LEU A 85  ? 2.1211 1.0290 1.0429 -0.4333 -0.1051 -0.1132 381 LEU A O   
601  C CB  . LEU A 85  ? 2.0248 1.1291 1.0541 -0.5569 -0.0941 -0.0970 381 LEU A CB  
602  C CG  . LEU A 85  ? 2.0613 1.0945 1.0572 -0.5252 -0.0901 -0.0913 381 LEU A CG  
603  C CD1 . LEU A 85  ? 1.8262 0.9616 0.9273 -0.5078 -0.0860 -0.0924 381 LEU A CD1 
604  C CD2 . LEU A 85  ? 2.2704 1.2345 1.1789 -0.5677 -0.0863 -0.0797 381 LEU A CD2 
605  N N   . GLU A 86  ? 2.2045 1.1664 1.1140 -0.5284 -0.1085 -0.1111 382 GLU A N   
606  C CA  . GLU A 86  ? 2.3227 1.1615 1.1307 -0.5077 -0.1133 -0.1129 382 GLU A CA  
607  C C   . GLU A 86  ? 2.1353 0.9828 0.9760 -0.4482 -0.1174 -0.1255 382 GLU A C   
608  O O   . GLU A 86  ? 2.2994 1.0512 1.0756 -0.3958 -0.1185 -0.1269 382 GLU A O   
609  C CB  . GLU A 86  ? 2.5708 1.3942 1.3254 -0.5687 -0.1165 -0.1101 382 GLU A CB  
610  C CG  . GLU A 86  ? 2.8309 1.5117 1.4615 -0.5569 -0.1213 -0.1091 382 GLU A CG  
611  C CD  . GLU A 86  ? 3.0167 1.6031 1.5359 -0.6063 -0.1199 -0.0961 382 GLU A CD  
612  O OE1 . GLU A 86  ? 3.1586 1.6166 1.5623 -0.5994 -0.1239 -0.0931 382 GLU A OE1 
613  O OE2 . GLU A 86  ? 3.0055 1.6456 1.5486 -0.6516 -0.1146 -0.0887 382 GLU A OE2 
614  N N   . GLU A 87  ? 1.8378 0.8035 0.7760 -0.4529 -0.1194 -0.1340 383 GLU A N   
615  C CA  . GLU A 87  ? 1.8033 0.7891 0.7766 -0.3994 -0.1228 -0.1462 383 GLU A CA  
616  C C   . GLU A 87  ? 1.9205 0.8807 0.9039 -0.3343 -0.1189 -0.1478 383 GLU A C   
617  O O   . GLU A 87  ? 1.7556 0.6551 0.6981 -0.2783 -0.1196 -0.1529 383 GLU A O   
618  C CB  . GLU A 87  ? 1.8100 0.9357 0.8883 -0.4197 -0.1256 -0.1527 383 GLU A CB  
619  C CG  . GLU A 87  ? 1.8721 1.0228 0.9788 -0.3759 -0.1300 -0.1651 383 GLU A CG  
620  C CD  . GLU A 87  ? 1.8698 1.1557 1.0706 -0.3989 -0.1341 -0.1694 383 GLU A CD  
621  O OE1 . GLU A 87  ? 1.7679 1.1462 1.0407 -0.4219 -0.1315 -0.1638 383 GLU A OE1 
622  O OE2 . GLU A 87  ? 1.8773 1.1778 1.0778 -0.3909 -0.1398 -0.1776 383 GLU A OE2 
623  N N   . VAL A 88  ? 1.8345 0.8457 0.8727 -0.3384 -0.1143 -0.1430 384 VAL A N   
624  C CA  . VAL A 88  ? 1.8247 0.8158 0.8730 -0.2779 -0.1107 -0.1440 384 VAL A CA  
625  C C   . VAL A 88  ? 1.9165 0.7805 0.8617 -0.2455 -0.1089 -0.1369 384 VAL A C   
626  O O   . VAL A 88  ? 1.9054 0.7305 0.8284 -0.1794 -0.1078 -0.1397 384 VAL A O   
627  C CB  . VAL A 88  ? 1.7897 0.8597 0.9153 -0.2928 -0.1066 -0.1397 384 VAL A CB  
628  C CG1 . VAL A 88  ? 1.7966 0.8360 0.9217 -0.2312 -0.1030 -0.1397 384 VAL A CG1 
629  C CG2 . VAL A 88  ? 1.7077 0.9051 0.9337 -0.3122 -0.1092 -0.1459 384 VAL A CG2 
630  N N   . ASN A 89  ? 2.0607 0.8637 0.9397 -0.2899 -0.1085 -0.1265 385 ASN A N   
631  C CA  . ASN A 89  ? 2.2447 0.9195 1.0122 -0.2639 -0.1083 -0.1180 385 ASN A CA  
632  C C   . ASN A 89  ? 2.2441 0.8497 0.9493 -0.2151 -0.1122 -0.1232 385 ASN A C   
633  O O   . ASN A 89  ? 2.2887 0.8414 0.9548 -0.1492 -0.1113 -0.1217 385 ASN A O   
634  C CB  . ASN A 89  ? 2.4290 1.0505 1.1264 -0.3302 -0.1083 -0.1071 385 ASN A CB  
635  C CG  . ASN A 89  ? 2.6037 1.0926 1.1818 -0.3080 -0.1084 -0.0965 385 ASN A CG  
636  O OD1 . ASN A 89  ? 2.6126 1.0896 1.1904 -0.2851 -0.1049 -0.0908 385 ASN A OD1 
637  N ND2 . ASN A 89  ? 2.7077 1.0946 1.1792 -0.3157 -0.1129 -0.0934 385 ASN A ND2 
638  N N   . LYS A 90  ? 2.1839 0.7986 0.8833 -0.2437 -0.1165 -0.1291 386 LYS A N   
639  C CA  . LYS A 90  ? 2.3199 0.8638 0.9529 -0.2005 -0.1201 -0.1333 386 LYS A CA  
640  C C   . LYS A 90  ? 2.2939 0.8951 0.9877 -0.1310 -0.1182 -0.1436 386 LYS A C   
641  O O   . LYS A 90  ? 2.3905 0.9323 1.0288 -0.0695 -0.1183 -0.1434 386 LYS A O   
642  C CB  . LYS A 90  ? 2.3403 0.8757 0.9463 -0.2537 -0.1254 -0.1365 386 LYS A CB  
643  C CG  . LYS A 90  ? 2.5169 0.9965 1.0543 -0.3241 -0.1263 -0.1252 386 LYS A CG  
644  C CD  . LYS A 90  ? 2.6230 1.0516 1.0928 -0.3634 -0.1321 -0.1261 386 LYS A CD  
645  C CE  . LYS A 90  ? 2.7470 1.1051 1.1298 -0.4286 -0.1323 -0.1133 386 LYS A CE  
646  N NZ  . LYS A 90  ? 2.8171 1.1041 1.1131 -0.4649 -0.1382 -0.1127 386 LYS A NZ  
647  N N   . GLU A 91  ? 2.1539 0.8718 0.9569 -0.1376 -0.1164 -0.1516 387 GLU A N   
648  C CA  . GLU A 91  ? 2.1035 0.8757 0.9585 -0.0714 -0.1134 -0.1601 387 GLU A CA  
649  C C   . GLU A 91  ? 2.2435 0.9955 1.0900 -0.0120 -0.1081 -0.1539 387 GLU A C   
650  O O   . GLU A 91  ? 2.1746 0.9373 1.0232 0.0565  -0.1051 -0.1566 387 GLU A O   
651  C CB  . GLU A 91  ? 1.9557 0.8510 0.9194 -0.0940 -0.1137 -0.1690 387 GLU A CB  
652  C CG  . GLU A 91  ? 1.8438 0.8010 0.8593 -0.0286 -0.1098 -0.1765 387 GLU A CG  
653  C CD  . GLU A 91  ? 1.7097 0.8267 0.8666 -0.0447 -0.1055 -0.1682 387 GLU A CD  
654  O OE1 . GLU A 91  ? 1.5554 0.7544 0.7815 0.0037  -0.0988 -0.1637 387 GLU A OE1 
655  O OE2 . GLU A 91  ? 1.7742 0.9348 0.9688 -0.1050 -0.1087 -0.1661 387 GLU A OE2 
656  N N   . ILE A 92  ? 2.3506 1.0820 1.1893 -0.0367 -0.1067 -0.1447 388 ILE A N   
657  C CA  . ILE A 92  ? 2.3891 1.0887 1.2041 0.0163  -0.1031 -0.1369 388 ILE A CA  
658  C C   . ILE A 92  ? 2.5021 1.0881 1.2014 0.0546  -0.1057 -0.1292 388 ILE A C   
659  O O   . ILE A 92  ? 2.5398 1.1090 1.2156 0.1188  -0.1040 -0.1242 388 ILE A O   
660  C CB  . ILE A 92  ? 2.3908 1.1006 1.2279 -0.0257 -0.1011 -0.1294 388 ILE A CB  
661  C CG1 . ILE A 92  ? 2.2554 1.0816 1.2079 -0.0445 -0.0987 -0.1363 388 ILE A CG1 
662  C CG2 . ILE A 92  ? 2.4940 1.1530 1.2865 0.0222  -0.0989 -0.1196 388 ILE A CG2 
663  C CD1 . ILE A 92  ? 2.1585 1.0040 1.1396 -0.0802 -0.0962 -0.1287 388 ILE A CD1 
664  N N   . GLU A 93  ? 2.6165 1.1260 1.2394 0.0179  -0.1105 -0.1274 389 GLU A N   
665  C CA  . GLU A 93  ? 2.6342 1.0375 1.1452 0.0613  -0.1141 -0.1216 389 GLU A CA  
666  C C   . GLU A 93  ? 2.5301 0.9703 1.0616 0.1240  -0.1134 -0.1297 389 GLU A C   
667  O O   . GLU A 93  ? 2.4463 0.8769 0.9526 0.1966  -0.1122 -0.1259 389 GLU A O   
668  C CB  . GLU A 93  ? 2.7255 1.0337 1.1444 0.0020  -0.1196 -0.1172 389 GLU A CB  
669  C CG  . GLU A 93  ? 2.8175 1.1005 1.2167 -0.0694 -0.1192 -0.1086 389 GLU A CG  
670  C CD  . GLU A 93  ? 2.8915 1.0870 1.2060 -0.0453 -0.1191 -0.0959 389 GLU A CD  
671  O OE1 . GLU A 93  ? 2.9623 1.1061 1.2201 0.0263  -0.1208 -0.0929 389 GLU A OE1 
672  O OE2 . GLU A 93  ? 2.8863 1.0690 1.1891 -0.0977 -0.1175 -0.0887 389 GLU A OE2 
673  N N   . SER A 94  ? 2.5604 1.0548 1.1423 0.0967  -0.1140 -0.1407 390 SER A N   
674  C CA  . SER A 94  ? 2.5145 1.0395 1.1084 0.1436  -0.1133 -0.1488 390 SER A CA  
675  C C   . SER A 94  ? 2.3785 0.9971 1.0458 0.2123  -0.1065 -0.1514 390 SER A C   
676  O O   . SER A 94  ? 2.2833 0.8853 0.9123 0.2809  -0.1054 -0.1468 390 SER A O   
677  C CB  . SER A 94  ? 2.5125 1.0895 1.1560 0.0899  -0.1156 -0.1600 390 SER A CB  
678  O OG  . SER A 94  ? 2.5780 1.2171 1.2624 0.1344  -0.1129 -0.1692 390 SER A OG  
679  N N   . THR A 95  ? 2.3593 1.0816 1.1307 0.1934  -0.1023 -0.1579 391 THR A N   
680  C CA  . THR A 95  ? 2.2676 1.0909 1.1172 0.2489  -0.0950 -0.1600 391 THR A CA  
681  C C   . THR A 95  ? 2.2118 1.0448 1.0748 0.2723  -0.0921 -0.1511 391 THR A C   
682  O O   . THR A 95  ? 2.0517 0.9651 0.9687 0.3251  -0.0861 -0.1500 391 THR A O   
683  C CB  . THR A 95  ? 2.1066 1.0330 1.0544 0.2184  -0.0927 -0.1711 391 THR A CB  
684  O OG1 . THR A 95  ? 2.0220 0.9596 1.0048 0.1596  -0.0949 -0.1706 391 THR A OG1 
685  C CG2 . THR A 95  ? 1.9610 0.8829 0.8971 0.1904  -0.0968 -0.1799 391 THR A CG2 
686  N N   . SER A 96  ? 2.3306 1.0907 1.1474 0.2323  -0.0958 -0.1441 392 SER A N   
687  C CA  . SER A 96  ? 2.3716 1.1306 1.1935 0.2456  -0.0940 -0.1353 392 SER A CA  
688  C C   . SER A 96  ? 2.2921 1.1430 1.2166 0.2177  -0.0899 -0.1398 392 SER A C   
689  O O   . SER A 96  ? 2.4261 1.2630 1.3537 0.1957  -0.0898 -0.1336 392 SER A O   
690  C CB  . SER A 96  ? 2.4232 1.1937 1.2232 0.3286  -0.0920 -0.1284 392 SER A CB  
691  O OG  . SER A 96  ? 2.3260 1.2140 1.2123 0.3706  -0.0857 -0.1335 392 SER A OG  
692  N N   . THR A 97  ? 2.0844 1.0263 1.0877 0.2186  -0.0869 -0.1501 393 THR A N   
693  C CA  . THR A 97  ? 1.8668 0.9329 0.9946 0.1793  -0.0833 -0.1414 393 THR A CA  
694  C C   . THR A 97  ? 1.8216 0.8989 0.9704 0.1063  -0.0875 -0.1449 393 THR A C   
695  O O   . THR A 97  ? 1.8104 0.7855 0.8686 0.0770  -0.0940 -0.1535 393 THR A O   
696  C CB  . THR A 97  ? 1.6365 0.8379 0.8660 0.2211  -0.0762 -0.1359 393 THR A CB  
697  O OG1 . THR A 97  ? 1.6550 0.9631 0.9937 0.1865  -0.0731 -0.1264 393 THR A OG1 
698  C CG2 . THR A 97  ? 1.6110 0.8438 0.8519 0.2268  -0.0759 -0.1424 393 THR A CG2 
699  N N   . TYR A 98  ? 1.6778 0.8770 0.9402 0.0764  -0.0845 -0.1384 394 TYR A N   
700  C CA  . TYR A 98  ? 1.6453 0.8773 0.9363 0.0184  -0.0885 -0.1419 394 TYR A CA  
701  C C   . TYR A 98  ? 1.4816 0.8562 0.8983 0.0135  -0.0839 -0.1344 394 TYR A C   
702  O O   . TYR A 98  ? 1.3286 0.7688 0.8061 0.0459  -0.0778 -0.1264 394 TYR A O   
703  C CB  . TYR A 98  ? 1.6890 0.8609 0.9350 -0.0464 -0.0936 -0.1428 394 TYR A CB  
704  C CG  . TYR A 98  ? 1.7287 0.9572 1.0368 -0.0689 -0.0897 -0.1328 394 TYR A CG  
705  C CD1 . TYR A 98  ? 1.6995 1.0247 1.0893 -0.1143 -0.0892 -0.1291 394 TYR A CD1 
706  C CD2 . TYR A 98  ? 1.7507 0.9354 1.0315 -0.0420 -0.0866 -0.1273 394 TYR A CD2 
707  C CE1 . TYR A 98  ? 1.5049 0.8813 0.9481 -0.1319 -0.0851 -0.1203 394 TYR A CE1 
708  C CE2 . TYR A 98  ? 1.6063 0.8411 0.9414 -0.0625 -0.0830 -0.1184 394 TYR A CE2 
709  C CZ  . TYR A 98  ? 1.4766 0.8059 0.8921 -0.1076 -0.0820 -0.1152 394 TYR A CZ  
710  O OH  . TYR A 98  ? 1.2830 0.6616 0.7491 -0.1249 -0.0779 -0.1069 394 TYR A OH  
711  N N   . GLN A 99  ? 1.5016 0.9208 0.9507 -0.0274 -0.0874 -0.1373 395 GLN A N   
712  C CA  . GLN A 99  ? 1.2763 0.8178 0.8305 -0.0335 -0.0843 -0.1311 395 GLN A CA  
713  C C   . GLN A 99  ? 1.1804 0.7630 0.7701 -0.0903 -0.0872 -0.1289 395 GLN A C   
714  O O   . GLN A 99  ? 1.1427 0.6763 0.6799 -0.1343 -0.0935 -0.1351 395 GLN A O   
715  C CB  . GLN A 99  ? 1.1406 0.7134 0.7058 -0.0207 -0.0858 -0.1362 395 GLN A CB  
716  C CG  . GLN A 99  ? 1.0835 0.6302 0.6168 0.0370  -0.0819 -0.1387 395 GLN A CG  
717  C CD  . GLN A 99  ? 1.2168 0.8441 0.8205 0.0763  -0.0736 -0.1289 395 GLN A CD  
718  O OE1 . GLN A 99  ? 1.3083 1.0245 0.9914 0.0659  -0.0709 -0.1220 395 GLN A OE1 
719  N NE2 . GLN A 99  ? 1.2487 0.8441 0.8182 0.1218  -0.0698 -0.1282 395 GLN A NE2 
720  N N   . LEU A 100 ? 0.9660 0.6399 0.6411 -0.0895 -0.0827 -0.1201 396 LEU A N   
721  C CA  . LEU A 100 ? 0.9783 0.7086 0.6954 -0.1342 -0.0843 -0.1173 396 LEU A CA  
722  C C   . LEU A 100 ? 1.0139 0.8129 0.7699 -0.1496 -0.0882 -0.1200 396 LEU A C   
723  O O   . LEU A 100 ? 1.0157 0.8502 0.8020 -0.1188 -0.0867 -0.1191 396 LEU A O   
724  C CB  . LEU A 100 ? 0.8290 0.6208 0.6131 -0.1215 -0.0779 -0.1072 396 LEU A CB  
725  C CG  . LEU A 100 ? 0.9896 0.7295 0.7473 -0.0984 -0.0738 -0.1032 396 LEU A CG  
726  C CD1 . LEU A 100 ? 0.9593 0.7653 0.7853 -0.0848 -0.0683 -0.0938 396 LEU A CD1 
727  C CD2 . LEU A 100 ? 1.1216 0.7856 0.8123 -0.1342 -0.0767 -0.1062 396 LEU A CD2 
728  N N   . LYS A 101 ? 1.0301 0.8522 0.7843 -0.1979 -0.0934 -0.1230 397 LYS A N   
729  C CA  . LYS A 101 ? 1.0244 0.9345 0.8292 -0.2116 -0.0971 -0.1235 397 LYS A CA  
730  C C   . LYS A 101 ? 0.9792 0.9739 0.8650 -0.1836 -0.0913 -0.1141 397 LYS A C   
731  O O   . LYS A 101 ? 1.0835 1.0792 0.9901 -0.1698 -0.0852 -0.1074 397 LYS A O   
732  C CB  . LYS A 101 ? 1.1248 1.0624 0.9204 -0.2685 -0.1027 -0.1267 397 LYS A CB  
733  C CG  . LYS A 101 ? 1.3418 1.1924 1.0494 -0.3093 -0.1095 -0.1358 397 LYS A CG  
734  C CD  . LYS A 101 ? 1.3952 1.2372 1.0777 -0.3106 -0.1170 -0.1442 397 LYS A CD  
735  C CE  . LYS A 101 ? 1.5387 1.2598 1.1169 -0.3316 -0.1225 -0.1536 397 LYS A CE  
736  N NZ  . LYS A 101 ? 1.5680 1.2702 1.1238 -0.3108 -0.1273 -0.1610 397 LYS A NZ  
737  N N   . ASP A 102 ? 0.8453 0.9075 0.7712 -0.1768 -0.0940 -0.1137 398 ASP A N   
738  C CA  . ASP A 102 ? 0.7782 0.9155 0.7702 -0.1554 -0.0899 -0.1053 398 ASP A CA  
739  C C   . ASP A 102 ? 0.8690 1.0447 0.8855 -0.1760 -0.0878 -0.1014 398 ASP A C   
740  O O   . ASP A 102 ? 0.7731 0.9646 0.8213 -0.1560 -0.0818 -0.0941 398 ASP A O   
741  C CB  . ASP A 102 ? 0.9429 1.1419 0.9616 -0.1501 -0.0948 -0.1062 398 ASP A CB  
742  C CG  . ASP A 102 ? 1.1398 1.3059 1.1335 -0.1319 -0.0968 -0.1102 398 ASP A CG  
743  O OD1 . ASP A 102 ? 1.2484 1.3430 1.1955 -0.1290 -0.0958 -0.1147 398 ASP A OD1 
744  O OD2 . ASP A 102 ? 1.1833 1.3939 1.2001 -0.1180 -0.0992 -0.1089 398 ASP A OD2 
745  N N   . THR A 103 ? 0.9460 1.1393 0.9459 -0.2181 -0.0928 -0.1063 399 THR A N   
746  C CA  . THR A 103 ? 0.8969 1.1370 0.9197 -0.2396 -0.0901 -0.1027 399 THR A CA  
747  C C   . THR A 103 ? 0.9540 1.1320 0.9537 -0.2424 -0.0840 -0.0993 399 THR A C   
748  O O   . THR A 103 ? 0.7363 0.9480 0.7670 -0.2380 -0.0786 -0.0934 399 THR A O   
749  C CB  . THR A 103 ? 0.9145 1.1946 0.9214 -0.2893 -0.0970 -0.1087 399 THR A CB  
750  O OG1 . THR A 103 ? 0.9641 1.1630 0.9036 -0.3188 -0.1021 -0.1164 399 THR A OG1 
751  C CG2 . THR A 103 ? 0.7575 1.1240 0.8006 -0.2806 -0.1028 -0.1103 399 THR A CG2 
752  N N   . GLU A 104 ? 1.0472 1.1324 0.9889 -0.2454 -0.0849 -0.1032 400 GLU A N   
753  C CA  . GLU A 104 ? 1.0873 1.1063 0.9988 -0.2433 -0.0800 -0.1001 400 GLU A CA  
754  C C   . GLU A 104 ? 1.0003 1.0237 0.9478 -0.1961 -0.0737 -0.0929 400 GLU A C   
755  O O   . GLU A 104 ? 1.0381 1.0460 0.9875 -0.1922 -0.0690 -0.0879 400 GLU A O   
756  C CB  . GLU A 104 ? 1.1123 1.0255 0.9418 -0.2538 -0.0836 -0.1066 400 GLU A CB  
757  C CG  . GLU A 104 ? 1.1555 1.0524 0.9374 -0.3087 -0.0906 -0.1139 400 GLU A CG  
758  C CD  . GLU A 104 ? 1.2139 0.9927 0.9025 -0.3168 -0.0952 -0.1213 400 GLU A CD  
759  O OE1 . GLU A 104 ? 1.2927 1.0449 0.9308 -0.3647 -0.1021 -0.1282 400 GLU A OE1 
760  O OE2 . GLU A 104 ? 1.2555 0.9687 0.9176 -0.2749 -0.0922 -0.1205 400 GLU A OE2 
761  N N   . LEU A 105 ? 0.8488 0.8946 0.8226 -0.1631 -0.0738 -0.0922 401 LEU A N   
762  C CA  . LEU A 105 ? 0.8083 0.8664 0.8159 -0.1243 -0.0684 -0.0852 401 LEU A CA  
763  C C   . LEU A 105 ? 0.7726 0.8990 0.8346 -0.1216 -0.0654 -0.0787 401 LEU A C   
764  O O   . LEU A 105 ? 0.8731 0.9978 0.9512 -0.1070 -0.0609 -0.0729 401 LEU A O   
765  C CB  . LEU A 105 ? 0.8286 0.8898 0.8413 -0.0958 -0.0691 -0.0861 401 LEU A CB  
766  C CG  . LEU A 105 ? 0.7404 0.8024 0.7720 -0.0595 -0.0639 -0.0798 401 LEU A CG  
767  C CD1 . LEU A 105 ? 0.7683 0.7681 0.7585 -0.0448 -0.0621 -0.0809 401 LEU A CD1 
768  C CD2 . LEU A 105 ? 0.6671 0.7559 0.7149 -0.0392 -0.0639 -0.0790 401 LEU A CD2 
769  N N   . ILE A 106 ? 0.6304 0.8165 0.7168 -0.1339 -0.0684 -0.0800 402 ILE A N   
770  C CA  . ILE A 106 ? 0.6142 0.8624 0.7443 -0.1252 -0.0658 -0.0745 402 ILE A CA  
771  C C   . ILE A 106 ? 0.7051 0.9582 0.8343 -0.1458 -0.0624 -0.0729 402 ILE A C   
772  O O   . ILE A 106 ? 0.6039 0.8704 0.7553 -0.1307 -0.0578 -0.0672 402 ILE A O   
773  C CB  . ILE A 106 ? 0.6905 1.0038 0.8414 -0.1269 -0.0706 -0.0766 402 ILE A CB  
774  C CG1 . ILE A 106 ? 0.4592 0.7619 0.6074 -0.1058 -0.0734 -0.0775 402 ILE A CG1 
775  C CG2 . ILE A 106 ? 0.8052 1.1772 0.9921 -0.1107 -0.0680 -0.0713 402 ILE A CG2 
776  C CD1 . ILE A 106 ? 0.4515 0.8030 0.6037 -0.1127 -0.0806 -0.0821 402 ILE A CD1 
777  N N   . TYR A 107 ? 0.7476 0.9852 0.8458 -0.1828 -0.0645 -0.0776 403 TYR A N   
778  C CA  . TYR A 107 ? 0.8121 1.0430 0.8998 -0.2065 -0.0605 -0.0756 403 TYR A CA  
779  C C   . TYR A 107 ? 0.8639 1.0301 0.9354 -0.1881 -0.0562 -0.0715 403 TYR A C   
780  O O   . TYR A 107 ? 0.8436 1.0252 0.9355 -0.1792 -0.0514 -0.0662 403 TYR A O   
781  C CB  . TYR A 107 ? 0.8542 1.0640 0.8979 -0.2549 -0.0642 -0.0813 403 TYR A CB  
782  C CG  . TYR A 107 ? 0.9860 1.1776 1.0071 -0.2859 -0.0599 -0.0788 403 TYR A CG  
783  C CD1 . TYR A 107 ? 1.0109 1.2775 1.0512 -0.3170 -0.0581 -0.0781 403 TYR A CD1 
784  C CD2 . TYR A 107 ? 1.0349 1.1376 1.0131 -0.2829 -0.0574 -0.0770 403 TYR A CD2 
785  C CE1 . TYR A 107 ? 0.9891 1.2414 1.0072 -0.3479 -0.0532 -0.0752 403 TYR A CE1 
786  C CE2 . TYR A 107 ? 1.0495 1.1308 1.0025 -0.3114 -0.0534 -0.0740 403 TYR A CE2 
787  C CZ  . TYR A 107 ? 1.0570 1.2122 1.0301 -0.3459 -0.0509 -0.0730 403 TYR A CZ  
788  O OH  . TYR A 107 ? 1.1568 1.2923 1.1027 -0.3770 -0.0461 -0.0695 403 TYR A OH  
789  N N   . GLY A 108 ? 0.8657 0.9604 0.8974 -0.1802 -0.0583 -0.0741 404 GLY A N   
790  C CA  . GLY A 108 ? 0.7607 0.7989 0.7731 -0.1599 -0.0551 -0.0705 404 GLY A CA  
791  C C   . GLY A 108 ? 0.7267 0.7985 0.7844 -0.1262 -0.0516 -0.0641 404 GLY A C   
792  O O   . GLY A 108 ? 0.6486 0.7066 0.7075 -0.1188 -0.0482 -0.0597 404 GLY A O   
793  N N   . ALA A 109 ? 0.7133 0.8260 0.8037 -0.1076 -0.0526 -0.0635 405 ALA A N   
794  C CA  . ALA A 109 ? 0.6794 0.8165 0.8039 -0.0809 -0.0498 -0.0573 405 ALA A CA  
795  C C   . ALA A 109 ? 0.6904 0.8663 0.8410 -0.0862 -0.0469 -0.0536 405 ALA A C   
796  O O   . ALA A 109 ? 0.6553 0.8262 0.8154 -0.0741 -0.0441 -0.0489 405 ALA A O   
797  C CB  . ALA A 109 ? 0.4614 0.6256 0.6052 -0.0638 -0.0517 -0.0570 405 ALA A CB  
798  N N   . LYS A 110 ? 0.6660 0.8852 0.8271 -0.1029 -0.0478 -0.0560 406 LYS A N   
799  C CA  . LYS A 110 ? 0.6187 0.8821 0.8034 -0.1017 -0.0445 -0.0529 406 LYS A CA  
800  C C   . LYS A 110 ? 0.6696 0.9109 0.8405 -0.1167 -0.0404 -0.0512 406 LYS A C   
801  O O   . LYS A 110 ? 0.6510 0.9094 0.8369 -0.1070 -0.0367 -0.0474 406 LYS A O   
802  C CB  . LYS A 110 ? 0.6314 0.9581 0.8298 -0.1138 -0.0464 -0.0561 406 LYS A CB  
803  C CG  . LYS A 110 ? 0.7666 1.1210 0.9800 -0.0929 -0.0503 -0.0567 406 LYS A CG  
804  C CD  . LYS A 110 ? 0.7589 1.1857 0.9864 -0.1002 -0.0529 -0.0596 406 LYS A CD  
805  C CE  . LYS A 110 ? 0.6884 1.1372 0.9257 -0.0750 -0.0572 -0.0595 406 LYS A CE  
806  N NZ  . LYS A 110 ? 0.6426 1.1704 0.8965 -0.0679 -0.0593 -0.0607 406 LYS A NZ  
807  N N   . HIS A 111 ? 0.6303 0.8257 0.7660 -0.1392 -0.0412 -0.0538 407 HIS A N   
808  C CA  . HIS A 111 ? 0.6050 0.7702 0.7186 -0.1553 -0.0376 -0.0516 407 HIS A CA  
809  C C   . HIS A 111 ? 0.6682 0.7823 0.7702 -0.1326 -0.0368 -0.0479 407 HIS A C   
810  O O   . HIS A 111 ? 0.6312 0.7349 0.7287 -0.1347 -0.0333 -0.0443 407 HIS A O   
811  C CB  . HIS A 111 ? 0.6679 0.7999 0.7381 -0.1930 -0.0393 -0.0557 407 HIS A CB  
812  C CG  . HIS A 111 ? 0.7527 0.9501 0.8359 -0.2240 -0.0390 -0.0581 407 HIS A CG  
813  N ND1 . HIS A 111 ? 0.8187 1.0345 0.8911 -0.2570 -0.0349 -0.0566 407 HIS A ND1 
814  C CD2 . HIS A 111 ? 0.7409 1.0004 0.8500 -0.2249 -0.0422 -0.0613 407 HIS A CD2 
815  C CE1 . HIS A 111 ? 0.7939 1.0857 0.8857 -0.2788 -0.0355 -0.0592 407 HIS A CE1 
816  N NE2 . HIS A 111 ? 0.7542 1.0731 0.8682 -0.2582 -0.0405 -0.0622 407 HIS A NE2 
817  N N   . ALA A 112 ? 0.5948 0.6841 0.6929 -0.1099 -0.0398 -0.0485 408 ALA A N   
818  C CA  . ALA A 112 ? 0.6929 0.7581 0.7907 -0.0849 -0.0393 -0.0444 408 ALA A CA  
819  C C   . ALA A 112 ? 0.7303 0.8343 0.8636 -0.0741 -0.0368 -0.0397 408 ALA A C   
820  O O   . ALA A 112 ? 0.7333 0.8235 0.8625 -0.0703 -0.0351 -0.0363 408 ALA A O   
821  C CB  . ALA A 112 ? 0.7472 0.8008 0.8422 -0.0626 -0.0423 -0.0456 408 ALA A CB  
822  N N   . TRP A 113 ? 0.5386 0.6863 0.7006 -0.0684 -0.0371 -0.0397 409 TRP A N   
823  C CA  . TRP A 113 ? 0.5147 0.6908 0.6989 -0.0589 -0.0349 -0.0362 409 TRP A CA  
824  C C   . TRP A 113 ? 0.6664 0.8540 0.8480 -0.0731 -0.0308 -0.0358 409 TRP A C   
825  O O   . TRP A 113 ? 0.7285 0.9107 0.9118 -0.0662 -0.0286 -0.0326 409 TRP A O   
826  C CB  . TRP A 113 ? 0.4326 0.6458 0.6358 -0.0496 -0.0362 -0.0368 409 TRP A CB  
827  C CG  . TRP A 113 ? 0.4665 0.6953 0.6804 -0.0347 -0.0348 -0.0335 409 TRP A CG  
828  C CD1 . TRP A 113 ? 0.5632 0.7770 0.7735 -0.0307 -0.0327 -0.0304 409 TRP A CD1 
829  C CD2 . TRP A 113 ? 0.4831 0.7377 0.7048 -0.0197 -0.0358 -0.0331 409 TRP A CD2 
830  N NE1 . TRP A 113 ? 0.5164 0.7412 0.7290 -0.0153 -0.0323 -0.0287 409 TRP A NE1 
831  C CE2 . TRP A 113 ? 0.4951 0.7427 0.7126 -0.0067 -0.0341 -0.0301 409 TRP A CE2 
832  C CE3 . TRP A 113 ? 0.4853 0.7648 0.7121 -0.0143 -0.0384 -0.0351 409 TRP A CE3 
833  C CZ2 . TRP A 113 ? 0.4837 0.7406 0.6960 0.0135  -0.0349 -0.0290 409 TRP A CZ2 
834  C CZ3 . TRP A 113 ? 0.5171 0.8117 0.7427 0.0067  -0.0392 -0.0335 409 TRP A CZ3 
835  C CH2 . TRP A 113 ? 0.5669 0.8465 0.7824 0.0213  -0.0374 -0.0305 409 TRP A CH2 
836  N N   . ARG A 114 ? 0.6151 0.8217 0.7909 -0.0954 -0.0297 -0.0390 410 ARG A N   
837  C CA  . ARG A 114 ? 0.6896 0.9218 0.8650 -0.1119 -0.0247 -0.0384 410 ARG A CA  
838  C C   . ARG A 114 ? 0.7602 0.9464 0.9115 -0.1200 -0.0223 -0.0355 410 ARG A C   
839  O O   . ARG A 114 ? 0.7203 0.9218 0.8748 -0.1224 -0.0176 -0.0331 410 ARG A O   
840  C CB  . ARG A 114 ? 0.6237 0.8883 0.7938 -0.1415 -0.0247 -0.0423 410 ARG A CB  
841  C CG  . ARG A 114 ? 0.6710 0.9874 0.8475 -0.1600 -0.0189 -0.0416 410 ARG A CG  
842  C CD  . ARG A 114 ? 0.7235 1.0734 0.8897 -0.1988 -0.0195 -0.0452 410 ARG A CD  
843  N NE  . ARG A 114 ? 0.7375 1.1620 0.9183 -0.2137 -0.0136 -0.0444 410 ARG A NE  
844  C CZ  . ARG A 114 ? 0.6939 1.1738 0.8726 -0.2497 -0.0133 -0.0469 410 ARG A CZ  
845  N NH1 . ARG A 114 ? 0.5736 1.1326 0.7680 -0.2603 -0.0070 -0.0457 410 ARG A NH1 
846  N NH2 . ARG A 114 ? 0.6568 1.1167 0.8157 -0.2759 -0.0192 -0.0509 410 ARG A NH2 
847  N N   . ASN A 115 ? 0.7052 0.8348 0.8291 -0.1208 -0.0254 -0.0357 411 ASN A N   
848  C CA  . ASN A 115 ? 0.7860 0.8645 0.8786 -0.1246 -0.0243 -0.0330 411 ASN A CA  
849  C C   . ASN A 115 ? 0.7145 0.7787 0.8155 -0.0968 -0.0258 -0.0293 411 ASN A C   
850  O O   . ASN A 115 ? 0.6178 0.6451 0.6947 -0.0954 -0.0254 -0.0266 411 ASN A O   
851  C CB  . ASN A 115 ? 0.5765 0.5960 0.6244 -0.1358 -0.0275 -0.0355 411 ASN A CB  
852  C CG  . ASN A 115 ? 0.8300 0.8556 0.8592 -0.1726 -0.0266 -0.0390 411 ASN A CG  
853  O OD1 . ASN A 115 ? 0.8866 0.9466 0.9219 -0.1965 -0.0220 -0.0378 411 ASN A OD1 
854  N ND2 . ASN A 115 ? 0.8888 0.8855 0.8939 -0.1786 -0.0310 -0.0435 411 ASN A ND2 
855  N N   . ALA A 116 ? 0.5121 0.6042 0.6427 -0.0768 -0.0279 -0.0290 412 ALA A N   
856  C CA  . ALA A 116 ? 0.6341 0.7204 0.7729 -0.0561 -0.0302 -0.0256 412 ALA A CA  
857  C C   . ALA A 116 ? 0.6527 0.7469 0.7960 -0.0562 -0.0272 -0.0228 412 ALA A C   
858  O O   . ALA A 116 ? 0.7091 0.8318 0.8705 -0.0510 -0.0258 -0.0227 412 ALA A O   
859  C CB  . ALA A 116 ? 0.4179 0.5294 0.5801 -0.0428 -0.0329 -0.0257 412 ALA A CB  
860  N N   . SER A 117 ? 0.6921 0.7561 0.8131 -0.0593 -0.0266 -0.0207 413 SER A N   
861  C CA  . SER A 117 ? 0.6539 0.7221 0.7734 -0.0624 -0.0229 -0.0184 413 SER A CA  
862  C C   . SER A 117 ? 0.6388 0.7189 0.7734 -0.0465 -0.0254 -0.0166 413 SER A C   
863  O O   . SER A 117 ? 0.5847 0.6766 0.7219 -0.0462 -0.0221 -0.0161 413 SER A O   
864  C CB  . SER A 117 ? 0.6265 0.6522 0.7123 -0.0686 -0.0225 -0.0159 413 SER A CB  
865  O OG  . SER A 117 ? 0.5892 0.5848 0.6594 -0.0531 -0.0283 -0.0152 413 SER A OG  
866  N N   . ARG A 118 ? 0.5681 0.6458 0.7089 -0.0348 -0.0310 -0.0159 414 ARG A N   
867  C CA  . ARG A 118 ? 0.5168 0.6021 0.6656 -0.0266 -0.0345 -0.0141 414 ARG A CA  
868  C C   . ARG A 118 ? 0.5191 0.6222 0.6803 -0.0241 -0.0340 -0.0153 414 ARG A C   
869  O O   . ARG A 118 ? 0.5218 0.6208 0.6799 -0.0207 -0.0371 -0.0138 414 ARG A O   
870  C CB  . ARG A 118 ? 0.4594 0.5435 0.6079 -0.0190 -0.0407 -0.0122 414 ARG A CB  
871  C CG  . ARG A 118 ? 0.4740 0.5381 0.6036 -0.0133 -0.0425 -0.0107 414 ARG A CG  
872  C CD  . ARG A 118 ? 0.5997 0.6784 0.7308 -0.0018 -0.0492 -0.0082 414 ARG A CD  
873  N NE  . ARG A 118 ? 0.5858 0.6480 0.6959 0.0079  -0.0518 -0.0062 414 ARG A NE  
874  C CZ  . ARG A 118 ? 0.6706 0.7496 0.7772 0.0229  -0.0579 -0.0042 414 ARG A CZ  
875  N NH1 . ARG A 118 ? 0.7255 0.8428 0.8501 0.0264  -0.0612 -0.0038 414 ARG A NH1 
876  N NH2 . ARG A 118 ? 0.8335 0.8953 0.9169 0.0349  -0.0606 -0.0023 414 ARG A NH2 
877  N N   . CYS A 119 ? 0.5128 0.6326 0.6824 -0.0258 -0.0308 -0.0179 415 CYS A N   
878  C CA  . CYS A 119 ? 0.4787 0.6127 0.6547 -0.0181 -0.0310 -0.0188 415 CYS A CA  
879  C C   . CYS A 119 ? 0.4289 0.5774 0.6015 -0.0123 -0.0262 -0.0202 415 CYS A C   
880  O O   . CYS A 119 ? 0.4738 0.6449 0.6516 -0.0191 -0.0215 -0.0220 415 CYS A O   
881  C CB  . CYS A 119 ? 0.4373 0.5874 0.6242 -0.0194 -0.0316 -0.0208 415 CYS A CB  
882  S SG  . CYS A 119 ? 0.4950 0.6637 0.6850 -0.0066 -0.0319 -0.0218 415 CYS A SG  
883  N N   . VAL A 120 ? 0.6090 0.7447 0.7685 0.0000  -0.0274 -0.0195 416 VAL A N   
884  C CA  . VAL A 120 ? 0.6367 0.7854 0.7871 0.0139  -0.0228 -0.0213 416 VAL A CA  
885  C C   . VAL A 120 ? 0.6347 0.8114 0.7893 0.0284  -0.0218 -0.0234 416 VAL A C   
886  O O   . VAL A 120 ? 0.5595 0.7665 0.7124 0.0419  -0.0170 -0.0254 416 VAL A O   
887  C CB  . VAL A 120 ? 0.6684 0.7798 0.7909 0.0238  -0.0251 -0.0203 416 VAL A CB  
888  C CG1 . VAL A 120 ? 0.6409 0.7255 0.7436 0.0338  -0.0300 -0.0195 416 VAL A CG1 
889  C CG2 . VAL A 120 ? 0.4575 0.5801 0.5675 0.0380  -0.0190 -0.0223 416 VAL A CG2 
890  N N   . GLY A 121 ? 0.5567 0.7307 0.7171 0.0274  -0.0259 -0.0229 417 GLY A N   
891  C CA  . GLY A 121 ? 0.5513 0.7489 0.7114 0.0444  -0.0260 -0.0245 417 GLY A CA  
892  C C   . GLY A 121 ? 0.5727 0.8196 0.7580 0.0349  -0.0242 -0.0271 417 GLY A C   
893  O O   . GLY A 121 ? 0.7564 1.0252 0.9451 0.0453  -0.0261 -0.0283 417 GLY A O   
894  N N   . ARG A 122 ? 0.4659 0.7272 0.6634 0.0137  -0.0210 -0.0280 418 ARG A N   
895  C CA  . ARG A 122 ? 0.4960 0.7900 0.7089 -0.0049 -0.0205 -0.0304 418 ARG A CA  
896  C C   . ARG A 122 ? 0.6093 0.9675 0.8323 0.0001  -0.0174 -0.0332 418 ARG A C   
897  O O   . ARG A 122 ? 0.5848 0.9753 0.8183 -0.0193 -0.0177 -0.0355 418 ARG A O   
898  C CB  . ARG A 122 ? 0.5091 0.7875 0.7193 -0.0306 -0.0182 -0.0300 418 ARG A CB  
899  C CG  . ARG A 122 ? 0.6414 0.8712 0.8440 -0.0369 -0.0223 -0.0284 418 ARG A CG  
900  C CD  . ARG A 122 ? 0.6483 0.8578 0.8385 -0.0572 -0.0202 -0.0280 418 ARG A CD  
901  N NE  . ARG A 122 ? 0.6532 0.8517 0.8354 -0.0550 -0.0170 -0.0255 418 ARG A NE  
902  C CZ  . ARG A 122 ? 0.6238 0.8091 0.7914 -0.0717 -0.0136 -0.0245 418 ARG A CZ  
903  N NH1 . ARG A 122 ? 0.5113 0.6876 0.6661 -0.0938 -0.0132 -0.0257 418 ARG A NH1 
904  N NH2 . ARG A 122 ? 0.7563 0.9322 0.9164 -0.0676 -0.0108 -0.0221 418 ARG A NH2 
905  N N   . ILE A 123 ? 0.5409 0.9204 0.7576 0.0257  -0.0146 -0.0332 419 ILE A N   
906  C CA  . ILE A 123 ? 0.4206 0.8732 0.6471 0.0379  -0.0120 -0.0358 419 ILE A CA  
907  C C   . ILE A 123 ? 0.6143 1.0869 0.8488 0.0428  -0.0177 -0.0374 419 ILE A C   
908  O O   . ILE A 123 ? 0.6144 1.1562 0.8632 0.0406  -0.0174 -0.0401 419 ILE A O   
909  C CB  . ILE A 123 ? 0.5266 0.9878 0.7358 0.0764  -0.0091 -0.0357 419 ILE A CB  
910  C CG1 . ILE A 123 ? 0.6426 1.1969 0.8651 0.0868  -0.0041 -0.0383 419 ILE A CG1 
911  C CG2 . ILE A 123 ? 0.5553 0.9723 0.7407 0.1086  -0.0150 -0.0348 419 ILE A CG2 
912  C CD1 . ILE A 123 ? 0.7755 1.3467 0.9767 0.1378  -0.0034 -0.0393 419 ILE A CD1 
913  N N   . GLN A 124 ? 0.5672 0.9838 0.7923 0.0470  -0.0230 -0.0357 420 GLN A N   
914  C CA  . GLN A 124 ? 0.6619 1.0857 0.8892 0.0546  -0.0285 -0.0365 420 GLN A CA  
915  C C   . GLN A 124 ? 0.6195 1.0411 0.8599 0.0232  -0.0311 -0.0382 420 GLN A C   
916  O O   . GLN A 124 ? 0.4108 0.8335 0.6520 0.0269  -0.0357 -0.0390 420 GLN A O   
917  C CB  . GLN A 124 ? 0.7081 1.0710 0.9114 0.0759  -0.0322 -0.0330 420 GLN A CB  
918  C CG  . GLN A 124 ? 0.8402 1.1966 1.0167 0.1133  -0.0317 -0.0321 420 GLN A CG  
919  C CD  . GLN A 124 ? 0.9769 1.3616 1.1447 0.1414  -0.0355 -0.0329 420 GLN A CD  
920  O OE1 . GLN A 124 ? 0.9747 1.4048 1.1645 0.1309  -0.0377 -0.0351 420 GLN A OE1 
921  N NE2 . GLN A 124 ? 1.0829 1.4355 1.2124 0.1781  -0.0368 -0.0312 420 GLN A NE2 
922  N N   . TRP A 125 ? 0.6435 1.0582 0.8878 -0.0062 -0.0283 -0.0390 421 TRP A N   
923  C CA  . TRP A 125 ? 0.5952 0.9825 0.8378 -0.0317 -0.0310 -0.0404 421 TRP A CA  
924  C C   . TRP A 125 ? 0.6474 1.0727 0.8968 -0.0407 -0.0350 -0.0443 421 TRP A C   
925  O O   . TRP A 125 ? 0.8032 1.2002 1.0472 -0.0466 -0.0389 -0.0455 421 TRP A O   
926  C CB  . TRP A 125 ? 0.5585 0.9308 0.7938 -0.0599 -0.0274 -0.0407 421 TRP A CB  
927  C CG  . TRP A 125 ? 0.6050 1.0354 0.8456 -0.0824 -0.0247 -0.0434 421 TRP A CG  
928  C CD1 . TRP A 125 ? 0.5391 1.0220 0.7883 -0.0784 -0.0195 -0.0428 421 TRP A CD1 
929  C CD2 . TRP A 125 ? 0.6640 1.1115 0.8995 -0.1137 -0.0272 -0.0472 421 TRP A CD2 
930  N NE1 . TRP A 125 ? 0.4980 1.0383 0.7514 -0.1080 -0.0182 -0.0456 421 TRP A NE1 
931  C CE2 . TRP A 125 ? 0.6230 1.1388 0.8661 -0.1326 -0.0234 -0.0484 421 TRP A CE2 
932  C CE3 . TRP A 125 ? 0.5578 0.9688 0.7791 -0.1285 -0.0324 -0.0500 421 TRP A CE3 
933  C CZ2 . TRP A 125 ? 0.6874 1.2361 0.9239 -0.1712 -0.0253 -0.0519 421 TRP A CZ2 
934  C CZ3 . TRP A 125 ? 0.6400 1.0741 0.8507 -0.1638 -0.0345 -0.0542 421 TRP A CZ3 
935  C CH2 . TRP A 125 ? 0.7162 1.2186 0.9344 -0.1874 -0.0313 -0.0550 421 TRP A CH2 
936  N N   . SER A 126 ? 0.6285 1.1231 0.8889 -0.0413 -0.0342 -0.0466 422 SER A N   
937  C CA  . SER A 126 ? 0.7544 1.2922 1.0210 -0.0531 -0.0390 -0.0507 422 SER A CA  
938  C C   . SER A 126 ? 0.8008 1.3334 1.0674 -0.0234 -0.0442 -0.0501 422 SER A C   
939  O O   . SER A 126 ? 0.9071 1.4355 1.1715 -0.0336 -0.0491 -0.0527 422 SER A O   
940  C CB  . SER A 126 ? 0.8573 1.4848 1.1374 -0.0620 -0.0371 -0.0530 422 SER A CB  
941  O OG  . SER A 126 ? 0.9223 1.6035 1.2118 -0.0250 -0.0392 -0.0529 422 SER A OG  
942  N N   . LYS A 127 ? 0.7455 1.2726 1.0080 0.0128  -0.0434 -0.0466 423 LYS A N   
