data_9CVP
# 
_entry.id   9CVP 
# 
_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   9CVP         pdb_00009cvp 10.2210/pdb9cvp/pdb 
WWPDB D_1000286182 ?            ?                   
# 
_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                        9CVP 
_pdbx_database_status.recvd_initial_deposition_date   2024-07-29 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    RCSB 
_pdbx_database_status.process_site                    RCSB 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           N 
# 
_pdbx_contact_author.id                 2 
_pdbx_contact_author.email              poulos@uci.edu 
_pdbx_contact_author.name_first         Thomas 
_pdbx_contact_author.name_last          Poulos 
_pdbx_contact_author.name_mi            L 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0002-5648-3510 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Li, H.'       1 0000-0003-4867-367X 
'Poulos, T.L.' 2 0000-0002-5648-3510 
# 
_citation.abstract                  ? 
_citation.abstract_id_CAS           ? 
_citation.book_id_ISBN              ? 
_citation.book_publisher            ? 
_citation.book_publisher_city       ? 
_citation.book_title                ? 
_citation.coordinate_linkage        ? 
_citation.country                   UK 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            Bioorg.Med.Chem. 
_citation.journal_id_ASTM           BMECEP 
_citation.journal_id_CSD            1200 
_citation.journal_id_ISSN           1464-3391 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            124 
_citation.language                  ? 
_citation.page_first                118193 
_citation.page_last                 118193 
_citation.title                     
;Truncated pyridinylbenzylamines: Potent, selective, and highly membrane permeable inhibitors of human neuronal nitric oxide synthase.
;
_citation.year                      2025 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1016/j.bmc.2025.118193 
_citation.pdbx_database_id_PubMed   40252563 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Vasu, D.'        1 ? 
primary 'Do, H.T.'        2 ? 
primary 'Li, H.'          3 ? 
primary 'Hardy, C.D.'     4 ? 
primary 'Poulos, T.L.'    5 ? 
primary 'Silverman, R.B.' 6 ? 
# 
loop_
_entity.id 
_entity.type 
_entity.src_method 
_entity.pdbx_description 
_entity.formula_weight 
_entity.pdbx_number_of_molecules 
_entity.pdbx_ec 
_entity.pdbx_mutation 
_entity.pdbx_fragment 
_entity.details 
1 polymer     man 'Nitric oxide synthase, brain'                                                         48726.410 1  1.14.13.39 
R349A ? ? 
2 non-polymer syn 'PROTOPORPHYRIN IX CONTAINING FE'                                                      616.487   1  ?          ? 
? ? 
3 non-polymer syn 5,6,7,8-TETRAHYDROBIOPTERIN                                                            241.247   1  ?          ? 
? ? 
4 non-polymer syn 'ZINC ION'                                                                             65.409    1  ?          ? 
? ? 
5 non-polymer syn '(6M)-6-(2,3-difluoro-5-{[(2-fluoroethyl)amino]methyl}phenyl)-4-methylpyridin-2-amine' 295.303   1  ?          ? 
? ? 
6 water       nat water                                                                                  18.015    39 ?          ? 
? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        'BNOS,Constitutive NOS,NC-NOS,NOS type I,Neuronal NOS,nNOS,Peptidyl-cysteine S-nitrosylase NOS1' 
# 
_entity_poly.entity_id                      1 
_entity_poly.type                           'polypeptide(L)' 
_entity_poly.nstd_linkage                   no 
_entity_poly.nstd_monomer                   no 
_entity_poly.pdbx_seq_one_letter_code       
;CPRFLKVKNWETDVVLTDTLHLKSTLETGCTEHICMGSIMLPSQHTRKPEDVATKDQLFPLAKEFLDQYYSSIKRFGSKA
HMDRLEEVNKEIESTSTYQLKDTELIYGAKHAWRNASRCVGRIQWSKLQVFDARDCTTAHGMFNYICNHVKYATNKGNLR
SAITIFPQRTDGKHDFRVWNSQLIRYAGYKQPDGSTLGDPANVQFTEICIQQGWKAPRGRFDVLPLLLQANGNDPELFQI
PPELVLEVPIRHPKFDWFKDLGLKWYGLPAVSNMLLEIGGLEFSACPFSGWYMGTEIGVRDYCDNSRYNILEEVAKKMDL
DMRKTSSLWKDQALVEINIAVLYSFQSDKVTIVDHHSATESFIKHMENEYRCRGGCPADWVWIVPPMSGSITPVFHQEML
NYRLTPSFEYQPDPWNTHVWKG
;
_entity_poly.pdbx_seq_one_letter_code_can   
;CPRFLKVKNWETDVVLTDTLHLKSTLETGCTEHICMGSIMLPSQHTRKPEDVATKDQLFPLAKEFLDQYYSSIKRFGSKA
HMDRLEEVNKEIESTSTYQLKDTELIYGAKHAWRNASRCVGRIQWSKLQVFDARDCTTAHGMFNYICNHVKYATNKGNLR
SAITIFPQRTDGKHDFRVWNSQLIRYAGYKQPDGSTLGDPANVQFTEICIQQGWKAPRGRFDVLPLLLQANGNDPELFQI
PPELVLEVPIRHPKFDWFKDLGLKWYGLPAVSNMLLEIGGLEFSACPFSGWYMGTEIGVRDYCDNSRYNILEEVAKKMDL
DMRKTSSLWKDQALVEINIAVLYSFQSDKVTIVDHHSATESFIKHMENEYRCRGGCPADWVWIVPPMSGSITPVFHQEML
NYRLTPSFEYQPDPWNTHVWKG
;
_entity_poly.pdbx_strand_id                 A 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 'PROTOPORPHYRIN IX CONTAINING FE'                                                      HEM   
3 5,6,7,8-TETRAHYDROBIOPTERIN                                                            H4B   
4 'ZINC ION'                                                                             ZN    
5 '(6M)-6-(2,3-difluoro-5-{[(2-fluoroethyl)amino]methyl}phenyl)-4-methylpyridin-2-amine' A1AZ9 
6 water                                                                                  HOH   
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   CYS n 
1 2   PRO n 
1 3   ARG n 
1 4   PHE n 
1 5   LEU n 
1 6   LYS n 
1 7   VAL n 
1 8   LYS n 
1 9   ASN n 
1 10  TRP n 
1 11  GLU n 
1 12  THR n 
1 13  ASP n 
1 14  VAL n 
1 15  VAL n 
1 16  LEU n 
1 17  THR n 
1 18  ASP n 
1 19  THR n 
1 20  LEU n 
1 21  HIS n 
1 22  LEU n 
1 23  LYS n 
1 24  SER n 
1 25  THR n 
1 26  LEU n 
1 27  GLU n 
1 28  THR n 
1 29  GLY n 
1 30  CYS n 
1 31  THR n 
1 32  GLU n 
1 33  HIS n 
1 34  ILE n 
1 35  CYS n 
1 36  MET n 
1 37  GLY n 
1 38  SER n 
1 39  ILE n 
1 40  MET n 
1 41  LEU n 
1 42  PRO n 
1 43  SER n 
1 44  GLN n 
1 45  HIS n 
1 46  THR n 
1 47  ARG n 
1 48  LYS n 
1 49  PRO n 
1 50  GLU n 
1 51  ASP n 
1 52  VAL n 
1 53  ALA n 
1 54  THR n 
1 55  LYS n 
1 56  ASP n 
1 57  GLN n 
1 58  LEU n 
1 59  PHE n 
1 60  PRO n 
1 61  LEU n 
1 62  ALA n 
1 63  LYS n 
1 64  GLU n 
1 65  PHE n 
1 66  LEU n 
1 67  ASP n 
1 68  GLN n 
1 69  TYR n 
1 70  TYR n 
1 71  SER n 
1 72  SER n 
1 73  ILE n 
1 74  LYS n 
1 75  ARG n 
1 76  PHE n 
1 77  GLY n 
1 78  SER n 
1 79  LYS n 
1 80  ALA n 
1 81  HIS n 
1 82  MET n 
1 83  ASP n 
1 84  ARG n 
1 85  LEU n 
1 86  GLU n 
1 87  GLU n 
1 88  VAL n 
1 89  ASN n 
1 90  LYS n 
1 91  GLU n 
1 92  ILE n 
1 93  GLU n 
1 94  SER n 
1 95  THR n 
1 96  SER n 
1 97  THR n 
1 98  TYR n 
1 99  GLN n 
1 100 LEU n 
1 101 LYS n 
1 102 ASP n 
1 103 THR n 
1 104 GLU n 
1 105 LEU n 
1 106 ILE n 
1 107 TYR n 
1 108 GLY n 
1 109 ALA n 
1 110 LYS n 
1 111 HIS n 
1 112 ALA n 
1 113 TRP n 
1 114 ARG n 
1 115 ASN n 
1 116 ALA n 
1 117 SER n 
1 118 ARG n 
1 119 CYS n 
1 120 VAL n 
1 121 GLY n 
1 122 ARG n 
1 123 ILE n 
1 124 GLN n 
1 125 TRP n 
1 126 SER n 
1 127 LYS n 
1 128 LEU n 
1 129 GLN n 
1 130 VAL n 
1 131 PHE n 
1 132 ASP n 
1 133 ALA n 
1 134 ARG n 
1 135 ASP n 
1 136 CYS n 
1 137 THR n 
1 138 THR n 
1 139 ALA n 
1 140 HIS n 
1 141 GLY n 
1 142 MET n 
1 143 PHE n 
1 144 ASN n 
1 145 TYR n 
1 146 ILE n 
1 147 CYS n 
1 148 ASN n 
1 149 HIS n 
1 150 VAL n 
1 151 LYS n 
1 152 TYR n 
1 153 ALA n 
1 154 THR n 
1 155 ASN n 
1 156 LYS n 
1 157 GLY n 
1 158 ASN n 
1 159 LEU n 
1 160 ARG n 
1 161 SER n 
1 162 ALA n 
1 163 ILE n 
1 164 THR n 
1 165 ILE n 
1 166 PHE n 
1 167 PRO n 
1 168 GLN n 
1 169 ARG n 
1 170 THR n 
1 171 ASP n 
1 172 GLY n 
1 173 LYS n 
1 174 HIS n 
1 175 ASP n 
1 176 PHE n 
1 177 ARG n 
1 178 VAL n 
1 179 TRP n 
1 180 ASN n 
1 181 SER n 
1 182 GLN n 
1 183 LEU n 
1 184 ILE n 
1 185 ARG n 
1 186 TYR n 
1 187 ALA n 
1 188 GLY n 
1 189 TYR n 
1 190 LYS n 
1 191 GLN n 
1 192 PRO n 
1 193 ASP n 
1 194 GLY n 
1 195 SER n 
1 196 THR n 
1 197 LEU n 
1 198 GLY n 
1 199 ASP n 
1 200 PRO n 
1 201 ALA n 
1 202 ASN n 
1 203 VAL n 
1 204 GLN n 
1 205 PHE n 
1 206 THR n 
1 207 GLU n 
1 208 ILE n 
1 209 CYS n 
1 210 ILE n 
1 211 GLN n 
1 212 GLN n 
1 213 GLY n 
1 214 TRP n 
1 215 LYS n 
1 216 ALA n 
1 217 PRO n 
1 218 ARG n 
1 219 GLY n 
1 220 ARG n 
1 221 PHE n 
1 222 ASP n 
1 223 VAL n 
1 224 LEU n 
1 225 PRO n 
1 226 LEU n 
1 227 LEU n 
1 228 LEU n 
1 229 GLN n 
1 230 ALA n 
1 231 ASN n 
1 232 GLY n 
1 233 ASN n 
1 234 ASP n 
1 235 PRO n 
1 236 GLU n 
1 237 LEU n 
1 238 PHE n 
1 239 GLN n 
1 240 ILE n 
1 241 PRO n 
1 242 PRO n 
1 243 GLU n 
1 244 LEU n 
1 245 VAL n 
1 246 LEU n 
1 247 GLU n 
1 248 VAL n 
1 249 PRO n 
1 250 ILE n 
1 251 ARG n 
1 252 HIS n 
1 253 PRO n 
1 254 LYS n 
1 255 PHE n 
1 256 ASP n 
1 257 TRP n 
1 258 PHE n 
1 259 LYS n 
1 260 ASP n 
1 261 LEU n 
1 262 GLY n 
1 263 LEU n 
1 264 LYS n 
1 265 TRP n 
1 266 TYR n 
1 267 GLY n 
1 268 LEU n 
1 269 PRO n 
1 270 ALA n 
1 271 VAL n 
1 272 SER n 
1 273 ASN n 
1 274 MET n 
1 275 LEU n 
1 276 LEU n 
1 277 GLU n 
1 278 ILE n 
1 279 GLY n 
1 280 GLY n 
1 281 LEU n 
1 282 GLU n 
1 283 PHE n 
1 284 SER n 
1 285 ALA n 
1 286 CYS n 
1 287 PRO n 
1 288 PHE n 
1 289 SER n 
1 290 GLY n 
1 291 TRP n 
1 292 TYR n 
1 293 MET n 
1 294 GLY n 
1 295 THR n 
1 296 GLU n 
1 297 ILE n 
1 298 GLY n 
1 299 VAL n 
1 300 ARG n 
1 301 ASP n 
1 302 TYR n 
1 303 CYS n 
1 304 ASP n 
1 305 ASN n 
1 306 SER n 
1 307 ARG n 
1 308 TYR n 
1 309 ASN n 
1 310 ILE n 
1 311 LEU n 
1 312 GLU n 
1 313 GLU n 
1 314 VAL n 
1 315 ALA n 
1 316 LYS n 
1 317 LYS n 
1 318 MET n 
1 319 ASP n 
1 320 LEU n 
1 321 ASP n 
1 322 MET n 
1 323 ARG n 
1 324 LYS n 
1 325 THR n 
1 326 SER n 
1 327 SER n 
1 328 LEU n 
1 329 TRP n 
1 330 LYS n 
1 331 ASP n 
1 332 GLN n 
1 333 ALA n 
1 334 LEU n 
1 335 VAL n 
1 336 GLU n 
1 337 ILE n 
1 338 ASN n 
1 339 ILE n 
1 340 ALA n 
1 341 VAL n 
1 342 LEU n 
1 343 TYR n 
1 344 SER n 
1 345 PHE n 
1 346 GLN n 
1 347 SER n 
1 348 ASP n 
1 349 LYS n 
1 350 VAL n 
1 351 THR n 
1 352 ILE n 
1 353 VAL n 
1 354 ASP n 
1 355 HIS n 
1 356 HIS n 
1 357 SER n 
1 358 ALA n 
1 359 THR n 
1 360 GLU n 
1 361 SER n 
1 362 PHE n 
1 363 ILE n 
1 364 LYS n 
1 365 HIS n 
1 366 MET n 
1 367 GLU n 
1 368 ASN n 
1 369 GLU n 
1 370 TYR n 
1 371 ARG n 
1 372 CYS n 
1 373 ARG n 
1 374 GLY n 
1 375 GLY n 
1 376 CYS n 
1 377 PRO n 
1 378 ALA n 
1 379 ASP n 
1 380 TRP n 
1 381 VAL n 
1 382 TRP n 
1 383 ILE n 
1 384 VAL n 
1 385 PRO n 
1 386 PRO n 
1 387 MET n 
1 388 SER n 
1 389 GLY n 
1 390 SER n 
1 391 ILE n 
1 392 THR n 
1 393 PRO n 
1 394 VAL n 
1 395 PHE n 
1 396 HIS n 
1 397 GLN n 
1 398 GLU n 
1 399 MET n 
1 400 LEU n 
1 401 ASN n 
1 402 TYR n 
1 403 ARG n 
1 404 LEU n 
1 405 THR n 
1 406 PRO n 
1 407 SER n 
1 408 PHE n 
1 409 GLU n 
1 410 TYR n 
1 411 GLN n 
1 412 PRO n 
1 413 ASP n 
1 414 PRO n 
1 415 TRP n 
1 416 ASN n 
1 417 THR n 
1 418 HIS n 
1 419 VAL n 
1 420 TRP n 
1 421 LYS n 
1 422 GLY n 
# 
_entity_src_gen.entity_id                          1 
_entity_src_gen.pdbx_src_id                        1 
_entity_src_gen.pdbx_alt_source_flag               sample 
_entity_src_gen.pdbx_seq_type                      'Biological sequence' 
_entity_src_gen.pdbx_beg_seq_num                   1 
_entity_src_gen.pdbx_end_seq_num                   422 
_entity_src_gen.gene_src_common_name               'Norway rat' 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 'Nos1, Bnos' 
_entity_src_gen.gene_src_species                   ? 
_entity_src_gen.gene_src_strain                    ? 
_entity_src_gen.gene_src_tissue                    ? 
_entity_src_gen.gene_src_tissue_fraction           ? 
_entity_src_gen.gene_src_details                   ? 
_entity_src_gen.pdbx_gene_src_fragment             ? 
_entity_src_gen.pdbx_gene_src_scientific_name      'Rattus norvegicus' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     10116 
_entity_src_gen.pdbx_gene_src_variant              ? 
_entity_src_gen.pdbx_gene_src_cell_line            ? 
_entity_src_gen.pdbx_gene_src_atcc                 ? 
_entity_src_gen.pdbx_gene_src_organ                brain 
_entity_src_gen.pdbx_gene_src_organelle            ? 
_entity_src_gen.pdbx_gene_src_cell                 ? 
_entity_src_gen.pdbx_gene_src_cellular_location    ? 
_entity_src_gen.host_org_common_name               ? 
_entity_src_gen.pdbx_host_org_scientific_name      'Escherichia coli BL21(DE3)' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     469008 
_entity_src_gen.host_org_genus                     ? 
_entity_src_gen.pdbx_host_org_gene                 ? 
_entity_src_gen.pdbx_host_org_organ                ? 
_entity_src_gen.host_org_species                   ? 
_entity_src_gen.pdbx_host_org_tissue               ? 
_entity_src_gen.pdbx_host_org_tissue_fraction      ? 
_entity_src_gen.pdbx_host_org_strain               ? 
_entity_src_gen.pdbx_host_org_variant              ? 
_entity_src_gen.pdbx_host_org_cell_line            ? 
_entity_src_gen.pdbx_host_org_atcc                 ? 
_entity_src_gen.pdbx_host_org_culture_collection   ? 
_entity_src_gen.pdbx_host_org_cell                 ? 
_entity_src_gen.pdbx_host_org_organelle            ? 
_entity_src_gen.pdbx_host_org_cellular_location    ? 
_entity_src_gen.pdbx_host_org_vector_type          plasmid 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       pET22b 
_entity_src_gen.plasmid_details                    ? 
_entity_src_gen.pdbx_description                   ? 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
A1AZ9 non-polymer         . '(6M)-6-(2,3-difluoro-5-{[(2-fluoroethyl)amino]methyl}phenyl)-4-methylpyridin-2-amine' ?    
'C15 H16 F3 N3'    295.303 
ALA   'L-peptide linking' y ALANINE                                                                                ?    
'C3 H7 N O2'       89.093  
ARG   'L-peptide linking' y ARGININE                                                                               ?    
'C6 H15 N4 O2 1'   175.209 
ASN   'L-peptide linking' y ASPARAGINE                                                                             ?    
'C4 H8 N2 O3'      132.118 
ASP   'L-peptide linking' y 'ASPARTIC ACID'                                                                        ?    
'C4 H7 N O4'       133.103 
CYS   'L-peptide linking' y CYSTEINE                                                                               ?    
'C3 H7 N O2 S'     121.158 
GLN   'L-peptide linking' y GLUTAMINE                                                                              ?    
'C5 H10 N2 O3'     146.144 
GLU   'L-peptide linking' y 'GLUTAMIC ACID'                                                                        ?    
'C5 H9 N O4'       147.129 
GLY   'peptide linking'   y GLYCINE                                                                                ?    
'C2 H5 N O2'       75.067  
H4B   non-polymer         . 5,6,7,8-TETRAHYDROBIOPTERIN                                                            ?    
'C9 H15 N5 O3'     241.247 
HEM   non-polymer         . 'PROTOPORPHYRIN IX CONTAINING FE'                                                      HEME 
'C34 H32 Fe N4 O4' 616.487 
HIS   'L-peptide linking' y HISTIDINE                                                                              ?    
'C6 H10 N3 O2 1'   156.162 
HOH   non-polymer         . WATER                                                                                  ?    'H2 O' 
18.015  
ILE   'L-peptide linking' y ISOLEUCINE                                                                             ?    
'C6 H13 N O2'      131.173 
LEU   'L-peptide linking' y LEUCINE                                                                                ?    
'C6 H13 N O2'      131.173 
LYS   'L-peptide linking' y LYSINE                                                                                 ?    
'C6 H15 N2 O2 1'   147.195 
MET   'L-peptide linking' y METHIONINE                                                                             ?    
'C5 H11 N O2 S'    149.211 
PHE   'L-peptide linking' y PHENYLALANINE                                                                          ?    
'C9 H11 N O2'      165.189 
PRO   'L-peptide linking' y PROLINE                                                                                ?    
'C5 H9 N O2'       115.130 
SER   'L-peptide linking' y SERINE                                                                                 ?    
'C3 H7 N O3'       105.093 
THR   'L-peptide linking' y THREONINE                                                                              ?    
'C4 H9 N O3'       119.119 
TRP   'L-peptide linking' y TRYPTOPHAN                                                                             ?    
'C11 H12 N2 O2'    204.225 
TYR   'L-peptide linking' y TYROSINE                                                                               ?    
'C9 H11 N O3'      181.189 
VAL   'L-peptide linking' y VALINE                                                                                 ?    
'C5 H11 N O2'      117.146 
ZN    non-polymer         . 'ZINC ION'                                                                             ?    'Zn 2' 
65.409  
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   CYS 1   297 ?   ?   ?   A . n 
A 1 2   PRO 2   298 ?   ?   ?   A . n 
A 1 3   ARG 3   299 299 ARG ARG A . n 
A 1 4   PHE 4   300 300 PHE PHE A . n 
A 1 5   LEU 5   301 301 LEU LEU A . n 
A 1 6   LYS 6   302 302 LYS LYS A . n 
A 1 7   VAL 7   303 303 VAL VAL A . n 
A 1 8   LYS 8   304 304 LYS LYS A . n 
A 1 9   ASN 9   305 305 ASN ASN A . n 
A 1 10  TRP 10  306 306 TRP TRP A . n 
A 1 11  GLU 11  307 307 GLU GLU A . n 
A 1 12  THR 12  308 308 THR THR A . n 
A 1 13  ASP 13  309 309 ASP ASP A . n 
A 1 14  VAL 14  310 310 VAL VAL A . n 
A 1 15  VAL 15  311 311 VAL VAL A . n 
A 1 16  LEU 16  312 312 LEU LEU A . n 
A 1 17  THR 17  313 313 THR THR A . n 
A 1 18  ASP 18  314 314 ASP ASP A . n 
A 1 19  THR 19  315 315 THR THR A . n 
A 1 20  LEU 20  316 316 LEU LEU A . n 
A 1 21  HIS 21  317 317 HIS HIS A . n 
A 1 22  LEU 22  318 318 LEU LEU A . n 
A 1 23  LYS 23  319 319 LYS LYS A . n 
A 1 24  SER 24  320 320 SER SER A . n 
A 1 25  THR 25  321 321 THR THR A . n 
A 1 26  LEU 26  322 322 LEU LEU A . n 
A 1 27  GLU 27  323 323 GLU GLU A . n 
A 1 28  THR 28  324 324 THR THR A . n 
A 1 29  GLY 29  325 325 GLY GLY A . n 
A 1 30  CYS 30  326 326 CYS CYS A . n 
A 1 31  THR 31  327 327 THR THR A . n 
A 1 32  GLU 32  328 328 GLU GLU A . n 
A 1 33  HIS 33  329 329 HIS HIS A . n 
A 1 34  ILE 34  330 330 ILE ILE A . n 
A 1 35  CYS 35  331 331 CYS CYS A . n 
A 1 36  MET 36  332 332 MET MET A . n 
A 1 37  GLY 37  333 333 GLY GLY A . n 
A 1 38  SER 38  334 334 SER SER A . n 
A 1 39  ILE 39  335 335 ILE ILE A . n 
A 1 40  MET 40  336 336 MET MET A . n 
A 1 41  LEU 41  337 337 LEU LEU A . n 
A 1 42  PRO 42  338 338 PRO PRO A . n 
A 1 43  SER 43  339 339 SER SER A . n 
A 1 44  GLN 44  340 ?   ?   ?   A . n 
A 1 45  HIS 45  341 ?   ?   ?   A . n 
A 1 46  THR 46  342 ?   ?   ?   A . n 
A 1 47  ARG 47  343 ?   ?   ?   A . n 
A 1 48  LYS 48  344 ?   ?   ?   A . n 
A 1 49  PRO 49  345 ?   ?   ?   A . n 
A 1 50  GLU 50  346 ?   ?   ?   A . n 
A 1 51  ASP 51  347 ?   ?   ?   A . n 
A 1 52  VAL 52  348 348 VAL VAL A . n 
A 1 53  ALA 53  349 349 ALA ALA A . n 
A 1 54  THR 54  350 350 THR THR A . n 
A 1 55  LYS 55  351 351 LYS LYS A . n 
A 1 56  ASP 56  352 352 ASP ASP A . n 
A 1 57  GLN 57  353 353 GLN GLN A . n 
A 1 58  LEU 58  354 354 LEU LEU A . n 
A 1 59  PHE 59  355 355 PHE PHE A . n 
A 1 60  PRO 60  356 356 PRO PRO A . n 
A 1 61  LEU 61  357 357 LEU LEU A . n 
A 1 62  ALA 62  358 358 ALA ALA A . n 
A 1 63  LYS 63  359 359 LYS LYS A . n 
A 1 64  GLU 64  360 360 GLU GLU A . n 
A 1 65  PHE 65  361 361 PHE PHE A . n 
A 1 66  LEU 66  362 362 LEU LEU A . n 
A 1 67  ASP 67  363 363 ASP ASP A . n 
A 1 68  GLN 68  364 364 GLN GLN A . n 
A 1 69  TYR 69  365 365 TYR TYR A . n 
A 1 70  TYR 70  366 366 TYR TYR A . n 
A 1 71  SER 71  367 367 SER SER A . n 
A 1 72  SER 72  368 368 SER SER A . n 
A 1 73  ILE 73  369 369 ILE ILE A . n 
A 1 74  LYS 74  370 370 LYS LYS A . n 
A 1 75  ARG 75  371 371 ARG ARG A . n 
A 1 76  PHE 76  372 372 PHE PHE A . n 
A 1 77  GLY 77  373 373 GLY GLY A . n 
A 1 78  SER 78  374 374 SER SER A . n 
A 1 79  LYS 79  375 375 LYS LYS A . n 
A 1 80  ALA 80  376 376 ALA ALA A . n 
A 1 81  HIS 81  377 377 HIS HIS A . n 
A 1 82  MET 82  378 378 MET MET A . n 
A 1 83  ASP 83  379 379 ASP ASP A . n 
A 1 84  ARG 84  380 380 ARG ARG A . n 
A 1 85  LEU 85  381 381 LEU LEU A . n 
A 1 86  GLU 86  382 382 GLU GLU A . n 
A 1 87  GLU 87  383 383 GLU GLU A . n 
A 1 88  VAL 88  384 384 VAL VAL A . n 
A 1 89  ASN 89  385 385 ASN ASN A . n 
A 1 90  LYS 90  386 386 LYS LYS A . n 
A 1 91  GLU 91  387 387 GLU GLU A . n 
A 1 92  ILE 92  388 388 ILE ILE A . n 
A 1 93  GLU 93  389 389 GLU GLU A . n 
A 1 94  SER 94  390 390 SER SER A . n 
A 1 95  THR 95  391 391 THR THR A . n 
A 1 96  SER 96  392 392 SER SER A . n 
A 1 97  THR 97  393 393 THR THR A . n 
A 1 98  TYR 98  394 394 TYR TYR A . n 
A 1 99  GLN 99  395 395 GLN GLN A . n 
A 1 100 LEU 100 396 396 LEU LEU A . n 
A 1 101 LYS 101 397 397 LYS LYS A . n 
A 1 102 ASP 102 398 398 ASP ASP A . n 
A 1 103 THR 103 399 399 THR THR A . n 
A 1 104 GLU 104 400 400 GLU GLU A . n 
A 1 105 LEU 105 401 401 LEU LEU A . n 
A 1 106 ILE 106 402 402 ILE ILE A . n 
A 1 107 TYR 107 403 403 TYR TYR A . n 
A 1 108 GLY 108 404 404 GLY GLY A . n 
A 1 109 ALA 109 405 405 ALA ALA A . n 
A 1 110 LYS 110 406 406 LYS LYS A . n 
A 1 111 HIS 111 407 407 HIS HIS A . n 
A 1 112 ALA 112 408 408 ALA ALA A . n 
A 1 113 TRP 113 409 409 TRP TRP A . n 
A 1 114 ARG 114 410 410 ARG ARG A . n 
A 1 115 ASN 115 411 411 ASN ASN A . n 
A 1 116 ALA 116 412 412 ALA ALA A . n 
A 1 117 SER 117 413 413 SER SER A . n 
A 1 118 ARG 118 414 414 ARG ARG A . n 
A 1 119 CYS 119 415 415 CYS CYS A . n 
A 1 120 VAL 120 416 416 VAL VAL A . n 
A 1 121 GLY 121 417 417 GLY GLY A . n 
A 1 122 ARG 122 418 418 ARG ARG A . n 
A 1 123 ILE 123 419 419 ILE ILE A . n 
A 1 124 GLN 124 420 420 GLN GLN A . n 
A 1 125 TRP 125 421 421 TRP TRP A . n 
A 1 126 SER 126 422 422 SER SER A . n 
A 1 127 LYS 127 423 423 LYS LYS A . n 
A 1 128 LEU 128 424 424 LEU LEU A . n 
A 1 129 GLN 129 425 425 GLN GLN A . n 
A 1 130 VAL 130 426 426 VAL VAL A . n 
A 1 131 PHE 131 427 427 PHE PHE A . n 
A 1 132 ASP 132 428 428 ASP ASP A . n 
A 1 133 ALA 133 429 429 ALA ALA A . n 
A 1 134 ARG 134 430 430 ARG ARG A . n 
A 1 135 ASP 135 431 431 ASP ASP A . n 
A 1 136 CYS 136 432 432 CYS CYS A . n 
A 1 137 THR 137 433 433 THR THR A . n 
A 1 138 THR 138 434 434 THR THR A . n 
A 1 139 ALA 139 435 435 ALA ALA A . n 
A 1 140 HIS 140 436 436 HIS HIS A . n 
A 1 141 GLY 141 437 437 GLY GLY A . n 
A 1 142 MET 142 438 438 MET MET A . n 
A 1 143 PHE 143 439 439 PHE PHE A . n 
A 1 144 ASN 144 440 440 ASN ASN A . n 
A 1 145 TYR 145 441 441 TYR TYR A . n 
A 1 146 ILE 146 442 442 ILE ILE A . n 
A 1 147 CYS 147 443 443 CYS CYS A . n 
A 1 148 ASN 148 444 444 ASN ASN A . n 
A 1 149 HIS 149 445 445 HIS HIS A . n 
A 1 150 VAL 150 446 446 VAL VAL A . n 
A 1 151 LYS 151 447 447 LYS LYS A . n 
A 1 152 TYR 152 448 448 TYR TYR A . n 
A 1 153 ALA 153 449 449 ALA ALA A . n 
A 1 154 THR 154 450 450 THR THR A . n 
A 1 155 ASN 155 451 451 ASN ASN A . n 
A 1 156 LYS 156 452 452 LYS LYS A . n 
A 1 157 GLY 157 453 453 GLY GLY A . n 
A 1 158 ASN 158 454 454 ASN ASN A . n 
A 1 159 LEU 159 455 455 LEU LEU A . n 
A 1 160 ARG 160 456 456 ARG ARG A . n 
A 1 161 SER 161 457 457 SER SER A . n 
A 1 162 ALA 162 458 458 ALA ALA A . n 
A 1 163 ILE 163 459 459 ILE ILE A . n 
A 1 164 THR 164 460 460 THR THR A . n 
A 1 165 ILE 165 461 461 ILE ILE A . n 
A 1 166 PHE 166 462 462 PHE PHE A . n 
A 1 167 PRO 167 463 463 PRO PRO A . n 
A 1 168 GLN 168 464 464 GLN GLN A . n 
A 1 169 ARG 169 465 465 ARG ARG A . n 
A 1 170 THR 170 466 466 THR THR A . n 
A 1 171 ASP 171 467 467 ASP ASP A . n 
A 1 172 GLY 172 468 468 GLY GLY A . n 
A 1 173 LYS 173 469 469 LYS LYS A . n 
A 1 174 HIS 174 470 470 HIS HIS A . n 
A 1 175 ASP 175 471 471 ASP ASP A . n 
A 1 176 PHE 176 472 472 PHE PHE A . n 
A 1 177 ARG 177 473 473 ARG ARG A . n 
A 1 178 VAL 178 474 474 VAL VAL A . n 
A 1 179 TRP 179 475 475 TRP TRP A . n 
A 1 180 ASN 180 476 476 ASN ASN A . n 
A 1 181 SER 181 477 477 SER SER A . n 
A 1 182 GLN 182 478 478 GLN GLN A . n 
A 1 183 LEU 183 479 479 LEU LEU A . n 
A 1 184 ILE 184 480 480 ILE ILE A . n 
A 1 185 ARG 185 481 481 ARG ARG A . n 
A 1 186 TYR 186 482 482 TYR TYR A . n 
A 1 187 ALA 187 483 483 ALA ALA A . n 
A 1 188 GLY 188 484 484 GLY GLY A . n 
A 1 189 TYR 189 485 485 TYR TYR A . n 
A 1 190 LYS 190 486 486 LYS LYS A . n 
A 1 191 GLN 191 487 487 GLN GLN A . n 
A 1 192 PRO 192 488 488 PRO PRO A . n 
A 1 193 ASP 193 489 489 ASP ASP A . n 
A 1 194 GLY 194 490 490 GLY GLY A . n 
A 1 195 SER 195 491 491 SER SER A . n 
A 1 196 THR 196 492 492 THR THR A . n 
A 1 197 LEU 197 493 493 LEU LEU A . n 
A 1 198 GLY 198 494 494 GLY GLY A . n 
A 1 199 ASP 199 495 495 ASP ASP A . n 
A 1 200 PRO 200 496 496 PRO PRO A . n 
A 1 201 ALA 201 497 497 ALA ALA A . n 
A 1 202 ASN 202 498 498 ASN ASN A . n 
A 1 203 VAL 203 499 499 VAL VAL A . n 
A 1 204 GLN 204 500 500 GLN GLN A . n 
A 1 205 PHE 205 501 501 PHE PHE A . n 
A 1 206 THR 206 502 502 THR THR A . n 
A 1 207 GLU 207 503 503 GLU GLU A . n 
A 1 208 ILE 208 504 504 ILE ILE A . n 
A 1 209 CYS 209 505 505 CYS CYS A . n 
A 1 210 ILE 210 506 506 ILE ILE A . n 
A 1 211 GLN 211 507 507 GLN GLN A . n 
A 1 212 GLN 212 508 508 GLN GLN A . n 
A 1 213 GLY 213 509 509 GLY GLY A . n 
A 1 214 TRP 214 510 510 TRP TRP A . n 
A 1 215 LYS 215 511 511 LYS LYS A . n 
A 1 216 ALA 216 512 512 ALA ALA A . n 
A 1 217 PRO 217 513 513 PRO PRO A . n 
A 1 218 ARG 218 514 514 ARG ARG A . n 
A 1 219 GLY 219 515 515 GLY GLY A . n 
A 1 220 ARG 220 516 516 ARG ARG A . n 
A 1 221 PHE 221 517 517 PHE PHE A . n 
A 1 222 ASP 222 518 518 ASP ASP A . n 
A 1 223 VAL 223 519 519 VAL VAL A . n 
A 1 224 LEU 224 520 520 LEU LEU A . n 
A 1 225 PRO 225 521 521 PRO PRO A . n 
A 1 226 LEU 226 522 522 LEU LEU A . n 
A 1 227 LEU 227 523 523 LEU LEU A . n 
A 1 228 LEU 228 524 524 LEU LEU A . n 
A 1 229 GLN 229 525 525 GLN GLN A . n 
A 1 230 ALA 230 526 526 ALA ALA A . n 
A 1 231 ASN 231 527 527 ASN ASN A . n 
A 1 232 GLY 232 528 528 GLY GLY A . n 
A 1 233 ASN 233 529 529 ASN ASN A . n 
A 1 234 ASP 234 530 530 ASP ASP A . n 
A 1 235 PRO 235 531 531 PRO PRO A . n 
A 1 236 GLU 236 532 532 GLU GLU A . n 
A 1 237 LEU 237 533 533 LEU LEU A . n 
A 1 238 PHE 238 534 534 PHE PHE A . n 
A 1 239 GLN 239 535 535 GLN GLN A . n 
A 1 240 ILE 240 536 536 ILE ILE A . n 
A 1 241 PRO 241 537 537 PRO PRO A . n 
A 1 242 PRO 242 538 538 PRO PRO A . n 
A 1 243 GLU 243 539 539 GLU GLU A . n 
A 1 244 LEU 244 540 540 LEU LEU A . n 
A 1 245 VAL 245 541 541 VAL VAL A . n 
A 1 246 LEU 246 542 542 LEU LEU A . n 
A 1 247 GLU 247 543 543 GLU GLU A . n 
A 1 248 VAL 248 544 544 VAL VAL A . n 
A 1 249 PRO 249 545 545 PRO PRO A . n 
A 1 250 ILE 250 546 546 ILE ILE A . n 
A 1 251 ARG 251 547 547 ARG ARG A . n 
A 1 252 HIS 252 548 548 HIS HIS A . n 
A 1 253 PRO 253 549 549 PRO PRO A . n 
A 1 254 LYS 254 550 550 LYS LYS A . n 
A 1 255 PHE 255 551 551 PHE PHE A . n 
A 1 256 ASP 256 552 552 ASP ASP A . n 
A 1 257 TRP 257 553 553 TRP TRP A . n 
A 1 258 PHE 258 554 554 PHE PHE A . n 
A 1 259 LYS 259 555 555 LYS LYS A . n 
A 1 260 ASP 260 556 556 ASP ASP A . n 
A 1 261 LEU 261 557 557 LEU LEU A . n 
A 1 262 GLY 262 558 558 GLY GLY A . n 
A 1 263 LEU 263 559 559 LEU LEU A . n 
A 1 264 LYS 264 560 560 LYS LYS A . n 
A 1 265 TRP 265 561 561 TRP TRP A . n 
A 1 266 TYR 266 562 562 TYR TYR A . n 
A 1 267 GLY 267 563 563 GLY GLY A . n 
A 1 268 LEU 268 564 564 LEU LEU A . n 
A 1 269 PRO 269 565 565 PRO PRO A . n 
A 1 270 ALA 270 566 566 ALA ALA A . n 
A 1 271 VAL 271 567 567 VAL VAL A . n 
A 1 272 SER 272 568 568 SER SER A . n 
A 1 273 ASN 273 569 569 ASN ASN A . n 
A 1 274 MET 274 570 570 MET MET A . n 
A 1 275 LEU 275 571 571 LEU LEU A . n 
A 1 276 LEU 276 572 572 LEU LEU A . n 
A 1 277 GLU 277 573 573 GLU GLU A . n 
A 1 278 ILE 278 574 574 ILE ILE A . n 
A 1 279 GLY 279 575 575 GLY GLY A . n 
A 1 280 GLY 280 576 576 GLY GLY A . n 
A 1 281 LEU 281 577 577 LEU LEU A . n 
A 1 282 GLU 282 578 578 GLU GLU A . n 
A 1 283 PHE 283 579 579 PHE PHE A . n 
A 1 284 SER 284 580 580 SER SER A . n 
A 1 285 ALA 285 581 581 ALA ALA A . n 
A 1 286 CYS 286 582 582 CYS CYS A . n 
A 1 287 PRO 287 583 583 PRO PRO A . n 
A 1 288 PHE 288 584 584 PHE PHE A . n 