943  C CA  . LYS A 127 ? 0.6481 1.1607 0.9011 0.0414  -0.0480 -0.0448 423 LYS A CA  
944  C C   . LYS A 127 ? 0.7010 1.1382 0.9421 0.0370  -0.0487 -0.0416 423 LYS A C   
945  O O   . LYS A 127 ? 0.6050 0.9975 0.8317 0.0519  -0.0472 -0.0373 423 LYS A O   
946  C CB  . LYS A 127 ? 0.5691 1.0942 0.8097 0.0818  -0.0471 -0.0423 423 LYS A CB  
947  C CG  . LYS A 127 ? 0.7334 1.2978 0.9679 0.1111  -0.0524 -0.0431 423 LYS A CG  
948  C CD  . LYS A 127 ? 0.7948 1.3217 0.9958 0.1560  -0.0531 -0.0389 423 LYS A CD  
949  C CE  . LYS A 127 ? 0.9806 1.5284 1.1676 0.1850  -0.0596 -0.0387 423 LYS A CE  
950  N NZ  . LYS A 127 ? 1.0767 1.5732 1.2175 0.2297  -0.0611 -0.0344 423 LYS A NZ  
951  N N   . LEU A 128 ? 0.7445 1.1701 0.9886 0.0151  -0.0510 -0.0441 424 LEU A N   
952  C CA  . LEU A 128 ? 0.6508 1.0203 0.8858 0.0113  -0.0514 -0.0417 424 LEU A CA  
953  C C   . LEU A 128 ? 0.6619 1.0372 0.8948 0.0093  -0.0559 -0.0441 424 LEU A C   
954  O O   . LEU A 128 ? 0.5103 0.9200 0.7484 -0.0052 -0.0587 -0.0493 424 LEU A O   
955  C CB  . LEU A 128 ? 0.5538 0.8930 0.7879 -0.0111 -0.0485 -0.0426 424 LEU A CB  
956  C CG  . LEU A 128 ? 0.4923 0.7855 0.7177 -0.0136 -0.0487 -0.0410 424 LEU A CG  
957  C CD1 . LEU A 128 ? 0.3507 0.6197 0.5721 0.0015  -0.0474 -0.0349 424 LEU A CD1 
958  C CD2 . LEU A 128 ? 0.5341 0.8009 0.7518 -0.0313 -0.0469 -0.0431 424 LEU A CD2 
959  N N   . GLN A 129 ? 0.6994 1.0420 0.9223 0.0209  -0.0567 -0.0402 425 GLN A N   
960  C CA  . GLN A 129 ? 0.6247 0.9689 0.8424 0.0223  -0.0604 -0.0415 425 GLN A CA  
961  C C   . GLN A 129 ? 0.6081 0.9192 0.8217 0.0087  -0.0588 -0.0425 425 GLN A C   
962  O O   . GLN A 129 ? 0.6935 0.9750 0.9032 0.0114  -0.0557 -0.0379 425 GLN A O   
963  C CB  . GLN A 129 ? 0.6886 1.0201 0.8918 0.0454  -0.0618 -0.0358 425 GLN A CB  
964  C CG  . GLN A 129 ? 0.7972 1.1217 0.9917 0.0470  -0.0644 -0.0354 425 GLN A CG  
965  C CD  . GLN A 129 ? 0.8092 1.1743 1.0104 0.0424  -0.0694 -0.0421 425 GLN A CD  
966  O OE1 . GLN A 129 ? 0.7861 1.1936 0.9931 0.0505  -0.0725 -0.0443 425 GLN A OE1 
967  N NE2 . GLN A 129 ? 0.8799 1.2358 1.0785 0.0298  -0.0704 -0.0456 425 GLN A NE2 
968  N N   . VAL A 130 ? 0.5219 0.8391 0.7326 -0.0055 -0.0612 -0.0486 426 VAL A N   
969  C CA  . VAL A 130 ? 0.5278 0.8114 0.7269 -0.0135 -0.0599 -0.0509 426 VAL A CA  
970  C C   . VAL A 130 ? 0.5040 0.7846 0.6950 -0.0046 -0.0616 -0.0509 426 VAL A C   
971  O O   . VAL A 130 ? 0.3245 0.6286 0.5145 -0.0042 -0.0660 -0.0537 426 VAL A O   
972  C CB  . VAL A 130 ? 0.5299 0.8063 0.7174 -0.0357 -0.0615 -0.0581 426 VAL A CB  
973  C CG1 . VAL A 130 ? 0.4525 0.6820 0.6173 -0.0368 -0.0600 -0.0604 426 VAL A CG1 
974  C CG2 . VAL A 130 ? 0.3996 0.6900 0.5961 -0.0467 -0.0594 -0.0574 426 VAL A CG2 
975  N N   . PHE A 131 ? 0.5485 0.8069 0.7342 0.0031  -0.0582 -0.0473 427 PHE A N   
976  C CA  . PHE A 131 ? 0.5695 0.8259 0.7461 0.0111  -0.0582 -0.0466 427 PHE A CA  
977  C C   . PHE A 131 ? 0.6112 0.8451 0.7718 0.0097  -0.0570 -0.0521 427 PHE A C   
978  O O   . PHE A 131 ? 0.5022 0.7220 0.6611 0.0140  -0.0533 -0.0501 427 PHE A O   
979  C CB  . PHE A 131 ? 0.4654 0.7205 0.6441 0.0201  -0.0546 -0.0377 427 PHE A CB  
980  C CG  . PHE A 131 ? 0.4940 0.7560 0.6729 0.0258  -0.0565 -0.0325 427 PHE A CG  
981  C CD1 . PHE A 131 ? 0.5528 0.8267 0.7243 0.0329  -0.0603 -0.0332 427 PHE A CD1 
982  C CD2 . PHE A 131 ? 0.4776 0.7298 0.6580 0.0267  -0.0548 -0.0269 427 PHE A CD2 
983  C CE1 . PHE A 131 ? 0.5910 0.8657 0.7542 0.0444  -0.0625 -0.0284 427 PHE A CE1 
984  C CE2 . PHE A 131 ? 0.4757 0.7236 0.6449 0.0368  -0.0569 -0.0226 427 PHE A CE2 
985  C CZ  . PHE A 131 ? 0.6219 0.8802 0.7814 0.0475  -0.0607 -0.0231 427 PHE A CZ  
986  N N   . ASP A 132 ? 0.6210 0.8503 0.7655 0.0054  -0.0607 -0.0592 428 ASP A N   
987  C CA  . ASP A 132 ? 0.4816 0.6787 0.5983 0.0074  -0.0603 -0.0655 428 ASP A CA  
988  C C   . ASP A 132 ? 0.5430 0.7448 0.6560 0.0262  -0.0561 -0.0622 428 ASP A C   
989  O O   . ASP A 132 ? 0.7176 0.9322 0.8276 0.0297  -0.0574 -0.0625 428 ASP A O   
990  C CB  . ASP A 132 ? 0.5460 0.7323 0.6404 -0.0080 -0.0666 -0.0747 428 ASP A CB  
991  C CG  . ASP A 132 ? 0.6243 0.7601 0.6760 -0.0065 -0.0670 -0.0823 428 ASP A CG  
992  O OD1 . ASP A 132 ? 0.6496 0.7633 0.6726 -0.0251 -0.0726 -0.0905 428 ASP A OD1 
993  O OD2 . ASP A 132 ? 0.5592 0.6773 0.6017 0.0137  -0.0621 -0.0803 428 ASP A OD2 
994  N N   . ALA A 133 ? 0.6480 0.8461 0.7619 0.0381  -0.0510 -0.0585 429 ALA A N   
995  C CA  . ALA A 133 ? 0.5165 0.7276 0.6249 0.0557  -0.0462 -0.0559 429 ALA A CA  
996  C C   . ALA A 133 ? 0.6076 0.7900 0.6832 0.0726  -0.0451 -0.0629 429 ALA A C   
997  O O   . ALA A 133 ? 0.7502 0.9495 0.8225 0.0925  -0.0400 -0.0604 429 ALA A O   
998  C CB  . ALA A 133 ? 0.3966 0.6375 0.5283 0.0578  -0.0413 -0.0459 429 ALA A CB  
999  N N   . ARG A 134 ? 0.5458 0.6849 0.5921 0.0653  -0.0500 -0.0717 430 ARG A N   
1000 C CA  . ARG A 134 ? 0.6972 0.7920 0.6976 0.0835  -0.0498 -0.0790 430 ARG A CA  
1001 C C   . ARG A 134 ? 0.7346 0.8284 0.7105 0.1023  -0.0483 -0.0834 430 ARG A C   
1002 O O   . ARG A 134 ? 0.7750 0.8365 0.7103 0.1272  -0.0467 -0.0886 430 ARG A O   
1003 C CB  . ARG A 134 ? 0.8053 0.8435 0.7705 0.0641  -0.0558 -0.0869 430 ARG A CB  
1004 C CG  . ARG A 134 ? 0.8103 0.8307 0.7775 0.0570  -0.0556 -0.0842 430 ARG A CG  
1005 C CD  . ARG A 134 ? 0.9454 0.9082 0.8707 0.0316  -0.0613 -0.0917 430 ARG A CD  
1006 N NE  . ARG A 134 ? 0.8955 0.8830 0.8385 0.0001  -0.0660 -0.0938 430 ARG A NE  
1007 C CZ  . ARG A 134 ? 0.9190 0.8719 0.8276 -0.0298 -0.0718 -0.1009 430 ARG A CZ  
1008 N NH1 . ARG A 134 ? 1.0164 0.8942 0.8635 -0.0342 -0.0737 -0.1066 430 ARG A NH1 
1009 N NH2 . ARG A 134 ? 0.7895 0.7829 0.7207 -0.0558 -0.0762 -0.1023 430 ARG A NH2 
1010 N N   . ASP A 135 ? 0.6809 0.8065 0.6753 0.0944  -0.0487 -0.0815 431 ASP A N   
1011 C CA  . ASP A 135 ? 0.8128 0.9456 0.7879 0.1126  -0.0461 -0.0842 431 ASP A CA  
1012 C C   . ASP A 135 ? 0.8325 1.0183 0.8305 0.1321  -0.0374 -0.0754 431 ASP A C   
1013 O O   . ASP A 135 ? 0.7978 1.0006 0.7839 0.1473  -0.0336 -0.0762 431 ASP A O   
1014 C CB  . ASP A 135 ? 0.7652 0.9086 0.7462 0.0949  -0.0510 -0.0857 431 ASP A CB  
1015 C CG  . ASP A 135 ? 0.8370 1.0263 0.8642 0.0803  -0.0504 -0.0753 431 ASP A CG  
1016 O OD1 . ASP A 135 ? 0.8260 1.0436 0.8621 0.0841  -0.0479 -0.0704 431 ASP A OD1 
1017 O OD2 . ASP A 135 ? 0.7106 0.9033 0.7600 0.0666  -0.0521 -0.0719 431 ASP A OD2 
1018 N N   . CYS A 136 ? 0.6684 0.8835 0.6973 0.1293  -0.0341 -0.0672 432 CYS A N   
1019 C CA  . CYS A 136 ? 0.7410 1.0143 0.7936 0.1381  -0.0265 -0.0578 432 CYS A CA  
1020 C C   . CYS A 136 ? 0.8402 1.1248 0.8694 0.1728  -0.0213 -0.0610 432 CYS A C   
1021 O O   . CYS A 136 ? 0.9601 1.2021 0.9585 0.1904  -0.0238 -0.0682 432 CYS A O   
1022 C CB  . CYS A 136 ? 0.6222 0.9184 0.7098 0.1202  -0.0262 -0.0488 432 CYS A CB  
1023 S SG  . CYS A 136 ? 0.6217 0.9899 0.7379 0.1145  -0.0185 -0.0356 432 CYS A SG  
1024 N N   . THR A 137 ? 0.6993 1.0415 0.7381 0.1838  -0.0139 -0.0555 433 THR A N   
1025 C CA  . THR A 137 ? 0.7455 1.1141 0.7623 0.2222  -0.0079 -0.0584 433 THR A CA  
1026 C C   . THR A 137 ? 0.7404 1.1968 0.7884 0.2255  -0.0001 -0.0479 433 THR A C   
1027 O O   . THR A 137 ? 0.7295 1.2203 0.7640 0.2606  0.0045  -0.0497 433 THR A O   
1028 C CB  . THR A 137 ? 0.8916 1.2499 0.8759 0.2404  -0.0055 -0.0649 433 THR A CB  
1029 O OG1 . THR A 137 ? 0.8622 1.2881 0.8712 0.2308  0.0018  -0.0560 433 THR A OG1 
1030 C CG2 . THR A 137 ? 0.9645 1.2536 0.9270 0.2223  -0.0137 -0.0728 433 THR A CG2 
1031 N N   . THR A 138 ? 0.7813 1.2751 0.8651 0.1904  0.0014  -0.0372 434 THR A N   
1032 C CA  . THR A 138 ? 0.6455 1.2252 0.7533 0.1833  0.0091  -0.0268 434 THR A CA  
1033 C C   . THR A 138 ? 0.5930 1.1849 0.7308 0.1478  0.0064  -0.0176 434 THR A C   
1034 O O   . THR A 138 ? 0.5352 1.0725 0.6770 0.1261  0.0000  -0.0178 434 THR A O   
1035 C CB  . THR A 138 ? 0.5920 1.2023 0.6984 0.1711  0.0151  -0.0218 434 THR A CB  
1036 O OG1 . THR A 138 ? 0.6001 1.1488 0.7005 0.1494  0.0092  -0.0232 434 THR A OG1 
1037 C CG2 . THR A 138 ? 0.5712 1.2037 0.6505 0.2114  0.0212  -0.0288 434 THR A CG2 
1038 N N   . ALA A 139 ? 0.5204 1.1885 0.6768 0.1419  0.0114  -0.0095 435 ALA A N   
1039 C CA  . ALA A 139 ? 0.5893 1.2701 0.7680 0.1041  0.0089  -0.0004 435 ALA A CA  
1040 C C   . ALA A 139 ? 0.6431 1.3005 0.8204 0.0650  0.0088  0.0071  435 ALA A C   
1041 O O   . ALA A 139 ? 0.7322 1.3592 0.9149 0.0362  0.0042  0.0119  435 ALA A O   
1042 C CB  . ALA A 139 ? 0.6458 1.4215 0.8417 0.1023  0.0138  0.0065  435 ALA A CB  
1043 N N   . HIS A 140 ? 0.7074 1.3734 0.8720 0.0660  0.0137  0.0082  436 HIS A N   
1044 C CA  . HIS A 140 ? 0.6499 1.2800 0.8041 0.0349  0.0126  0.0147  436 HIS A CA  
1045 C C   . HIS A 140 ? 0.5692 1.1179 0.7148 0.0403  0.0043  0.0075  436 HIS A C   
1046 O O   . HIS A 140 ? 0.5889 1.0977 0.7298 0.0170  -0.0001 0.0123  436 HIS A O   
1047 C CB  . HIS A 140 ? 0.7095 1.3728 0.8502 0.0350  0.0202  0.0182  436 HIS A CB  
1048 C CG  . HIS A 140 ? 0.7080 1.4491 0.8537 0.0092  0.0285  0.0299  436 HIS A CG  
1049 N ND1 . HIS A 140 ? 0.6734 1.4085 0.8033 -0.0314 0.0309  0.0415  436 HIS A ND1 
1050 C CD2 . HIS A 140 ? 0.6776 1.5076 0.8385 0.0172  0.0350  0.0319  436 HIS A CD2 
1051 C CE1 . HIS A 140 ? 0.6415 1.4585 0.7769 -0.0530 0.0387  0.0504  436 HIS A CE1 
1052 N NE2 . HIS A 140 ? 0.6999 1.5827 0.8575 -0.0230 0.0414  0.0447  436 HIS A NE2 
1053 N N   . GLY A 141 ? 0.5244 1.0480 0.6627 0.0708  0.0018  -0.0040 437 GLY A N   
1054 C CA  . GLY A 141 ? 0.6007 1.0587 0.7332 0.0721  -0.0065 -0.0112 437 GLY A CA  
1055 C C   . GLY A 141 ? 0.6279 1.0634 0.7745 0.0601  -0.0117 -0.0102 437 GLY A C   
1056 O O   . GLY A 141 ? 0.6303 1.0271 0.7767 0.0471  -0.0171 -0.0098 437 GLY A O   
1057 N N   . MET A 142 ? 0.5925 1.0550 0.7500 0.0672  -0.0100 -0.0099 438 MET A N   
1058 C CA  . MET A 142 ? 0.5231 0.9675 0.6931 0.0545  -0.0144 -0.0082 438 MET A CA  
1059 C C   . MET A 142 ? 0.5513 0.9924 0.7239 0.0228  -0.0150 0.0018  438 MET A C   
1060 O O   . MET A 142 ? 0.5218 0.9204 0.6930 0.0128  -0.0201 0.0018  438 MET A O   
1061 C CB  . MET A 142 ? 0.5767 1.0592 0.7561 0.0671  -0.0125 -0.0081 438 MET A CB  
1062 C CG  . MET A 142 ? 0.5699 1.0346 0.7351 0.1013  -0.0135 -0.0182 438 MET A CG  
1063 S SD  . MET A 142 ? 0.5949 1.1119 0.7657 0.1241  -0.0113 -0.0172 438 MET A SD  
1064 C CE  . MET A 142 ? 0.5338 1.0253 0.7203 0.1019  -0.0173 -0.0141 438 MET A CE  
1065 N N   . PHE A 143 ? 0.5541 1.0368 0.7240 0.0070  -0.0096 0.0105  439 PHE A N   
1066 C CA  . PHE A 143 ? 0.5400 1.0103 0.6998 -0.0266 -0.0101 0.0208  439 PHE A CA  
1067 C C   . PHE A 143 ? 0.5970 1.0085 0.7369 -0.0303 -0.0141 0.0210  439 PHE A C   
1068 O O   . PHE A 143 ? 0.5823 0.9535 0.7093 -0.0459 -0.0181 0.0253  439 PHE A O   
1069 C CB  . PHE A 143 ? 0.3844 0.9140 0.5403 -0.0463 -0.0030 0.0299  439 PHE A CB  
1070 C CG  . PHE A 143 ? 0.6197 1.1259 0.7505 -0.0848 -0.0030 0.0410  439 PHE A CG  
1071 C CD1 . PHE A 143 ? 0.7040 1.2126 0.8123 -0.0979 0.0015  0.0475  439 PHE A CD1 
1072 C CD2 . PHE A 143 ? 0.4907 0.9656 0.6130 -0.1079 -0.0078 0.0451  439 PHE A CD2 
1073 C CE1 . PHE A 143 ? 0.7367 1.2111 0.8101 -0.1346 0.0012  0.0584  439 PHE A CE1 
1074 C CE2 . PHE A 143 ? 0.5316 0.9706 0.6176 -0.1437 -0.0083 0.0552  439 PHE A CE2 
1075 C CZ  . PHE A 143 ? 0.7391 1.1748 0.7987 -0.1574 -0.0040 0.0620  439 PHE A CZ  
1076 N N   . ASN A 144 ? 0.6578 1.0632 0.7922 -0.0126 -0.0136 0.0159  440 ASN A N   
1077 C CA  . ASN A 144 ? 0.5090 0.8671 0.6263 -0.0103 -0.0185 0.0150  440 ASN A CA  
1078 C C   . ASN A 144 ? 0.6469 0.9696 0.7726 -0.0012 -0.0256 0.0082  440 ASN A C   
1079 O O   . ASN A 144 ? 0.8315 1.1197 0.9445 -0.0081 -0.0296 0.0118  440 ASN A O   
1080 C CB  . ASN A 144 ? 0.5770 0.9436 0.6876 0.0064  -0.0171 0.0099  440 ASN A CB  
1081 C CG  . ASN A 144 ? 0.5707 0.9005 0.6604 0.0069  -0.0217 0.0113  440 ASN A CG  
1082 O OD1 . ASN A 144 ? 0.6690 0.9809 0.7354 -0.0087 -0.0209 0.0210  440 ASN A OD1 
1083 N ND2 . ASN A 144 ? 0.5705 0.8876 0.6631 0.0243  -0.0270 0.0016  440 ASN A ND2 
1084 N N   . TYR A 145 ? 0.6556 0.9847 0.7977 0.0148  -0.0270 -0.0014 441 TYR A N   
1085 C CA  . TYR A 145 ? 0.6827 0.9848 0.8326 0.0192  -0.0329 -0.0075 441 TYR A CA  
1086 C C   . TYR A 145 ? 0.5322 0.8217 0.6850 0.0063  -0.0340 -0.0019 441 TYR A C   
1087 O O   . TYR A 145 ? 0.6231 0.8867 0.7725 0.0068  -0.0383 -0.0027 441 TYR A O   
1088 C CB  . TYR A 145 ? 0.5358 0.8409 0.6945 0.0325  -0.0334 -0.0169 441 TYR A CB  
1089 C CG  . TYR A 145 ? 0.4768 0.7707 0.6251 0.0434  -0.0362 -0.0258 441 TYR A CG  
1090 C CD1 . TYR A 145 ? 0.5252 0.8306 0.6625 0.0565  -0.0329 -0.0297 441 TYR A CD1 
1091 C CD2 . TYR A 145 ? 0.4607 0.7359 0.6077 0.0406  -0.0424 -0.0306 441 TYR A CD2 
1092 C CE1 . TYR A 145 ? 0.4473 0.7356 0.5681 0.0645  -0.0361 -0.0385 441 TYR A CE1 
1093 C CE2 . TYR A 145 ? 0.5444 0.8117 0.6794 0.0453  -0.0459 -0.0391 441 TYR A CE2 
1094 C CZ  . TYR A 145 ? 0.6213 0.8900 0.7410 0.0562  -0.0431 -0.0432 441 TYR A CZ  
1095 O OH  . TYR A 145 ? 0.6273 0.8813 0.7279 0.0592  -0.0474 -0.0522 441 TYR A OH  
1096 N N   . ILE A 146 ? 0.5143 0.8259 0.6720 -0.0043 -0.0303 0.0035  442 ILE A N   
1097 C CA  . ILE A 146 ? 0.4718 0.7700 0.6291 -0.0185 -0.0319 0.0081  442 ILE A CA  
1098 C C   . ILE A 146 ? 0.4407 0.7051 0.5701 -0.0337 -0.0334 0.0160  442 ILE A C   
1099 O O   . ILE A 146 ? 0.4965 0.7273 0.6159 -0.0362 -0.0369 0.0168  442 ILE A O   
1100 C CB  . ILE A 146 ? 0.5699 0.9082 0.7387 -0.0272 -0.0285 0.0114  442 ILE A CB  
1101 C CG1 . ILE A 146 ? 0.5332 0.8886 0.7199 -0.0057 -0.0284 0.0031  442 ILE A CG1 
1102 C CG2 . ILE A 146 ? 0.5440 0.8678 0.7061 -0.0480 -0.0307 0.0171  442 ILE A CG2 
1103 C CD1 . ILE A 146 ? 0.3880 0.7880 0.5858 -0.0064 -0.0261 0.0056  442 ILE A CD1 
1104 N N   . CYS A 147 ? 0.6424 0.9092 0.7524 -0.0421 -0.0307 0.0219  443 CYS A N   
1105 C CA  . CYS A 147 ? 0.5147 0.7344 0.5858 -0.0540 -0.0329 0.0296  443 CYS A CA  
1106 C C   . CYS A 147 ? 0.5370 0.7213 0.5994 -0.0314 -0.0384 0.0247  443 CYS A C   
1107 O O   . CYS A 147 ? 0.6998 0.8398 0.7352 -0.0304 -0.0420 0.0276  443 CYS A O   
1108 C CB  . CYS A 147 ? 0.5143 0.7395 0.5609 -0.0681 -0.0288 0.0374  443 CYS A CB  
1109 S SG  . CYS A 147 ? 0.6205 0.8910 0.6640 -0.1043 -0.0220 0.0469  443 CYS A SG  
1110 N N   . ASN A 148 ? 0.5270 0.7323 0.6091 -0.0124 -0.0393 0.0170  444 ASN A N   
1111 C CA  . ASN A 148 ? 0.5426 0.7313 0.6210 0.0077  -0.0449 0.0119  444 ASN A CA  
1112 C C   . ASN A 148 ? 0.6345 0.8175 0.7271 0.0138  -0.0478 0.0072  444 ASN A C   
1113 O O   . ASN A 148 ? 0.5403 0.7072 0.6218 0.0285  -0.0521 0.0058  444 ASN A O   
1114 C CB  . ASN A 148 ? 0.5927 0.8097 0.6887 0.0201  -0.0459 0.0039  444 ASN A CB  
1115 C CG  . ASN A 148 ? 0.6588 0.8746 0.7338 0.0212  -0.0449 0.0079  444 ASN A CG  
1116 O OD1 . ASN A 148 ? 0.7082 0.9008 0.7535 0.0111  -0.0430 0.0175  444 ASN A OD1 
1117 N ND2 . ASN A 148 ? 0.4885 0.7251 0.5734 0.0315  -0.0463 0.0007  444 ASN A ND2 
1118 N N   . HIS A 149 ? 0.5956 0.7960 0.7119 0.0055  -0.0453 0.0047  445 HIS A N   
1119 C CA  . HIS A 149 ? 0.6008 0.7939 0.7276 0.0080  -0.0471 0.0015  445 HIS A CA  
1120 C C   . HIS A 149 ? 0.6002 0.7554 0.6981 0.0017  -0.0481 0.0085  445 HIS A C   
1121 O O   . HIS A 149 ? 0.6625 0.7967 0.7478 0.0150  -0.0511 0.0072  445 HIS A O   
1122 C CB  . HIS A 149 ? 0.7239 0.9404 0.8766 0.0020  -0.0445 -0.0022 445 HIS A CB  
1123 C CG  . HIS A 149 ? 0.5361 0.7453 0.6986 0.0023  -0.0456 -0.0048 445 HIS A CG  
1124 N ND1 . HIS A 149 ? 0.4504 0.6730 0.6323 0.0051  -0.0452 -0.0113 445 HIS A ND1 
1125 C CD2 . HIS A 149 ? 0.5939 0.7794 0.7441 0.0001  -0.0469 -0.0018 445 HIS A CD2 
1126 C CE1 . HIS A 149 ? 0.5986 0.8110 0.7835 0.0035  -0.0459 -0.0117 445 HIS A CE1 
1127 N NE2 . HIS A 149 ? 0.5379 0.7297 0.7053 0.0014  -0.0469 -0.0063 445 HIS A NE2 
1128 N N   . VAL A 150 ? 0.4647 0.6116 0.5476 -0.0190 -0.0456 0.0157  446 VAL A N   
1129 C CA  . VAL A 150 ? 0.5705 0.6705 0.6141 -0.0315 -0.0471 0.0227  446 VAL A CA  
1130 C C   . VAL A 150 ? 0.6895 0.7431 0.6925 -0.0141 -0.0507 0.0247  446 VAL A C   
1131 O O   . VAL A 150 ? 0.7227 0.7403 0.7027 -0.0023 -0.0536 0.0242  446 VAL A O   
1132 C CB  . VAL A 150 ? 0.5945 0.6947 0.6189 -0.0624 -0.0444 0.0313  446 VAL A CB  
1133 C CG1 . VAL A 150 ? 0.6581 0.6944 0.6273 -0.0794 -0.0471 0.0385  446 VAL A CG1 
1134 C CG2 . VAL A 150 ? 0.6200 0.7731 0.6814 -0.0756 -0.0414 0.0298  446 VAL A CG2 
1135 N N   . LYS A 151 ? 0.6225 0.6767 0.6130 -0.0091 -0.0505 0.0270  447 LYS A N   
1136 C CA  . LYS A 151 ? 0.7406 0.7486 0.6853 0.0105  -0.0545 0.0299  447 LYS A CA  
1137 C C   . LYS A 151 ? 0.7907 0.8110 0.7496 0.0433  -0.0583 0.0223  447 LYS A C   
1138 O O   . LYS A 151 ? 0.9102 0.8889 0.8318 0.0618  -0.0616 0.0235  447 LYS A O   
1139 C CB  . LYS A 151 ? 0.7347 0.7493 0.6682 0.0108  -0.0537 0.0333  447 LYS A CB  
1140 C CG  . LYS A 151 ? 0.7738 0.7322 0.6488 0.0301  -0.0579 0.0383  447 LYS A CG  
1141 C CD  . LYS A 151 ? 0.7497 0.7050 0.6040 0.0226  -0.0563 0.0441  447 LYS A CD  
1142 C CE  . LYS A 151 ? 0.7612 0.6424 0.5405 0.0354  -0.0602 0.0520  447 LYS A CE  
1143 N NZ  . LYS A 151 ? 0.8105 0.6902 0.5691 0.0273  -0.0582 0.0580  447 LYS A NZ  
1144 N N   . TYR A 152 ? 0.7512 0.8287 0.7595 0.0506  -0.0581 0.0142  448 TYR A N   
1145 C CA  . TYR A 152 ? 0.8110 0.9139 0.8369 0.0747  -0.0614 0.0069  448 TYR A CA  
1146 C C   . TYR A 152 ? 0.7323 0.8232 0.7596 0.0761  -0.0607 0.0055  448 TYR A C   
1147 O O   . TYR A 152 ? 0.7815 0.8554 0.7849 0.0997  -0.0632 0.0051  448 TYR A O   
1148 C CB  . TYR A 152 ? 0.7390 0.8996 0.8119 0.0719  -0.0613 -0.0014 448 TYR A CB  
1149 C CG  . TYR A 152 ? 0.7213 0.9169 0.8143 0.0875  -0.0640 -0.0087 448 TYR A CG  
1150 C CD1 . TYR A 152 ? 0.7667 0.9856 0.8528 0.1101  -0.0690 -0.0111 448 TYR A CD1 
1151 C CD2 . TYR A 152 ? 0.5641 0.7739 0.6812 0.0792  -0.0618 -0.0125 448 TYR A CD2 
1152 C CE1 . TYR A 152 ? 0.6626 0.9263 0.7680 0.1220  -0.0712 -0.0172 448 TYR A CE1 
1153 C CE2 . TYR A 152 ? 0.5136 0.7606 0.6473 0.0896  -0.0634 -0.0183 448 TYR A CE2 
1154 C CZ  . TYR A 152 ? 0.5804 0.8583 0.7095 0.1100  -0.0680 -0.0206 448 TYR A CZ  
1155 O OH  . TYR A 152 ? 0.6413 0.9698 0.7882 0.1184  -0.0694 -0.0261 448 TYR A OH  
1156 N N   . ALA A 153 ? 0.7281 0.8301 0.7814 0.0544  -0.0573 0.0044  449 ALA A N   
1157 C CA  . ALA A 153 ? 0.5999 0.6951 0.6574 0.0558  -0.0566 0.0024  449 ALA A CA  
1158 C C   . ALA A 153 ? 0.7670 0.8013 0.7718 0.0626  -0.0583 0.0079  449 ALA A C   
1159 O O   . ALA A 153 ? 0.7282 0.7527 0.7253 0.0764  -0.0587 0.0055  449 ALA A O   
1160 C CB  . ALA A 153 ? 0.5898 0.7011 0.6763 0.0322  -0.0534 0.0015  449 ALA A CB  
1161 N N   . THR A 154 ? 0.7028 0.6921 0.6654 0.0526  -0.0591 0.0153  450 THR A N   
1162 C CA  . THR A 154 ? 0.7229 0.6383 0.6214 0.0544  -0.0613 0.0209  450 THR A CA  
1163 C C   . THR A 154 ? 0.8884 0.7728 0.7440 0.0939  -0.0651 0.0206  450 THR A C   
1164 O O   . THR A 154 ? 0.8782 0.7251 0.6987 0.1148  -0.0668 0.0196  450 THR A O   
1165 C CB  . THR A 154 ? 0.7941 0.6718 0.6584 0.0209  -0.0606 0.0295  450 THR A CB  
1166 O OG1 . THR A 154 ? 0.6797 0.5939 0.5822 -0.0113 -0.0576 0.0295  450 THR A OG1 
1167 C CG2 . THR A 154 ? 0.9235 0.7112 0.7080 0.0189  -0.0638 0.0355  450 THR A CG2 
1168 N N   . ASN A 155 ? 0.9153 0.8161 0.7703 0.1084  -0.0667 0.0213  451 ASN A N   
1169 C CA  . ASN A 155 ? 0.9353 0.8263 0.7584 0.1525  -0.0710 0.0199  451 ASN A CA  
1170 C C   . ASN A 155 ? 0.9714 0.7682 0.7086 0.1709  -0.0739 0.0252  451 ASN A C   
1171 O O   . ASN A 155 ? 1.0789 0.8663 0.7907 0.2114  -0.0763 0.0221  451 ASN A O   
1172 C CB  . ASN A 155 ? 0.8998 0.8636 0.7727 0.1764  -0.0710 0.0109  451 ASN A CB  
1173 C CG  . ASN A 155 ? 0.9678 0.9490 0.8197 0.2227  -0.0756 0.0089  451 ASN A CG  
1174 O OD1 . ASN A 155 ? 1.0199 0.9685 0.8309 0.2368  -0.0791 0.0135  451 ASN A OD1 
1175 N ND2 . ASN A 155 ? 1.0002 1.0357 0.8776 0.2472  -0.0756 0.0024  451 ASN A ND2 
1176 N N   . LYS A 156 ? 0.8679 0.5937 0.5549 0.1405  -0.0736 0.0333  452 LYS A N   
1177 C CA  . LYS A 156 ? 1.1405 0.7571 0.7278 0.1513  -0.0772 0.0398  452 LYS A CA  
1178 C C   . LYS A 156 ? 1.0638 0.6376 0.6237 0.1528  -0.0775 0.0375  452 LYS A C   
1179 O O   . LYS A 156 ? 1.3048 0.7829 0.7755 0.1716  -0.0811 0.0407  452 LYS A O   
1180 C CB  . LYS A 156 ? 1.3549 0.9430 0.8907 0.2054  -0.0821 0.0403  452 LYS A CB  
1181 C CG  . LYS A 156 ? 1.4888 1.1075 1.0366 0.2103  -0.0833 0.0430  452 LYS A CG  
1182 C CD  . LYS A 156 ? 1.6357 1.1975 1.1053 0.2630  -0.0894 0.0460  452 LYS A CD  
1183 C CE  . LYS A 156 ? 1.7427 1.3201 1.2037 0.3189  -0.0922 0.0390  452 LYS A CE  
1184 N NZ  . LYS A 156 ? 1.7005 1.4035 1.2474 0.3425  -0.0923 0.0301  452 LYS A NZ  
1185 N N   . GLY A 157 ? 1.0724 0.7098 0.7019 0.1339  -0.0740 0.0319  453 GLY A N   
1186 C CA  . GLY A 157 ? 1.0466 0.6631 0.6658 0.1381  -0.0737 0.0281  453 GLY A CA  
1187 C C   . GLY A 157 ? 1.0579 0.7444 0.7263 0.1765  -0.0721 0.0194  453 GLY A C   
1188 O O   . GLY A 157 ? 1.0352 0.7327 0.7209 0.1736  -0.0701 0.0153  453 GLY A O   
1189 N N   . ASN A 158 ? 0.9468 0.6841 0.6364 0.2107  -0.0730 0.0167  454 ASN A N   
1190 C CA  . ASN A 158 ? 0.9738 0.7957 0.7173 0.2395  -0.0711 0.0087  454 ASN A CA  
1191 C C   . ASN A 158 ? 0.9059 0.8133 0.7383 0.2046  -0.0674 0.0049  454 ASN A C   
1192 O O   . ASN A 158 ? 0.8256 0.7988 0.7019 0.2076  -0.0676 0.0022  454 ASN A O   
1193 C CB  . ASN A 158 ? 0.9516 0.8001 0.6796 0.2878  -0.0746 0.0072  454 ASN A CB  
1194 C CG  . ASN A 158 ? 1.0899 1.0248 0.8604 0.3192  -0.0729 -0.0005 454 ASN A CG  
1195 O OD1 . ASN A 158 ? 1.2012 1.1800 1.0201 0.3000  -0.0684 -0.0047 454 ASN A OD1 
1196 N ND2 . ASN A 158 ? 1.1188 1.0821 0.8696 0.3675  -0.0763 -0.0020 454 ASN A ND2 
1197 N N   . LEU A 159 ? 0.8116 0.7142 0.6650 0.1728  -0.0643 0.0046  455 LEU A N   
1198 C CA  . LEU A 159 ? 0.8503 0.8096 0.7705 0.1373  -0.0613 0.0027  455 LEU A CA  
1199 C C   . LEU A 159 ? 0.6832 0.7276 0.6625 0.1470  -0.0594 -0.0044 455 LEU A C   
1200 O O   . LEU A 159 ? 0.7605 0.8326 0.7428 0.1726  -0.0587 -0.0085 455 LEU A O   
1201 C CB  . LEU A 159 ? 0.7889 0.7278 0.7143 0.1084  -0.0593 0.0034  455 LEU A CB  
1202 C CG  . LEU A 159 ? 0.8727 0.7690 0.7757 0.0728  -0.0602 0.0101  455 LEU A CG  
1203 C CD1 . LEU A 159 ? 0.9246 0.7481 0.7558 0.0810  -0.0637 0.0162  455 LEU A CD1 
1204 C CD2 . LEU A 159 ? 1.0120 0.8857 0.9089 0.0487  -0.0599 0.0110  455 LEU A CD2 
1205 N N   . ARG A 160 ? 0.6694 0.7548 0.6919 0.1245  -0.0586 -0.0057 456 ARG A N   
1206 C CA  . ARG A 160 ? 0.6213 0.7785 0.6939 0.1224  -0.0576 -0.0121 456 ARG A CA  
1207 C C   . ARG A 160 ? 0.5262 0.6954 0.6338 0.0896  -0.0548 -0.0133 456 ARG A C   
1208 O O   . ARG A 160 ? 0.6517 0.7932 0.7523 0.0720  -0.0545 -0.0091 456 ARG A O   
1209 C CB  . ARG A 160 ? 0.7086 0.8949 0.7849 0.1335  -0.0611 -0.0131 456 ARG A CB  
1210 C CG  . ARG A 160 ? 0.7549 0.9278 0.7902 0.1717  -0.0649 -0.0112 456 ARG A CG  
1211 C CD  . ARG A 160 ? 0.6231 0.8249 0.6603 0.1824  -0.0693 -0.0117 456 ARG A CD  
1212 N NE  . ARG A 160 ? 0.6379 0.7899 0.6502 0.1691  -0.0701 -0.0057 456 ARG A NE  
1213 C CZ  . ARG A 160 ? 0.7931 0.9477 0.7916 0.1791  -0.0737 -0.0040 456 ARG A CZ  
1214 N NH1 . ARG A 160 ? 0.6186 0.8254 0.6261 0.2039  -0.0782 -0.0082 456 ARG A NH1 
1215 N NH2 . ARG A 160 ? 0.8110 0.9196 0.7852 0.1631  -0.0730 0.0023  456 ARG A NH2 
1216 N N   . SER A 161 ? 0.4625 0.6730 0.6034 0.0816  -0.0527 -0.0185 457 SER A N   
1217 C CA  . SER A 161 ? 0.6449 0.8555 0.8081 0.0561  -0.0503 -0.0194 457 SER A CA  
1218 C C   . SER A 161 ? 0.6358 0.8710 0.8183 0.0448  -0.0513 -0.0226 457 SER A C   
1219 O O   . SER A 161 ? 0.7156 0.9823 0.9045 0.0513  -0.0535 -0.0262 457 SER A O   
1220 C CB  . SER A 161 ? 0.7058 0.9322 0.8842 0.0505  -0.0473 -0.0225 457 SER A CB  
1221 O OG  . SER A 161 ? 0.8250 1.0989 1.0186 0.0553  -0.0470 -0.0274 457 SER A OG  
1222 N N   . ALA A 162 ? 0.5459 0.7677 0.7344 0.0295  -0.0500 -0.0216 458 ALA A N   
1223 C CA  . ALA A 162 ? 0.5219 0.7555 0.7181 0.0232  -0.0508 -0.0242 458 ALA A CA  
1224 C C   . ALA A 162 ? 0.5027 0.7271 0.7051 0.0116  -0.0487 -0.0244 458 ALA A C   
1225 O O   . ALA A 162 ? 0.6291 0.8396 0.8296 0.0079  -0.0471 -0.0207 458 ALA A O   
1226 C CB  . ALA A 162 ? 0.4032 0.6279 0.5839 0.0304  -0.0524 -0.0201 458 ALA A CB  
1227 N N   . ILE A 163 ? 0.5516 0.7835 0.7574 0.0078  -0.0491 -0.0290 459 ILE A N   
1228 C CA  . ILE A 163 ? 0.5317 0.7543 0.7362 0.0047  -0.0474 -0.0298 459 ILE A CA  
1229 C C   . ILE A 163 ? 0.4839 0.7110 0.6822 0.0082  -0.0481 -0.0325 459 ILE A C   
1230 O O   . ILE A 163 ? 0.5724 0.8074 0.7685 0.0074  -0.0507 -0.0366 459 ILE A O   
1231 C CB  . ILE A 163 ? 0.4719 0.6842 0.6750 -0.0019 -0.0470 -0.0344 459 ILE A CB  
1232 C CG1 . ILE A 163 ? 0.3973 0.5948 0.5915 0.0026  -0.0457 -0.0347 459 ILE A CG1 
1233 C CG2 . ILE A 163 ? 0.3215 0.5376 0.5188 -0.0100 -0.0493 -0.0413 459 ILE A CG2 
1234 C CD1 . ILE A 163 ? 0.4799 0.6547 0.6621 -0.0031 -0.0457 -0.0385 459 ILE A CD1 
1235 N N   . THR A 164 ? 0.4406 0.6684 0.6357 0.0128  -0.0458 -0.0301 460 THR A N   
1236 C CA  . THR A 164 ? 0.5112 0.7433 0.6973 0.0193  -0.0454 -0.0329 460 THR A CA  
1237 C C   . THR A 164 ? 0.5710 0.7905 0.7455 0.0270  -0.0442 -0.0374 460 THR A C   
1238 O O   . THR A 164 ? 0.7203 0.9452 0.8976 0.0323  -0.0421 -0.0341 460 THR A O   
1239 C CB  . THR A 164 ? 0.5642 0.8132 0.7512 0.0211  -0.0428 -0.0259 460 THR A CB  
1240 O OG1 . THR A 164 ? 0.5186 0.7648 0.7047 0.0161  -0.0445 -0.0214 460 THR A OG1 
1241 C CG2 . THR A 164 ? 0.4596 0.7162 0.6367 0.0292  -0.0418 -0.0290 460 THR A CG2 
1242 N N   . ILE A 165 ? 0.6300 0.8305 0.7860 0.0285  -0.0463 -0.0450 461 ILE A N   
1243 C CA  . ILE A 165 ? 0.5806 0.7506 0.7105 0.0370  -0.0463 -0.0506 461 ILE A CA  
1244 C C   . ILE A 165 ? 0.6737 0.8440 0.7851 0.0554  -0.0447 -0.0533 461 ILE A C   
1245 O O   . ILE A 165 ? 0.6231 0.7855 0.7211 0.0533  -0.0467 -0.0582 461 ILE A O   
1246 C CB  . ILE A 165 ? 0.6521 0.7890 0.7622 0.0212  -0.0501 -0.0576 461 ILE A CB  
1247 C CG1 . ILE A 165 ? 0.6824 0.8211 0.8072 0.0073  -0.0501 -0.0547 461 ILE A CG1 
1248 C CG2 . ILE A 165 ? 0.7135 0.8029 0.7807 0.0307  -0.0509 -0.0638 461 ILE A CG2 
1249 C CD1 . ILE A 165 ? 0.7734 0.9076 0.8928 -0.0155 -0.0533 -0.0594 461 ILE A CD1 
1250 N N   . PHE A 166 ? 0.6635 0.8472 0.7727 0.0745  -0.0412 -0.0504 462 PHE A N   
1251 C CA  . PHE A 166 ? 0.6085 0.8013 0.6996 0.0974  -0.0385 -0.0527 462 PHE A CA  
1252 C C   . PHE A 166 ? 0.7410 0.8808 0.7849 0.1153  -0.0403 -0.0613 462 PHE A C   
1253 O O   . PHE A 166 ? 0.6689 0.7667 0.6954 0.1074  -0.0434 -0.0641 462 PHE A O   
1254 C CB  . PHE A 166 ? 0.5900 0.8363 0.7021 0.1090  -0.0337 -0.0449 462 PHE A CB  
1255 C CG  . PHE A 166 ? 0.6661 0.9526 0.8083 0.0899  -0.0318 -0.0369 462 PHE A CG  
1256 C CD1 . PHE A 166 ? 0.6840 0.9893 0.8243 0.0909  -0.0293 -0.0361 462 PHE A CD1 
1257 C CD2 . PHE A 166 ? 0.6179 0.9153 0.7827 0.0711  -0.0326 -0.0302 462 PHE A CD2 
1258 C CE1 . PHE A 166 ? 0.7391 1.0701 0.8969 0.0724  -0.0278 -0.0280 462 PHE A CE1 
1259 C CE2 . PHE A 166 ? 0.5013 0.8206 0.6805 0.0534  -0.0314 -0.0227 462 PHE A CE2 
1260 C CZ  . PHE A 166 ? 0.6331 0.9673 0.8074 0.0534  -0.0290 -0.0213 462 PHE A CZ  
1261 N N   . PRO A 167 ? 0.8115 0.9455 0.8267 0.1394  -0.0386 -0.0660 463 PRO A N   
1262 C CA  . PRO A 167 ? 0.7876 0.8539 0.7431 0.1570  -0.0413 -0.0753 463 PRO A CA  
1263 C C   . PRO A 167 ? 0.9800 1.0167 0.9136 0.1724  -0.0419 -0.0748 463 PRO A C   
1264 O O   . PRO A 167 ? 1.0327 1.1154 0.9915 0.1875  -0.0389 -0.0682 463 PRO A O   
1265 C CB  . PRO A 167 ? 0.5636 0.6458 0.4980 0.1892  -0.0374 -0.0783 463 PRO A CB  
1266 C CG  . PRO A 167 ? 0.7434 0.8858 0.7221 0.1734  -0.0346 -0.0727 463 PRO A CG  
1267 C CD  . PRO A 167 ? 0.7846 0.9668 0.8136 0.1497  -0.0342 -0.0633 463 PRO A CD  
1268 N N   . GLN A 168 ? 0.9820 0.9404 0.8648 0.1659  -0.0464 -0.0815 464 GLN A N   
1269 C CA  . GLN A 168 ? 0.9074 0.8241 0.7611 0.1766  -0.0477 -0.0808 464 GLN A CA  
1270 C C   . GLN A 168 ? 0.9138 0.8275 0.7323 0.2283  -0.0455 -0.0818 464 GLN A C   
1271 O O   . GLN A 168 ? 1.0217 0.9408 0.8182 0.2557  -0.0435 -0.0859 464 GLN A O   
1272 C CB  . GLN A 168 ? 0.8357 0.6606 0.6308 0.1540  -0.0530 -0.0877 464 GLN A CB  
1273 C CG  . GLN A 168 ? 0.8159 0.5826 0.5495 0.1631  -0.0555 -0.0975 464 GLN A CG  
1274 C CD  . GLN A 168 ? 1.0436 0.7392 0.7337 0.1214  -0.0613 -0.1038 464 GLN A CD  
1275 O OE1 . GLN A 168 ? 1.2833 0.8855 0.8921 0.1264  -0.0648 -0.1102 464 GLN A OE1 
1276 N NE2 . GLN A 168 ? 1.0359 0.7752 0.7753 0.0795  -0.0627 -0.1020 464 GLN A NE2 
1277 N N   . ARG A 169 ? 0.8497 0.7557 0.6593 0.2446  -0.0460 -0.0782 465 ARG A N   
1278 C CA  . ARG A 169 ? 0.9103 0.8068 0.6756 0.2992  -0.0450 -0.0799 465 ARG A CA  
1279 C C   . ARG A 169 ? 1.1396 0.9305 0.8134 0.3178  -0.0482 -0.0901 465 ARG A C   
1280 O O   . ARG A 169 ? 1.3337 1.0436 0.9691 0.2851  -0.0525 -0.0944 465 ARG A O   
1281 C CB  . ARG A 169 ? 1.1154 1.0155 0.8810 0.3134  -0.0463 -0.0745 465 ARG A CB  
1282 C CG  . ARG A 169 ? 1.2201 1.1254 0.9429 0.3765  -0.0457 -0.0757 465 ARG A CG  
1283 C CD  . ARG A 169 ? 1.3184 1.2162 1.0292 0.3947  -0.0484 -0.0711 465 ARG A CD  
1284 N NE  . ARG A 169 ? 1.2165 1.2236 1.0061 0.3843  -0.0466 -0.0621 465 ARG A NE  