A 1 289 SER 289 585 585 SER SER A . n 
A 1 290 GLY 290 586 586 GLY GLY A . n 
A 1 291 TRP 291 587 587 TRP TRP A . n 
A 1 292 TYR 292 588 588 TYR TYR A . n 
A 1 293 MET 293 589 589 MET MET A . n 
A 1 294 GLY 294 590 590 GLY GLY A . n 
A 1 295 THR 295 591 591 THR THR A . n 
A 1 296 GLU 296 592 592 GLU GLU A . n 
A 1 297 ILE 297 593 593 ILE ILE A . n 
A 1 298 GLY 298 594 594 GLY GLY A . n 
A 1 299 VAL 299 595 595 VAL VAL A . n 
A 1 300 ARG 300 596 596 ARG ARG A . n 
A 1 301 ASP 301 597 597 ASP ASP A . n 
A 1 302 TYR 302 598 598 TYR TYR A . n 
A 1 303 CYS 303 599 599 CYS CYS A . n 
A 1 304 ASP 304 600 600 ASP ASP A . n 
A 1 305 ASN 305 601 601 ASN ASN A . n 
A 1 306 SER 306 602 602 SER SER A . n 
A 1 307 ARG 307 603 603 ARG ARG A . n 
A 1 308 TYR 308 604 604 TYR TYR A . n 
A 1 309 ASN 309 605 605 ASN ASN A . n 
A 1 310 ILE 310 606 606 ILE ILE A . n 
A 1 311 LEU 311 607 607 LEU LEU A . n 
A 1 312 GLU 312 608 608 GLU GLU A . n 
A 1 313 GLU 313 609 609 GLU GLU A . n 
A 1 314 VAL 314 610 610 VAL VAL A . n 
A 1 315 ALA 315 611 611 ALA ALA A . n 
A 1 316 LYS 316 612 612 LYS LYS A . n 
A 1 317 LYS 317 613 613 LYS LYS A . n 
A 1 318 MET 318 614 614 MET MET A . n 
A 1 319 ASP 319 615 615 ASP ASP A . n 
A 1 320 LEU 320 616 616 LEU LEU A . n 
A 1 321 ASP 321 617 617 ASP ASP A . n 
A 1 322 MET 322 618 618 MET MET A . n 
A 1 323 ARG 323 619 619 ARG ARG A . n 
A 1 324 LYS 324 620 620 LYS LYS A . n 
A 1 325 THR 325 621 621 THR THR A . n 
A 1 326 SER 326 622 622 SER SER A . n 
A 1 327 SER 327 623 623 SER SER A . n 
A 1 328 LEU 328 624 624 LEU LEU A . n 
A 1 329 TRP 329 625 625 TRP TRP A . n 
A 1 330 LYS 330 626 626 LYS LYS A . n 
A 1 331 ASP 331 627 627 ASP ASP A . n 
A 1 332 GLN 332 628 628 GLN GLN A . n 
A 1 333 ALA 333 629 629 ALA ALA A . n 
A 1 334 LEU 334 630 630 LEU LEU A . n 
A 1 335 VAL 335 631 631 VAL VAL A . n 
A 1 336 GLU 336 632 632 GLU GLU A . n 
A 1 337 ILE 337 633 633 ILE ILE A . n 
A 1 338 ASN 338 634 634 ASN ASN A . n 
A 1 339 ILE 339 635 635 ILE ILE A . n 
A 1 340 ALA 340 636 636 ALA ALA A . n 
A 1 341 VAL 341 637 637 VAL VAL A . n 
A 1 342 LEU 342 638 638 LEU LEU A . n 
A 1 343 TYR 343 639 639 TYR TYR A . n 
A 1 344 SER 344 640 640 SER SER A . n 
A 1 345 PHE 345 641 641 PHE PHE A . n 
A 1 346 GLN 346 642 642 GLN GLN A . n 
A 1 347 SER 347 643 643 SER SER A . n 
A 1 348 ASP 348 644 644 ASP ASP A . n 
A 1 349 LYS 349 645 645 LYS LYS A . n 
A 1 350 VAL 350 646 646 VAL VAL A . n 
A 1 351 THR 351 647 647 THR THR A . n 
A 1 352 ILE 352 648 648 ILE ILE A . n 
A 1 353 VAL 353 649 649 VAL VAL A . n 
A 1 354 ASP 354 650 650 ASP ASP A . n 
A 1 355 HIS 355 651 651 HIS HIS A . n 
A 1 356 HIS 356 652 652 HIS HIS A . n 
A 1 357 SER 357 653 653 SER SER A . n 
A 1 358 ALA 358 654 654 ALA ALA A . n 
A 1 359 THR 359 655 655 THR THR A . n 
A 1 360 GLU 360 656 656 GLU GLU A . n 
A 1 361 SER 361 657 657 SER SER A . n 
A 1 362 PHE 362 658 658 PHE PHE A . n 
A 1 363 ILE 363 659 659 ILE ILE A . n 
A 1 364 LYS 364 660 660 LYS LYS A . n 
A 1 365 HIS 365 661 661 HIS HIS A . n 
A 1 366 MET 366 662 662 MET MET A . n 
A 1 367 GLU 367 663 663 GLU GLU A . n 
A 1 368 ASN 368 664 664 ASN ASN A . n 
A 1 369 GLU 369 665 665 GLU GLU A . n 
A 1 370 TYR 370 666 666 TYR TYR A . n 
A 1 371 ARG 371 667 667 ARG ARG A . n 
A 1 372 CYS 372 668 668 CYS CYS A . n 
A 1 373 ARG 373 669 669 ARG ARG A . n 
A 1 374 GLY 374 670 670 GLY GLY A . n 
A 1 375 GLY 375 671 671 GLY GLY A . n 
A 1 376 CYS 376 672 672 CYS CYS A . n 
A 1 377 PRO 377 673 673 PRO PRO A . n 
A 1 378 ALA 378 674 674 ALA ALA A . n 
A 1 379 ASP 379 675 675 ASP ASP A . n 
A 1 380 TRP 380 676 676 TRP TRP A . n 
A 1 381 VAL 381 677 677 VAL VAL A . n 
A 1 382 TRP 382 678 678 TRP TRP A . n 
A 1 383 ILE 383 679 679 ILE ILE A . n 
A 1 384 VAL 384 680 680 VAL VAL A . n 
A 1 385 PRO 385 681 681 PRO PRO A . n 
A 1 386 PRO 386 682 682 PRO PRO A . n 
A 1 387 MET 387 683 683 MET MET A . n 
A 1 388 SER 388 684 684 SER SER A . n 
A 1 389 GLY 389 685 685 GLY GLY A . n 
A 1 390 SER 390 686 686 SER SER A . n 
A 1 391 ILE 391 687 687 ILE ILE A . n 
A 1 392 THR 392 688 688 THR THR A . n 
A 1 393 PRO 393 689 689 PRO PRO A . n 
A 1 394 VAL 394 690 690 VAL VAL A . n 
A 1 395 PHE 395 691 691 PHE PHE A . n 
A 1 396 HIS 396 692 692 HIS HIS A . n 
A 1 397 GLN 397 693 693 GLN GLN A . n 
A 1 398 GLU 398 694 694 GLU GLU A . n 
A 1 399 MET 399 695 695 MET MET A . n 
A 1 400 LEU 400 696 696 LEU LEU A . n 
A 1 401 ASN 401 697 697 ASN ASN A . n 
A 1 402 TYR 402 698 698 TYR TYR A . n 
A 1 403 ARG 403 699 699 ARG ARG A . n 
A 1 404 LEU 404 700 700 LEU LEU A . n 
A 1 405 THR 405 701 701 THR THR A . n 
A 1 406 PRO 406 702 702 PRO PRO A . n 
A 1 407 SER 407 703 703 SER SER A . n 
A 1 408 PHE 408 704 704 PHE PHE A . n 
A 1 409 GLU 409 705 705 GLU GLU A . n 
A 1 410 TYR 410 706 706 TYR TYR A . n 
A 1 411 GLN 411 707 707 GLN GLN A . n 
A 1 412 PRO 412 708 708 PRO PRO A . n 
A 1 413 ASP 413 709 709 ASP ASP A . n 
A 1 414 PRO 414 710 710 PRO PRO A . n 
A 1 415 TRP 415 711 711 TRP TRP A . n 
A 1 416 ASN 416 712 712 ASN ASN A . n 
A 1 417 THR 417 713 713 THR THR A . n 
A 1 418 HIS 418 714 714 HIS HIS A . n 
A 1 419 VAL 419 715 715 VAL VAL A . n 
A 1 420 TRP 420 716 716 TRP TRP A . n 
A 1 421 LYS 421 717 717 LYS LYS A . n 
A 1 422 GLY 422 718 ?   ?   ?   A . n 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        A1AZ9 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   A1AZ9 
_pdbx_entity_instance_feature.auth_asym_id   ? 
_pdbx_entity_instance_feature.auth_seq_num   ? 
_pdbx_entity_instance_feature.feature_type   'SUBJECT OF INVESTIGATION' 
_pdbx_entity_instance_feature.details        ? 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
B 2 HEM   1  801 750 HEM   HEM A . 
C 3 H4B   1  802 760 H4B   BH4 A . 
D 4 ZN    1  803 900 ZN    ZN  A . 
E 5 A1AZ9 1  804 800 A1AZ9 2V9 A . 
F 6 HOH   1  901 10  HOH   HOH A . 
F 6 HOH   2  902 37  HOH   HOH A . 
F 6 HOH   3  903 26  HOH   HOH A . 
F 6 HOH   4  904 11  HOH   HOH A . 
F 6 HOH   5  905 20  HOH   HOH A . 
F 6 HOH   6  906 18  HOH   HOH A . 
F 6 HOH   7  907 25  HOH   HOH A . 
F 6 HOH   8  908 16  HOH   HOH A . 
F 6 HOH   9  909 14  HOH   HOH A . 
F 6 HOH   10 910 21  HOH   HOH A . 
F 6 HOH   11 911 39  HOH   HOH A . 
F 6 HOH   12 912 8   HOH   HOH A . 
F 6 HOH   13 913 22  HOH   HOH A . 
F 6 HOH   14 914 32  HOH   HOH A . 
F 6 HOH   15 915 19  HOH   HOH A . 
F 6 HOH   16 916 15  HOH   HOH A . 
F 6 HOH   17 917 31  HOH   HOH A . 
F 6 HOH   18 918 9   HOH   HOH A . 
F 6 HOH   19 919 1   HOH   HOH A . 
F 6 HOH   20 920 23  HOH   HOH A . 
F 6 HOH   21 921 5   HOH   HOH A . 
F 6 HOH   22 922 4   HOH   HOH A . 
F 6 HOH   23 923 7   HOH   HOH A . 
F 6 HOH   24 924 30  HOH   HOH A . 
F 6 HOH   25 925 2   HOH   HOH A . 
F 6 HOH   26 926 28  HOH   HOH A . 
F 6 HOH   27 927 34  HOH   HOH A . 
F 6 HOH   28 928 24  HOH   HOH A . 
F 6 HOH   29 929 33  HOH   HOH A . 
F 6 HOH   30 930 38  HOH   HOH A . 
F 6 HOH   31 931 27  HOH   HOH A . 
F 6 HOH   32 932 35  HOH   HOH A . 
F 6 HOH   33 933 12  HOH   HOH A . 
F 6 HOH   34 934 6   HOH   HOH A . 
F 6 HOH   35 935 17  HOH   HOH A . 
F 6 HOH   36 936 13  HOH   HOH A . 
F 6 HOH   37 937 36  HOH   HOH A . 
F 6 HOH   38 938 29  HOH   HOH A . 
F 6 HOH   39 939 3   HOH   HOH A . 
# 
loop_
_software.citation_id 
_software.classification 
_software.compiler_name 
_software.compiler_version 
_software.contact_author 
_software.contact_author_email 
_software.date 
_software.description 
_software.dependencies 
_software.hardware 
_software.language 
_software.location 
_software.mods 
_software.name 
_software.os 
_software.os_version 
_software.type 
_software.version 
_software.pdbx_ordinal 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? Aimless ? ? ? .           1 
? refinement       ? ? ? ? ? ? ? ? ? ? ? PHENIX  ? ? ? 1.11.1_2575 2 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? XDS     ? ? ? .           3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? REFMAC  ? ? ? .           4 
# 
_cell.angle_alpha                  90.00 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   90.00 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.00 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     9CVP 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     48.781 
_cell.length_a_esd                 ? 
_cell.length_b                     113.364 
_cell.length_b_esd                 ? 
_cell.length_c                     164.030 
_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                         9CVP 
_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                   9CVP 
_exptl.crystals_number            1 
_exptl.details                    ? 
_exptl.method                     'X-RAY DIFFRACTION' 
_exptl.method_details             ? 
# 
_exptl_crystal.colour                       ? 
_exptl_crystal.density_diffrn               ? 
_exptl_crystal.density_Matthews             2.48 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          50.4 
_exptl_crystal.description                  bricks 
_exptl_crystal.F_000                        ? 
_exptl_crystal.id                           1 
_exptl_crystal.preparation                  ? 
_exptl_crystal.size_max                     ? 
_exptl_crystal.size_mid                     ? 
_exptl_crystal.size_min                     ? 
_exptl_crystal.size_rad                     ? 
_exptl_crystal.colour_lustre                ? 
_exptl_crystal.colour_modifier              ? 
_exptl_crystal.colour_primary               ? 
_exptl_crystal.density_meas                 ? 
_exptl_crystal.density_meas_esd             ? 
_exptl_crystal.density_meas_gt              ? 
_exptl_crystal.density_meas_lt              ? 
_exptl_crystal.density_meas_temp            ? 
_exptl_crystal.density_meas_temp_esd        ? 
_exptl_crystal.density_meas_temp_gt         ? 
_exptl_crystal.density_meas_temp_lt         ? 
_exptl_crystal.pdbx_crystal_image_url       ? 
_exptl_crystal.pdbx_crystal_image_format    ? 
_exptl_crystal.pdbx_mosaicity               ? 
_exptl_crystal.pdbx_mosaicity_esd           ? 
_exptl_crystal.pdbx_mosaic_method           ? 
_exptl_crystal.pdbx_mosaic_block_size       ? 
_exptl_crystal.pdbx_mosaic_block_size_esd   ? 
# 
_exptl_crystal_grow.apparatus       ? 
_exptl_crystal_grow.atmosphere      ? 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.details         ? 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, SITTING DROP' 
_exptl_crystal_grow.method_ref      ? 
_exptl_crystal_grow.pH              5.8 
_exptl_crystal_grow.pressure        ? 
_exptl_crystal_grow.pressure_esd    ? 
_exptl_crystal_grow.seeding         ? 
_exptl_crystal_grow.seeding_ref     ? 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.temp_esd        ? 
_exptl_crystal_grow.time            ? 
_exptl_crystal_grow.pdbx_details    
;20-24% PEG3350, 0.1M MES
0.14-0.20M AMMONIUM ACETATE, 
10% ETHYLENE GLYCOL,
30uM SDS, 5 mM GSH
;
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            278 
# 
_diffrn.ambient_environment              ? 
_diffrn.ambient_temp                     100 
_diffrn.ambient_temp_details             ? 
_diffrn.ambient_temp_esd                 ? 
_diffrn.crystal_id                       1 
_diffrn.crystal_support                  ? 
_diffrn.crystal_treatment                ? 
_diffrn.details                          ? 
_diffrn.id                               1 
_diffrn.ambient_pressure                 ? 
_diffrn.ambient_pressure_esd             ? 
_diffrn.ambient_pressure_gt              ? 
_diffrn.ambient_pressure_lt              ? 
_diffrn.ambient_temp_gt                  ? 
_diffrn.ambient_temp_lt                  ? 
_diffrn.pdbx_serial_crystal_experiment   N 
# 
_diffrn_detector.details                      mirrors 
_diffrn_detector.detector                     CCD 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'ADSC QUANTUM 315' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2022-09-17 
_diffrn_detector.pdbx_frequency               ? 
_diffrn_detector.id                           ? 
_diffrn_detector.number_of_axes               ? 
# 
_diffrn_radiation.collimation                      ? 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.filter_edge                      ? 
_diffrn_radiation.inhomogeneity                    ? 
_diffrn_radiation.monochromator                    'DOUBLE CRYSTAL SI(III)' 
_diffrn_radiation.polarisn_norm                    ? 
_diffrn_radiation.polarisn_ratio                   ? 
_diffrn_radiation.probe                            ? 
_diffrn_radiation.type                             ? 
_diffrn_radiation.xray_symbol                      ? 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.pdbx_wavelength_list             ? 
_diffrn_radiation.pdbx_wavelength                  ? 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_analyzer                    ? 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   1.000 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.current                     ? 
_diffrn_source.details                     ? 
_diffrn_source.diffrn_id                   1 
_diffrn_source.power                       ? 
_diffrn_source.size                        ? 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.target                      ? 
_diffrn_source.type                        'ALS BEAMLINE 8.2.1' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        1.000 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   8.2.1 
_diffrn_source.pdbx_synchrotron_site       ALS 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       9CVP 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              1.97 
_reflns.d_resolution_low                               46.63 
_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                                     32396 
_reflns.observed_criterion                             ? 
_reflns.observed_criterion_F_max                       ? 
_reflns.observed_criterion_F_min                       ? 
_reflns.observed_criterion_I_max                       ? 
_reflns.observed_criterion_I_min                       ? 
_reflns.observed_criterion_sigma_F                     ? 
_reflns.observed_criterion_sigma_I                     ? 
_reflns.percent_possible_obs                           99.2 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                5.8 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          9.0 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               1.05 
_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                                0.128 
_reflns.pdbx_Rpim_I_all                                0.052 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       189140 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.999 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              0.116 
_reflns.pdbx_Rmerge_I_all                              ? 
_reflns.pdbx_Rsym_value                                ? 
_reflns.pdbx_CC_split_method                           ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_1                 ? 
_reflns.pdbx_aniso_diffraction_limit_2                 ? 
_reflns.pdbx_aniso_diffraction_limit_3                 ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_1               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_2               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_3               ? 
_reflns.pdbx_orthogonalization_convention              ? 
_reflns.pdbx_percent_possible_ellipsoidal              ? 
_reflns.pdbx_percent_possible_spherical                ? 
_reflns.pdbx_percent_possible_ellipsoidal_anomalous    ? 
_reflns.pdbx_percent_possible_spherical_anomalous      ? 
_reflns.pdbx_redundancy_anomalous                      ? 
_reflns.pdbx_CC_half_anomalous                         ? 
_reflns.pdbx_absDiff_over_sigma_anomalous              ? 
_reflns.pdbx_percent_possible_anomalous                ? 
_reflns.pdbx_observed_signal_threshold                 ? 
_reflns.pdbx_signal_type                               ? 
_reflns.pdbx_signal_details                            ? 
_reflns.pdbx_signal_software_id                        ? 
# 
_reflns_shell.d_res_high                                    1.97 
_reflns_shell.d_res_low                                     2.02 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           ? 
_reflns_shell.number_measured_all                           13333 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             2232 
_reflns_shell.percent_possible_obs                          99.2 
_reflns_shell.Rmerge_F_all                                  ? 
_reflns_shell.Rmerge_F_obs                                  ? 
_reflns_shell.meanI_over_sigI_gt                            ? 
_reflns_shell.meanI_over_uI_all                             ? 
_reflns_shell.meanI_over_uI_gt                              ? 
_reflns_shell.number_measured_gt                            ? 
_reflns_shell.number_unique_gt                              ? 
_reflns_shell.percent_possible_gt                           ? 
_reflns_shell.Rmerge_F_gt                                   ? 
_reflns_shell.Rmerge_I_gt                                   ? 
_reflns_shell.pdbx_redundancy                               6.0 
_reflns_shell.pdbx_chi_squared                              0.97 
_reflns_shell.pdbx_netI_over_sigmaI_all                     ? 
_reflns_shell.pdbx_netI_over_sigmaI_obs                     0.4 
_reflns_shell.pdbx_Rrim_I_all                               7.810 
_reflns_shell.pdbx_Rpim_I_all                               3.155 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.321 
_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                                  7.128 
_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                                 9CVP 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.ls_abs_structure_details                 ? 
_refine.ls_abs_structure_Flack                   ? 
_refine.ls_abs_structure_Flack_esd               ? 
_refine.ls_abs_structure_Rogers                  ? 
_refine.ls_abs_structure_Rogers_esd              ? 
_refine.ls_d_res_high                            1.970 
_refine.ls_d_res_low                             46.629 
_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                     30418 
_refine.ls_number_reflns_R_free                  2887 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    92.56 
_refine.ls_percent_reflns_R_free                 5.02 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.2313 
_refine.ls_R_factor_R_free                       0.2881 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.2283 
_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                 45.33 
_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                            0.28 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.overall_SU_R_free                        ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.pdbx_average_fsc_overall                 ? 
_refine.pdbx_average_fsc_work                    ? 
_refine.pdbx_average_fsc_free                    ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.pdbx_number_atoms_protein        3341 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         82 
_refine_hist.number_atoms_solvent             39 
_refine_hist.number_atoms_total               3462 
_refine_hist.d_res_high                       1.970 
_refine_hist.d_res_low                        46.629 
# 
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  ? 3531 ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 1.096  ? 4804 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 19.079 ? 2056 ? f_dihedral_angle_d ? ? 
'X-RAY DIFFRACTION' ? 0.049  ? 498  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.005  ? 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' 1.9700 2.0023 . . 108 2080 76.00  . . . . 0.4022 . . . . . . . . . . . 0.4489 
'X-RAY DIFFRACTION' 2.0023 2.0368 . . 104 2172 76.00  . . . . 0.3949 . . . . . . . . . . . 0.4205 
'X-RAY DIFFRACTION' 2.0368 2.0739 . . 85  2261 79.00  . . . . 0.4038 . . . . . . . . . . . 0.4800 
'X-RAY DIFFRACTION' 2.0739 2.1137 . . 133 2247 80.00  . . . . 0.3871 . . . . . . . . . . . 0.4899 
'X-RAY DIFFRACTION' 2.1137 2.1569 . . 124 2338 85.00  . . . . 0.3955 . . . . . . . . . . . 0.4486 
'X-RAY DIFFRACTION' 2.1569 2.2038 . . 124 2523 87.00  . . . . 0.4065 . . . . . . . . . . . 0.4814 
'X-RAY DIFFRACTION' 2.2038 2.2551 . . 155 2420 89.00  . . . . 0.4061 . . . . . . . . . . . 0.5165 
'X-RAY DIFFRACTION' 2.2551 2.3115 . . 146 2580 91.00  . . . . 0.3461 . . . . . . . . . . . 0.4774 
'X-RAY DIFFRACTION' 2.3115 2.3739 . . 140 2750 97.00  . . . . 0.3274 . . . . . . . . . . . 0.3874 
'X-RAY DIFFRACTION' 2.3739 2.4438 . . 138 2750 98.00  . . . . 0.3050 . . . . . . . . . . . 0.3800 
'X-RAY DIFFRACTION' 2.4438 2.5227 . . 134 2714 98.00  . . . . 0.3030 . . . . . . . . . . . 0.4240 
'X-RAY DIFFRACTION' 2.5227 2.6128 . . 116 2734 97.00  . . . . 0.3110 . . . . . . . . . . . 0.3719 
'X-RAY DIFFRACTION' 2.6128 2.7174 . . 147 2806 98.00  . . . . 0.3143 . . . . . . . . . . . 0.3986 
'X-RAY DIFFRACTION' 2.7174 2.8411 . . 140 2749 98.00  . . . . 0.2939 . . . . . . . . . . . 0.4049 
'X-RAY DIFFRACTION' 2.8411 2.9909 . . 116 2819 99.00  . . . . 0.2784 . . . . . . . . . . . 0.3682 
'X-RAY DIFFRACTION' 2.9909 3.1782 . . 171 2746 99.00  . . . . 0.2771 . . . . . . . . . . . 0.3853 
'X-RAY DIFFRACTION' 3.1782 3.4235 . . 176 2780 99.00  . . . . 0.2524 . . . . . . . . . . . 0.3252 
'X-RAY DIFFRACTION' 3.4235 3.7679 . . 156 2770 100.00 . . . . 0.2091 . . . . . . . . . . . 0.2428 
'X-RAY DIFFRACTION' 3.7679 4.3128 . . 162 2779 100.00 . . . . 0.1788 . . . . . . . . . . . 0.2262 
'X-RAY DIFFRACTION' 4.3128 5.4324 . . 156 2797 99.00  . . . . 0.1530 . . . . . . . . . . . 0.2052 
'X-RAY DIFFRACTION' 5.4324 46.629 . . 156 2788 99.00  . . . . 0.1518 . . . . . . . . . . . 0.1956 
# 
_struct.entry_id                     9CVP 
_struct.title                        
;Structure of rat neuronal nitric oxide synthase R349A mutant bound with 6-(2,3-difluoro-5-(((2-fluoroethyl)amino)methyl)phenyl)-4-methylpyridin-2-amine dihydrochloride
;
_struct.pdbx_model_details           ? 
_struct.pdbx_formula_weight          ? 
_struct.pdbx_formula_weight_method   ? 
_struct.pdbx_model_type_details      ? 
_struct.pdbx_CASP_flag               N 
# 
_struct_keywords.entry_id        9CVP 
_struct_keywords.text            'nitric oxide synthase inhibitor binding, OXIDOREDUCTASE' 
_struct_keywords.pdbx_keywords   OXIDOREDUCTASE 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 2 ? 
C N N 3 ? 
D N N 4 ? 
E N N 5 ? 
F N N 6 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    NOS1_RAT 
_struct_ref.pdbx_db_accession          P29476 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;CPRFLKVKNWETDVVLTDTLHLKSTLETGCTEHICMGSIMLPSQHTRKPEDVRTKDQLFPLAKEFLDQYYSSIKRFGSKA
HMDRLEEVNKEIESTSTYQLKDTELIYGAKHAWRNASRCVGRIQWSKLQVFDARDCTTAHGMFNYICNHVKYATNKGNLR
SAITIFPQRTDGKHDFRVWNSQLIRYAGYKQPDGSTLGDPANVQFTEICIQQGWKAPRGRFDVLPLLLQANGNDPELFQI
PPELVLEVPIRHPKFDWFKDLGLKWYGLPAVSNMLLEIGGLEFSACPFSGWYMGTEIGVRDYCDNSRYNILEEVAKKMDL
DMRKTSSLWKDQALVEINIAVLYSFQSDKVTIVDHHSATESFIKHMENEYRCRGGCPADWVWIVPPMSGSITPVFHQEML
NYRLTPSFEYQPDPWNTHVWKG
;
_struct_ref.pdbx_align_begin           297 
# 
_struct_ref_seq.align_id                      1 
_struct_ref_seq.ref_id                        1 
_struct_ref_seq.pdbx_PDB_id_code              9CVP 
_struct_ref_seq.pdbx_strand_id                A 
_struct_ref_seq.seq_align_beg                 1 
_struct_ref_seq.pdbx_seq_align_beg_ins_code   ? 
_struct_ref_seq.seq_align_end                 422 
_struct_ref_seq.pdbx_seq_align_end_ins_code   ? 
_struct_ref_seq.pdbx_db_accession             P29476 
_struct_ref_seq.db_align_beg                  297 
_struct_ref_seq.pdbx_db_align_beg_ins_code    ? 
_struct_ref_seq.db_align_end                  718 
_struct_ref_seq.pdbx_db_align_end_ins_code    ? 
_struct_ref_seq.pdbx_auth_seq_align_beg       297 
_struct_ref_seq.pdbx_auth_seq_align_end       718 
# 
_struct_ref_seq_dif.align_id                     1 
_struct_ref_seq_dif.pdbx_pdb_id_code             9CVP 
_struct_ref_seq_dif.mon_id                       ALA 
_struct_ref_seq_dif.pdbx_pdb_strand_id           A 
_struct_ref_seq_dif.seq_num                      53 
_struct_ref_seq_dif.pdbx_pdb_ins_code            ? 
_struct_ref_seq_dif.pdbx_seq_db_name             UNP 
_struct_ref_seq_dif.pdbx_seq_db_accession_code   P29476 
_struct_ref_seq_dif.db_mon_id                    ARG 
_struct_ref_seq_dif.pdbx_seq_db_seq_num          349 
_struct_ref_seq_dif.details                      'engineered mutation' 
_struct_ref_seq_dif.pdbx_auth_seq_num            349 
_struct_ref_seq_dif.pdbx_ordinal                 1 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_defined_assembly 
_pdbx_struct_assembly.method_details       ? 
_pdbx_struct_assembly.oligomeric_details   monomeric 
_pdbx_struct_assembly.oligomeric_count     1 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,D,E,F 
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   'gel filtration' 
_pdbx_struct_assembly_auth_evidence.details                ? 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1  AA1 THR A 19  ? SER A 24  ? THR A 315 SER A 320 5 ? 6  
HELX_P HELX_P2  AA2 THR A 54  ? ILE A 73  ? THR A 350 ILE A 369 1 ? 20 
HELX_P HELX_P3  AA3 SER A 78  ? THR A 95  ? SER A 374 THR A 391 1 ? 18 
HELX_P HELX_P4  AA4 LYS A 101 ? ASN A 115 ? LYS A 397 ASN A 411 1 ? 15 
HELX_P HELX_P5  AA5 GLY A 121 ? TRP A 125 ? GLY A 417 TRP A 421 5 ? 5  
HELX_P HELX_P6  AA6 THR A 138 ? ASN A 155 ? THR A 434 ASN A 451 1 ? 18 
HELX_P HELX_P7  AA7 LYS A 156 ? ASN A 158 ? LYS A 452 ASN A 454 5 ? 3  
HELX_P HELX_P8  AA8 ASN A 202 ? GLN A 212 ? ASN A 498 GLN A 508 1 ? 11 
HELX_P HELX_P9  AA9 PRO A 241 ? VAL A 245 ? PRO A 537 VAL A 541 5 ? 5  
HELX_P HELX_P10 AB1 PHE A 255 ? GLY A 262 ? PHE A 551 GLY A 558 5 ? 8  
HELX_P HELX_P11 AB2 GLY A 294 ? VAL A 299 ? GLY A 590 VAL A 595 1 ? 6  
HELX_P HELX_P12 AB3 VAL A 299 ? ASP A 304 ? VAL A 595 ASP A 600 1 ? 6  
HELX_P HELX_P13 AB4 ILE A 310 ? ASP A 319 ? ILE A 606 ASP A 615 1 ? 10 
HELX_P HELX_P14 AB5 LYS A 324 ? SER A 327 ? LYS A 620 SER A 623 5 ? 4  
HELX_P HELX_P15 AB6 LEU A 328 ? ASP A 348 ? LEU A 624 ASP A 644 1 ? 21 
HELX_P HELX_P16 AB7 ASP A 354 ? ARG A 373 ? ASP A 650 ARG A 669 1 ? 20 
HELX_P HELX_P17 AB8 ASP A 379 ? VAL A 384 ? ASP A 675 VAL A 680 1 ? 6  
HELX_P HELX_P18 AB9 SER A 388 ? GLN A 397 ? SER A 684 GLN A 693 5 ? 10 
HELX_P HELX_P19 AC1 ASP A 413 ? HIS A 418 ? ASP A 709 HIS A 714 1 ? 6  
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_conn.id 
_struct_conn.conn_type_id 
_struct_conn.pdbx_leaving_atom_flag 
_struct_conn.pdbx_PDB_id 
_struct_conn.ptnr1_label_asym_id 
_struct_conn.ptnr1_label_comp_id 
_struct_conn.ptnr1_label_seq_id 
_struct_conn.ptnr1_label_atom_id 
_struct_conn.pdbx_ptnr1_label_alt_id 
_struct_conn.pdbx_ptnr1_PDB_ins_code 
_struct_conn.pdbx_ptnr1_standard_comp_id 
_struct_conn.ptnr1_symmetry 
_struct_conn.ptnr2_label_asym_id 
_struct_conn.ptnr2_label_comp_id 
_struct_conn.ptnr2_label_seq_id 
_struct_conn.ptnr2_label_atom_id 
_struct_conn.pdbx_ptnr2_label_alt_id 
_struct_conn.pdbx_ptnr2_PDB_ins_code 
_struct_conn.ptnr1_auth_asym_id 
_struct_conn.ptnr1_auth_comp_id 
_struct_conn.ptnr1_auth_seq_id 
_struct_conn.ptnr2_auth_asym_id 
_struct_conn.ptnr2_auth_comp_id 
_struct_conn.ptnr2_auth_seq_id 
_struct_conn.ptnr2_symmetry 
_struct_conn.pdbx_ptnr3_label_atom_id 
_struct_conn.pdbx_ptnr3_label_seq_id 
_struct_conn.pdbx_ptnr3_label_comp_id 
_struct_conn.pdbx_ptnr3_label_asym_id 
_struct_conn.pdbx_ptnr3_label_alt_id 
_struct_conn.pdbx_ptnr3_PDB_ins_code 
_struct_conn.details 
_struct_conn.pdbx_dist_value 
_struct_conn.pdbx_value_order 
_struct_conn.pdbx_role 
metalc1 metalc ? ? A CYS 30  SG ? ? ? 1_555 D ZN  . ZN ? ? A CYS 326 A ZN  803 1_555 ? ? ? ? ? ? ? 2.398 ? ? 
metalc2 metalc ? ? A CYS 30  SG ? ? ? 1_555 D ZN  . ZN ? ? A CYS 326 A ZN  803 3_455 ? ? ? ? ? ? ? 2.402 ? ? 
metalc3 metalc ? ? A CYS 35  SG ? ? ? 1_555 D ZN  . ZN ? ? A CYS 331 A ZN  803 1_555 ? ? ? ? ? ? ? 2.380 ? ? 
metalc4 metalc ? ? A CYS 35  SG ? ? ? 1_555 D ZN  . ZN ? ? A CYS 331 A ZN  803 3_455 ? ? ? ? ? ? ? 2.368 ? ? 
metalc5 metalc ? ? A CYS 119 SG ? ? ? 1_555 B HEM . FE ? ? A CYS 415 A HEM 801 1_555 ? ? ? ? ? ? ? 2.405 ? ? 
# 
_struct_conn_type.id          metalc 
_struct_conn_type.criteria    ? 
_struct_conn_type.reference   ? 
# 
loop_
_pdbx_struct_conn_angle.id 
_pdbx_struct_conn_angle.ptnr1_label_atom_id 
_pdbx_struct_conn_angle.ptnr1_label_alt_id 
_pdbx_struct_conn_angle.ptnr1_label_asym_id 
_pdbx_struct_conn_angle.ptnr1_label_comp_id 
_pdbx_struct_conn_angle.ptnr1_label_seq_id 
_pdbx_struct_conn_angle.ptnr1_auth_atom_id 
_pdbx_struct_conn_angle.ptnr1_auth_asym_id 
_pdbx_struct_conn_angle.ptnr1_auth_comp_id 
_pdbx_struct_conn_angle.ptnr1_auth_seq_id 
_pdbx_struct_conn_angle.ptnr1_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr1_symmetry 
_pdbx_struct_conn_angle.ptnr2_label_atom_id 
_pdbx_struct_conn_angle.ptnr2_label_alt_id 
_pdbx_struct_conn_angle.ptnr2_label_asym_id 
_pdbx_struct_conn_angle.ptnr2_label_comp_id 
_pdbx_struct_conn_angle.ptnr2_label_seq_id 
_pdbx_struct_conn_angle.ptnr2_auth_atom_id 
_pdbx_struct_conn_angle.ptnr2_auth_asym_id 
_pdbx_struct_conn_angle.ptnr2_auth_comp_id 
_pdbx_struct_conn_angle.ptnr2_auth_seq_id 
_pdbx_struct_conn_angle.ptnr2_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr2_symmetry 
_pdbx_struct_conn_angle.ptnr3_label_atom_id 
_pdbx_struct_conn_angle.ptnr3_label_alt_id 
_pdbx_struct_conn_angle.ptnr3_label_asym_id 
_pdbx_struct_conn_angle.ptnr3_label_comp_id 
_pdbx_struct_conn_angle.ptnr3_label_seq_id 
_pdbx_struct_conn_angle.ptnr3_auth_atom_id 
_pdbx_struct_conn_angle.ptnr3_auth_asym_id 
_pdbx_struct_conn_angle.ptnr3_auth_comp_id 
_pdbx_struct_conn_angle.ptnr3_auth_seq_id 
_pdbx_struct_conn_angle.ptnr3_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr3_symmetry 
_pdbx_struct_conn_angle.value 
_pdbx_struct_conn_angle.value_esd 
1  SG ? A CYS 30  ? A CYS 326 ? 1_555 ZN ? D ZN  . ? A ZN  803 ? 1_555 SG ? A CYS 30 ? A CYS 326 ? 1_555 0.0   ? 
2  SG ? A CYS 30  ? A CYS 326 ? 1_555 ZN ? D ZN  . ? A ZN  803 ? 1_555 SG ? A CYS 35 ? A CYS 331 ? 1_555 110.3 ? 
3  SG ? A CYS 30  ? A CYS 326 ? 1_555 ZN ? D ZN  . ? A ZN  803 ? 1_555 SG ? A CYS 35 ? A CYS 331 ? 1_555 110.3 ? 
4  SG ? A CYS 30  ? A CYS 326 ? 1_555 ZN ? D ZN  . ? A ZN  803 ? 1_555 SG ? A CYS 35 ? A CYS 331 ? 1_555 110.3 ? 
5  SG ? A CYS 30  ? A CYS 326 ? 1_555 ZN ? D ZN  . ? A ZN  803 ? 1_555 SG ? A CYS 35 ? A CYS 331 ? 1_555 110.3 ? 
6  SG ? A CYS 35  ? A CYS 331 ? 1_555 ZN ? D ZN  . ? A ZN  803 ? 1_555 SG ? A CYS 35 ? A CYS 331 ? 1_555 0.0   ? 
7  SG ? A CYS 119 ? A CYS 415 ? 1_555 FE ? B HEM . ? A HEM 801 ? 1_555 NA ? B HEM .  ? A HEM 801 ? 1_555 102.3 ? 
8  SG ? A CYS 119 ? A CYS 415 ? 1_555 FE ? B HEM . ? A HEM 801 ? 1_555 NB ? B HEM .  ? A HEM 801 ? 1_555 98.3  ? 
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 85.9  ? 
10 SG ? A CYS 119 ? A CYS 415 ? 1_555 FE ? B HEM . ? A HEM 801 ? 1_555 NC ? B HEM .  ? A HEM 801 ? 1_555 100.1 ? 
11 NA ? B HEM .   ? A HEM 801 ? 1_555 FE ? B HEM . ? A HEM 801 ? 1_555 NC ? B HEM .  ? A HEM 801 ? 1_555 155.8 ? 
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 82.0  ? 
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_555 111.4 ? 
14 NA ? B HEM .   ? A HEM 801 ? 1_555 FE ? B HEM . ? A HEM 801 ? 1_555 ND ? B HEM .  ? A HEM 801 ? 1_555 89.9  ? 
15 NB ? B HEM .   ? A HEM 801 ? 1_555 FE ? B HEM . ? A HEM 801 ? 1_555 ND ? B HEM .  ? A HEM 801 ? 1_555 150.2 ? 
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 90.3  ? 
# 
_struct_mon_prot_cis.pdbx_id                1 
_struct_mon_prot_cis.label_comp_id          THR 
_struct_mon_prot_cis.label_seq_id           405 
_struct_mon_prot_cis.label_asym_id          A 
_struct_mon_prot_cis.label_alt_id           . 
_struct_mon_prot_cis.pdbx_PDB_ins_code      ? 
_struct_mon_prot_cis.auth_comp_id           THR 
_struct_mon_prot_cis.auth_seq_id            701 
_struct_mon_prot_cis.auth_asym_id           A 
_struct_mon_prot_cis.pdbx_label_comp_id_2   PRO 
_struct_mon_prot_cis.pdbx_label_seq_id_2    406 
_struct_mon_prot_cis.pdbx_label_asym_id_2   A 
_struct_mon_prot_cis.pdbx_PDB_ins_code_2    ? 
_struct_mon_prot_cis.pdbx_auth_comp_id_2    PRO 
_struct_mon_prot_cis.pdbx_auth_seq_id_2     702 
_struct_mon_prot_cis.pdbx_auth_asym_id_2    A 
_struct_mon_prot_cis.pdbx_PDB_model_num     1 
_struct_mon_prot_cis.pdbx_omega_angle       -1.90 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 2 ? 
AA2 ? 4 ? 
AA3 ? 3 ? 
AA4 ? 2 ? 
AA5 ? 2 ? 
AA6 ? 3 ? 
AA7 ? 2 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? anti-parallel 
AA2 1 2 ? parallel      
AA2 2 3 ? anti-parallel 
AA2 3 4 ? anti-parallel 
AA3 1 2 ? anti-parallel 
AA3 2 3 ? anti-parallel 
AA4 1 2 ? anti-parallel 
AA5 1 2 ? anti-parallel 
AA6 1 2 ? anti-parallel 
AA6 2 3 ? anti-parallel 
AA7 1 2 ? parallel      
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 LYS A 6   ? LYS A 8   ? LYS A 302 LYS A 304 
AA1 2 VAL A 15  ? THR A 17  ? VAL A 311 THR A 313 
AA2 1 GLN A 129 ? ASP A 132 ? GLN A 425 ASP A 428 
AA2 2 ALA A 162 ? ILE A 165 ? ALA A 458 ILE A 461 
AA2 3 PHE A 288 ? SER A 289 ? PHE A 584 SER A 585 
AA2 4 ALA A 270 ? VAL A 271 ? ALA A 566 VAL A 567 
AA3 1 ARG A 177 ? VAL A 178 ? ARG A 473 VAL A 474 
AA3 2 LEU A 226 ? GLN A 229 ? LEU A 522 GLN A 525 
AA3 3 GLU A 236 ? PHE A 238 ? GLU A 532 PHE A 534 
AA4 1 GLY A 188 ? LYS A 190 ? GLY A 484 LYS A 486 
AA4 2 THR A 196 ? GLY A 198 ? THR A 492 GLY A 494 
AA5 1 GLU A 247 ? PRO A 249 ? GLU A 543 PRO A 545 
AA5 2 LYS A 264 ? TYR A 266 ? LYS A 560 TYR A 562 
AA6 1 LEU A 281 ? PHE A 283 ? LEU A 577 PHE A 579 
AA6 2 LEU A 275 ? ILE A 278 ? LEU A 571 ILE A 574 
AA6 3 SER A 407 ? GLU A 409 ? SER A 703 GLU A 705 
AA7 1 TYR A 292 ? MET A 293 ? TYR A 588 MET A 589 
AA7 2 ILE A 352 ? VAL A 353 ? ILE A 648 VAL A 649 
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2 N VAL A 7   ? N VAL A 303 O LEU A 16  ? O LEU A 312 
AA2 1 2 N PHE A 131 ? N PHE A 427 O ILE A 163 ? O ILE A 459 
AA2 2 3 N ALA A 162 ? N ALA A 458 O SER A 289 ? O SER A 585 
AA2 3 4 O PHE A 288 ? O PHE A 584 N VAL A 271 ? N VAL A 567 
AA3 1 2 N ARG A 177 ? N ARG A 473 O GLN A 229 ? O GLN A 525 
AA3 2 3 N LEU A 226 ? N LEU A 522 O PHE A 238 ? O PHE A 534 
AA4 1 2 N TYR A 189 ? N TYR A 485 O LEU A 197 ? O LEU A 493 
AA5 1 2 N VAL A 248 ? N VAL A 544 O TRP A 265 ? O TRP A 561 
AA6 1 2 O LEU A 281 ? O LEU A 577 N ILE A 278 ? N ILE A 574 
AA6 2 3 N 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                   9CVP 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.has_protein_modification   N 
# 
loop_
_pdbx_validate_close_contact.id 
_pdbx_validate_close_contact.PDB_model_num 
_pdbx_validate_close_contact.auth_atom_id_1 
_pdbx_validate_close_contact.auth_asym_id_1 
_pdbx_validate_close_contact.auth_comp_id_1 
_pdbx_validate_close_contact.auth_seq_id_1 
_pdbx_validate_close_contact.PDB_ins_code_1 
_pdbx_validate_close_contact.label_alt_id_1 
_pdbx_validate_close_contact.auth_atom_id_2 
_pdbx_validate_close_contact.auth_asym_id_2 
_pdbx_validate_close_contact.auth_comp_id_2 
_pdbx_validate_close_contact.auth_seq_id_2 
_pdbx_validate_close_contact.PDB_ins_code_2 
_pdbx_validate_close_contact.label_alt_id_2 
_pdbx_validate_close_contact.dist 
1 1 O   A VAL 348 ? ? O A HOH 901 ? ? 2.06 
2 1 OD2 A ASP 530 ? ? O A HOH 902 ? ? 2.12 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1  1 ARG A 371 ? ? -112.36 60.71   
2  1 SER A 374 ? ? -64.15  -178.35 
3  1 THR A 393 ? ? -163.91 -169.98 
4  1 THR A 466 ? ? -121.94 -98.05  
5  1 SER A 491 ? ? -66.50  -176.29 
6  1 ARG A 514 ? ? 15.40   63.90   
7  1 ARG A 516 ? ? -87.70  -80.94  
8  1 LYS A 550 ? ? -124.88 -52.71  
9  1 CYS A 582 ? ? -153.73 55.51   
10 1 ARG A 603 ? ? -113.38 -130.51 
11 1 ASP A 615 ? ? 59.98   79.24   
12 1 ARG A 669 ? ? -154.81 -18.18  
13 1 CYS A 672 ? ? -163.96 100.60  
# 
_pdbx_struct_special_symmetry.id              1 
_pdbx_struct_special_symmetry.PDB_model_num   1 
_pdbx_struct_special_symmetry.auth_asym_id    A 
_pdbx_struct_special_symmetry.auth_comp_id    ZN 
_pdbx_struct_special_symmetry.auth_seq_id     803 
_pdbx_struct_special_symmetry.PDB_ins_code    ? 
_pdbx_struct_special_symmetry.label_asym_id   D 
_pdbx_struct_special_symmetry.label_comp_id   ZN 
_pdbx_struct_special_symmetry.label_seq_id    . 
# 
_pdbx_refine_tls.id               1 
_pdbx_refine_tls.pdbx_refine_id   'X-RAY DIFFRACTION' 
_pdbx_refine_tls.details          ? 
_pdbx_refine_tls.method           refined 
_pdbx_refine_tls.origin_x         -23.6282 
_pdbx_refine_tls.origin_y         -4.8865 
_pdbx_refine_tls.origin_z         22.3232 
_pdbx_refine_tls.T[1][1]          0.3356 
_pdbx_refine_tls.T[1][1]_esd      ? 
_pdbx_refine_tls.T[1][2]          -0.0307 
_pdbx_refine_tls.T[1][2]_esd      ? 
_pdbx_refine_tls.T[1][3]          -0.0903 
_pdbx_refine_tls.T[1][3]_esd      ? 
_pdbx_refine_tls.T[2][2]          0.3638 
_pdbx_refine_tls.T[2][2]_esd      ? 
_pdbx_refine_tls.T[2][3]          -0.0093 
_pdbx_refine_tls.T[2][3]_esd      ? 
_pdbx_refine_tls.T[3][3]          0.4336 
_pdbx_refine_tls.T[3][3]_esd      ? 
_pdbx_refine_tls.L[1][1]          1.1740 
_pdbx_refine_tls.L[1][1]_esd      ? 
_pdbx_refine_tls.L[1][2]          -0.0837 
_pdbx_refine_tls.L[1][2]_esd      ? 
_pdbx_refine_tls.L[1][3]          0.5234 
_pdbx_refine_tls.L[1][3]_esd      ? 
_pdbx_refine_tls.L[2][2]          1.7575 
_pdbx_refine_tls.L[2][2]_esd      ? 
_pdbx_refine_tls.L[2][3]          -0.2534 
_pdbx_refine_tls.L[2][3]_esd      ? 
_pdbx_refine_tls.L[3][3]          9.6729 
_pdbx_refine_tls.L[3][3]_esd      ? 
_pdbx_refine_tls.S[1][1]          -0.0481 
_pdbx_refine_tls.S[1][1]_esd      ? 
_pdbx_refine_tls.S[1][2]          0.1985 
_pdbx_refine_tls.S[1][2]_esd      ? 
_pdbx_refine_tls.S[1][3]          0.0510 
_pdbx_refine_tls.S[1][3]_esd      ? 
_pdbx_refine_tls.S[2][1]          0.0262 
_pdbx_refine_tls.S[2][1]_esd      ? 
_pdbx_refine_tls.S[2][2]          -0.0133 
_pdbx_refine_tls.S[2][2]_esd      ? 
_pdbx_refine_tls.S[2][3]          -0.0639 
_pdbx_refine_tls.S[2][3]_esd      ? 
_pdbx_refine_tls.S[3][1]          -0.9908 
_pdbx_refine_tls.S[3][1]_esd      ? 
_pdbx_refine_tls.S[3][2]          0.3370 
_pdbx_refine_tls.S[3][2]_esd      ? 
_pdbx_refine_tls.S[3][3]          0.0224 
_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 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 
A1AZ9 C14  C  Y N 1   
A1AZ9 C13  C  Y N 2   
A1AZ9 C12  C  Y N 3   
A1AZ9 C11  C  Y N 4   
A1AZ9 C15  C  Y N 5   
A1AZ9 C16  C  Y N 6   
A1AZ9 C17  C  N N 7   
A1AZ9 C19  C  N N 8   
A1AZ9 C20  C  N N 9   
A1AZ9 C02  C  Y N 10  
A1AZ9 C03  C  Y N 11  
A1AZ9 C04  C  Y N 12  
A1AZ9 C05  C  Y N 13  
A1AZ9 C06  C  Y N 14  
A1AZ9 C07  C  N N 15  
A1AZ9 F12  F  N N 16  
A1AZ9 F13  F  N N 17  
A1AZ9 F21  F  N N 18  
A1AZ9 N01  N  Y N 19  
A1AZ9 N02  N  N N 20  
A1AZ9 N18  N  N N 21  
A1AZ9 H1   H  N N 22  
A1AZ9 H2   H  N N 23  
A1AZ9 H3   H  N N 24  
A1AZ9 H4   H  N N 25  
A1AZ9 H5   H  N N 26  
A1AZ9 H6   H  N N 27  
A1AZ9 H7   H  N N 28  
A1AZ9 H8   H  N N 29  
A1AZ9 H9   H  N N 30  
A1AZ9 H10  H  N N 31  
A1AZ9 H11  H  N N 32  
A1AZ9 H12  H  N N 33  
A1AZ9 H13  H  N N 34  
A1AZ9 H14  H  N N 35  
A1AZ9 H15  H  N N 36  
A1AZ9 H16  H  N N 37  
ALA   N    N  N N 38  
ALA   CA   C  N S 39  
ALA   C    C  N N 40  
ALA   O    O  N N 41  
ALA   CB   C  N N 42  
ALA   OXT  O  N N 43  
ALA   H    H  N N 44  
ALA   H2   H  N N 45  
ALA   HA   H  N N 46  
ALA   HB1  H  N N 47  
ALA   HB2  H  N N 48  
ALA   HB3  H  N N 49  
ALA   HXT  H  N N 50  
ARG   N    N  N N 51  
ARG   CA   C  N S 52  
ARG   C    C  N N 53  
ARG   O    O  N N 54  
ARG   CB   C  N N 55  
ARG   CG   C  N N 56  
ARG   CD   C  N N 57  
ARG   NE   N  N N 58  
ARG   CZ   C  N N 59  
ARG   NH1  N  N N 60  
ARG   NH2  N  N N 61  
ARG   OXT  O  N N 62  
ARG   H    H  N N 63  
ARG   H2   H  N N 64  
ARG   HA   H  N N 65  
ARG   HB2  H  N N 66  
ARG   HB3  H  N N 67  
ARG   HG2  H  N N 68  
ARG   HG3  H  N N 69  
ARG   HD2  H  N N 70  
ARG   HD3  H  N N 71  
ARG   HE   H  N N 72  
ARG   HH11 H  N N 73  
ARG   HH12 H  N N 74  
ARG   HH21 H  N N 75  
ARG   HH22 H  N N 76  
ARG   HXT  H  N N 77  
ASN   N    N  N N 78  
ASN   CA   C  N S 79  
ASN   C    C  N N 80  
ASN   O    O  N N 81  
ASN   CB   C  N N 82  
ASN   CG   C  N N 83  
ASN   OD1  O  N N 84  
ASN   ND2  N  N N 85  
ASN   OXT  O  N N 86  
ASN   H    H  N N 87  
ASN   H2   H  N N 88  
ASN   HA   H  N N 89  
ASN   HB2  H  N N 90  
ASN   HB3  H  N N 91  
ASN   HD21 H  N N 92  
ASN   HD22 H  N N 93  
ASN   HXT  H  N N 94  
ASP   N    N  N N 95  
ASP   CA   C  N S 96  
ASP   C    C  N N 97  
ASP   O    O  N N 98  
ASP   CB   C  N N 99  
ASP   CG   C  N N 100 
ASP   OD1  O  N N 101 
ASP   OD2  O  N N 102 
ASP   OXT  O  N N 103 
ASP   H    H  N N 104 
ASP   H2   H  N N 105 
ASP   HA   H  N N 106 
ASP   HB2  H  N N 107 
ASP   HB3  H  N N 108 
ASP   HD2  H  N N 109 
ASP   HXT  H  N N 110 
CYS   N    N  N N 111 
CYS   CA   C  N R 112 
CYS   C    C  N N 113 
CYS   O    O  N N 114 
CYS   CB   C  N N 115 
CYS   SG   S  N N 116 
CYS   OXT  O  N N 117 
CYS   H    H  N N 118 
CYS   H2   H  N N 119 
CYS   HA   H  N N 120 
CYS   HB2  H  N N 121 
CYS   HB3  H  N N 122 
CYS   HG   H  N N 123 
CYS   HXT  H  N N 124 
GLN   N    N  N N 125 
GLN   CA   C  N S 126 
GLN   C    C  N N 127 
GLN   O    O  N N 128 
GLN   CB   C  N N 129 
GLN   CG   C  N N 130 
GLN   CD   C  N N 131 
GLN   OE1  O  N N 132 
GLN   NE2  N  N N 133 
GLN   OXT  O  N N 134 
GLN   H    H  N N 135 
GLN   H2   H  N N 136 
GLN   HA   H  N N 137 
GLN   HB2  H  N N 138 
GLN   HB3  H  N N 139 
GLN   HG2  H  N N 140 
GLN   HG3  H  N N 141 
GLN   HE21 H  N N 142 
GLN   HE22 H  N N 143 
GLN   HXT  H  N N 144 
GLU   N    N  N N 145 
GLU   CA   C  N S 146 
GLU   C    C  N N 147 
GLU   O    O  N N 148 
GLU   CB   C  N N 149 
GLU   CG   C  N N 150 
GLU   CD   C  N N 151 
GLU   OE1  O  N N 152 
GLU   OE2  O  N N 153 
GLU   OXT  O  N N 154 
GLU   H    H  N N 155 
GLU   H2   H  N N 156 
GLU   HA   H  N N 157 
GLU   HB2  H  N N 158 
GLU   HB3  H  N N 159 
GLU   HG2  H  N N 160 
GLU   HG3  H  N N 161 
GLU   HE2  H  N N 162 
GLU   HXT  H  N N 163 
GLY   N    N  N N 164 
GLY   CA   C  N N 165 
GLY   C    C  N N 166 
GLY   O    O  N N 167 
GLY   OXT  O  N N 168 
GLY   H    H  N N 169 
GLY   H2   H  N N 170 
GLY   HA2  H  N N 171 
GLY   HA3  H  N N 172 
GLY   HXT  H  N N 173 
H4B   N1   N  Y N 174 
H4B   C2   C  Y N 175 
H4B   N2   N  N N 176 
H4B   N3   N  Y N 177 
H4B   C4   C  Y N 178 
H4B   O4   O  N N 179 
H4B   C4A  C  Y N 180 
H4B   C8A  C  Y N 181 
H4B   N5   N  N N 182 
H4B   N8   N  N N 183 
H4B   C6   C  N R 184 
H4B   C7   C  N N 185 
H4B   C9   C  N R 186 
H4B   O9   O  N N 187 
H4B   C10  C  N S 188 
H4B   C11  C  N N 189 
H4B   O10  O  N N 190 
H4B   HN21 H  N N 191 
H4B   HN22 H  N N 192 
H4B   HN3  H  N N 193 
H4B   HN5  H  N N 194 
H4B   HN8  H  N N 195 
H4B   H6   H  N N 196 
H4B   H71  H  N N 197 
H4B   H72  H  N N 198 
H4B   H9   H  N N 199 
H4B   HO9  H  N N 200 
H4B   H10  H  N N 201 
H4B   H111 H  N N 202 
H4B   H112 H  N N 203 
H4B   H113 H  N N 204 
H4B   HO0  H  N N 205 
HEM   CHA  C  N N 206 
HEM   CHB  C  N N 207 
HEM   CHC  C  N N 208 
HEM   CHD  C  N N 209 
HEM   C1A  C  Y N 210 
HEM   C2A  C  Y N 211 
HEM   C3A  C  Y N 212 
HEM   C4A  C  Y N 213 
HEM   CMA  C  N N 214 
HEM   CAA  C  N N 215 
HEM   CBA  C  N N 216 
HEM   CGA  C  N N 217 
HEM   O1A  O  N N 218 
HEM   O2A  O  N N 219 
HEM   C1B  C  N N 220 
HEM   C2B  C  N N 221 
HEM   C3B  C  N N 222 
HEM   C4B  C  N N 223 
HEM   CMB  C  N N 224 
HEM   CAB  C  N N 225 
HEM   CBB  C  N N 226 
HEM   C1C  C  Y N 227 
HEM   C2C  C  Y N 228 
HEM   C3C  C  Y N 229 
HEM   C4C  C  Y N 230 
HEM   CMC  C  N N 231 
HEM   CAC  C  N N 232 
HEM   CBC  C  N N 233 
HEM   C1D  C  N N 234 
HEM   C2D  C  N N 235 
HEM   C3D  C  N N 236 
HEM   C4D  C  N N 237 
HEM   CMD  C  N N 238 
HEM   CAD  C  N N 239 
HEM   CBD  C  N N 240 
HEM   CGD  C  N N 241 
HEM   O1D  O  N N 242 
HEM   O2D  O  N N 243 
HEM   NA   N  Y N 244 
HEM   NB   N  N N 245 
HEM   NC   N  Y N 246 
HEM   ND   N  N N 247 
HEM   FE   FE N N 248 
HEM   HHB  H  N N 249 
HEM   HHC  H  N N 250 
HEM   HHD  H  N N 251 
HEM   HMA  H  N N 252 
HEM   HMAA H  N N 253 
HEM   HMAB H  N N 254 
HEM   HAA  H  N N 255 
HEM   HAAA H  N N 256 
HEM   HBA  H  N N 257 
HEM   HBAA H  N N 258 
HEM   HMB  H  N N 259 
HEM   HMBA H  N N 260 
HEM   HMBB H  N N 261 
HEM   HAB  H  N N 262 
HEM   HBB  H  N N 263 
HEM   HBBA H  N N 264 
HEM   HMC  H  N N 265 
HEM   HMCA H  N N 266 
HEM   HMCB H  N N 267 
HEM   HAC  H  N N 268 
HEM   HBC  H  N N 269 
HEM   HBCA H  N N 270 
HEM   HMD  H  N N 271 
HEM   HMDA H  N N 272 
HEM   HMDB H  N N 273 
HEM   HAD  H  N N 274 
HEM   HADA H  N N 275 
HEM   HBD  H  N N 276 
HEM   HBDA H  N N 277 
HEM   H2A  H  N N 278 
HEM   H2D  H  N N 279 
HEM   HHA  H  N N 280 
HIS   N    N  N N 281 
HIS   CA   C  N S 282 
HIS   C    C  N N 283 
HIS   O    O  N N 284 
HIS   CB   C  N N 285 
HIS   CG   C  Y N 286 
HIS   ND1  N  Y N 287 
HIS   CD2  C  Y N 288 
HIS   CE1  C  Y N 289 
HIS   NE2  N  Y N 290 
HIS   OXT  O  N N 291 
HIS   H    H  N N 292 
HIS   H2   H  N N 293 
HIS   HA   H  N N 294 
HIS   HB2  H  N N 295 
HIS   HB3  H  N N 296 
HIS   HD1  H  N N 297 
HIS   HD2  H  N N 298 
HIS   HE1  H  N N 299 
HIS   HE2  H  N N 300 
HIS   HXT  H  N N 301 
HOH   O    O  N N 302 
HOH   H1   H  N N 303 
HOH   H2   H  N N 304 
ILE   N    N  N N 305 
ILE   CA   C  N S 306 
ILE   C    C  N N 307 
ILE   O    O  N N 308 
ILE   CB   C  N S 309 
ILE   CG1  C  N N 310 
ILE   CG2  C  N N 311 
ILE   CD1  C  N N 312 
ILE   OXT  O  N N 313 
ILE   H    H  N N 314 
ILE   H2   H  N N 315 
ILE   HA   H  N N 316 
ILE   HB   H  N N 317 
ILE   HG12 H  N N 318 
ILE   HG13 H  N N 319 
ILE   HG21 H  N N 320 
ILE   HG22 H  N N 321 
ILE   HG23 H  N N 322 
ILE   HD11 H  N N 323 
ILE   HD12 H  N N 324 
ILE   HD13 H  N N 325 
ILE   HXT  H  N N 326 
LEU   N    N  N N 327 
LEU   CA   C  N S 328 
LEU   C    C  N N 329 
LEU   O    O  N N 330 
LEU   CB   C  N N 331 
LEU   CG   C  N N 332 
LEU   CD1  C  N N 333 
LEU   CD2  C  N N 334 
LEU   OXT  O  N N 335 
LEU   H    H  N N 336 
LEU   H2   H  N N 337 
LEU   HA   H  N N 338 
LEU   HB2  H  N N 339 
LEU   HB3  H  N N 340 
LEU   HG   H  N N 341 
LEU   HD11 H  N N 342 
LEU   HD12 H  N N 343 
LEU   HD13 H  N N 344 
LEU   HD21 H  N N 345 
LEU   HD22 H  N N 346 
LEU   HD23 H  N N 347 
LEU   HXT  H  N N 348 
LYS   N    N  N N 349 
LYS   CA   C  N S 350 
LYS   C    C  N N 351 
LYS   O    O  N N 352 
LYS   CB   C  N N 353 
LYS   CG   C  N N 354 
LYS   CD   C  N N 355 
LYS   CE   C  N N 356 
LYS   NZ   N  N N 357 
LYS   OXT  O  N N 358 
LYS   H    H  N N 359 
LYS   H2   H  N N 360 
LYS   HA   H  N N 361 
LYS   HB2  H  N N 362 
LYS   HB3  H  N N 363 
LYS   HG2  H  N N 364 
LYS   HG3  H  N N 365 
LYS   HD2  H  N N 366 
LYS   HD3  H  N N 367 
LYS   HE2  H  N N 368 
LYS   HE3  H  N N 369 
LYS   HZ1  H  N N 370 
LYS   HZ2  H  N N 371 
LYS   HZ3  H  N N 372 
LYS   HXT  H  N N 373 
MET   N    N  N N 374 
MET   CA   C  N S 375 
MET   C    C  N N 376 
MET   O    O  N N 377 
MET   CB   C  N N 378 
MET   CG   C  N N 379 
MET   SD   S  N N 380 
MET   CE   C  N N 381 
MET   OXT  O  N N 382 
MET   H    H  N N 383 
MET   H2   H  N N 384 
MET   HA   H  N N 385 
MET   HB2  H  N N 386 
MET   HB3  H  N N 387 
MET   HG2  H  N N 388 
MET   HG3  H  N N 389 
MET   HE1  H  N N 390 
MET   HE2  H  N N 391 
MET   HE3  H  N N 392 
MET   HXT  H  N N 393 
PHE   N    N  N N 394 
PHE   CA   C  N S 395 
PHE   C    C  N N 396 
PHE   O    O  N N 397 
PHE   CB   C  N N 398 
PHE   CG   C  Y N 399 
PHE   CD1  C  Y N 400 
PHE   CD2  C  Y N 401 
PHE   CE1  C  Y N 402 
PHE   CE2  C  Y N 403 
PHE   CZ   C  Y N 404 
PHE   OXT  O  N N 405 
PHE   H    H  N N 406 
PHE   H2   H  N N 407 
PHE   HA   H  N N 408 
PHE   HB2  H  N N 409 
PHE   HB3  H  N N 410 
PHE   HD1  H  N N 411 
PHE   HD2  H  N N 412 
PHE   HE1  H  N N 413 
PHE   HE2  H  N N 414 
PHE   HZ   H  N N 415 
PHE   HXT  H  N N 416 
PRO   N    N  N N 417 
PRO   CA   C  N S 418 
PRO   C    C  N N 419 
PRO   O    O  N N 420 
PRO   CB   C  N N 421 
PRO   CG   C  N N 422 
PRO   CD   C  N N 423 
PRO   OXT  O  N N 424 
PRO   H    H  N N 425 
PRO   HA   H  N N 426 
PRO   HB2  H  N N 427 
PRO   HB3  H  N N 428 
PRO   HG2  H  N N 429 
PRO   HG3  H  N N 430 
PRO   HD2  H  N N 431 
PRO   HD3  H  N N 432 
PRO   HXT  H  N N 433 
SER   N    N  N N 434 
SER   CA   C  N S 435 
SER   C    C  N N 436 
SER   O    O  N N 437 
SER   CB   C  N N 438 
SER   OG   O  N N 439 
SER   OXT  O  N N 440 
SER   H    H  N N 441 
SER   H2   H  N N 442 
SER   HA   H  N N 443 
SER   HB2  H  N N 444 
SER   HB3  H  N N 445 
SER   HG   H  N N 446 
SER   HXT  H  N N 447 
THR   N    N  N N 448 
THR   CA   C  N S 449 
THR   C    C  N N 450 
THR   O    O  N N 451 
THR   CB   C  N R 452 
THR   OG1  O  N N 453 
THR   CG2  C  N N 454 
THR   OXT  O  N N 455 
THR   H    H  N N 456 
THR   H2   H  N N 457 
THR   HA   H  N N 458 
THR   HB   H  N N 459 
THR   HG1  H  N N 460 
THR   HG21 H  N N 461 
THR   HG22 H  N N 462 
THR   HG23 H  N N 463 
THR   HXT  H  N N 464 
TRP   N    N  N N 465 
TRP   CA   C  N S 466 
TRP   C    C  N N 467 
TRP   O    O  N N 468 
TRP   CB   C  N N 469 
TRP   CG   C  Y N 470 
TRP   CD1  C  Y N 471 
TRP   CD2  C  Y N 472 
TRP   NE1  N  Y N 473 
TRP   CE2  C  Y N 474 
TRP   CE3  C  Y N 475 
TRP   CZ2  C  Y N 476 
TRP   CZ3  C  Y N 477 
TRP   CH2  C  Y N 478 
TRP   OXT  O  N N 479 
TRP   H    H  N N 480 
TRP   H2   H  N N 481 
TRP   HA   H  N N 482 
TRP   HB2  H  N N 483 
TRP   HB3  H  N N 484 
TRP   HD1  H  N N 485 
TRP   HE1  H  N N 486 
TRP   HE3  H  N N 487 
TRP   HZ2  H  N N 488 
TRP   HZ3  H  N N 489 
TRP   HH2  H  N N 490 
TRP   HXT  H  N N 491 
TYR   N    N  N N 492 
TYR   CA   C  N S 493 
TYR   C    C  N N 494 
TYR   O    O  N N 495 
TYR   CB   C  N N 496 
TYR   CG   C  Y N 497 
TYR   CD1  C  Y N 498 
TYR   CD2  C  Y N 499 
TYR   CE1  C  Y N 500 
TYR   CE2  C  Y N 501 
TYR   CZ   C  Y N 502 
TYR   OH   O  N N 503 
TYR   OXT  O  N N 504 
TYR   H    H  N N 505 
TYR   H2   H  N N 506 
TYR   HA   H  N N 507 
TYR   HB2  H  N N 508 
TYR   HB3  H  N N 509 
TYR   HD1  H  N N 510 
TYR   HD2  H  N N 511 
TYR   HE1  H  N N 512 
TYR   HE2  H  N N 513 
TYR   HH   H  N N 514 
TYR   HXT  H  N N 515 
VAL   N    N  N N 516 
VAL   CA   C  N S 517 
VAL   C    C  N N 518 
VAL   O    O  N N 519 
VAL   CB   C  N N 520 
VAL   CG1  C  N N 521 
VAL   CG2  C  N N 522 
VAL   OXT  O  N N 523 
VAL   H    H  N N 524 
VAL   H2   H  N N 525 
VAL   HA   H  N N 526 
VAL   HB   H  N N 527 
VAL   HG11 H  N N 528 
VAL   HG12 H  N N 529 
VAL   HG13 H  N N 530 
VAL   HG21 H  N N 531 
VAL   HG22 H  N N 532 
VAL   HG23 H  N N 533 
VAL   HXT  H  N N 534 
ZN    ZN   ZN N N 535 
# 
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 
A1AZ9 C07 C04  sing N N 1   
A1AZ9 C04 C05  doub Y N 2   
A1AZ9 C04 C03  sing Y N 3   
A1AZ9 C05 C06  sing Y N 4   
A1AZ9 C03 C02  doub Y N 5   
A1AZ9 C06 C11  sing N N 6   