1285 C CZ  . ARG A 169 ? 1.2228 1.2409 1.0540 0.3440  -0.0480 -0.0566 465 ARG A CZ  
1286 N NH1 . ARG A 169 ? 1.2082 1.1443 1.0145 0.3114  -0.0505 -0.0588 465 ARG A NH1 
1287 N NH2 . ARG A 169 ? 1.2248 1.3366 1.1187 0.3351  -0.0469 -0.0491 465 ARG A NH2 
1288 N N   . THR A 170 ? 1.0895 0.8833 0.7256 0.3687  -0.0459 -0.0943 466 THR A N   
1289 C CA  . THR A 170 ? 1.2447 0.9310 0.7829 0.3928  -0.0490 -0.1047 466 THR A CA  
1290 C C   . THR A 170 ? 1.4356 1.0851 0.9099 0.4543  -0.0497 -0.1055 466 THR A C   
1291 O O   . THR A 170 ? 1.6570 1.2292 1.0840 0.4513  -0.0541 -0.1051 466 THR A O   
1292 C CB  . THR A 170 ? 1.2706 0.9797 0.8066 0.4040  -0.0461 -0.1103 466 THR A CB  
1293 O OG1 . THR A 170 ? 1.1704 0.9950 0.7613 0.4372  -0.0392 -0.1047 466 THR A OG1 
1294 C CG2 . THR A 170 ? 1.2141 0.9304 0.7901 0.3436  -0.0478 -0.1112 466 THR A CG2 
1295 N N   . ASP A 171 ? 1.4370 1.1418 0.9057 0.5120  -0.0454 -0.1063 467 ASP A N   
1296 C CA  . ASP A 171 ? 1.5745 1.2597 0.9854 0.5717  -0.0471 -0.1048 467 ASP A CA  
1297 C C   . ASP A 171 ? 1.5989 1.3591 1.0670 0.5723  -0.0469 -0.0952 467 ASP A C   
1298 O O   . ASP A 171 ? 1.7168 1.4179 1.1374 0.5818  -0.0519 -0.0922 467 ASP A O   
1299 C CB  . ASP A 171 ? 1.6322 1.3841 1.0352 0.6125  -0.0444 -0.1017 467 ASP A CB  
1300 C CG  . ASP A 171 ? 1.5547 1.4540 1.0591 0.6029  -0.0364 -0.0972 467 ASP A CG  
1301 O OD1 . ASP A 171 ? 1.4927 1.4168 1.0588 0.5624  -0.0333 -0.0995 467 ASP A OD1 
1302 O OD2 . ASP A 171 ? 1.5344 1.5248 1.0537 0.6307  -0.0338 -0.0905 467 ASP A OD2 
1303 N N   . GLY A 172 ? 1.5061 1.3959 1.0732 0.5568  -0.0418 -0.0890 468 GLY A N   
1304 C CA  . GLY A 172 ? 1.4590 1.4345 1.0821 0.5562  -0.0420 -0.0794 468 GLY A CA  
1305 C C   . GLY A 172 ? 1.3978 1.5196 1.0918 0.5559  -0.0363 -0.0719 468 GLY A C   
1306 O O   . GLY A 172 ? 1.3013 1.5082 1.0676 0.5291  -0.0354 -0.0643 468 GLY A O   
1307 N N   . LYS A 173 ? 1.4668 1.6153 1.1353 0.5817  -0.0329 -0.0736 469 LYS A N   
1308 C CA  . LYS A 173 ? 1.4790 1.7608 1.2084 0.5744  -0.0266 -0.0668 469 LYS A CA  
1309 C C   . LYS A 173 ? 1.3913 1.7118 1.1841 0.5338  -0.0220 -0.0666 469 LYS A C   
1310 O O   . LYS A 173 ? 1.3781 1.7979 1.2402 0.5022  -0.0183 -0.0584 469 LYS A O   
1311 C CB  . LYS A 173 ? 1.5604 1.8610 1.2382 0.6179  -0.0248 -0.0681 469 LYS A CB  
1312 C CG  . LYS A 173 ? 1.6661 1.9410 1.2762 0.6641  -0.0295 -0.0677 469 LYS A CG  
1313 C CD  . LYS A 173 ? 1.7619 1.8913 1.2740 0.6925  -0.0359 -0.0751 469 LYS A CD  
1314 C CE  . LYS A 173 ? 1.8612 1.9641 1.2955 0.7433  -0.0410 -0.0738 469 LYS A CE  
1315 N NZ  . LYS A 173 ? 2.0071 1.9526 1.3402 0.7608  -0.0486 -0.0789 469 LYS A NZ  
1316 N N   . HIS A 174 ? 1.2663 1.5045 1.0292 0.5324  -0.0224 -0.0757 470 HIS A N   
1317 C CA  . HIS A 174 ? 1.2136 1.4758 1.0244 0.4886  -0.0191 -0.0752 470 HIS A CA  
1318 C C   . HIS A 174 ? 1.2819 1.5094 1.1282 0.4291  -0.0239 -0.0712 470 HIS A C   
1319 O O   . HIS A 174 ? 1.3604 1.4867 1.1679 0.4121  -0.0291 -0.0766 470 HIS A O   
1320 C CB  . HIS A 174 ? 1.2222 1.4103 0.9760 0.5019  -0.0186 -0.0853 470 HIS A CB  
1321 C CG  . HIS A 174 ? 1.2826 1.4933 0.9906 0.5573  -0.0153 -0.0876 470 HIS A CG  
1322 N ND1 . HIS A 174 ? 1.4058 1.5154 1.0210 0.5938  -0.0204 -0.0945 470 HIS A ND1 
1323 C CD2 . HIS A 174 ? 1.2888 1.6065 1.0251 0.5659  -0.0103 -0.0795 470 HIS A CD2 
1324 C CE1 . HIS A 174 ? 1.4731 1.6305 1.0643 0.6284  -0.0190 -0.0907 470 HIS A CE1 
1325 N NE2 . HIS A 174 ? 1.3962 1.6818 1.0606 0.6122  -0.0124 -0.0823 470 HIS A NE2 
1326 N N   . ASP A 175 ? 1.2325 1.5467 1.1490 0.3976  -0.0219 -0.0615 471 ASP A N   
1327 C CA  . ASP A 175 ? 1.1172 1.4150 1.0694 0.3500  -0.0259 -0.0566 471 ASP A CA  
1328 C C   . ASP A 175 ? 1.0085 1.3784 1.0241 0.3078  -0.0226 -0.0489 471 ASP A C   
1329 O O   . ASP A 175 ? 1.0792 1.5412 1.1248 0.3137  -0.0179 -0.0430 471 ASP A O   
1330 C CB  . ASP A 175 ? 1.0977 1.4145 1.0542 0.3640  -0.0289 -0.0523 471 ASP A CB  
1331 C CG  . ASP A 175 ? 1.1913 1.4063 1.0835 0.3869  -0.0340 -0.0585 471 ASP A CG  
1332 O OD1 . ASP A 175 ? 1.3650 1.5290 1.1947 0.4282  -0.0340 -0.0658 471 ASP A OD1 
1333 O OD2 . ASP A 175 ? 1.2186 1.3994 1.1169 0.3630  -0.0380 -0.0560 471 ASP A OD2 
1334 N N   . PHE A 176 ? 0.9072 1.2355 0.9380 0.2656  -0.0250 -0.0487 472 PHE A N   
1335 C CA  . PHE A 176 ? 0.8422 1.2207 0.9233 0.2256  -0.0230 -0.0410 472 PHE A CA  
1336 C C   . PHE A 176 ? 0.7389 1.1356 0.8493 0.2038  -0.0258 -0.0344 472 PHE A C   
1337 O O   . PHE A 176 ? 0.7860 1.1266 0.8838 0.1983  -0.0301 -0.0369 472 PHE A O   
1338 C CB  . PHE A 176 ? 0.8045 1.1334 0.8841 0.1974  -0.0248 -0.0442 472 PHE A CB  
1339 C CG  . PHE A 176 ? 0.7315 1.0559 0.7889 0.2124  -0.0220 -0.0494 472 PHE A CG  
1340 C CD1 . PHE A 176 ? 0.6598 0.9299 0.6651 0.2440  -0.0232 -0.0589 472 PHE A CD1 
1341 C CD2 . PHE A 176 ? 0.5936 0.9619 0.6756 0.1952  -0.0182 -0.0446 472 PHE A CD2 
1342 C CE1 . PHE A 176 ? 0.8358 1.0992 0.8172 0.2581  -0.0209 -0.0642 472 PHE A CE1 
1343 C CE2 . PHE A 176 ? 0.7342 1.1001 0.7953 0.2095  -0.0155 -0.0492 472 PHE A CE2 
1344 C CZ  . PHE A 176 ? 0.7340 1.0491 0.7462 0.2412  -0.0169 -0.0593 472 PHE A CZ  
1345 N N   . ARG A 177 ? 0.6148 1.0892 0.7598 0.1900  -0.0232 -0.0261 473 ARG A N   
1346 C CA  . ARG A 177 ? 0.6336 1.1291 0.8029 0.1680  -0.0262 -0.0198 473 ARG A CA  
1347 C C   . ARG A 177 ? 0.6665 1.2075 0.8666 0.1286  -0.0243 -0.0114 473 ARG A C   
1348 O O   . ARG A 177 ? 0.7359 1.3396 0.9448 0.1273  -0.0196 -0.0074 473 ARG A O   
1349 C CB  . ARG A 177 ? 0.6845 1.2315 0.8512 0.1980  -0.0270 -0.0185 473 ARG A CB  
1350 C CG  . ARG A 177 ? 0.7176 1.2040 0.8446 0.2356  -0.0303 -0.0256 473 ARG A CG  
1351 C CD  . ARG A 177 ? 0.7769 1.1979 0.9021 0.2126  -0.0351 -0.0259 473 ARG A CD  
1352 N NE  . ARG A 177 ? 0.8695 1.3376 1.0260 0.1913  -0.0374 -0.0188 473 ARG A NE  
1353 C CZ  . ARG A 177 ? 0.8167 1.2991 0.9672 0.2092  -0.0410 -0.0175 473 ARG A CZ  
1354 N NH1 . ARG A 177 ? 0.8792 1.3275 0.9900 0.2517  -0.0426 -0.0224 473 ARG A NH1 
1355 N NH2 . ARG A 177 ? 0.7480 1.2733 0.9262 0.1846  -0.0436 -0.0113 473 ARG A NH2 
1356 N N   . VAL A 178 ? 0.5879 1.0943 0.7983 0.0968  -0.0276 -0.0086 474 VAL A N   
1357 C CA  . VAL A 178 ? 0.4555 0.9932 0.6836 0.0595  -0.0275 -0.0001 474 VAL A CA  
1358 C C   . VAL A 178 ? 0.6822 1.2675 0.9214 0.0561  -0.0300 0.0040  474 VAL A C   
1359 O O   . VAL A 178 ? 0.6474 1.2001 0.8846 0.0579  -0.0344 0.0022  474 VAL A O   
1360 C CB  . VAL A 178 ? 0.5363 1.0119 0.7625 0.0333  -0.0303 0.0004  474 VAL A CB  
1361 C CG1 . VAL A 178 ? 0.5846 1.0780 0.8143 -0.0034 -0.0301 0.0092  474 VAL A CG1 
1362 C CG2 . VAL A 178 ? 0.6764 1.1057 0.8914 0.0417  -0.0295 -0.0053 474 VAL A CG2 
1363 N N   . TRP A 179 ? 0.6717 1.3394 0.9220 0.0501  -0.0274 0.0097  475 TRP A N   
1364 C CA  . TRP A 179 ? 0.6253 1.3505 0.8866 0.0478  -0.0307 0.0133  475 TRP A CA  
1365 C C   . TRP A 179 ? 0.5843 1.2876 0.8488 0.0052  -0.0355 0.0183  475 TRP A C   
1366 O O   . TRP A 179 ? 0.5431 1.2655 0.8123 0.0049  -0.0403 0.0191  475 TRP A O   
1367 C CB  . TRP A 179 ? 0.5650 1.3620 0.8205 0.0482  -0.0249 0.0174  475 TRP A CB  
1368 C CG  . TRP A 179 ? 0.5477 1.3614 0.7888 0.0989  -0.0213 0.0116  475 TRP A CG  
1369 C CD1 . TRP A 179 ? 0.7171 1.4870 0.9481 0.1354  -0.0211 0.0039  475 TRP A CD1 
1370 C CD2 . TRP A 179 ? 0.5746 1.4498 0.8026 0.1200  -0.0181 0.0126  475 TRP A CD2 
1371 N NE1 . TRP A 179 ? 0.8492 1.6412 1.0568 0.1788  -0.0179 0.0000  475 TRP A NE1 
1372 C CE2 . TRP A 179 ? 0.8073 1.6674 1.0141 0.1715  -0.0159 0.0054  475 TRP A CE2 
1373 C CE3 . TRP A 179 ? 0.5590 1.5016 0.7871 0.1002  -0.0171 0.0188  475 TRP A CE3 
1374 C CZ2 . TRP A 179 ? 0.8756 1.7846 1.0603 0.2065  -0.0128 0.0042  475 TRP A CZ2 
1375 C CZ3 . TRP A 179 ? 0.7102 1.7104 0.9215 0.1339  -0.0140 0.0177  475 TRP A CZ3 
1376 C CH2 . TRP A 179 ? 0.8343 1.8173 1.0238 0.1879  -0.0118 0.0105  475 TRP A CH2 
1377 N N   . ASN A 180 ? 0.5250 1.1842 0.7817 -0.0279 -0.0348 0.0214  476 ASN A N   
1378 C CA  . ASN A 180 ? 0.5410 1.1608 0.7894 -0.0628 -0.0396 0.0249  476 ASN A CA  
1379 C C   . ASN A 180 ? 0.6011 1.1597 0.8467 -0.0453 -0.0436 0.0190  476 ASN A C   
1380 O O   . ASN A 180 ? 0.4472 0.9669 0.6908 -0.0172 -0.0421 0.0127  476 ASN A O   
1381 C CB  . ASN A 180 ? 0.5844 1.1548 0.8146 -0.0914 -0.0380 0.0285  476 ASN A CB  
1382 C CG  . ASN A 180 ? 0.6122 1.2366 0.8397 -0.1134 -0.0335 0.0353  476 ASN A CG  
1383 O OD1 . ASN A 180 ? 0.7315 1.3960 0.9690 -0.0912 -0.0283 0.0336  476 ASN A OD1 
1384 N ND2 . ASN A 180 ? 0.5784 1.2019 0.7871 -0.1587 -0.0352 0.0430  476 ASN A ND2 
1385 N N   . SER A 181 ? 0.4972 1.0472 0.7393 -0.0651 -0.0487 0.0213  477 SER A N   
1386 C CA  . SER A 181 ? 0.4184 0.9103 0.6557 -0.0528 -0.0518 0.0166  477 SER A CA  
1387 C C   . SER A 181 ? 0.5605 0.9784 0.7838 -0.0620 -0.0509 0.0150  477 SER A C   
1388 O O   . SER A 181 ? 0.4877 0.8635 0.7105 -0.0425 -0.0501 0.0095  477 SER A O   
1389 C CB  . SER A 181 ? 0.6175 1.1252 0.8534 -0.0690 -0.0576 0.0191  477 SER A CB  
1390 O OG  . SER A 181 ? 0.7044 1.2273 0.9296 -0.1105 -0.0598 0.0255  477 SER A OG  
1391 N N   . GLN A 182 ? 0.6493 1.0513 0.8569 -0.0917 -0.0512 0.0200  478 GLN A N   
1392 C CA  . GLN A 182 ? 0.5535 0.8947 0.7441 -0.0939 -0.0499 0.0191  478 GLN A CA  
1393 C C   . GLN A 182 ? 0.4118 0.7662 0.5936 -0.1071 -0.0468 0.0236  478 GLN A C   
1394 O O   . GLN A 182 ? 0.4957 0.8976 0.6769 -0.1281 -0.0462 0.0292  478 GLN A O   
1395 C CB  . GLN A 182 ? 0.5591 0.8461 0.7229 -0.1129 -0.0536 0.0208  478 GLN A CB  
1396 C CG  . GLN A 182 ? 0.4490 0.7280 0.6157 -0.1098 -0.0571 0.0184  478 GLN A CG  
1397 C CD  . GLN A 182 ? 0.5842 0.8114 0.7161 -0.1319 -0.0610 0.0207  478 GLN A CD  
1398 O OE1 . GLN A 182 ? 0.5458 0.7339 0.6467 -0.1464 -0.0611 0.0240  478 GLN A OE1 
1399 N NE2 . GLN A 182 ? 0.4754 0.6960 0.6057 -0.1332 -0.0644 0.0191  478 GLN A NE2 
1400 N N   . LEU A 183 ? 0.3681 0.6831 0.5407 -0.0971 -0.0449 0.0217  479 LEU A N   
1401 C CA  . LEU A 183 ? 0.4613 0.7860 0.6229 -0.1075 -0.0418 0.0262  479 LEU A CA  
1402 C C   . LEU A 183 ? 0.5290 0.8388 0.6579 -0.1455 -0.0434 0.0347  479 LEU A C   
1403 O O   . LEU A 183 ? 0.5640 0.9077 0.6863 -0.1656 -0.0406 0.0407  479 LEU A O   
1404 C CB  . LEU A 183 ? 0.4601 0.7426 0.6135 -0.0899 -0.0409 0.0228  479 LEU A CB  
1405 C CG  . LEU A 183 ? 0.5407 0.8268 0.7163 -0.0595 -0.0399 0.0143  479 LEU A CG  
1406 C CD1 . LEU A 183 ? 0.3437 0.5961 0.5062 -0.0508 -0.0401 0.0128  479 LEU A CD1 
1407 C CD2 . LEU A 183 ? 0.7049 1.0438 0.8990 -0.0485 -0.0366 0.0127  479 LEU A CD2 
1408 N N   . ILE A 184 ? 0.5866 0.8423 0.6889 -0.1572 -0.0477 0.0354  480 ILE A N   
1409 C CA  . ILE A 184 ? 0.4986 0.7194 0.5555 -0.1952 -0.0504 0.0429  480 ILE A CA  
1410 C C   . ILE A 184 ? 0.6022 0.8275 0.6550 -0.2140 -0.0552 0.0431  480 ILE A C   
1411 O O   . ILE A 184 ? 0.6882 0.8769 0.7397 -0.1977 -0.0579 0.0382  480 ILE A O   
1412 C CB  . ILE A 184 ? 0.5672 0.7005 0.5770 -0.1904 -0.0520 0.0438  480 ILE A CB  
1413 C CG1 . ILE A 184 ? 0.6817 0.8170 0.6880 -0.1819 -0.0480 0.0460  480 ILE A CG1 
1414 C CG2 . ILE A 184 ? 0.5916 0.6668 0.5404 -0.2286 -0.0562 0.0505  480 ILE A CG2 
1415 C CD1 . ILE A 184 ? 0.8201 0.8871 0.7962 -0.1579 -0.0495 0.0441  480 ILE A CD1 
1416 N N   . ARG A 185 ? 0.6890 0.9668 0.7413 -0.2485 -0.0560 0.0488  481 ARG A N   
1417 C CA  . ARG A 185 ? 0.6813 0.9712 0.7252 -0.2747 -0.0617 0.0500  481 ARG A CA  
1418 C C   . ARG A 185 ? 0.7292 1.0378 0.7395 -0.3296 -0.0632 0.0590  481 ARG A C   
1419 O O   . ARG A 185 ? 0.8349 1.1897 0.8514 -0.3422 -0.0585 0.0640  481 ARG A O   
1420 C CB  . ARG A 185 ? 0.6900 1.0600 0.7857 -0.2531 -0.0620 0.0458  481 ARG A CB  
1421 C CG  . ARG A 185 ? 0.6549 1.0005 0.7751 -0.2073 -0.0611 0.0375  481 ARG A CG  
1422 C CD  . ARG A 185 ? 0.5925 0.9864 0.7406 -0.1949 -0.0642 0.0344  481 ARG A CD  
1423 N NE  . ARG A 185 ? 0.6745 1.0358 0.7974 -0.2184 -0.0706 0.0352  481 ARG A NE  
1424 C CZ  . ARG A 185 ? 0.6516 1.0319 0.7887 -0.2082 -0.0746 0.0322  481 ARG A CZ  
1425 N NH1 . ARG A 185 ? 0.5285 0.9559 0.7010 -0.1738 -0.0727 0.0287  481 ARG A NH1 
1426 N NH2 . ARG A 185 ? 0.6029 0.9493 0.7121 -0.2318 -0.0806 0.0327  481 ARG A NH2 
1427 N N   . TYR A 186 ? 0.6107 0.8842 0.5827 -0.3645 -0.0700 0.0610  482 TYR A N   
1428 C CA  . TYR A 186 ? 0.7121 1.0000 0.6449 -0.4260 -0.0729 0.0695  482 TYR A CA  
1429 C C   . TYR A 186 ? 0.8172 1.2187 0.7884 -0.4262 -0.0705 0.0703  482 TYR A C   
1430 O O   . TYR A 186 ? 0.9223 1.3718 0.9352 -0.3984 -0.0720 0.0650  482 TYR A O   
1431 C CB  . TYR A 186 ? 0.8987 1.0917 0.7644 -0.4578 -0.0811 0.0699  482 TYR A CB  
1432 C CG  . TYR A 186 ? 1.0256 1.0935 0.8364 -0.4380 -0.0805 0.0687  482 TYR A CG  
1433 C CD1 . TYR A 186 ? 0.9800 0.9814 0.7827 -0.4002 -0.0827 0.0614  482 TYR A CD1 
1434 C CD2 . TYR A 186 ? 0.8953 0.9199 0.6650 -0.4519 -0.0770 0.0750  482 TYR A CD2 
1435 C CE1 . TYR A 186 ? 1.0721 0.9719 0.8265 -0.3755 -0.0820 0.0600  482 TYR A CE1 
1436 C CE2 . TYR A 186 ? 1.0192 0.9337 0.7367 -0.4271 -0.0769 0.0739  482 TYR A CE2 
1437 C CZ  . TYR A 186 ? 1.1099 0.9665 0.8216 -0.3868 -0.0795 0.0662  482 TYR A CZ  
1438 O OH  . TYR A 186 ? 1.1496 0.9086 0.8108 -0.3565 -0.0794 0.0649  482 TYR A OH  
1439 N N   . ALA A 187 ? 0.9079 1.3452 0.8565 -0.4547 -0.0665 0.0771  483 ALA A N   
1440 C CA  . ALA A 187 ? 0.9512 1.4966 0.9281 -0.4515 -0.0630 0.0785  483 ALA A CA  
1441 C C   . ALA A 187 ? 1.1302 1.6899 1.0967 -0.4649 -0.0690 0.0776  483 ALA A C   
1442 O O   . ALA A 187 ? 1.1432 1.6244 1.0676 -0.4878 -0.0756 0.0773  483 ALA A O   
1443 C CB  . ALA A 187 ? 0.9913 1.5662 0.9366 -0.4861 -0.0588 0.0864  483 ALA A CB  
1444 N N   . GLY A 188 ? 1.1340 1.7936 1.1357 -0.4482 -0.0664 0.0771  484 GLY A N   
1445 C CA  . GLY A 188 ? 1.1950 1.8837 1.1913 -0.4590 -0.0713 0.0767  484 GLY A CA  
1446 C C   . GLY A 188 ? 1.2223 2.0121 1.2177 -0.4752 -0.0683 0.0818  484 GLY A C   
1447 O O   . GLY A 188 ? 1.2405 2.1158 1.2766 -0.4401 -0.0629 0.0802  484 GLY A O   
1448 N N   . TYR A 189 ? 1.2380 2.0172 1.1812 -0.5283 -0.0719 0.0878  485 TYR A N   
1449 C CA  . TYR A 189 ? 1.1606 2.0383 1.0956 -0.5522 -0.0700 0.0934  485 TYR A CA  
1450 C C   . TYR A 189 ? 1.1915 2.0839 1.1103 -0.5729 -0.0760 0.0939  485 TYR A C   
1451 O O   . TYR A 189 ? 1.1142 1.9203 0.9872 -0.6053 -0.0825 0.0946  485 TYR A O   
1452 C CB  . TYR A 189 ? 1.1908 2.0542 1.0716 -0.6044 -0.0694 0.1011  485 TYR A CB  
1453 C CG  . TYR A 189 ? 1.0650 1.8708 0.9421 -0.5966 -0.0657 0.1011  485 TYR A CG  
1454 C CD1 . TYR A 189 ? 1.0836 1.7647 0.9146 -0.6166 -0.0699 0.1012  485 TYR A CD1 
1455 C CD2 . TYR A 189 ? 1.0990 1.9735 1.0137 -0.5684 -0.0582 0.1010  485 TYR A CD2 
1456 C CE1 . TYR A 189 ? 1.1580 1.7878 0.9831 -0.6096 -0.0665 0.1017  485 TYR A CE1 
1457 C CE2 . TYR A 189 ? 1.0649 1.8895 0.9761 -0.5626 -0.0546 0.1015  485 TYR A CE2 
1458 C CZ  . TYR A 189 ? 1.1370 1.8413 1.0046 -0.5840 -0.0587 0.1020  485 TYR A CZ  
1459 O OH  . TYR A 189 ? 1.2317 1.8882 1.0941 -0.5778 -0.0549 0.1030  485 TYR A OH  
1460 N N   . LYS A 190 ? 1.2308 2.2295 1.1832 -0.5522 -0.0738 0.0934  486 LYS A N   
1461 C CA  . LYS A 190 ? 1.3382 2.3715 1.2707 -0.5804 -0.0786 0.0957  486 LYS A CA  
1462 C C   . LYS A 190 ? 1.4376 2.5086 1.3184 -0.6417 -0.0787 0.1047  486 LYS A C   
1463 O O   . LYS A 190 ? 1.4168 2.5357 1.2959 -0.6482 -0.0736 0.1083  486 LYS A O   
1464 C CB  . LYS A 190 ? 1.3138 2.4476 1.2966 -0.5344 -0.0765 0.0919  486 LYS A CB  
1465 C CG  . LYS A 190 ? 1.3355 2.5979 1.3194 -0.5442 -0.0718 0.0971  486 LYS A CG  
1466 C CD  . LYS A 190 ? 1.2594 2.6117 1.2922 -0.4842 -0.0685 0.0921  486 LYS A CD  
1467 C CE  . LYS A 190 ? 1.1709 2.5129 1.2417 -0.4247 -0.0631 0.0864  486 LYS A CE  
1468 N NZ  . LYS A 190 ? 1.1079 2.5368 1.2128 -0.3656 -0.0594 0.0820  486 LYS A NZ  
1469 N N   . GLN A 191 ? 1.5545 2.5999 1.3888 -0.6885 -0.0849 0.1081  487 GLN A N   
1470 C CA  . GLN A 191 ? 1.6500 2.7108 1.4215 -0.7549 -0.0867 0.1167  487 GLN A CA  
1471 C C   . GLN A 191 ? 1.6666 2.8657 1.4489 -0.7678 -0.0848 0.1208  487 GLN A C   
1472 O O   . GLN A 191 ? 1.6549 2.9189 1.4835 -0.7296 -0.0837 0.1168  487 GLN A O   
1473 C CB  . GLN A 191 ? 1.7342 2.6757 1.4337 -0.8037 -0.0950 0.1187  487 GLN A CB  
1474 C CG  . GLN A 191 ? 1.7381 2.5393 1.4087 -0.7988 -0.0971 0.1158  487 GLN A CG  
1475 C CD  . GLN A 191 ? 1.7904 2.5687 1.4222 -0.8267 -0.0949 0.1205  487 GLN A CD  
1476 O OE1 . GLN A 191 ? 1.7353 2.5946 1.4071 -0.8072 -0.0885 0.1213  487 GLN A OE1 
1477 N NE2 . GLN A 191 ? 1.8762 2.5387 1.4245 -0.8711 -0.1008 0.1233  487 GLN A NE2 
1478 N N   . PRO A 192 ? 1.7012 2.9512 1.4388 -0.8212 -0.0845 0.1286  488 PRO A N   
1479 C CA  . PRO A 192 ? 1.7148 3.0992 1.4547 -0.8406 -0.0833 0.1331  488 PRO A CA  
1480 C C   . PRO A 192 ? 1.7989 3.1739 1.5219 -0.8615 -0.0889 0.1334  488 PRO A C   
1481 O O   . PRO A 192 ? 1.8123 3.3010 1.5617 -0.8517 -0.0871 0.1340  488 PRO A O   
1482 C CB  . PRO A 192 ? 1.7470 3.1575 1.4264 -0.9060 -0.0842 0.1415  488 PRO A CB  
1483 C CG  . PRO A 192 ? 1.7989 3.0609 1.4284 -0.9302 -0.0882 0.1416  488 PRO A CG  
1484 C CD  . PRO A 192 ? 1.7466 2.9453 1.4323 -0.8626 -0.0851 0.1333  488 PRO A CD  
1485 N N   . ASP A 193 ? 1.8197 3.0619 1.4976 -0.8877 -0.0958 0.1327  489 ASP A N   
1486 C CA  . ASP A 193 ? 1.8169 3.0355 1.4744 -0.9077 -0.1019 0.1326  489 ASP A CA  
1487 C C   . ASP A 193 ? 1.6603 2.8549 1.3773 -0.8450 -0.1030 0.1234  489 ASP A C   
1488 O O   . ASP A 193 ? 1.6199 2.7407 1.3146 -0.8559 -0.1096 0.1213  489 ASP A O   
1489 C CB  . ASP A 193 ? 1.9508 3.0346 1.5183 -0.9683 -0.1095 0.1365  489 ASP A CB  
1490 C CG  . ASP A 193 ? 1.9678 2.9249 1.5126 -0.9579 -0.1100 0.1338  489 ASP A CG  
1491 O OD1 . ASP A 193 ? 1.9512 2.9392 1.5107 -0.9486 -0.1050 0.1349  489 ASP A OD1 
1492 O OD2 . ASP A 193 ? 1.9890 2.8166 1.4991 -0.9581 -0.1155 0.1306  489 ASP A OD2 
1493 N N   . GLY A 194 ? 1.5519 2.8035 1.3390 -0.7801 -0.0971 0.1178  490 GLY A N   
1494 C CA  . GLY A 194 ? 1.4647 2.7000 1.3049 -0.7210 -0.0987 0.1091  490 GLY A CA  
1495 C C   . GLY A 194 ? 1.4310 2.5323 1.2724 -0.6975 -0.1019 0.1029  490 GLY A C   
1496 O O   . GLY A 194 ? 1.3331 2.4303 1.2272 -0.6387 -0.1005 0.0956  490 GLY A O   
1497 N N   . SER A 195 ? 1.5248 2.5147 1.3035 -0.7425 -0.1062 0.1058  491 SER A N   
1498 C CA  . SER A 195 ? 1.5654 2.4253 1.3359 -0.7232 -0.1095 0.1001  491 SER A CA  
1499 C C   . SER A 195 ? 1.5986 2.4484 1.4031 -0.6861 -0.1033 0.0975  491 SER A C   
1500 O O   . SER A 195 ? 1.5700 2.5167 1.4148 -0.6638 -0.0965 0.0985  491 SER A O   
1501 C CB  . SER A 195 ? 1.6431 2.3847 1.3258 -0.7792 -0.1155 0.1041  491 SER A CB  
1502 O OG  . SER A 195 ? 1.7012 2.4525 1.3362 -0.8248 -0.1131 0.1120  491 SER A OG  
1503 N N   . THR A 196 ? 1.5853 2.3185 1.3710 -0.6783 -0.1054 0.0940  492 THR A N   
1504 C CA  . THR A 196 ? 1.5025 2.2217 1.3251 -0.6390 -0.1000 0.0906  492 THR A CA  
1505 C C   . THR A 196 ? 1.5304 2.1257 1.2973 -0.6612 -0.1018 0.0916  492 THR A C   
1506 O O   . THR A 196 ? 1.5785 2.0724 1.2992 -0.6755 -0.1082 0.0897  492 THR A O   
1507 C CB  . THR A 196 ? 1.3821 2.1061 1.2675 -0.5785 -0.1003 0.0817  492 THR A CB  
1508 O OG1 . THR A 196 ? 1.3152 2.1428 1.2408 -0.5574 -0.0998 0.0807  492 THR A OG1 
1509 C CG2 . THR A 196 ? 1.2935 2.0200 1.2198 -0.5378 -0.0940 0.0787  492 THR A CG2 
1510 N N   . LEU A 197 ? 1.4927 2.0945 1.2605 -0.6613 -0.0963 0.0943  493 LEU A N   
1511 C CA  . LEU A 197 ? 1.4879 1.9773 1.2056 -0.6756 -0.0973 0.0952  493 LEU A CA  
1512 C C   . LEU A 197 ? 1.2779 1.7519 1.0478 -0.6251 -0.0927 0.0897  493 LEU A C   
1513 O O   . LEU A 197 ? 1.1618 1.7257 0.9949 -0.5914 -0.0865 0.0883  493 LEU A O   
1514 C CB  . LEU A 197 ? 1.5777 2.0772 1.2449 -0.7217 -0.0955 0.1032  493 LEU A CB  
1515 C CG  . LEU A 197 ? 1.6275 2.0129 1.2330 -0.7395 -0.0966 0.1049  493 LEU A CG  
1516 C CD1 . LEU A 197 ? 1.6780 1.9238 1.2219 -0.7446 -0.1038 0.1017  493 LEU A CD1 
1517 C CD2 . LEU A 197 ? 1.7404 2.1388 1.2849 -0.7942 -0.0973 0.1127  493 LEU A CD2 
1518 N N   . GLY A 198 ? 1.2426 1.6010 0.9810 -0.6190 -0.0958 0.0864  494 GLY A N   
1519 C CA  . GLY A 198 ? 1.2120 1.5487 0.9924 -0.5763 -0.0920 0.0817  494 GLY A CA  
1520 C C   . GLY A 198 ? 1.1671 1.5093 0.9978 -0.5344 -0.0945 0.0735  494 GLY A C   
1521 O O   . GLY A 198 ? 1.3415 1.6268 1.1442 -0.5407 -0.1010 0.0704  494 GLY A O   
1522 N N   . ASP A 199 ? 1.0213 1.4297 0.9217 -0.4914 -0.0896 0.0698  495 ASP A N   
1523 C CA  . ASP A 199 ? 0.9387 1.3591 0.8863 -0.4507 -0.0923 0.0621  495 ASP A CA  
1524 C C   . ASP A 199 ? 0.9433 1.4744 0.9380 -0.4306 -0.0903 0.0615  495 ASP A C   
1525 O O   . ASP A 199 ? 0.8440 1.4494 0.8715 -0.4122 -0.0836 0.0631  495 ASP A O   
1526 C CB  . ASP A 199 ? 0.8251 1.2256 0.8078 -0.4137 -0.0894 0.0577  495 ASP A CB  
1527 C CG  . ASP A 199 ? 0.9725 1.3474 0.9805 -0.3824 -0.0944 0.0500  495 ASP A CG  
1528 O OD1 . ASP A 199 ? 0.9780 1.3814 0.9968 -0.3770 -0.0986 0.0476  495 ASP A OD1 
1529 O OD2 . ASP A 199 ? 0.9293 1.2478 0.9401 -0.3543 -0.0917 0.0464  495 ASP A OD2 
1530 N N   . PRO A 200 ? 1.0046 1.5476 0.9989 -0.4320 -0.0960 0.0594  496 PRO A N   
1531 C CA  . PRO A 200 ? 0.9329 1.5786 0.9675 -0.4087 -0.0945 0.0588  496 PRO A CA  
1532 C C   . PRO A 200 ? 0.8012 1.4845 0.8913 -0.3514 -0.0913 0.0533  496 PRO A C   
1533 O O   . PRO A 200 ? 0.6876 1.4553 0.8054 -0.3264 -0.0873 0.0536  496 PRO A O   
1534 C CB  . PRO A 200 ? 0.9787 1.6079 0.9950 -0.4231 -0.1026 0.0572  496 PRO A CB  
1535 C CG  . PRO A 200 ? 1.0511 1.5814 1.0038 -0.4676 -0.1069 0.0594  496 PRO A CG  
1536 C CD  . PRO A 200 ? 1.0100 1.4727 0.9570 -0.4585 -0.1040 0.0581  496 PRO A CD  
1537 N N   . ALA A 201 ? 0.8233 1.4442 0.9246 -0.3294 -0.0932 0.0482  497 ALA A N   
1538 C CA  . ALA A 201 ? 0.7548 1.4030 0.9009 -0.2770 -0.0905 0.0432  497 ALA A CA  
1539 C C   . ALA A 201 ? 0.8836 1.5841 1.0487 -0.2586 -0.0816 0.0451  497 ALA A C   
1540 O O   . ALA A 201 ? 0.9257 1.6706 1.1200 -0.2148 -0.0785 0.0420  497 ALA A O   
1541 C CB  . ALA A 201 ? 0.5905 1.1626 0.7392 -0.2649 -0.0937 0.0386  497 ALA A CB  
1542 N N   . ASN A 202 ? 0.9344 1.6254 1.0771 -0.2907 -0.0776 0.0502  498 ASN A N   
1543 C CA  . ASN A 202 ? 0.8665 1.5965 1.0238 -0.2754 -0.0694 0.0518  498 ASN A CA  
1544 C C   . ASN A 202 ? 0.9278 1.7432 1.0805 -0.2863 -0.0647 0.0568  498 ASN A C   
1545 O O   . ASN A 202 ? 1.0170 1.8694 1.1774 -0.2758 -0.0578 0.0585  498 ASN A O   
1546 C CB  . ASN A 202 ? 0.8043 1.4718 0.9390 -0.3014 -0.0677 0.0547  498 ASN A CB  
1547 C CG  . ASN A 202 ? 0.7427 1.3318 0.8805 -0.2896 -0.0719 0.0500  498 ASN A CG  
1548 O OD1 . ASN A 202 ? 0.7830 1.3778 0.9531 -0.2493 -0.0723 0.0442  498 ASN A OD1 
1549 N ND2 . ASN A 202 ? 0.6175 1.1293 0.7148 -0.3248 -0.0751 0.0526  498 ASN A ND2 
1550 N N   . VAL A 203 ? 0.9143 1.7653 1.0533 -0.3072 -0.0684 0.0593  499 VAL A N   
1551 C CA  . VAL A 203 ? 0.9532 1.8871 1.0808 -0.3271 -0.0643 0.0651  499 VAL A CA  
1552 C C   . VAL A 203 ? 0.9734 1.9888 1.1317 -0.2785 -0.0579 0.0627  499 VAL A C   
1553 O O   . VAL A 203 ? 1.0175 2.0941 1.1705 -0.2852 -0.0521 0.0668  499 VAL A O   
1554 C CB  . VAL A 203 ? 0.9787 1.9368 1.0849 -0.3590 -0.0699 0.0680  499 VAL A CB  
1555 C CG1 . VAL A 203 ? 1.0048 2.0535 1.0954 -0.3853 -0.0659 0.0747  499 VAL A CG1 
1556 C CG2 . VAL A 203 ? 1.0718 1.9364 1.1380 -0.4041 -0.0765 0.0697  499 VAL A CG2 
1557 N N   . GLN A 204 ? 0.9897 2.0042 1.1744 -0.2284 -0.0592 0.0561  500 GLN A N   
1558 C CA  . GLN A 204 ? 1.0269 2.0997 1.2305 -0.1772 -0.0533 0.0530  500 GLN A CA  
1559 C C   . GLN A 204 ? 1.0113 2.0630 1.2198 -0.1659 -0.0471 0.0524  500 GLN A C   
1560 O O   . GLN A 204 ? 1.0282 2.1401 1.2358 -0.1542 -0.0406 0.0541  500 GLN A O   
1561 C CB  . GLN A 204 ? 1.0639 2.1213 1.2841 -0.1270 -0.0569 0.0462  500 GLN A CB  
1562 C CG  . GLN A 204 ? 1.1293 2.2629 1.3530 -0.0802 -0.0532 0.0440  500 GLN A CG  
1563 C CD  . GLN A 204 ? 1.1962 2.3394 1.4229 -0.0424 -0.0459 0.0413  500 GLN A CD  
1564 O OE1 . GLN A 204 ? 1.1995 2.2779 1.4331 -0.0252 -0.0456 0.0375  500 GLN A OE1 
1565 N NE2 . GLN A 204 ? 1.2362 2.4629 1.4553 -0.0295 -0.0402 0.0433  500 GLN A NE2 
1566 N N   . PHE A 205 ? 0.9267 1.8961 1.1390 -0.1699 -0.0491 0.0501  501 PHE A N   
1567 C CA  . PHE A 205 ? 0.8903 1.8362 1.1065 -0.1626 -0.0436 0.0496  501 PHE A CA  
1568 C C   . PHE A 205 ? 0.8403 1.8137 1.0362 -0.2052 -0.0395 0.0571  501 PHE A C   
1569 O O   . PHE A 205 ? 0.7442 1.7607 0.9426 -0.1914 -0.0330 0.0581  501 PHE A O   
1570 C CB  . PHE A 205 ? 0.8869 1.7436 1.1072 -0.1654 -0.0474 0.0465  501 PHE A CB  
1571 C CG  . PHE A 205 ? 0.9738 1.8063 1.2002 -0.1535 -0.0423 0.0453  501 PHE A CG  
1572 C CD1 . PHE A 205 ? 1.0071 1.8449 1.2505 -0.1034 -0.0391 0.0392  501 PHE A CD1 
1573 C CD2 . PHE A 205 ? 1.0182 1.8179 1.2276 -0.1923 -0.0411 0.0504  501 PHE A CD2 
1574 C CE1 . PHE A 205 ? 0.9774 1.7942 1.2249 -0.0926 -0.0346 0.0377  501 PHE A CE1 
1575 C CE2 . PHE A 205 ? 1.0103 1.7913 1.2257 -0.1806 -0.0365 0.0495  501 PHE A CE2 
1576 C CZ  . PHE A 205 ? 0.9470 1.7395 1.1835 -0.1309 -0.0333 0.0429  501 PHE A CZ  
1577 N N   . THR A 206 ? 0.8719 1.8166 1.0416 -0.2579 -0.0438 0.0625  502 THR A N   
1578 C CA  . THR A 206 ? 0.9131 1.8721 1.0530 -0.3048 -0.0413 0.0703  502 THR A CA  
1579 C C   . THR A 206 ? 0.8982 1.9615 1.0391 -0.3001 -0.0363 0.0735  502 THR A C   
1580 O O   . THR A 206 ? 0.8444 1.9349 0.9735 -0.3159 -0.0316 0.0779  502 THR A O   
1581 C CB  . THR A 206 ? 0.8807 1.7928 0.9819 -0.3598 -0.0480 0.0751  502 THR A CB  
1582 O OG1 . THR A 206 ? 0.8300 1.6427 0.9243 -0.3631 -0.0527 0.0721  502 THR A OG1 
1583 C CG2 . THR A 206 ? 0.7937 1.7145 0.8533 -0.4120 -0.0464 0.0835  502 THR A CG2 
1584 N N   . GLU A 207 ? 0.9168 2.0417 1.0692 -0.2783 -0.0375 0.0714  503 GLU A N   
1585 C CA  . GLU A 207 ? 0.9489 2.1799 1.1013 -0.2677 -0.0328 0.0738  503 GLU A CA  
1586 C C   . GLU A 207 ? 1.0054 2.2604 1.1756 -0.2193 -0.0259 0.0700  503 GLU A C   
1587 O O   . GLU A 207 ? 1.1132 2.4284 1.2747 -0.2260 -0.0212 0.0738  503 GLU A O   
1588 C CB  . GLU A 207 ? 0.8924 2.1811 1.0519 -0.2486 -0.0355 0.0719  503 GLU A CB  
1589 C CG  . GLU A 207 ? 0.9929 2.3368 1.1266 -0.3002 -0.0383 0.0789  503 GLU A CG  
1590 C CD  . GLU A 207 ? 1.0611 2.4011 1.1965 -0.3018 -0.0444 0.0771  503 GLU A CD  
1591 O OE1 . GLU A 207 ? 1.0318 2.3706 1.1909 -0.2507 -0.0451 0.0706  503 GLU A OE1 
1592 O OE2 . GLU A 207 ? 1.0922 2.4258 1.2009 -0.3548 -0.0490 0.0822  503 GLU A OE2 
1593 N N   . ILE A 208 ? 0.9561 2.1626 1.1474 -0.1713 -0.0259 0.0624  504 ILE A N   
1594 C CA  . ILE A 208 ? 0.9793 2.1948 1.1809 -0.1248 -0.0199 0.0580  504 ILE A CA  
1595 C C   . ILE A 208 ? 0.8993 2.0873 1.0948 -0.1501 -0.0160 0.0615  504 ILE A C   
1596 O O   . ILE A 208 ? 0.9349 2.1591 1.1307 -0.1281 -0.0102 0.0610  504 ILE A O   
1597 C CB  . ILE A 208 ? 0.8960 2.0521 1.1136 -0.0748 -0.0218 0.0492  504 ILE A CB  
1598 C CG1 . ILE A 208 ? 0.8828 2.0570 1.1025 -0.0548 -0.0266 0.0465  504 ILE A CG1 
1599 C CG2 . ILE A 208 ? 0.8517 2.0195 1.0708 -0.0235 -0.0161 0.0440  504 ILE A CG2 
1600 C CD1 . ILE A 208 ? 0.9081 2.0244 1.1365 -0.0070 -0.0294 0.0384  504 ILE A CD1 
1601 N N   . CYS A 209 ? 0.9309 2.0526 1.1170 -0.1949 -0.0194 0.0651  505 CYS A N   
1602 C CA  . CYS A 209 ? 0.9236 2.0145 1.0981 -0.2218 -0.0161 0.0693  505 CYS A CA  
1603 C C   . CYS A 209 ? 1.0392 2.1975 1.1908 -0.2586 -0.0135 0.0772  505 CYS A C   
1604 O O   . CYS A 209 ? 1.0823 2.2710 1.2333 -0.2505 -0.0079 0.0786  505 CYS A O   
1605 C CB  . CYS A 209 ? 0.9024 1.9003 1.0637 -0.2585 -0.0212 0.0712  505 CYS A CB  
1606 S SG  . CYS A 209 ? 0.8856 1.8010 1.0707 -0.2214 -0.0223 0.0633  505 CYS A SG  
1607 N N   . ILE A 210 ? 1.0494 2.2315 1.1790 -0.3013 -0.0180 0.0825  506 ILE A N   
1608 C CA  . ILE A 210 ? 1.1091 2.3663 1.2147 -0.3371 -0.0167 0.0897  506 ILE A CA  
1609 C C   . ILE A 210 ? 1.1455 2.5044 1.2687 -0.2926 -0.0116 0.0873  506 ILE A C   
1610 O O   . ILE A 210 ? 1.0903 2.5098 1.2027 -0.3041 -0.0083 0.0916  506 ILE A O   
1611 C CB  . ILE A 210 ? 1.0354 2.3045 1.1118 -0.3885 -0.0231 0.0949  506 ILE A CB  
1612 C CG1 . ILE A 210 ? 1.0187 2.1754 1.0735 -0.4221 -0.0290 0.0956  506 ILE A CG1 
1613 C CG2 . ILE A 210 ? 1.0851 2.4162 1.1279 -0.4374 -0.0231 0.1030  506 ILE A CG2 
1614 C CD1 . ILE A 210 ? 1.0750 2.2309 1.0990 -0.4664 -0.0359 0.0991  506 ILE A CD1 
1615 N N   . GLN A 211 ? 1.2061 2.5819 1.3525 -0.2400 -0.0114 0.0804  507 GLN A N   
1616 C CA  . GLN A 211 ? 1.2428 2.7030 1.3985 -0.1894 -0.0069 0.0771  507 GLN A CA  
1617 C C   . GLN A 211 ? 1.2143 2.6680 1.3746 -0.1630 -0.0009 0.0752  507 GLN A C   
1618 O O   . GLN A 211 ? 1.2271 2.7600 1.3800 -0.1541 0.0025  0.0774  507 GLN A O   
1619 C CB  . GLN A 211 ? 1.2449 2.6965 1.4169 -0.1356 -0.0084 0.0692  507 GLN A CB  
1620 C CG  . GLN A 211 ? 1.2951 2.8498 1.4620 -0.1075 -0.0076 0.0688  507 GLN A CG  
1621 C CD  . GLN A 211 ? 1.3088 2.8741 1.4799 -0.0339 -0.0041 0.0610  507 GLN A CD  
1622 O OE1 . GLN A 211 ? 1.2788 2.7631 1.4589 -0.0022 -0.0039 0.0545  507 GLN A OE1 
1623 N NE2 . GLN A 211 ? 1.3446 3.0090 1.5040 -0.0063 -0.0017 0.0614  507 GLN A NE2 
1624 N N   . GLN A 212 ? 1.1564 2.5194 1.3279 -0.1504 0.0000  0.0710  508 GLN A N   
1625 C CA  . GLN A 212 ? 1.1275 2.4753 1.3023 -0.1289 0.0056  0.0691  508 GLN A CA  
1626 C C   . GLN A 212 ? 1.0710 2.4147 1.2300 -0.1817 0.0073  0.0772  508 GLN A C   