A1AZ9 C06 N01  doub Y N 7   
A1AZ9 C02 N01  sing Y N 8   
A1AZ9 C02 N02  sing N N 9   
A1AZ9 F12 C12  sing N N 10  
A1AZ9 C11 C12  doub Y N 11  
A1AZ9 C11 C16  sing Y N 12  
A1AZ9 C12 C13  sing Y N 13  
A1AZ9 C16 C15  doub Y N 14  
A1AZ9 C13 F13  sing N N 15  
A1AZ9 C13 C14  doub Y N 16  
A1AZ9 C15 C14  sing Y N 17  
A1AZ9 C15 C17  sing N N 18  
A1AZ9 C17 N18  sing N N 19  
A1AZ9 C20 C19  sing N N 20  
A1AZ9 C20 F21  sing N N 21  
A1AZ9 N18 C19  sing N N 22  
A1AZ9 C14 H1   sing N N 23  
A1AZ9 C16 H2   sing N N 24  
A1AZ9 C17 H3   sing N N 25  
A1AZ9 C17 H4   sing N N 26  
A1AZ9 C19 H5   sing N N 27  
A1AZ9 C19 H6   sing N N 28  
A1AZ9 C20 H7   sing N N 29  
A1AZ9 C20 H8   sing N N 30  
A1AZ9 C03 H9   sing N N 31  
A1AZ9 C05 H10  sing N N 32  
A1AZ9 C07 H11  sing N N 33  
A1AZ9 C07 H12  sing N N 34  
A1AZ9 C07 H13  sing N N 35  
A1AZ9 N02 H14  sing N N 36  
A1AZ9 N02 H15  sing N N 37  
A1AZ9 N18 H16  sing N N 38  
ALA   N   CA   sing N N 39  
ALA   N   H    sing N N 40  
ALA   N   H2   sing N N 41  
ALA   CA  C    sing N N 42  
ALA   CA  CB   sing N N 43  
ALA   CA  HA   sing N N 44  
ALA   C   O    doub N N 45  
ALA   C   OXT  sing N N 46  
ALA   CB  HB1  sing N N 47  
ALA   CB  HB2  sing N N 48  
ALA   CB  HB3  sing N N 49  
ALA   OXT HXT  sing N N 50  
ARG   N   CA   sing N N 51  
ARG   N   H    sing N N 52  
ARG   N   H2   sing N N 53  
ARG   CA  C    sing N N 54  
ARG   CA  CB   sing N N 55  
ARG   CA  HA   sing N N 56  
ARG   C   O    doub N N 57  
ARG   C   OXT  sing N N 58  
ARG   CB  CG   sing N N 59  
ARG   CB  HB2  sing N N 60  
ARG   CB  HB3  sing N N 61  
ARG   CG  CD   sing N N 62  
ARG   CG  HG2  sing N N 63  
ARG   CG  HG3  sing N N 64  
ARG   CD  NE   sing N N 65  
ARG   CD  HD2  sing N N 66  
ARG   CD  HD3  sing N N 67  
ARG   NE  CZ   sing N N 68  
ARG   NE  HE   sing N N 69  
ARG   CZ  NH1  sing N N 70  
ARG   CZ  NH2  doub N N 71  
ARG   NH1 HH11 sing N N 72  
ARG   NH1 HH12 sing N N 73  
ARG   NH2 HH21 sing N N 74  
ARG   NH2 HH22 sing N N 75  
ARG   OXT HXT  sing N N 76  
ASN   N   CA   sing N N 77  
ASN   N   H    sing N N 78  
ASN   N   H2   sing N N 79  
ASN   CA  C    sing N N 80  
ASN   CA  CB   sing N N 81  
ASN   CA  HA   sing N N 82  
ASN   C   O    doub N N 83  
ASN   C   OXT  sing N N 84  
ASN   CB  CG   sing N N 85  
ASN   CB  HB2  sing N N 86  
ASN   CB  HB3  sing N N 87  
ASN   CG  OD1  doub N N 88  
ASN   CG  ND2  sing N N 89  
ASN   ND2 HD21 sing N N 90  
ASN   ND2 HD22 sing N N 91  
ASN   OXT HXT  sing N N 92  
ASP   N   CA   sing N N 93  
ASP   N   H    sing N N 94  
ASP   N   H2   sing N N 95  
ASP   CA  C    sing N N 96  
ASP   CA  CB   sing N N 97  
ASP   CA  HA   sing N N 98  
ASP   C   O    doub N N 99  
ASP   C   OXT  sing N N 100 
ASP   CB  CG   sing N N 101 
ASP   CB  HB2  sing N N 102 
ASP   CB  HB3  sing N N 103 
ASP   CG  OD1  doub N N 104 
ASP   CG  OD2  sing N N 105 
ASP   OD2 HD2  sing N N 106 
ASP   OXT HXT  sing N N 107 
CYS   N   CA   sing N N 108 
CYS   N   H    sing N N 109 
CYS   N   H2   sing N N 110 
CYS   CA  C    sing N N 111 
CYS   CA  CB   sing N N 112 
CYS   CA  HA   sing N N 113 
CYS   C   O    doub N N 114 
CYS   C   OXT  sing N N 115 
CYS   CB  SG   sing N N 116 
CYS   CB  HB2  sing N N 117 
CYS   CB  HB3  sing N N 118 
CYS   SG  HG   sing N N 119 
CYS   OXT HXT  sing N N 120 
GLN   N   CA   sing N N 121 
GLN   N   H    sing N N 122 
GLN   N   H2   sing N N 123 
GLN   CA  C    sing N N 124 
GLN   CA  CB   sing N N 125 
GLN   CA  HA   sing N N 126 
GLN   C   O    doub N N 127 
GLN   C   OXT  sing N N 128 
GLN   CB  CG   sing N N 129 
GLN   CB  HB2  sing N N 130 
GLN   CB  HB3  sing N N 131 
GLN   CG  CD   sing N N 132 
GLN   CG  HG2  sing N N 133 
GLN   CG  HG3  sing N N 134 
GLN   CD  OE1  doub N N 135 
GLN   CD  NE2  sing N N 136 
GLN   NE2 HE21 sing N N 137 
GLN   NE2 HE22 sing N N 138 
GLN   OXT HXT  sing N N 139 
GLU   N   CA   sing N N 140 
GLU   N   H    sing N N 141 
GLU   N   H2   sing N N 142 
GLU   CA  C    sing N N 143 
GLU   CA  CB   sing N N 144 
GLU   CA  HA   sing N N 145 
GLU   C   O    doub N N 146 
GLU   C   OXT  sing N N 147 
GLU   CB  CG   sing N N 148 
GLU   CB  HB2  sing N N 149 
GLU   CB  HB3  sing N N 150 
GLU   CG  CD   sing N N 151 
GLU   CG  HG2  sing N N 152 
GLU   CG  HG3  sing N N 153 
GLU   CD  OE1  doub N N 154 
GLU   CD  OE2  sing N N 155 
GLU   OE2 HE2  sing N N 156 
GLU   OXT HXT  sing N N 157 
GLY   N   CA   sing N N 158 
GLY   N   H    sing N N 159 
GLY   N   H2   sing N N 160 
GLY   CA  C    sing N N 161 
GLY   CA  HA2  sing N N 162 
GLY   CA  HA3  sing N N 163 
GLY   C   O    doub N N 164 
GLY   C   OXT  sing N N 165 
GLY   OXT HXT  sing N N 166 
H4B   N1  C2   doub Y N 167 
H4B   N1  C8A  sing Y N 168 
H4B   C2  N2   sing N N 169 
H4B   C2  N3   sing Y N 170 
H4B   N2  HN21 sing N N 171 
H4B   N2  HN22 sing N N 172 
H4B   N3  C4   sing Y N 173 
H4B   N3  HN3  sing N N 174 
H4B   C4  O4   doub N N 175 
H4B   C4  C4A  sing Y N 176 
H4B   C4A C8A  doub Y N 177 
H4B   C4A N5   sing N N 178 
H4B   C8A N8   sing N N 179 
H4B   N5  C6   sing N N 180 
H4B   N5  HN5  sing N N 181 
H4B   N8  C7   sing N N 182 
H4B   N8  HN8  sing N N 183 
H4B   C6  C7   sing N N 184 
H4B   C6  C9   sing N N 185 
H4B   C6  H6   sing N N 186 
H4B   C7  H71  sing N N 187 
H4B   C7  H72  sing N N 188 
H4B   C9  O9   sing N N 189 
H4B   C9  C10  sing N N 190 
H4B   C9  H9   sing N N 191 
H4B   O9  HO9  sing N N 192 
H4B   C10 C11  sing N N 193 
H4B   C10 O10  sing N N 194 
H4B   C10 H10  sing N N 195 
H4B   C11 H111 sing N N 196 
H4B   C11 H112 sing N N 197 
H4B   C11 H113 sing N N 198 
H4B   O10 HO0  sing N N 199 
HEM   CHA C1A  sing N N 200 
HEM   CHA C4D  doub N N 201 
HEM   CHA HHA  sing N N 202 
HEM   CHB C4A  sing N N 203 
HEM   CHB C1B  doub N N 204 
HEM   CHB HHB  sing N N 205 
HEM   CHC C4B  sing N N 206 
HEM   CHC C1C  doub N N 207 
HEM   CHC HHC  sing N N 208 
HEM   CHD C4C  doub N N 209 
HEM   CHD C1D  sing N N 210 
HEM   CHD HHD  sing N N 211 
HEM   C1A C2A  doub Y N 212 
HEM   C1A NA   sing Y N 213 
HEM   C2A C3A  sing Y N 214 
HEM   C2A CAA  sing N N 215 
HEM   C3A C4A  doub Y N 216 
HEM   C3A CMA  sing N N 217 
HEM   C4A NA   sing Y N 218 
HEM   CMA HMA  sing N N 219 
HEM   CMA HMAA sing N N 220 
HEM   CMA HMAB sing N N 221 
HEM   CAA CBA  sing N N 222 
HEM   CAA HAA  sing N N 223 
HEM   CAA HAAA sing N N 224 
HEM   CBA CGA  sing N N 225 
HEM   CBA HBA  sing N N 226 
HEM   CBA HBAA sing N N 227 
HEM   CGA O1A  doub N N 228 
HEM   CGA O2A  sing N N 229 
HEM   C1B C2B  sing N N 230 
HEM   C1B NB   sing N N 231 
HEM   C2B C3B  doub N N 232 
HEM   C2B CMB  sing N N 233 
HEM   C3B C4B  sing N N 234 
HEM   C3B CAB  sing N N 235 
HEM   C4B NB   doub N N 236 
HEM   CMB HMB  sing N N 237 
HEM   CMB HMBA sing N N 238 
HEM   CMB HMBB sing N N 239 
HEM   CAB CBB  doub N N 240 
HEM   CAB HAB  sing N N 241 
HEM   CBB HBB  sing N N 242 
HEM   CBB HBBA sing N N 243 
HEM   C1C C2C  sing Y N 244 
HEM   C1C NC   sing Y N 245 
HEM   C2C C3C  doub Y N 246 
HEM   C2C CMC  sing N N 247 
HEM   C3C C4C  sing Y N 248 
HEM   C3C CAC  sing N N 249 
HEM   C4C NC   sing Y N 250 
HEM   CMC HMC  sing N N 251 
HEM   CMC HMCA sing N N 252 
HEM   CMC HMCB sing N N 253 
HEM   CAC CBC  doub N N 254 
HEM   CAC HAC  sing N N 255 
HEM   CBC HBC  sing N N 256 
HEM   CBC HBCA sing N N 257 
HEM   C1D C2D  sing N N 258 
HEM   C1D ND   doub N N 259 
HEM   C2D C3D  doub N N 260 
HEM   C2D CMD  sing N N 261 
HEM   C3D C4D  sing N N 262 
HEM   C3D CAD  sing N N 263 
HEM   C4D ND   sing N N 264 
HEM   CMD HMD  sing N N 265 
HEM   CMD HMDA sing N N 266 
HEM   CMD HMDB sing N N 267 
HEM   CAD CBD  sing N N 268 
HEM   CAD HAD  sing N N 269 
HEM   CAD HADA sing N N 270 
HEM   CBD CGD  sing N N 271 
HEM   CBD HBD  sing N N 272 
HEM   CBD HBDA sing N N 273 
HEM   CGD O1D  doub N N 274 
HEM   CGD O2D  sing N N 275 
HEM   O2A H2A  sing N N 276 
HEM   O2D H2D  sing N N 277 
HEM   FE  NA   sing N N 278 
HEM   FE  NB   sing N N 279 
HEM   FE  NC   sing N N 280 
HEM   FE  ND   sing N N 281 
HIS   N   CA   sing N N 282 
HIS   N   H    sing N N 283 
HIS   N   H2   sing N N 284 
HIS   CA  C    sing N N 285 
HIS   CA  CB   sing N N 286 
HIS   CA  HA   sing N N 287 
HIS   C   O    doub N N 288 
HIS   C   OXT  sing N N 289 
HIS   CB  CG   sing N N 290 
HIS   CB  HB2  sing N N 291 
HIS   CB  HB3  sing N N 292 
HIS   CG  ND1  sing Y N 293 
HIS   CG  CD2  doub Y N 294 
HIS   ND1 CE1  doub Y N 295 
HIS   ND1 HD1  sing N N 296 
HIS   CD2 NE2  sing Y N 297 
HIS   CD2 HD2  sing N N 298 
HIS   CE1 NE2  sing Y N 299 
HIS   CE1 HE1  sing N N 300 
HIS   NE2 HE2  sing N N 301 
HIS   OXT HXT  sing N N 302 
HOH   O   H1   sing N N 303 
HOH   O   H2   sing N N 304 
ILE   N   CA   sing N N 305 
ILE   N   H    sing N N 306 
ILE   N   H2   sing N N 307 
ILE   CA  C    sing N N 308 
ILE   CA  CB   sing N N 309 
ILE   CA  HA   sing N N 310 
ILE   C   O    doub N N 311 
ILE   C   OXT  sing N N 312 
ILE   CB  CG1  sing N N 313 
ILE   CB  CG2  sing N N 314 
ILE   CB  HB   sing N N 315 
ILE   CG1 CD1  sing N N 316 
ILE   CG1 HG12 sing N N 317 
ILE   CG1 HG13 sing N N 318 
ILE   CG2 HG21 sing N N 319 
ILE   CG2 HG22 sing N N 320 
ILE   CG2 HG23 sing N N 321 
ILE   CD1 HD11 sing N N 322 
ILE   CD1 HD12 sing N N 323 
ILE   CD1 HD13 sing N N 324 
ILE   OXT HXT  sing N N 325 
LEU   N   CA   sing N N 326 
LEU   N   H    sing N N 327 
LEU   N   H2   sing N N 328 
LEU   CA  C    sing N N 329 
LEU   CA  CB   sing N N 330 
LEU   CA  HA   sing N N 331 
LEU   C   O    doub N N 332 
LEU   C   OXT  sing N N 333 
LEU   CB  CG   sing N N 334 
LEU   CB  HB2  sing N N 335 
LEU   CB  HB3  sing N N 336 
LEU   CG  CD1  sing N N 337 
LEU   CG  CD2  sing N N 338 
LEU   CG  HG   sing N N 339 
LEU   CD1 HD11 sing N N 340 
LEU   CD1 HD12 sing N N 341 
LEU   CD1 HD13 sing N N 342 
LEU   CD2 HD21 sing N N 343 
LEU   CD2 HD22 sing N N 344 
LEU   CD2 HD23 sing N N 345 
LEU   OXT HXT  sing N N 346 
LYS   N   CA   sing N N 347 
LYS   N   H    sing N N 348 
LYS   N   H2   sing N N 349 
LYS   CA  C    sing N N 350 
LYS   CA  CB   sing N N 351 
LYS   CA  HA   sing N N 352 
LYS   C   O    doub N N 353 
LYS   C   OXT  sing N N 354 
LYS   CB  CG   sing N N 355 
LYS   CB  HB2  sing N N 356 
LYS   CB  HB3  sing N N 357 
LYS   CG  CD   sing N N 358 
LYS   CG  HG2  sing N N 359 
LYS   CG  HG3  sing N N 360 
LYS   CD  CE   sing N N 361 
LYS   CD  HD2  sing N N 362 
LYS   CD  HD3  sing N N 363 
LYS   CE  NZ   sing N N 364 
LYS   CE  HE2  sing N N 365 
LYS   CE  HE3  sing N N 366 
LYS   NZ  HZ1  sing N N 367 
LYS   NZ  HZ2  sing N N 368 
LYS   NZ  HZ3  sing N N 369 
LYS   OXT HXT  sing N N 370 
MET   N   CA   sing N N 371 
MET   N   H    sing N N 372 
MET   N   H2   sing N N 373 
MET   CA  C    sing N N 374 
MET   CA  CB   sing N N 375 
MET   CA  HA   sing N N 376 
MET   C   O    doub N N 377 
MET   C   OXT  sing N N 378 
MET   CB  CG   sing N N 379 
MET   CB  HB2  sing N N 380 
MET   CB  HB3  sing N N 381 
MET   CG  SD   sing N N 382 
MET   CG  HG2  sing N N 383 
MET   CG  HG3  sing N N 384 
MET   SD  CE   sing N N 385 
MET   CE  HE1  sing N N 386 
MET   CE  HE2  sing N N 387 
MET   CE  HE3  sing N N 388 
MET   OXT HXT  sing N N 389 
PHE   N   CA   sing N N 390 
PHE   N   H    sing N N 391 
PHE   N   H2   sing N N 392 
PHE   CA  C    sing N N 393 
PHE   CA  CB   sing N N 394 
PHE   CA  HA   sing N N 395 
PHE   C   O    doub N N 396 
PHE   C   OXT  sing N N 397 
PHE   CB  CG   sing N N 398 
PHE   CB  HB2  sing N N 399 
PHE   CB  HB3  sing N N 400 
PHE   CG  CD1  doub Y N 401 
PHE   CG  CD2  sing Y N 402 
PHE   CD1 CE1  sing Y N 403 
PHE   CD1 HD1  sing N N 404 
PHE   CD2 CE2  doub Y N 405 
PHE   CD2 HD2  sing N N 406 
PHE   CE1 CZ   doub Y N 407 
PHE   CE1 HE1  sing N N 408 
PHE   CE2 CZ   sing Y N 409 
PHE   CE2 HE2  sing N N 410 
PHE   CZ  HZ   sing N N 411 
PHE   OXT HXT  sing N N 412 
PRO   N   CA   sing N N 413 
PRO   N   CD   sing N N 414 
PRO   N   H    sing N N 415 
PRO   CA  C    sing N N 416 
PRO   CA  CB   sing N N 417 
PRO   CA  HA   sing N N 418 
PRO   C   O    doub N N 419 
PRO   C   OXT  sing N N 420 
PRO   CB  CG   sing N N 421 
PRO   CB  HB2  sing N N 422 
PRO   CB  HB3  sing N N 423 
PRO   CG  CD   sing N N 424 
PRO   CG  HG2  sing N N 425 
PRO   CG  HG3  sing N N 426 
PRO   CD  HD2  sing N N 427 
PRO   CD  HD3  sing N N 428 
PRO   OXT HXT  sing N N 429 
SER   N   CA   sing N N 430 
SER   N   H    sing N N 431 
SER   N   H2   sing N N 432 
SER   CA  C    sing N N 433 
SER   CA  CB   sing N N 434 
SER   CA  HA   sing N N 435 
SER   C   O    doub N N 436 
SER   C   OXT  sing N N 437 
SER   CB  OG   sing N N 438 
SER   CB  HB2  sing N N 439 
SER   CB  HB3  sing N N 440 
SER   OG  HG   sing N N 441 
SER   OXT HXT  sing N N 442 
THR   N   CA   sing N N 443 
THR   N   H    sing N N 444 
THR   N   H2   sing N N 445 
THR   CA  C    sing N N 446 
THR   CA  CB   sing N N 447 
THR   CA  HA   sing N N 448 
THR   C   O    doub N N 449 
THR   C   OXT  sing N N 450 
THR   CB  OG1  sing N N 451 
THR   CB  CG2  sing N N 452 
THR   CB  HB   sing N N 453 
THR   OG1 HG1  sing N N 454 
THR   CG2 HG21 sing N N 455 
THR   CG2 HG22 sing N N 456 
THR   CG2 HG23 sing N N 457 
THR   OXT HXT  sing N N 458 
TRP   N   CA   sing N N 459 
TRP   N   H    sing N N 460 
TRP   N   H2   sing N N 461 
TRP   CA  C    sing N N 462 
TRP   CA  CB   sing N N 463 
TRP   CA  HA   sing N N 464 
TRP   C   O    doub N N 465 
TRP   C   OXT  sing N N 466 
TRP   CB  CG   sing N N 467 
TRP   CB  HB2  sing N N 468 
TRP   CB  HB3  sing N N 469 
TRP   CG  CD1  doub Y N 470 
TRP   CG  CD2  sing Y N 471 
TRP   CD1 NE1  sing Y N 472 
TRP   CD1 HD1  sing N N 473 
TRP   CD2 CE2  doub Y N 474 
TRP   CD2 CE3  sing Y N 475 
TRP   NE1 CE2  sing Y N 476 
TRP   NE1 HE1  sing N N 477 
TRP   CE2 CZ2  sing Y N 478 
TRP   CE3 CZ3  doub Y N 479 
TRP   CE3 HE3  sing N N 480 
TRP   CZ2 CH2  doub Y N 481 
TRP   CZ2 HZ2  sing N N 482 
TRP   CZ3 CH2  sing Y N 483 
TRP   CZ3 HZ3  sing N N 484 
TRP   CH2 HH2  sing N N 485 
TRP   OXT HXT  sing N N 486 
TYR   N   CA   sing N N 487 
TYR   N   H    sing N N 488 
TYR   N   H2   sing N N 489 
TYR   CA  C    sing N N 490 
TYR   CA  CB   sing N N 491 
TYR   CA  HA   sing N N 492 
TYR   C   O    doub N N 493 
TYR   C   OXT  sing N N 494 
TYR   CB  CG   sing N N 495 
TYR   CB  HB2  sing N N 496 
TYR   CB  HB3  sing N N 497 
TYR   CG  CD1  doub Y N 498 
TYR   CG  CD2  sing Y N 499 
TYR   CD1 CE1  sing Y N 500 
TYR   CD1 HD1  sing N N 501 
TYR   CD2 CE2  doub Y N 502 
TYR   CD2 HD2  sing N N 503 
TYR   CE1 CZ   doub Y N 504 
TYR   CE1 HE1  sing N N 505 
TYR   CE2 CZ   sing Y N 506 
TYR   CE2 HE2  sing N N 507 
TYR   CZ  OH   sing N N 508 
TYR   OH  HH   sing N N 509 
TYR   OXT HXT  sing N N 510 
VAL   N   CA   sing N N 511 
VAL   N   H    sing N N 512 
VAL   N   H2   sing N N 513 
VAL   CA  C    sing N N 514 
VAL   CA  CB   sing N N 515 
VAL   CA  HA   sing N N 516 
VAL   C   O    doub N N 517 
VAL   C   OXT  sing N N 518 
VAL   CB  CG1  sing N N 519 
VAL   CB  CG2  sing N N 520 
VAL   CB  HB   sing N N 521 
VAL   CG1 HG11 sing N N 522 
VAL   CG1 HG12 sing N N 523 
VAL   CG1 HG13 sing N N 524 
VAL   CG2 HG21 sing N N 525 
VAL   CG2 HG22 sing N N 526 
VAL   CG2 HG23 sing N N 527 
VAL   OXT HXT  sing N N 528 
# 
_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                    9CVP 
_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]   0.020500 
_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]   0.008821 
_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]   0.006096 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
_atom_sites.solution_primary            ? 
_atom_sites.solution_secondary          ? 
_atom_sites.solution_hydrogens          ? 
_atom_sites.special_details             ? 
# 
loop_
_atom_type.symbol 
C  
F  
FE 
N  
O  
S  
ZN 
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N  N   . ARG   A 1 3   ? -38.514 -24.836 42.313 1.00 128.22 ? 299 ARG   A N   1 
ATOM   2    C  CA  . ARG   A 1 3   ? -38.160 -25.090 40.916 1.00 129.11 ? 299 ARG   A CA  1 
ATOM   3    C  C   . ARG   A 1 3   ? -38.652 -23.988 39.974 1.00 124.39 ? 299 ARG   A C   1 
ATOM   4    O  O   . ARG   A 1 3   ? -38.088 -23.781 38.897 1.00 127.90 ? 299 ARG   A O   1 
ATOM   5    C  CB  . ARG   A 1 3   ? -38.729 -26.436 40.461 1.00 136.86 ? 299 ARG   A CB  1 
ATOM   6    C  CG  . ARG   A 1 3   ? -38.170 -26.967 39.134 1.00 140.14 ? 299 ARG   A CG  1 
ATOM   7    C  CD  . ARG   A 1 3   ? -36.701 -27.368 39.256 1.00 141.53 ? 299 ARG   A CD  1 
ATOM   8    N  NE  . ARG   A 1 3   ? -35.790 -26.262 38.968 1.00 139.02 ? 299 ARG   A NE  1 
ATOM   9    C  CZ  . ARG   A 1 3   ? -35.071 -26.159 37.855 1.00 137.39 ? 299 ARG   A CZ  1 
ATOM   10   N  NH1 . ARG   A 1 3   ? -35.148 -27.102 36.923 1.00 139.46 ? 299 ARG   A NH1 1 
ATOM   11   N  NH2 . ARG   A 1 3   ? -34.270 -25.116 37.676 1.00 132.46 ? 299 ARG   A NH2 1 
ATOM   12   N  N   . PHE   A 1 4   ? -39.704 -23.286 40.389 1.00 116.34 ? 300 PHE   A N   1 
ATOM   13   C  CA  . PHE   A 1 4   ? -40.416 -22.302 39.569 1.00 108.58 ? 300 PHE   A CA  1 
ATOM   14   C  C   . PHE   A 1 4   ? -40.407 -20.965 40.322 1.00 109.32 ? 300 PHE   A C   1 
ATOM   15   O  O   . PHE   A 1 4   ? -41.403 -20.570 40.933 1.00 123.30 ? 300 PHE   A O   1 
ATOM   16   C  CB  . PHE   A 1 4   ? -41.836 -22.843 39.285 1.00 106.97 ? 300 PHE   A CB  1 
ATOM   17   C  CG  . PHE   A 1 4   ? -41.887 -24.356 39.143 1.00 107.73 ? 300 PHE   A CG  1 
ATOM   18   C  CD1 . PHE   A 1 4   ? -42.321 -25.162 40.200 1.00 104.48 ? 300 PHE   A CD1 1 
ATOM   19   C  CD2 . PHE   A 1 4   ? -41.474 -24.973 37.962 1.00 107.13 ? 300 PHE   A CD2 1 
ATOM   20   C  CE1 . PHE   A 1 4   ? -42.359 -26.548 40.077 1.00 105.95 ? 300 PHE   A CE1 1 
ATOM   21   C  CE2 . PHE   A 1 4   ? -41.507 -26.360 37.831 1.00 109.91 ? 300 PHE   A CE2 1 
ATOM   22   C  CZ  . PHE   A 1 4   ? -41.950 -27.147 38.891 1.00 112.30 ? 300 PHE   A CZ  1 
ATOM   23   N  N   . LEU   A 1 5   ? -39.278 -20.254 40.233 1.00 97.10  ? 301 LEU   A N   1 
ATOM   24   C  CA  . LEU   A 1 5   ? -38.786 -19.328 41.254 1.00 84.14  ? 301 LEU   A CA  1 
ATOM   25   C  C   . LEU   A 1 5   ? -39.479 -17.966 41.229 1.00 83.65  ? 301 LEU   A C   1 
ATOM   26   O  O   . LEU   A 1 5   ? -40.054 -17.540 40.223 1.00 85.12  ? 301 LEU   A O   1 
ATOM   27   C  CB  . LEU   A 1 5   ? -37.284 -19.107 41.084 1.00 72.25  ? 301 LEU   A CB  1 
ATOM   28   C  CG  . LEU   A 1 5   ? -36.391 -20.345 41.000 1.00 72.32  ? 301 LEU   A CG  1 
ATOM   29   C  CD1 . LEU   A 1 5   ? -35.219 -20.041 40.100 1.00 77.01  ? 301 LEU   A CD1 1 
ATOM   30   C  CD2 . LEU   A 1 5   ? -35.902 -20.774 42.354 1.00 69.48  ? 301 LEU   A CD2 1 
ATOM   31   N  N   . LYS   A 1 6   ? -39.368 -17.262 42.359 1.00 76.85  ? 302 LYS   A N   1 
ATOM   32   C  CA  . LYS   A 1 6   ? -39.944 -15.939 42.560 1.00 76.22  ? 302 LYS   A CA  1 
ATOM   33   C  C   . LYS   A 1 6   ? -38.845 -14.880 42.576 1.00 72.15  ? 302 LYS   A C   1 
ATOM   34   O  O   . LYS   A 1 6   ? -37.782 -15.082 43.171 1.00 64.84  ? 302 LYS   A O   1 
ATOM   35   C  CB  . LYS   A 1 6   ? -40.732 -15.879 43.875 1.00 89.85  ? 302 LYS   A CB  1 
ATOM   36   C  CG  . LYS   A 1 6   ? -41.785 -16.975 44.049 1.00 97.36  ? 302 LYS   A CG  1 
ATOM   37   C  CD  . LYS   A 1 6   ? -42.890 -16.870 42.996 1.00 100.60 ? 302 LYS   A CD  1 
ATOM   38   C  CE  . LYS   A 1 6   ? -43.895 -18.022 43.105 1.00 103.58 ? 302 LYS   A CE  1 
ATOM   39   N  NZ  . LYS   A 1 6   ? -44.582 -18.089 44.438 1.00 103.37 ? 302 LYS   A NZ  1 
ATOM   40   N  N   . VAL   A 1 7   ? -39.093 -13.756 41.902 1.00 75.68  ? 303 VAL   A N   1 
ATOM   41   C  CA  . VAL   A 1 7   ? -38.227 -12.586 41.974 1.00 70.26  ? 303 VAL   A CA  1 
ATOM   42   C  C   . VAL   A 1 7   ? -39.080 -11.400 42.387 1.00 75.77  ? 303 VAL   A C   1 
ATOM   43   O  O   . VAL   A 1 7   ? -40.203 -11.229 41.898 1.00 82.93  ? 303 VAL   A O   1 
ATOM   44   C  CB  . VAL   A 1 7   ? -37.489 -12.306 40.646 1.00 69.35  ? 303 VAL   A CB  1 
ATOM   45   C  CG1 . VAL   A 1 7   ? -36.871 -13.575 40.125 1.00 73.82  ? 303 VAL   A CG1 1 
ATOM   46   C  CG2 . VAL   A 1 7   ? -38.411 -11.690 39.607 1.00 66.82  ? 303 VAL   A CG2 1 
ATOM   47   N  N   . LYS   A 1 8   ? -38.548 -10.593 43.298 1.00 68.73  ? 304 LYS   A N   1 
ATOM   48   C  CA  . LYS   A 1 8   ? -39.292 -9.527  43.943 1.00 67.43  ? 304 LYS   A CA  1 
ATOM   49   C  C   . LYS   A 1 8   ? -38.692 -8.182  43.555 1.00 60.76  ? 304 LYS   A C   1 
ATOM   50   O  O   . LYS   A 1 8   ? -37.521 -8.082  43.180 1.00 64.18  ? 304 LYS   A O   1 
ATOM   51   C  CB  . LYS   A 1 8   ? -39.282 -9.700  45.481 1.00 71.02  ? 304 LYS   A CB  1 
ATOM   52   C  CG  . LYS   A 1 8   ? -40.009 -8.611  46.268 1.00 74.89  ? 304 LYS   A CG  1 
ATOM   53   C  CD  . LYS   A 1 8   ? -40.233 -8.992  47.735 1.00 84.00  ? 304 LYS   A CD  1 
ATOM   54   C  CE  . LYS   A 1 8   ? -40.729 -7.798  48.553 1.00 87.05  ? 304 LYS   A CE  1 
ATOM   55   N  NZ  . LYS   A 1 8   ? -41.076 -8.163  49.950 1.00 95.39  ? 304 LYS   A NZ  1 
ATOM   56   N  N   . ASN   A 1 9   ? -39.517 -7.147  43.615 1.00 59.87  ? 305 ASN   A N   1 
ATOM   57   C  CA  . ASN   A 1 9   ? -39.052 -5.770  43.549 1.00 65.57  ? 305 ASN   A CA  1 
ATOM   58   C  C   . ASN   A 1 9   ? -39.237 -5.168  44.932 1.00 68.76  ? 305 ASN   A C   1 
ATOM   59   O  O   . ASN   A 1 9   ? -40.346 -5.184  45.470 1.00 72.87  ? 305 ASN   A O   1 
ATOM   60   C  CB  . ASN   A 1 9   ? -39.811 -4.971  42.476 1.00 74.83  ? 305 ASN   A CB  1 
ATOM   61   C  CG  . ASN   A 1 9   ? -39.299 -3.536  42.331 1.00 75.09  ? 305 ASN   A CG  1 
ATOM   62   O  OD1 . ASN   A 1 9   ? -39.161 -2.818  43.322 1.00 74.37  ? 305 ASN   A OD1 1 
ATOM   63   N  ND2 . ASN   A 1 9   ? -39.015 -3.115  41.097 1.00 63.24  ? 305 ASN   A ND2 1 
ATOM   64   N  N   . TRP   A 1 10  ? -38.155 -4.652  45.507 1.00 68.41  ? 306 TRP   A N   1 
ATOM   65   C  CA  . TRP   A 1 10  ? -38.184 -4.108  46.859 1.00 82.64  ? 306 TRP   A CA  1 
ATOM   66   C  C   . TRP   A 1 10  ? -38.481 -2.612  46.893 1.00 87.10  ? 306 TRP   A C   1 
ATOM   67   O  O   . TRP   A 1 10  ? -38.397 -2.001  47.963 1.00 89.38  ? 306 TRP   A O   1 
ATOM   68   C  CB  . TRP   A 1 10  ? -36.866 -4.413  47.577 1.00 79.69  ? 306 TRP   A CB  1 
ATOM   69   C  CG  . TRP   A 1 10  ? -36.618 -5.893  47.727 1.00 76.69  ? 306 TRP   A CG  1 
ATOM   70   C  CD1 . TRP   A 1 10  ? -35.987 -6.713  46.840 1.00 71.48  ? 306 TRP   A CD1 1 
ATOM   71   C  CD2 . TRP   A 1 10  ? -37.014 -6.724  48.826 1.00 74.32  ? 306 TRP   A CD2 1 
ATOM   72   N  NE1 . TRP   A 1 10  ? -35.955 -8.001  47.323 1.00 68.33  ? 306 TRP   A NE1 1 
ATOM   73   C  CE2 . TRP   A 1 10  ? -36.579 -8.033  48.541 1.00 74.33  ? 306 TRP   A CE2 1 
ATOM   74   C  CE3 . TRP   A 1 10  ? -37.679 -6.486  50.025 1.00 72.97  ? 306 TRP   A CE3 1 