1627 O O   . GLN A 212 ? 0.9867 2.2961 1.1483 -0.1735 0.0115  0.0764  508 GLN A O   
1628 C CB  . GLN A 212 ? 1.1317 2.3883 1.3223 -0.0964 0.0056  0.0614  508 GLN A CB  
1629 C CG  . GLN A 212 ? 1.1691 2.4171 1.3691 -0.0410 0.0037  0.0527  508 GLN A CG  
1630 C CD  . GLN A 212 ? 1.2079 2.5114 1.4001 0.0133  0.0080  0.0482  508 GLN A CD  
1631 O OE1 . GLN A 212 ? 1.2110 2.5157 1.4001 0.0587  0.0063  0.0420  508 GLN A OE1 
1632 N NE2 . GLN A 212 ? 1.2166 2.5627 1.4008 0.0100  0.0130  0.0514  508 GLN A NE2 
1633 N N   . GLY A 213 ? 1.0803 2.4548 1.2189 -0.2363 0.0036  0.0849  509 GLY A N   
1634 C CA  . GLY A 213 ? 1.0542 2.4216 1.1683 -0.2901 0.0040  0.0929  509 GLY A CA  
1635 C C   . GLY A 213 ? 1.0273 2.2875 1.1264 -0.3289 0.0012  0.0955  509 GLY A C   
1636 O O   . GLY A 213 ? 1.0200 2.2417 1.1073 -0.3460 0.0042  0.0987  509 GLY A O   
1637 N N   . TRP A 214 ? 1.1069 2.3162 1.2032 -0.3418 -0.0046 0.0943  510 TRP A N   
1638 C CA  . TRP A 214 ? 1.1231 2.2329 1.1933 -0.3841 -0.0085 0.0977  510 TRP A CA  
1639 C C   . TRP A 214 ? 1.1655 2.2808 1.1884 -0.4499 -0.0137 0.1058  510 TRP A C   
1640 O O   . TRP A 214 ? 1.1084 2.2964 1.1256 -0.4627 -0.0164 0.1075  510 TRP A O   
1641 C CB  . TRP A 214 ? 1.0864 2.1266 1.1708 -0.3672 -0.0131 0.0922  510 TRP A CB  
1642 C CG  . TRP A 214 ? 1.1197 2.0518 1.1762 -0.3997 -0.0164 0.0950  510 TRP A CG  
1643 C CD1 . TRP A 214 ? 1.1362 2.0180 1.1840 -0.4031 -0.0126 0.0971  510 TRP A CD1 
1644 C CD2 . TRP A 214 ? 1.1689 2.0278 1.1965 -0.4318 -0.0241 0.0961  510 TRP A CD2 
1645 N NE1 . TRP A 214 ? 1.1723 1.9528 1.1853 -0.4338 -0.0175 0.0998  510 TRP A NE1 
1646 C CE2 . TRP A 214 ? 1.1699 1.9320 1.1685 -0.4512 -0.0249 0.0988  510 TRP A CE2 
1647 C CE3 . TRP A 214 ? 1.1840 2.0479 1.2037 -0.4448 -0.0304 0.0952  510 TRP A CE3 
1648 C CZ2 . TRP A 214 ? 1.1624 1.8283 1.1203 -0.4804 -0.0321 0.1001  510 TRP A CZ2 
1649 C CZ3 . TRP A 214 ? 1.2137 1.9848 1.1967 -0.4754 -0.0374 0.0962  510 TRP A CZ3 
1650 C CH2 . TRP A 214 ? 1.2273 1.8984 1.1779 -0.4916 -0.0384 0.0984  510 TRP A CH2 
1651 N N   . LYS A 215 ? 1.2310 2.2666 1.2146 -0.4918 -0.0154 0.1108  511 LYS A N   
1652 C CA  . LYS A 215 ? 1.3301 2.3519 1.2556 -0.5577 -0.0209 0.1182  511 LYS A CA  
1653 C C   . LYS A 215 ? 1.2422 2.1561 1.1307 -0.5857 -0.0284 0.1183  511 LYS A C   
1654 O O   . LYS A 215 ? 1.2735 2.0841 1.1298 -0.6003 -0.0295 0.1199  511 LYS A O   
1655 C CB  . LYS A 215 ? 1.4720 2.4772 1.3708 -0.5813 -0.0175 0.1234  511 LYS A CB  
1656 C CG  . LYS A 215 ? 1.4843 2.4979 1.4267 -0.5294 -0.0084 0.1200  511 LYS A CG  
1657 C CD  . LYS A 215 ? 1.5193 2.6448 1.4850 -0.5100 -0.0025 0.1204  511 LYS A CD  
1658 C CE  . LYS A 215 ? 1.5053 2.7365 1.4973 -0.4869 -0.0039 0.1172  511 LYS A CE  
1659 N NZ  . LYS A 215 ? 1.4824 2.8161 1.4974 -0.4552 0.0019  0.1164  511 LYS A NZ  
1660 N N   . ALA A 216 ? 1.1973 2.1346 1.0872 -0.5906 -0.0333 0.1167  512 ALA A N   
1661 C CA  . ALA A 216 ? 1.0483 1.8901 0.9145 -0.6022 -0.0399 0.1148  512 ALA A CA  
1662 C C   . ALA A 216 ? 1.0984 1.8556 0.8825 -0.6659 -0.0469 0.1205  512 ALA A C   
1663 O O   . ALA A 216 ? 1.1538 1.9576 0.9025 -0.7093 -0.0500 0.1251  512 ALA A O   
1664 C CB  . ALA A 216 ? 0.9868 1.8825 0.8783 -0.5878 -0.0428 0.1114  512 ALA A CB  
1665 N N   . PRO A 217 ? 1.1386 1.7694 0.8849 -0.6728 -0.0500 0.1200  513 PRO A N   
1666 C CA  . PRO A 217 ? 1.3515 1.8851 1.0072 -0.7288 -0.0582 0.1239  513 PRO A CA  
1667 C C   . PRO A 217 ? 1.5210 2.0523 1.1503 -0.7534 -0.0657 0.1232  513 PRO A C   
1668 O O   . PRO A 217 ? 1.7146 2.1903 1.2651 -0.8056 -0.0727 0.1266  513 PRO A O   
1669 C CB  . PRO A 217 ? 1.3387 1.7378 0.9650 -0.7144 -0.0589 0.1224  513 PRO A CB  
1670 C CG  . PRO A 217 ? 1.1171 1.5469 0.8236 -0.6549 -0.0531 0.1171  513 PRO A CG  
1671 C CD  . PRO A 217 ? 1.0231 1.5936 0.8004 -0.6295 -0.0463 0.1161  513 PRO A CD  
1672 N N   . ARG A 218 ? 1.4881 2.0738 1.1764 -0.7175 -0.0645 0.1187  514 ARG A N   
1673 C CA  . ARG A 218 ? 1.5250 2.1292 1.1998 -0.7359 -0.0703 0.1183  514 ARG A CA  
1674 C C   . ARG A 218 ? 1.6533 2.1238 1.2511 -0.7668 -0.0789 0.1181  514 ARG A C   
1675 O O   . ARG A 218 ? 1.7283 2.1864 1.2676 -0.8134 -0.0852 0.1214  514 ARG A O   
1676 C CB  . ARG A 218 ? 1.5237 2.2358 1.1872 -0.7727 -0.0707 0.1235  514 ARG A CB  
1677 C CG  . ARG A 218 ? 1.4562 2.3091 1.1991 -0.7303 -0.0637 0.1216  514 ARG A CG  
1678 C CD  . ARG A 218 ? 1.5391 2.4943 1.2755 -0.7573 -0.0658 0.1251  514 ARG A CD  
1679 N NE  . ARG A 218 ? 1.5011 2.5307 1.3006 -0.7093 -0.0630 0.1203  514 ARG A NE  
1680 C CZ  . ARG A 218 ? 1.4178 2.5332 1.2800 -0.6558 -0.0560 0.1169  514 ARG A CZ  
1681 N NH1 . ARG A 218 ? 1.3971 2.5666 1.3050 -0.6134 -0.0547 0.1122  514 ARG A NH1 
1682 N NH2 . ARG A 218 ? 1.3417 2.4841 1.2163 -0.6433 -0.0505 0.1178  514 ARG A NH2 
1683 N N   . GLY A 219 ? 1.6446 2.0146 1.2396 -0.7384 -0.0793 0.1140  515 GLY A N   
1684 C CA  . GLY A 219 ? 1.6900 1.9321 1.2192 -0.7512 -0.0870 0.1120  515 GLY A CA  
1685 C C   . GLY A 219 ? 1.5907 1.8245 1.1677 -0.7100 -0.0880 0.1054  515 GLY A C   
1686 O O   . GLY A 219 ? 1.5432 1.8783 1.1957 -0.6818 -0.0847 0.1027  515 GLY A O   
1687 N N   . ARG A 220 ? 1.5941 1.7021 1.1219 -0.7039 -0.0930 0.1021  516 ARG A N   
1688 C CA  . ARG A 220 ? 1.5521 1.6394 1.1161 -0.6671 -0.0951 0.0952  516 ARG A CA  
1689 C C   . ARG A 220 ? 1.4573 1.5430 1.0809 -0.6178 -0.0902 0.0907  516 ARG A C   
1690 O O   . ARG A 220 ? 1.3461 1.5056 1.0473 -0.5828 -0.0879 0.0858  516 ARG A O   
1691 C CB  . ARG A 220 ? 1.6393 1.5927 1.1167 -0.6813 -0.1032 0.0932  516 ARG A CB  
1692 C CG  . ARG A 220 ? 1.6060 1.5420 1.1143 -0.6489 -0.1064 0.0859  516 ARG A CG  
1693 C CD  . ARG A 220 ? 1.6057 1.5634 1.0930 -0.6762 -0.1119 0.0866  516 ARG A CD  
1694 N NE  . ARG A 220 ? 1.7185 1.5504 1.1276 -0.6808 -0.1189 0.0835  516 ARG A NE  
1695 C CZ  . ARG A 220 ? 1.7129 1.5336 1.1354 -0.6640 -0.1229 0.0780  516 ARG A CZ  
1696 N NH1 . ARG A 220 ? 1.6774 1.6037 1.1877 -0.6429 -0.1211 0.0748  516 ARG A NH1 
1697 N NH2 . ARG A 220 ? 1.6918 1.3929 1.0347 -0.6664 -0.1288 0.0753  516 ARG A NH2 
1698 N N   . PHE A 221 ? 1.4265 1.4251 1.0091 -0.6146 -0.0890 0.0922  517 PHE A N   
1699 C CA  . PHE A 221 ? 1.3075 1.2831 0.9301 -0.5721 -0.0854 0.0887  517 PHE A CA  
1700 C C   . PHE A 221 ? 1.4227 1.4484 1.0738 -0.5689 -0.0776 0.0935  517 PHE A C   
1701 O O   . PHE A 221 ? 1.4922 1.4416 1.1044 -0.5657 -0.0757 0.0967  517 PHE A O   
1702 C CB  . PHE A 221 ? 1.2584 1.0829 0.8055 -0.5620 -0.0902 0.0866  517 PHE A CB  
1703 C CG  . PHE A 221 ? 1.3469 1.1187 0.8654 -0.5589 -0.0974 0.0808  517 PHE A CG  
1704 C CD1 . PHE A 221 ? 1.4836 1.1561 0.9035 -0.5849 -0.1035 0.0820  517 PHE A CD1 
1705 C CD2 . PHE A 221 ? 1.1677 0.9863 0.7529 -0.5295 -0.0986 0.0737  517 PHE A CD2 
1706 C CE1 . PHE A 221 ? 1.4299 1.0530 0.8206 -0.5805 -0.1096 0.0769  517 PHE A CE1 
1707 C CE2 . PHE A 221 ? 1.2364 1.0041 0.7926 -0.5263 -0.1048 0.0685  517 PHE A CE2 
1708 C CZ  . PHE A 221 ? 1.3192 0.9912 0.7797 -0.5514 -0.1099 0.0703  517 PHE A CZ  
1709 N N   . ASP A 222 ? 1.3473 1.5024 1.0647 -0.5651 -0.0726 0.0940  518 ASP A N   
1710 C CA  . ASP A 222 ? 1.1335 1.3536 0.8862 -0.5569 -0.0645 0.0975  518 ASP A CA  
1711 C C   . ASP A 222 ? 1.0867 1.3524 0.9178 -0.5068 -0.0603 0.0918  518 ASP A C   
1712 O O   . ASP A 222 ? 1.1111 1.4520 1.0011 -0.4800 -0.0604 0.0861  518 ASP A O   
1713 C CB  . ASP A 222 ? 1.0732 1.4070 0.8464 -0.5755 -0.0615 0.1006  518 ASP A CB  
1714 C CG  . ASP A 222 ? 1.2755 1.5776 0.9731 -0.6293 -0.0673 0.1056  518 ASP A CG  
1715 O OD1 . ASP A 222 ? 1.4270 1.6104 1.0498 -0.6509 -0.0733 0.1064  518 ASP A OD1 
1716 O OD2 . ASP A 222 ? 1.2996 1.6948 1.0076 -0.6490 -0.0662 0.1084  518 ASP A OD2 
1717 N N   . VAL A 223 ? 1.0995 1.3153 0.9253 -0.4890 -0.0567 0.0930  519 VAL A N   
1718 C CA  . VAL A 223 ? 1.0640 1.3178 0.9546 -0.4252 -0.0521 0.0848  519 VAL A CA  
1719 C C   . VAL A 223 ? 1.0229 1.4078 0.9752 -0.4209 -0.0459 0.0856  519 VAL A C   
1720 O O   . VAL A 223 ? 0.9880 1.4151 0.9299 -0.4505 -0.0409 0.0932  519 VAL A O   
1721 C CB  . VAL A 223 ? 1.0032 1.1786 0.8669 -0.3961 -0.0492 0.0844  519 VAL A CB  
1722 C CG1 . VAL A 223 ? 0.7791 0.9974 0.7068 -0.3373 -0.0450 0.0758  519 VAL A CG1 
1723 C CG2 . VAL A 223 ? 1.1301 1.1798 0.9299 -0.3911 -0.0553 0.0830  519 VAL A CG2 
1724 N N   . LEU A 224 ? 0.9323 1.3800 0.9441 -0.3818 -0.0460 0.0778  520 LEU A N   
1725 C CA  . LEU A 224 ? 0.8178 1.3816 0.8823 -0.3633 -0.0402 0.0769  520 LEU A CA  
1726 C C   . LEU A 224 ? 0.8569 1.4222 0.9363 -0.3310 -0.0330 0.0753  520 LEU A C   
1727 O O   . LEU A 224 ? 0.9186 1.3989 0.9794 -0.3095 -0.0335 0.0721  520 LEU A O   
1728 C CB  . LEU A 224 ? 0.6833 1.2894 0.7922 -0.3231 -0.0428 0.0685  520 LEU A CB  
1729 C CG  . LEU A 224 ? 0.7026 1.3144 0.7966 -0.3416 -0.0483 0.0687  520 LEU A CG  
1730 C CD1 . LEU A 224 ? 0.6975 1.2893 0.8170 -0.3119 -0.0540 0.0611  520 LEU A CD1 
1731 C CD2 . LEU A 224 ? 0.7193 1.4247 0.8227 -0.3406 -0.0445 0.0708  520 LEU A CD2 
1732 N N   . PRO A 225 ? 0.8310 1.4898 0.9388 -0.3233 -0.0264 0.0768  521 PRO A N   
1733 C CA  . PRO A 225 ? 0.8842 1.5486 1.0094 -0.2858 -0.0200 0.0734  521 PRO A CA  
1734 C C   . PRO A 225 ? 0.8103 1.4830 0.9746 -0.2285 -0.0210 0.0623  521 PRO A C   
1735 O O   . PRO A 225 ? 0.8607 1.5474 1.0419 -0.2186 -0.0257 0.0584  521 PRO A O   
1736 C CB  . PRO A 225 ? 0.8913 1.6447 1.0203 -0.2968 -0.0126 0.0786  521 PRO A CB  
1737 C CG  . PRO A 225 ? 0.9259 1.7258 1.0529 -0.3043 -0.0157 0.0784  521 PRO A CG  
1738 C CD  . PRO A 225 ? 0.9139 1.6473 1.0179 -0.3334 -0.0241 0.0794  521 PRO A CD  
1739 N N   . LEU A 226 ? 0.7616 1.4209 0.9345 -0.1928 -0.0168 0.0573  522 LEU A N   
1740 C CA  . LEU A 226 ? 0.6870 1.3468 0.8869 -0.1418 -0.0173 0.0468  522 LEU A CA  
1741 C C   . LEU A 226 ? 0.6715 1.4281 0.8964 -0.1170 -0.0121 0.0453  522 LEU A C   
1742 O O   . LEU A 226 ? 0.8186 1.6276 1.0420 -0.1253 -0.0056 0.0498  522 LEU A O   
1743 C CB  . LEU A 226 ? 0.6069 1.1970 0.7973 -0.1177 -0.0168 0.0413  522 LEU A CB  
1744 C CG  . LEU A 226 ? 0.5867 1.0845 0.7522 -0.1295 -0.0219 0.0415  522 LEU A CG  
1745 C CD1 . LEU A 226 ? 0.6938 1.1479 0.8514 -0.1076 -0.0208 0.0373  522 LEU A CD1 
1746 C CD2 . LEU A 226 ? 0.5407 1.0088 0.7157 -0.1184 -0.0276 0.0361  522 LEU A CD2 
1747 N N   . LEU A 227 ? 0.5438 1.3240 0.7876 -0.0847 -0.0147 0.0390  523 LEU A N   
1748 C CA  . LEU A 227 ? 0.6669 1.5003 0.9149 -0.0445 -0.0101 0.0347  523 LEU A CA  
1749 C C   . LEU A 227 ? 0.6988 1.4939 0.9536 0.0011  -0.0114 0.0247  523 LEU A C   
1750 O O   . LEU A 227 ? 0.7460 1.5022 1.0013 0.0186  -0.0166 0.0195  523 LEU A O   
1751 C CB  . LEU A 227 ? 0.7264 1.5998 0.9723 -0.0398 -0.0121 0.0353  523 LEU A CB  
1752 C CG  . LEU A 227 ? 0.8153 1.7682 1.0511 -0.0407 -0.0066 0.0396  523 LEU A CG  
1753 C CD1 . LEU A 227 ? 0.8790 1.8704 1.1134 -0.0037 -0.0078 0.0354  523 LEU A CD1 
1754 C CD2 . LEU A 227 ? 0.8332 1.8088 1.0641 -0.0263 0.0007  0.0393  523 LEU A CD2 
1755 N N   . LEU A 228 ? 0.5891 1.3731 0.8352 0.0180  -0.0065 0.0218  524 LEU A N   
1756 C CA  . LEU A 228 ? 0.6590 1.3755 0.8923 0.0531  -0.0078 0.0118  524 LEU A CA  
1757 C C   . LEU A 228 ? 0.7343 1.4942 0.9615 0.0996  -0.0035 0.0061  524 LEU A C   
1758 O O   . LEU A 228 ? 0.6235 1.4437 0.8512 0.1033  0.0031  0.0090  524 LEU A O   
1759 C CB  . LEU A 228 ? 0.5690 1.2302 0.7902 0.0379  -0.0068 0.0117  524 LEU A CB  
1760 C CG  . LEU A 228 ? 0.5761 1.2006 0.7946 -0.0049 -0.0100 0.0188  524 LEU A CG  
1761 C CD1 . LEU A 228 ? 0.5543 1.1453 0.7571 -0.0192 -0.0080 0.0214  524 LEU A CD1 
1762 C CD2 . LEU A 228 ? 0.6089 1.1705 0.8275 -0.0034 -0.0168 0.0144  524 LEU A CD2 
1763 N N   . GLN A 229 ? 0.7869 1.5111 1.0020 0.1353  -0.0072 -0.0019 525 GLN A N   
1764 C CA  . GLN A 229 ? 0.8239 1.5668 1.0192 0.1869  -0.0045 -0.0087 525 GLN A CA  
1765 C C   . GLN A 229 ? 0.7661 1.4184 0.9304 0.2051  -0.0059 -0.0183 525 GLN A C   
1766 O O   . GLN A 229 ? 0.6172 1.1917 0.7718 0.1969  -0.0117 -0.0224 525 GLN A O   
1767 C CB  . GLN A 229 ? 0.8980 1.6463 1.0834 0.2122  -0.0082 -0.0103 525 GLN A CB  
1768 C CG  . GLN A 229 ? 0.9228 1.6320 1.0684 0.2683  -0.0090 -0.0198 525 GLN A CG  
1769 C CD  . GLN A 229 ? 0.8808 1.5794 1.0117 0.2889  -0.0138 -0.0206 525 GLN A CD  
1770 O OE1 . GLN A 229 ? 0.8363 1.5752 0.9889 0.2639  -0.0154 -0.0139 525 GLN A OE1 
1771 N NE2 . GLN A 229 ? 0.9221 1.5603 1.0102 0.3343  -0.0164 -0.0289 525 GLN A NE2 
1772 N N   . ALA A 230 ? 0.7841 1.4499 0.9317 0.2269  -0.0007 -0.0218 526 ALA A N   
1773 C CA  . ALA A 230 ? 0.8316 1.4174 0.9467 0.2395  -0.0023 -0.0309 526 ALA A CA  
1774 C C   . ALA A 230 ? 0.8659 1.4384 0.9388 0.2947  -0.0010 -0.0398 526 ALA A C   
1775 O O   . ALA A 230 ? 0.8807 1.5277 0.9528 0.3240  0.0051  -0.0383 526 ALA A O   
1776 C CB  . ALA A 230 ? 0.8379 1.4361 0.9598 0.2180  0.0019  -0.0282 526 ALA A CB  
1777 N N   . ASN A 231 ? 0.8923 1.3699 0.9253 0.3088  -0.0067 -0.0489 527 ASN A N   
1778 C CA  . ASN A 231 ? 0.9392 1.3747 0.9144 0.3611  -0.0069 -0.0585 527 ASN A CA  
1779 C C   . ASN A 231 ? 0.9836 1.4889 0.9562 0.4051  -0.0039 -0.0560 527 ASN A C   
1780 O O   . ASN A 231 ? 1.0517 1.5854 0.9950 0.4441  0.0004  -0.0585 527 ASN A O   
1781 C CB  . ASN A 231 ? 1.0770 1.5000 1.0247 0.3756  -0.0030 -0.0645 527 ASN A CB  
1782 C CG  . ASN A 231 ? 1.1627 1.4958 1.0350 0.4178  -0.0061 -0.0768 527 ASN A CG  
1783 O OD1 . ASN A 231 ? 1.1884 1.4382 1.0269 0.4174  -0.0129 -0.0814 527 ASN A OD1 
1784 N ND2 . ASN A 231 ? 1.1807 1.5252 1.0202 0.4536  -0.0011 -0.0821 527 ASN A ND2 
1785 N N   . GLY A 232 ? 0.9733 1.5023 0.9716 0.3937  -0.0072 -0.0503 528 GLY A N   
1786 C CA  . GLY A 232 ? 1.0191 1.5998 1.0067 0.4192  -0.0067 -0.0462 528 GLY A CA  
1787 C C   . GLY A 232 ? 1.0262 1.7111 1.0381 0.4062  -0.0003 -0.0376 528 GLY A C   
1788 O O   . GLY A 232 ? 1.1301 1.8644 1.1304 0.4233  -0.0002 -0.0341 528 GLY A O   
1789 N N   . ASN A 233 ? 0.9606 1.6806 1.0029 0.3757  0.0046  -0.0342 529 ASN A N   
1790 C CA  . ASN A 233 ? 0.9530 1.7664 1.0107 0.3616  0.0106  -0.0259 529 ASN A CA  
1791 C C   . ASN A 233 ? 0.9984 1.8730 1.0956 0.3184  0.0099  -0.0156 529 ASN A C   
1792 O O   . ASN A 233 ? 1.0245 1.8699 1.1457 0.2912  0.0054  -0.0140 529 ASN A O   
1793 C CB  . ASN A 233 ? 0.9264 1.7519 0.9964 0.3427  0.0163  -0.0250 529 ASN A CB  
1794 C CG  . ASN A 233 ? 0.9478 1.7504 0.9726 0.3878  0.0189  -0.0329 529 ASN A CG  
1795 O OD1 . ASN A 233 ? 1.0339 1.8978 1.0459 0.4025  0.0228  -0.0295 529 ASN A OD1 
1796 N ND2 . ASN A 233 ? 0.8608 1.5732 0.8570 0.4097  0.0160  -0.0438 529 ASN A ND2 
1797 N N   . ASP A 234 ? 1.0502 2.0105 1.1498 0.3123  0.0138  -0.0089 530 ASP A N   
1798 C CA  . ASP A 234 ? 1.0255 2.0459 1.1550 0.2676  0.0133  0.0008  530 ASP A CA  
1799 C C   . ASP A 234 ? 0.8785 1.8833 1.0400 0.2125  0.0141  0.0063  530 ASP A C   
1800 O O   . ASP A 234 ? 1.0627 2.0662 1.2252 0.2040  0.0187  0.0069  530 ASP A O   
1801 C CB  . ASP A 234 ? 1.1224 2.2413 1.2436 0.2698  0.0170  0.0067  530 ASP A CB  
1802 C CG  . ASP A 234 ? 1.2335 2.3739 1.3181 0.3276  0.0155  0.0019  530 ASP A CG  
1803 O OD1 . ASP A 234 ? 1.2632 2.4828 1.3340 0.3415  0.0181  0.0051  530 ASP A OD1 
1804 O OD2 . ASP A 234 ? 1.2913 2.3689 1.3567 0.3599  0.0111  -0.0050 530 ASP A OD2 
1805 N N   . PRO A 235 ? 0.5963 1.5869 0.7796 0.1759  0.0097  0.0105  531 PRO A N   
1806 C CA  . PRO A 235 ? 0.5147 1.4708 0.7194 0.1305  0.0089  0.0145  531 PRO A CA  
1807 C C   . PRO A 235 ? 0.5716 1.5810 0.7818 0.0855  0.0133  0.0246  531 PRO A C   
1808 O O   . PRO A 235 ? 0.6894 1.7693 0.8921 0.0805  0.0158  0.0294  531 PRO A O   
1809 C CB  . PRO A 235 ? 0.5141 1.4387 0.7321 0.1121  0.0017  0.0155  531 PRO A CB  
1810 C CG  . PRO A 235 ? 0.4319 1.4111 0.6419 0.1235  0.0010  0.0173  531 PRO A CG  
1811 C CD  . PRO A 235 ? 0.5344 1.5370 0.7200 0.1762  0.0047  0.0116  531 PRO A CD  
1812 N N   . GLU A 236 ? 0.5804 1.5546 0.7999 0.0516  0.0137  0.0280  532 GLU A N   
1813 C CA  . GLU A 236 ? 0.5598 1.5687 0.7763 0.0082  0.0181  0.0376  532 GLU A CA  
1814 C C   . GLU A 236 ? 0.5797 1.5470 0.8011 -0.0431 0.0140  0.0441  532 GLU A C   
1815 O O   . GLU A 236 ? 0.6201 1.5260 0.8508 -0.0403 0.0091  0.0402  532 GLU A O   
1816 C CB  . GLU A 236 ? 0.5284 1.5361 0.7389 0.0229  0.0246  0.0358  532 GLU A CB  
1817 C CG  . GLU A 236 ? 0.5445 1.5720 0.7427 0.0799  0.0277  0.0272  532 GLU A CG  
1818 C CD  . GLU A 236 ? 0.5928 1.5882 0.7846 0.1014  0.0318  0.0216  532 GLU A CD  
1819 O OE1 . GLU A 236 ? 0.5374 1.5429 0.7305 0.0714  0.0366  0.0279  532 GLU A OE1 
1820 O OE2 . GLU A 236 ? 0.6153 1.5715 0.7964 0.1470  0.0301  0.0109  532 GLU A OE2 
1821 N N   . LEU A 237 ? 0.6181 1.6168 0.8276 -0.0904 0.0151  0.0541  533 LEU A N   
1822 C CA  . LEU A 237 ? 0.7218 1.6769 0.9228 -0.1419 0.0104  0.0610  533 LEU A CA  
1823 C C   . LEU A 237 ? 0.7098 1.6202 0.9005 -0.1677 0.0131  0.0659  533 LEU A C   
1824 O O   . LEU A 237 ? 0.6649 1.6037 0.8433 -0.1787 0.0198  0.0709  533 LEU A O   
1825 C CB  . LEU A 237 ? 0.7845 1.7852 0.9663 -0.1839 0.0091  0.0692  533 LEU A CB  
1826 C CG  . LEU A 237 ? 0.7278 1.7502 0.9158 -0.1759 0.0036  0.0665  533 LEU A CG  
1827 C CD1 . LEU A 237 ? 0.7859 1.8546 0.9514 -0.2220 0.0015  0.0746  533 LEU A CD1 
1828 C CD2 . LEU A 237 ? 0.6762 1.6251 0.8727 -0.1762 -0.0031 0.0628  533 LEU A CD2 
1829 N N   . PHE A 238 ? 0.7376 1.5640 0.9226 -0.1750 0.0070  0.0643  534 PHE A N   
1830 C CA  . PHE A 238 ? 0.6747 1.4158 0.8249 -0.1937 0.0066  0.0681  534 PHE A CA  
1831 C C   . PHE A 238 ? 0.7398 1.4029 0.8618 -0.2269 -0.0010 0.0719  534 PHE A C   
1832 O O   . PHE A 238 ? 0.5759 1.2126 0.7098 -0.2137 -0.0072 0.0662  534 PHE A O   
1833 C CB  . PHE A 238 ? 0.5359 1.2179 0.6882 -0.1497 0.0055  0.0586  534 PHE A CB  
1834 C CG  . PHE A 238 ? 0.5732 1.3125 0.7477 -0.1084 0.0110  0.0516  534 PHE A CG  
1835 C CD1 . PHE A 238 ? 0.6471 1.4035 0.8446 -0.0695 0.0087  0.0422  534 PHE A CD1 
1836 C CD2 . PHE A 238 ? 0.6642 1.4322 0.8291 -0.1067 0.0184  0.0544  534 PHE A CD2 
1837 C CE1 . PHE A 238 ? 0.6308 1.4270 0.8368 -0.0279 0.0133  0.0353  534 PHE A CE1 
1838 C CE2 . PHE A 238 ? 0.6014 1.4166 0.7800 -0.0652 0.0235  0.0473  534 PHE A CE2 
1839 C CZ  . PHE A 238 ? 0.4602 1.2858 0.6568 -0.0245 0.0207  0.0373  534 PHE A CZ  
1840 N N   . GLN A 239 ? 0.8439 1.4628 0.9220 -0.2681 -0.0004 0.0814  535 GLN A N   
1841 C CA  . GLN A 239 ? 0.8567 1.3906 0.8928 -0.3003 -0.0075 0.0857  535 GLN A CA  
1842 C C   . GLN A 239 ? 0.8562 1.2847 0.8628 -0.2776 -0.0110 0.0827  535 GLN A C   
1843 O O   . GLN A 239 ? 0.8949 1.2952 0.8730 -0.2816 -0.0078 0.0872  535 GLN A O   
1844 C CB  . GLN A 239 ? 0.9914 1.5362 0.9851 -0.3635 -0.0054 0.0987  535 GLN A CB  
1845 C CG  . GLN A 239 ? 1.1668 1.5941 1.0914 -0.3966 -0.0116 0.1046  535 GLN A CG  
1846 C CD  . GLN A 239 ? 1.3602 1.7336 1.2295 -0.4176 -0.0078 0.1135  535 GLN A CD  
1847 O OE1 . GLN A 239 ? 1.4666 1.7518 1.3071 -0.3911 -0.0105 0.1114  535 GLN A OE1 
1848 N NE2 . GLN A 239 ? 1.3541 1.7843 1.2067 -0.4655 -0.0016 0.1239  535 GLN A NE2 
1849 N N   . ILE A 240 ? 0.8358 1.2123 0.8492 -0.2529 -0.0175 0.0751  536 ILE A N   
1850 C CA  . ILE A 240 ? 0.8452 1.1302 0.8311 -0.2302 -0.0220 0.0720  536 ILE A CA  
1851 C C   . ILE A 240 ? 0.8978 1.1123 0.8149 -0.2642 -0.0228 0.0824  536 ILE A C   
1852 O O   . ILE A 240 ? 0.8607 1.0622 0.7439 -0.3079 -0.0241 0.0899  536 ILE A O   
1853 C CB  . ILE A 240 ? 0.8521 1.0966 0.8460 -0.2121 -0.0285 0.0649  536 ILE A CB  
1854 C CG1 . ILE A 240 ? 0.8886 1.2025 0.9388 -0.1936 -0.0279 0.0575  536 ILE A CG1 
1855 C CG2 . ILE A 240 ? 0.7627 0.9459 0.7473 -0.1760 -0.0318 0.0590  536 ILE A CG2 
1856 C CD1 . ILE A 240 ? 0.9602 1.3051 1.0127 -0.2233 -0.0299 0.0608  536 ILE A CD1 
1857 N N   . PRO A 241 ? 0.9198 1.0860 0.8089 -0.2479 -0.0225 0.0837  537 PRO A N   
1858 C CA  . PRO A 241 ? 0.9652 1.0508 0.7773 -0.2773 -0.0239 0.0942  537 PRO A CA  
1859 C C   . PRO A 241 ? 0.9451 0.9459 0.7102 -0.2864 -0.0312 0.0948  537 PRO A C   
1860 O O   . PRO A 241 ? 0.8273 0.8033 0.6094 -0.2497 -0.0359 0.0862  537 PRO A O   
1861 C CB  . PRO A 241 ? 0.9691 1.0186 0.7682 -0.2415 -0.0241 0.0923  537 PRO A CB  
1862 C CG  . PRO A 241 ? 0.9381 1.0728 0.8094 -0.2094 -0.0203 0.0831  537 PRO A CG  
1863 C CD  . PRO A 241 ? 0.9247 1.1021 0.8448 -0.2023 -0.0219 0.0756  537 PRO A CD  
1864 N N   . PRO A 242 ? 1.0719 1.0298 0.7766 -0.3368 -0.0324 0.1045  538 PRO A N   
1865 C CA  . PRO A 242 ? 1.1492 1.0259 0.8058 -0.3467 -0.0397 0.1040  538 PRO A CA  
1866 C C   . PRO A 242 ? 1.1922 0.9647 0.7984 -0.3065 -0.0451 0.1013  538 PRO A C   
1867 O O   . PRO A 242 ? 1.2857 1.0109 0.8777 -0.2898 -0.0506 0.0961  538 PRO A O   
1868 C CB  . PRO A 242 ? 1.2478 1.0932 0.8368 -0.4147 -0.0395 0.1161  538 PRO A CB  
1869 C CG  . PRO A 242 ? 1.2252 1.1826 0.8609 -0.4406 -0.0312 0.1207  538 PRO A CG  
1870 C CD  . PRO A 242 ? 1.1715 1.1586 0.8483 -0.3908 -0.0269 0.1160  538 PRO A CD  
1871 N N   . GLU A 243 ? 1.1752 0.9170 0.7553 -0.2865 -0.0437 0.1044  539 GLU A N   
1872 C CA  . GLU A 243 ? 1.1624 0.8192 0.6985 -0.2403 -0.0492 0.1013  539 GLU A CA  
1873 C C   . GLU A 243 ? 1.1086 0.8097 0.7133 -0.1880 -0.0512 0.0885  539 GLU A C   
1874 O O   . GLU A 243 ? 1.0913 0.7321 0.6639 -0.1503 -0.0564 0.0847  539 GLU A O   
1875 C CB  . GLU A 243 ? 1.3062 0.9355 0.8071 -0.2276 -0.0476 0.1071  539 GLU A CB  
1876 C CG  . GLU A 243 ? 1.2568 0.9856 0.8371 -0.2062 -0.0423 0.1021  539 GLU A CG  
1877 C CD  . GLU A 243 ? 1.3094 1.1008 0.9050 -0.2503 -0.0344 0.1095  539 GLU A CD  
1878 O OE1 . GLU A 243 ? 1.3121 1.1241 0.9042 -0.2966 -0.0323 0.1142  539 GLU A OE1 
1879 O OE2 . GLU A 243 ? 1.2626 1.0873 0.8730 -0.2385 -0.0304 0.1106  539 GLU A OE2 
1880 N N   . LEU A 244 ? 0.9816 0.7859 0.6745 -0.1847 -0.0472 0.0819  540 LEU A N   
1881 C CA  . LEU A 244 ? 0.9190 0.7692 0.6765 -0.1446 -0.0484 0.0702  540 LEU A CA  
1882 C C   . LEU A 244 ? 0.9269 0.7778 0.6990 -0.1510 -0.0508 0.0659  540 LEU A C   
1883 O O   . LEU A 244 ? 0.7796 0.6526 0.5919 -0.1188 -0.0522 0.0570  540 LEU A O   
1884 C CB  . LEU A 244 ? 0.8042 0.7517 0.6375 -0.1373 -0.0434 0.0651  540 LEU A CB  
1885 C CG  . LEU A 244 ? 0.8712 0.8289 0.7055 -0.1177 -0.0417 0.0652  540 LEU A CG  
1886 C CD1 . LEU A 244 ? 0.8012 0.8475 0.7052 -0.1079 -0.0373 0.0584  540 LEU A CD1 
1887 C CD2 . LEU A 244 ? 0.8093 0.7176 0.6195 -0.0769 -0.0475 0.0612  540 LEU A CD2 
1888 N N   . VAL A 245 ? 1.0443 0.8772 0.7860 -0.1941 -0.0512 0.0720  541 VAL A N   
1889 C CA  . VAL A 245 ? 1.0220 0.8581 0.7753 -0.2045 -0.0539 0.0684  541 VAL A CA  
1890 C C   . VAL A 245 ? 1.0643 0.7915 0.7373 -0.2017 -0.0597 0.0701  541 VAL A C   
1891 O O   . VAL A 245 ? 1.1000 0.7609 0.7001 -0.2388 -0.0618 0.0784  541 VAL A O   
1892 C CB  . VAL A 245 ? 1.0064 0.8975 0.7755 -0.2535 -0.0519 0.0733  541 VAL A CB  
1893 C CG1 . VAL A 245 ? 1.0022 0.9020 0.7874 -0.2602 -0.0556 0.0687  541 VAL A CG1 
1894 C CG2 . VAL A 245 ? 1.0040 0.9986 0.8423 -0.2491 -0.0457 0.0718  541 VAL A CG2 
1895 N N   . LEU A 246 ? 1.1013 0.8099 0.7837 -0.1590 -0.0622 0.0622  542 LEU A N   
1896 C CA  . LEU A 246 ? 1.0784 0.6863 0.6846 -0.1436 -0.0673 0.0622  542 LEU A CA  
1897 C C   . LEU A 246 ? 1.1384 0.7287 0.7330 -0.1678 -0.0702 0.0606  542 LEU A C   
1898 O O   . LEU A 246 ? 1.0242 0.6768 0.6828 -0.1578 -0.0690 0.0538  542 LEU A O   
1899 C CB  . LEU A 246 ? 1.0682 0.6754 0.6894 -0.0837 -0.0682 0.0545  542 LEU A CB  
1900 C CG  . LEU A 246 ? 1.2327 0.7549 0.7886 -0.0586 -0.0727 0.0520  542 LEU A CG  
1901 C CD1 . LEU A 246 ? 1.3671 0.7689 0.8093 -0.0647 -0.0769 0.0598  542 LEU A CD1 
1902 C CD2 . LEU A 246 ? 1.1868 0.7391 0.7744 -0.0008 -0.0724 0.0436  542 LEU A CD2 
1903 N N   . GLU A 247 ? 1.2201 0.7185 0.7262 -0.1992 -0.0744 0.0667  543 GLU A N   
1904 C CA  . GLU A 247 ? 1.2569 0.7313 0.7396 -0.2321 -0.0782 0.0661  543 GLU A CA  
1905 C C   . GLU A 247 ? 1.3709 0.7195 0.7558 -0.2137 -0.0838 0.0650  543 GLU A C   
1906 O O   . GLU A 247 ? 1.5312 0.7924 0.8395 -0.1964 -0.0856 0.0688  543 GLU A O   
1907 C CB  . GLU A 247 ? 1.2339 0.7226 0.6972 -0.3011 -0.0786 0.0749  543 GLU A CB  
1908 C CG  . GLU A 247 ? 1.0383 0.6604 0.5979 -0.3170 -0.0730 0.0753  543 GLU A CG  
1909 C CD  . GLU A 247 ? 1.2429 0.8887 0.7804 -0.3844 -0.0731 0.0844  543 GLU A CD  
1910 O OE1 . GLU A 247 ? 1.4528 1.0607 0.9394 -0.4081 -0.0715 0.0928  543 GLU A OE1 
1911 O OE2 . GLU A 247 ? 1.2644 0.9683 0.8321 -0.4149 -0.0748 0.0836  543 GLU A OE2 
1912 N N   . VAL A 248 ? 1.4616 0.7997 0.8458 -0.2141 -0.0867 0.0595  544 VAL A N   
1913 C CA  . VAL A 248 ? 1.5192 0.7443 0.8149 -0.1909 -0.0917 0.0565  544 VAL A CA  
1914 C C   . VAL A 248 ? 1.4359 0.5958 0.6624 -0.2494 -0.0977 0.0600  544 VAL A C   
1915 O O   . VAL A 248 ? 1.4159 0.6425 0.6953 -0.2783 -0.0983 0.0576  544 VAL A O   
1916 C CB  . VAL A 248 ? 1.4717 0.7366 0.8193 -0.1386 -0.0899 0.0462  544 VAL A CB  
1917 C CG1 . VAL A 248 ? 1.5101 0.6617 0.7633 -0.1169 -0.0948 0.0427  544 VAL A CG1 
1918 C CG2 . VAL A 248 ? 1.3255 0.6496 0.7303 -0.0842 -0.0849 0.0428  544 VAL A CG2 
1919 N N   . PRO A 249 ? 1.5253 0.5547 0.6303 -0.2695 -0.1029 0.0656  545 PRO A N   
1920 C CA  . PRO A 249 ? 1.7163 0.6832 0.7495 -0.3194 -0.1094 0.0654  545 PRO A CA  
1921 C C   . PRO A 249 ? 1.7310 0.6503 0.7378 -0.2820 -0.1126 0.0559  545 PRO A C   
1922 O O   . PRO A 249 ? 1.6760 0.5406 0.6521 -0.2190 -0.1117 0.0516  545 PRO A O   
1923 C CB  . PRO A 249 ? 1.7998 0.6768 0.7273 -0.3319 -0.1123 0.0668  545 PRO A CB  
1924 C CG  . PRO A 249 ? 1.7703 0.6041 0.6808 -0.2701 -0.1093 0.0675  545 PRO A CG  
1925 C CD  . PRO A 249 ? 1.6614 0.6054 0.6904 -0.2477 -0.1030 0.0712  545 PRO A CD  
1926 N N   . ILE A 250 ? 1.7794 0.7318 0.8031 -0.3181 -0.1159 0.0528  546 ILE A N   
1927 C CA  . ILE A 250 ? 1.5923 0.5230 0.6117 -0.2887 -0.1179 0.0444  546 ILE A CA  
1928 C C   . ILE A 250 ? 1.7634 0.5905 0.6659 -0.2934 -0.1238 0.0409  546 ILE A C   
1929 O O   . ILE A 250 ? 1.8083 0.6359 0.6791 -0.3485 -0.1285 0.0434  546 ILE A O   
1930 C CB  . ILE A 250 ? 1.4880 0.5183 0.5955 -0.3216 -0.1186 0.0428  546 ILE A CB  
1931 C CG1 . ILE A 250 ? 1.3207 0.4905 0.5552 -0.3088 -0.1112 0.0437  546 ILE A CG1 
1932 C CG2 . ILE A 250 ? 1.5088 0.5141 0.6120 -0.2873 -0.1203 0.0336  546 ILE A CG2 
1933 C CD1 . ILE A 250 ? 1.3327 0.5297 0.6142 -0.2350 -0.1044 0.0382  546 ILE A CD1 
1934 N N   . ARG A 251 ? 1.9060 0.6485 0.7421 -0.2336 -0.1235 0.0351  547 ARG A N   
1935 C CA  . ARG A 251 ? 2.0343 0.6768 0.7586 -0.2276 -0.1288 0.0303  547 ARG A CA  
1936 C C   . ARG A 251 ? 2.0984 0.7326 0.8305 -0.1751 -0.1274 0.0224  547 ARG A C   
1937 O O   . ARG A 251 ? 1.9972 0.6852 0.8038 -0.1287 -0.1219 0.0193  547 ARG A O   
1938 C CB  . ARG A 251 ? 2.0839 0.6230 0.6980 -0.2027 -0.1305 0.0290  547 ARG A CB  
1939 C CG  . ARG A 251 ? 2.1329 0.6578 0.7501 -0.1224 -0.1253 0.0245  547 ARG A CG  
1940 C CD  . ARG A 251 ? 2.0828 0.6704 0.7722 -0.1242 -0.1208 0.0311  547 ARG A CD  
1941 N NE  . ARG A 251 ? 2.0338 0.6160 0.7250 -0.0519 -0.1166 0.0286  547 ARG A NE  
1942 C CZ  . ARG A 251 ? 2.0866 0.7262 0.8430 -0.0428 -0.1127 0.0350  547 ARG A CZ  
1943 N NH1 . ARG A 251 ? 2.1390 0.7813 0.8958 0.0243  -0.1097 0.0328  547 ARG A NH1 
1944 N NH2 . ARG A 251 ? 2.0624 0.7644 0.8838 -0.1008 -0.1119 0.0440  547 ARG A NH2 
1945 N N   . HIS A 252 ? 2.1094 0.6752 0.7590 -0.1837 -0.1326 0.0196  548 HIS A N   
1946 C CA  . HIS A 252 ? 2.1734 0.7143 0.8048 -0.1363 -0.1319 0.0124  548 HIS A CA  
1947 C C   . HIS A 252 ? 2.3840 0.8252 0.9063 -0.0789 -0.1321 0.0080  548 HIS A C   
1948 O O   . HIS A 252 ? 2.4761 0.8352 0.8998 -0.0981 -0.1367 0.0102  548 HIS A O   
1949 C CB  . HIS A 252 ? 2.0984 0.6271 0.7039 -0.1820 -0.1377 0.0134  548 HIS A CB  
1950 C CG  . HIS A 252 ? 2.1197 0.6713 0.7602 -0.1449 -0.1353 0.0068  548 HIS A CG  
1951 N ND1 . HIS A 252 ? 2.2262 0.7010 0.7836 -0.1004 -0.1361 0.0023  548 HIS A ND1 
1952 C CD2 . HIS A 252 ? 1.9666 0.6098 0.7142 -0.1426 -0.1318 0.0034  548 HIS A CD2 
1953 C CE1 . HIS A 252 ? 2.1076 0.6296 0.7227 -0.0735 -0.1326 -0.0033 548 HIS A CE1 
1954 N NE2 . HIS A 252 ? 1.9725 0.5938 0.7014 -0.0987 -0.1302 -0.0034 548 HIS A NE2 
1955 N N   . PRO A 253 ? 2.3538 0.8012 0.8855 -0.0075 -0.1272 0.0014  549 PRO A N   
1956 C CA  . PRO A 253 ? 2.3676 0.7326 0.7968 0.0521  -0.1270 -0.0028 549 PRO A CA  
1957 C C   . PRO A 253 ? 2.4913 0.7552 0.8001 0.0497  -0.1331 -0.0040 549 PRO A C   
1958 O O   . PRO A 253 ? 2.6302 0.8194 0.8426 0.1005  -0.1336 -0.0074 549 PRO A O   
1959 C CB  . PRO A 253 ? 2.1038 0.5413 0.6044 0.1277  -0.1186 -0.0084 549 PRO A CB  
1960 C CG  . PRO A 253 ? 2.0069 0.5507 0.6388 0.1033  -0.1151 -0.0079 549 PRO A CG  
1961 C CD  . PRO A 253 ? 1.9610 0.4933 0.5915 0.0216  -0.1216 -0.0029 549 PRO A CD  
1962 N N   . LYS A 254 ? 2.3684 0.6291 0.6772 -0.0065 -0.1380 -0.0007 550 LYS A N   
1963 C CA  . LYS A 254 ? 2.6102 0.7670 0.7959 -0.0225 -0.1454 0.0008  550 LYS A CA  
1964 C C   . LYS A 254 ? 2.7245 0.8424 0.8607 -0.1069 -0.1534 0.0081  550 LYS A C   
1965 O O   . LYS A 254 ? 2.8250 0.8387 0.8426 -0.1189 -0.1587 0.0095  550 LYS A O   
1966 C CB  . LYS A 254 ? 2.7286 0.9094 0.9423 -0.0098 -0.1447 -0.0013 550 LYS A CB  
1967 C CG  . LYS A 254 ? 2.6947 0.9473 0.9869 0.0629  -0.1357 -0.0081 550 LYS A CG  
1968 C CD  . LYS A 254 ? 2.8312 1.0277 1.0420 0.1412  -0.1331 -0.0118 550 LYS A CD  
1969 C CE  . LYS A 254 ? 2.7428 1.0146 1.0215 0.2086  -0.1247 -0.0175 550 LYS A CE  
1970 N NZ  . LYS A 254 ? 2.8333 1.0855 1.0568 0.2888  -0.1208 -0.0205 550 LYS A NZ  
1971 N N   . PHE A 255 ? 2.6337 0.8429 0.8690 -0.1649 -0.1532 0.0124  551 PHE A N   
1972 C CA  . PHE A 255 ? 2.7014 0.9014 0.9059 -0.2476 -0.1603 0.0200  551 PHE A CA  
1973 C C   . PHE A 255 ? 2.7857 0.9906 0.9832 -0.2877 -0.1611 0.0244  551 PHE A C   
1974 O O   . PHE A 255 ? 2.5970 0.8994 0.9031 -0.2973 -0.1561 0.0258  551 PHE A O   
1975 C CB  . PHE A 255 ? 2.5134 0.8213 0.8302 -0.2848 -0.1595 0.0221  551 PHE A CB  
1976 C CG  . PHE A 255 ? 2.5489 0.8641 0.8880 -0.2435 -0.1577 0.0165  551 PHE A CG  
1977 C CD1 . PHE A 255 ? 2.4379 0.8618 0.9046 -0.2351 -0.1528 0.0126  551 PHE A CD1 
1978 C CD2 . PHE A 255 ? 2.6576 0.8690 0.8853 -0.2138 -0.1611 0.0150  551 PHE A CD2 
1979 C CE1 . PHE A 255 ? 2.4102 0.8410 0.8952 -0.1986 -0.1509 0.0066  551 PHE A CE1 
1980 C CE2 . PHE A 255 ? 2.6860 0.9072 0.9343 -0.1757 -0.1590 0.0101  551 PHE A CE2 
1981 C CZ  . PHE A 255 ? 2.4969 0.8284 0.8744 -0.1689 -0.1538 0.0056  551 PHE A CZ  
1982 N N   . ASP A 256 ? 2.9664 1.0637 1.0315 -0.3125 -0.1675 0.0267  552 ASP A N   
1983 C CA  . ASP A 256 ? 2.9633 1.0537 1.0063 -0.3515 -0.1687 0.0301  552 ASP A CA  
1984 C C   . ASP A 256 ? 2.8248 1.0066 0.9339 -0.4329 -0.1704 0.0385  552 ASP A C   
1985 O O   . ASP A 256 ? 2.8327 1.0656 0.9851 -0.4597 -0.1681 0.0415  552 ASP A O   
1986 C CB  . ASP A 256 ? 3.3172 1.2781 1.2277 -0.3540 -0.1725 0.0290  552 ASP A CB  
1987 C CG  . ASP A 256 ? 3.5137 1.4253 1.3901 -0.3014 -0.1688 0.0236  552 ASP A CG  
1988 O OD1 . ASP A 256 ? 3.6393 1.4716 1.4495 -0.2395 -0.1677 0.0178  552 ASP A OD1 
1989 O OD2 . ASP A 256 ? 3.4971 1.4531 1.4135 -0.3205 -0.1669 0.0252  552 ASP A OD2 
1990 N N   . TRP A 257 ? 2.8486 1.0539 0.9628 -0.4722 -0.1742 0.0427  553 TRP A N   
1991 C CA  . TRP A 257 ? 2.7136 1.0278 0.9045 -0.5422 -0.1748 0.0505  553 TRP A CA  
1992 C C   . TRP A 257 ? 2.4842 0.9384 0.8341 -0.5284 -0.1669 0.0497  553 TRP A C   
1993 O O   . TRP A 257 ? 2.4151 0.9683 0.8324 -0.5792 -0.1660 0.0559  553 TRP A O   
1994 C CB  . TRP A 257 ? 2.6893 1.0106 0.8650 -0.5775 -0.1796 0.0544  553 TRP A CB  
1995 C CG  . TRP A 257 ? 2.7063 1.0314 0.9217 -0.5241 -0.1774 0.0483  553 TRP A CG  
1996 C CD1 . TRP A 257 ? 2.8052 1.0213 0.9252 -0.4860 -0.1805 0.0446  553 TRP A CD1 
1997 C CD2 . TRP A 257 ? 2.4959 0.9386 0.8516 -0.5028 -0.1718 0.0447  553 TRP A CD2 
1998 N NE1 . TRP A 257 ? 2.7552 1.0174 0.9503 -0.4430 -0.1767 0.0391  553 TRP A NE1 
1999 C CE2 . TRP A 257 ? 2.5661 0.9640 0.9039 -0.4538 -0.1717 0.0385  553 TRP A CE2 
2000 C CE3 . TRP A 257 ? 2.2745 0.8539 0.7638 -0.5196 -0.1671 0.0459  553 TRP A CE3 
2001 C CZ2 . TRP A 257 ? 2.3939 0.8766 0.8413 -0.4243 -0.1672 0.0327  553 TRP A CZ2 
2002 C CZ3 . TRP A 257 ? 2.1842 0.8435 0.7786 -0.4894 -0.1631 0.0403  553 TRP A CZ3 
2003 C CH2 . TRP A 257 ? 2.1444 0.7541 0.7170 -0.4436 -0.1634 0.0334  553 TRP A CH2 
2004 N N   . PHE A 258 ? 2.3058 0.7724 0.7130 -0.4608 -0.1612 0.0426  554 PHE A N   
2005 C CA  . PHE A 258 ? 2.2774 0.8680 0.8276 -0.4470 -0.1542 0.0418  554 PHE A CA  
2006 C C   . PHE A 258 ? 2.2453 0.8770 0.8284 -0.4644 -0.1508 0.0461  554 PHE A C   
2007 O O   . PHE A 258 ? 2.1571 0.9055 0.8485 -0.4849 -0.1468 0.0495  554 PHE A O   
2008 C CB  . PHE A 258 ? 2.2898 0.8739 0.8791 -0.3707 -0.1490 0.0334  554 PHE A CB  
2009 C CG  . PHE A 258 ? 2.1139 0.8173 0.8390 -0.3627 -0.1441 0.0315  554 PHE A CG  
2010 C CD1 . PHE A 258 ? 2.0723 0.8139 0.8347 -0.3689 -0.1458 0.0287  554 PHE A CD1 
2011 C CD2 . PHE A 258 ? 2.0331 0.8082 0.8446 -0.3505 -0.1382 0.0326  554 PHE A CD2 
2012 C CE1 . PHE A 258 ? 1.8891 0.7365 0.7695 -0.3624 -0.1422 0.0256  554 PHE A CE1 
2013 C CE2 . PHE A 258 ? 1.9147 0.7953 0.8442 -0.3449 -0.1345 0.0304  554 PHE A CE2 
2014 C CZ  . PHE A 258 ? 1.8633 0.7791 0.8258 -0.3506 -0.1367 0.0262  554 PHE A CZ  
2015 N N   . LYS A 259 ? 2.3141 0.8523 0.8039 -0.4542 -0.1522 0.0455  555 LYS A N   
2016 C CA  . LYS A 259 ? 2.4388 1.0075 0.9475 -0.4763 -0.1497 0.0499  555 LYS A CA  
2017 C C   . LYS A 259 ? 2.4391 1.0871 0.9749 -0.5534 -0.1517 0.0582  555 LYS A C   
2018 O O   . LYS A 259 ? 2.2080 0.9520 0.8266 -0.5722 -0.1470 0.0627  555 LYS A O   
2019 C CB  . LYS A 259 ? 2.6400 1.0811 1.0218 -0.4615 -0.1528 0.0471  555 LYS A CB  
2020 C CG  . LYS A 259 ? 2.7142 1.0807 1.0597 -0.3803 -0.1503 0.0390  555 LYS A CG  
2021 C CD  . LYS A 259 ? 2.9188 1.1394 1.1067 -0.3698 -0.1561 0.0346  555 LYS A CD  
2022 C CE  . LYS A 259 ? 2.9466 1.1115 1.1064 -0.2821 -0.1526 0.0264  555 LYS A CE  
2023 N NZ  . LYS A 259 ? 2.7760 1.0225 1.0421 -0.2385 -0.1470 0.0243  555 LYS A NZ  
2024 N N   . ASP A 260 ? 2.4697 1.0798 0.9316 -0.5976 -0.1586 0.0607  556 ASP A N   
2025 C CA  . ASP A 260 ? 2.5292 1.2093 0.9993 -0.6716 -0.1611 0.0688  556 ASP A CA  
2026 C C   . ASP A 260 ? 2.3335 1.1678 0.9401 -0.6852 -0.1566 0.0720  556 ASP A C   
2027 O O   . ASP A 260 ? 2.4029 1.3284 1.0445 -0.7367 -0.1562 0.0788  556 ASP A O   
2028 C CB  . ASP A 260 ? 2.7094 1.3004 1.0546 -0.7144 -0.1699 0.0713  556 ASP A CB  
2029 C CG  . ASP A 260 ? 2.8381 1.2658 1.0362 -0.6956 -0.1748 0.0667  556 ASP A CG  
2030 O OD1 . ASP A 260 ? 2.8561 1.2530 1.0440 -0.6700 -0.1720 0.0636  556 ASP A OD1 
2031 O OD2 . ASP A 260 ? 2.9498 1.2788 1.0400 -0.7044 -0.1815 0.0663  556 ASP A OD2 
2032 N N   . LEU A 261 ? 2.1852 1.0526 0.8670 -0.6381 -0.1533 0.0667  557 LEU A N   
2033 C CA  . LEU A 261 ? 2.1766 1.1899 0.9912 -0.6428 -0.1487 0.0680  557 LEU A CA  
2034 C C   . LEU A 261 ? 2.2094 1.3077 1.1019 -0.6421 -0.1421 0.0710  557 LEU A C   
2035 O O   . LEU A 261 ? 2.2051 1.4331 1.1925 -0.6603 -0.1386 0.0742  557 LEU A O   
2036 C CB  . LEU A 261 ? 2.0458 1.0660 0.9166 -0.5911 -0.1471 0.0602  557 LEU A CB  
2037 C CG  . LEU A 261 ? 2.1194 1.0890 0.9387 -0.5948 -0.1529 0.0577  557 LEU A CG  
2038 C CD1 . LEU A 261 ? 1.9052 0.8804 0.7787 -0.5407 -0.1510 0.0487  557 LEU A CD1 
2039 C CD2 . LEU A 261 ? 2.2291 1.2823 1.0697 -0.6539 -0.1559 0.0643  557 LEU A CD2 
2040 N N   . GLY A 262 ? 2.2938 1.3215 1.1436 -0.6202 -0.1403 0.0702  558 GLY A N   
2041 C CA  . GLY A 262 ? 2.2646 1.3591 1.1695 -0.6262 -0.1345 0.0745  558 GLY A CA  
2042 C C   . GLY A 262 ? 2.0903 1.2948 1.1248 -0.5955 -0.1274 0.0734  558 GLY A C   
2043 O O   . GLY A 262 ? 2.0511 1.3576 1.1544 -0.6137 -0.1226 0.0783  558 GLY A O   
2044 N N   . LEU A 263 ? 1.9759 1.1630 1.0422 -0.5491 -0.1268 0.0668  559 LEU A N   
2045 C CA  . LEU A 263 ? 1.7743 1.0578 0.9561 -0.5210 -0.1213 0.0645  559 LEU A CA  
2046 C C   . LEU A 263 ? 1.7436 0.9900 0.9340 -0.4785 -0.1163 0.0644  559 LEU A C   
2047 O O   . LEU A 263 ? 1.8299 0.9642 0.9374 -0.4528 -0.1175 0.0634  559 LEU A O   
2048 C CB  . LEU A 263 ? 1.6412 0.9301 0.8540 -0.4954 -0.1237 0.0568  559 LEU A CB  
2049 C CG  . LEU A 263 ? 1.7250 1.0369 0.9223 -0.5300 -0.1292 0.0569  559 LEU A CG  
2050 C CD1 . LEU A 263 ? 1.6323 0.8878 0.8142 -0.4948 -0.1321 0.0485  559 LEU A CD1 
2051 C CD2 . LEU A 263 ? 1.7397 1.1998 1.0339 -0.5555 -0.1273 0.0597  559 LEU A CD2 
2052 N N   . LYS A 264 ? 1.6175 0.9617 0.9069 -0.4686 -0.1109 0.0656  560 LYS A N   
2053 C CA  . LYS A 264 ? 1.5225 0.8613 0.8403 -0.4165 -0.1049 0.0648  560 LYS A CA  
2054 C C   . LYS A 264 ? 1.3082 0.7790 0.7501 -0.3815 -0.0991 0.0590  560 LYS A C   
2055 O O   . LYS A 264 ? 1.2797 0.8369 0.7772 -0.4062 -0.1002 0.0581  560 LYS A O   
2056 C CB  . LYS A 264 ? 1.5621 0.8903 0.8548 -0.4358 -0.1015 0.0738  560 LYS A CB  
2057 C CG  . LYS A 264 ? 1.5816 1.0178 0.9251 -0.4900 -0.0989 0.0805  560 LYS A CG  
2058 C CD  . LYS A 264 ? 1.6758 1.1020 0.9976 -0.4985 -0.0941 0.0886  560 LYS A CD  
2059 C CE  . LYS A 264 ? 1.6589 1.1744 0.9972 -0.5493 -0.0923 0.0935  560 LYS A CE  
2060 N NZ  . LYS A 264 ? 1.5478 1.0664 0.8771 -0.5551 -0.0866 0.1009  560 LYS A NZ  
2061 N N   . TRP A 265 ? 1.1841 0.6673 0.6635 -0.3234 -0.0936 0.0550  561 TRP A N   
2062 C CA  . TRP A 265 ? 1.1224 0.7207 0.7098 -0.2927 -0.0879 0.0502  561 TRP A CA  
2063 C C   . TRP A 265 ? 1.1342 0.7468 0.7451 -0.2568 -0.0822 0.0508  561 TRP A C   
2064 O O   . TRP A 265 ? 1.2042 0.7349 0.7506 -0.2417 -0.0830 0.0531  561 TRP A O   
2065 C CB  . TRP A 265 ? 1.0242 0.6331 0.6437 -0.2561 -0.0881 0.0414  561 TRP A CB  
2066 C CG  . TRP A 265 ? 0.8640 0.5882 0.5828 -0.2454 -0.0843 0.0379  561 TRP A CG  
2067 C CD1 . TRP A 265 ? 0.8873 0.6605 0.6680 -0.2012 -0.0789 0.0325  561 TRP A CD1 
2068 C CD2 . TRP A 265 ? 0.9621 0.7631 0.7212 -0.2799 -0.0861 0.0398  561 TRP A CD2 
2069 N NE1 . TRP A 265 ? 0.9549 0.8178 0.8053 -0.2050 -0.0773 0.0308  561 TRP A NE1 
2070 C CE2 . TRP A 265 ? 0.9972 0.8820 0.8373 -0.2494 -0.0816 0.0352  561 TRP A CE2 
2071 C CE3 . TRP A 265 ? 0.9746 0.7834 0.7056 -0.3342 -0.0915 0.0449  561 TRP A CE3 
2072 C CZ2 . TRP A 265 ? 0.8792 0.8510 0.7702 -0.2644 -0.0824 0.0356  561 TRP A CZ2 
2073 C CZ3 . TRP A 265 ? 0.9604 0.8694 0.7496 -0.3510 -0.0922 0.0454  561 TRP A CZ3 
2074 C CH2 . TRP A 265 ? 0.7968 0.7844 0.6641 -0.3126 -0.0877 0.0407  561 TRP A CH2 
2075 N N   . TYR A 266 ? 0.9769 0.6916 0.6753 -0.2428 -0.0771 0.0486  562 TYR A N   
2076 C CA  . TYR A 266 ? 0.9428 0.6824 0.6718 -0.2092 -0.0721 0.0478  562 TYR A CA  
2077 C C   . TYR A 266 ? 0.9644 0.7053 0.7211 -0.1562 -0.0706 0.0394  562 TYR A C   
2078 O O   . TYR A 266 ? 1.0150 0.7782 0.8010 -0.1459 -0.0709 0.0339  562 TYR A O   
2079 C CB  . TYR A 266 ? 0.7026 0.5454 0.5035 -0.2202 -0.0676 0.0490  562 TYR A CB  
2080 C CG  . TYR A 266 ? 0.7501 0.6694 0.6165 -0.2168 -0.0671 0.0439  562 TYR A CG  
2081 C CD1 . TYR A 266 ? 0.8192 0.7728 0.7377 -0.1765 -0.0644 0.0363  562 TYR A CD1 
2082 C CD2 . TYR A 266 ? 0.6442 0.6024 0.5163 -0.2550 -0.0697 0.0469  562 TYR A CD2 
2083 C CE1 . TYR A 266 ? 0.7969 0.8094 0.7654 -0.1724 -0.0641 0.0323  562 TYR A CE1 
2084 C CE2 . TYR A 266 ? 0.6153 0.6419 0.5430 -0.2466 -0.0698 0.0425  562 TYR A CE2 
2085 C CZ  . TYR A 266 ? 0.6902 0.7376 0.6625 -0.2046 -0.0669 0.0354  562 TYR A CZ  
2086 O OH  . TYR A 266 ? 0.8159 0.9198 0.8331 -0.1960 -0.0673 0.0317  562 TYR A OH  
2087 N N   . GLY A 267 ? 0.8630 0.5834 0.6084 -0.1237 -0.0690 0.0389  563 GLY A N   
2088 C CA  . GLY A 267 ? 0.8886 0.6134 0.6527 -0.0756 -0.0678 0.0316  563 GLY A CA  
2089 C C   . GLY A 267 ? 0.9711 0.7873 0.8213 -0.0602 -0.0636 0.0256  563 GLY A C   
2090 O O   . GLY A 267 ? 1.0652 0.8946 0.9354 -0.0313 -0.0626 0.0194  563 GLY A O   
2091 N N   . LEU A 268 ? 0.7323 0.6096 0.6284 -0.0790 -0.0612 0.0272  564 LEU A N   
2092 C CA  . LEU A 268 ? 0.7469 0.6943 0.7091 -0.0604 -0.0577 0.0217  564 LEU A CA  
2093 C C   . LEU A 268 ? 0.7661 0.7648 0.7735 -0.0735 -0.0566 0.0193  564 LEU A C   
2094 O O   . LEU A 268 ? 0.6663 0.6983 0.6871 -0.0971 -0.0561 0.0230  564 LEU A O   
2095 C CB  . LEU A 268 ? 0.6975 0.6721 0.6733 -0.0606 -0.0556 0.0239  564 LEU A CB  
2096 C CG  . LEU A 268 ? 0.6587 0.6889 0.6869 -0.0392 -0.0529 0.0176  564 LEU A CG  
2097 C CD1 . LEU A 268 ? 0.7336 0.7539 0.7574 -0.0074 -0.0539 0.0130  564 LEU A CD1 
2098 C CD2 . LEU A 268 ? 0.5480 0.6102 0.5904 -0.0486 -0.0507 0.0201  564 LEU A CD2 
2099 N N   . PRO A 269 ? 0.7346 0.7447 0.7646 -0.0575 -0.0560 0.0137  565 PRO A N   
2100 C CA  . PRO A 269 ? 0.5621 0.6185 0.6326 -0.0641 -0.0551 0.0113  565 PRO A CA  
2101 C C   . PRO A 269 ? 0.4448 0.5478 0.5564 -0.0507 -0.0519 0.0077  565 PRO A C   
2102 O O   . PRO A 269 ? 0.5211 0.6264 0.6434 -0.0313 -0.0504 0.0031  565 PRO A O   
2103 C CB  . PRO A 269 ? 0.6914 0.7294 0.7585 -0.0522 -0.0555 0.0073  565 PRO A CB  
2104 C CG  . PRO A 269 ? 0.7475 0.7605 0.7975 -0.0274 -0.0544 0.0048  565 PRO A CG  
2105 C CD  . PRO A 269 ? 0.7803 0.7644 0.7971 -0.0306 -0.0559 0.0094  565 PRO A CD  
2106 N N   . ALA A 270 ? 0.4352 0.5763 0.5652 -0.0616 -0.0511 0.0097  566 ALA A N   
2107 C CA  . ALA A 270 ? 0.4532 0.6287 0.6106 -0.0485 -0.0483 0.0062  566 ALA A CA  
2108 C C   . ALA A 270 ? 0.4855 0.7018 0.6647 -0.0499 -0.0478 0.0057  566 ALA A C   
2109 O O   . ALA A 270 ? 0.5231 0.7702 0.7039 -0.0612 -0.0473 0.0099  566 ALA A O   
2110 C CB  . ALA A 270 ? 0.3550 0.5320 0.5019 -0.0512 -0.0472 0.0093  566 ALA A CB  
2111 N N   . VAL A 271 ? 0.4196 0.6377 0.6123 -0.0374 -0.0477 0.0009  567 VAL A N   
2112 C CA  . VAL A 271 ? 0.4242 0.6729 0.6297 -0.0318 -0.0479 0.0002  567 VAL A CA  
2113 C C   . VAL A 271 ? 0.3938 0.6637 0.6074 -0.0169 -0.0455 -0.0027 567 VAL A C   
2114 O O   . VAL A 271 ? 0.7334 0.9854 0.9462 -0.0078 -0.0442 -0.0073 567 VAL A O   
2115 C CB  . VAL A 271 ? 0.4185 0.6501 0.6255 -0.0240 -0.0488 -0.0032 567 VAL A CB  
2116 C CG1 . VAL A 271 ? 0.4875 0.7383 0.7002 -0.0077 -0.0487 -0.0056 567 VAL A CG1 
2117 C CG2 . VAL A 271 ? 0.4052 0.6273 0.6033 -0.0381 -0.0517 0.0002  567 VAL A CG2 
2118 N N   . SER A 272 ? 0.4563 0.7676 0.6754 -0.0145 -0.0450 -0.0002 568 SER A N   
2119 C CA  . SER A 272 ? 0.5831 0.9174 0.8046 0.0013  -0.0422 -0.0024 568 SER A CA  
2120 C C   . SER A 272 ? 0.6030 0.9584 0.8242 0.0253  -0.0423 -0.0054 568 SER A C   
2121 O O   . SER A 272 ? 0.6108 0.9805 0.8273 0.0441  -0.0400 -0.0082 568 SER A O   
2122 C CB  . SER A 272 ? 0.6246 0.9962 0.8476 -0.0134 -0.0403 0.0035  568 SER A CB  
2123 O OG  . SER A 272 ? 0.5514 0.9501 0.7756 -0.0342 -0.0423 0.0096  568 SER A OG  
2124 N N   . ASN A 273 ? 0.5478 0.9025 0.7686 0.0283  -0.0452 -0.0049 569 ASN A N   
2125 C CA  . ASN A 273 ? 0.5340 0.9159 0.7502 0.0538  -0.0461 -0.0060 569 ASN A CA  
2126 C C   . ASN A 273 ? 0.5817 0.9127 0.7779 0.0734  -0.0473 -0.0115 569 ASN A C   
2127 O O   . ASN A 273 ? 0.7497 1.0911 0.9340 0.0972  -0.0491 -0.0121 569 ASN A O   
2128 C CB  . ASN A 273 ? 0.6149 1.0464 0.8419 0.0443  -0.0492 -0.0005 569 ASN A CB  
2129 C CG  . ASN A 273 ? 0.4941 0.8932 0.7204 0.0241  -0.0527 0.0009  569 ASN A CG  
2130 O OD1 . ASN A 273 ? 0.4818 0.8255 0.7005 0.0221  -0.0523 -0.0023 569 ASN A OD1 
2131 N ND2 . ASN A 273 ? 0.5349 0.9736 0.7679 0.0081  -0.0563 0.0057  569 ASN A ND2 
2132 N N   . MET A 274 ? 0.4902 0.7686 0.6787 0.0643  -0.0466 -0.0151 570 MET A N   
2133 C CA  . MET A 274 ? 0.5647 0.7915 0.7292 0.0741  -0.0474 -0.0196 570 MET A CA  
2134 C C   . MET A 274 ? 0.5920 0.7847 0.7325 0.0859  -0.0460 -0.0257 570 MET A C   
2135 O O   . MET A 274 ? 0.6785 0.8871 0.8253 0.0855  -0.0443 -0.0269 570 MET A O   
2136 C CB  . MET A 274 ? 0.7017 0.8999 0.8720 0.0514  -0.0476 -0.0192 570 MET A CB  
2137 C CG  . MET A 274 ? 0.7197 0.9403 0.9040 0.0414  -0.0496 -0.0141 570 MET A CG  
2138 S SD  . MET A 274 ? 0.5306 0.7142 0.7134 0.0239  -0.0491 -0.0146 570 MET A SD  
2139 C CE  . MET A 274 ? 0.4537 0.5981 0.6068 0.0393  -0.0496 -0.0173 570 MET A CE  
2140 N N   . LEU A 275 ? 0.5158 0.6560 0.6227 0.0947  -0.0471 -0.0295 571 LEU A N   
2141 C CA  . LEU A 275 ? 0.6399 0.7338 0.7086 0.1063  -0.0470 -0.0359 571 LEU A CA  
2142 C C   . LEU A 275 ? 0.7300 0.7778 0.7869 0.0790  -0.0470 -0.0393 571 LEU A C   
2143 O O   . LEU A 275 ? 0.6850 0.7129 0.7383 0.0660  -0.0473 -0.0377 571 LEU A O   
2144 C CB  . LEU A 275 ? 0.7386 0.8006 0.7631 0.1394  -0.0488 -0.0376 571 LEU A CB  
2145 C CG  . LEU A 275 ? 0.8908 0.9088 0.8672 0.1624  -0.0490 -0.0441 571 LEU A CG  
2146 C CD1 . LEU A 275 ? 0.9154 0.9432 0.8637 0.2090  -0.0500 -0.0440 571 LEU A CD1 
2147 C CD2 . LEU A 275 ? 0.9717 0.9036 0.8990 0.1457  -0.0505 -0.0492 571 LEU A CD2 
2148 N N   . LEU A 276 ? 0.7153 0.7512 0.7653 0.0696  -0.0468 -0.0440 572 LEU A N   
2149 C CA  . LEU A 276 ? 0.6523 0.6582 0.6923 0.0409  -0.0473 -0.0476 572 LEU A CA  
2150 C C   . LEU A 276 ? 0.8035 0.7388 0.7826 0.0428  -0.0492 -0.0536 572 LEU A C   
2151 O O   . LEU A 276 ? 0.9139 0.8304 0.8674 0.0544  -0.0503 -0.0586 572 LEU A O   
2152 C CB  . LEU A 276 ? 0.6137 0.6535 0.6816 0.0271  -0.0470 -0.0490 572 LEU A CB  
2153 C CG  . LEU A 276 ? 0.6538 0.6786 0.7124 -0.0002 -0.0484 -0.0538 572 LEU A CG  
2154 C CD1 . LEU A 276 ? 0.5777 0.6002 0.6416 -0.0226 -0.0475 -0.0521 572 LEU A CD1 
2155 C CD2 . LEU A 276 ? 0.6343 0.7032 0.7245 -0.0053 -0.0487 -0.0538 572 LEU A CD2 
2156 N N   . GLU A 277 ? 0.9025 0.7932 0.8520 0.0300  -0.0497 -0.0534 573 GLU A N   
2157 C CA  . GLU A 277 ? 0.9465 0.7561 0.8261 0.0252  -0.0519 -0.0586 573 GLU A CA  
2158 C C   . GLU A 277 ? 0.9089 0.7078 0.7821 -0.0183 -0.0525 -0.0623 573 GLU A C   
2159 O O   . GLU A 277 ? 0.7800 0.6088 0.6826 -0.0448 -0.0506 -0.0593 573 GLU A O   
2160 C CB  . GLU A 277 ? 1.0727 0.8310 0.9116 0.0343  -0.0523 -0.0557 573 GLU A CB  
2161 C CG  . GLU A 277 ? 1.2480 0.9373 1.0168 0.0699  -0.0549 -0.0589 573 GLU A CG  
2162 C CD  . GLU A 277 ? 1.4322 1.0372 1.1331 0.0666  -0.0564 -0.0579 573 GLU A CD  
2163 O OE1 . GLU A 277 ? 1.4844 1.0468 1.1574 0.0248  -0.0563 -0.0593 573 GLU A OE1 
2164 O OE2 . GLU A 277 ? 1.4689 1.0528 1.1421 0.1053  -0.0577 -0.0554 573 GLU A OE2 
2165 N N   . ILE A 278 ? 0.9512 0.7141 0.7866 -0.0249 -0.0554 -0.0691 574 ILE A N   
2166 C CA  . ILE A 278 ? 0.8905 0.6430 0.7113 -0.0687 -0.0573 -0.0735 574 ILE A CA  
2167 C C   . ILE A 278 ? 1.0189 0.6734 0.7511 -0.0750 -0.0612 -0.0800 574 ILE A C   
2168 O O   . ILE A 278 ? 1.1476 0.7712 0.8492 -0.0458 -0.0632 -0.0844 574 ILE A O   
2169 C CB  . ILE A 278 ? 0.9864 0.8040 0.8542 -0.0763 -0.0583 -0.0759 574 ILE A CB  
2170 C CG1 . ILE A 278 ? 0.8955 0.7972 0.8391 -0.0672 -0.0549 -0.0695 574 ILE A CG1 
2171 C CG2 . ILE A 278 ? 1.0435 0.8581 0.8943 -0.1220 -0.0612 -0.0806 574 ILE A CG2 
2172 C CD1 . ILE A 278 ? 0.7205 0.6770 0.7017 -0.0666 -0.0561 -0.0710 574 ILE A CD1 
2173 N N   . GLY A 279 ? 1.0542 0.6575 0.7400 -0.1134 -0.0622 -0.0807 575 GLY A N   
2174 C CA  . GLY A 279 ? 1.1535 0.6501 0.7421 -0.1271 -0.0667 -0.0871 575 GLY A CA  
2175 C C   . GLY A 279 ? 1.2293 0.6528 0.7596 -0.0749 -0.0680 -0.0889 575 GLY A C   
2176 O O   . GLY A 279 ? 1.3892 0.7463 0.8554 -0.0661 -0.0720 -0.0962 575 GLY A O   
2177 N N   . GLY A 280 ? 1.2089 0.6486 0.7603 -0.0371 -0.0650 -0.0827 576 GLY A N   
2178 C CA  . GLY A 280 ? 1.3110 0.6972 0.8118 0.0183  -0.0662 -0.0837 576 GLY A CA  
2179 C C   . GLY A 280 ? 1.2498 0.6925 0.7881 0.0606  -0.0653 -0.0859 576 GLY A C   
2180 O O   . GLY A 280 ? 1.3962 0.8092 0.8961 0.1118  -0.0658 -0.0870 576 GLY A O   
2181 N N   . LEU A 281 ? 1.1847 0.7093 0.7933 0.0428  -0.0640 -0.0864 577 LEU A N   
2182 C CA  . LEU A 281 ? 1.1532 0.7396 0.8026 0.0791  -0.0621 -0.0869 577 LEU A CA  
2183 C C   . LEU A 281 ? 1.0475 0.7286 0.7795 0.0920  -0.0581 -0.0783 577 LEU A C   
2184 O O   . LEU A 281 ? 1.0797 0.7961 0.8554 0.0633  -0.0568 -0.0733 577 LEU A O   
2185 C CB  . LEU A 281 ? 1.0840 0.6977 0.7534 0.0551  -0.0635 -0.0921 577 LEU A CB  
2186 C CG  . LEU A 281 ? 1.1172 0.6391 0.7033 0.0355  -0.0686 -0.1014 577 LEU A CG  
2187 C CD1 . LEU A 281 ? 1.0873 0.6493 0.7017 0.0065  -0.0708 -0.1061 577 LEU A CD1 
2188 C CD2 . LEU A 281 ? 1.3679 0.8161 0.8774 0.0844  -0.0697 -0.1064 577 LEU A CD2 
2189 N N   . GLU A 282 ? 0.9722 0.6938 0.7205 0.1352  -0.0561 -0.0767 578 GLU A N   
2190 C CA  . GLU A 282 ? 0.9043 0.7077 0.7167 0.1496  -0.0531 -0.0687 578 GLU A CA  
2191 C C   . GLU A 282 ? 0.8784 0.7617 0.7467 0.1532  -0.0504 -0.0672 578 GLU A C   
2192 O O   . GLU A 282 ? 0.8801 0.7691 0.7300 0.1827  -0.0494 -0.0705 578 GLU A O   
2193 C CB  . GLU A 282 ? 0.9470 0.7377 0.7268 0.1963  -0.0535 -0.0669 578 GLU A CB  
2194 C CG  . GLU A 282 ? 1.1317 0.8198 0.8302 0.2031  -0.0568 -0.0697 578 GLU A CG  
2195 C CD  . GLU A 282 ? 1.3006 0.9904 0.9785 0.2487  -0.0576 -0.0659 578 GLU A CD  
2196 O OE1 . GLU A 282 ? 1.2898 1.0160 0.9646 0.2943  -0.0567 -0.0667 578 GLU A OE1 
2197 O OE2 . GLU A 282 ? 1.2942 0.9555 0.9599 0.2394  -0.0590 -0.0619 578 GLU A OE2 
2198 N N   . PHE A 283 ? 0.8137 0.7546 0.7439 0.1248  -0.0489 -0.0622 579 PHE A N   
2199 C CA  . PHE A 283 ? 0.6681 0.6783 0.6471 0.1235  -0.0464 -0.0594 579 PHE A CA  
2200 C C   . PHE A 283 ? 0.6064 0.6793 0.6254 0.1352  -0.0442 -0.0515 579 PHE A C   
2201 O O   . PHE A 283 ? 0.7325 0.8230 0.7812 0.1158  -0.0445 -0.0466 579 PHE A O   
2202 C CB  . PHE A 283 ? 0.7510 0.7751 0.7602 0.0870  -0.0472 -0.0595 579 PHE A CB  
2203 C CG  . PHE A 283 ? 0.8408 0.8141 0.8120 0.0708  -0.0503 -0.0674 579 PHE A CG  
2204 C CD1 . PHE A 283 ? 0.8684 0.7958 0.8142 0.0453  -0.0528 -0.0701 579 PHE A CD1 
2205 C CD2 . PHE A 283 ? 0.8939 0.8658 0.8510 0.0787  -0.0508 -0.0723 579 PHE A CD2 
2206 C CE1 . PHE A 283 ? 0.8835 0.7670 0.7907 0.0238  -0.0563 -0.0774 579 PHE A CE1 
2207 C CE2 . PHE A 283 ? 0.8998 0.8241 0.8178 0.0605  -0.0547 -0.0802 579 PHE A CE2 
2208 C CZ  . PHE A 283 ? 0.9798 0.8604 0.8723 0.0313  -0.0578 -0.0828 579 PHE A CZ  
2209 N N   . SER A 284 ? 0.6329 0.7414 0.6491 0.1668  -0.0422 -0.0505 580 SER A N   
2210 C CA  . SER A 284 ? 0.5192 0.6924 0.5677 0.1765  -0.0410 -0.0433 580 SER A CA  
2211 C C   . SER A 284 ? 0.5899 0.8232 0.6903 0.1485  -0.0390 -0.0367 580 SER A C   
2212 O O   . SER A 284 ? 0.5004 0.7820 0.6272 0.1440  -0.0389 -0.0304 580 SER A O   
2213 C CB  . SER A 284 ? 0.4737 0.6787 0.5029 0.2191  -0.0391 -0.0443 580 SER A CB  
2214 O OG  . SER A 284 ? 0.7897 0.9727 0.7932 0.2307  -0.0374 -0.0503 580 SER A OG  
2215 N N   . ALA A 285 ? 0.5603 0.7888 0.6698 0.1301  -0.0380 -0.0382 581 ALA A N   
2216 C CA  . ALA A 285 ? 0.5075 0.7785 0.6530 0.1063  -0.0364 -0.0322 581 ALA A CA  
2217 C C   . ALA A 285 ? 0.5134 0.7489 0.6633 0.0815  -0.0385 -0.0341 581 ALA A C   
2218 O O   . ALA A 285 ? 0.5764 0.7853 0.7108 0.0805  -0.0393 -0.0397 581 ALA A O   
2219 C CB  . ALA A 285 ? 0.4308 0.7392 0.5786 0.1152  -0.0327 -0.0315 581 ALA A CB  
2220 N N   . CYS A 286 ? 0.5716 0.8093 0.7400 0.0630  -0.0396 -0.0299 582 CYS A N   
2221 C CA  . CYS A 286 ? 0.4334 0.6455 0.6048 0.0449  -0.0414 -0.0320 582 CYS A CA  
2222 C C   . CYS A 286 ? 0.4973 0.7240 0.6895 0.0286  -0.0416 -0.0259 582 CYS A C   
2223 O O   . CYS A 286 ? 0.5723 0.7819 0.7666 0.0198  -0.0428 -0.0265 582 CYS A O   
2224 C CB  . CYS A 286 ? 0.6379 0.8087 0.7896 0.0438  -0.0432 -0.0371 582 CYS A CB  
2225 S SG  . CYS A 286 ? 0.5154 0.6833 0.6661 0.0503  -0.0434 -0.0333 582 CYS A SG  
2226 N N   . PRO A 287 ? 0.4854 0.7390 0.6872 0.0234  -0.0404 -0.0201 583 PRO A N   
2227 C CA  . PRO A 287 ? 0.2663 0.5202 0.4747 0.0082  -0.0412 -0.0143 583 PRO A CA  
2228 C C   . PRO A 287 ? 0.4237 0.6534 0.6308 0.0033  -0.0428 -0.0165 583 PRO A C   
2229 O O   . PRO A 287 ? 0.5106 0.7367 0.7152 0.0057  -0.0434 -0.0197 583 PRO A O   
2230 C CB  . PRO A 287 ? 0.2890 0.5644 0.4961 0.0008  -0.0397 -0.0086 583 PRO A CB  
2231 C CG  . PRO A 287 ? 0.3130 0.5936 0.5164 0.0125  -0.0382 -0.0129 583 PRO A CG  
2232 C CD  . PRO A 287 ? 0.3517 0.6288 0.5517 0.0286  -0.0382 -0.0189 583 PRO A CD  
2233 N N   . PHE A 288 ? 0.5066 0.7246 0.7144 -0.0022 -0.0437 -0.0149 584 PHE A N   
2234 C CA  . PHE A 288 ? 0.5086 0.7124 0.7152 -0.0030 -0.0445 -0.0170 584 PHE A CA  
2235 C C   . PHE A 288 ? 0.5553 0.7462 0.7529 -0.0078 -0.0452 -0.0119 584 PHE A C   
2236 O O   . PHE A 288 ? 0.4795 0.6687 0.6739 -0.0153 -0.0457 -0.0081 584 PHE A O   
2237 C CB  . PHE A 288 ? 0.5460 0.7424 0.7552 -0.0029 -0.0440 -0.0218 584 PHE A CB  
2238 C CG  . PHE A 288 ? 0.5952 0.7849 0.8036 -0.0042 -0.0438 -0.0199 584 PHE A CG  
2239 C CD1 . PHE A 288 ? 0.5351 0.7184 0.7420 -0.0086 -0.0442 -0.0165 584 PHE A CD1 
2240 C CD2 . PHE A 288 ? 0.5563 0.7413 0.7594 0.0011  -0.0437 -0.0221 584 PHE A CD2 
2241 C CE1 . PHE A 288 ? 0.4109 0.5903 0.6165 -0.0102 -0.0447 -0.0149 584 PHE A CE1 
2242 C CE2 . PHE A 288 ? 0.3494 0.5297 0.5496 0.0027  -0.0442 -0.0201 584 PHE A CE2 
2243 C CZ  . PHE A 288 ? 0.4264 0.6069 0.6304 -0.0042 -0.0448 -0.0166 584 PHE A CZ  
2244 N N   . SER A 289 ? 0.5771 0.7582 0.7659 -0.0024 -0.0460 -0.0121 585 SER A N   
2245 C CA  . SER A 289 ? 0.5693 0.7252 0.7358 -0.0035 -0.0472 -0.0073 585 SER A CA  
2246 C C   . SER A 289 ? 0.5246 0.6726 0.6841 0.0099  -0.0474 -0.0100 585 SER A C   
2247 O O   . SER A 289 ? 0.3980 0.5681 0.5694 0.0189  -0.0471 -0.0144 585 SER A O   
2248 C CB  . SER A 289 ? 0.5755 0.7211 0.7233 -0.0059 -0.0482 -0.0026 585 SER A CB  
2249 O OG  . SER A 289 ? 0.5706 0.7196 0.7150 0.0087  -0.0491 -0.0049 585 SER A OG  
2250 N N   . GLY A 290 ? 0.4528 0.5729 0.5911 0.0109  -0.0480 -0.0076 586 GLY A N   
2251 C CA  . GLY A 290 ? 0.5517 0.6642 0.6758 0.0299  -0.0478 -0.0097 586 GLY A CA  
2252 C C   . GLY A 290 ? 0.6936 0.7562 0.7715 0.0372  -0.0502 -0.0055 586 GLY A C   
2253 O O   . GLY A 290 ? 0.6709 0.7117 0.7250 0.0385  -0.0522 -0.0018 586 GLY A O   
2254 N N   . TRP A 291 ? 0.7269 0.7648 0.7853 0.0423  -0.0500 -0.0059 587 TRP A N   
2255 C CA  . TRP A 291 ? 0.6300 0.6052 0.6335 0.0449  -0.0528 -0.0022 587 TRP A CA  
2256 C C   . TRP A 291 ? 0.8151 0.7740 0.8131 0.0334  -0.0527 -0.0028 587 TRP A C   
2257 O O   . TRP A 291 ? 0.8459 0.8417 0.8793 0.0326  -0.0499 -0.0063 587 TRP A O   
2258 C CB  . TRP A 291 ? 0.7418 0.6943 0.7086 0.0800  -0.0534 -0.0035 587 TRP A CB  
2259 C CG  . TRP A 291 ? 0.7810 0.7755 0.7696 0.1040  -0.0500 -0.0092 587 TRP A CG  
2260 C CD1 . TRP A 291 ? 0.8377 0.8245 0.8178 0.1112  -0.0479 -0.0116 587 TRP A CD1 
2261 C CD2 . TRP A 291 ? 0.7304 0.7866 0.7514 0.1215  -0.0482 -0.0130 587 TRP A CD2 
2262 N NE1 . TRP A 291 ? 0.8115 0.8554 0.8182 0.1320  -0.0440 -0.0162 587 TRP A NE1 
2263 C CE2 . TRP A 291 ? 0.8518 0.9407 0.8840 0.1369  -0.0444 -0.0172 587 TRP A CE2 
2264 C CE3 . TRP A 291 ? 0.8024 0.8924 0.8427 0.1238  -0.0496 -0.0133 587 TRP A CE3 
2265 C CZ2 . TRP A 291 ? 0.9094 1.0689 0.9726 0.1506  -0.0420 -0.0213 587 TRP A CZ2 
2266 C CZ3 . TRP A 291 ? 0.7132 0.8682 0.7826 0.1383  -0.0481 -0.0180 587 TRP A CZ3 
2267 C CH2 . TRP A 291 ? 0.8226 1.0145 0.9038 0.1499  -0.0444 -0.0218 587 TRP A CH2 
2268 N N   . TYR A 292 ? 0.8772 0.7770 0.8260 0.0217  -0.0563 0.0008  588 TYR A N   
2269 C CA  . TYR A 292 ? 0.8037 0.6887 0.7459 0.0044  -0.0576 0.0006  588 TYR A CA  
2270 C C   . TYR A 292 ? 0.8233 0.6879 0.7442 0.0298  -0.0560 -0.0036 588 TYR A C   
2271 O O   . TYR A 292 ? 0.8484 0.6778 0.7283 0.0576  -0.0560 -0.0046 588 TYR A O   
2272 C CB  . TYR A 292 ? 0.8187 0.6491 0.7119 -0.0244 -0.0628 0.0059  588 TYR A CB  
2273 C CG  . TYR A 292 ? 0.8356 0.7019 0.7563 -0.0601 -0.0643 0.0100  588 TYR A CG  
2274 C CD1 . TYR A 292 ? 0.7589 0.6129 0.6598 -0.0788 -0.0658 0.0154  588 TYR A CD1 
2275 C CD2 . TYR A 292 ? 0.7770 0.6894 0.7379 -0.0736 -0.0643 0.0088  588 TYR A CD2 
2276 C CE1 . TYR A 292 ? 0.7963 0.6914 0.7202 -0.1098 -0.0666 0.0194  588 TYR A CE1 
2277 C CE2 . TYR A 292 ? 0.7415 0.6940 0.7242 -0.1014 -0.0659 0.0127  588 TYR A CE2 
2278 C CZ  . TYR A 292 ? 0.7466 0.6944 0.7124 -0.1193 -0.0667 0.0178  588 TYR A CZ  
2279 O OH  . TYR A 292 ? 0.6707 0.6674 0.6569 -0.1457 -0.0674 0.0220  588 TYR A OH  
2280 N N   . MET A 293 ? 0.7636 0.6523 0.7104 0.0230  -0.0543 -0.0060 589 MET A N   
2281 C CA  . MET A 293 ? 0.7596 0.6142 0.6734 0.0352  -0.0540 -0.0087 589 MET A CA  
2282 C C   . MET A 293 ? 0.7183 0.5081 0.5793 0.0111  -0.0604 -0.0058 589 MET A C   
2283 O O   . MET A 293 ? 0.7305 0.5326 0.6059 -0.0222 -0.0639 -0.0024 589 MET A O   
2284 C CB  . MET A 293 ? 0.7088 0.6107 0.6661 0.0335  -0.0500 -0.0116 589 MET A CB  
2285 C CG  . MET A 293 ? 0.8326 0.7061 0.7594 0.0466  -0.0488 -0.0146 589 MET A CG  
2286 S SD  . MET A 293 ? 0.7737 0.7067 0.7508 0.0464  -0.0425 -0.0172 589 MET A SD  
2287 C CE  . MET A 293 ? 0.6821 0.6145 0.6743 0.0109  -0.0481 -0.0141 589 MET A CE  
2288 N N   . GLY A 294 ? 0.8059 0.5277 0.6017 0.0283  -0.0621 -0.0073 590 GLY A N   
2289 C CA  . GLY A 294 ? 0.8610 0.5045 0.5892 0.0032  -0.0692 -0.0046 590 GLY A CA  
2290 C C   . GLY A 294 ? 0.8744 0.5317 0.6176 -0.0362 -0.0732 -0.0033 590 GLY A C   
2291 O O   . GLY A 294 ? 0.7963 0.4255 0.5105 -0.0736 -0.0794 0.0010  590 GLY A O   
2292 N N   . THR A 295 ? 0.8124 0.5163 0.5988 -0.0298 -0.0702 -0.0066 591 THR A N   
2293 C CA  . THR A 295 ? 0.9271 0.6410 0.7206 -0.0606 -0.0749 -0.0059 591 THR A CA  
2294 C C   . THR A 295 ? 0.9054 0.6780 0.7458 -0.0915 -0.0773 -0.0015 591 THR A C   
2295 O O   . THR A 295 ? 0.8419 0.6173 0.6734 -0.1240 -0.0836 0.0007  591 THR A O   
2296 C CB  . THR A 295 ? 0.8536 0.5980 0.6760 -0.0428 -0.0706 -0.0101 591 THR A CB  
2297 O OG1 . THR A 295 ? 0.8900 0.6931 0.7673 -0.0191 -0.0628 -0.0115 591 THR A OG1 
2298 C CG2 . THR A 295 ? 0.7439 0.4229 0.5048 -0.0218 -0.0705 -0.0144 591 THR A CG2 
2299 N N   . GLU A 296 ? 0.7991 0.6225 0.6876 -0.0815 -0.0727 -0.0003 592 GLU A N   
2300 C CA  . GLU A 296 ? 0.7684 0.6467 0.6957 -0.1057 -0.0746 0.0035  592 GLU A CA  
2301 C C   . GLU A 296 ? 0.8171 0.6677 0.7036 -0.1425 -0.0810 0.0085  592 GLU A C   
2302 O O   . GLU A 296 ? 0.8961 0.7806 0.7930 -0.1718 -0.0858 0.0110  592 GLU A O   
2303 C CB  . GLU A 296 ? 0.8200 0.7404 0.7897 -0.0889 -0.0691 0.0036  592 GLU A CB  
2304 C CG  . GLU A 296 ? 0.7250 0.6742 0.7310 -0.0605 -0.0631 -0.0008 592 GLU A CG  
2305 C CD  . GLU A 296 ? 0.7853 0.7737 0.8275 -0.0513 -0.0593 -0.0007 592 GLU A CD  
2306 O OE1 . GLU A 296 ? 0.6633 0.6854 0.7275 -0.0658 -0.0607 0.0019  592 GLU A OE1 
2307 O OE2 . GLU A 296 ? 0.6124 0.5997 0.6576 -0.0295 -0.0553 -0.0034 592 GLU A OE2 
2308 N N   . ILE A 297 ? 0.9537 0.7419 0.7882 -0.1420 -0.0816 0.0100  593 ILE A N   
2309 C CA  . ILE A 297 ? 0.8830 0.6290 0.6637 -0.1816 -0.0876 0.0153  593 ILE A CA  
2310 C C   . ILE A 297 ? 0.8786 0.5685 0.6029 -0.2046 -0.0946 0.0142  593 ILE A C   
2311 O O   . ILE A 297 ? 0.9210 0.6277 0.6364 -0.2478 -0.1008 0.0175  593 ILE A O   