ATOM   75   C  CZ2 . TRP   A 1 10  ? -36.795 -9.100  49.412 1.00 72.13  ? 306 TRP   A CZ2 1 
ATOM   76   C  CZ3 . TRP   A 1 10  ? -37.896 -7.550  50.890 1.00 75.68  ? 306 TRP   A CZ3 1 
ATOM   77   C  CH2 . TRP   A 1 10  ? -37.454 -8.836  50.582 1.00 73.48  ? 306 TRP   A CH2 1 
ATOM   78   N  N   . GLU   A 1 11  ? -38.808 -2.010  45.749 1.00 85.03  ? 307 GLU   A N   1 
ATOM   79   C  CA  . GLU   A 1 11  ? -39.426 -0.688  45.720 1.00 88.04  ? 307 GLU   A CA  1 
ATOM   80   C  C   . GLU   A 1 11  ? -40.947 -0.798  45.683 1.00 93.09  ? 307 GLU   A C   1 
ATOM   81   O  O   . GLU   A 1 11  ? -41.637 -0.050  46.383 1.00 104.42 ? 307 GLU   A O   1 
ATOM   82   C  CB  . GLU   A 1 11  ? -38.929 0.122   44.507 1.00 82.78  ? 307 GLU   A CB  1 
ATOM   83   C  CG  . GLU   A 1 11  ? -39.006 1.656   44.661 1.00 87.21  ? 307 GLU   A CG  1 
ATOM   84   C  CD  . GLU   A 1 11  ? -38.937 2.422   43.319 1.00 96.48  ? 307 GLU   A CD  1 
ATOM   85   O  OE1 . GLU   A 1 11  ? -39.693 3.408   43.154 1.00 96.71  ? 307 GLU   A OE1 1 
ATOM   86   O  OE2 . GLU   A 1 11  ? -38.135 2.044   42.428 1.00 96.13  ? 307 GLU   A OE2 1 
ATOM   87   N  N   . THR   A 1 12  ? -41.477 -1.755  44.916 1.00 89.40  ? 308 THR   A N   1 
ATOM   88   C  CA  . THR   A 1 12  ? -42.901 -1.840  44.615 1.00 92.52  ? 308 THR   A CA  1 
ATOM   89   C  C   . THR   A 1 12  ? -43.606 -3.032  45.254 1.00 97.03  ? 308 THR   A C   1 
ATOM   90   O  O   . THR   A 1 12  ? -44.833 -3.137  45.136 1.00 100.82 ? 308 THR   A O   1 
ATOM   91   C  CB  . THR   A 1 12  ? -43.108 -1.900  43.096 1.00 95.39  ? 308 THR   A CB  1 
ATOM   92   O  OG1 . THR   A 1 12  ? -42.804 -3.218  42.621 1.00 90.69  ? 308 THR   A OG1 1 
ATOM   93   C  CG2 . THR   A 1 12  ? -42.189 -0.914  42.401 1.00 93.65  ? 308 THR   A CG2 1 
ATOM   94   N  N   . ASP   A 1 13  ? -42.876 -3.938  45.909 1.00 98.94  ? 309 ASP   A N   1 
ATOM   95   C  CA  . ASP   A 1 13  ? -43.430 -5.169  46.484 1.00 107.13 ? 309 ASP   A CA  1 
ATOM   96   C  C   . ASP   A 1 13  ? -44.072 -6.064  45.427 1.00 110.31 ? 309 ASP   A C   1 
ATOM   97   O  O   . ASP   A 1 13  ? -44.909 -6.913  45.751 1.00 117.44 ? 309 ASP   A O   1 
ATOM   98   C  CB  . ASP   A 1 13  ? -44.441 -4.871  47.601 1.00 116.73 ? 309 ASP   A CB  1 
ATOM   99   C  CG  . ASP   A 1 13  ? -43.779 -4.628  48.943 1.00 119.48 ? 309 ASP   A CG  1 
ATOM   100  O  OD1 . ASP   A 1 13  ? -43.371 -5.617  49.588 1.00 119.28 ? 309 ASP   A OD1 1 
ATOM   101  O  OD2 . ASP   A 1 13  ? -43.656 -3.451  49.344 1.00 120.57 ? 309 ASP   A OD2 1 
ATOM   102  N  N   . VAL   A 1 14  ? -43.697 -5.894  44.166 1.00 100.53 ? 310 VAL   A N   1 
ATOM   103  C  CA  . VAL   A 1 14  ? -44.223 -6.725  43.092 1.00 96.84  ? 310 VAL   A CA  1 
ATOM   104  C  C   . VAL   A 1 14  ? -43.398 -7.998  43.001 1.00 99.16  ? 310 VAL   A C   1 
ATOM   105  O  O   . VAL   A 1 14  ? -42.180 -7.986  43.220 1.00 105.73 ? 310 VAL   A O   1 
ATOM   106  C  CB  . VAL   A 1 14  ? -44.223 -5.953  41.763 1.00 83.51  ? 310 VAL   A CB  1 
ATOM   107  C  CG1 . VAL   A 1 14  ? -44.272 -6.902  40.581 1.00 80.63  ? 310 VAL   A CG1 1 
ATOM   108  C  CG2 . VAL   A 1 14  ? -45.407 -5.010  41.721 1.00 85.26  ? 310 VAL   A CG2 1 
ATOM   109  N  N   . VAL   A 1 15  ? -44.065 -9.112  42.709 1.00 95.61  ? 311 VAL   A N   1 
ATOM   110  C  CA  . VAL   A 1 15  ? -43.400 -10.396 42.563 1.00 90.93  ? 311 VAL   A CA  1 
ATOM   111  C  C   . VAL   A 1 15  ? -43.832 -11.024 41.250 1.00 95.09  ? 311 VAL   A C   1 
ATOM   112  O  O   . VAL   A 1 15  ? -44.988 -10.894 40.831 1.00 103.18 ? 311 VAL   A O   1 
ATOM   113  C  CB  . VAL   A 1 15  ? -43.702 -11.338 43.743 1.00 93.11  ? 311 VAL   A CB  1 
ATOM   114  C  CG1 . VAL   A 1 15  ? -42.843 -12.590 43.649 1.00 90.37  ? 311 VAL   A CG1 1 
ATOM   115  C  CG2 . VAL   A 1 15  ? -43.455 -10.622 45.053 1.00 96.74  ? 311 VAL   A CG2 1 
ATOM   116  N  N   . LEU   A 1 16  ? -42.893 -11.697 40.598 1.00 85.77  ? 312 LEU   A N   1 
ATOM   117  C  CA  . LEU   A 1 16  ? -43.161 -12.400 39.357 1.00 86.43  ? 312 LEU   A CA  1 
ATOM   118  C  C   . LEU   A 1 16  ? -42.516 -13.773 39.427 1.00 86.01  ? 312 LEU   A C   1 
ATOM   119  O  O   . LEU   A 1 16  ? -41.439 -13.930 40.012 1.00 81.48  ? 312 LEU   A O   1 
ATOM   120  C  CB  . LEU   A 1 16  ? -42.634 -11.606 38.162 1.00 81.93  ? 312 LEU   A CB  1 
ATOM   121  C  CG  . LEU   A 1 16  ? -43.515 -10.392 37.856 1.00 91.52  ? 312 LEU   A CG  1 
ATOM   122  C  CD1 . LEU   A 1 16  ? -42.951 -9.572  36.709 1.00 88.96  ? 312 LEU   A CD1 1 
ATOM   123  C  CD2 . LEU   A 1 16  ? -44.953 -10.839 37.560 1.00 99.17  ? 312 LEU   A CD2 1 
ATOM   124  N  N   . THR   A 1 17  ? -43.191 -14.765 38.853 1.00 84.56  ? 313 THR   A N   1 
ATOM   125  C  CA  . THR   A 1 17  ? -42.695 -16.133 38.835 1.00 80.97  ? 313 THR   A CA  1 
ATOM   126  C  C   . THR   A 1 17  ? -41.954 -16.397 37.536 1.00 87.51  ? 313 THR   A C   1 
ATOM   127  O  O   . THR   A 1 17  ? -42.479 -16.136 36.449 1.00 92.03  ? 313 THR   A O   1 
ATOM   128  C  CB  . THR   A 1 17  ? -43.825 -17.148 38.985 1.00 86.19  ? 313 THR   A CB  1 
ATOM   129  O  OG1 . THR   A 1 17  ? -44.690 -16.755 40.056 1.00 87.13  ? 313 THR   A OG1 1 
ATOM   130  C  CG2 . THR   A 1 17  ? -43.247 -18.525 39.281 1.00 86.86  ? 313 THR   A CG2 1 
ATOM   131  N  N   . ASP   A 1 18  ? -40.747 -16.936 37.654 1.00 81.75  ? 314 ASP   A N   1 
ATOM   132  C  CA  . ASP   A 1 18  ? -39.910 -17.249 36.504 1.00 77.33  ? 314 ASP   A CA  1 
ATOM   133  C  C   . ASP   A 1 18  ? -39.963 -18.751 36.260 1.00 81.20  ? 314 ASP   A C   1 
ATOM   134  O  O   . ASP   A 1 18  ? -39.529 -19.534 37.109 1.00 83.39  ? 314 ASP   A O   1 
ATOM   135  C  CB  . ASP   A 1 18  ? -38.475 -16.781 36.752 1.00 71.53  ? 314 ASP   A CB  1 
ATOM   136  C  CG  . ASP   A 1 18  ? -37.634 -16.748 35.487 1.00 66.90  ? 314 ASP   A CG  1 
ATOM   137  O  OD1 . ASP   A 1 18  ? -37.368 -17.831 34.924 1.00 58.10  ? 314 ASP   A OD1 1 
ATOM   138  O  OD2 . ASP   A 1 18  ? -37.242 -15.636 35.063 1.00 65.72  ? 314 ASP   A OD2 1 
ATOM   139  N  N   . THR   A 1 19  ? -40.538 -19.150 35.123 1.00 81.40  ? 315 THR   A N   1 
ATOM   140  C  CA  . THR   A 1 19  ? -40.466 -20.529 34.664 1.00 79.50  ? 315 THR   A CA  1 
ATOM   141  C  C   . THR   A 1 19  ? -39.616 -20.689 33.415 1.00 75.86  ? 315 THR   A C   1 
ATOM   142  O  O   . THR   A 1 19  ? -39.201 -21.813 33.107 1.00 67.85  ? 315 THR   A O   1 
ATOM   143  C  CB  . THR   A 1 19  ? -41.871 -21.078 34.389 1.00 78.54  ? 315 THR   A CB  1 
ATOM   144  O  OG1 . THR   A 1 19  ? -42.805 -19.991 34.350 1.00 84.78  ? 315 THR   A OG1 1 
ATOM   145  C  CG2 . THR   A 1 19  ? -42.279 -22.069 35.482 1.00 72.43  ? 315 THR   A CG2 1 
ATOM   146  N  N   . LEU   A 1 20  ? -39.318 -19.583 32.726 1.00 68.09  ? 316 LEU   A N   1 
ATOM   147  C  CA  . LEU   A 1 20  ? -38.519 -19.617 31.511 1.00 72.63  ? 316 LEU   A CA  1 
ATOM   148  C  C   . LEU   A 1 20  ? -37.137 -20.213 31.747 1.00 73.54  ? 316 LEU   A C   1 
ATOM   149  O  O   . LEU   A 1 20  ? -36.524 -20.746 30.812 1.00 80.15  ? 316 LEU   A O   1 
ATOM   150  C  CB  . LEU   A 1 20  ? -38.406 -18.196 30.950 1.00 72.10  ? 316 LEU   A CB  1 
ATOM   151  C  CG  . LEU   A 1 20  ? -37.763 -18.010 29.584 1.00 66.56  ? 316 LEU   A CG  1 
ATOM   152  C  CD1 . LEU   A 1 20  ? -38.656 -18.629 28.539 1.00 70.32  ? 316 LEU   A CD1 1 
ATOM   153  C  CD2 . LEU   A 1 20  ? -37.513 -16.534 29.297 1.00 61.66  ? 316 LEU   A CD2 1 
ATOM   154  N  N   . HIS   A 1 21  ? -36.625 -20.125 32.974 1.00 70.88  ? 317 HIS   A N   1 
ATOM   155  C  CA  . HIS   A 1 21  ? -35.303 -20.649 33.296 1.00 60.57  ? 317 HIS   A CA  1 
ATOM   156  C  C   . HIS   A 1 21  ? -35.213 -22.160 33.143 1.00 61.98  ? 317 HIS   A C   1 
ATOM   157  O  O   . HIS   A 1 21  ? -34.101 -22.692 33.090 1.00 62.98  ? 317 HIS   A O   1 
ATOM   158  C  CB  . HIS   A 1 21  ? -34.912 -20.244 34.731 1.00 53.85  ? 317 HIS   A CB  1 
ATOM   159  C  CG  . HIS   A 1 21  ? -35.687 -20.957 35.792 1.00 56.49  ? 317 HIS   A CG  1 
ATOM   160  N  ND1 . HIS   A 1 21  ? -36.866 -20.468 36.312 1.00 64.70  ? 317 HIS   A ND1 1 
ATOM   161  C  CD2 . HIS   A 1 21  ? -35.456 -22.134 36.420 1.00 63.13  ? 317 HIS   A CD2 1 
ATOM   162  C  CE1 . HIS   A 1 21  ? -37.320 -21.307 37.229 1.00 72.63  ? 317 HIS   A CE1 1 
ATOM   163  N  NE2 . HIS   A 1 21  ? -36.487 -22.329 37.309 1.00 71.12  ? 317 HIS   A NE2 1 
ATOM   164  N  N   . LEU   A 1 22  ? -36.341 -22.868 33.053 1.00 67.53  ? 318 LEU   A N   1 
ATOM   165  C  CA  . LEU   A 1 22  ? -36.275 -24.304 32.793 1.00 82.52  ? 318 LEU   A CA  1 
ATOM   166  C  C   . LEU   A 1 22  ? -35.780 -24.599 31.377 1.00 84.66  ? 318 LEU   A C   1 
ATOM   167  O  O   . LEU   A 1 22  ? -35.136 -25.630 31.146 1.00 87.48  ? 318 LEU   A O   1 
ATOM   168  C  CB  . LEU   A 1 22  ? -37.642 -24.945 33.034 1.00 88.57  ? 318 LEU   A CB  1 
ATOM   169  C  CG  . LEU   A 1 22  ? -38.255 -24.632 34.400 1.00 92.70  ? 318 LEU   A CG  1 
ATOM   170  C  CD1 . LEU   A 1 22  ? -39.686 -25.141 34.496 1.00 99.72  ? 318 LEU   A CD1 1 
ATOM   171  C  CD2 . LEU   A 1 22  ? -37.400 -25.206 35.513 1.00 88.76  ? 318 LEU   A CD2 1 
ATOM   172  N  N   . LYS   A 1 23  ? -36.056 -23.709 30.423 1.00 75.86  ? 319 LYS   A N   1 
ATOM   173  C  CA  . LYS   A 1 23  ? -35.491 -23.846 29.087 1.00 77.17  ? 319 LYS   A CA  1 
ATOM   174  C  C   . LYS   A 1 23  ? -34.015 -23.474 29.041 1.00 75.60  ? 319 LYS   A C   1 
ATOM   175  O  O   . LYS   A 1 23  ? -33.417 -23.561 27.967 1.00 73.32  ? 319 LYS   A O   1 
ATOM   176  C  CB  . LYS   A 1 23  ? -36.278 -22.992 28.079 1.00 64.36  ? 319 LYS   A CB  1 
ATOM   177  C  CG  . LYS   A 1 23  ? -37.759 -23.396 27.915 1.00 69.06  ? 319 LYS   A CG  1 
ATOM   178  C  CD  . LYS   A 1 23  ? -37.924 -24.811 27.334 1.00 84.34  ? 319 LYS   A CD  1 
ATOM   179  C  CE  . LYS   A 1 23  ? -38.176 -24.809 25.831 1.00 90.88  ? 319 LYS   A CE  1 
ATOM   180  N  NZ  . LYS   A 1 23  ? -39.557 -24.353 25.513 1.00 98.35  ? 319 LYS   A NZ  1 
ATOM   181  N  N   . SER   A 1 24  ? -33.424 -23.062 30.165 1.00 73.81  ? 320 SER   A N   1 
ATOM   182  C  CA  . SER   A 1 24  ? -32.003 -22.731 30.196 1.00 75.14  ? 320 SER   A CA  1 
ATOM   183  C  C   . SER   A 1 24  ? -31.167 -23.936 29.789 1.00 83.23  ? 320 SER   A C   1 
ATOM   184  O  O   . SER   A 1 24  ? -31.400 -25.066 30.240 1.00 76.61  ? 320 SER   A O   1 
ATOM   185  C  CB  . SER   A 1 24  ? -31.585 -22.256 31.591 1.00 79.98  ? 320 SER   A CB  1 
ATOM   186  O  OG  . SER   A 1 24  ? -30.190 -22.023 31.662 1.00 87.37  ? 320 SER   A OG  1 
ATOM   187  N  N   . THR   A 1 25  ? -30.195 -23.688 28.919 1.00 94.10  ? 321 THR   A N   1 
ATOM   188  C  CA  . THR   A 1 25  ? -29.359 -24.746 28.382 1.00 105.61 ? 321 THR   A CA  1 
ATOM   189  C  C   . THR   A 1 25  ? -27.919 -24.611 28.859 1.00 97.14  ? 321 THR   A C   1 
ATOM   190  O  O   . THR   A 1 25  ? -27.395 -25.518 29.521 1.00 86.39  ? 321 THR   A O   1 
ATOM   191  C  CB  . THR   A 1 25  ? -29.461 -24.741 26.841 1.00 108.67 ? 321 THR   A CB  1 
ATOM   192  O  OG1 . THR   A 1 25  ? -28.362 -25.454 26.261 1.00 112.18 ? 321 THR   A OG1 1 
ATOM   193  C  CG2 . THR   A 1 25  ? -29.522 -23.311 26.283 1.00 103.97 ? 321 THR   A CG2 1 
ATOM   194  N  N   . LEU   A 1 26  ? -27.294 -23.465 28.593 1.00 94.66  ? 322 LEU   A N   1 
ATOM   195  C  CA  . LEU   A 1 26  ? -25.889 -23.244 28.893 1.00 89.61  ? 322 LEU   A CA  1 
ATOM   196  C  C   . LEU   A 1 26  ? -25.679 -23.094 30.400 1.00 87.86  ? 322 LEU   A C   1 
ATOM   197  O  O   . LEU   A 1 26  ? -26.609 -23.192 31.210 1.00 90.25  ? 322 LEU   A O   1 
ATOM   198  C  CB  . LEU   A 1 26  ? -25.379 -22.010 28.147 1.00 82.97  ? 322 LEU   A CB  1 
ATOM   199  C  CG  . LEU   A 1 26  ? -25.616 -21.949 26.629 1.00 75.36  ? 322 LEU   A CG  1 
ATOM   200  C  CD1 . LEU   A 1 26  ? -25.591 -20.503 26.123 1.00 71.28  ? 322 LEU   A CD1 1 
ATOM   201  C  CD2 . LEU   A 1 26  ? -24.584 -22.805 25.903 1.00 64.47  ? 322 LEU   A CD2 1 
ATOM   202  N  N   . GLU   A 1 27  ? -24.429 -22.844 30.775 1.00 82.86  ? 323 GLU   A N   1 
ATOM   203  C  CA  . GLU   A 1 27  ? -24.024 -22.767 32.167 1.00 77.01  ? 323 GLU   A CA  1 
ATOM   204  C  C   . GLU   A 1 27  ? -23.544 -21.357 32.500 1.00 78.55  ? 323 GLU   A C   1 
ATOM   205  O  O   . GLU   A 1 27  ? -23.188 -20.565 31.616 1.00 80.09  ? 323 GLU   A O   1 
ATOM   206  C  CB  . GLU   A 1 27  ? -22.933 -23.799 32.486 1.00 76.94  ? 323 GLU   A CB  1 
ATOM   207  C  CG  . GLU   A 1 27  ? -23.368 -25.240 32.259 1.00 89.28  ? 323 GLU   A CG  1 
ATOM   208  C  CD  . GLU   A 1 27  ? -22.441 -26.246 32.923 1.00 106.14 ? 323 GLU   A CD  1 
ATOM   209  O  OE1 . GLU   A 1 27  ? -21.629 -25.831 33.775 1.00 107.74 ? 323 GLU   A OE1 1 
ATOM   210  O  OE2 . GLU   A 1 27  ? -22.526 -27.451 32.595 1.00 112.64 ? 323 GLU   A OE2 1 
ATOM   211  N  N   . THR   A 1 28  ? -23.535 -21.066 33.804 1.00 71.10  ? 324 THR   A N   1 
ATOM   212  C  CA  . THR   A 1 28  ? -23.328 -19.721 34.324 1.00 67.38  ? 324 THR   A CA  1 
ATOM   213  C  C   . THR   A 1 28  ? -21.930 -19.484 34.877 1.00 68.35  ? 324 THR   A C   1 
ATOM   214  O  O   . THR   A 1 28  ? -21.415 -18.365 34.776 1.00 68.06  ? 324 THR   A O   1 
ATOM   215  C  CB  . THR   A 1 28  ? -24.340 -19.442 35.437 1.00 65.13  ? 324 THR   A CB  1 
ATOM   216  O  OG1 . THR   A 1 28  ? -24.185 -20.428 36.476 1.00 64.57  ? 324 THR   A OG1 1 
ATOM   217  C  CG2 . THR   A 1 28  ? -25.752 -19.507 34.892 1.00 63.14  ? 324 THR   A CG2 1 
ATOM   218  N  N   . GLY   A 1 29  ? -21.303 -20.500 35.448 1.00 73.87  ? 325 GLY   A N   1 
ATOM   219  C  CA  . GLY   A 1 29  ? -20.073 -20.341 36.181 1.00 75.81  ? 325 GLY   A CA  1 
ATOM   220  C  C   . GLY   A 1 29  ? -20.262 -20.396 37.676 1.00 80.14  ? 325 GLY   A C   1 
ATOM   221  O  O   . GLY   A 1 29  ? -19.317 -20.728 38.404 1.00 92.97  ? 325 GLY   A O   1 
ATOM   222  N  N   . CYS   A 1 30  ? -21.462 -20.087 38.148 1.00 72.90  ? 326 CYS   A N   1 
ATOM   223  C  CA  . CYS   A 1 30  ? -21.792 -20.271 39.546 1.00 67.21  ? 326 CYS   A CA  1 
ATOM   224  C  C   . CYS   A 1 30  ? -22.036 -21.750 39.824 1.00 68.34  ? 326 CYS   A C   1 
ATOM   225  O  O   . CYS   A 1 30  ? -22.466 -22.509 38.951 1.00 60.71  ? 326 CYS   A O   1 
ATOM   226  C  CB  . CYS   A 1 30  ? -23.027 -19.450 39.917 1.00 52.48  ? 326 CYS   A CB  1 
ATOM   227  S  SG  . CYS   A 1 30  ? -22.956 -17.697 39.467 1.00 57.10  ? 326 CYS   A SG  1 
ATOM   228  N  N   . THR   A 1 31  ? -21.715 -22.163 41.038 1.00 68.80  ? 327 THR   A N   1 
ATOM   229  C  CA  . THR   A 1 31  ? -22.053 -23.486 41.550 1.00 67.92  ? 327 THR   A CA  1 
ATOM   230  C  C   . THR   A 1 31  ? -22.961 -23.312 42.761 1.00 73.26  ? 327 THR   A C   1 
ATOM   231  O  O   . THR   A 1 31  ? -23.246 -22.193 43.195 1.00 75.57  ? 327 THR   A O   1 
ATOM   232  C  CB  . THR   A 1 31  ? -20.797 -24.288 41.900 1.00 63.42  ? 327 THR   A CB  1 
ATOM   233  O  OG1 . THR   A 1 31  ? -20.117 -23.670 42.994 1.00 63.92  ? 327 THR   A OG1 1 
ATOM   234  C  CG2 . THR   A 1 31  ? -19.848 -24.327 40.723 1.00 65.32  ? 327 THR   A CG2 1 
ATOM   235  N  N   . GLU   A 1 32  ? -23.426 -24.428 43.314 1.00 84.26  ? 328 GLU   A N   1 
ATOM   236  C  CA  . GLU   A 1 32  ? -24.176 -24.340 44.562 1.00 88.92  ? 328 GLU   A CA  1 
ATOM   237  C  C   . GLU   A 1 32  ? -23.352 -23.720 45.689 1.00 90.37  ? 328 GLU   A C   1 
ATOM   238  O  O   . GLU   A 1 32  ? -23.920 -23.343 46.724 1.00 83.88  ? 328 GLU   A O   1 
ATOM   239  C  CB  . GLU   A 1 32  ? -24.679 -25.736 44.965 1.00 98.62  ? 328 GLU   A CB  1 
ATOM   240  C  CG  . GLU   A 1 32  ? -25.876 -26.250 44.146 1.00 110.31 ? 328 GLU   A CG  1 
ATOM   241  C  CD  . GLU   A 1 32  ? -25.504 -27.327 43.125 1.00 120.20 ? 328 GLU   A CD  1 
ATOM   242  O  OE1 . GLU   A 1 32  ? -26.151 -28.400 43.119 1.00 126.22 ? 328 GLU   A OE1 1 
ATOM   243  O  OE2 . GLU   A 1 32  ? -24.564 -27.100 42.332 1.00 120.55 ? 328 GLU   A OE2 1 
ATOM   244  N  N   . HIS   A 1 33  ? -22.039 -23.570 45.496 1.00 86.44  ? 329 HIS   A N   1 
ATOM   245  C  CA  . HIS   A 1 33  ? -21.126 -23.141 46.542 1.00 79.62  ? 329 HIS   A CA  1 
ATOM   246  C  C   . HIS   A 1 33  ? -20.340 -21.880 46.205 1.00 76.19  ? 329 HIS   A C   1 
ATOM   247  O  O   . HIS   A 1 33  ? -19.541 -21.434 47.038 1.00 80.34  ? 329 HIS   A O   1 
ATOM   248  C  CB  . HIS   A 1 33  ? -20.146 -24.274 46.864 1.00 93.41  ? 329 HIS   A CB  1 
ATOM   249  C  CG  . HIS   A 1 33  ? -20.812 -25.592 47.123 1.00 107.70 ? 329 HIS   A CG  1 
ATOM   250  N  ND1 . HIS   A 1 33  ? -21.097 -26.491 46.117 1.00 113.54 ? 329 HIS   A ND1 1 
ATOM   251  C  CD2 . HIS   A 1 33  ? -21.264 -26.156 48.269 1.00 111.86 ? 329 HIS   A CD2 1 
ATOM   252  C  CE1 . HIS   A 1 33  ? -21.685 -27.556 46.633 1.00 117.38 ? 329 HIS   A CE1 1 
ATOM   253  N  NE2 . HIS   A 1 33  ? -21.799 -27.378 47.937 1.00 116.29 ? 329 HIS   A NE2 1 
ATOM   254  N  N   . ILE   A 1 34  ? -20.531 -21.296 45.017 1.00 72.88  ? 330 ILE   A N   1 
ATOM   255  C  CA  . ILE   A 1 34  ? -19.864 -20.056 44.640 1.00 64.70  ? 330 ILE   A CA  1 
ATOM   256  C  C   . ILE   A 1 34  ? -20.704 -19.358 43.586 1.00 62.60  ? 330 ILE   A C   1 
ATOM   257  O  O   . ILE   A 1 34  ? -21.381 -19.992 42.774 1.00 61.13  ? 330 ILE   A O   1 
ATOM   258  C  CB  . ILE   A 1 34  ? -18.423 -20.283 44.122 1.00 68.82  ? 330 ILE   A CB  1 
ATOM   259  C  CG1 . ILE   A 1 34  ? -17.670 -18.954 44.040 1.00 61.78  ? 330 ILE   A CG1 1 
ATOM   260  C  CG2 . ILE   A 1 34  ? -18.438 -20.923 42.737 1.00 75.17  ? 330 ILE   A CG2 1 
ATOM   261  C  CD1 . ILE   A 1 34  ? -16.165 -19.109 44.090 1.00 59.26  ? 330 ILE   A CD1 1 
ATOM   262  N  N   . CYS   A 1 35  ? -20.664 -18.041 43.608 1.00 64.86  ? 331 CYS   A N   1 
ATOM   263  C  CA  . CYS   A 1 35  ? -21.364 -17.222 42.634 1.00 54.64  ? 331 CYS   A CA  1 
ATOM   264  C  C   . CYS   A 1 35  ? -20.358 -16.311 41.968 1.00 60.41  ? 331 CYS   A C   1 
ATOM   265  O  O   . CYS   A 1 35  ? -19.507 -15.720 42.644 1.00 53.53  ? 331 CYS   A O   1 
ATOM   266  C  CB  . CYS   A 1 35  ? -22.465 -16.415 43.299 1.00 46.73  ? 331 CYS   A CB  1 
ATOM   267  S  SG  . CYS   A 1 35  ? -23.124 -15.082 42.383 1.00 53.85  ? 331 CYS   A SG  1 
ATOM   268  N  N   . MET   A 1 36  ? -20.461 -16.234 40.636 1.00 70.21  ? 332 MET   A N   1 
ATOM   269  C  CA  . MET   A 1 36  ? -19.510 -15.534 39.784 1.00 69.46  ? 332 MET   A CA  1 
ATOM   270  C  C   . MET   A 1 36  ? -20.168 -14.388 39.025 1.00 61.62  ? 332 MET   A C   1 
ATOM   271  O  O   . MET   A 1 36  ? -19.592 -13.876 38.054 1.00 52.44  ? 332 MET   A O   1 
ATOM   272  C  CB  . MET   A 1 36  ? -18.867 -16.508 38.802 1.00 76.57  ? 332 MET   A CB  1 
ATOM   273  C  CG  . MET   A 1 36  ? -18.400 -17.780 39.440 1.00 84.28  ? 332 MET   A CG  1 
ATOM   274  S  SD  . MET   A 1 36  ? -16.737 -18.211 38.916 1.00 91.46  ? 332 MET   A SD  1 
ATOM   275  C  CE  . MET   A 1 36  ? -16.514 -19.757 39.794 1.00 90.11  ? 332 MET   A CE  1 
ATOM   276  N  N   . GLY   A 1 37  ? -21.351 -13.955 39.469 1.00 50.68  ? 333 GLY   A N   1 
ATOM   277  C  CA  . GLY   A 1 37  ? -22.134 -12.972 38.752 1.00 58.84  ? 333 GLY   A CA  1 
ATOM   278  C  C   . GLY   A 1 37  ? -21.520 -11.594 38.659 1.00 51.47  ? 333 GLY   A C   1 
ATOM   279  O  O   . GLY   A 1 37  ? -22.172 -10.672 38.168 1.00 55.62  ? 333 GLY   A O   1 
ATOM   280  N  N   . SER   A 1 38  ? -20.290 -11.433 39.157 1.00 43.28  ? 334 SER   A N   1 
ATOM   281  C  CA  . SER   A 1 38  ? -19.496 -10.230 38.953 1.00 52.39  ? 334 SER   A CA  1 
ATOM   282  C  C   . SER   A 1 38  ? -18.181 -10.519 38.240 1.00 52.40  ? 334 SER   A C   1 
ATOM   283  O  O   . SER   A 1 38  ? -17.369 -9.599  38.074 1.00 56.23  ? 334 SER   A O   1 
ATOM   284  C  CB  . SER   A 1 38  ? -19.212 -9.520  40.284 1.00 54.71  ? 334 SER   A CB  1 
ATOM   285  O  OG  . SER   A 1 38  ? -18.201 -10.189 41.024 1.00 56.48  ? 334 SER   A OG  1 
ATOM   286  N  N   . ILE   A 1 39  ? -17.936 -11.771 37.850 1.00 50.04  ? 335 ILE   A N   1 
ATOM   287  C  CA  . ILE   A 1 39  ? -16.875 -12.078 36.895 1.00 57.38  ? 335 ILE   A CA  1 
ATOM   288  C  C   . ILE   A 1 39  ? -17.298 -11.604 35.513 1.00 56.37  ? 335 ILE   A C   1 
ATOM   289  O  O   . ILE   A 1 39  ? -18.427 -11.862 35.072 1.00 51.70  ? 335 ILE   A O   1 
ATOM   290  C  CB  . ILE   A 1 39  ? -16.571 -13.581 36.884 1.00 53.44  ? 335 ILE   A CB  1 
ATOM   291  C  CG1 . ILE   A 1 39  ? -16.212 -14.091 38.292 1.00 48.42  ? 335 ILE   A CG1 1 
ATOM   292  C  CG2 . ILE   A 1 39  ? -15.451 -13.878 35.919 1.00 56.70  ? 335 ILE   A CG2 1 
ATOM   293  C  CD1 . ILE   A 1 39  ? -15.190 -13.223 39.074 1.00 53.30  ? 335 ILE   A CD1 1 
ATOM   294  N  N   . MET   A 1 40  ? -16.388 -10.914 34.817 1.00 59.47  ? 336 MET   A N   1 
ATOM   295  C  CA  . MET   A 1 40  ? -16.765 -10.204 33.593 1.00 60.72  ? 336 MET   A CA  1 
ATOM   296  C  C   . MET   A 1 40  ? -16.974 -11.157 32.413 1.00 71.15  ? 336 MET   A C   1 
ATOM   297  O  O   . MET   A 1 40  ? -17.899 -10.970 31.608 1.00 68.43  ? 336 MET   A O   1 
ATOM   298  C  CB  . MET   A 1 40  ? -15.701 -9.154  33.261 1.00 59.23  ? 336 MET   A CB  1 
ATOM   299  C  CG  . MET   A 1 40  ? -15.966 -8.371  31.981 1.00 80.44  ? 336 MET   A CG  1 
ATOM   300  S  SD  . MET   A 1 40  ? -16.422 -6.648  32.285 1.00 94.52  ? 336 MET   A SD  1 
ATOM   301  C  CE  . MET   A 1 40  ? -14.837 -5.819  32.277 1.00 92.44  ? 336 MET   A CE  1 
ATOM   302  N  N   . LEU   A 1 41  ? -16.133 -12.184 32.292 1.00 81.04  ? 337 LEU   A N   1 
ATOM   303  C  CA  . LEU   A 1 41  ? -16.137 -13.072 31.126 1.00 83.91  ? 337 LEU   A CA  1 
ATOM   304  C  C   . LEU   A 1 41  ? -15.823 -14.495 31.565 1.00 94.02  ? 337 LEU   A C   1 
ATOM   305  O  O   . LEU   A 1 41  ? -14.700 -14.986 31.385 1.00 102.54 ? 337 LEU   A O   1 
ATOM   306  C  CB  . LEU   A 1 41  ? -15.125 -12.602 30.074 1.00 84.06  ? 337 LEU   A CB  1 
ATOM   307  C  CG  . LEU   A 1 41  ? -14.915 -11.116 29.751 1.00 85.59  ? 337 LEU   A CG  1 
ATOM   308  C  CD1 . LEU   A 1 41  ? -13.580 -10.920 29.038 1.00 85.75  ? 337 LEU   A CD1 1 
ATOM   309  C  CD2 . LEU   A 1 41  ? -16.055 -10.546 28.912 1.00 83.39  ? 337 LEU   A CD2 1 
ATOM   310  N  N   . PRO   A 1 42  ? -16.792 -15.199 32.143 1.00 94.85  ? 338 PRO   A N   1 
ATOM   311  C  CA  . PRO   A 1 42  ? -16.540 -16.546 32.672 1.00 96.61  ? 338 PRO   A CA  1 
ATOM   312  C  C   . PRO   A 1 42  ? -16.675 -17.619 31.586 1.00 101.03 ? 338 PRO   A C   1 
ATOM   313  O  O   . PRO   A 1 42  ? -16.964 -17.346 30.414 1.00 91.72  ? 338 PRO   A O   1 
ATOM   314  C  CB  . PRO   A 1 42  ? -17.617 -16.706 33.754 1.00 95.37  ? 338 PRO   A CB  1 
ATOM   315  C  CG  . PRO   A 1 42  ? -18.559 -15.484 33.603 1.00 93.62  ? 338 PRO   A CG  1 
ATOM   316  C  CD  . PRO   A 1 42  ? -18.195 -14.789 32.330 1.00 92.34  ? 338 PRO   A CD  1 
ATOM   317  N  N   . SER   A 1 43  ? -16.461 -18.867 32.002 1.00 103.44 ? 339 SER   A N   1 
ATOM   318  C  CA  . SER   A 1 43  ? -16.629 -20.033 31.132 1.00 107.30 ? 339 SER   A CA  1 
ATOM   319  C  C   . SER   A 1 43  ? -17.299 -21.172 31.884 1.00 110.38 ? 339 SER   A C   1 
ATOM   320  O  O   . SER   A 1 43  ? -16.817 -22.305 31.857 1.00 114.56 ? 339 SER   A O   1 
ATOM   321  C  CB  . SER   A 1 43  ? -15.284 -20.500 30.569 1.00 106.87 ? 339 SER   A CB  1 
ATOM   322  O  OG  . SER   A 1 43  ? -15.067 -19.973 29.269 1.00 103.75 ? 339 SER   A OG  1 
ATOM   323  N  N   . VAL   A 1 52  ? -13.516 -26.868 17.257 1.00 134.52 ? 348 VAL   A N   1 
ATOM   324  C  CA  . VAL   A 1 52  ? -14.451 -27.206 16.185 1.00 135.30 ? 348 VAL   A CA  1 
ATOM   325  C  C   . VAL   A 1 52  ? -15.719 -27.802 16.808 1.00 138.47 ? 348 VAL   A C   1 
ATOM   326  O  O   . VAL   A 1 52  ? -15.689 -28.235 17.960 1.00 146.97 ? 348 VAL   A O   1 
ATOM   327  C  CB  . VAL   A 1 52  ? -13.797 -28.169 15.149 1.00 130.39 ? 348 VAL   A CB  1 
ATOM   328  C  CG1 . VAL   A 1 52  ? -13.818 -29.620 15.641 1.00 131.18 ? 348 VAL   A CG1 1 
ATOM   329  C  CG2 . VAL   A 1 52  ? -14.454 -28.028 13.782 1.00 122.50 ? 348 VAL   A CG2 1 
ATOM   330  N  N   . ALA   A 1 53  ? -16.832 -27.801 16.066 1.00 127.73 ? 349 ALA   A N   1 
ATOM   331  C  CA  . ALA   A 1 53  ? -18.100 -28.361 16.531 1.00 114.98 ? 349 ALA   A CA  1 
ATOM   332  C  C   . ALA   A 1 53  ? -18.587 -29.395 15.524 1.00 115.66 ? 349 ALA   A C   1 
ATOM   333  O  O   . ALA   A 1 53  ? -18.839 -29.058 14.362 1.00 117.91 ? 349 ALA   A O   1 
ATOM   334  C  CB  . ALA   A 1 53  ? -19.151 -27.268 16.733 1.00 100.85 ? 349 ALA   A CB  1 
ATOM   335  N  N   . THR   A 1 54  ? -18.739 -30.644 15.976 1.00 109.50 ? 350 THR   A N   1 
ATOM   336  C  CA  . THR   A 1 54  ? -18.987 -31.783 15.099 1.00 105.75 ? 350 THR   A CA  1 
ATOM   337  C  C   . THR   A 1 54  ? -20.475 -31.968 14.806 1.00 107.65 ? 350 THR   A C   1 
ATOM   338  O  O   . THR   A 1 54  ? -21.344 -31.289 15.358 1.00 106.50 ? 350 THR   A O   1 
ATOM   339  C  CB  . THR   A 1 54  ? -18.435 -33.069 15.706 1.00 103.66 ? 350 THR   A CB  1 
ATOM   340  O  OG1 . THR   A 1 54  ? -19.351 -33.551 16.695 1.00 107.43 ? 350 THR   A OG1 1 
ATOM   341  C  CG2 . THR   A 1 54  ? -17.072 -32.814 16.339 1.00 98.00  ? 350 THR   A CG2 1 
ATOM   342  N  N   . LYS   A 1 55  ? -20.764 -32.932 13.929 1.00 113.50 ? 351 LYS   A N   1 
ATOM   343  C  CA  . LYS   A 1 55  ? -22.122 -33.091 13.428 1.00 117.76 ? 351 LYS   A CA  1 
ATOM   344  C  C   . LYS   A 1 55  ? -23.000 -33.911 14.355 1.00 116.53 ? 351 LYS   A C   1 
ATOM   345  O  O   . LYS   A 1 55  ? -24.229 -33.826 14.253 1.00 109.11 ? 351 LYS   A O   1 
ATOM   346  C  CB  . LYS   A 1 55  ? -22.116 -33.717 12.026 1.00 120.46 ? 351 LYS   A CB  1 
ATOM   347  C  CG  . LYS   A 1 55  ? -21.123 -34.845 11.803 1.00 125.93 ? 351 LYS   A CG  1 
ATOM   348  C  CD  . LYS   A 1 55  ? -21.286 -35.424 10.388 1.00 129.42 ? 351 LYS   A CD  1 
ATOM   349  C  CE  . LYS   A 1 55  ? -20.048 -36.195 9.930  1.00 135.11 ? 351 LYS   A CE  1 
ATOM   350  N  NZ  . LYS   A 1 55  ? -20.325 -37.620 9.557  1.00 141.04 ? 351 LYS   A NZ  1 
ATOM   351  N  N   . ASP   A 1 56  ? -22.402 -34.697 15.251 1.00 123.74 ? 352 ASP   A N   1 
ATOM   352  C  CA  . ASP   A 1 56  ? -23.196 -35.399 16.251 1.00 127.85 ? 352 ASP   A CA  1 
ATOM   353  C  C   . ASP   A 1 56  ? -23.931 -34.404 17.132 1.00 115.47 ? 352 ASP   A C   1 
ATOM   354  O  O   . ASP   A 1 56  ? -25.146 -34.510 17.339 1.00 116.28 ? 352 ASP   A O   1 
ATOM   355  C  CB  . ASP   A 1 56  ? -22.293 -36.305 17.089 1.00 139.49 ? 352 ASP   A CB  1 
ATOM   356  C  CG  . ASP   A 1 56  ? -21.374 -37.165 16.232 1.00 149.62 ? 352 ASP   A CG  1 
ATOM   357  O  OD1 . ASP   A 1 56  ? -21.852 -38.161 15.646 1.00 154.68 ? 352 ASP   A OD1 1 
ATOM   358  O  OD2 . ASP   A 1 56  ? -20.174 -36.829 16.130 1.00 151.57 ? 352 ASP   A OD2 1 
ATOM   359  N  N   . GLN   A 1 57  ? -23.205 -33.405 17.633 1.00 105.70 ? 353 GLN   A N   1 
ATOM   360  C  CA  . GLN   A 1 57  ? -23.773 -32.402 18.521 1.00 101.59 ? 353 GLN   A CA  1 
ATOM   361  C  C   . GLN   A 1 57  ? -24.707 -31.444 17.798 1.00 95.97  ? 353 GLN   A C   1 
ATOM   362  O  O   . GLN   A 1 57  ? -25.501 -30.762 18.455 1.00 87.63  ? 353 GLN   A O   1 
ATOM   363  C  CB  . GLN   A 1 57  ? -22.643 -31.611 19.177 1.00 101.91 ? 353 GLN   A CB  1 
ATOM   364  C  CG  . GLN   A 1 57  ? -21.309 -32.344 19.168 1.00 114.04 ? 353 GLN   A CG  1 
ATOM   365  C  CD  . GLN   A 1 57  ? -20.138 -31.422 18.893 1.00 118.37 ? 353 GLN   A CD  1 
ATOM   366  O  OE1 . GLN   A 1 57  ? -20.322 -30.260 18.529 1.00 113.93 ? 353 GLN   A OE1 1 
ATOM   367  N  NE2 . GLN   A 1 57  ? -18.924 -31.936 19.063 1.00 125.40 ? 353 GLN   A NE2 1 
ATOM   368  N  N   . LEU   A 1 58  ? -24.638 -31.390 16.465 1.00 95.91  ? 354 LEU   A N   1 
ATOM   369  C  CA  . LEU   A 1 58  ? -25.269 -30.304 15.729 1.00 92.07  ? 354 LEU   A CA  1 
ATOM   370  C  C   . LEU   A 1 58  ? -26.766 -30.517 15.523 1.00 98.45  ? 354 LEU   A C   1 
ATOM   371  O  O   . LEU   A 1 58  ? -27.513 -29.535 15.443 1.00 91.59  ? 354 LEU   A O   1 
ATOM   372  C  CB  . LEU   A 1 58  ? -24.574 -30.128 14.376 1.00 92.25  ? 354 LEU   A CB  1 
ATOM   373  C  CG  . LEU   A 1 58  ? -24.437 -28.709 13.813 1.00 84.87  ? 354 LEU   A CG  1 
ATOM   374  C  CD1 . LEU   A 1 58  ? -23.407 -27.902 14.600 1.00 81.62  ? 354 LEU   A CD1 1 
ATOM   375  C  CD2 . LEU   A 1 58  ? -24.084 -28.733 12.323 1.00 85.98  ? 354 LEU   A CD2 1 
ATOM   376  N  N   . PHE   A 1 59  ? -27.237 -31.773 15.418 1.00 104.32 ? 355 PHE   A N   1 
ATOM   377  C  CA  . PHE   A 1 59  ? -28.669 -31.955 15.184 1.00 110.64 ? 355 PHE   A CA  1 
ATOM   378  C  C   . PHE   A 1 59  ? -29.526 -31.703 16.423 1.00 111.32 ? 355 PHE   A C   1 
ATOM   379  O  O   . PHE   A 1 59  ? -30.629 -31.160 16.287 1.00 116.29 ? 355 PHE   A O   1 
ATOM   380  C  CB  . PHE   A 1 59  ? -28.996 -33.344 14.645 1.00 120.97 ? 355 PHE   A CB  1 
ATOM   381  C  CG  . PHE   A 1 59  ? -30.458 -33.520 14.326 1.00 130.63 ? 355 PHE   A CG  1 
ATOM   382  C  CD1 . PHE   A 1 59  ? -31.027 -32.864 13.242 1.00 131.98 ? 355 PHE   A CD1 1 
ATOM   383  C  CD2 . PHE   A 1 59  ? -31.268 -34.317 15.118 1.00 137.62 ? 355 PHE   A CD2 1 
ATOM   384  C  CE1 . PHE   A 1 59  ? -32.373 -33.008 12.948 1.00 133.92 ? 355 PHE   A CE1 1 
ATOM   385  C  CE2 . PHE   A 1 59  ? -32.615 -34.471 14.830 1.00 140.95 ? 355 PHE   A CE2 1 
ATOM   386  C  CZ  . PHE   A 1 59  ? -33.168 -33.813 13.744 1.00 139.60 ? 355 PHE   A CZ  1 
ATOM   387  N  N   . PRO   A 1 60  ? -29.110 -32.108 17.629 1.00 108.78 ? 356 PRO   A N   1 
ATOM   388  C  CA  . PRO   A 1 60  ? -29.861 -31.669 18.821 1.00 97.70  ? 356 PRO   A CA  1 
ATOM   389  C  C   . PRO   A 1 60  ? -30.112 -30.173 18.846 1.00 86.66  ? 356 PRO   A C   1 
ATOM   390  O  O   . PRO   A 1 60  ? -31.262 -29.736 18.993 1.00 84.71  ? 356 PRO   A O   1 
ATOM   391  C  CB  . PRO   A 1 60  ? -28.961 -32.122 19.975 1.00 98.80  ? 356 PRO   A CB  1 
ATOM   392  C  CG  . PRO   A 1 60  ? -28.308 -33.342 19.465 1.00 108.94 ? 356 PRO   A CG  1 
ATOM   393  C  CD  . PRO   A 1 60  ? -28.093 -33.120 17.977 1.00 113.57 ? 356 PRO   A CD  1 
ATOM   394  N  N   . LEU   A 1 61  ? -29.052 -29.377 18.668 1.00 80.97  ? 357 LEU   A N   1 
ATOM   395  C  CA  . LEU   A 1 61  ? -29.165 -27.923 18.723 1.00 75.93  ? 357 LEU   A CA  1 
ATOM   396  C  C   . LEU   A 1 61  ? -30.068 -27.396 17.617 1.00 78.48  ? 357 LEU   A C   1 
ATOM   397  O  O   . LEU   A 1 61  ? -30.945 -26.556 17.870 1.00 71.57  ? 357 LEU   A O   1 
ATOM   398  C  CB  . LEU   A 1 61  ? -27.772 -27.301 18.629 1.00 74.09  ? 357 LEU   A CB  1 
ATOM   399  C  CG  . LEU   A 1 61  ? -26.747 -27.833 19.639 1.00 78.59  ? 357 LEU   A CG  1 
ATOM   400  C  CD1 . LEU   A 1 61  ? -25.334 -27.357 19.336 1.00 73.85  ? 357 LEU   A CD1 1 
ATOM   401  C  CD2 . LEU   A 1 61  ? -27.149 -27.449 21.067 1.00 80.42  ? 357 LEU   A CD2 1 
ATOM   402  N  N   . ALA   A 1 62  ? -29.862 -27.881 16.384 1.00 73.54  ? 358 ALA   A N   1 
ATOM   403  C  CA  . ALA   A 1 62  ? -30.735 -27.511 15.278 1.00 67.45  ? 358 ALA   A CA  1 
ATOM   404  C  C   . ALA   A 1 62  ? -32.186 -27.854 15.584 1.00 80.00  ? 358 ALA   A C   1 
ATOM   405  O  O   . ALA   A 1 62  ? -33.094 -27.056 15.312 1.00 81.26  ? 358 ALA   A O   1 
ATOM   406  C  CB  . ALA   A 1 62  ? -30.290 -28.227 13.999 1.00 78.19  ? 358 ALA   A CB  1 
ATOM   407  N  N   . LYS   A 1 63  ? -32.412 -29.047 16.145 1.00 84.25  ? 359 LYS   A N   1 
ATOM   408  C  CA  . LYS   A 1 63  ? -33.758 -29.513 16.472 1.00 85.85  ? 359 LYS   A CA  1 
ATOM   409  C  C   . LYS   A 1 63  ? -34.430 -28.596 17.477 1.00 90.61  ? 359 LYS   A C   1 
ATOM   410  O  O   . LYS   A 1 63  ? -35.554 -28.132 17.260 1.00 96.33  ? 359 LYS   A O   1 
ATOM   411  C  CB  . LYS   A 1 63  ? -33.696 -30.933 17.029 1.00 75.11  ? 359 LYS   A CB  1 
ATOM   412  C  CG  . LYS   A 1 63  ? -35.051 -31.533 17.319 1.00 87.23  ? 359 LYS   A CG  1 
ATOM   413  C  CD  . LYS   A 1 63  ? -34.901 -32.940 17.886 1.00 95.36  ? 359 LYS   A CD  1 
ATOM   414  C  CE  . LYS   A 1 63  ? -36.161 -33.764 17.688 1.00 103.97 ? 359 LYS   A CE  1 
ATOM   415  N  NZ  . LYS   A 1 63  ? -37.370 -33.055 18.188 1.00 104.96 ? 359 LYS   A NZ  1 
ATOM   416  N  N   . GLU   A 1 64  ? -33.757 -28.339 18.597 1.00 83.64  ? 360 GLU   A N   1 
ATOM   417  C  CA  . GLU   A 1 64  ? -34.333 -27.483 19.621 1.00 84.37  ? 360 GLU   A CA  1 
ATOM   418  C  C   . GLU   A 1 64  ? -34.655 -26.101 19.059 1.00 82.45  ? 360 GLU   A C   1 
ATOM   419  O  O   . GLU   A 1 64  ? -35.725 -25.550 19.341 1.00 79.04  ? 360 GLU   A O   1 
ATOM   420  C  CB  . GLU   A 1 64  ? -33.372 -27.412 20.812 1.00 87.56  ? 360 GLU   A CB  1 
ATOM   421  C  CG  . GLU   A 1 64  ? -33.659 -26.352 21.860 1.00 90.68  ? 360 GLU   A CG  1 
ATOM   422  C  CD  . GLU   A 1 64  ? -32.411 -26.016 22.663 1.00 97.83  ? 360 GLU   A CD  1 
ATOM   423  O  OE1 . GLU   A 1 64  ? -31.438 -26.804 22.579 1.00 97.50  ? 360 GLU   A OE1 1 
ATOM   424  O  OE2 . GLU   A 1 64  ? -32.397 -24.972 23.364 1.00 96.28  ? 360 GLU   A OE2 1 
ATOM   425  N  N   . PHE   A 1 65  ? -33.765 -25.541 18.228 1.00 76.97  ? 361 PHE   A N   1 
ATOM   426  C  CA  . PHE   A 1 65  ? -34.049 -24.234 17.632 1.00 67.64  ? 361 PHE   A CA  1 
ATOM   427  C  C   . PHE   A 1 65  ? -35.256 -24.307 16.709 1.00 68.80  ? 361 PHE   A C   1 
ATOM   428  O  O   . PHE   A 1 65  ? -36.158 -23.464 16.784 1.00 70.78  ? 361 PHE   A O   1 
ATOM   429  C  CB  . PHE   A 1 65  ? -32.840 -23.699 16.864 1.00 59.56  ? 361 PHE   A CB  1 
ATOM   430  C  CG  . PHE   A 1 65  ? -33.156 -22.492 15.995 1.00 52.65  ? 361 PHE   A CG  1 
ATOM   431  C  CD1 . PHE   A 1 65  ? -33.260 -21.219 16.554 1.00 61.89  ? 361 PHE   A CD1 1 
ATOM   432  C  CD2 . PHE   A 1 65  ? -33.368 -22.628 14.623 1.00 66.07  ? 361 PHE   A CD2 1 
ATOM   433  C  CE1 . PHE   A 1 65  ? -33.562 -20.116 15.768 1.00 64.70  ? 361 PHE   A CE1 1 
ATOM   434  C  CE2 . PHE   A 1 65  ? -33.665 -21.517 13.832 1.00 58.37  ? 361 PHE   A CE2 1 
ATOM   435  C  CZ  . PHE   A 1 65  ? -33.760 -20.260 14.409 1.00 56.81  ? 361 PHE   A CZ  1 
ATOM   436  N  N   . LEU   A 1 66  ? -35.285 -25.304 15.820 1.00 66.59  ? 362 LEU   A N   1 
ATOM   437  C  CA  . LEU   A 1 66  ? -36.389 -25.408 14.873 1.00 70.25  ? 362 LEU   A CA  1 
ATOM   438  C  C   . LEU   A 1 66  ? -37.717 -25.635 15.581 1.00 82.25  ? 362 LEU   A C   1 
ATOM   439  O  O   . LEU   A 1 66  ? -38.769 -25.236 15.072 1.00 82.75  ? 362 LEU   A O   1 
ATOM   440  C  CB  . LEU   A 1 66  ? -36.128 -26.532 13.870 1.00 78.76  ? 362 LEU   A CB  1 
ATOM   441  C  CG  . LEU   A 1 66  ? -35.136 -26.282 12.731 1.00 76.11  ? 362 LEU   A CG  1 
ATOM   442  C  CD1 . LEU   A 1 66  ? -35.330 -27.328 11.667 1.00 80.18  ? 362 LEU   A CD1 1 
ATOM   443  C  CD2 . LEU   A 1 66  ? -35.272 -24.874 12.150 1.00 66.12  ? 362 LEU   A CD2 1 
ATOM   444  N  N   . ASP   A 1 67  ? -37.692 -26.268 16.753 1.00 93.40  ? 363 ASP   A N   1 
ATOM   445  C  CA  . ASP   A 1 67  ? -38.937 -26.532 17.469 1.00 94.01  ? 363 ASP   A CA  1 
ATOM   446  C  C   . ASP   A 1 67  ? -39.494 -25.258 18.103 1.00 81.09  ? 363 ASP   A C   1 
ATOM   447  O  O   . ASP   A 1 67  ? -40.711 -25.035 18.091 1.00 76.94  ? 363 ASP   A O   1 
ATOM   448  C  CB  . ASP   A 1 67  ? -38.709 -27.628 18.511 1.00 97.18  ? 363 ASP   A CB  1 
ATOM   449  C  CG  . ASP   A 1 67  ? -38.814 -29.027 17.919 1.00 111.02 ? 363 ASP   A CG  1 
ATOM   450  O  OD1 . ASP   A 1 67  ? -39.935 -29.581 17.898 1.00 120.52 ? 363 ASP   A OD1 1 
ATOM   451  O  OD2 . ASP   A 1 67  ? -37.786 -29.568 17.456 1.00 114.22 ? 363 ASP   A OD2 1 
ATOM   452  N  N   . GLN   A 1 68  ? -38.628 -24.400 18.646 1.00 76.77  ? 364 GLN   A N   1 
ATOM   453  C  CA  . GLN   A 1 68  ? -39.130 -23.159 19.222 1.00 80.47  ? 364 GLN   A CA  1 
ATOM   454  C  C   . GLN   A 1 68  ? -39.515 -22.160 18.138 1.00 83.00  ? 364 GLN   A C   1 
ATOM   455  O  O   . GLN   A 1 68  ? -40.436 -21.361 18.342 1.00 84.10  ? 364 GLN   A O   1 
ATOM   456  C  CB  . GLN   A 1 68  ? -38.103 -22.554 20.205 1.00 70.46  ? 364 GLN   A CB  1 
ATOM   457  C  CG  . GLN   A 1 68  ? -36.741 -22.225 19.591 1.00 74.97  ? 364 GLN   A CG  1 
ATOM   458  C  CD  . GLN   A 1 68  ? -35.684 -21.816 20.611 1.00 74.06  ? 364 GLN   A CD  1 
ATOM   459  O  OE1 . GLN   A 1 68  ? -35.320 -20.633 20.712 1.00 77.09  ? 364 GLN   A OE1 1 
ATOM   460  N  NE2 . GLN   A 1 68  ? -35.153 -22.796 21.338 1.00 67.30  ? 364 GLN   A NE2 1 
ATOM   461  N  N   . TYR   A 1 69  ? -38.860 -22.207 16.975 1.00 86.43  ? 365 TYR   A N   1 
ATOM   462  C  CA  . TYR   A 1 69  ? -39.250 -21.316 15.883 1.00 78.36  ? 365 TYR   A CA  1 
ATOM   463  C  C   . TYR   A 1 69  ? -40.610 -21.699 15.310 1.00 79.49  ? 365 TYR   A C   1 
ATOM   464  O  O   . TYR   A 1 69  ? -41.418 -20.826 14.967 1.00 77.80  ? 365 TYR   A O   1 
ATOM   465  C  CB  . TYR   A 1 69  ? -38.191 -21.315 14.780 1.00 75.49  ? 365 TYR   A CB  1 
ATOM   466  C  CG  . TYR   A 1 69  ? -38.693 -20.701 13.487 1.00 75.51  ? 365 TYR   A CG  1 
ATOM   467  C  CD1 . TYR   A 1 69  ? -39.121 -19.379 13.440 1.00 74.46  ? 365 TYR   A CD1 1 
ATOM   468  C  CD2 . TYR   A 1 69  ? -38.757 -21.450 12.320 1.00 77.94  ? 365 TYR   A CD2 1 
ATOM   469  C  CE1 . TYR   A 1 69  ? -39.592 -18.820 12.275 1.00 78.39  ? 365 TYR   A CE1 1 
ATOM   470  C  CE2 . TYR   A 1 69  ? -39.225 -20.895 11.145 1.00 86.65  ? 365 TYR   A CE2 1 
ATOM   471  C  CZ  . TYR   A 1 69  ? -39.641 -19.582 11.131 1.00 86.21  ? 365 TYR   A CZ  1 
ATOM   472  O  OH  . TYR   A 1 69  ? -40.108 -19.029 9.963  1.00 89.95  ? 365 TYR   A OH  1 
ATOM   473  N  N   . TYR   A 1 70  ? -40.883 -22.995 15.182 1.00 86.98  ? 366 TYR   A N   1 
ATOM   474  C  CA  . TYR   A 1 70  ? -42.183 -23.381 14.653 1.00 96.99  ? 366 TYR   A CA  1 
ATOM   475  C  C   . TYR   A 1 70  ? -43.269 -23.209 15.702 1.00 103.43 ? 366 TYR   A C   1 
ATOM   476  O  O   . TYR   A 1 70  ? -44.398 -22.830 15.372 1.00 111.38 ? 366 TYR   A O   1 
ATOM   477  C  CB  . TYR   A 1 70  ? -42.134 -24.810 14.105 1.00 102.08 ? 366 TYR   A CB  1 
ATOM   478  C  CG  . TYR   A 1 70  ? -41.593 -24.836 12.691 1.00 97.62  ? 366 TYR   A CG  1 
ATOM   479  C  CD1 . TYR   A 1 70  ? -40.242 -25.055 12.446 1.00 93.13  ? 366 TYR   A CD1 1 
ATOM   480  C  CD2 . TYR   A 1 70  ? -42.425 -24.593 11.604 1.00 99.56  ? 366 TYR   A CD2 1 
ATOM   481  C  CE1 . TYR   A 1 70  ? -39.735 -25.055 11.153 1.00 90.13  ? 366 TYR   A CE1 1 
ATOM   482  C  CE2 . TYR   A 1 70  ? -41.924 -24.591 10.305 1.00 97.67  ? 366 TYR   A CE2 1 
ATOM   483  C  CZ  . TYR   A 1 70  ? -40.579 -24.823 10.090 1.00 92.51  ? 366 TYR   A CZ  1 
ATOM   484  O  OH  . TYR   A 1 70  ? -40.066 -24.816 8.816  1.00 91.02  ? 366 TYR   A OH  1 
ATOM   485  N  N   . SER   A 1 71  ? -42.941 -23.459 16.969 1.00 101.71 ? 367 SER   A N   1 
ATOM   486  C  CA  . SER   A 1 71  ? -43.840 -23.060 18.042 1.00 102.50 ? 367 SER   A CA  1 
ATOM   487  C  C   . SER   A 1 71  ? -44.169 -21.577 17.930 1.00 98.12  ? 367 SER   A C   1 
ATOM   488  O  O   . SER   A 1 71  ? -45.328 -21.174 18.076 1.00 103.50 ? 367 SER   A O   1 
ATOM   489  C  CB  . SER   A 1 71  ? -43.204 -23.380 19.397 1.00 101.13 ? 367 SER   A CB  1 
ATOM   490  O  OG  . SER   A 1 71  ? -44.147 -23.326 20.458 1.00 105.92 ? 367 SER   A OG  1 
ATOM   491  N  N   . SER   A 1 72  ? -43.164 -20.761 17.606 1.00 90.40  ? 368 SER   A N   1 
ATOM   492  C  CA  . SER   A 1 72  ? -43.341 -19.312 17.596 1.00 88.19  ? 368 SER   A CA  1 
ATOM   493  C  C   . SER   A 1 72  ? -44.395 -18.867 16.584 1.00 96.43  ? 368 SER   A C   1 
ATOM   494  O  O   . SER   A 1 72  ? -45.239 -18.018 16.898 1.00 103.88 ? 368 SER   A O   1 
ATOM   495  C  CB  . SER   A 1 72  ? -42.002 -18.630 17.315 1.00 82.44  ? 368 SER   A CB  1 
ATOM   496  O  OG  . SER   A 1 72  ? -42.121 -17.638 16.308 1.00 84.50  ? 368 SER   A OG  1 
ATOM   497  N  N   . ILE   A 1 73  ? -44.374 -19.424 15.369 1.00 92.63  ? 369 ILE   A N   1 
ATOM   498  C  CA  . ILE   A 1 73  ? -45.287 -18.961 14.327 1.00 97.36  ? 369 ILE   A CA  1 
ATOM   499  C  C   . ILE   A 1 73  ? -46.641 -19.653 14.453 1.00 104.70 ? 369 ILE   A C   1 
ATOM   500  O  O   . ILE   A 1 73  ? -47.461 -19.609 13.529 1.00 110.56 ? 369 ILE   A O   1 
ATOM   501  C  CB  . ILE   A 1 73  ? -44.680 -19.165 12.924 1.00 103.22 ? 369 ILE   A CB  1 
ATOM   502  C  CG1 . ILE   A 1 73  ? -44.300 -20.629 12.690 1.00 103.05 ? 369 ILE   A CG1 1 
ATOM   503  C  CG2 . ILE   A 1 73  ? -43.459 -18.265 12.738 1.00 100.82 ? 369 ILE   A CG2 1 
ATOM   504  C  CD1 . ILE   A 1 73  ? -43.463 -20.841 11.445 1.00 102.41 ? 369 ILE   A CD1 1 
ATOM   505  N  N   . LYS   A 1 74  ? -46.886 -20.276 15.607 1.00 110.64 ? 370 LYS   A N   1 
ATOM   506  C  CA  . LYS   A 1 74  ? -48.135 -20.936 15.986 1.00 121.82 ? 370 LYS   A CA  1 
ATOM   507  C  C   . LYS   A 1 74  ? -48.412 -22.191 15.166 1.00 128.47 ? 370 LYS   A C   1 
ATOM   508  O  O   . LYS   A 1 74  ? -49.508 -22.761 15.272 1.00 139.91 ? 370 LYS   A O   1 
ATOM   509  C  CB  . LYS   A 1 74  ? -49.339 -19.985 15.903 1.00 127.36 ? 370 LYS   A CB  1 
ATOM   510  C  CG  . LYS   A 1 74  ? -49.098 -18.613 16.540 1.00 126.14 ? 370 LYS   A CG  1 
ATOM   511  C  CD  . LYS   A 1 74  ? -50.039 -18.325 17.701 1.00 128.45 ? 370 LYS   A CD  1 
ATOM   512  C  CE  . LYS   A 1 74  ? -49.365 -17.443 18.767 1.00 127.60 ? 370 LYS   A CE  1 
ATOM   513  N  NZ  . LYS   A 1 74  ? -49.509 -15.968 18.558 1.00 127.09 ? 370 LYS   A NZ  1 
ATOM   514  N  N   . ARG   A 1 75  ? -47.450 -22.642 14.356 1.00 116.04 ? 371 ARG   A N   1 
ATOM   515  C  CA  . ARG   A 1 75  ? -47.554 -23.922 13.665 1.00 108.15 ? 371 ARG   A CA  1 
ATOM   516  C  C   . ARG   A 1 75  ? -46.530 -24.921 14.197 1.00 113.57 ? 371 ARG   A C   1 
ATOM   517  O  O   . ARG   A 1 75  ? -45.662 -25.395 13.451 1.00 105.70 ? 371 ARG   A O   1 
ATOM   518  C  CB  . ARG   A 1 75  ? -47.387 -23.724 12.165 1.00 101.80 ? 371 ARG   A CB  1 
ATOM   519  C  CG  . ARG   A 1 75  ? -48.345 -22.694 11.613 1.00 107.68 ? 371 ARG   A CG  1 
ATOM   520  C  CD  . ARG   A 1 75  ? -47.586 -21.487 11.103 1.00 106.51 ? 371 ARG   A CD  1 
ATOM   521  N  NE  . ARG   A 1 75  ? -47.764 -21.311 9.668  1.00 105.57 ? 371 ARG   A NE  1 
ATOM   522  C  CZ  . ARG   A 1 75  ? -47.131 -22.027 8.745  1.00 107.79 ? 371 ARG   A CZ  1 
ATOM   523  N  NH1 . ARG   A 1 75  ? -47.352 -21.796 7.451  1.00 108.39 ? 371 ARG   A NH1 1 
ATOM   524  N  NH2 . ARG   A 1 75  ? -46.280 -22.977 9.115  1.00 103.84 ? 371 ARG   A NH2 1 
ATOM   525  N  N   . PHE   A 1 76  ? -46.636 -25.227 15.497 1.00 119.17 ? 372 PHE   A N   1 
ATOM   526  C  CA  . PHE   A 1 76  ? -45.806 -26.224 16.169 1.00 120.80 ? 372 PHE   A CA  1 
ATOM   527  C  C   . PHE   A 1 76  ? -46.166 -27.614 15.653 1.00 129.12 ? 372 PHE   A C   1 
ATOM   528  O  O   . PHE   A 1 76  ? -47.322 -28.040 15.754 1.00 136.14 ? 372 PHE   A O   1 
ATOM   529  C  CB  . PHE   A 1 76  ? -46.036 -26.115 17.685 1.00 125.40 ? 372 PHE   A CB  1 
ATOM   530  C  CG  . PHE   A 1 76  ? -45.055 -26.893 18.561 1.00 121.57 ? 372 PHE   A CG  1 
ATOM   531  C  CD1 . PHE   A 1 76  ? -44.241 -27.896 18.053 1.00 118.12 ? 372 PHE   A CD1 1 
ATOM   532  C  CD2 . PHE   A 1 76  ? -44.983 -26.614 19.923 1.00 126.91 ? 372 PHE   A CD2 1 
ATOM   533  C  CE1 . PHE   A 1 76  ? -43.372 -28.592 18.874 1.00 116.97 ? 372 PHE   A CE1 1 
ATOM   534  C  CE2 . PHE   A 1 76  ? -44.114 -27.306 20.756 1.00 125.30 ? 372 PHE   A CE2 1 
ATOM   535  C  CZ  . PHE   A 1 76  ? -43.308 -28.296 20.229 1.00 123.21 ? 372 PHE   A CZ  1 
ATOM   536  N  N   . GLY   A 1 77  ? -45.183 -28.319 15.091 1.00 129.88 ? 373 GLY   A N   1 
ATOM   537  C  CA  . GLY   A 1 77  ? -45.351 -29.714 14.727 1.00 136.81 ? 373 GLY   A CA  1 
ATOM   538  C  C   . GLY   A 1 77  ? -46.165 -29.979 13.479 1.00 141.69 ? 373 GLY   A C   1 
ATOM   539  O  O   . GLY   A 1 77  ? -46.425 -31.149 13.161 1.00 144.38 ? 373 GLY   A O   1 
ATOM   540  N  N   . SER   A 1 78  ? -46.566 -28.940 12.754 1.00 136.37 ? 374 SER   A N   1 
ATOM   541  C  CA  . SER   A 1 78  ? -47.311 -29.118 11.519 1.00 134.68 ? 374 SER   A CA  1 
ATOM   542  C  C   . SER   A 1 78  ? -46.459 -29.836 10.479 1.00 130.10 ? 374 SER   A C   1 
ATOM   543  O  O   . SER   A 1 78  ? -45.316 -30.219 10.761 1.00 128.28 ? 374 SER   A O   1 
ATOM   544  C  CB  . SER   A 1 78  ? -47.781 -27.761 10.997 1.00 133.03 ? 374 SER   A CB  1 
ATOM   545  O  OG  . SER   A 1 78  ? -46.729 -26.815 11.056 1.00 126.65 ? 374 SER   A OG  1 
ATOM   546  N  N   . LYS   A 1 79  ? -47.020 -30.032 9.280  1.00 122.38 ? 375 LYS   A N   1 
ATOM   547  C  CA  . LYS   A 1 79  ? -46.269 -30.654 8.191  1.00 117.56 ? 375 LYS   A CA  1 
ATOM   548  C  C   . LYS   A 1 79  ? -45.015 -29.852 7.856  1.00 109.36 ? 375 LYS   A C   1 
ATOM   549  O  O   . LYS   A 1 79  ? -43.973 -30.428 7.516  1.00 99.75  ? 375 LYS   A O   1 
ATOM   550  C  CB  . LYS   A 1 79  ? -47.159 -30.796 6.953  1.00 119.81 ? 375 LYS   A CB  1 
ATOM   551  C  CG  . LYS   A 1 79  ? -46.497 -31.519 5.777  1.00 114.00 ? 375 LYS   A CG  1 
ATOM   552  C  CD  . LYS   A 1 79  ? -46.993 -32.958 5.653  1.00 129.89 ? 375 LYS   A CD  1 
ATOM   553  C  CE  . LYS   A 1 79  ? -46.268 -33.729 4.555  1.00 123.01 ? 375 LYS   A CE  1 
ATOM   554  N  NZ  . LYS   A 1 79  ? -44.824 -33.925 4.866  1.00 121.28 ? 375 LYS   A NZ  1 
ATOM   555  N  N   . ALA   A 1 80  ? -45.095 -28.522 7.943  1.00 110.60 ? 376 ALA   A N   1 
ATOM   556  C  CA  . ALA   A 1 80  ? -43.919 -27.695 7.694  1.00 111.63 ? 376 ALA   A CA  1 
ATOM   557  C  C   . ALA   A 1 80  ? -42.795 -28.040 8.665  1.00 110.61 ? 376 ALA   A C   1 
ATOM   558  O  O   . ALA   A 1 80  ? -41.673 -28.350 8.246  1.00 109.75 ? 376 ALA   A O   1 
ATOM   559  C  CB  . ALA   A 1 80  ? -44.289 -26.216 7.788  1.00 114.79 ? 376 ALA   A CB  1 
ATOM   560  N  N   . HIS   A 1 81  ? -43.089 -28.016 9.971  1.00 109.37 ? 377 HIS   A N   1 
ATOM   561  C  CA  . HIS   A 1 81  ? -42.074 -28.341 10.972 1.00 104.80 ? 377 HIS   A CA  1 