2312 C CB  . ILE A 297 ? 0.8351 0.5163 0.5647 -0.1712 -0.0864 0.0176  593 ILE A CB  
2313 C CG1 . ILE A 297 ? 0.9644 0.6982 0.7466 -0.1462 -0.0800 0.0179  593 ILE A CG1 
2314 C CG2 . ILE A 297 ? 0.8698 0.5074 0.5417 -0.2180 -0.0921 0.0240  593 ILE A CG2 
2315 C CD1 . ILE A 297 ? 1.0361 0.7105 0.7732 -0.1196 -0.0784 0.0183  593 ILE A CD1 
2316 N N   . GLY A 298 ? 0.9778 0.5999 0.6577 -0.1765 -0.0940 0.0095  594 GLY A N   
2317 C CA  . GLY A 298 ? 1.0710 0.6142 0.6758 -0.1958 -0.1010 0.0079  594 GLY A CA  
2318 C C   . GLY A 298 ? 1.0302 0.6097 0.6591 -0.2098 -0.1047 0.0052  594 GLY A C   
2319 O O   . GLY A 298 ? 1.1777 0.7015 0.7466 -0.2380 -0.1123 0.0045  594 GLY A O   
2320 N N   . VAL A 299 ? 1.0072 0.6714 0.7151 -0.1907 -0.0999 0.0035  595 VAL A N   
2321 C CA  . VAL A 299 ? 1.0159 0.7213 0.7502 -0.2015 -0.1035 0.0017  595 VAL A CA  
2322 C C   . VAL A 299 ? 0.9567 0.7534 0.7484 -0.2269 -0.1061 0.0060  595 VAL A C   
2323 O O   . VAL A 299 ? 0.9364 0.7507 0.7159 -0.2639 -0.1142 0.0080  595 VAL A O   
2324 C CB  . VAL A 299 ? 0.9497 0.6728 0.7174 -0.1590 -0.0965 -0.0033 595 VAL A CB  
2325 C CG1 . VAL A 299 ? 0.8624 0.6112 0.6423 -0.1696 -0.1010 -0.0050 595 VAL A CG1 
2326 C CG2 . VAL A 299 ? 0.8800 0.5276 0.5947 -0.1277 -0.0928 -0.0075 595 VAL A CG2 
2327 N N   . ARG A 300 ? 0.9332 0.7905 0.7843 -0.2070 -0.0995 0.0074  596 ARG A N   
2328 C CA  . ARG A 300 ? 0.7319 0.6785 0.6375 -0.2189 -0.1010 0.0104  596 ARG A CA  
2329 C C   . ARG A 300 ? 1.0050 0.9744 0.9002 -0.2571 -0.1047 0.0162  596 ARG A C   
2330 O O   . ARG A 300 ? 1.1286 1.1391 1.0226 -0.2910 -0.1118 0.0189  596 ARG A O   
2331 C CB  . ARG A 300 ? 0.6297 0.6225 0.5933 -0.1818 -0.0927 0.0089  596 ARG A CB  
2332 C CG  . ARG A 300 ? 0.6712 0.6470 0.6442 -0.1498 -0.0882 0.0041  596 ARG A CG  
2333 C CD  . ARG A 300 ? 0.7596 0.7482 0.7299 -0.1589 -0.0940 0.0032  596 ARG A CD  
2334 N NE  . ARG A 300 ? 0.7373 0.7996 0.7436 -0.1690 -0.0980 0.0063  596 ARG A NE  
2335 C CZ  . ARG A 300 ? 0.6425 0.7522 0.6924 -0.1452 -0.0937 0.0063  596 ARG A CZ  
2336 N NH1 . ARG A 300 ? 0.4110 0.5023 0.4744 -0.1176 -0.0856 0.0036  596 ARG A NH1 
2337 N NH2 . ARG A 300 ? 0.4945 0.6703 0.5701 -0.1487 -0.0977 0.0089  596 ARG A NH2 
2338 N N   . ASP A 301 ? 0.9090 0.8588 0.7970 -0.2528 -0.1000 0.0184  597 ASP A N   
2339 C CA  . ASP A 301 ? 0.9140 0.8824 0.7883 -0.2900 -0.1021 0.0246  597 ASP A CA  
2340 C C   . ASP A 301 ? 0.8750 0.7979 0.6840 -0.3401 -0.1111 0.0273  597 ASP A C   
2341 O O   . ASP A 301 ? 0.9391 0.9178 0.7524 -0.3816 -0.1159 0.0319  597 ASP A O   
2342 C CB  . ASP A 301 ? 0.9389 0.8676 0.7983 -0.2758 -0.0962 0.0262  597 ASP A CB  
2343 C CG  . ASP A 301 ? 0.8365 0.8182 0.7589 -0.2358 -0.0883 0.0240  597 ASP A CG  
2344 O OD1 . ASP A 301 ? 0.7787 0.8407 0.7541 -0.2314 -0.0872 0.0242  597 ASP A OD1 
2345 O OD2 . ASP A 301 ? 0.8399 0.7807 0.7536 -0.2078 -0.0837 0.0219  597 ASP A OD2 
2346 N N   . TYR A 302 ? 0.8339 0.6562 0.5777 -0.3375 -0.1135 0.0243  598 TYR A N   
2347 C CA  . TYR A 302 ? 1.0785 0.8355 0.7432 -0.3876 -0.1223 0.0267  598 TYR A CA  
2348 C C   . TYR A 302 ? 1.1701 0.9476 0.8297 -0.4119 -0.1309 0.0243  598 TYR A C   
2349 O O   . TYR A 302 ? 1.2620 1.0271 0.8748 -0.4627 -0.1381 0.0280  598 TYR A O   
2350 C CB  . TYR A 302 ? 1.2944 0.9208 0.8751 -0.3724 -0.1221 0.0244  598 TYR A CB  
2351 C CG  . TYR A 302 ? 1.3079 0.8925 0.8592 -0.3701 -0.1179 0.0290  598 TYR A CG  
2352 C CD1 . TYR A 302 ? 1.3529 0.8361 0.8440 -0.3358 -0.1155 0.0266  598 TYR A CD1 
2353 C CD2 . TYR A 302 ? 1.3357 0.9855 0.9179 -0.3989 -0.1162 0.0358  598 TYR A CD2 
2354 C CE1 . TYR A 302 ? 1.4259 0.8685 0.8859 -0.3307 -0.1124 0.0311  598 TYR A CE1 
2355 C CE2 . TYR A 302 ? 1.3537 0.9626 0.9057 -0.3972 -0.1123 0.0404  598 TYR A CE2 
2356 C CZ  . TYR A 302 ? 1.3971 0.9004 0.8875 -0.3631 -0.1109 0.0381  598 TYR A CZ  
2357 O OH  . TYR A 302 ? 1.3240 0.7852 0.7811 -0.3582 -0.1078 0.0429  598 TYR A OH  
2358 N N   . CYS A 303 ? 1.0632 0.8731 0.7671 -0.3756 -0.1291 0.0191  599 CYS A N   
2359 C CA  . CYS A 303 ? 1.1355 0.9466 0.8230 -0.3935 -0.1375 0.0161  599 CYS A CA  
2360 C C   . CYS A 303 ? 1.0948 1.0156 0.8571 -0.3819 -0.1386 0.0158  599 CYS A C   
2361 O O   . CYS A 303 ? 1.1350 1.0664 0.8851 -0.3994 -0.1467 0.0139  599 CYS A O   
2362 C CB  . CYS A 303 ? 1.1829 0.8989 0.8234 -0.3630 -0.1365 0.0095  599 CYS A CB  
2363 S SG  . CYS A 303 ? 1.2732 0.8407 0.8011 -0.3724 -0.1380 0.0088  599 CYS A SG  
2364 N N   . ASP A 304 ? 0.9733 0.9695 0.8053 -0.3514 -0.1313 0.0172  600 ASP A N   
2365 C CA  . ASP A 304 ? 0.9817 1.0822 0.8729 -0.3445 -0.1337 0.0181  600 ASP A CA  
2366 C C   . ASP A 304 ? 1.1207 1.2793 0.9999 -0.3980 -0.1440 0.0224  600 ASP A C   
2367 O O   . ASP A 304 ? 1.2506 1.3976 1.1003 -0.4297 -0.1421 0.0274  600 ASP A O   
2368 C CB  . ASP A 304 ? 0.9524 1.1176 0.9055 -0.3106 -0.1251 0.0197  600 ASP A CB  
2369 C CG  . ASP A 304 ? 0.9378 1.0808 0.9182 -0.2582 -0.1169 0.0152  600 ASP A CG  
2370 O OD1 . ASP A 304 ? 0.9573 1.0282 0.9081 -0.2454 -0.1152 0.0113  600 ASP A OD1 
2371 O OD2 . ASP A 304 ? 0.7830 0.9819 0.8111 -0.2305 -0.1120 0.0156  600 ASP A OD2 
2372 N N   . ASN A 305 ? 1.1681 1.3859 1.0661 -0.4003 -0.1510 0.0215  601 ASN A N   
2373 C CA  . ASN A 305 ? 1.2411 1.5125 1.1278 -0.4301 -0.1511 0.0274  601 ASN A CA  
2374 C C   . ASN A 305 ? 1.1937 1.5498 1.1158 -0.4298 -0.1431 0.0338  601 ASN A C   
2375 O O   . ASN A 305 ? 1.3274 1.6910 1.2190 -0.4653 -0.1402 0.0401  601 ASN A O   
2376 C CB  . ASN A 305 ? 1.3254 1.6507 1.2316 -0.4203 -0.1578 0.0254  601 ASN A CB  
2377 C CG  . ASN A 305 ? 1.4987 1.7592 1.3448 -0.4511 -0.1648 0.0239  601 ASN A CG  
2378 O OD1 . ASN A 305 ? 1.5771 1.7659 1.3635 -0.4847 -0.1638 0.0264  601 ASN A OD1 
2379 N ND2 . ASN A 305 ? 1.5171 1.7991 1.3736 -0.4384 -0.1720 0.0201  601 ASN A ND2 
2380 N N   . SER A 306 ? 1.0753 1.4926 1.0561 -0.3897 -0.1393 0.0324  602 SER A N   
2381 C CA  . SER A 306 ? 1.0821 1.5779 1.0958 -0.3809 -0.1310 0.0372  602 SER A CA  
2382 C C   . SER A 306 ? 1.0998 1.5539 1.1053 -0.3859 -0.1247 0.0388  602 SER A C   
2383 O O   . SER A 306 ? 1.0659 1.5782 1.1043 -0.3683 -0.1177 0.0411  602 SER A O   
2384 C CB  . SER A 306 ? 1.0442 1.6161 1.1148 -0.3308 -0.1296 0.0348  602 SER A CB  
2385 O OG  . SER A 306 ? 1.1034 1.6627 1.1795 -0.3121 -0.1376 0.0302  602 SER A OG  
2386 N N   . ARG A 307 ? 1.0707 1.4231 1.0292 -0.4063 -0.1271 0.0374  603 ARG A N   
2387 C CA  . ARG A 307 ? 1.0884 1.3951 1.0294 -0.4140 -0.1218 0.0397  603 ARG A CA  
2388 C C   . ARG A 307 ? 1.2257 1.4690 1.0944 -0.4611 -0.1227 0.0449  603 ARG A C   
2389 O O   . ARG A 307 ? 1.3520 1.6418 1.2064 -0.4893 -0.1227 0.0503  603 ARG A O   
2390 C CB  . ARG A 307 ? 0.9393 1.1732 0.8826 -0.3844 -0.1215 0.0338  603 ARG A CB  
2391 C CG  . ARG A 307 ? 0.8243 1.1061 0.8289 -0.3285 -0.1159 0.0300  603 ARG A CG  
2392 C CD  . ARG A 307 ? 0.7911 1.1493 0.8418 -0.3115 -0.1096 0.0326  603 ARG A CD  
2393 N NE  . ARG A 307 ? 0.7847 1.0944 0.8179 -0.3140 -0.1033 0.0344  603 ARG A NE  
2394 C CZ  . ARG A 307 ? 0.7991 1.0437 0.8294 -0.2809 -0.0973 0.0306  603 ARG A CZ  
2395 N NH1 . ARG A 307 ? 0.7234 0.9448 0.7669 -0.2468 -0.0960 0.0252  603 ARG A NH1 
2396 N NH2 . ARG A 307 ? 0.9035 1.1096 0.9159 -0.2831 -0.0926 0.0326  603 ARG A NH2 
2397 N N   . TYR A 308 ? 1.2364 1.3716 1.0527 -0.4694 -0.1237 0.0437  604 TYR A N   
2398 C CA  . TYR A 308 ? 1.2269 1.2922 0.9640 -0.5109 -0.1243 0.0495  604 TYR A CA  
2399 C C   . TYR A 308 ? 1.2291 1.2463 0.9107 -0.5354 -0.1312 0.0490  604 TYR A C   
2400 O O   . TYR A 308 ? 1.2957 1.2845 0.9161 -0.5756 -0.1323 0.0553  604 TYR A O   
2401 C CB  . TYR A 308 ? 1.1708 1.1293 0.8609 -0.5053 -0.1229 0.0486  604 TYR A CB  
2402 C CG  . TYR A 308 ? 1.2242 1.2194 0.9350 -0.5068 -0.1160 0.0539  604 TYR A CG  
2403 C CD1 . TYR A 308 ? 1.1678 1.2430 0.9575 -0.4749 -0.1113 0.0519  604 TYR A CD1 
2404 C CD2 . TYR A 308 ? 1.2614 1.2098 0.9082 -0.5401 -0.1146 0.0609  604 TYR A CD2 
2405 C CE1 . TYR A 308 ? 1.0513 1.1604 0.8585 -0.4752 -0.1047 0.0565  604 TYR A CE1 
2406 C CE2 . TYR A 308 ? 1.2685 1.2512 0.9328 -0.5422 -0.1083 0.0657  604 TYR A CE2 
2407 C CZ  . TYR A 308 ? 1.2275 1.2915 0.9735 -0.5094 -0.1031 0.0634  604 TYR A CZ  
2408 O OH  . TYR A 308 ? 1.3031 1.4010 1.0652 -0.5101 -0.0966 0.0680  604 TYR A OH  
2409 N N   . ASN A 309 ? 1.1065 1.1126 0.8040 -0.5137 -0.1361 0.0419  605 ASN A N   
2410 C CA  . ASN A 309 ? 1.1882 1.1710 0.8469 -0.5336 -0.1426 0.0411  605 ASN A CA  
2411 C C   . ASN A 309 ? 1.3513 1.2230 0.9085 -0.5682 -0.1449 0.0449  605 ASN A C   
2412 O O   . ASN A 309 ? 1.4216 1.3076 0.9406 -0.6092 -0.1463 0.0520  605 ASN A O   
2413 C CB  . ASN A 309 ? 1.1111 1.2133 0.8117 -0.5488 -0.1428 0.0456  605 ASN A CB  
2414 C CG  . ASN A 309 ? 1.1721 1.2603 0.8414 -0.5670 -0.1499 0.0445  605 ASN A CG  
2415 O OD1 . ASN A 309 ? 1.1989 1.2060 0.8377 -0.5547 -0.1547 0.0380  605 ASN A OD1 
2416 N ND2 . ASN A 309 ? 1.1229 1.2885 0.7955 -0.5963 -0.1503 0.0507  605 ASN A ND2 
2417 N N   . ILE A 310 ? 1.3926 1.1510 0.9017 -0.5488 -0.1451 0.0404  606 ILE A N   
2418 C CA  . ILE A 310 ? 1.4747 1.1125 0.8788 -0.5699 -0.1468 0.0436  606 ILE A CA  
2419 C C   . ILE A 310 ? 1.4866 1.0299 0.8265 -0.5630 -0.1524 0.0384  606 ILE A C   
2420 O O   . ILE A 310 ? 1.4825 0.9241 0.7255 -0.5807 -0.1548 0.0416  606 ILE A O   
2421 C CB  . ILE A 310 ? 1.4938 1.0604 0.8716 -0.5490 -0.1424 0.0432  606 ILE A CB  
2422 C CG1 . ILE A 310 ? 1.4731 0.9829 0.8613 -0.4980 -0.1420 0.0331  606 ILE A CG1 
2423 C CG2 . ILE A 310 ? 1.2712 0.9317 0.7155 -0.5526 -0.1365 0.0479  606 ILE A CG2 
2424 C CD1 . ILE A 310 ? 1.3106 0.7420 0.6654 -0.4712 -0.1378 0.0322  606 ILE A CD1 
2425 N N   . LEU A 311 ? 1.3325 0.9024 0.7171 -0.5367 -0.1548 0.0305  607 LEU A N   
2426 C CA  . LEU A 311 ? 1.4651 0.9487 0.7888 -0.5284 -0.1597 0.0252  607 LEU A CA  
2427 C C   . LEU A 311 ? 1.6733 1.1275 0.9253 -0.5754 -0.1643 0.0326  607 LEU A C   
2428 O O   . LEU A 311 ? 1.7327 1.0734 0.8926 -0.5761 -0.1671 0.0321  607 LEU A O   
2429 C CB  . LEU A 311 ? 1.2172 0.7579 0.6056 -0.5032 -0.1624 0.0169  607 LEU A CB  
2430 C CG  . LEU A 311 ? 1.2684 0.7812 0.6852 -0.4519 -0.1598 0.0065  607 LEU A CG  
2431 C CD1 . LEU A 311 ? 1.2435 0.8388 0.7345 -0.4350 -0.1631 0.0004  607 LEU A CD1 
2432 C CD2 . LEU A 311 ? 1.2872 0.6680 0.6163 -0.4275 -0.1596 0.0008  607 LEU A CD2 
2433 N N   . GLU A 312 ? 1.8274 1.3831 1.1165 -0.6136 -0.1649 0.0399  608 GLU A N   
2434 C CA  . GLU A 312 ? 1.9958 1.5360 1.2189 -0.6649 -0.1690 0.0481  608 GLU A CA  
2435 C C   . GLU A 312 ? 2.0638 1.4788 1.1749 -0.6839 -0.1695 0.0531  608 GLU A C   
2436 O O   . GLU A 312 ? 2.0265 1.3436 1.0482 -0.6961 -0.1744 0.0539  608 GLU A O   
2437 C CB  . GLU A 312 ? 2.0153 1.6887 1.2948 -0.6989 -0.1669 0.0559  608 GLU A CB  
2438 C CG  . GLU A 312 ? 1.9354 1.7352 1.3162 -0.6789 -0.1670 0.0518  608 GLU A CG  
2439 C CD  . GLU A 312 ? 1.9719 1.8424 1.3513 -0.7174 -0.1708 0.0572  608 GLU A CD  
2440 O OE1 . GLU A 312 ? 2.0592 1.8558 1.3566 -0.7514 -0.1756 0.0605  608 GLU A OE1 
2441 O OE2 . GLU A 312 ? 1.9117 1.9105 1.3678 -0.7125 -0.1690 0.0583  608 GLU A OE2 
2442 N N   . GLU A 313 ? 2.1959 1.6095 1.3067 -0.6844 -0.1649 0.0566  609 GLU A N   
2443 C CA  . GLU A 313 ? 2.4164 1.7199 1.4183 -0.7060 -0.1661 0.0621  609 GLU A CA  
2444 C C   . GLU A 313 ? 2.4673 1.6327 1.3991 -0.6620 -0.1668 0.0555  609 GLU A C   
2445 O O   . GLU A 313 ? 2.6620 1.7134 1.4802 -0.6764 -0.1707 0.0586  609 GLU A O   
2446 C CB  . GLU A 313 ? 2.5195 1.8708 1.5444 -0.7203 -0.1612 0.0675  609 GLU A CB  
2447 C CG  . GLU A 313 ? 2.6620 2.0766 1.6678 -0.7823 -0.1623 0.0778  609 GLU A CG  
2448 C CD  . GLU A 313 ? 2.8751 2.1759 1.7471 -0.8249 -0.1685 0.0835  609 GLU A CD  
2449 O OE1 . GLU A 313 ? 2.9186 2.1713 1.7448 -0.8335 -0.1737 0.0829  609 GLU A OE1 
2450 O OE2 . GLU A 313 ? 2.9691 2.2245 1.7769 -0.8501 -0.1686 0.0885  609 GLU A OE2 
2451 N N   . VAL A 314 ? 2.1261 1.2990 1.1177 -0.6074 -0.1631 0.0465  610 VAL A N   
2452 C CA  . VAL A 314 ? 2.0390 1.0905 0.9660 -0.5590 -0.1626 0.0398  610 VAL A CA  
2453 C C   . VAL A 314 ? 2.0757 1.0516 0.9325 -0.5572 -0.1679 0.0375  610 VAL A C   
2454 O O   . VAL A 314 ? 2.1832 1.0368 0.9313 -0.5466 -0.1702 0.0381  610 VAL A O   
2455 C CB  . VAL A 314 ? 1.9041 0.9926 0.9149 -0.5034 -0.1570 0.0307  610 VAL A CB  
2456 C CG1 . VAL A 314 ? 1.9032 0.8781 0.8503 -0.4470 -0.1552 0.0236  610 VAL A CG1 
2457 C CG2 . VAL A 314 ? 1.8788 1.0312 0.9480 -0.5070 -0.1519 0.0342  610 VAL A CG2 
2458 N N   . ALA A 315 ? 1.8006 0.8488 0.7147 -0.5675 -0.1703 0.0352  611 ALA A N   
2459 C CA  . ALA A 315 ? 1.9271 0.9118 0.7832 -0.5653 -0.1752 0.0327  611 ALA A CA  
2460 C C   . ALA A 315 ? 2.1306 1.0495 0.8820 -0.6173 -0.1810 0.0425  611 ALA A C   
2461 O O   . ALA A 315 ? 2.2203 1.0339 0.8793 -0.6095 -0.1848 0.0420  611 ALA A O   
2462 C CB  . ALA A 315 ? 1.7045 0.7906 0.6500 -0.5668 -0.1770 0.0279  611 ALA A CB  
2463 N N   . LYS A 316 ? 2.1570 1.1370 0.9176 -0.6704 -0.1815 0.0517  612 LYS A N   
2464 C CA  . LYS A 316 ? 2.2837 1.1962 0.9351 -0.7240 -0.1866 0.0616  612 LYS A CA  
2465 C C   . LYS A 316 ? 2.3641 1.1245 0.8941 -0.7026 -0.1878 0.0616  612 LYS A C   
2466 O O   . LYS A 316 ? 2.4221 1.0732 0.8462 -0.7063 -0.1929 0.0631  612 LYS A O   
2467 C CB  . LYS A 316 ? 2.2840 1.2916 0.9679 -0.7775 -0.1852 0.0706  612 LYS A CB  
2468 C CG  . LYS A 316 ? 2.1835 1.3107 0.9263 -0.8205 -0.1870 0.0750  612 LYS A CG  
2469 C CD  . LYS A 316 ? 2.1787 1.3537 0.8928 -0.8852 -0.1873 0.0863  612 LYS A CD  
2470 C CE  . LYS A 316 ? 2.3430 1.3769 0.9084 -0.9180 -0.1921 0.0926  612 LYS A CE  
2471 N NZ  . LYS A 316 ? 2.4347 1.5080 0.9584 -0.9872 -0.1933 0.1035  612 LYS A NZ  
2472 N N   . LYS A 317 ? 2.2774 1.0289 0.8193 -0.6770 -0.1832 0.0597  613 LYS A N   
2473 C CA  . LYS A 317 ? 2.4073 1.0227 0.8340 -0.6553 -0.1843 0.0594  613 LYS A CA  
2474 C C   . LYS A 317 ? 2.4253 0.9418 0.8010 -0.5930 -0.1845 0.0516  613 LYS A C   
2475 O O   . LYS A 317 ? 2.5430 0.9325 0.7983 -0.5769 -0.1873 0.0521  613 LYS A O   
2476 C CB  . LYS A 317 ? 2.3610 1.0023 0.8274 -0.6356 -0.1788 0.0578  613 LYS A CB  
2477 C CG  . LYS A 317 ? 2.4082 1.0715 0.8468 -0.6937 -0.1801 0.0665  613 LYS A CG  
2478 C CD  . LYS A 317 ? 2.3181 1.1409 0.8767 -0.7296 -0.1770 0.0705  613 LYS A CD  
2479 C CE  . LYS A 317 ? 2.4440 1.2924 0.9698 -0.7878 -0.1778 0.0793  613 LYS A CE  
2480 N NZ  . LYS A 317 ? 2.3576 1.3573 1.0072 -0.7981 -0.1717 0.0814  613 LYS A NZ  
2481 N N   . MET A 318 ? 2.4359 1.0091 0.8975 -0.5551 -0.1814 0.0439  614 MET A N   
2482 C CA  . MET A 318 ? 2.4939 0.9848 0.9075 -0.5003 -0.1814 0.0370  614 MET A CA  
2483 C C   . MET A 318 ? 2.6997 1.1368 1.0403 -0.5298 -0.1883 0.0410  614 MET A C   
2484 O O   . MET A 318 ? 2.8303 1.1820 1.1071 -0.4883 -0.1891 0.0370  614 MET A O   
2485 C CB  . MET A 318 ? 2.2425 0.8141 0.7715 -0.4501 -0.1753 0.0267  614 MET A CB  
2486 C CG  . MET A 318 ? 2.3537 0.9571 0.9399 -0.4099 -0.1682 0.0222  614 MET A CG  
2487 S SD  . MET A 318 ? 2.1550 0.8611 0.8768 -0.3626 -0.1614 0.0110  614 MET A SD  
2488 C CE  . MET A 318 ? 2.1312 0.7584 0.7928 -0.3109 -0.1613 0.0035  614 MET A CE  
2489 N N   . ASP A 319 ? 2.7886 1.2758 1.1350 -0.5991 -0.1928 0.0491  615 ASP A N   
2490 C CA  . ASP A 319 ? 2.9019 1.3613 1.1982 -0.6339 -0.1992 0.0532  615 ASP A CA  
2491 C C   . ASP A 319 ? 2.7798 1.2719 1.1396 -0.5919 -0.1978 0.0438  615 ASP A C   
2492 O O   . ASP A 319 ? 2.8384 1.2366 1.1312 -0.5502 -0.1985 0.0398  615 ASP A O   
2493 C CB  . ASP A 319 ? 3.1750 1.4772 1.3070 -0.6422 -0.2050 0.0591  615 ASP A CB  
2494 C CG  . ASP A 319 ? 3.3529 1.6415 1.4189 -0.7198 -0.2123 0.0700  615 ASP A CG  
2495 O OD1 . ASP A 319 ? 3.3579 1.7281 1.4612 -0.7754 -0.2123 0.0765  615 ASP A OD1 
2496 O OD2 . ASP A 319 ? 3.4687 1.6670 1.4439 -0.7251 -0.2178 0.0724  615 ASP A OD2 
2497 N N   . LEU A 320 ? 2.6128 1.2385 1.0988 -0.6005 -0.1957 0.0400  616 LEU A N   
2498 C CA  . LEU A 320 ? 2.4604 1.1305 1.0173 -0.5613 -0.1942 0.0296  616 LEU A CA  
2499 C C   . LEU A 320 ? 2.4378 1.1679 1.0206 -0.6051 -0.2001 0.0317  616 LEU A C   
2500 O O   . LEU A 320 ? 2.4369 1.2299 1.0339 -0.6633 -0.2031 0.0400  616 LEU A O   
2501 C CB  . LEU A 320 ? 2.2082 0.9817 0.8886 -0.5278 -0.1876 0.0218  616 LEU A CB  
2502 C CG  . LEU A 320 ? 2.0482 0.7707 0.7194 -0.4680 -0.1808 0.0161  616 LEU A CG  
2503 C CD1 . LEU A 320 ? 1.8593 0.6870 0.6541 -0.4390 -0.1750 0.0082  616 LEU A CD1 
2504 C CD2 . LEU A 320 ? 2.1571 0.7711 0.7483 -0.4163 -0.1800 0.0106  616 LEU A CD2 
2505 N N   . ASP A 321 ? 2.3822 1.0949 0.9692 -0.5748 -0.2014 0.0238  617 ASP A N   
2506 C CA  . ASP A 321 ? 2.3229 1.0961 0.9425 -0.6063 -0.2071 0.0232  617 ASP A CA  
2507 C C   . ASP A 321 ? 2.1772 1.1064 0.9267 -0.6198 -0.2061 0.0210  617 ASP A C   
2508 O O   . ASP A 321 ? 1.9427 0.9289 0.7712 -0.5799 -0.2036 0.0109  617 ASP A O   
2509 C CB  . ASP A 321 ? 2.3552 1.0794 0.9587 -0.5607 -0.2076 0.0133  617 ASP A CB  
2510 C CG  . ASP A 321 ? 2.4326 1.1800 1.0311 -0.5955 -0.2151 0.0138  617 ASP A CG  
2511 O OD1 . ASP A 321 ? 2.3993 1.0893 0.9629 -0.5650 -0.2163 0.0074  617 ASP A OD1 
2512 O OD2 . ASP A 321 ? 2.4605 1.2850 1.0881 -0.6516 -0.2196 0.0207  617 ASP A OD2 
2513 N N   . MET A 322 ? 2.2540 1.2543 1.0232 -0.6738 -0.2077 0.0305  618 MET A N   
2514 C CA  . MET A 322 ? 2.2578 1.4082 1.1459 -0.6814 -0.2059 0.0297  618 MET A CA  
2515 C C   . MET A 322 ? 2.3096 1.5557 1.2411 -0.7149 -0.2119 0.0310  618 MET A C   
2516 O O   . MET A 322 ? 2.2711 1.6478 1.2959 -0.7210 -0.2110 0.0313  618 MET A O   
2517 C CB  . MET A 322 ? 2.2212 1.4075 1.1169 -0.7093 -0.2018 0.0387  618 MET A CB  
2518 C CG  . MET A 322 ? 2.2051 1.3504 1.1084 -0.6660 -0.1952 0.0348  618 MET A CG  
2519 S SD  . MET A 322 ? 2.1464 1.3453 1.0691 -0.6959 -0.1904 0.0443  618 MET A SD  
2520 C CE  . MET A 322 ? 2.0206 1.4078 1.0734 -0.7138 -0.1896 0.0454  618 MET A CE  
2521 N N   . ARG A 323 ? 2.4200 1.6053 1.2844 -0.7339 -0.2180 0.0316  619 ARG A N   
2522 C CA  . ARG A 323 ? 2.3772 1.6531 1.2859 -0.7577 -0.2242 0.0307  619 ARG A CA  
2523 C C   . ARG A 323 ? 2.2986 1.6290 1.2871 -0.7079 -0.2251 0.0181  619 ARG A C   
2524 O O   . ARG A 323 ? 2.2731 1.7255 1.3423 -0.7123 -0.2282 0.0166  619 ARG A O   
2525 C CB  . ARG A 323 ? 2.4727 1.6615 1.2819 -0.7931 -0.2308 0.0349  619 ARG A CB  
2526 C CG  . ARG A 323 ? 2.6204 1.7580 1.3418 -0.8507 -0.2313 0.0484  619 ARG A CG  
2527 C CD  . ARG A 323 ? 2.8351 1.8203 1.4267 -0.8622 -0.2360 0.0512  619 ARG A CD  
2528 N NE  . ARG A 323 ? 2.9234 1.7909 1.4690 -0.8036 -0.2323 0.0446  619 ARG A NE  
2529 C CZ  . ARG A 323 ? 3.1063 1.8243 1.5278 -0.8003 -0.2342 0.0481  619 ARG A CZ  
2530 N NH1 . ARG A 323 ? 3.2434 1.9031 1.5698 -0.8568 -0.2402 0.0583  619 ARG A NH1 
2531 N NH2 . ARG A 323 ? 3.1358 1.7636 1.5247 -0.7394 -0.2300 0.0417  619 ARG A NH2 
2532 N N   . LYS A 324 ? 2.2319 1.4748 1.1954 -0.6582 -0.2223 0.0094  620 LYS A N   
2533 C CA  . LYS A 324 ? 2.0262 1.2998 1.0439 -0.6126 -0.2233 -0.0026 620 LYS A CA  
2534 C C   . LYS A 324 ? 1.8908 1.2141 0.9837 -0.5718 -0.2168 -0.0078 620 LYS A C   
2535 O O   . LYS A 324 ? 1.8963 1.1575 0.9632 -0.5524 -0.2102 -0.0074 620 LYS A O   
2536 C CB  . LYS A 324 ? 2.0459 1.1953 0.9845 -0.5822 -0.2233 -0.0093 620 LYS A CB  
2537 C CG  . LYS A 324 ? 2.1061 1.2226 0.9883 -0.6127 -0.2313 -0.0077 620 LYS A CG  
2538 C CD  . LYS A 324 ? 2.2396 1.2758 1.0246 -0.6612 -0.2336 0.0040  620 LYS A CD  
2539 C CE  . LYS A 324 ? 2.3142 1.3210 1.0455 -0.6928 -0.2421 0.0051  620 LYS A CE  
2540 N NZ  . LYS A 324 ? 2.4200 1.3371 1.0440 -0.7421 -0.2449 0.0170  620 LYS A NZ  
2541 N N   . THR A 325 ? 1.7112 1.1460 0.8935 -0.5586 -0.2194 -0.0120 621 THR A N   
2542 C CA  . THR A 325 ? 1.6384 1.1118 0.8862 -0.5158 -0.2145 -0.0182 621 THR A CA  
2543 C C   . THR A 325 ? 1.6279 0.9998 0.8335 -0.4686 -0.2095 -0.0279 621 THR A C   
2544 O O   . THR A 325 ? 1.4833 0.8382 0.7053 -0.4382 -0.2024 -0.0311 621 THR A O   
2545 C CB  . THR A 325 ? 1.6880 1.2819 1.0199 -0.5061 -0.2201 -0.0208 621 THR A CB  
2546 O OG1 . THR A 325 ? 1.6617 1.2561 1.0290 -0.4591 -0.2171 -0.0290 621 THR A OG1 
2547 C CG2 . THR A 325 ? 1.8557 1.4544 1.1650 -0.5189 -0.2286 -0.0229 621 THR A CG2 
2548 N N   . SER A 326 ? 1.7952 1.1017 0.9451 -0.4602 -0.2122 -0.0327 622 SER A N   
2549 C CA  . SER A 326 ? 1.7937 1.0213 0.9084 -0.4099 -0.2065 -0.0428 622 SER A CA  
2550 C C   . SER A 326 ? 1.7864 0.8925 0.8168 -0.3918 -0.1994 -0.0417 622 SER A C   
2551 O O   . SER A 326 ? 1.7218 0.7641 0.7189 -0.3442 -0.1928 -0.0495 622 SER A O   
2552 C CB  . SER A 326 ? 1.7500 0.9670 0.8422 -0.4062 -0.2121 -0.0479 622 SER A CB  
2553 O OG  . SER A 326 ? 1.7626 1.0146 0.8474 -0.4564 -0.2215 -0.0408 622 SER A OG  
2554 N N   . SER A 327 ? 1.8276 0.9020 0.8192 -0.4248 -0.2000 -0.0318 623 SER A N   
2555 C CA  . SER A 327 ? 1.8011 0.7632 0.7123 -0.4013 -0.1938 -0.0298 623 SER A CA  
2556 C C   . SER A 327 ? 1.7304 0.7028 0.6805 -0.3599 -0.1849 -0.0342 623 SER A C   
2557 O O   . SER A 327 ? 1.7236 0.6105 0.6133 -0.3275 -0.1789 -0.0341 623 SER A O   
2558 C CB  . SER A 327 ? 1.9512 0.8714 0.7995 -0.4512 -0.1978 -0.0170 623 SER A CB  
2559 O OG  . SER A 327 ? 1.9493 0.9629 0.8626 -0.4874 -0.1987 -0.0107 623 SER A OG  
2560 N N   . LEU A 328 ? 1.6358 0.7115 0.6822 -0.3590 -0.1843 -0.0376 624 LEU A N   
2561 C CA  . LEU A 328 ? 1.5043 0.6034 0.5964 -0.3304 -0.1769 -0.0404 624 LEU A CA  
2562 C C   . LEU A 328 ? 1.6327 0.6929 0.6886 -0.3482 -0.1750 -0.0311 624 LEU A C   
2563 O O   . LEU A 328 ? 1.7446 0.7720 0.7944 -0.3143 -0.1677 -0.0331 624 LEU A O   
2564 C CB  . LEU A 328 ? 1.5343 0.5880 0.6141 -0.2663 -0.1677 -0.0514 624 LEU A CB  
2565 C CG  . LEU A 328 ? 1.6243 0.7291 0.7456 -0.2474 -0.1669 -0.0576 624 LEU A CG  
2566 C CD1 . LEU A 328 ? 1.5383 0.6701 0.7033 -0.1798 -0.1494 -0.0591 624 LEU A CD1 
2567 C CD2 . LEU A 328 ? 1.4771 0.7032 0.6888 -0.2796 -0.1723 -0.0515 624 LEU A CD2 
2568 N N   . TRP A 329 ? 1.6125 0.6803 0.6434 -0.4021 -0.1813 -0.0208 625 TRP A N   
2569 C CA  . TRP A 329 ? 1.6763 0.7207 0.6767 -0.4264 -0.1798 -0.0112 625 TRP A CA  
2570 C C   . TRP A 329 ? 1.6322 0.7603 0.7185 -0.4208 -0.1755 -0.0113 625 TRP A C   
2571 O O   . TRP A 329 ? 1.6837 0.7743 0.7500 -0.4082 -0.1707 -0.0089 625 TRP A O   
2572 C CB  . TRP A 329 ? 1.7920 0.8484 0.7582 -0.4897 -0.1866 0.0000  625 TRP A CB  
2573 C CG  . TRP A 329 ? 1.7660 0.9583 0.8212 -0.5271 -0.1901 0.0033  625 TRP A CG  
2574 C CD1 . TRP A 329 ? 1.8164 1.0694 0.9037 -0.5425 -0.1960 0.0015  625 TRP A CD1 
2575 C CD2 . TRP A 329 ? 1.7854 1.0717 0.9058 -0.5486 -0.1877 0.0094  625 TRP A CD2 
2576 N NE1 . TRP A 329 ? 1.7269 1.1075 0.8941 -0.5692 -0.1974 0.0061  625 TRP A NE1 
2577 C CE2 . TRP A 329 ? 1.7146 1.1185 0.9037 -0.5729 -0.1919 0.0111  625 TRP A CE2 
2578 C CE3 . TRP A 329 ? 1.7339 1.0170 0.8589 -0.5472 -0.1822 0.0136  625 TRP A CE3 
2579 C CZ2 . TRP A 329 ? 1.5895 1.1093 0.8511 -0.5919 -0.1900 0.0170  625 TRP A CZ2 
2580 C CZ3 . TRP A 329 ? 1.7266 1.1230 0.9246 -0.5704 -0.1805 0.0193  625 TRP A CZ3 
2581 C CH2 . TRP A 329 ? 1.6712 1.1849 0.9358 -0.5909 -0.1839 0.0211  625 TRP A CH2 
2582 N N   . LYS A 330 ? 1.5746 0.8153 0.7542 -0.4274 -0.1777 -0.0140 626 LYS A N   
2583 C CA  . LYS A 330 ? 1.4314 0.7497 0.6921 -0.4169 -0.1737 -0.0144 626 LYS A CA  
2584 C C   . LYS A 330 ? 1.3738 0.6395 0.6319 -0.3631 -0.1666 -0.0231 626 LYS A C   
2585 O O   . LYS A 330 ? 1.3825 0.6344 0.6432 -0.3532 -0.1615 -0.0207 626 LYS A O   
2586 C CB  . LYS A 330 ? 1.3498 0.7932 0.7028 -0.4256 -0.1781 -0.0155 626 LYS A CB  
2587 C CG  . LYS A 330 ? 1.4330 0.9684 0.8210 -0.4706 -0.1806 -0.0048 626 LYS A CG  
2588 C CD  . LYS A 330 ? 1.4401 1.1043 0.9212 -0.4664 -0.1838 -0.0054 626 LYS A CD  
2589 C CE  . LYS A 330 ? 1.4008 1.1581 0.9076 -0.5062 -0.1855 0.0046  626 LYS A CE  
2590 N NZ  . LYS A 330 ? 1.2355 1.1127 0.8196 -0.4958 -0.1896 0.0040  626 LYS A NZ  
2591 N N   . ASP A 331 ? 1.4506 0.6953 0.7065 -0.3216 -0.1628 -0.0305 627 ASP A N   
2592 C CA  . ASP A 331 ? 1.3849 0.6115 0.6543 -0.2574 -0.1489 -0.0330 627 ASP A CA  
2593 C C   . ASP A 331 ? 1.3590 0.4726 0.5391 -0.2457 -0.1480 -0.0341 627 ASP A C   
2594 O O   . ASP A 331 ? 1.3293 0.4525 0.5338 -0.2084 -0.1384 -0.0325 627 ASP A O   
2595 C CB  . ASP A 331 ? 1.3061 0.5237 0.5725 -0.2188 -0.1443 -0.0394 627 ASP A CB  
2596 C CG  . ASP A 331 ? 1.2324 0.5467 0.5718 -0.2312 -0.1466 -0.0380 627 ASP A CG  
2597 O OD1 . ASP A 331 ? 1.2889 0.6162 0.6152 -0.2799 -0.1592 -0.0369 627 ASP A OD1 
2598 O OD2 . ASP A 331 ? 1.2255 0.6028 0.6319 -0.1931 -0.1361 -0.0378 627 ASP A OD2 
2599 N N   . GLN A 332 ? 1.5890 0.6128 0.6740 -0.2700 -0.1548 -0.0322 628 GLN A N   
2600 C CA  . GLN A 332 ? 1.7541 0.6776 0.7521 -0.2451 -0.1511 -0.0288 628 GLN A CA  
2601 C C   . GLN A 332 ? 1.7333 0.6643 0.7365 -0.2653 -0.1504 -0.0209 628 GLN A C   
2602 O O   . GLN A 332 ? 1.7172 0.6040 0.6946 -0.2266 -0.1445 -0.0215 628 GLN A O   
2603 C CB  . GLN A 332 ? 1.9730 0.8149 0.8744 -0.2646 -0.1570 -0.0238 628 GLN A CB  
2604 C CG  . GLN A 332 ? 2.1324 0.8686 0.9417 -0.2140 -0.1529 -0.0251 628 GLN A CG  
2605 C CD  . GLN A 332 ? 2.2819 0.9495 1.0130 -0.2179 -0.1577 -0.0242 628 GLN A CD  
2606 O OE1 . GLN A 332 ? 2.2237 0.9059 0.9500 -0.2704 -0.1654 -0.0196 628 GLN A OE1 
2607 N NE2 . GLN A 332 ? 2.4035 1.0011 1.0734 -0.1602 -0.1529 -0.0279 628 GLN A NE2 
2608 N N   . ALA A 333 ? 1.7392 0.7335 0.7775 -0.3231 -0.1556 -0.0131 629 ALA A N   
2609 C CA  . ALA A 333 ? 1.7486 0.7576 0.7937 -0.3446 -0.1542 -0.0054 629 ALA A CA  
2610 C C   . ALA A 333 ? 1.7513 0.8283 0.8843 -0.3193 -0.1485 -0.0095 629 ALA A C   
2611 O O   . ALA A 333 ? 1.8195 0.8897 0.9511 -0.3181 -0.1453 -0.0050 629 ALA A O   
2612 C CB  . ALA A 333 ? 1.7121 0.7817 0.7713 -0.4107 -0.1598 0.0044  629 ALA A CB  
2613 N N   . LEU A 334 ? 1.4805 0.6254 0.6884 -0.2977 -0.1467 -0.0167 630 LEU A N   
2614 C CA  . LEU A 334 ? 1.4246 0.6678 0.7335 -0.2607 -0.1355 -0.0142 630 LEU A CA  
2615 C C   . LEU A 334 ? 1.3633 0.5583 0.6508 -0.1997 -0.1260 -0.0172 630 LEU A C   
2616 O O   . LEU A 334 ? 1.4696 0.7088 0.8047 -0.1795 -0.1190 -0.0139 630 LEU A O   
2617 C CB  . LEU A 334 ? 1.2364 0.5816 0.6342 -0.2470 -0.1323 -0.0161 630 LEU A CB  
2618 C CG  . LEU A 334 ? 1.1642 0.6042 0.6593 -0.2127 -0.1214 -0.0138 630 LEU A CG  
2619 C CD1 . LEU A 334 ? 1.0498 0.5631 0.5954 -0.2474 -0.1238 -0.0071 630 LEU A CD1 
2620 C CD2 . LEU A 334 ? 1.1703 0.6749 0.7270 -0.1858 -0.1163 -0.0169 630 LEU A CD2 
2621 N N   . VAL A 335 ? 1.3926 0.5037 0.6097 -0.1669 -0.1255 -0.0237 631 VAL A N   
2622 C CA  . VAL A 335 ? 1.4837 0.5581 0.6778 -0.1044 -0.1166 -0.0267 631 VAL A CA  
2623 C C   . VAL A 335 ? 1.5408 0.5249 0.6558 -0.1081 -0.1198 -0.0233 631 VAL A C   
2624 O O   . VAL A 335 ? 1.5651 0.5664 0.7005 -0.0708 -0.1130 -0.0217 631 VAL A O   
2625 C CB  . VAL A 335 ? 1.5990 0.6134 0.7362 -0.0629 -0.1145 -0.0348 631 VAL A CB  
2626 C CG1 . VAL A 335 ? 1.4615 0.4324 0.5588 0.0027  -0.1067 -0.0376 631 VAL A CG1 
2627 C CG2 . VAL A 335 ? 1.5775 0.6872 0.7978 -0.0522 -0.1090 -0.0375 631 VAL A CG2 
2628 N N   . GLU A 336 ? 1.6328 0.5280 0.6576 -0.1527 -0.1297 -0.0206 632 GLU A N   
2629 C CA  . GLU A 336 ? 1.8300 0.6617 0.7854 -0.1561 -0.1305 -0.0130 632 GLU A CA  
2630 C C   . GLU A 336 ? 1.7175 0.6055 0.7328 -0.1784 -0.1290 -0.0077 632 GLU A C   
2631 O O   . GLU A 336 ? 1.7135 0.5654 0.6982 -0.1547 -0.1261 -0.0047 632 GLU A O   
2632 C CB  . GLU A 336 ? 1.9550 0.7262 0.8250 -0.2051 -0.1385 -0.0060 632 GLU A CB  
2633 C CG  . GLU A 336 ? 2.1110 0.8195 0.9129 -0.1898 -0.1412 -0.0092 632 GLU A CG  
2634 C CD  . GLU A 336 ? 2.2746 0.9008 0.9997 -0.1225 -0.1371 -0.0127 632 GLU A CD  
2635 O OE1 . GLU A 336 ? 2.2581 0.8757 0.9803 -0.0876 -0.1325 -0.0127 632 GLU A OE1 
2636 O OE2 . GLU A 336 ? 2.3443 0.9184 1.0110 -0.1032 -0.1386 -0.0151 632 GLU A OE2 
2637 N N   . ILE A 337 ? 1.7008 0.6813 0.8000 -0.2226 -0.1312 -0.0062 633 ILE A N   
2638 C CA  . ILE A 337 ? 1.5883 0.6479 0.7545 -0.2431 -0.1282 0.0012  633 ILE A CA  
2639 C C   . ILE A 337 ? 1.5503 0.6750 0.7894 -0.1833 -0.1172 0.0001  633 ILE A C   
2640 O O   . ILE A 337 ? 1.6646 0.7960 0.9114 -0.1786 -0.1143 0.0049  633 ILE A O   
2641 C CB  . ILE A 337 ? 1.4004 0.5693 0.6452 -0.2945 -0.1316 0.0045  633 ILE A CB  
2642 C CG1 . ILE A 337 ? 1.3830 0.5183 0.5636 -0.3555 -0.1399 0.0102  633 ILE A CG1 
2643 C CG2 . ILE A 337 ? 1.3479 0.6184 0.6792 -0.2993 -0.1259 0.0105  633 ILE A CG2 
2644 C CD1 . ILE A 337 ? 1.5359 0.7752 0.7829 -0.3955 -0.1441 0.0116  633 ILE A CD1 
2645 N N   . ASN A 338 ? 1.5239 0.6970 0.8138 -0.1390 -0.1110 -0.0059 634 ASN A N   
2646 C CA  . ASN A 338 ? 1.3865 0.6229 0.7407 -0.0875 -0.1011 -0.0070 634 ASN A CA  
2647 C C   . ASN A 338 ? 1.4378 0.5920 0.7188 -0.0356 -0.0987 -0.0095 634 ASN A C   
2648 O O   . ASN A 338 ? 1.3670 0.5640 0.6860 0.0002  -0.0924 -0.0089 634 ASN A O   
2649 C CB  . ASN A 338 ? 1.2692 0.5965 0.7070 -0.0649 -0.0948 -0.0114 634 ASN A CB  
2650 C CG  . ASN A 338 ? 1.1147 0.5345 0.6325 -0.1054 -0.0965 -0.0082 634 ASN A CG  
2651 O OD1 . ASN A 338 ? 1.1433 0.6465 0.7381 -0.1019 -0.0916 -0.0058 634 ASN A OD1 
2652 N ND2 . ASN A 338 ? 1.1099 0.5123 0.6034 -0.1429 -0.1041 -0.0084 634 ASN A ND2 
2653 N N   . ILE A 339 ? 1.6129 0.6510 0.7867 -0.0281 -0.1038 -0.0128 635 ILE A N   