ATOM   562  C  C   . HIS   A 1 81  ? -41.493 -29.731 10.744 1.00 97.67  ? 377 HIS   A C   1 
ATOM   563  O  O   . HIS   A 1 81  ? -40.271 -29.914 10.767 1.00 91.51  ? 377 HIS   A O   1 
ATOM   564  C  CB  . HIS   A 1 81  ? -42.664 -28.242 12.379 1.00 109.50 ? 377 HIS   A CB  1 
ATOM   565  C  CG  . HIS   A 1 81  ? -41.684 -28.553 13.472 1.00 113.20 ? 377 HIS   A CG  1 
ATOM   566  N  ND1 . HIS   A 1 81  ? -40.318 -28.490 13.292 1.00 111.76 ? 377 HIS   A ND1 1 
ATOM   567  C  CD2 . HIS   A 1 81  ? -41.875 -28.925 14.760 1.00 115.12 ? 377 HIS   A CD2 1 
ATOM   568  C  CE1 . HIS   A 1 81  ? -39.710 -28.804 14.423 1.00 110.17 ? 377 HIS   A CE1 1 
ATOM   569  N  NE2 . HIS   A 1 81  ? -40.633 -29.078 15.327 1.00 112.12 ? 377 HIS   A NE2 1 
ATOM   570  N  N   . MET   A 1 82  ? -42.350 -30.725 10.532 1.00 102.01 ? 378 MET   A N   1 
ATOM   571  C  CA  . MET   A 1 82  ? -41.852 -32.072 10.292 1.00 112.37 ? 378 MET   A CA  1 
ATOM   572  C  C   . MET   A 1 82  ? -40.848 -32.093 9.143  1.00 113.58 ? 378 MET   A C   1 
ATOM   573  O  O   . MET   A 1 82  ? -39.689 -32.483 9.327  1.00 116.39 ? 378 MET   A O   1 
ATOM   574  C  CB  . MET   A 1 82  ? -43.017 -33.023 10.029 1.00 127.90 ? 378 MET   A CB  1 
ATOM   575  C  CG  . MET   A 1 82  ? -43.579 -33.593 11.307 1.00 141.62 ? 378 MET   A CG  1 
ATOM   576  S  SD  . MET   A 1 82  ? -42.231 -34.091 12.402 1.00 148.95 ? 378 MET   A SD  1 
ATOM   577  C  CE  . MET   A 1 82  ? -41.475 -35.414 11.453 1.00 152.83 ? 378 MET   A CE  1 
ATOM   578  N  N   . ASP   A 1 83  ? -41.263 -31.644 7.954  1.00 107.48 ? 379 ASP   A N   1 
ATOM   579  C  CA  . ASP   A 1 83  ? -40.377 -31.727 6.797  1.00 103.33 ? 379 ASP   A CA  1 
ATOM   580  C  C   . ASP   A 1 83  ? -39.120 -30.892 6.989  1.00 98.59  ? 379 ASP   A C   1 
ATOM   581  O  O   . ASP   A 1 83  ? -38.030 -31.310 6.585  1.00 104.60 ? 379 ASP   A O   1 
ATOM   582  C  CB  . ASP   A 1 83  ? -41.108 -31.306 5.522  1.00 108.64 ? 379 ASP   A CB  1 
ATOM   583  C  CG  . ASP   A 1 83  ? -41.966 -32.415 4.962  1.00 113.35 ? 379 ASP   A CG  1 
ATOM   584  O  OD1 . ASP   A 1 83  ? -43.194 -32.222 4.852  1.00 115.47 ? 379 ASP   A OD1 1 
ATOM   585  O  OD2 . ASP   A 1 83  ? -41.414 -33.494 4.661  1.00 114.81 ? 379 ASP   A OD2 1 
ATOM   586  N  N   . ARG   A 1 84  ? -39.244 -29.716 7.612  1.00 92.16  ? 380 ARG   A N   1 
ATOM   587  C  CA  . ARG   A 1 84  ? -38.063 -28.883 7.826  1.00 94.48  ? 380 ARG   A CA  1 
ATOM   588  C  C   . ARG   A 1 84  ? -37.082 -29.538 8.786  1.00 92.95  ? 380 ARG   A C   1 
ATOM   589  O  O   . ARG   A 1 84  ? -35.878 -29.272 8.718  1.00 99.90  ? 380 ARG   A O   1 
ATOM   590  C  CB  . ARG   A 1 84  ? -38.464 -27.502 8.343  1.00 92.07  ? 380 ARG   A CB  1 
ATOM   591  C  CG  . ARG   A 1 84  ? -37.288 -26.609 8.689  1.00 86.33  ? 380 ARG   A CG  1 
ATOM   592  C  CD  . ARG   A 1 84  ? -36.919 -25.687 7.556  1.00 85.58  ? 380 ARG   A CD  1 
ATOM   593  N  NE  . ARG   A 1 84  ? -35.621 -25.067 7.793  1.00 81.81  ? 380 ARG   A NE  1 
ATOM   594  C  CZ  . ARG   A 1 84  ? -34.498 -25.494 7.230  1.00 72.05  ? 380 ARG   A CZ  1 
ATOM   595  N  NH1 . ARG   A 1 84  ? -34.545 -26.530 6.405  1.00 74.93  ? 380 ARG   A NH1 1 
ATOM   596  N  NH2 . ARG   A 1 84  ? -33.334 -24.895 7.489  1.00 59.82  ? 380 ARG   A NH2 1 
ATOM   597  N  N   . LEU   A 1 85  ? -37.568 -30.393 9.681  1.00 83.13  ? 381 LEU   A N   1 
ATOM   598  C  CA  . LEU   A 1 85  ? -36.658 -31.145 10.531 1.00 82.95  ? 381 LEU   A CA  1 
ATOM   599  C  C   . LEU   A 1 85  ? -35.949 -32.239 9.738  1.00 89.07  ? 381 LEU   A C   1 
ATOM   600  O  O   . LEU   A 1 85  ? -34.715 -32.322 9.734  1.00 85.77  ? 381 LEU   A O   1 
ATOM   601  C  CB  . LEU   A 1 85  ? -37.418 -31.740 11.712 1.00 92.98  ? 381 LEU   A CB  1 
ATOM   602  C  CG  . LEU   A 1 85  ? -36.479 -32.089 12.862 1.00 88.35  ? 381 LEU   A CG  1 
ATOM   603  C  CD1 . LEU   A 1 85  ? -36.510 -31.000 13.911 1.00 82.49  ? 381 LEU   A CD1 1 
ATOM   604  C  CD2 . LEU   A 1 85  ? -36.852 -33.452 13.424 1.00 100.46 ? 381 LEU   A CD2 1 
ATOM   605  N  N   . GLU   A 1 86  ? -36.723 -33.097 9.066  1.00 99.14  ? 382 GLU   A N   1 
ATOM   606  C  CA  . GLU   A 1 86  ? -36.138 -34.101 8.182  1.00 108.98 ? 382 GLU   A CA  1 
ATOM   607  C  C   . GLU   A 1 86  ? -35.161 -33.463 7.207  1.00 104.34 ? 382 GLU   A C   1 
ATOM   608  O  O   . GLU   A 1 86  ? -34.065 -33.987 6.975  1.00 103.21 ? 382 GLU   A O   1 
ATOM   609  C  CB  . GLU   A 1 86  ? -37.246 -34.836 7.422  1.00 127.90 ? 382 GLU   A CB  1 
ATOM   610  C  CG  . GLU   A 1 86  ? -36.769 -35.981 6.536  1.00 142.15 ? 382 GLU   A CG  1 
ATOM   611  C  CD  . GLU   A 1 86  ? -36.523 -37.275 7.303  1.00 157.21 ? 382 GLU   A CD  1 
ATOM   612  O  OE1 . GLU   A 1 86  ? -35.997 -38.230 6.689  1.00 162.82 ? 382 GLU   A OE1 1 
ATOM   613  O  OE2 . GLU   A 1 86  ? -36.857 -37.343 8.509  1.00 159.16 ? 382 GLU   A OE2 1 
ATOM   614  N  N   . GLU   A 1 87  ? -35.534 -32.313 6.647  1.00 86.47  ? 383 GLU   A N   1 
ATOM   615  C  CA  . GLU   A 1 87  ? -34.667 -31.625 5.698  1.00 84.48  ? 383 GLU   A CA  1 
ATOM   616  C  C   . GLU   A 1 87  ? -33.342 -31.229 6.343  1.00 82.75  ? 383 GLU   A C   1 
ATOM   617  O  O   . GLU   A 1 87  ? -32.269 -31.455 5.771  1.00 81.31  ? 383 GLU   A O   1 
ATOM   618  C  CB  . GLU   A 1 87  ? -35.394 -30.401 5.137  1.00 85.34  ? 383 GLU   A CB  1 
ATOM   619  C  CG  . GLU   A 1 87  ? -34.545 -29.511 4.261  1.00 91.11  ? 383 GLU   A CG  1 
ATOM   620  C  CD  . GLU   A 1 87  ? -35.345 -28.380 3.643  1.00 92.87  ? 383 GLU   A CD  1 
ATOM   621  O  OE1 . GLU   A 1 87  ? -35.862 -27.529 4.399  1.00 82.14  ? 383 GLU   A OE1 1 
ATOM   622  O  OE2 . GLU   A 1 87  ? -35.461 -28.356 2.391  1.00 97.51  ? 383 GLU   A OE2 1 
ATOM   623  N  N   . VAL   A 1 88  ? -33.393 -30.661 7.552  1.00 76.21  ? 384 VAL   A N   1 
ATOM   624  C  CA  . VAL   A 1 88  ? -32.167 -30.187 8.188  1.00 77.50  ? 384 VAL   A CA  1 
ATOM   625  C  C   . VAL   A 1 88  ? -31.293 -31.360 8.596  1.00 87.27  ? 384 VAL   A C   1 
ATOM   626  O  O   . VAL   A 1 88  ? -30.067 -31.317 8.448  1.00 88.39  ? 384 VAL   A O   1 
ATOM   627  C  CB  . VAL   A 1 88  ? -32.494 -29.281 9.387  1.00 76.32  ? 384 VAL   A CB  1 
ATOM   628  C  CG1 . VAL   A 1 88  ? -31.253 -29.077 10.233 1.00 76.95  ? 384 VAL   A CG1 1 
ATOM   629  C  CG2 . VAL   A 1 88  ? -33.013 -27.946 8.897  1.00 78.97  ? 384 VAL   A CG2 1 
ATOM   630  N  N   . ASN   A 1 89  ? -31.909 -32.419 9.124  1.00 94.75  ? 385 ASN   A N   1 
ATOM   631  C  CA  . ASN   A 1 89  ? -31.190 -33.654 9.416  1.00 100.96 ? 385 ASN   A CA  1 
ATOM   632  C  C   . ASN   A 1 89  ? -30.460 -34.166 8.176  1.00 102.12 ? 385 ASN   A C   1 
ATOM   633  O  O   . ASN   A 1 89  ? -29.271 -34.504 8.229  1.00 102.40 ? 385 ASN   A O   1 
ATOM   634  C  CB  . ASN   A 1 89  ? -32.181 -34.697 9.944  1.00 109.77 ? 385 ASN   A CB  1 
ATOM   635  C  CG  . ASN   A 1 89  ? -31.516 -35.790 10.764 1.00 116.05 ? 385 ASN   A CG  1 
ATOM   636  O  OD1 . ASN   A 1 89  ? -30.666 -35.517 11.620 1.00 108.05 ? 385 ASN   A OD1 1 
ATOM   637  N  ND2 . ASN   A 1 89  ? -31.906 -37.044 10.508 1.00 119.54 ? 385 ASN   A ND2 1 
ATOM   638  N  N   . LYS   A 1 90  ? -31.157 -34.208 7.038  1.00 96.73  ? 386 LYS   A N   1 
ATOM   639  C  CA  . LYS   A 1 90  ? -30.534 -34.686 5.808  1.00 110.16 ? 386 LYS   A CA  1 
ATOM   640  C  C   . LYS   A 1 90  ? -29.354 -33.807 5.403  1.00 108.39 ? 386 LYS   A C   1 
ATOM   641  O  O   . LYS   A 1 90  ? -28.316 -34.315 4.960  1.00 111.00 ? 386 LYS   A O   1 
ATOM   642  C  CB  . LYS   A 1 90  ? -31.572 -34.748 4.683  1.00 119.53 ? 386 LYS   A CB  1 
ATOM   643  C  CG  . LYS   A 1 90  ? -32.640 -35.834 4.837  1.00 123.41 ? 386 LYS   A CG  1 
ATOM   644  C  CD  . LYS   A 1 90  ? -33.680 -35.747 3.714  1.00 123.93 ? 386 LYS   A CD  1 
ATOM   645  C  CE  . LYS   A 1 90  ? -34.651 -36.925 3.742  1.00 129.63 ? 386 LYS   A CE  1 
ATOM   646  N  NZ  . LYS   A 1 90  ? -35.753 -36.791 2.740  1.00 127.51 ? 386 LYS   A NZ  1 
ATOM   647  N  N   . GLU   A 1 91  ? -29.489 -32.484 5.547  1.00 100.95 ? 387 GLU   A N   1 
ATOM   648  C  CA  . GLU   A 1 91  ? -28.387 -31.594 5.198  1.00 96.52  ? 387 GLU   A CA  1 
ATOM   649  C  C   . GLU   A 1 91  ? -27.232 -31.706 6.189  1.00 98.43  ? 387 GLU   A C   1 
ATOM   650  O  O   . GLU   A 1 91  ? -26.094 -31.368 5.839  1.00 94.53  ? 387 GLU   A O   1 
ATOM   651  C  CB  . GLU   A 1 91  ? -28.877 -30.142 5.106  1.00 95.69  ? 387 GLU   A CB  1 
ATOM   652  C  CG  . GLU   A 1 91  ? -27.895 -29.197 4.404  1.00 92.16  ? 387 GLU   A CG  1 
ATOM   653  C  CD  . GLU   A 1 91  ? -28.333 -27.732 4.377  1.00 91.93  ? 387 GLU   A CD  1 
ATOM   654  O  OE1 . GLU   A 1 91  ? -27.471 -26.877 4.080  1.00 88.40  ? 387 GLU   A OE1 1 
ATOM   655  O  OE2 . GLU   A 1 91  ? -29.518 -27.422 4.646  1.00 90.05  ? 387 GLU   A OE2 1 
ATOM   656  N  N   . ILE   A 1 92  ? -27.494 -32.177 7.412  1.00 99.46  ? 388 ILE   A N   1 
ATOM   657  C  CA  . ILE   A 1 92  ? -26.414 -32.418 8.364  1.00 96.17  ? 388 ILE   A CA  1 
ATOM   658  C  C   . ILE   A 1 92  ? -25.765 -33.780 8.141  1.00 110.37 ? 388 ILE   A C   1 
ATOM   659  O  O   . ILE   A 1 92  ? -24.600 -33.973 8.508  1.00 118.03 ? 388 ILE   A O   1 
ATOM   660  C  CB  . ILE   A 1 92  ? -26.905 -32.292 9.817  1.00 84.86  ? 388 ILE   A CB  1 
ATOM   661  C  CG1 . ILE   A 1 92  ? -27.563 -30.930 10.048 1.00 74.49  ? 388 ILE   A CG1 1 
ATOM   662  C  CG2 . ILE   A 1 92  ? -25.739 -32.415 10.781 1.00 92.25  ? 388 ILE   A CG2 1 
ATOM   663  C  CD1 . ILE   A 1 92  ? -27.920 -30.637 11.526 1.00 69.62  ? 388 ILE   A CD1 1 
ATOM   664  N  N   . GLU   A 1 93  ? -26.482 -34.742 7.557  1.00 112.47 ? 389 GLU   A N   1 
ATOM   665  C  CA  . GLU   A 1 93  ? -25.805 -35.930 7.048  1.00 122.56 ? 389 GLU   A CA  1 
ATOM   666  C  C   . GLU   A 1 93  ? -24.887 -35.550 5.897  1.00 121.68 ? 389 GLU   A C   1 
ATOM   667  O  O   . GLU   A 1 93  ? -23.684 -35.841 5.913  1.00 114.51 ? 389 GLU   A O   1 
ATOM   668  C  CB  . GLU   A 1 93  ? -26.823 -36.977 6.582  1.00 131.19 ? 389 GLU   A CB  1 
ATOM   669  C  CG  . GLU   A 1 93  ? -27.931 -37.308 7.569  1.00 137.86 ? 389 GLU   A CG  1 
ATOM   670  C  CD  . GLU   A 1 93  ? -27.476 -38.207 8.703  1.00 142.82 ? 389 GLU   A CD  1 
ATOM   671  O  OE1 . GLU   A 1 93  ? -26.315 -38.669 8.674  1.00 144.85 ? 389 GLU   A OE1 1 
ATOM   672  O  OE2 . GLU   A 1 93  ? -28.285 -38.453 9.626  1.00 144.95 ? 389 GLU   A OE2 1 
ATOM   673  N  N   . SER   A 1 94  ? -25.448 -34.866 4.901  1.00 127.96 ? 390 SER   A N   1 
ATOM   674  C  CA  . SER   A 1 94  ? -24.788 -34.527 3.649  1.00 131.28 ? 390 SER   A CA  1 
ATOM   675  C  C   . SER   A 1 94  ? -23.582 -33.624 3.870  1.00 129.84 ? 390 SER   A C   1 
ATOM   676  O  O   . SER   A 1 94  ? -22.449 -34.017 3.572  1.00 131.46 ? 390 SER   A O   1 
ATOM   677  C  CB  . SER   A 1 94  ? -25.796 -33.859 2.714  1.00 134.38 ? 390 SER   A CB  1 
ATOM   678  O  OG  . SER   A 1 94  ? -25.176 -32.894 1.886  1.00 137.67 ? 390 SER   A OG  1 
ATOM   679  N  N   . THR   A 1 95  ? -23.816 -32.420 4.397  1.00 130.32 ? 391 THR   A N   1 
ATOM   680  C  CA  . THR   A 1 95  ? -22.783 -31.398 4.536  1.00 130.03 ? 391 THR   A CA  1 
ATOM   681  C  C   . THR   A 1 95  ? -22.157 -31.351 5.923  1.00 118.01 ? 391 THR   A C   1 
ATOM   682  O  O   . THR   A 1 95  ? -21.235 -30.559 6.137  1.00 111.47 ? 391 THR   A O   1 
ATOM   683  C  CB  . THR   A 1 95  ? -23.354 -30.009 4.215  1.00 137.58 ? 391 THR   A CB  1 
ATOM   684  O  OG1 . THR   A 1 95  ? -24.651 -30.139 3.619  1.00 146.09 ? 391 THR   A OG1 1 
ATOM   685  C  CG2 . THR   A 1 95  ? -22.433 -29.253 3.265  1.00 137.40 ? 391 THR   A CG2 1 
ATOM   686  N  N   . SER   A 1 96  ? -22.633 -32.165 6.864  1.00 116.03 ? 392 SER   A N   1 
ATOM   687  C  CA  . SER   A 1 96  ? -22.234 -32.088 8.270  1.00 121.54 ? 392 SER   A CA  1 
ATOM   688  C  C   . SER   A 1 96  ? -22.526 -30.717 8.868  1.00 116.71 ? 392 SER   A C   1 
ATOM   689  O  O   . SER   A 1 96  ? -21.906 -30.323 9.860  1.00 118.89 ? 392 SER   A O   1 
ATOM   690  C  CB  . SER   A 1 96  ? -20.756 -32.447 8.464  1.00 131.65 ? 392 SER   A CB  1 
ATOM   691  O  OG  . SER   A 1 96  ? -19.908 -31.477 7.872  1.00 134.49 ? 392 SER   A OG  1 
ATOM   692  N  N   . THR   A 1 97  ? -23.459 -29.983 8.268  1.00 108.58 ? 393 THR   A N   1 
ATOM   693  C  CA  . THR   A 1 97  ? -23.889 -28.666 8.729  1.00 95.40  ? 393 THR   A CA  1 
ATOM   694  C  C   . THR   A 1 97  ? -25.211 -28.362 8.035  1.00 91.90  ? 393 THR   A C   1 
ATOM   695  O  O   . THR   A 1 97  ? -25.799 -29.236 7.392  1.00 97.86  ? 393 THR   A O   1 
ATOM   696  C  CB  . THR   A 1 97  ? -22.825 -27.602 8.442  1.00 89.34  ? 393 THR   A CB  1 
ATOM   697  O  OG1 . THR   A 1 97  ? -23.219 -26.366 9.043  1.00 88.66  ? 393 THR   A OG1 1 
ATOM   698  C  CG2 . THR   A 1 97  ? -22.675 -27.399 6.939  1.00 89.78  ? 393 THR   A CG2 1 
ATOM   699  N  N   . TYR   A 1 98  ? -25.687 -27.127 8.148  1.00 78.04  ? 394 TYR   A N   1 
ATOM   700  C  CA  . TYR   A 1 98  ? -26.902 -26.777 7.425  1.00 85.99  ? 394 TYR   A CA  1 
ATOM   701  C  C   . TYR   A 1 98  ? -26.981 -25.259 7.282  1.00 80.79  ? 394 TYR   A C   1 
ATOM   702  O  O   . TYR   A 1 98  ? -26.100 -24.516 7.728  1.00 73.78  ? 394 TYR   A O   1 
ATOM   703  C  CB  . TYR   A 1 98  ? -28.146 -27.365 8.109  1.00 84.84  ? 394 TYR   A CB  1 
ATOM   704  C  CG  . TYR   A 1 98  ? -28.468 -26.721 9.424  1.00 80.01  ? 394 TYR   A CG  1 
ATOM   705  C  CD1 . TYR   A 1 98  ? -29.504 -25.803 9.534  1.00 78.86  ? 394 TYR   A CD1 1 
ATOM   706  C  CD2 . TYR   A 1 98  ? -27.722 -27.013 10.564 1.00 82.73  ? 394 TYR   A CD2 1 
ATOM   707  C  CE1 . TYR   A 1 98  ? -29.788 -25.193 10.741 1.00 76.01  ? 394 TYR   A CE1 1 
ATOM   708  C  CE2 . TYR   A 1 98  ? -27.998 -26.423 11.756 1.00 72.38  ? 394 TYR   A CE2 1 
ATOM   709  C  CZ  . TYR   A 1 98  ? -29.032 -25.508 11.853 1.00 72.54  ? 394 TYR   A CZ  1 
ATOM   710  O  OH  . TYR   A 1 98  ? -29.301 -24.915 13.070 1.00 69.55  ? 394 TYR   A OH  1 
ATOM   711  N  N   . GLN   A 1 99  ? -28.049 -24.808 6.634  1.00 72.68  ? 395 GLN   A N   1 
ATOM   712  C  CA  . GLN   A 1 99  ? -28.247 -23.405 6.311  1.00 66.90  ? 395 GLN   A CA  1 
ATOM   713  C  C   . GLN   A 1 99  ? -29.604 -22.958 6.827  1.00 60.92  ? 395 GLN   A C   1 
ATOM   714  O  O   . GLN   A 1 99  ? -30.600 -23.680 6.706  1.00 58.56  ? 395 GLN   A O   1 
ATOM   715  C  CB  . GLN   A 1 99  ? -28.157 -23.158 4.766  1.00 65.47  ? 395 GLN   A CB  1 
ATOM   716  C  CG  . GLN   A 1 99  ? -26.758 -23.291 4.169  1.00 64.27  ? 395 GLN   A CG  1 
ATOM   717  C  CD  . GLN   A 1 99  ? -25.771 -22.273 4.735  1.00 77.05  ? 395 GLN   A CD  1 
ATOM   718  O  OE1 . GLN   A 1 99  ? -24.627 -22.607 5.044  1.00 79.59  ? 395 GLN   A OE1 1 
ATOM   719  N  NE2 . GLN   A 1 99  ? -26.212 -21.027 4.872  1.00 81.21  ? 395 GLN   A NE2 1 
ATOM   720  N  N   . LEU   A 1 100 ? -29.636 -21.765 7.401  1.00 54.86  ? 396 LEU   A N   1 
ATOM   721  C  CA  . LEU   A 1 100 ? -30.877 -21.200 7.909  1.00 46.90  ? 396 LEU   A CA  1 
ATOM   722  C  C   . LEU   A 1 100 ? -31.704 -20.619 6.775  1.00 58.69  ? 396 LEU   A C   1 
ATOM   723  O  O   . LEU   A 1 100 ? -31.160 -20.009 5.848  1.00 59.04  ? 396 LEU   A O   1 
ATOM   724  C  CB  . LEU   A 1 100 ? -30.570 -20.103 8.930  1.00 44.27  ? 396 LEU   A CB  1 
ATOM   725  C  CG  . LEU   A 1 100 ? -29.821 -20.632 10.144 1.00 52.49  ? 396 LEU   A CG  1 
ATOM   726  C  CD1 . LEU   A 1 100 ? -29.319 -19.494 11.005 1.00 56.32  ? 396 LEU   A CD1 1 
ATOM   727  C  CD2 . LEU   A 1 100 ? -30.730 -21.553 10.937 1.00 45.73  ? 396 LEU   A CD2 1 
ATOM   728  N  N   . LYS   A 1 101 ? -33.023 -20.800 6.848  1.00 56.21  ? 397 LYS   A N   1 
ATOM   729  C  CA  . LYS   A 1 101 ? -33.906 -20.005 6.005  1.00 70.23  ? 397 LYS   A CA  1 
ATOM   730  C  C   . LYS   A 1 101 ? -33.800 -18.543 6.414  1.00 71.56  ? 397 LYS   A C   1 
ATOM   731  O  O   . LYS   A 1 101 ? -33.436 -18.221 7.549  1.00 68.43  ? 397 LYS   A O   1 
ATOM   732  C  CB  . LYS   A 1 101 ? -35.351 -20.469 6.138  1.00 76.75  ? 397 LYS   A CB  1 
ATOM   733  C  CG  . LYS   A 1 101 ? -35.537 -21.957 6.042  1.00 80.93  ? 397 LYS   A CG  1 
ATOM   734  C  CD  . LYS   A 1 101 ? -35.663 -22.385 4.605  1.00 81.83  ? 397 LYS   A CD  1 
ATOM   735  C  CE  . LYS   A 1 101 ? -34.696 -23.499 4.273  1.00 87.30  ? 397 LYS   A CE  1 
ATOM   736  N  NZ  . LYS   A 1 101 ? -34.633 -23.698 2.786  1.00 94.20  ? 397 LYS   A NZ  1 
ATOM   737  N  N   . ASP   A 1 102 ? -34.113 -17.644 5.479  1.00 62.48  ? 398 ASP   A N   1 
ATOM   738  C  CA  . ASP   A 1 102 ? -34.128 -16.220 5.822  1.00 59.00  ? 398 ASP   A CA  1 
ATOM   739  C  C   . ASP   A 1 102 ? -35.033 -15.949 7.013  1.00 60.19  ? 398 ASP   A C   1 
ATOM   740  O  O   . ASP   A 1 102 ? -34.686 -15.164 7.907  1.00 58.50  ? 398 ASP   A O   1 
ATOM   741  C  CB  . ASP   A 1 102 ? -34.598 -15.386 4.627  1.00 76.39  ? 398 ASP   A CB  1 
ATOM   742  C  CG  . ASP   A 1 102 ? -33.590 -15.343 3.505  1.00 75.71  ? 398 ASP   A CG  1 
ATOM   743  O  OD1 . ASP   A 1 102 ? -32.368 -15.373 3.769  1.00 73.63  ? 398 ASP   A OD1 1 
ATOM   744  O  OD2 . ASP   A 1 102 ? -34.029 -15.266 2.344  1.00 87.43  ? 398 ASP   A OD2 1 
ATOM   745  N  N   . THR   A 1 103 ? -36.218 -16.559 7.023  1.00 61.56  ? 399 THR   A N   1 
ATOM   746  C  CA  . THR   A 1 103 ? -37.113 -16.427 8.166  1.00 68.49  ? 399 THR   A CA  1 
ATOM   747  C  C   . THR   A 1 103 ? -36.412 -16.835 9.458  1.00 72.31  ? 399 THR   A C   1 
ATOM   748  O  O   . THR   A 1 103 ? -36.391 -16.079 10.438 1.00 71.42  ? 399 THR   A O   1 
ATOM   749  C  CB  . THR   A 1 103 ? -38.354 -17.281 7.928  1.00 70.32  ? 399 THR   A CB  1 
ATOM   750  O  OG1 . THR   A 1 103 ? -37.939 -18.562 7.437  1.00 70.78  ? 399 THR   A OG1 1 
ATOM   751  C  CG2 . THR   A 1 103 ? -39.267 -16.625 6.894  1.00 63.31  ? 399 THR   A CG2 1 
ATOM   752  N  N   . GLU   A 1 104 ? -35.796 -18.021 9.463  1.00 70.90  ? 400 GLU   A N   1 
ATOM   753  C  CA  . GLU   A 1 104 ? -35.141 -18.527 10.669 1.00 62.53  ? 400 GLU   A CA  1 
ATOM   754  C  C   . GLU   A 1 104 ? -33.964 -17.655 11.090 1.00 63.52  ? 400 GLU   A C   1 
ATOM   755  O  O   . GLU   A 1 104 ? -33.663 -17.556 12.291 1.00 64.91  ? 400 GLU   A O   1 
ATOM   756  C  CB  . GLU   A 1 104 ? -34.673 -19.966 10.434 1.00 61.27  ? 400 GLU   A CB  1 
ATOM   757  C  CG  . GLU   A 1 104 ? -35.689 -20.829 9.682  1.00 65.64  ? 400 GLU   A CG  1 
ATOM   758  C  CD  . GLU   A 1 104 ? -35.142 -22.196 9.317  1.00 75.77  ? 400 GLU   A CD  1 
ATOM   759  O  OE1 . GLU   A 1 104 ? -35.952 -23.130 9.124  1.00 79.77  ? 400 GLU   A OE1 1 
ATOM   760  O  OE2 . GLU   A 1 104 ? -33.902 -22.327 9.202  1.00 76.32  ? 400 GLU   A OE2 1 
ATOM   761  N  N   . LEU   A 1 105 ? -33.272 -17.029 10.127 1.00 61.76  ? 401 LEU   A N   1 
ATOM   762  C  CA  . LEU   A 1 105 ? -32.157 -16.149 10.480 1.00 62.22  ? 401 LEU   A CA  1 
ATOM   763  C  C   . LEU   A 1 105 ? -32.637 -14.909 11.234 1.00 57.22  ? 401 LEU   A C   1 
ATOM   764  O  O   . LEU   A 1 105 ? -32.030 -14.513 12.242 1.00 49.32  ? 401 LEU   A O   1 
ATOM   765  C  CB  . LEU   A 1 105 ? -31.386 -15.753 9.220  1.00 57.81  ? 401 LEU   A CB  1 
ATOM   766  C  CG  . LEU   A 1 105 ? -30.060 -15.013 9.444  1.00 58.10  ? 401 LEU   A CG  1 
ATOM   767  C  CD1 . LEU   A 1 105 ? -28.931 -15.982 9.808  1.00 56.55  ? 401 LEU   A CD1 1 
ATOM   768  C  CD2 . LEU   A 1 105 ? -29.710 -14.237 8.212  1.00 64.52  ? 401 LEU   A CD2 1 
ATOM   769  N  N   . ILE   A 1 106 ? -33.730 -14.296 10.761 1.00 53.42  ? 402 ILE   A N   1 
ATOM   770  C  CA  . ILE   A 1 106 ? -34.279 -13.086 11.377 1.00 51.37  ? 402 ILE   A CA  1 
ATOM   771  C  C   . ILE   A 1 106 ? -34.843 -13.402 12.764 1.00 56.51  ? 402 ILE   A C   1 
ATOM   772  O  O   . ILE   A 1 106 ? -34.677 -12.625 13.711 1.00 53.62  ? 402 ILE   A O   1 
ATOM   773  C  CB  . ILE   A 1 106 ? -35.330 -12.464 10.427 1.00 54.53  ? 402 ILE   A CB  1 
ATOM   774  C  CG1 . ILE   A 1 106 ? -34.647 -12.005 9.137  1.00 52.05  ? 402 ILE   A CG1 1 
ATOM   775  C  CG2 . ILE   A 1 106 ? -36.043 -11.282 11.047 1.00 57.84  ? 402 ILE   A CG2 1 
ATOM   776  C  CD1 . ILE   A 1 106 ? -35.601 -11.538 7.988  1.00 52.68  ? 402 ILE   A CD1 1 
ATOM   777  N  N   . TYR   A 1 107 ? -35.501 -14.552 12.908 1.00 56.82  ? 403 TYR   A N   1 
ATOM   778  C  CA  . TYR   A 1 107 ? -35.977 -14.982 14.213 1.00 60.33  ? 403 TYR   A CA  1 
ATOM   779  C  C   . TYR   A 1 107 ? -34.812 -15.194 15.169 1.00 65.56  ? 403 TYR   A C   1 
ATOM   780  O  O   . TYR   A 1 107 ? -34.794 -14.645 16.278 1.00 57.75  ? 403 TYR   A O   1 
ATOM   781  C  CB  . TYR   A 1 107 ? -36.793 -16.263 14.061 1.00 66.27  ? 403 TYR   A CB  1 
ATOM   782  C  CG  . TYR   A 1 107 ? -37.178 -16.918 15.367 1.00 72.39  ? 403 TYR   A CG  1 
ATOM   783  C  CD1 . TYR   A 1 107 ? -38.434 -16.715 15.928 1.00 77.13  ? 403 TYR   A CD1 1 
ATOM   784  C  CD2 . TYR   A 1 107 ? -36.290 -17.757 16.039 1.00 78.31  ? 403 TYR   A CD2 1 
ATOM   785  C  CE1 . TYR   A 1 107 ? -38.786 -17.327 17.133 1.00 80.26  ? 403 TYR   A CE1 1 
ATOM   786  C  CE2 . TYR   A 1 107 ? -36.631 -18.361 17.238 1.00 79.19  ? 403 TYR   A CE2 1 
ATOM   787  C  CZ  . TYR   A 1 107 ? -37.877 -18.147 17.781 1.00 80.39  ? 403 TYR   A CZ  1 
ATOM   788  O  OH  . TYR   A 1 107 ? -38.199 -18.766 18.971 1.00 78.93  ? 403 TYR   A OH  1 
ATOM   789  N  N   . GLY   A 1 108 ? -33.828 -15.997 14.755 1.00 66.63  ? 404 GLY   A N   1 
ATOM   790  C  CA  . GLY   A 1 108 ? -32.694 -16.271 15.626 1.00 58.55  ? 404 GLY   A CA  1 
ATOM   791  C  C   . GLY   A 1 108 ? -31.978 -15.010 16.064 1.00 55.35  ? 404 GLY   A C   1 
ATOM   792  O  O   . GLY   A 1 108 ? -31.576 -14.882 17.217 1.00 50.51  ? 404 GLY   A O   1 
ATOM   793  N  N   . ALA   A 1 109 ? -31.828 -14.056 15.156 1.00 49.49  ? 405 ALA   A N   1 
ATOM   794  C  CA  . ALA   A 1 109 ? -31.123 -12.826 15.479 1.00 55.21  ? 405 ALA   A CA  1 
ATOM   795  C  C   . ALA   A 1 109 ? -31.899 -12.006 16.501 1.00 59.37  ? 405 ALA   A C   1 
ATOM   796  O  O   . ALA   A 1 109 ? -31.345 -11.589 17.526 1.00 60.01  ? 405 ALA   A O   1 
ATOM   797  C  CB  . ALA   A 1 109 ? -30.882 -12.030 14.191 1.00 52.60  ? 405 ALA   A CB  1 
ATOM   798  N  N   . LYS   A 1 110 ? -33.190 -11.772 16.249 1.00 58.84  ? 406 LYS   A N   1 
ATOM   799  C  CA  . LYS   A 1 110 ? -33.984 -10.996 17.199 1.00 56.72  ? 406 LYS   A CA  1 
ATOM   800  C  C   . LYS   A 1 110 ? -33.993 -11.642 18.576 1.00 57.02  ? 406 LYS   A C   1 
ATOM   801  O  O   . LYS   A 1 110 ? -34.030 -10.934 19.594 1.00 58.36  ? 406 LYS   A O   1 
ATOM   802  C  CB  . LYS   A 1 110 ? -35.413 -10.834 16.687 1.00 58.82  ? 406 LYS   A CB  1 
ATOM   803  C  CG  . LYS   A 1 110 ? -35.527 -9.838  15.554 1.00 53.84  ? 406 LYS   A CG  1 
ATOM   804  C  CD  . LYS   A 1 110 ? -36.931 -9.821  14.989 1.00 53.49  ? 406 LYS   A CD  1 
ATOM   805  C  CE  . LYS   A 1 110 ? -37.078 -8.749  13.926 1.00 61.53  ? 406 LYS   A CE  1 