2654 C CA  . ILE A 339 ? 1.5923 0.5348 0.6761 0.0194  -0.1034 -0.0142 635 ILE A CA  
2655 C C   . ILE A 339 ? 1.6592 0.5573 0.7052 -0.0053 -0.1071 -0.0066 635 ILE A C   
2656 O O   . ILE A 339 ? 1.6731 0.5527 0.6985 0.0380  -0.1040 -0.0056 635 ILE A O   
2657 C CB  . ILE A 339 ? 1.6136 0.4327 0.5801 0.0306  -0.1087 -0.0193 635 ILE A CB  
2658 C CG1 . ILE A 339 ? 1.6354 0.4956 0.6349 0.0649  -0.1036 -0.0274 635 ILE A CG1 
2659 C CG2 . ILE A 339 ? 1.7613 0.5072 0.6359 0.0743  -0.1081 -0.0176 635 ILE A CG2 
2660 C CD1 . ILE A 339 ? 1.7158 0.4896 0.6162 0.0808  -0.1067 -0.0301 635 ILE A CD1 
2661 N N   . ALA A 340 ? 1.6492 0.5406 0.6901 -0.0753 -0.1135 -0.0008 636 ALA A N   
2662 C CA  . ALA A 340 ? 1.7224 0.5736 0.7243 -0.1085 -0.1168 0.0074  636 ALA A CA  
2663 C C   . ALA A 340 ? 1.6010 0.5675 0.7079 -0.1031 -0.1100 0.0116  636 ALA A C   
2664 O O   . ALA A 340 ? 1.4760 0.4103 0.5526 -0.0941 -0.1094 0.0165  636 ALA A O   
2665 C CB  . ALA A 340 ? 1.7428 0.5930 0.7211 -0.1838 -0.1234 0.0125  636 ALA A CB  
2666 N N   . VAL A 341 ? 1.4320 0.5270 0.6553 -0.1108 -0.1056 0.0102  637 VAL A N   
2667 C CA  . VAL A 341 ? 1.2932 0.4924 0.6112 -0.0981 -0.0989 0.0127  637 VAL A CA  
2668 C C   . VAL A 341 ? 1.3564 0.5504 0.6717 -0.0311 -0.0935 0.0093  637 VAL A C   
2669 O O   . VAL A 341 ? 1.3904 0.5716 0.6915 -0.0181 -0.0925 0.0132  637 VAL A O   
2670 C CB  . VAL A 341 ? 1.1428 0.4666 0.5733 -0.1097 -0.0953 0.0106  637 VAL A CB  
2671 C CG1 . VAL A 341 ? 1.1102 0.5290 0.6269 -0.0977 -0.0890 0.0129  637 VAL A CG1 
2672 C CG2 . VAL A 341 ? 1.2004 0.5385 0.6322 -0.1720 -0.1015 0.0140  637 VAL A CG2 
2673 N N   . LEU A 342 ? 1.4340 0.6399 0.7591 0.0124  -0.0900 0.0021  638 LEU A N   
2674 C CA  . LEU A 342 ? 1.2784 0.5010 0.6090 0.0773  -0.0845 -0.0016 638 LEU A CA  
2675 C C   . LEU A 342 ? 1.4284 0.5460 0.6575 0.1031  -0.0881 0.0011  638 LEU A C   
2676 O O   . LEU A 342 ? 1.4031 0.5472 0.6491 0.1254  -0.0861 0.0038  638 LEU A O   
2677 C CB  . LEU A 342 ? 1.4082 0.6422 0.7409 0.1156  -0.0807 -0.0092 638 LEU A CB  
2678 C CG  . LEU A 342 ? 1.2930 0.6385 0.7297 0.1022  -0.0755 -0.0118 638 LEU A CG  
2679 C CD1 . LEU A 342 ? 1.3080 0.6552 0.7350 0.1366  -0.0716 -0.0187 638 LEU A CD1 
2680 C CD2 . LEU A 342 ? 1.0738 0.5237 0.6006 0.1131  -0.0697 -0.0108 638 LEU A CD2 
2681 N N   . TYR A 343 ? 1.5537 0.5448 0.6697 0.0988  -0.0943 0.0007  639 TYR A N   
2682 C CA  . TYR A 343 ? 1.8571 0.7266 0.8565 0.1262  -0.0985 0.0032  639 TYR A CA  
2683 C C   . TYR A 343 ? 1.8950 0.7612 0.8948 0.0966  -0.1003 0.0118  639 TYR A C   
2684 O O   . TYR A 343 ? 1.8173 0.6651 0.7902 0.1386  -0.0994 0.0137  639 TYR A O   
2685 C CB  . TYR A 343 ? 2.0242 0.7865 0.9158 0.1027  -0.1044 0.0011  639 TYR A CB  
2686 C CG  . TYR A 343 ? 1.9092 0.5821 0.6910 0.1192  -0.1071 0.0013  639 TYR A CG  
2687 C CD1 . TYR A 343 ? 1.8936 0.5488 0.6302 0.1920  -0.1040 -0.0045 639 TYR A CD1 
2688 C CD2 . TYR A 343 ? 2.0836 0.6932 0.8030 0.0616  -0.1128 0.0066  639 TYR A CD2 
2689 C CE1 . TYR A 343 ? 2.0129 0.5796 0.6401 0.2092  -0.1069 -0.0056 639 TYR A CE1 
2690 C CE2 . TYR A 343 ? 2.1926 0.7106 0.8017 0.0766  -0.1157 0.0053  639 TYR A CE2 
2691 C CZ  . TYR A 343 ? 2.2636 0.7563 0.8252 0.1515  -0.1129 -0.0011 639 TYR A CZ  
2692 O OH  . TYR A 343 ? 2.5588 0.9563 1.0047 0.1687  -0.1160 -0.0035 639 TYR A OH  
2693 N N   . SER A 344 ? 1.8990 0.7874 0.9280 0.0255  -0.1027 0.0173  640 SER A N   
2694 C CA  . SER A 344 ? 1.7378 0.6188 0.7589 -0.0083 -0.1039 0.0261  640 SER A CA  
2695 C C   . SER A 344 ? 1.7159 0.7053 0.8307 0.0249  -0.0975 0.0264  640 SER A C   
2696 O O   . SER A 344 ? 1.7329 0.6862 0.8088 0.0448  -0.0980 0.0307  640 SER A O   
2697 C CB  . SER A 344 ? 1.7317 0.6425 0.7798 -0.0892 -0.1066 0.0313  640 SER A CB  
2698 O OG  . SER A 344 ? 1.9294 0.7574 0.9007 -0.1214 -0.1130 0.0294  640 SER A OG  
2699 N N   . PHE A 345 ? 1.4075 0.5247 0.6395 0.0324  -0.0918 0.0216  641 PHE A N   
2700 C CA  . PHE A 345 ? 1.2879 0.5088 0.6084 0.0564  -0.0863 0.0213  641 PHE A CA  
2701 C C   . PHE A 345 ? 1.4315 0.6346 0.7207 0.1254  -0.0852 0.0182  641 PHE A C   
2702 O O   . PHE A 345 ? 1.5025 0.7392 0.8134 0.1420  -0.0840 0.0208  641 PHE A O   
2703 C CB  . PHE A 345 ? 1.1471 0.4912 0.5828 0.0514  -0.0810 0.0162  641 PHE A CB  
2704 C CG  . PHE A 345 ? 1.0855 0.4965 0.5870 -0.0026 -0.0803 0.0202  641 PHE A CG  
2705 C CD1 . PHE A 345 ? 1.2510 0.6272 0.7223 -0.0559 -0.0847 0.0241  641 PHE A CD1 
2706 C CD2 . PHE A 345 ? 0.9278 0.4400 0.5191 0.0010  -0.0756 0.0197  641 PHE A CD2 
2707 C CE1 . PHE A 345 ? 1.1734 0.6234 0.7063 -0.1004 -0.0838 0.0277  641 PHE A CE1 
2708 C CE2 . PHE A 345 ? 0.8655 0.4403 0.5136 -0.0414 -0.0747 0.0227  641 PHE A CE2 
2709 C CZ  . PHE A 345 ? 0.9439 0.4917 0.5640 -0.0902 -0.0786 0.0269  641 PHE A CZ  
2710 N N   . GLN A 346 ? 1.3872 0.5415 0.6238 0.1683  -0.0857 0.0127  642 GLN A N   
2711 C CA  . GLN A 346 ? 1.5408 0.6937 0.7505 0.2408  -0.0844 0.0090  642 GLN A CA  
2712 C C   . GLN A 346 ? 1.7037 0.7286 0.7900 0.2654  -0.0902 0.0137  642 GLN A C   
2713 O O   . GLN A 346 ? 1.6989 0.7376 0.7737 0.3180  -0.0900 0.0135  642 GLN A O   
2714 C CB  . GLN A 346 ? 1.6270 0.7879 0.8297 0.2822  -0.0816 0.0009  642 GLN A CB  
2715 C CG  . GLN A 346 ? 1.4423 0.7239 0.7580 0.2643  -0.0754 -0.0038 642 GLN A CG  
2716 C CD  . GLN A 346 ? 1.4710 0.7216 0.7579 0.2730  -0.0743 -0.0094 642 GLN A CD  
2717 O OE1 . GLN A 346 ? 1.5205 0.6529 0.7059 0.2741  -0.0794 -0.0094 642 GLN A OE1 
2718 N NE2 . GLN A 346 ? 1.3717 0.7246 0.7437 0.2770  -0.0679 -0.0142 642 GLN A NE2 
2719 N N   . SER A 347 ? 1.7318 0.6286 0.7178 0.2305  -0.0959 0.0177  643 SER A N   
2720 C CA  . SER A 347 ? 1.8795 0.6862 0.7630 0.2372  -0.0984 0.0173  643 SER A CA  
2721 C C   . SER A 347 ? 1.8718 0.6882 0.7723 0.2146  -0.0996 0.0271  643 SER A C   
2722 O O   . SER A 347 ? 1.9492 0.7120 0.7809 0.2319  -0.1006 0.0259  643 SER A O   
2723 C CB  . SER A 347 ? 1.9448 0.6465 0.7325 0.1907  -0.1027 0.0152  643 SER A CB  
2724 O OG  . SER A 347 ? 2.0191 0.7077 0.7861 0.2090  -0.1022 0.0075  643 SER A OG  
2725 N N   . ASP A 348 ? 1.7649 0.6692 0.7642 0.1731  -0.0978 0.0331  644 ASP A N   
2726 C CA  . ASP A 348 ? 1.6474 0.5964 0.6857 0.1512  -0.0966 0.0398  644 ASP A CA  
2727 C C   . ASP A 348 ? 1.6729 0.7498 0.8122 0.1935  -0.0920 0.0354  644 ASP A C   
2728 O O   . ASP A 348 ? 1.5655 0.6866 0.7416 0.1812  -0.0909 0.0398  644 ASP A O   
2729 C CB  . ASP A 348 ? 1.5854 0.5774 0.6767 0.0717  -0.0952 0.0445  644 ASP A CB  
2730 C CG  . ASP A 348 ? 1.7335 0.6009 0.7169 0.0176  -0.1006 0.0518  644 ASP A CG  
2731 O OD1 . ASP A 348 ? 1.8316 0.5838 0.7021 0.0398  -0.1045 0.0501  644 ASP A OD1 
2732 O OD2 . ASP A 348 ? 1.6857 0.5898 0.7046 -0.0484 -0.1000 0.0557  644 ASP A OD2 
2733 N N   . LYS A 349 ? 1.5343 0.6731 0.7173 0.2394  -0.0892 0.0268  645 LYS A N   
2734 C CA  . LYS A 349 ? 1.5766 0.8353 0.8461 0.2791  -0.0855 0.0221  645 LYS A CA  
2735 C C   . LYS A 349 ? 1.4544 0.8304 0.8430 0.2346  -0.0810 0.0214  645 LYS A C   
2736 O O   . LYS A 349 ? 1.3671 0.8289 0.8192 0.2489  -0.0792 0.0200  645 LYS A O   
2737 C CB  . LYS A 349 ? 1.7642 0.9961 0.9857 0.3216  -0.0889 0.0256  645 LYS A CB  
2738 C CG  . LYS A 349 ? 1.8831 1.1837 1.1258 0.3930  -0.0881 0.0191  645 LYS A CG  
2739 C CD  . LYS A 349 ? 1.9851 1.2873 1.2171 0.4246  -0.0858 0.0119  645 LYS A CD  
2740 C CE  . LYS A 349 ? 2.0777 1.4334 1.3019 0.4970  -0.0842 0.0049  645 LYS A CE  
2741 N NZ  . LYS A 349 ? 1.9917 1.4591 1.2909 0.5126  -0.0846 0.0053  645 LYS A NZ  
2742 N N   . VAL A 350 ? 1.3744 0.7506 0.7870 0.1817  -0.0799 0.0224  646 VAL A N   
2743 C CA  . VAL A 350 ? 1.2153 0.6935 0.7314 0.1428  -0.0758 0.0214  646 VAL A CA  
2744 C C   . VAL A 350 ? 1.1606 0.7079 0.7381 0.1562  -0.0720 0.0136  646 VAL A C   
2745 O O   . VAL A 350 ? 1.2455 0.7480 0.7869 0.1593  -0.0726 0.0112  646 VAL A O   
2746 C CB  . VAL A 350 ? 1.1738 0.6213 0.6794 0.0798  -0.0770 0.0273  646 VAL A CB  
2747 C CG1 . VAL A 350 ? 1.0131 0.5658 0.6196 0.0475  -0.0729 0.0263  646 VAL A CG1 
2748 C CG2 . VAL A 350 ? 1.1024 0.4660 0.5290 0.0629  -0.0806 0.0360  646 VAL A CG2 
2749 N N   . THR A 351 ? 1.0008 0.6524 0.6660 0.1607  -0.0680 0.0098  647 THR A N   
2750 C CA  . THR A 351 ? 1.0199 0.7426 0.7426 0.1743  -0.0638 0.0028  647 THR A CA  
2751 C C   . THR A 351 ? 1.0079 0.7250 0.7471 0.1383  -0.0627 0.0023  647 THR A C   
2752 O O   . THR A 351 ? 1.0636 0.8047 0.8402 0.0978  -0.0625 0.0049  647 THR A O   
2753 C CB  . THR A 351 ? 0.9884 0.8136 0.7939 0.1734  -0.0607 -0.0002 647 THR A CB  
2754 O OG1 . THR A 351 ? 1.0053 0.8383 0.7981 0.1980  -0.0629 0.0011  647 THR A OG1 
2755 C CG2 . THR A 351 ? 0.8718 0.7674 0.7237 0.1918  -0.0563 -0.0069 647 THR A CG2 
2756 N N   . ILE A 352 ? 1.0484 0.7380 0.7588 0.1563  -0.0620 -0.0012 648 ILE A N   
2757 C CA  . ILE A 352 ? 0.9886 0.6828 0.7183 0.1294  -0.0610 -0.0029 648 ILE A CA  
2758 C C   . ILE A 352 ? 0.9730 0.6937 0.7096 0.1642  -0.0568 -0.0090 648 ILE A C   
2759 O O   . ILE A 352 ? 0.9632 0.6680 0.6612 0.2091  -0.0562 -0.0114 648 ILE A O   
2760 C CB  . ILE A 352 ? 0.9819 0.5826 0.6418 0.1001  -0.0664 0.0010  648 ILE A CB  
2761 C CG1 . ILE A 352 ? 0.9388 0.5663 0.6366 0.0605  -0.0664 0.0007  648 ILE A CG1 
2762 C CG2 . ILE A 352 ? 0.9268 0.4423 0.5004 0.1343  -0.0685 -0.0012 648 ILE A CG2 
2763 C CD1 . ILE A 352 ? 0.9942 0.5571 0.6414 0.0169  -0.0725 0.0057  648 ILE A CD1 
2764 N N   . VAL A 353 ? 0.9444 0.7099 0.7292 0.1455  -0.0536 -0.0115 649 VAL A N   
2765 C CA  . VAL A 353 ? 0.8851 0.6844 0.6818 0.1722  -0.0484 -0.0167 649 VAL A CA  
2766 C C   . VAL A 353 ? 0.8838 0.6429 0.6600 0.1521  -0.0495 -0.0173 649 VAL A C   
2767 O O   . VAL A 353 ? 0.7951 0.5451 0.5854 0.1116  -0.0528 -0.0144 649 VAL A O   
2768 C CB  . VAL A 353 ? 0.9449 0.8472 0.8221 0.1699  -0.0426 -0.0192 649 VAL A CB  
2769 C CG1 . VAL A 353 ? 0.8899 0.8187 0.8149 0.1294  -0.0418 -0.0182 649 VAL A CG1 
2770 C CG2 . VAL A 353 ? 0.8522 0.8009 0.7346 0.2063  -0.0366 -0.0240 649 VAL A CG2 
2771 N N   . ASP A 354 ? 0.9763 0.7121 0.7150 0.1821  -0.0472 -0.0213 650 ASP A N   
2772 C CA  . ASP A 354 ? 0.9443 0.6355 0.6554 0.1653  -0.0489 -0.0224 650 ASP A CA  
2773 C C   . ASP A 354 ? 0.9964 0.7634 0.7728 0.1561  -0.0428 -0.0246 650 ASP A C   
2774 O O   . ASP A 354 ? 0.9726 0.8155 0.7980 0.1713  -0.0364 -0.0263 650 ASP A O   
2775 C CB  . ASP A 354 ? 0.9247 0.5364 0.5486 0.2026  -0.0501 -0.0256 650 ASP A CB  
2776 C CG  . ASP A 354 ? 1.1720 0.8360 0.8056 0.2526  -0.0422 -0.0307 650 ASP A CG  
2777 O OD1 . ASP A 354 ? 1.2973 0.9527 0.8954 0.2977  -0.0413 -0.0321 650 ASP A OD1 
2778 O OD2 . ASP A 354 ? 1.2337 0.9521 0.9096 0.2474  -0.0366 -0.0330 650 ASP A OD2 
2779 N N   . HIS A 355 ? 1.0081 0.7543 0.7827 0.1273  -0.0454 -0.0242 651 HIS A N   
2780 C CA  . HIS A 355 ? 0.8653 0.6745 0.6973 0.1138  -0.0406 -0.0251 651 HIS A CA  
2781 C C   . HIS A 355 ? 0.8465 0.6924 0.6828 0.1470  -0.0320 -0.0293 651 HIS A C   
2782 O O   . HIS A 355 ? 0.8574 0.7682 0.7456 0.1388  -0.0262 -0.0295 651 HIS A O   
2783 C CB  . HIS A 355 ? 0.9283 0.7057 0.7498 0.0808  -0.0461 -0.0238 651 HIS A CB  
2784 C CG  . HIS A 355 ? 0.8641 0.5600 0.6102 0.0874  -0.0505 -0.0260 651 HIS A CG  
2785 N ND1 . HIS A 355 ? 0.9068 0.5253 0.5866 0.0874  -0.0568 -0.0251 651 HIS A ND1 
2786 C CD2 . HIS A 355 ? 0.8982 0.5708 0.6181 0.0918  -0.0499 -0.0291 651 HIS A CD2 
2787 C CE1 . HIS A 355 ? 1.1528 0.6995 0.7651 0.0917  -0.0603 -0.0280 651 HIS A CE1 
2788 N NE2 . HIS A 355 ? 0.9623 0.5426 0.5994 0.0957  -0.0561 -0.0308 651 HIS A NE2 
2789 N N   . HIS A 356 ? 1.0087 0.8144 0.7875 0.1848  -0.0309 -0.0326 652 HIS A N   
2790 C CA  . HIS A 356 ? 1.0145 0.8684 0.7977 0.2216  -0.0218 -0.0366 652 HIS A CA  
2791 C C   . HIS A 356 ? 0.9479 0.8877 0.7794 0.2374  -0.0163 -0.0366 652 HIS A C   
2792 O O   . HIS A 356 ? 0.7456 0.7647 0.6249 0.2345  -0.0087 -0.0374 652 HIS A O   
2793 C CB  . HIS A 356 ? 1.0818 0.8652 0.7821 0.2638  -0.0228 -0.0403 652 HIS A CB  
2794 C CG  . HIS A 356 ? 1.2231 0.9196 0.8691 0.2461  -0.0287 -0.0412 652 HIS A CG  
2795 N ND1 . HIS A 356 ? 1.1678 0.8735 0.8167 0.2422  -0.0249 -0.0435 652 HIS A ND1 
2796 C CD2 . HIS A 356 ? 1.2722 0.8742 0.8602 0.2256  -0.0386 -0.0396 652 HIS A CD2 
2797 C CE1 . HIS A 356 ? 1.2794 0.9000 0.8742 0.2225  -0.0328 -0.0440 652 HIS A CE1 
2798 N NE2 . HIS A 356 ? 1.1846 0.7425 0.7417 0.2097  -0.0413 -0.0416 652 HIS A NE2 
2799 N N   . SER A 357 ? 1.0692 0.9937 0.8852 0.2514  -0.0205 -0.0355 653 SER A N   
2800 C CA  . SER A 357 ? 1.0404 1.0468 0.8969 0.2684  -0.0166 -0.0360 653 SER A CA  
2801 C C   . SER A 357 ? 0.7326 0.7997 0.6608 0.2264  -0.0159 -0.0335 653 SER A C   
2802 O O   . SER A 357 ? 0.8053 0.9548 0.7758 0.2297  -0.0112 -0.0346 653 SER A O   
2803 C CB  . SER A 357 ? 1.0686 1.0356 0.8825 0.2971  -0.0221 -0.0352 653 SER A CB  
2804 O OG  . SER A 357 ? 1.0764 1.1296 0.9267 0.3182  -0.0188 -0.0363 653 SER A OG  
2805 N N   . ALA A 358 ? 0.6777 0.7062 0.6161 0.1873  -0.0209 -0.0304 654 ALA A N   
2806 C CA  . ALA A 358 ? 0.6874 0.7635 0.6843 0.1522  -0.0204 -0.0285 654 ALA A CA  
2807 C C   . ALA A 358 ? 0.7081 0.8254 0.7365 0.1349  -0.0143 -0.0292 654 ALA A C   
2808 O O   . ALA A 358 ? 0.6658 0.8398 0.7361 0.1181  -0.0108 -0.0291 654 ALA A O   
2809 C CB  . ALA A 358 ? 0.7068 0.7346 0.7013 0.1220  -0.0277 -0.0248 654 ALA A CB  
2810 N N   . THR A 359 ? 0.5690 0.6530 0.5727 0.1362  -0.0132 -0.0297 655 THR A N   
2811 C CA  . THR A 359 ? 0.6304 0.7519 0.6593 0.1211  -0.0069 -0.0298 655 THR A CA  
2812 C C   . THR A 359 ? 0.6675 0.8590 0.7087 0.1414  0.0022  -0.0323 655 THR A C   
2813 O O   . THR A 359 ? 0.6271 0.8720 0.7013 0.1210  0.0080  -0.0316 655 THR A O   
2814 C CB  . THR A 359 ? 0.6640 0.7346 0.6626 0.1176  -0.0084 -0.0297 655 THR A CB  
2815 O OG1 . THR A 359 ? 0.7414 0.7742 0.6893 0.1511  -0.0085 -0.0326 655 THR A OG1 
2816 C CG2 . THR A 359 ? 0.6963 0.7190 0.6915 0.0916  -0.0174 -0.0268 655 THR A CG2 
2817 N N   . GLU A 360 ? 0.6927 0.8864 0.7042 0.1812  0.0034  -0.0350 656 GLU A N   
2818 C CA  . GLU A 360 ? 0.7713 1.0473 0.7961 0.2047  0.0120  -0.0375 656 GLU A CA  
2819 C C   . GLU A 360 ? 0.8268 1.1751 0.8985 0.1861  0.0128  -0.0368 656 GLU A C   
2820 O O   . GLU A 360 ? 0.9530 1.3757 1.0556 0.1702  0.0200  -0.0369 656 GLU A O   
2821 C CB  . GLU A 360 ? 0.8018 1.0623 0.7792 0.2586  0.0119  -0.0407 656 GLU A CB  
2822 C CG  . GLU A 360 ? 0.9031 1.2343 0.8769 0.2914  0.0219  -0.0438 656 GLU A CG  
2823 C CD  . GLU A 360 ? 1.1092 1.4891 1.0696 0.3405  0.0227  -0.0464 656 GLU A CD  
2824 O OE1 . GLU A 360 ? 1.2261 1.7106 1.2302 0.3367  0.0274  -0.0467 656 GLU A OE1 
2825 O OE2 . GLU A 360 ? 1.1279 1.4403 1.0297 0.3823  0.0179  -0.0482 656 GLU A OE2 
2826 N N   . SER A 361 ? 0.7476 1.0728 0.8214 0.1846  0.0054  -0.0360 657 SER A N   
2827 C CA  A SER A 361 ? 0.6392 1.0267 0.7527 0.1667  0.0049  -0.0359 657 SER A CA  
2828 C CA  B SER A 361 ? 0.6445 1.0299 0.7578 0.1663  0.0047  -0.0359 657 SER A CA  
2829 C C   . SER A 361 ? 0.6475 1.0466 0.7936 0.1186  0.0066  -0.0341 657 SER A C   
2830 O O   . SER A 361 ? 0.7538 1.2194 0.9285 0.0990  0.0100  -0.0348 657 SER A O   
2831 C CB  A SER A 361 ? 0.5213 0.8717 0.6256 0.1745  -0.0035 -0.0351 657 SER A CB  
2832 C CB  B SER A 361 ? 0.5211 0.8639 0.6253 0.1710  -0.0039 -0.0348 657 SER A CB  
2833 O OG  A SER A 361 ? 0.5057 0.8297 0.5671 0.2202  -0.0054 -0.0363 657 SER A OG  
2834 O OG  B SER A 361 ? 0.4795 0.7652 0.5886 0.1381  -0.0086 -0.0321 657 SER A OG  
2835 N N   . PHE A 362 ? 0.6411 0.9757 0.7783 0.0992  0.0039  -0.0318 658 PHE A N   
2836 C CA  . PHE A 362 ? 0.6227 0.9581 0.7806 0.0599  0.0050  -0.0299 658 PHE A CA  
2837 C C   . PHE A 362 ? 0.5916 0.9767 0.7572 0.0471  0.0141  -0.0299 658 PHE A C   
2838 O O   . PHE A 362 ? 0.7013 1.1220 0.8850 0.0172  0.0167  -0.0294 658 PHE A O   
2839 C CB  . PHE A 362 ? 0.5787 0.8424 0.7233 0.0481  -0.0002 -0.0274 658 PHE A CB  
2840 C CG  . PHE A 362 ? 0.6190 0.8753 0.7774 0.0151  -0.0005 -0.0254 658 PHE A CG  
2841 C CD1 . PHE A 362 ? 0.5875 0.8524 0.7619 -0.0011 -0.0035 -0.0256 658 PHE A CD1 
2842 C CD2 . PHE A 362 ? 0.7402 0.9775 0.8893 0.0024  0.0024  -0.0234 658 PHE A CD2 
2843 C CE1 . PHE A 362 ? 0.6130 0.8609 0.7890 -0.0273 -0.0040 -0.0242 658 PHE A CE1 
2844 C CE2 . PHE A 362 ? 0.7191 0.9407 0.8709 -0.0238 0.0018  -0.0214 658 PHE A CE2 
2845 C CZ  . PHE A 362 ? 0.6454 0.8696 0.8082 -0.0378 -0.0015 -0.0219 658 PHE A CZ  
2846 N N   . ILE A 363 ? 0.6777 1.0627 0.8247 0.0672  0.0191  -0.0304 659 ILE A N   
2847 C CA  . ILE A 363 ? 0.6681 1.1143 0.8221 0.0583  0.0293  -0.0302 659 ILE A CA  
2848 C C   . ILE A 363 ? 0.7279 1.2653 0.9055 0.0574  0.0330  -0.0321 659 ILE A C   
2849 O O   . ILE A 363 ? 0.7411 1.3293 0.9353 0.0232  0.0381  -0.0309 659 ILE A O   
2850 C CB  . ILE A 363 ? 0.6904 1.1294 0.8178 0.0902  0.0343  -0.0315 659 ILE A CB  
2851 C CG1 . ILE A 363 ? 0.4902 0.8453 0.5942 0.0838  0.0302  -0.0297 659 ILE A CG1 
2852 C CG2 . ILE A 363 ? 0.6795 1.1976 0.8159 0.0840  0.0462  -0.0313 659 ILE A CG2 
2853 C CD1 . ILE A 363 ? 0.6718 1.0276 0.7794 0.0520  0.0355  -0.0265 659 ILE A CD1 
2854 N N   . LYS A 364 ? 0.7874 1.3441 0.9624 0.0934  0.0297  -0.0348 660 LYS A N   
2855 C CA  . LYS A 364 ? 0.8030 1.4513 1.0006 0.0969  0.0313  -0.0368 660 LYS A CA  
2856 C C   . LYS A 364 ? 0.7345 1.3918 0.9558 0.0517  0.0273  -0.0359 660 LYS A C   
2857 O O   . LYS A 364 ? 0.6446 1.3784 0.8852 0.0243  0.0315  -0.0363 660 LYS A O   
2858 C CB  . LYS A 364 ? 0.8727 1.5185 1.0551 0.1467  0.0261  -0.0393 660 LYS A CB  
2859 C CG  . LYS A 364 ? 0.9411 1.6953 1.1409 0.1662  0.0287  -0.0418 660 LYS A CG  
2860 C CD  . LYS A 364 ? 0.9532 1.7837 1.1502 0.1876  0.0393  -0.0429 660 LYS A CD  
2861 C CE  . LYS A 364 ? 1.0158 1.9243 1.2092 0.2077  0.0374  -0.0438 660 LYS A CE  
2862 N NZ  . LYS A 364 ? 1.0457 1.9152 1.2140 0.2527  0.0287  -0.0452 660 LYS A NZ  
2863 N N   . HIS A 365 ? 0.7745 1.3550 0.9911 0.0422  0.0191  -0.0350 661 HIS A N   
2864 C CA  . HIS A 365 ? 0.7741 1.3491 1.0048 0.0022  0.0152  -0.0347 661 HIS A CA  
2865 C C   . HIS A 365 ? 0.8064 1.3788 1.0347 -0.0404 0.0205  -0.0325 661 HIS A C   
2866 O O   . HIS A 365 ? 0.9191 1.5285 1.1552 -0.0762 0.0214  -0.0330 661 HIS A O   
2867 C CB  . HIS A 365 ? 0.7188 1.2120 0.9416 0.0043  0.0066  -0.0338 661 HIS A CB  
2868 C CG  . HIS A 365 ? 0.6887 1.1591 0.9167 -0.0325 0.0029  -0.0336 661 HIS A CG  
2869 N ND1 . HIS A 365 ? 0.6648 1.0616 0.8815 -0.0422 -0.0011 -0.0316 661 HIS A ND1 
2870 C CD2 . HIS A 365 ? 0.6205 1.1297 0.8586 -0.0595 0.0021  -0.0356 661 HIS A CD2 
2871 C CE1 . HIS A 365 ? 0.5959 0.9824 0.8124 -0.0695 -0.0037 -0.0325 661 HIS A CE1 
2872 N NE2 . HIS A 365 ? 0.6533 1.1026 0.8810 -0.0829 -0.0021 -0.0350 661 HIS A NE2 
2873 N N   . MET A 366 ? 0.7231 1.2485 0.9353 -0.0387 0.0235  -0.0300 662 MET A N   
2874 C CA  . MET A 366 ? 0.7482 1.2583 0.9498 -0.0768 0.0282  -0.0271 662 MET A CA  
2875 C C   . MET A 366 ? 0.6246 1.2211 0.8341 -0.1020 0.0369  -0.0270 662 MET A C   
2876 O O   . MET A 366 ? 0.6177 1.2092 0.8174 -0.1465 0.0387  -0.0252 662 MET A O   
2877 C CB  . MET A 366 ? 0.7991 1.2557 0.9820 -0.0642 0.0302  -0.0246 662 MET A CB  
2878 C CG  . MET A 366 ? 0.7956 1.1769 0.9607 -0.0879 0.0264  -0.0215 662 MET A CG  
2879 S SD  . MET A 366 ? 0.7440 1.0675 0.8895 -0.0672 0.0259  -0.0192 662 MET A SD  
2880 C CE  . MET A 366 ? 0.8841 1.1531 1.0050 -0.1026 0.0260  -0.0147 662 MET A CE  
2881 N N   . GLU A 367 ? 0.5339 1.2105 0.7566 -0.0749 0.0423  -0.0289 663 GLU A N   
2882 C CA  . GLU A 367 ? 0.6234 1.4010 0.8575 -0.0997 0.0508  -0.0287 663 GLU A CA  
2883 C C   . GLU A 367 ? 0.7419 1.5558 0.9871 -0.1384 0.0466  -0.0301 663 GLU A C   
2884 O O   . GLU A 367 ? 0.8743 1.7017 1.1102 -0.1904 0.0500  -0.0281 663 GLU A O   
2885 C CB  . GLU A 367 ? 0.7127 1.5789 0.9594 -0.0543 0.0561  -0.0313 663 GLU A CB  
2886 C CG  . GLU A 367 ? 0.8655 1.6868 1.0941 -0.0057 0.0579  -0.0316 663 GLU A CG  
2887 C CD  . GLU A 367 ? 0.9527 1.8354 1.1841 0.0507  0.0586  -0.0354 663 GLU A CD  
2888 O OE1 . GLU A 367 ? 0.9805 1.9082 1.2280 0.0586  0.0534  -0.0376 663 GLU A OE1 
2889 O OE2 . GLU A 367 ? 0.9035 1.7874 1.1168 0.0889  0.0641  -0.0362 663 GLU A OE2 
2890 N N   . ASN A 368 ? 0.7291 1.5554 0.9890 -0.1148 0.0387  -0.0336 664 ASN A N   
2891 C CA  . ASN A 368 ? 0.6124 1.4624 0.8741 -0.1436 0.0327  -0.0355 664 ASN A CA  
2892 C C   . ASN A 368 ? 0.6354 1.4187 0.8811 -0.1953 0.0295  -0.0345 664 ASN A C   
2893 O O   . ASN A 368 ? 0.7145 1.5045 0.9410 -0.2351 0.0283  -0.0344 664 ASN A O   
2894 C CB  . ASN A 368 ? 0.6008 1.4543 0.8754 -0.1038 0.0245  -0.0387 664 ASN A CB  
2895 C CG  . ASN A 368 ? 0.6270 1.5245 0.9042 -0.0466 0.0268  -0.0396 664 ASN A CG  
2896 O OD1 . ASN A 368 ? 0.7465 1.7058 1.0169 -0.0403 0.0319  -0.0391 664 ASN A OD1 
2897 N ND2 . ASN A 368 ? 0.5931 1.4545 0.8737 -0.0040 0.0223  -0.0409 664 ASN A ND2 
2898 N N   . GLU A 369 ? 0.6576 1.3392 0.8875 -0.1854 0.0261  -0.0329 665 GLU A N   
2899 C CA  . GLU A 369 ? 0.7092 1.3070 0.9092 -0.2235 0.0226  -0.0315 665 GLU A CA  
2900 C C   . GLU A 369 ? 0.9168 1.5168 1.0914 -0.2704 0.0301  -0.0280 665 GLU A C   
2901 O O   . GLU A 369 ? 1.0787 1.6521 1.2262 -0.3167 0.0281  -0.0280 665 GLU A O   
2902 C CB  . GLU A 369 ? 0.7419 1.2419 0.9294 -0.1959 0.0182  -0.0299 665 GLU A CB  
2903 C CG  . GLU A 369 ? 0.7992 1.2783 1.0008 -0.1645 0.0099  -0.0326 665 GLU A CG  
2904 C CD  . GLU A 369 ? 0.8401 1.2923 1.0308 -0.1891 0.0035  -0.0352 665 GLU A CD  
2905 O OE1 . GLU A 369 ? 1.0994 1.4776 1.2599 -0.2076 0.0015  -0.0339 665 GLU A OE1 
2906 O OE2 . GLU A 369 ? 0.6368 1.1407 0.8447 -0.1883 0.0002  -0.0386 665 GLU A OE2 
2907 N N   . TYR A 370 ? 0.9036 1.5268 1.0793 -0.2608 0.0387  -0.0248 666 TYR A N   
2908 C CA  . TYR A 370 ? 0.9091 1.5357 1.0575 -0.3079 0.0467  -0.0206 666 TYR A CA  
2909 C C   . TYR A 370 ? 0.9840 1.6920 1.1304 -0.3380 0.0489  -0.0214 666 TYR A C   
2910 O O   . TYR A 370 ? 0.9807 1.6640 1.0875 -0.3836 0.0508  -0.0186 666 TYR A O   
2911 C CB  . TYR A 370 ? 0.7439 1.3703 0.8900 -0.2865 0.0550  -0.0168 666 TYR A CB  
2912 C CG  . TYR A 370 ? 0.6957 1.2067 0.8137 -0.2732 0.0511  -0.0140 666 TYR A CG  
2913 C CD1 . TYR A 370 ? 0.7286 1.1990 0.8600 -0.2248 0.0449  -0.0159 666 TYR A CD1 
2914 C CD2 . TYR A 370 ? 0.7870 1.2296 0.8608 -0.3104 0.0530  -0.0094 666 TYR A CD2 
2915 C CE1 . TYR A 370 ? 0.8181 1.1966 0.9266 -0.2134 0.0405  -0.0134 666 TYR A CE1 
2916 C CE2 . TYR A 370 ? 0.8972 1.2415 0.9451 -0.2933 0.0484  -0.0069 666 TYR A CE2 
2917 C CZ  . TYR A 370 ? 0.9023 1.2213 0.9710 -0.2450 0.0421  -0.0091 666 TYR A CZ  
2918 O OH  . TYR A 370 ? 0.8737 1.1088 0.9195 -0.2287 0.0370  -0.0067 666 TYR A OH  
2919 N N   . ARG A 371 ? 1.0368 1.8222 1.2121 -0.3069 0.0464  -0.0251 667 ARG A N   
2920 C CA  . ARG A 371 ? 1.1679 2.0229 1.3342 -0.3264 0.0456  -0.0264 667 ARG A CA  
2921 C C   . ARG A 371 ? 1.2576 2.0803 1.4046 -0.3576 0.0371  -0.0289 667 ARG A C   
2922 O O   . ARG A 371 ? 1.3396 2.1255 1.4458 -0.4075 0.0370  -0.0273 667 ARG A O   
2923 C CB  . ARG A 371 ? 1.1976 2.1455 1.3950 -0.2770 0.0461  -0.0290 667 ARG A CB  
2924 C CG  . ARG A 371 ? 1.2551 2.2654 1.4542 -0.2633 0.0551  -0.0267 667 ARG A CG  
2925 C CD  . ARG A 371 ? 1.2652 2.3141 1.4893 -0.1962 0.0567  -0.0286 667 ARG A CD  
2926 N NE  . ARG A 371 ? 1.2668 2.3006 1.5068 -0.1610 0.0485  -0.0323 667 ARG A NE  
2927 C CZ  . ARG A 371 ? 1.2304 2.3162 1.4738 -0.1477 0.0426  -0.0351 667 ARG A CZ  
2928 N NH1 . ARG A 371 ? 1.2221 2.3845 1.4557 -0.1675 0.0434  -0.0350 667 ARG A NH1 
2929 N NH2 . ARG A 371 ? 1.2059 2.2680 1.4602 -0.1160 0.0355  -0.0377 667 ARG A NH2 
2930 N N   . CYS A 372 ? 1.2252 2.0549 1.3954 -0.3287 0.0299  -0.0329 668 CYS A N   
2931 C CA  A CYS A 372 ? 1.2582 2.0672 1.4123 -0.3534 0.0221  -0.0359 668 CYS A CA  
2932 C CA  B CYS A 372 ? 1.2592 2.0683 1.4127 -0.3542 0.0222  -0.0359 668 CYS A CA  
2933 C C   . CYS A 372 ? 1.2441 1.9435 1.3722 -0.3760 0.0172  -0.0361 668 CYS A C   
2934 O O   . CYS A 372 ? 1.3197 1.9926 1.4385 -0.3850 0.0098  -0.0395 668 CYS A O   
2935 C CB  A CYS A 372 ? 1.2339 2.0924 1.4198 -0.3121 0.0164  -0.0398 668 CYS A CB  
2936 C CB  B CYS A 372 ? 1.2367 2.0980 1.4214 -0.3141 0.0165  -0.0398 668 CYS A CB  
2937 S SG  A CYS A 372 ? 1.2423 2.2196 1.4317 -0.3103 0.0169  -0.0414 668 CYS A SG  
2938 S SG  B CYS A 372 ? 1.1880 1.9907 1.3993 -0.2703 0.0098  -0.0421 668 CYS A SG  
2939 N N   . ARG A 373 ? 1.1114 1.7456 1.2239 -0.3839 0.0209  -0.0328 669 ARG A N   
2940 C CA  . ARG A 373 ? 1.0479 1.5729 1.1266 -0.4024 0.0157  -0.0331 669 ARG A CA  
2941 C C   . ARG A 373 ? 1.0414 1.4990 1.0793 -0.4281 0.0212  -0.0280 669 ARG A C   
2942 O O   . ARG A 373 ? 1.0277 1.3871 1.0144 -0.4529 0.0174  -0.0274 669 ARG A O   
2943 C CB  . ARG A 373 ? 0.9577 1.4571 1.0687 -0.3631 0.0100  -0.0361 669 ARG A CB  
2944 C CG  . ARG A 373 ? 0.9762 1.3636 1.0471 -0.3679 0.0022  -0.0378 669 ARG A CG  
2945 C CD  . ARG A 373 ? 0.9161 1.2532 1.0033 -0.3123 -0.0018 -0.0376 669 ARG A CD  
2946 N NE  . ARG A 373 ? 0.9909 1.2401 1.0436 -0.3119 -0.0092 -0.0400 669 ARG A NE  
2947 C CZ  . ARG A 373 ? 0.8984 1.0928 0.9523 -0.2730 -0.0128 -0.0395 669 ARG A CZ  
2948 N NH1 . ARG A 373 ? 0.7259 0.9381 0.8116 -0.2361 -0.0106 -0.0366 669 ARG A NH1 
2949 N NH2 . ARG A 373 ? 0.8464 0.9700 0.8666 -0.2718 -0.0188 -0.0420 669 ARG A NH2 
2950 N N   . GLY A 374 ? 1.1158 1.6201 1.1699 -0.4195 0.0300  -0.0242 670 GLY A N   
2951 C CA  . GLY A 374 ? 1.1643 1.6114 1.1789 -0.4435 0.0361  -0.0185 670 GLY A CA  
2952 C C   . GLY A 374 ? 1.1286 1.4954 1.1384 -0.4141 0.0352  -0.0162 670 GLY A C   
2953 O O   . GLY A 374 ? 1.2228 1.5065 1.1824 -0.4329 0.0366  -0.0117 670 GLY A O   
2954 N N   . GLY A 375 ? 0.8839 1.2609 0.9339 -0.3586 0.0315  -0.0187 671 GLY A N   
2955 C CA  . GLY A 375 ? 0.5515 0.8489 0.5923 -0.3210 0.0283  -0.0167 671 GLY A CA  
2956 C C   . GLY A 375 ? 0.7320 1.0293 0.8073 -0.2737 0.0211  -0.0204 671 GLY A C   
2957 O O   . GLY A 375 ? 0.8959 1.2321 0.9936 -0.2703 0.0170  -0.0246 671 GLY A O   
2958 N N   . CYS A 376 ? 0.7917 1.0435 0.8681 -0.2389 0.0192  -0.0184 672 CYS A N   
2959 C CA  . CYS A 376 ? 0.7122 0.9549 0.8142 -0.1979 0.0125  -0.0208 672 CYS A CA  
2960 C C   . CYS A 376 ? 0.7788 0.9470 0.8607 -0.1790 0.0084  -0.0180 672 CYS A C   
2961 O O   . CYS A 376 ? 0.7964 0.9625 0.8809 -0.1630 0.0110  -0.0155 672 CYS A O   
2962 C CB  . CYS A 376 ? 0.6513 0.9609 0.7900 -0.1684 0.0154  -0.0221 672 CYS A CB  
2963 S SG  . CYS A 376 ? 0.6755 0.9725 0.8372 -0.1256 0.0073  -0.0245 672 CYS A SG  
2964 N N   . PRO A 377 ? 0.8530 0.9626 0.9132 -0.1781 0.0018  -0.0186 673 PRO A N   
2965 C CA  . PRO A 377 ? 0.8048 0.8584 0.8504 -0.1540 -0.0029 -0.0162 673 PRO A CA  
2966 C C   . PRO A 377 ? 0.7010 0.7828 0.7817 -0.1223 -0.0050 -0.0163 673 PRO A C   
2967 O O   . PRO A 377 ? 0.5496 0.6659 0.6583 -0.1108 -0.0069 -0.0192 673 PRO A O   
2968 C CB  . PRO A 377 ? 0.9296 0.9377 0.9546 -0.1514 -0.0096 -0.0184 673 PRO A CB  
2969 C CG  . PRO A 377 ? 0.7972 0.8467 0.8411 -0.1655 -0.0096 -0.0228 673 PRO A CG  
2970 C CD  . PRO A 377 ? 0.8597 0.9608 0.9117 -0.1924 -0.0023 -0.0223 673 PRO A CD  
2971 N N   . ALA A 378 ? 0.5608 0.6240 0.6345 -0.1096 -0.0050 -0.0132 674 ALA A N   
2972 C CA  . ALA A 378 ? 0.6345 0.7187 0.7322 -0.0857 -0.0069 -0.0135 674 ALA A CA  
2973 C C   . ALA A 378 ? 0.6763 0.7246 0.7594 -0.0726 -0.0114 -0.0105 674 ALA A C   
2974 O O   . ALA A 378 ? 0.6273 0.6497 0.6854 -0.0803 -0.0091 -0.0076 674 ALA A O   
2975 C CB  . ALA A 378 ? 0.6279 0.7572 0.7382 -0.0858 0.0003  -0.0142 674 ALA A CB  
2976 N N   . ASP A 379 ? 0.5548 0.6037 0.6513 -0.0549 -0.0178 -0.0108 675 ASP A N   
2977 C CA  . ASP A 379 ? 0.5173 0.5441 0.6029 -0.0438 -0.0235 -0.0082 675 ASP A CA  
2978 C C   . ASP A 379 ? 0.5880 0.6278 0.6809 -0.0368 -0.0237 -0.0085 675 ASP A C   
2979 O O   . ASP A 379 ? 0.5360 0.5885 0.6425 -0.0302 -0.0269 -0.0100 675 ASP A O   
2980 C CB  . ASP A 379 ? 0.4842 0.5063 0.5743 -0.0327 -0.0311 -0.0081 675 ASP A CB  
2981 C CG  . ASP A 379 ? 0.6225 0.6336 0.7015 -0.0212 -0.0377 -0.0052 675 ASP A CG  
2982 O OD1 . ASP A 379 ? 0.6062 0.6119 0.6786 -0.0100 -0.0428 -0.0044 675 ASP A OD1 
2983 O OD2 . ASP A 379 ? 0.7177 0.7283 0.7925 -0.0216 -0.0380 -0.0041 675 ASP A OD2 
2984 N N   . TRP A 380 ? 0.5367 0.5670 0.6141 -0.0390 -0.0203 -0.0071 676 TRP A N   
2985 C CA  . TRP A 380 ? 0.4885 0.5218 0.5627 -0.0315 -0.0203 -0.0079 676 TRP A CA  
2986 C C   . TRP A 380 ? 0.5205 0.5440 0.5941 -0.0250 -0.0301 -0.0076 676 TRP A C   
2987 O O   . TRP A 380 ? 0.6416 0.6643 0.7126 -0.0207 -0.0320 -0.0094 676 TRP A O   
2988 C CB  . TRP A 380 ? 0.4704 0.4910 0.5238 -0.0355 -0.0156 -0.0058 676 TRP A CB  
2989 C CG  . TRP A 380 ? 0.6359 0.6596 0.6799 -0.0275 -0.0126 -0.0075 676 TRP A CG  
2990 C CD1 . TRP A 380 ? 0.4259 0.4716 0.4678 -0.0263 -0.0028 -0.0089 676 TRP A CD1 
2991 C CD2 . TRP A 380 ? 0.6519 0.6563 0.6825 -0.0196 -0.0196 -0.0082 676 TRP A CD2 
2992 N NE1 . TRP A 380 ? 0.5071 0.5435 0.5329 -0.0136 -0.0028 -0.0107 676 TRP A NE1 
2993 C CE2 . TRP A 380 ? 0.6095 0.6157 0.6258 -0.0115 -0.0134 -0.0105 676 TRP A CE2 
2994 C CE3 . TRP A 380 ? 0.4308 0.4205 0.4580 -0.0199 -0.0306 -0.0073 676 TRP A CE3 
2995 C CZ2 . TRP A 380 ? 0.6210 0.6025 0.6140 -0.0040 -0.0184 -0.0124 676 TRP A CZ2 
2996 C CZ3 . TRP A 380 ? 0.5935 0.5661 0.6015 -0.0174 -0.0358 -0.0088 676 TRP A CZ3 
2997 C CH2 . TRP A 380 ? 0.6224 0.5849 0.6107 -0.0098 -0.0300 -0.0115 676 TRP A CH2 
2998 N N   . VAL A 381 ? 0.5511 0.5668 0.6218 -0.0242 -0.0366 -0.0051 677 VAL A N   
2999 C CA  . VAL A 381 ? 0.3906 0.4101 0.4618 -0.0222 -0.0460 -0.0044 677 VAL A CA  
3000 C C   . VAL A 381 ? 0.5381 0.5709 0.6236 -0.0245 -0.0481 -0.0061 677 VAL A C   
3001 O O   . VAL A 381 ? 0.4330 0.4630 0.5114 -0.0293 -0.0535 -0.0063 677 VAL A O   
3002 C CB  . VAL A 381 ? 0.5557 0.5779 0.6235 -0.0159 -0.0524 -0.0016 677 VAL A CB  
3003 C CG1 . VAL A 381 ? 0.5342 0.5769 0.6066 -0.0171 -0.0620 -0.0008 677 VAL A CG1 
3004 C CG2 . VAL A 381 ? 0.5791 0.5789 0.6234 -0.0122 -0.0511 0.0007  677 VAL A CG2 
3005 N N   . TRP A 382 ? 0.6020 0.6449 0.7022 -0.0235 -0.0441 -0.0072 678 TRP A N   
3006 C CA  . TRP A 382 ? 0.4663 0.5204 0.5784 -0.0246 -0.0455 -0.0082 678 TRP A CA  
3007 C C   . TRP A 382 ? 0.6040 0.6553 0.7137 -0.0212 -0.0400 -0.0108 678 TRP A C   
3008 O O   . TRP A 382 ? 0.5878 0.6356 0.6944 -0.0205 -0.0423 -0.0113 678 TRP A O   
3009 C CB  . TRP A 382 ? 0.4921 0.5601 0.6193 -0.0226 -0.0453 -0.0082 678 TRP A CB  
3010 C CG  . TRP A 382 ? 0.5646 0.6461 0.6950 -0.0200 -0.0523 -0.0059 678 TRP A CG  
3011 C CD1 . TRP A 382 ? 0.6622 0.7436 0.7833 -0.0140 -0.0563 -0.0039 678 TRP A CD1 
3012 C CD2 . TRP A 382 ? 0.5715 0.6755 0.7142 -0.0214 -0.0559 -0.0051 678 TRP A CD2 
3013 N NE1 . TRP A 382 ? 0.6405 0.7500 0.7695 -0.0095 -0.0623 -0.0022 678 TRP A NE1 
3014 C CE2 . TRP A 382 ? 0.6733 0.7981 0.8163 -0.0159 -0.0617 -0.0029 678 TRP A CE2 
3015 C CE3 . TRP A 382 ? 0.6106 0.7213 0.7619 -0.0260 -0.0547 -0.0058 678 TRP A CE3 
3016 C CZ2 . TRP A 382 ? 0.6491 0.8084 0.8037 -0.0163 -0.0654 -0.0013 678 TRP A CZ2 
3017 C CZ3 . TRP A 382 ? 0.7287 0.8650 0.8889 -0.0286 -0.0584 -0.0040 678 TRP A CZ3 
3018 C CH2 . TRP A 382 ? 0.6649 0.8285 0.8280 -0.0248 -0.0634 -0.0018 678 TRP A CH2 
3019 N N   . ILE A 383 ? 0.4205 0.4753 0.5283 -0.0184 -0.0326 -0.0122 679 ILE A N   
3020 C CA  . ILE A 383 ? 0.5049 0.5698 0.6117 -0.0097 -0.0273 -0.0149 679 ILE A CA  
3021 C C   . ILE A 383 ? 0.6358 0.6770 0.7169 -0.0005 -0.0289 -0.0159 679 ILE A C   
3022 O O   . ILE A 383 ? 0.6316 0.6650 0.7014 0.0103  -0.0293 -0.0175 679 ILE A O   
3023 C CB  . ILE A 383 ? 0.4441 0.5331 0.5577 -0.0120 -0.0186 -0.0158 679 ILE A CB  
3024 C CG1 . ILE A 383 ? 0.5747 0.6771 0.7037 -0.0237 -0.0179 -0.0156 679 ILE A CG1 
3025 C CG2 . ILE A 383 ? 0.5754 0.6876 0.6873 0.0019  -0.0129 -0.0186 679 ILE A CG2 
3026 C CD1 . ILE A 383 ? 0.6678 0.7851 0.8116 -0.0198 -0.0203 -0.0172 679 ILE A CD1 
3027 N N   . VAL A 384 ? 0.5823 0.6056 0.6474 -0.0034 -0.0304 -0.0152 680 VAL A N   
3028 C CA  . VAL A 384 ? 0.5118 0.5040 0.5441 0.0039  -0.0324 -0.0169 680 VAL A CA  
3029 C C   . VAL A 384 ? 0.5823 0.5474 0.5979 -0.0025 -0.0411 -0.0164 680 VAL A C   
3030 O O   . VAL A 384 ? 0.7168 0.6858 0.7415 -0.0184 -0.0480 -0.0138 680 VAL A O   
3031 C CB  . VAL A 384 ? 0.5396 0.5187 0.5585 -0.0016 -0.0338 -0.0159 680 VAL A CB  
3032 C CG1 . VAL A 384 ? 0.6122 0.5533 0.5910 0.0052  -0.0365 -0.0185 680 VAL A CG1 
3033 C CG2 . VAL A 384 ? 0.6292 0.6310 0.6584 0.0009  -0.0246 -0.0155 680 VAL A CG2 
3034 N N   . PRO A 385 ? 0.6481 0.5852 0.6345 0.0091  -0.0413 -0.0185 681 PRO A N   
3035 C CA  . PRO A 385 ? 0.6279 0.5318 0.5904 -0.0027 -0.0495 -0.0172 681 PRO A CA  
3036 C C   . PRO A 385 ? 0.8615 0.7405 0.8012 -0.0231 -0.0577 -0.0162 681 PRO A C   
3037 O O   . PRO A 385 ? 0.8947 0.7629 0.8203 -0.0198 -0.0570 -0.0179 681 PRO A O   
3038 C CB  . PRO A 385 ? 0.7022 0.5675 0.6231 0.0193  -0.0475 -0.0201 681 PRO A CB  
3039 C CG  . PRO A 385 ? 0.6861 0.5920 0.6306 0.0434  -0.0377 -0.0223 681 PRO A CG  
3040 C CD  . PRO A 385 ? 0.6858 0.6229 0.6570 0.0350  -0.0339 -0.0218 681 PRO A CD  
3041 N N   . PRO A 386 ? 0.7089 0.5817 0.6427 -0.0460 -0.0657 -0.0135 682 PRO A N   
3042 C CA  . PRO A 386 ? 0.7196 0.5850 0.6374 -0.0707 -0.0748 -0.0121 682 PRO A CA  
3043 C C   . PRO A 386 ? 0.8851 0.6848 0.7395 -0.0783 -0.0800 -0.0146 682 PRO A C   
3044 O O   . PRO A 386 ? 0.8450 0.6348 0.6784 -0.1061 -0.0892 -0.0135 682 PRO A O   
3045 C CB  . PRO A 386 ? 0.7386 0.6322 0.6742 -0.0932 -0.0801 -0.0081 682 PRO A CB  
3046 C CG  . PRO A 386 ? 0.6489 0.5222 0.5754 -0.0836 -0.0761 -0.0081 682 PRO A CG  
3047 C CD  . PRO A 386 ? 0.6040 0.4708 0.5346 -0.0512 -0.0671 -0.0116 682 PRO A CD  
3048 N N   . MET A 387 ? 0.9245 0.6799 0.7440 -0.0538 -0.0748 -0.0182 683 MET A N   
3049 C CA  . MET A 387 ? 0.8545 0.5412 0.6076 -0.0520 -0.0783 -0.0219 683 MET A CA  
3050 C C   . MET A 387 ? 0.9276 0.6070 0.6721 -0.0117 -0.0683 -0.0261 683 MET A C   
3051 O O   . MET A 387 ? 0.9041 0.6235 0.6847 0.0105  -0.0599 -0.0259 683 MET A O   
3052 C CB  . MET A 387 ? 0.9895 0.6057 0.6786 -0.0671 -0.0852 -0.0215 683 MET A CB  
3053 C CG  . MET A 387 ? 0.9667 0.5543 0.6350 -0.0374 -0.0795 -0.0223 683 MET A CG  
3054 S SD  . MET A 387 ? 1.2871 0.7785 0.8685 -0.0577 -0.0882 -0.0206 683 MET A SD  
3055 C CE  . MET A 387 ? 1.1534 0.5449 0.6396 -0.0420 -0.0913 -0.0269 683 MET A CE  
3056 N N   . SER A 388 ? 0.9403 0.5716 0.6345 -0.0033 -0.0694 -0.0302 684 SER A N   
3057 C CA  . SER A 388 ? 0.9112 0.5329 0.5855 0.0375  -0.0599 -0.0347 684 SER A CA  
3058 C C   . SER A 388 ? 0.9208 0.6241 0.6629 0.0527  -0.0489 -0.0335 684 SER A C   
3059 O O   . SER A 388 ? 0.9764 0.7019 0.7237 0.0845  -0.0395 -0.0355 684 SER A O   
3060 C CB  . SER A 388 ? 0.9433 0.5146 0.5676 0.0650  -0.0585 -0.0369 684 SER A CB  
3061 O OG  . SER A 388 ? 1.1005 0.5853 0.6529 0.0448  -0.0692 -0.0373 684 SER A OG  
3062 N N   . GLY A 389 ? 0.8631 0.6112 0.6525 0.0294  -0.0504 -0.0300 685 GLY A N   
3063 C CA  . GLY A 389 ? 0.8261 0.6408 0.6723 0.0356  -0.0413 -0.0280 685 GLY A CA  
3064 C C   . GLY A 389 ? 0.8670 0.7005 0.7087 0.0637  -0.0297 -0.0309 685 GLY A C   
3065 O O   . GLY A 389 ? 0.7946 0.6756 0.6673 0.0765  -0.0212 -0.0306 685 GLY A O   
3066 N N   . SER A 390 ? 0.8430 0.6448 0.6455 0.0724  -0.0292 -0.0339 686 SER A N   
3067 C CA  . SER A 390 ? 0.8847 0.7179 0.6885 0.0963  -0.0170 -0.0358 686 SER A CA  
3068 C C   . SER A 390 ? 0.9867 0.8087 0.7544 0.1355  -0.0108 -0.0406 686 SER A C   
3069 O O   . SER A 390 ? 1.0705 0.9344 0.8434 0.1581  0.0005  -0.0422 686 SER A O   
3070 C CB  . SER A 390 ? 1.0017 0.8165 0.7845 0.0898  -0.0175 -0.0364 686 SER A CB  
3071 O OG  . SER A 390 ? 1.0003 0.7443 0.7259 0.0877  -0.0273 -0.0398 686 SER A OG  
3072 N N   . ILE A 391 ? 1.0841 0.8536 0.8125 0.1458  -0.0176 -0.0427 687 ILE A N   
3073 C CA  . ILE A 391 ? 1.0252 0.7882 0.7195 0.1894  -0.0119 -0.0467 687 ILE A CA  
3074 C C   . ILE A 391 ? 0.9878 0.8087 0.7262 0.1973  -0.0080 -0.0445 687 ILE A C   
3075 O O   . ILE A 391 ? 1.0847 0.9108 0.7993 0.2362  -0.0039 -0.0474 687 ILE A O   
3076 C CB  . ILE A 391 ? 1.1868 0.8478 0.7967 0.2032  -0.0208 -0.0504 687 ILE A CB  
3077 C CG1 . ILE A 391 ? 1.1606 0.7851 0.7676 0.1769  -0.0313 -0.0471 687 ILE A CG1 
3078 C CG2 . ILE A 391 ? 1.2900 0.8898 0.8497 0.1930  -0.0257 -0.0534 687 ILE A CG2 
3079 C CD1 . ILE A 391 ? 1.2079 0.7242 0.7229 0.1854  -0.0401 -0.0500 687 ILE A CD1 
3080 N N   . THR A 392 ? 0.8698 0.7367 0.6710 0.1630  -0.0096 -0.0397 688 THR A N   
3081 C CA  . THR A 392 ? 0.9360 0.8704 0.7874 0.1643  -0.0048 -0.0378 688 THR A CA  
3082 C C   . THR A 392 ? 0.8949 0.9064 0.7938 0.1550  0.0053  -0.0363 688 THR A C   
3083 O O   . THR A 392 ? 0.8537 0.8619 0.7581 0.1359  0.0063  -0.0348 688 THR A O   
3084 C CB  . THR A 392 ? 0.8364 0.7643 0.7164 0.1335  -0.0129 -0.0339 688 THR A CB  
3085 O OG1 . THR A 392 ? 0.7294 0.6690 0.6405 0.1002  -0.0149 -0.0307 688 THR A OG1 
3086 C CG2 . THR A 392 ? 0.8635 0.7140 0.6943 0.1324  -0.0232 -0.0340 688 THR A CG2 
3087 N N   . PRO A 393 ? 0.8521 0.9338 0.7823 0.1660  0.0126  -0.0365 689 PRO A N   
3088 C CA  . PRO A 393 ? 0.8488 1.0029 0.8145 0.1535  0.0230  -0.0350 689 PRO A CA  
3089 C C   . PRO A 393 ? 0.8016 0.9634 0.8038 0.1105  0.0210  -0.0305 689 PRO A C   
3090 O O   . PRO A 393 ? 0.8843 1.0802 0.9002 0.0943  0.0284  -0.0285 689 PRO A O   
3091 C CB  . PRO A 393 ? 0.9485 1.1769 0.9343 0.1741  0.0292  -0.0366 689 PRO A CB  
3092 C CG  . PRO A 393 ? 0.9239 1.1186 0.9040 0.1816  0.0200  -0.0369 689 PRO A CG  
3093 C CD  . PRO A 393 ? 0.8997 0.9996 0.8284 0.1909  0.0118  -0.0380 689 PRO A CD  
3094 N N   . VAL A 394 ? 0.6738 0.8043 0.6874 0.0927  0.0118  -0.0286 690 VAL A N   
3095 C CA  . VAL A 394 ? 0.6826 0.8190 0.7243 0.0588  0.0101  -0.0247 690 VAL A CA  
3096 C C   . VAL A 394 ? 0.7970 0.8944 0.8230 0.0455  0.0075  -0.0226 690 VAL A C   
3097 O O   . VAL A 394 ? 0.6307 0.7310 0.6705 0.0227  0.0076  -0.0192 690 VAL A O   
3098 C CB  . VAL A 394 ? 0.6903 0.8132 0.7491 0.0475  0.0019  -0.0236 690 VAL A CB  
3099 C CG1 . VAL A 394 ? 0.5368 0.7035 0.6132 0.0579  0.0045  -0.0254 690 VAL A CG1 
3100 C CG2 . VAL A 394 ? 0.8432 0.9089 0.8775 0.0519  -0.0079 -0.0237 690 VAL A CG2 
3101 N N   . PHE A 395 ? 0.7645 0.8218 0.7563 0.0601  0.0046  -0.0246 691 PHE A N   
3102 C CA  . PHE A 395 ? 0.5477 0.5738 0.5245 0.0476  0.0014  -0.0228 691 PHE A CA  
3103 C C   . PHE A 395 ? 0.7604 0.8188 0.7434 0.0406  0.0117  -0.0208 691 PHE A C   
3104 O O   . PHE A 395 ? 0.8353 0.8801 0.8183 0.0227  0.0099  -0.0172 691 PHE A O   
3105 C CB  . PHE A 395 ? 0.7749 0.7513 0.7077 0.0630  -0.0034 -0.0262 691 PHE A CB  
3106 C CG  . PHE A 395 ? 0.7031 0.6495 0.6182 0.0505  -0.0080 -0.0248 691 PHE A CG  
3107 C CD1 . PHE A 395 ? 0.7400 0.6561 0.6520 0.0326  -0.0201 -0.0231 691 PHE A CD1 
3108 C CD2 . PHE A 395 ? 0.7811 0.7359 0.6828 0.0564  -0.0002 -0.0250 691 PHE A CD2 
3109 C CE1 . PHE A 395 ? 0.6985 0.5943 0.5948 0.0220  -0.0255 -0.0219 691 PHE A CE1 
3110 C CE2 . PHE A 395 ? 0.8066 0.7335 0.6904 0.0457  -0.0050 -0.0236 691 PHE A CE2 
3111 C CZ  . PHE A 395 ? 0.8057 0.7034 0.6868 0.0294  -0.0182 -0.0222 691 PHE A CZ  
3112 N N   . PHE A 396 ? 0.7190 0.8230 0.7048 0.0548  0.0224  -0.0226 692 PHE A N   
3113 C CA  . PHE A 396 ? 0.7661 0.9085 0.7535 0.0473  0.0339  -0.0207 692 PHE A CA  
3114 C C   . PHE A 396 ? 0.7290 0.9202 0.7464 0.0218  0.0398  -0.0173 692 PHE A C   
3115 O O   . PHE A 396 ? 0.7473 0.9776 0.7653 0.0095  0.0503  -0.0151 692 PHE A O   
3116 C CB  . PHE A 396 ? 0.9156 1.0889 0.8849 0.0787  0.0429  -0.0248 692 PHE A CB  
3117 C CG  . PHE A 396 ? 0.8718 0.9865 0.7995 0.1057  0.0369  -0.0291 692 PHE A CG  
3118 C CD1 . PHE A 396 ? 0.9901 1.0659 0.8888 0.1036  0.0359  -0.0289 692 PHE A CD1 
3119 C CD2 . PHE A 396 ? 0.6967 0.7899 0.6075 0.1319  0.0317  -0.0333 692 PHE A CD2 
3120 C CE1 . PHE A 396 ? 0.9487 0.9648 0.8018 0.1249  0.0295  -0.0335 692 PHE A CE1 
3121 C CE2 . PHE A 396 ? 0.8349 0.8617 0.6951 0.1536  0.0256  -0.0374 692 PHE A CE2 
3122 C CZ  . PHE A 396 ? 0.8298 0.8176 0.6609 0.1485  0.0242  -0.0378 692 PHE A CZ  
3123 N N   . GLN A 397 ? 0.7437 0.9324 0.7820 0.0113  0.0335  -0.0170 693 GLN A N   
3124 C CA  . GLN A 397 ? 0.7601 0.9871 0.8202 -0.0143 0.0376  -0.0147 693 GLN A CA  
3125 C C   . GLN A 397 ? 0.6250 0.8067 0.6788 -0.0407 0.0324  -0.0104 693 GLN A C   
3126 O O   . GLN A 397 ? 0.5337 0.6742 0.5882 -0.0377 0.0222  -0.0103 693 GLN A O   
3127 C CB  . GLN A 397 ? 0.7193 0.9724 0.8016 -0.0065 0.0340  -0.0176 693 GLN A CB  
3128 C CG  . GLN A 397 ? 0.7907 1.0839 0.8923 -0.0350 0.0373  -0.0162 693 GLN A CG  
3129 C CD  . GLN A 397 ? 0.7723 1.1361 0.8779 -0.0473 0.0496  -0.0155 693 GLN A CD  
3130 O OE1 . GLN A 397 ? 0.6084 1.0288 0.7205 -0.0231 0.0553  -0.0185 693 GLN A OE1 
3131 N NE2 . GLN A 397 ? 0.8437 1.2049 0.9407 -0.0848 0.0539  -0.0114 693 GLN A NE2 
3132 N N   . GLU A 398 ? 0.7218 0.9107 0.7645 -0.0652 0.0396  -0.0065 694 GLU A N   
3133 C CA  . GLU A 398 ? 0.8130 0.9564 0.8411 -0.0890 0.0355  -0.0023 694 GLU A CA  
3134 C C   . GLU A 398 ? 0.8034 0.9534 0.8464 -0.1023 0.0319  -0.0034 694 GLU A C   
3135 O O   . GLU A 398 ? 0.8045 1.0063 0.8622 -0.1146 0.0378  -0.0049 694 GLU A O   
3136 C CB  . GLU A 398 ? 0.7690 0.9131 0.7725 -0.1153 0.0447  0.0026  694 GLU A CB  
3137 C CG  . GLU A 398 ? 0.7882 0.9204 0.7724 -0.1035 0.0483  0.0043  694 GLU A CG  
3138 C CD  . GLU A 398 ? 0.8456 0.9836 0.8040 -0.1318 0.0590  0.0097  694 GLU A CD  
3139 O OE1 . GLU A 398 ? 0.8965 1.0315 0.8386 -0.1233 0.0636  0.0111  694 GLU A OE1 
3140 O OE2 . GLU A 398 ? 0.8810 1.0232 0.8308 -0.1645 0.0628  0.0127  694 GLU A OE2 
3141 N N   . MET A 399 ? 0.7692 0.8713 0.8073 -0.0993 0.0220  -0.0028 695 MET A N   
3142 C CA  . MET A 399 ? 0.7961 0.8943 0.8419 -0.1097 0.0180  -0.0041 695 MET A CA  
3143 C C   . MET A 399 ? 0.8257 0.8658 0.8375 -0.1257 0.0148  -0.0005 695 MET A C   
3144 O O   . MET A 399 ? 0.8914 0.8893 0.8811 -0.1166 0.0111  0.0026  695 MET A O   
3145 C CB  . MET A 399 ? 0.6195 0.7168 0.6880 -0.0865 0.0093  -0.0074 695 MET A CB  
3146 C CG  . MET A 399 ? 0.5715 0.7104 0.6612 -0.0671 0.0113  -0.0109 695 MET A CG  
3147 S SD  . MET A 399 ? 0.6111 0.7288 0.7099 -0.0427 0.0010  -0.0128 695 MET A SD  
3148 C CE  . MET A 399 ? 0.5774 0.7195 0.6749 -0.0193 0.0050  -0.0159 695 MET A CE  
3149 N N   . LEU A 400 ? 0.8307 0.8675 0.8328 -0.1493 0.0161  -0.0009 696 LEU A N   
3150 C CA  . LEU A 400 ? 0.8581 0.8296 0.8185 -0.1625 0.0123  0.0015  696 LEU A CA  
3151 C C   . LEU A 400 ? 0.8740 0.8308 0.8456 -0.1453 0.0035  -0.0019 696 LEU A C   
3152 O O   . LEU A 400 ? 0.7409 0.7358 0.7394 -0.1490 0.0035  -0.0058 696 LEU A O   
3153 C CB  . LEU A 400 ? 0.8792 0.8496 0.8123 -0.2040 0.0190  0.0028  696 LEU A CB  
3154 C CG  . LEU A 400 ? 1.0034 0.9529 0.8996 -0.2257 0.0263  0.0084  696 LEU A CG  
3155 C CD1 . LEU A 400 ? 1.1028 1.0515 0.9676 -0.2744 0.0327  0.0100  696 LEU A CD1 
3156 C CD2 . LEU A 400 ? 1.0388 0.9065 0.8925 -0.2085 0.0198  0.0122  696 LEU A CD2 
3157 N N   . ASN A 401 ? 0.8993 0.8074 0.8507 -0.1246 -0.0040 -0.0004 697 ASN A N   
3158 C CA  . ASN A 401 ? 0.7211 0.6168 0.6784 -0.1070 -0.0117 -0.0031 697 ASN A CA  
3159 C C   . ASN A 401 ? 0.8357 0.6678 0.7409 -0.1179 -0.0135 -0.0027 697 ASN A C   
3160 O O   . ASN A 401 ? 0.7886 0.5647 0.6448 -0.1206 -0.0135 0.0012  697 ASN A O   
3161 C CB  . ASN A 401 ? 0.7353 0.6291 0.7038 -0.0747 -0.0192 -0.0022 697 ASN A CB  
3162 C CG  . ASN A 401 ? 0.7507 0.6646 0.7450 -0.0579 -0.0250 -0.0054 697 ASN A CG  
3163 O OD1 . ASN A 401 ? 0.6642 0.5963 0.6734 -0.0679 -0.0232 -0.0087 697 ASN A OD1 
3164 N ND2 . ASN A 401 ? 0.7073 0.6233 0.7068 -0.0335 -0.0320 -0.0043 697 ASN A ND2 
3165 N N   . TYR A 402 ? 0.8516 0.6866 0.7610 -0.1232 -0.0153 -0.0069 698 TYR A N   
3166 C CA  . TYR A 402 ? 0.8365 0.6039 0.6905 -0.1309 -0.0181 -0.0078 698 TYR A CA  
3167 C C   . TYR A 402 ? 0.8732 0.6585 0.7481 -0.1218 -0.0221 -0.0131 698 TYR A C   
3168 O O   . TYR A 402 ? 0.7629 0.6135 0.6923 -0.1192 -0.0213 -0.0156 698 TYR A O   
3169 C CB  . TYR A 402 ? 0.9277 0.6660 0.7393 -0.1754 -0.0121 -0.0063 698 TYR A CB  
3170 C CG  . TYR A 402 ? 1.0079 0.8207 0.8605 -0.2068 -0.0053 -0.0081 698 TYR A CG  
3171 C CD1 . TYR A 402 ? 0.9938 0.8336 0.8604 -0.2230 -0.0064 -0.0131 698 TYR A CD1 
3172 C CD2 . TYR A 402 ? 1.0465 0.9062 0.9214 -0.2180 0.0020  -0.0050 698 TYR A CD2 
3173 C CE1 . TYR A 402 ? 0.9645 0.8814 0.8679 -0.2482 -0.0009 -0.0148 698 TYR A CE1 
3174 C CE2 . TYR A 402 ? 1.0326 0.9689 0.9430 -0.2411 0.0083  -0.0068 698 TYR A CE2 
3175 C CZ  . TYR A 402 ? 1.0140 0.9812 0.9393 -0.2558 0.0066  -0.0116 698 TYR A CZ  
3176 O OH  . TYR A 402 ? 0.9251 0.9771 0.8857 -0.2750 0.0122  -0.0134 698 TYR A OH  
3177 N N   . ARG A 403 ? 0.9427 0.6645 0.7682 -0.1135 -0.0267 -0.0149 699 ARG A N   
3178 C CA  . ARG A 403 ? 1.1021 0.8316 0.9392 -0.0962 -0.0312 -0.0197 699 ARG A CA  
3179 C C   . ARG A 403 ? 1.1242 0.8302 0.9331 -0.1298 -0.0303 -0.0241 699 ARG A C   
3180 O O   . ARG A 403 ? 1.1131 0.7393 0.8513 -0.1426 -0.0316 -0.0245 699 ARG A O   
3181 C CB  . ARG A 403 ? 1.2440 0.9249 1.0445 -0.0560 -0.0372 -0.0194 699 ARG A CB  
3182 C CG  . ARG A 403 ? 1.2335 0.9405 1.0567 -0.0269 -0.0392 -0.0149 699 ARG A CG  
3183 C CD  . ARG A 403 ? 1.3276 1.0822 1.1889 0.0078  -0.0438 -0.0162 699 ARG A CD  
3184 N NE  . ARG A 403 ? 1.5229 1.2318 1.3361 0.0429  -0.0489 -0.0170 699 ARG A NE  
3185 C CZ  . ARG A 403 ? 1.5277 1.2752 1.3619 0.0764  -0.0528 -0.0179 699 ARG A CZ  
3186 N NH1 . ARG A 403 ? 1.4004 1.2259 1.3001 0.0739  -0.0525 -0.0177 699 ARG A NH1 
3187 N NH2 . ARG A 403 ? 1.6012 1.3083 1.3858 0.1130  -0.0570 -0.0188 699 ARG A NH2 
3188 N N   . LEU A 404 ? 1.0680 0.8406 0.9268 -0.1445 -0.0285 -0.0272 700 LEU A N   
3189 C CA  . LEU A 404 ? 1.0622 0.8287 0.9035 -0.1749 -0.0291 -0.0321 700 LEU A CA  
3190 C C   . LEU A 404 ? 1.0782 0.8525 0.9341 -0.1502 -0.0340 -0.0369 700 LEU A C   
3191 O O   . LEU A 404 ? 1.0174 0.8188 0.9076 -0.1143 -0.0358 -0.0359 700 LEU A O   
3192 C CB  . LEU A 404 ? 1.0416 0.8849 0.9258 -0.2076 -0.0241 -0.0325 700 LEU A CB  
3193 C CG  . LEU A 404 ? 0.9867 0.8404 0.8638 -0.2334 -0.0176 -0.0278 700 LEU A CG  
3194 C CD1 . LEU A 404 ? 0.9539 0.8977 0.8759 -0.2591 -0.0128 -0.0289 700 LEU A CD1 
3195 C CD2 . LEU A 404 ? 1.1066 0.8737 0.9041 -0.2643 -0.0175 -0.0263 700 LEU A CD2 
3196 N N   . THR A 405 ? 1.1415 0.8930 0.9684 -0.1731 -0.0362 -0.0421 701 THR A N   
3197 C CA  . THR A 405 ? 1.0157 0.7636 0.8445 -0.1519 -0.0407 -0.0471 701 THR A CA  
3198 C C   . THR A 405 ? 0.9720 0.7575 0.8148 -0.1853 -0.0415 -0.0520 701 THR A C   
3199 O O   . THR A 405 ? 0.9679 0.7450 0.7847 -0.2288 -0.0402 -0.0526 701 THR A O   
3200 C CB  . THR A 405 ? 1.1427 0.7916 0.8933 -0.1345 -0.0449 -0.0494 701 THR A CB  
3201 O OG1 . THR A 405 ? 0.9882 0.6407 0.7439 -0.1071 -0.0484 -0.0540 701 THR A OG1 
3202 C CG2 . THR A 405 ? 1.3028 0.8757 0.9775 -0.1773 -0.0459 -0.0519 701 THR A CG2 
3203 N N   . PRO A 406 ? 0.8473 0.6797 0.7304 -0.1683 -0.0437 -0.0551 702 PRO A N   
3204 C CA  . PRO A 406 ? 0.7201 0.5729 0.6348 -0.1248 -0.0451 -0.0545 702 PRO A CA  
3205 C C   . PRO A 406 ? 0.7892 0.6853 0.7508 -0.1017 -0.0421 -0.0484 702 PRO A C   
3206 O O   . PRO A 406 ? 0.7313 0.6594 0.7161 -0.1167 -0.0386 -0.0451 702 PRO A O   
3207 C CB  . PRO A 406 ? 0.7587 0.6658 0.7089 -0.1303 -0.0468 -0.0584 702 PRO A CB  
3208 C CG  . PRO A 406 ? 0.6686 0.5556 0.5829 -0.1710 -0.0489 -0.0633 702 PRO A CG  
3209 C CD  . PRO A 406 ? 0.7670 0.6353 0.6587 -0.2000 -0.0455 -0.0600 702 PRO A CD  
3210 N N   . SER A 407 ? 0.7159 0.6138 0.6878 -0.0663 -0.0436 -0.0470 703 SER A N   
3211 C CA  . SER A 407 ? 0.7559 0.6800 0.7569 -0.0469 -0.0422 -0.0413 703 SER A CA  
3212 C C   . SER A 407 ? 0.7489 0.7035 0.7755 -0.0168 -0.0439 -0.0402 703 SER A C   
3213 O O   . SER A 407 ? 0.7809 0.7199 0.7889 -0.0020 -0.0458 -0.0435 703 SER A O   
3214 C CB  . SER A 407 ? 0.8109 0.6816 0.7699 -0.0404 -0.0423 -0.0387 703 SER A CB  
3215 O OG  . SER A 407 ? 0.9728 0.8063 0.8977 -0.0089 -0.0456 -0.0397 703 SER A OG  
3216 N N   . PHE A 408 ? 0.6202 0.6178 0.6856 -0.0099 -0.0429 -0.0356 704 PHE A N   
3217 C CA  . PHE A 408 ? 0.6246 0.6543 0.7116 0.0129  -0.0444 -0.0328 704 PHE A CA  
3218 C C   . PHE A 408 ? 0.7083 0.7231 0.7774 0.0320  -0.0461 -0.0297 704 PHE A C   
3219 O O   . PHE A 408 ? 0.8791 0.8780 0.9406 0.0246  -0.0455 -0.0275 704 PHE A O   
3220 C CB  . PHE A 408 ? 0.5956 0.6725 0.7248 0.0051  -0.0434 -0.0294 704 PHE A CB  
3221 C CG  . PHE A 408 ? 0.5565 0.6545 0.7027 -0.0042 -0.0427 -0.0316 704 PHE A CG  
3222 C CD1 . PHE A 408 ? 0.5228 0.6310 0.6792 -0.0210 -0.0411 -0.0328 704 PHE A CD1 
3223 C CD2 . PHE A 408 ? 0.5736 0.6855 0.7240 0.0059  -0.0437 -0.0325 704 PHE A CD2 
3224 C CE1 . PHE A 408 ? 0.5962 0.7271 0.7659 -0.0255 -0.0413 -0.0348 704 PHE A CE1 
3225 C CE2 . PHE A 408 ? 0.4689 0.5980 0.6315 -0.0011 -0.0436 -0.0344 704 PHE A CE2 
3226 C CZ  . PHE A 408 ? 0.5743 0.7125 0.7462 -0.0159 -0.0429 -0.0355 704 PHE A CZ  
3227 N N   . GLU A 409 ? 0.6306 0.6550 0.6919 0.0583  -0.0481 -0.0296 705 GLU A N   
3228 C CA  . GLU A 409 ? 0.6241 0.6444 0.6674 0.0829  -0.0506 -0.0270 705 GLU A CA  
3229 C C   . GLU A 409 ? 0.7349 0.8203 0.8094 0.0983  -0.0520 -0.0237 705 GLU A C   
3230 O O   . GLU A 409 ? 0.7707 0.8891 0.8653 0.0971  -0.0507 -0.0243 705 GLU A O   
3231 C CB  . GLU A 409 ? 0.7685 0.7318 0.7543 0.1077  -0.0522 -0.0305 705 GLU A CB  
3232 C CG  . GLU A 409 ? 1.0176 0.9063 0.9579 0.0882  -0.0513 -0.0342 705 GLU A CG  
3233 C CD  . GLU A 409 ? 1.1645 1.0204 1.0874 0.0743  -0.0509 -0.0310 705 GLU A CD  
3234 O OE1 . GLU A 409 ? 1.1484 1.0377 1.0956 0.0812  -0.0518 -0.0263 705 GLU A OE1 
3235 O OE2 . GLU A 409 ? 1.2951 1.0912 1.1766 0.0537  -0.0499 -0.0331 705 GLU A OE2 
3236 N N   . TYR A 410 ? 0.6944 0.8009 0.7711 0.1105  -0.0548 -0.0198 706 TYR A N   
3237 C CA  . TYR A 410 ? 0.6556 0.8292 0.7546 0.1254  -0.0568 -0.0167 706 TYR A CA  
3238 C C   . TYR A 410 ? 0.7416 0.9173 0.8131 0.1626  -0.0572 -0.0194 706 TYR A C   
3239 O O   . TYR A 410 ? 0.7896 0.9040 0.8143 0.1824  -0.0578 -0.0229 706 TYR A O   
3240 C CB  . TYR A 410 ? 0.8626 1.0638 0.9684 0.1288  -0.0609 -0.0123 706 TYR A CB  
3241 C CG  . TYR A 410 ? 0.9007 1.0942 1.0241 0.0983  -0.0610 -0.0099 706 TYR A CG  
3242 C CD1 . TYR A 410 ? 1.0143 1.1557 1.1153 0.0944  -0.0608 -0.0103 706 TYR A CD1 
3243 C CD2 . TYR A 410 ? 0.8904 1.1259 1.0462 0.0742  -0.0614 -0.0070 706 TYR A CD2 
3244 C CE1 . TYR A 410 ? 0.9764 1.1137 1.0910 0.0706  -0.0604 -0.0085 706 TYR A CE1 
3245 C CE2 . TYR A 410 ? 0.9692 1.1911 1.1325 0.0511  -0.0618 -0.0055 706 TYR A CE2 
3246 C CZ  . TYR A 410 ? 0.9500 1.1262 1.0948 0.0512  -0.0610 -0.0065 706 TYR A CZ  
3247 O OH  . TYR A 410 ? 0.8443 1.0095 0.9947 0.0317  -0.0608 -0.0053 706 TYR A OH  
3248 N N   . GLN A 411 ? 0.7628 1.0085 0.8584 0.1722  -0.0570 -0.0175 707 GLN A N   
3249 C CA  . GLN A 411 ? 0.7956 1.0620 0.8693 0.2124  -0.0568 -0.0197 707 GLN A CA  
3250 C C   . GLN A 411 ? 0.7790 1.1431 0.8819 0.2230  -0.0586 -0.0147 707 GLN A C   
3251 O O   . GLN A 411 ? 0.8346 1.2463 0.9759 0.1901  -0.0592 -0.0100 707 GLN A O   
3252 C CB  . GLN A 411 ? 0.8919 1.1486 0.9636 0.2104  -0.0526 -0.0237 707 GLN A CB  
3253 C CG  . GLN A 411 ? 0.8443 1.1685 0.9625 0.1846  -0.0499 -0.0201 707 GLN A CG  
3254 C CD  . GLN A 411 ? 0.9108 1.2093 1.0271 0.1736  -0.0463 -0.0239 707 GLN A CD  
3255 O OE1 . GLN A 411 ? 1.0240 1.2744 1.1039 0.1941  -0.0457 -0.0298 707 GLN A OE1 
3256 N NE2 . GLN A 411 ? 0.8120 1.1366 0.9614 0.1411  -0.0445 -0.0206 707 GLN A NE2 
3257 N N   . PRO A 412 ? 0.7792 1.1754 0.8603 0.2685  -0.0598 -0.0156 708 PRO A N   
3258 C CA  . PRO A 412 ? 0.8045 1.3115 0.9153 0.2786  -0.0614 -0.0109 708 PRO A CA  
3259 C C   . PRO A 412 ? 0.8626 1.4355 1.0152 0.2457  -0.0572 -0.0079 708 PRO A C   
3260 O O   . PRO A 412 ? 0.8717 1.4110 1.0234 0.2338  -0.0526 -0.0106 708 PRO A O   
3261 C CB  . PRO A 412 ? 0.9083 1.4295 0.9806 0.3406  -0.0616 -0.0141 708 PRO A CB  
3262 C CG  . PRO A 412 ? 1.0216 1.4234 1.0349 0.3620  -0.0627 -0.0196 708 PRO A CG  
3263 C CD  . PRO A 412 ? 0.9617 1.2929 0.9839 0.3137  -0.0600 -0.0212 708 PRO A CD  
3264 N N   . ASP A 413 ? 0.9010 1.5609 1.0834 0.2269  -0.0584 -0.0021 709 ASP A N   
3265 C CA  . ASP A 413 ? 0.9117 1.6253 1.1152 0.1957  -0.0523 0.0014  709 ASP A CA  
3266 C C   . ASP A 413 ? 0.9312 1.6700 1.1123 0.2304  -0.0455 -0.0014 709 ASP A C   
3267 O O   . ASP A 413 ? 1.0030 1.7488 1.1544 0.2714  -0.0455 -0.0039 709 ASP A O   
3268 C CB  . ASP A 413 ? 0.9860 1.7608 1.2062 0.1599  -0.0532 0.0077  709 ASP A CB  
3269 C CG  . ASP A 413 ? 1.0355 1.7831 1.2729 0.1225  -0.0598 0.0103  709 ASP A CG  
3270 O OD1 . ASP A 413 ? 1.0142 1.7119 1.2603 0.1066  -0.0609 0.0089  709 ASP A OD1 
3271 O OD2 . ASP A 413 ? 1.0668 1.8425 1.3056 0.1096  -0.0639 0.0132  709 ASP A OD2 
3272 N N   . PRO A 414 ? 0.8643 1.6158 1.0545 0.2167  -0.0399 -0.0011 710 PRO A N   
3273 C CA  . PRO A 414 ? 0.8675 1.6327 1.0320 0.2536  -0.0340 -0.0048 710 PRO A CA  
3274 C C   . PRO A 414 ? 0.9187 1.7690 1.0776 0.2591  -0.0297 -0.0012 710 PRO A C   
3275 O O   . PRO A 414 ? 0.9685 1.8324 1.0957 0.3023  -0.0266 -0.0048 710 PRO A O   
3276 C CB  . PRO A 414 ? 0.7754 1.5277 0.9550 0.2317  -0.0300 -0.0051 710 PRO A CB  
3277 C CG  . PRO A 414 ? 0.6670 1.3852 0.8743 0.1911  -0.0346 -0.0028 710 PRO A CG  
3278 C CD  . PRO A 414 ? 0.8011 1.5443 1.0189 0.1711  -0.0390 0.0020  710 PRO A CD  
3279 N N   . TRP A 415 ? 0.8845 1.7915 1.0683 0.2162  -0.0298 0.0058  711 TRP A N   
3280 C CA  . TRP A 415 ? 0.9903 1.9850 1.1669 0.2200  -0.0263 0.0094  711 TRP A CA  
3281 C C   . TRP A 415 ? 1.1071 2.1170 1.2626 0.2570  -0.0297 0.0071  711 TRP A C   
3282 O O   . TRP A 415 ? 1.1465 2.2350 1.2933 0.2657  -0.0272 0.0094  711 TRP A O   
3283 C CB  . TRP A 415 ? 0.9434 1.9890 1.1442 0.1607  -0.0259 0.0175  711 TRP A CB  
3284 C CG  . TRP A 415 ? 0.9356 1.9559 1.1508 0.1298  -0.0329 0.0198  711 TRP A CG  
3285 C CD1 . TRP A 415 ? 0.9930 2.0516 1.2062 0.1270  -0.0367 0.0218  711 TRP A CD1 
3286 C CD2 . TRP A 415 ? 0.8923 1.8448 1.1233 0.0987  -0.0372 0.0201  711 TRP A CD2 
3287 N NE1 . TRP A 415 ? 0.9593 1.9748 1.1856 0.0955  -0.0433 0.0232  711 TRP A NE1 
3288 C CE2 . TRP A 415 ? 0.9232 1.8736 1.1596 0.0783  -0.0438 0.0222  711 TRP A CE2 
3289 C CE3 . TRP A 415 ? 0.8486 1.7449 1.0877 0.0873  -0.0363 0.0187  711 TRP A CE3 
3290 C CZ2 . TRP A 415 ? 0.8721 1.7645 1.1194 0.0480  -0.0495 0.0228  711 TRP A CZ2 
3291 C CZ3 . TRP A 415 ? 0.7835 1.6261 1.0345 0.0577  -0.0417 0.0194  711 TRP A CZ3 
3292 C CH2 . TRP A 415 ? 0.8638 1.7039 1.1178 0.0387  -0.0482 0.0214  711 TRP A CH2 
3293 N N   . ASN A 416 ? 1.1721 2.1105 1.3166 0.2789  -0.0354 0.0029  712 ASN A N   
3294 C CA  . ASN A 416 ? 1.1951 2.1318 1.3112 0.3197  -0.0390 0.0002  712 ASN A CA  
3295 C C   . ASN A 416 ? 1.1893 2.0516 1.2590 0.3759  -0.0395 -0.0073 712 ASN A C   
3296 O O   . ASN A 416 ? 1.2504 2.0846 1.2870 0.4116  -0.0433 -0.0100 712 ASN A O   
3297 C CB  . ASN A 416 ? 1.2580 2.1721 1.3916 0.2954  -0.0465 0.0027  712 ASN A CB  
3298 C CG  . ASN A 416 ? 1.2972 2.2789 1.4637 0.2418  -0.0468 0.0095  712 ASN A CG  
3299 O OD1 . ASN A 416 ? 1.3393 2.3978 1.5090 0.2301  -0.0417 0.0128  712 ASN A OD1 
3300 N ND2 . ASN A 416 ? 1.2261 2.1772 1.4116 0.2086  -0.0533 0.0118  712 ASN A ND2 
3301 N N   . THR A 417 ? 1.1671 1.9909 1.2276 0.3837  -0.0361 -0.0107 713 THR A N   
3302 C CA  . THR A 417 ? 1.2169 1.9641 1.2230 0.4349  -0.0364 -0.0181 713 THR A CA  
3303 C C   . THR A 417 ? 1.3337 2.0944 1.3227 0.4522  -0.0303 -0.0210 713 THR A C   
3304 O O   . THR A 417 ? 1.4722 2.1858 1.4043 0.5008  -0.0303 -0.0270 713 THR A O   
3305 C CB  . THR A 417 ? 1.2000 1.8430 1.2008 0.4288  -0.0415 -0.0213 713 THR A CB  
3306 O OG1 . THR A 417 ? 1.1228 1.7733 1.1730 0.3809  -0.0404 -0.0186 713 THR A OG1 
3307 C CG2 . THR A 417 ? 1.2220 1.8307 1.2169 0.4300  -0.0486 -0.0199 713 THR A CG2 
3308 N N   . HIS A 418 ? 1.2777 2.0953 1.3074 0.4145  -0.0255 -0.0168 714 HIS A N   
3309 C CA  . HIS A 418 ? 1.2917 2.1184 1.3077 0.4276  -0.0199 -0.0192 714 HIS A CA  
3310 C C   . HIS A 418 ? 1.3859 2.2726 1.3645 0.4702  -0.0168 -0.0199 714 HIS A C   
3311 O O   . HIS A 418 ? 1.3686 2.3427 1.3612 0.4619  -0.0156 -0.0149 714 HIS A O   
3312 C CB  . HIS A 418 ? 1.1791 2.0557 1.2451 0.3740  -0.0157 -0.0132 714 HIS A CB  
3313 C CG  . HIS A 418 ? 1.1335 1.9990 1.1912 0.3806  -0.0107 -0.0159 714 HIS A CG  
3314 N ND1 . HIS A 418 ? 1.0910 2.0180 1.1768 0.3461  -0.0053 -0.0102 714 HIS A ND1 
3315 C CD2 . HIS A 418 ? 1.1435 1.9392 1.1638 0.4161  -0.0107 -0.0238 714 HIS A CD2 
3316 C CE1 . HIS A 418 ? 1.1137 2.0149 1.1839 0.3620  -0.0019 -0.0144 714 HIS A CE1 
3317 N NE2 . HIS A 418 ? 1.1624 1.9840 1.1929 0.4042  -0.0051 -0.0230 714 HIS A NE2 
3318 N N   . VAL A 419 ? 1.4512 2.2893 1.3775 0.5167  -0.0163 -0.0265 715 VAL A N   
3319 C CA  . VAL A 419 ? 1.5001 2.3988 1.3908 0.5561  -0.0131 -0.0269 715 VAL A CA  
3320 C C   . VAL A 419 ? 1.5069 2.4786 1.4353 0.5233  -0.0069 -0.0220 715 VAL A C   
3321 O O   . VAL A 419 ? 1.5256 2.4569 1.4488 0.5231  -0.0048 -0.0250 715 VAL A O   
3322 C CB  . VAL A 419 ? 1.5174 2.3287 1.3317 0.6152  -0.0157 -0.0351 715 VAL A CB  
3323 C CG1 . VAL A 419 ? 1.5402 2.4166 1.3180 0.6558  -0.0129 -0.0349 715 VAL A CG1 
3324 C CG2 . VAL A 419 ? 1.5347 2.2728 1.3026 0.6465  -0.0220 -0.0388 715 VAL A CG2 
3325 N N   . TRP A 420 ? 1.4896 2.5663 1.4525 0.4937  -0.0043 -0.0144 716 TRP A N   
3326 C CA  . TRP A 420 ? 1.4753 2.6134 1.4807 0.4446  0.0006  -0.0077 716 TRP A CA  
3327 C C   . TRP A 420 ? 1.4592 2.6478 1.4442 0.4664  0.0052  -0.0073 716 TRP A C   
3328 O O   . TRP A 420 ? 1.5021 2.6621 1.4384 0.5209  0.0044  -0.0132 716 TRP A O   
3329 C CB  . TRP A 420 ? 1.5137 2.7381 1.5543 0.4012  0.0007  0.0007  716 TRP A CB  
3330 C CG  . TRP A 420 ? 1.5320 2.7546 1.6191 0.3340  0.0017  0.0068  716 TRP A CG  
3331 C CD1 . TRP A 420 ? 1.5011 2.6506 1.6051 0.3117  0.0020  0.0052  716 TRP A CD1 
3332 C CD2 . TRP A 420 ? 1.5394 2.8336 1.6548 0.2810  0.0020  0.0156  716 TRP A CD2 
3333 N NE1 . TRP A 420 ? 1.4564 2.6252 1.5956 0.2505  0.0024  0.0126  716 TRP A NE1 
3334 C CE2 . TRP A 420 ? 1.4792 2.7319 1.6236 0.2294  0.0022  0.0191  716 TRP A CE2 
3335 C CE3 . TRP A 420 ? 1.5554 2.9441 1.6699 0.2719  0.0018  0.0208  716 TRP A CE3 
3336 C CZ2 . TRP A 420 ? 1.4413 2.7335 1.6073 0.1695  0.0018  0.0276  716 TRP A CZ2 
3337 C CZ3 . TRP A 420 ? 1.5287 2.9609 1.6679 0.2095  0.0014  0.0291  716 TRP A CZ3 
3338 C CH2 . TRP A 420 ? 1.4777 2.8568 1.6396 0.1590  0.0012  0.0325  716 TRP A CH2 
# 