ATOM   806  N  NZ  . LYS   A 1 110 ? -38.509 -8.612  13.560 1.00 64.19  ? 406 LYS   A NZ  1 
ATOM   807  N  N   . HIS   A 1 111 ? -33.925 -12.976 18.633 1.00 50.94  ? 407 HIS   A N   1 
ATOM   808  C  CA  . HIS   A 1 111 ? -34.038 -13.677 19.908 1.00 58.89  ? 407 HIS   A CA  1 
ATOM   809  C  C   . HIS   A 1 111 ? -32.707 -13.771 20.649 1.00 59.55  ? 407 HIS   A C   1 
ATOM   810  O  O   . HIS   A 1 111 ? -32.701 -13.856 21.883 1.00 61.94  ? 407 HIS   A O   1 
ATOM   811  C  CB  . HIS   A 1 111 ? -34.649 -15.054 19.670 1.00 54.00  ? 407 HIS   A CB  1 
ATOM   812  C  CG  . HIS   A 1 111 ? -36.139 -15.013 19.545 1.00 53.18  ? 407 HIS   A CG  1 
ATOM   813  N  ND1 . HIS   A 1 111 ? -36.985 -15.269 20.609 1.00 52.98  ? 407 HIS   A ND1 1 
ATOM   814  C  CD2 . HIS   A 1 111 ? -36.935 -14.673 18.503 1.00 47.57  ? 407 HIS   A CD2 1 
ATOM   815  C  CE1 . HIS   A 1 111 ? -38.239 -15.136 20.210 1.00 54.14  ? 407 HIS   A CE1 1 
ATOM   816  N  NE2 . HIS   A 1 111 ? -38.235 -14.773 18.935 1.00 54.56  ? 407 HIS   A NE2 1 
ATOM   817  N  N   . ALA   A 1 112 ? -31.580 -13.732 19.932 1.00 53.75  ? 408 ALA   A N   1 
ATOM   818  C  CA  . ALA   A 1 112 ? -30.292 -13.572 20.600 1.00 51.60  ? 408 ALA   A CA  1 
ATOM   819  C  C   . ALA   A 1 112 ? -30.245 -12.258 21.370 1.00 58.62  ? 408 ALA   A C   1 
ATOM   820  O  O   . ALA   A 1 112 ? -29.757 -12.199 22.505 1.00 70.35  ? 408 ALA   A O   1 
ATOM   821  C  CB  . ALA   A 1 112 ? -29.170 -13.639 19.568 1.00 49.19  ? 408 ALA   A CB  1 
ATOM   822  N  N   . TRP   A 1 113 ? -30.767 -11.195 20.768 1.00 48.35  ? 409 TRP   A N   1 
ATOM   823  C  CA  . TRP   A 1 113 ? -30.939 -9.930  21.468 1.00 48.21  ? 409 TRP   A CA  1 
ATOM   824  C  C   . TRP   A 1 113 ? -31.873 -10.098 22.660 1.00 50.34  ? 409 TRP   A C   1 
ATOM   825  O  O   . TRP   A 1 113 ? -31.508 -9.807  23.800 1.00 57.83  ? 409 TRP   A O   1 
ATOM   826  C  CB  . TRP   A 1 113 ? -31.490 -8.893  20.488 1.00 43.97  ? 409 TRP   A CB  1 
ATOM   827  C  CG  . TRP   A 1 113 ? -31.605 -7.517  21.052 1.00 46.03  ? 409 TRP   A CG  1 
ATOM   828  C  CD1 . TRP   A 1 113 ? -31.201 -7.093  22.299 1.00 55.39  ? 409 TRP   A CD1 1 
ATOM   829  C  CD2 . TRP   A 1 113 ? -32.168 -6.372  20.404 1.00 48.83  ? 409 TRP   A CD2 1 
ATOM   830  N  NE1 . TRP   A 1 113 ? -31.485 -5.759  22.461 1.00 50.13  ? 409 TRP   A NE1 1 
ATOM   831  C  CE2 . TRP   A 1 113 ? -32.075 -5.290  21.312 1.00 46.62  ? 409 TRP   A CE2 1 
ATOM   832  C  CE3 . TRP   A 1 113 ? -32.752 -6.154  19.149 1.00 51.25  ? 409 TRP   A CE3 1 
ATOM   833  C  CZ2 . TRP   A 1 113 ? -32.535 -4.021  21.004 1.00 44.70  ? 409 TRP   A CZ2 1 
ATOM   834  C  CZ3 . TRP   A 1 113 ? -33.206 -4.885  18.839 1.00 56.23  ? 409 TRP   A CZ3 1 
ATOM   835  C  CH2 . TRP   A 1 113 ? -33.096 -3.832  19.763 1.00 57.64  ? 409 TRP   A CH2 1 
ATOM   836  N  N   . ARG   A 1 114 ? -33.089 -10.571 22.405 1.00 42.68  ? 410 ARG   A N   1 
ATOM   837  C  CA  . ARG   A 1 114 ? -34.100 -10.804 23.428 1.00 49.62  ? 410 ARG   A CA  1 
ATOM   838  C  C   . ARG   A 1 114 ? -33.520 -11.498 24.658 1.00 53.76  ? 410 ARG   A C   1 
ATOM   839  O  O   . ARG   A 1 114 ? -33.878 -11.167 25.799 1.00 53.79  ? 410 ARG   A O   1 
ATOM   840  C  CB  . ARG   A 1 114 ? -35.242 -11.647 22.843 1.00 45.49  ? 410 ARG   A CB  1 
ATOM   841  C  CG  . ARG   A 1 114 ? -36.462 -11.719 23.737 1.00 55.05  ? 410 ARG   A CG  1 
ATOM   842  C  CD  . ARG   A 1 114 ? -37.582 -12.539 23.115 1.00 57.11  ? 410 ARG   A CD  1 
ATOM   843  N  NE  . ARG   A 1 114 ? -38.841 -12.335 23.832 1.00 59.17  ? 410 ARG   A NE  1 
ATOM   844  C  CZ  . ARG   A 1 114 ? -40.002 -12.876 23.484 1.00 60.88  ? 410 ARG   A CZ  1 
ATOM   845  N  NH1 . ARG   A 1 114 ? -41.099 -12.632 24.194 1.00 59.19  ? 410 ARG   A NH1 1 
ATOM   846  N  NH2 . ARG   A 1 114 ? -40.074 -13.652 22.417 1.00 68.04  ? 410 ARG   A NH2 1 
ATOM   847  N  N   . ASN   A 1 115 ? -32.599 -12.434 24.429 1.00 46.98  ? 411 ASN   A N   1 
ATOM   848  C  CA  . ASN   A 1 115 ? -32.020 -13.255 25.484 1.00 46.41  ? 411 ASN   A CA  1 
ATOM   849  C  C   . ASN   A 1 115 ? -30.753 -12.665 26.094 1.00 49.20  ? 411 ASN   A C   1 
ATOM   850  O  O   . ASN   A 1 115 ? -30.127 -13.317 26.943 1.00 47.22  ? 411 ASN   A O   1 
ATOM   851  C  CB  . ASN   A 1 115 ? -31.691 -14.651 24.950 1.00 35.89  ? 411 ASN   A CB  1 
ATOM   852  C  CG  . ASN   A 1 115 ? -32.916 -15.395 24.459 1.00 46.12  ? 411 ASN   A CG  1 
ATOM   853  O  OD1 . ASN   A 1 115 ? -34.033 -15.120 24.888 1.00 52.22  ? 411 ASN   A OD1 1 
ATOM   854  N  ND2 . ASN   A 1 115 ? -32.713 -16.345 23.546 1.00 50.19  ? 411 ASN   A ND2 1 
ATOM   855  N  N   . ALA   A 1 116 ? -30.344 -11.477 25.675 1.00 42.84  ? 412 ALA   A N   1 
ATOM   856  C  CA  . ALA   A 1 116 ? -29.086 -10.882 26.118 1.00 48.46  ? 412 ALA   A CA  1 
ATOM   857  C  C   . ALA   A 1 116 ? -29.296 -10.303 27.513 1.00 46.79  ? 412 ALA   A C   1 
ATOM   858  O  O   . ALA   A 1 116 ? -29.787 -9.190  27.661 1.00 48.25  ? 412 ALA   A O   1 
ATOM   859  C  CB  . ALA   A 1 116 ? -28.633 -9.804  25.132 1.00 37.30  ? 412 ALA   A CB  1 
ATOM   860  N  N   . SER   A 1 117 ? -28.924 -11.052 28.551 1.00 52.04  ? 413 SER   A N   1 
ATOM   861  C  CA  . SER   A 1 117 ? -29.301 -10.652 29.906 1.00 59.30  ? 413 SER   A CA  1 
ATOM   862  C  C   . SER   A 1 117 ? -28.598 -9.380  30.361 1.00 53.78  ? 413 SER   A C   1 
ATOM   863  O  O   . SER   A 1 117 ? -29.116 -8.692  31.249 1.00 54.17  ? 413 SER   A O   1 
ATOM   864  C  CB  . SER   A 1 117 ? -29.047 -11.788 30.902 1.00 61.62  ? 413 SER   A CB  1 
ATOM   865  O  OG  . SER   A 1 117 ? -27.700 -12.208 30.897 1.00 61.98  ? 413 SER   A OG  1 
ATOM   866  N  N   . ARG   A 1 118 ? -27.465 -9.018  29.750 1.00 39.40  ? 414 ARG   A N   1 
ATOM   867  C  CA  . ARG   A 1 118 ? -26.769 -7.794  30.125 1.00 34.21  ? 414 ARG   A CA  1 
ATOM   868  C  C   . ARG   A 1 118 ? -27.269 -6.543  29.401 1.00 46.76  ? 414 ARG   A C   1 
ATOM   869  O  O   . ARG   A 1 118 ? -26.713 -5.467  29.633 1.00 40.09  ? 414 ARG   A O   1 
ATOM   870  C  CB  . ARG   A 1 118 ? -25.269 -7.959  29.890 1.00 43.14  ? 414 ARG   A CB  1 
ATOM   871  C  CG  . ARG   A 1 118 ? -24.653 -9.070  30.722 1.00 50.64  ? 414 ARG   A CG  1 
ATOM   872  C  CD  . ARG   A 1 118 ? -23.144 -9.144  30.528 1.00 52.73  ? 414 ARG   A CD  1 
ATOM   873  N  NE  . ARG   A 1 118 ? -22.523 -9.871  31.629 1.00 48.47  ? 414 ARG   A NE  1 
ATOM   874  C  CZ  . ARG   A 1 118 ? -21.248 -10.246 31.657 1.00 57.44  ? 414 ARG   A CZ  1 
ATOM   875  N  NH1 . ARG   A 1 118 ? -20.455 -9.985  30.627 1.00 56.54  ? 414 ARG   A NH1 1 
ATOM   876  N  NH2 . ARG   A 1 118 ? -20.771 -10.892 32.715 1.00 61.62  ? 414 ARG   A NH2 1 
ATOM   877  N  N   . CYS   A 1 119 ? -28.317 -6.638  28.563 1.00 49.90  ? 415 CYS   A N   1 
ATOM   878  C  CA  . CYS   A 1 119 ? -28.800 -5.508  27.760 1.00 51.41  ? 415 CYS   A CA  1 
ATOM   879  C  C   . CYS   A 1 119 ? -30.023 -4.864  28.408 1.00 44.03  ? 415 CYS   A C   1 
ATOM   880  O  O   . CYS   A 1 119 ? -31.084 -5.488  28.507 1.00 52.58  ? 415 CYS   A O   1 
ATOM   881  C  CB  . CYS   A 1 119 ? -29.143 -5.955  26.336 1.00 48.25  ? 415 CYS   A CB  1 
ATOM   882  S  SG  . CYS   A 1 119 ? -29.855 -4.639  25.281 1.00 51.46  ? 415 CYS   A SG  1 
ATOM   883  N  N   . VAL   A 1 120 ? -29.894 -3.589  28.788 1.00 46.83  ? 416 VAL   A N   1 
ATOM   884  C  CA  . VAL   A 1 120 ? -31.019 -2.866  29.381 1.00 50.78  ? 416 VAL   A CA  1 
ATOM   885  C  C   . VAL   A 1 120 ? -32.021 -2.411  28.325 1.00 50.93  ? 416 VAL   A C   1 
ATOM   886  O  O   . VAL   A 1 120 ? -33.192 -2.164  28.647 1.00 49.50  ? 416 VAL   A O   1 
ATOM   887  C  CB  . VAL   A 1 120 ? -30.519 -1.667  30.217 1.00 54.49  ? 416 VAL   A CB  1 
ATOM   888  C  CG1 . VAL   A 1 120 ? -29.810 -0.628  29.359 1.00 55.95  ? 416 VAL   A CG1 1 
ATOM   889  C  CG2 . VAL   A 1 120 ? -31.674 -1.022  31.025 1.00 50.31  ? 416 VAL   A CG2 1 
ATOM   890  N  N   . GLY   A 1 121 ? -31.611 -2.346  27.058 1.00 56.21  ? 417 GLY   A N   1 
ATOM   891  C  CA  . GLY   A 1 121 ? -32.462 -1.790  26.026 1.00 46.64  ? 417 GLY   A CA  1 
ATOM   892  C  C   . GLY   A 1 121 ? -33.392 -2.769  25.343 1.00 50.73  ? 417 GLY   A C   1 
ATOM   893  O  O   . GLY   A 1 121 ? -33.991 -2.415  24.330 1.00 65.34  ? 417 GLY   A O   1 
ATOM   894  N  N   . ARG   A 1 122 ? -33.555 -3.976  25.886 1.00 48.85  ? 418 ARG   A N   1 
ATOM   895  C  CA  . ARG   A 1 122 ? -34.188 -5.072  25.150 1.00 49.75  ? 418 ARG   A CA  1 
ATOM   896  C  C   . ARG   A 1 122 ? -35.658 -4.845  24.839 1.00 56.41  ? 418 ARG   A C   1 
ATOM   897  O  O   . ARG   A 1 122 ? -36.241 -5.653  24.102 1.00 57.66  ? 418 ARG   A O   1 
ATOM   898  C  CB  . ARG   A 1 122 ? -34.048 -6.381  25.927 1.00 45.79  ? 418 ARG   A CB  1 
ATOM   899  C  CG  . ARG   A 1 122 ? -32.657 -6.969  25.832 1.00 47.51  ? 418 ARG   A CG  1 
ATOM   900  C  CD  . ARG   A 1 122 ? -32.584 -8.257  26.570 1.00 55.40  ? 418 ARG   A CD  1 
ATOM   901  N  NE  . ARG   A 1 122 ? -32.379 -8.038  27.995 1.00 52.65  ? 418 ARG   A NE  1 
ATOM   902  C  CZ  . ARG   A 1 122 ? -32.510 -9.001  28.900 1.00 53.50  ? 418 ARG   A CZ  1 
ATOM   903  N  NH1 . ARG   A 1 122 ? -32.869 -10.213 28.503 1.00 33.08  ? 418 ARG   A NH1 1 
ATOM   904  N  NH2 . ARG   A 1 122 ? -32.302 -8.762  30.194 1.00 60.80  ? 418 ARG   A NH2 1 
ATOM   905  N  N   . ILE   A 1 123 ? -36.280 -3.791  25.369 1.00 54.09  ? 419 ILE   A N   1 
ATOM   906  C  CA  . ILE   A 1 123 ? -37.692 -3.558  25.110 1.00 54.20  ? 419 ILE   A CA  1 
ATOM   907  C  C   . ILE   A 1 123 ? -37.962 -3.431  23.605 1.00 69.22  ? 419 ILE   A C   1 
ATOM   908  O  O   . ILE   A 1 123 ? -39.103 -3.602  23.158 1.00 64.73  ? 419 ILE   A O   1 
ATOM   909  C  CB  . ILE   A 1 123 ? -38.140 -2.304  25.876 1.00 62.08  ? 419 ILE   A CB  1 
ATOM   910  C  CG1 . ILE   A 1 123 ? -39.668 -2.253  26.010 1.00 68.61  ? 419 ILE   A CG1 1 
ATOM   911  C  CG2 . ILE   A 1 123 ? -37.547 -1.063  25.210 1.00 56.95  ? 419 ILE   A CG2 1 
ATOM   912  C  CD1 . ILE   A 1 123 ? -40.231 -0.847  26.101 1.00 70.95  ? 419 ILE   A CD1 1 
ATOM   913  N  N   . GLN   A 1 124 ? -36.921 -3.161  22.816 1.00 68.72  ? 420 GLN   A N   1 
ATOM   914  C  CA  . GLN   A 1 124 ? -37.003 -2.980  21.373 1.00 73.07  ? 420 GLN   A CA  1 
ATOM   915  C  C   . GLN   A 1 124 ? -36.614 -4.231  20.590 1.00 64.33  ? 420 GLN   A C   1 
ATOM   916  O  O   . GLN   A 1 124 ? -36.432 -4.151  19.366 1.00 62.61  ? 420 GLN   A O   1 
ATOM   917  C  CB  . GLN   A 1 124 ? -36.100 -1.818  20.948 1.00 82.33  ? 420 GLN   A CB  1 
ATOM   918  C  CG  . GLN   A 1 124 ? -36.526 -0.457  21.455 1.00 92.01  ? 420 GLN   A CG  1 
ATOM   919  C  CD  . GLN   A 1 124 ? -37.134 0.393   20.356 1.00 100.83 ? 420 GLN   A CD  1 
ATOM   920  O  OE1 . GLN   A 1 124 ? -37.154 -0.006  19.191 1.00 98.06  ? 420 GLN   A OE1 1 
ATOM   921  N  NE2 . GLN   A 1 124 ? -37.638 1.567   20.720 1.00 106.54 ? 420 GLN   A NE2 1 
ATOM   922  N  N   . TRP   A 1 125 ? -36.496 -5.383  21.259 1.00 57.97  ? 421 TRP   A N   1 
ATOM   923  C  CA  . TRP   A 1 125 ? -35.874 -6.556  20.642 1.00 52.05  ? 421 TRP   A CA  1 
ATOM   924  C  C   . TRP   A 1 125 ? -36.581 -6.987  19.364 1.00 55.55  ? 421 TRP   A C   1 
ATOM   925  O  O   . TRP   A 1 125 ? -35.932 -7.505  18.450 1.00 65.99  ? 421 TRP   A O   1 
ATOM   926  C  CB  . TRP   A 1 125 ? -35.842 -7.727  21.629 1.00 46.61  ? 421 TRP   A CB  1 
ATOM   927  C  CG  . TRP   A 1 125 ? -37.181 -8.333  21.833 1.00 54.83  ? 421 TRP   A CG  1 
ATOM   928  C  CD1 . TRP   A 1 125 ? -38.122 -7.969  22.763 1.00 58.56  ? 421 TRP   A CD1 1 
ATOM   929  C  CD2 . TRP   A 1 125 ? -37.753 -9.408  21.085 1.00 55.15  ? 421 TRP   A CD2 1 
ATOM   930  N  NE1 . TRP   A 1 125 ? -39.241 -8.755  22.637 1.00 66.32  ? 421 TRP   A NE1 1 
ATOM   931  C  CE2 . TRP   A 1 125 ? -39.040 -9.644  21.609 1.00 62.39  ? 421 TRP   A CE2 1 
ATOM   932  C  CE3 . TRP   A 1 125 ? -37.306 -10.186 20.011 1.00 43.25  ? 421 TRP   A CE3 1 
ATOM   933  C  CZ2 . TRP   A 1 125 ? -39.878 -10.633 21.105 1.00 66.25  ? 421 TRP   A CZ2 1 
ATOM   934  C  CZ3 . TRP   A 1 125 ? -38.143 -11.181 19.516 1.00 51.71  ? 421 TRP   A CZ3 1 
ATOM   935  C  CH2 . TRP   A 1 125 ? -39.414 -11.388 20.054 1.00 59.82  ? 421 TRP   A CH2 1 
ATOM   936  N  N   . SER   A 1 126 ? -37.899 -6.803  19.280 1.00 55.92  ? 422 SER   A N   1 
ATOM   937  C  CA  . SER   A 1 126 ? -38.617 -7.203  18.068 1.00 64.67  ? 422 SER   A CA  1 
ATOM   938  C  C   . SER   A 1 126 ? -38.495 -6.200  16.922 1.00 69.63  ? 422 SER   A C   1 
ATOM   939  O  O   . SER   A 1 126 ? -38.848 -6.539  15.789 1.00 80.20  ? 422 SER   A O   1 
ATOM   940  C  CB  . SER   A 1 126 ? -40.100 -7.426  18.376 1.00 70.88  ? 422 SER   A CB  1 
ATOM   941  O  OG  . SER   A 1 126 ? -40.794 -6.193  18.506 1.00 69.14  ? 422 SER   A OG  1 
ATOM   942  N  N   . LYS   A 1 127 ? -38.045 -4.973  17.183 1.00 72.69  ? 423 LYS   A N   1 
ATOM   943  C  CA  . LYS   A 1 127 ? -37.829 -3.958  16.143 1.00 70.27  ? 423 LYS   A CA  1 
ATOM   944  C  C   . LYS   A 1 127 ? -36.343 -3.993  15.803 1.00 70.21  ? 423 LYS   A C   1 
ATOM   945  O  O   . LYS   A 1 127 ? -35.537 -3.237  16.350 1.00 56.97  ? 423 LYS   A O   1 
ATOM   946  C  CB  . LYS   A 1 127 ? -38.268 -2.572  16.609 1.00 73.63  ? 423 LYS   A CB  1 
ATOM   947  C  CG  . LYS   A 1 127 ? -39.593 -2.086  16.051 1.00 85.30  ? 423 LYS   A CG  1 
ATOM   948  C  CD  . LYS   A 1 127 ? -39.425 -0.752  15.298 1.00 88.13  ? 423 LYS   A CD  1 
ATOM   949  C  CE  . LYS   A 1 127 ? -40.707 -0.351  14.585 1.00 98.23  ? 423 LYS   A CE  1 
ATOM   950  N  NZ  . LYS   A 1 127 ? -40.497 0.764   13.604 1.00 110.29 ? 423 LYS   A NZ  1 
ATOM   951  N  N   . LEU   A 1 128 ? -35.977 -4.898  14.903 1.00 64.67  ? 424 LEU   A N   1 
ATOM   952  C  CA  . LEU   A 1 128 ? -34.579 -5.133  14.583 1.00 56.05  ? 424 LEU   A CA  1 
ATOM   953  C  C   . LEU   A 1 128 ? -34.483 -5.457  13.107 1.00 52.49  ? 424 LEU   A C   1 
ATOM   954  O  O   . LEU   A 1 128 ? -35.206 -6.327  12.613 1.00 60.62  ? 424 LEU   A O   1 
ATOM   955  C  CB  . LEU   A 1 128 ? -33.997 -6.284  15.404 1.00 38.50  ? 424 LEU   A CB  1 
ATOM   956  C  CG  . LEU   A 1 128 ? -32.561 -6.722  15.086 1.00 43.27  ? 424 LEU   A CG  1 
ATOM   957  C  CD1 . LEU   A 1 128 ? -31.543 -5.706  15.556 1.00 40.88  ? 424 LEU   A CD1 1 
ATOM   958  C  CD2 . LEU   A 1 128 ? -32.273 -8.094  15.704 1.00 33.03  ? 424 LEU   A CD2 1 
ATOM   959  N  N   . GLN   A 1 129 ? -33.591 -4.763  12.415 1.00 63.86  ? 425 GLN   A N   1 
ATOM   960  C  CA  . GLN   A 1 129 ? -33.405 -4.921  10.977 1.00 60.79  ? 425 GLN   A CA  1 
ATOM   961  C  C   . GLN   A 1 129 ? -32.243 -5.877  10.757 1.00 62.04  ? 425 GLN   A C   1 
ATOM   962  O  O   . GLN   A 1 129 ? -31.120 -5.610  11.199 1.00 65.16  ? 425 GLN   A O   1 
ATOM   963  C  CB  . GLN   A 1 129 ? -33.131 -3.570  10.326 1.00 63.06  ? 425 GLN   A CB  1 
ATOM   964  C  CG  . GLN   A 1 129 ? -32.884 -3.636  8.834  1.00 60.83  ? 425 GLN   A CG  1 
ATOM   965  C  CD  . GLN   A 1 129 ? -34.051 -4.227  8.078  1.00 69.85  ? 425 GLN   A CD  1 
ATOM   966  O  OE1 . GLN   A 1 129 ? -35.206 -4.093  8.489  1.00 70.34  ? 425 GLN   A OE1 1 
ATOM   967  N  NE2 . GLN   A 1 129 ? -33.755 -4.896  6.965  1.00 75.30  ? 425 GLN   A NE2 1 
ATOM   968  N  N   . VAL   A 1 130 ? -32.508 -7.001  10.110 1.00 60.41  ? 426 VAL   A N   1 
ATOM   969  C  CA  . VAL   A 1 130 ? -31.483 -8.013  9.883  1.00 51.05  ? 426 VAL   A CA  1 
ATOM   970  C  C   . VAL   A 1 130 ? -30.993 -7.873  8.446  1.00 55.60  ? 426 VAL   A C   1 
ATOM   971  O  O   . VAL   A 1 130 ? -31.764 -8.055  7.508  1.00 47.81  ? 426 VAL   A O   1 
ATOM   972  C  CB  . VAL   A 1 130 ? -32.018 -9.432  10.142 1.00 57.79  ? 426 VAL   A CB  1 
ATOM   973  C  CG1 . VAL   A 1 130 ? -30.904 -10.475 9.907  1.00 51.25  ? 426 VAL   A CG1 1 
ATOM   974  C  CG2 . VAL   A 1 130 ? -32.589 -9.546  11.546 1.00 58.05  ? 426 VAL   A CG2 1 
ATOM   975  N  N   . PHE   A 1 131 ? -29.716 -7.567  8.267  1.00 54.87  ? 427 PHE   A N   1 
ATOM   976  C  CA  . PHE   A 1 131 ? -29.095 -7.575  6.956  1.00 56.47  ? 427 PHE   A CA  1 
ATOM   977  C  C   . PHE   A 1 131 ? -28.355 -8.897  6.784  1.00 54.50  ? 427 PHE   A C   1 
ATOM   978  O  O   . PHE   A 1 131 ? -27.403 -9.185  7.516  1.00 46.59  ? 427 PHE   A O   1 
ATOM   979  C  CB  . PHE   A 1 131 ? -28.170 -6.368  6.783  1.00 44.76  ? 427 PHE   A CB  1 
ATOM   980  C  CG  . PHE   A 1 131 ? -28.899 -5.046  6.780  1.00 47.84  ? 427 PHE   A CG  1 
ATOM   981  C  CD1 . PHE   A 1 131 ? -29.849 -4.750  5.824  1.00 50.52  ? 427 PHE   A CD1 1 
ATOM   982  C  CD2 . PHE   A 1 131 ? -28.661 -4.119  7.778  1.00 55.69  ? 427 PHE   A CD2 1 
ATOM   983  C  CE1 . PHE   A 1 131 ? -30.520 -3.538  5.831  1.00 52.87  ? 427 PHE   A CE1 1 
ATOM   984  C  CE2 . PHE   A 1 131 ? -29.328 -2.911  7.791  1.00 58.25  ? 427 PHE   A CE2 1 
ATOM   985  C  CZ  . PHE   A 1 131 ? -30.251 -2.614  6.809  1.00 58.68  ? 427 PHE   A CZ  1 
ATOM   986  N  N   . ASP   A 1 132 ? -28.815 -9.704  5.829  1.00 58.32  ? 428 ASP   A N   1 
ATOM   987  C  CA  . ASP   A 1 132 ? -28.223 -11.003 5.508  1.00 50.11  ? 428 ASP   A CA  1 
ATOM   988  C  C   . ASP   A 1 132 ? -27.028 -10.780 4.593  1.00 54.81  ? 428 ASP   A C   1 
ATOM   989  O  O   . ASP   A 1 132 ? -27.192 -10.495 3.399  1.00 61.29  ? 428 ASP   A O   1 
ATOM   990  C  CB  . ASP   A 1 132 ? -29.242 -11.922 4.834  1.00 51.33  ? 428 ASP   A CB  1 
ATOM   991  C  CG  . ASP   A 1 132 ? -28.658 -13.290 4.471  1.00 53.44  ? 428 ASP   A CG  1 
ATOM   992  O  OD1 . ASP   A 1 132 ? -29.430 -14.142 3.976  1.00 47.33  ? 428 ASP   A OD1 1 
ATOM   993  O  OD2 . ASP   A 1 132 ? -27.447 -13.535 4.688  1.00 51.39  ? 428 ASP   A OD2 1 
ATOM   994  N  N   . ALA   A 1 133 ? -25.827 -10.934 5.143  1.00 56.45  ? 429 ALA   A N   1 
ATOM   995  C  CA  . ALA   A 1 133 ? -24.606 -10.830 4.360  1.00 54.25  ? 429 ALA   A CA  1 
ATOM   996  C  C   . ALA   A 1 133 ? -23.952 -12.184 4.146  1.00 52.84  ? 429 ALA   A C   1 
ATOM   997  O  O   . ALA   A 1 133 ? -22.740 -12.255 3.935  1.00 59.01  ? 429 ALA   A O   1 
ATOM   998  C  CB  . ALA   A 1 133 ? -23.637 -9.866  5.044  1.00 51.43  ? 429 ALA   A CB  1 
ATOM   999  N  N   . ARG   A 1 134 ? -24.725 -13.265 4.223  1.00 50.98  ? 430 ARG   A N   1 
ATOM   1000 C  CA  . ARG   A 1 134 ? -24.150 -14.595 4.031  1.00 55.04  ? 430 ARG   A CA  1 
ATOM   1001 C  C   . ARG   A 1 134 ? -23.719 -14.880 2.583  1.00 57.86  ? 430 ARG   A C   1 
ATOM   1002 O  O   . ARG   A 1 134 ? -23.150 -15.958 2.341  1.00 57.12  ? 430 ARG   A O   1 
ATOM   1003 C  CB  . ARG   A 1 134 ? -25.138 -15.659 4.521  1.00 52.61  ? 430 ARG   A CB  1 
ATOM   1004 C  CG  . ARG   A 1 134 ? -25.369 -15.626 6.074  1.00 56.94  ? 430 ARG   A CG  1 
ATOM   1005 C  CD  . ARG   A 1 134 ? -26.470 -16.595 6.523  1.00 58.31  ? 430 ARG   A CD  1 
ATOM   1006 N  NE  . ARG   A 1 134 ? -27.774 -16.267 5.963  1.00 63.12  ? 430 ARG   A NE  1 
ATOM   1007 C  CZ  . ARG   A 1 134 ? -28.796 -17.114 5.880  1.00 63.62  ? 430 ARG   A CZ  1 
ATOM   1008 N  NH1 . ARG   A 1 134 ? -28.677 -18.356 6.326  1.00 66.09  ? 430 ARG   A NH1 1 
ATOM   1009 N  NH2 . ARG   A 1 134 ? -29.939 -16.723 5.318  1.00 60.23  ? 430 ARG   A NH2 1 
ATOM   1010 N  N   . ASP   A 1 135 ? -23.940 -13.962 1.625  1.00 52.46  ? 431 ASP   A N   1 
ATOM   1011 C  CA  . ASP   A 1 135 ? -23.395 -14.135 0.277  1.00 59.32  ? 431 ASP   A CA  1 
ATOM   1012 C  C   . ASP   A 1 135 ? -22.035 -13.465 0.111  1.00 61.13  ? 431 ASP   A C   1 
ATOM   1013 O  O   . ASP   A 1 135 ? -21.433 -13.563 -0.963 1.00 64.53  ? 431 ASP   A O   1 
ATOM   1014 C  CB  . ASP   A 1 135 ? -24.385 -13.619 -0.804 1.00 59.88  ? 431 ASP   A CB  1 
ATOM   1015 C  CG  . ASP   A 1 135 ? -24.694 -12.104 -0.703 1.00 66.21  ? 431 ASP   A CG  1 
ATOM   1016 O  OD1 . ASP   A 1 135 ? -25.537 -11.626 -1.499 1.00 65.22  ? 431 ASP   A OD1 1 
ATOM   1017 O  OD2 . ASP   A 1 135 ? -24.112 -11.382 0.138  1.00 69.23  ? 431 ASP   A OD2 1 
ATOM   1018 N  N   . CYS   A 1 136 ? -21.534 -12.820 1.161  1.00 59.96  ? 432 CYS   A N   1 
ATOM   1019 C  CA  . CYS   A 1 136 ? -20.279 -12.081 1.121  1.00 65.31  ? 432 CYS   A CA  1 
ATOM   1020 C  C   . CYS   A 1 136 ? -19.106 -13.039 0.964  1.00 69.38  ? 432 CYS   A C   1 
ATOM   1021 O  O   . CYS   A 1 136 ? -19.123 -14.162 1.480  1.00 71.17  ? 432 CYS   A O   1 
ATOM   1022 C  CB  . CYS   A 1 136 ? -20.118 -11.257 2.404  1.00 59.39  ? 432 CYS   A CB  1 
ATOM   1023 S  SG  . CYS   A 1 136 ? -18.820 -10.005 2.405  1.00 63.13  ? 432 CYS   A SG  1 
ATOM   1024 N  N   . THR   A 1 137 ? -18.079 -12.593 0.230  1.00 68.62  ? 433 THR   A N   1 
ATOM   1025 C  CA  . THR   A 1 137 ? -16.911 -13.432 -0.032 1.00 62.65  ? 433 THR   A CA  1 
ATOM   1026 C  C   . THR   A 1 137 ? -15.561 -12.744 0.174  1.00 66.47  ? 433 THR   A C   1 
ATOM   1027 O  O   . THR   A 1 137 ? -14.535 -13.438 0.160  1.00 70.86  ? 433 THR   A O   1 
ATOM   1028 C  CB  . THR   A 1 137 ? -16.948 -13.981 -1.471 1.00 67.09  ? 433 THR   A CB  1 
ATOM   1029 O  OG1 . THR   A 1 137 ? -16.890 -12.891 -2.396 1.00 63.48  ? 433 THR   A OG1 1 
ATOM   1030 C  CG2 . THR   A 1 137 ? -18.218 -14.790 -1.734 1.00 61.26  ? 433 THR   A CG2 1 
ATOM   1031 N  N   . THR   A 1 138 ? -15.519 -11.421 0.350  1.00 63.83  ? 434 THR   A N   1 
ATOM   1032 C  CA  . THR   A 1 138 ? -14.265 -10.675 0.410  1.00 68.10  ? 434 THR   A CA  1 
ATOM   1033 C  C   . THR   A 1 138 ? -14.349 -9.635  1.518  1.00 58.26  ? 434 THR   A C   1 
ATOM   1034 O  O   . THR   A 1 138 ? -15.433 -9.221  1.931  1.00 65.27  ? 434 THR   A O   1 
ATOM   1035 C  CB  . THR   A 1 138 ? -13.932 -9.959  -0.921 1.00 79.25  ? 434 THR   A CB  1 
ATOM   1036 O  OG1 . THR   A 1 138 ? -15.047 -9.162  -1.347 1.00 83.69  ? 434 THR   A OG1 1 
ATOM   1037 C  CG2 . THR   A 1 138 ? -13.542 -10.950 -2.032 1.00 78.13  ? 434 THR   A CG2 1 
ATOM   1038 N  N   . ALA   A 1 139 ? -13.177 -9.197  1.979  1.00 64.01  ? 435 ALA   A N   1 
ATOM   1039 C  CA  . ALA   A 1 139 ? -13.131 -8.083  2.914  1.00 69.65  ? 435 ALA   A CA  1 
ATOM   1040 C  C   . ALA   A 1 139 ? -13.752 -6.830  2.307  1.00 77.11  ? 435 ALA   A C   1 
ATOM   1041 O  O   . ALA   A 1 139 ? -14.402 -6.050  3.014  1.00 78.79  ? 435 ALA   A O   1 
ATOM   1042 C  CB  . ALA   A 1 139 ? -11.687 -7.818  3.336  1.00 72.96  ? 435 ALA   A CB  1 
ATOM   1043 N  N   . HIS   A 1 140 ? -13.567 -6.622  0.995  1.00 82.80  ? 436 HIS   A N   1 
ATOM   1044 C  CA  . HIS   A 1 140 ? -14.176 -5.475  0.325  1.00 73.18  ? 436 HIS   A CA  1 
ATOM   1045 C  C   . HIS   A 1 140 ? -15.689 -5.550  0.370  1.00 63.05  ? 436 HIS   A C   1 
ATOM   1046 O  O   . HIS   A 1 140 ? -16.364 -4.533  0.562  1.00 65.81  ? 436 HIS   A O   1 
ATOM   1047 C  CB  . HIS   A 1 140 ? -13.721 -5.399  -1.124 1.00 74.19  ? 436 HIS   A CB  1 
ATOM   1048 C  CG  . HIS   A 1 140 ? -12.394 -4.746  -1.306 1.00 78.73  ? 436 HIS   A CG  1 
ATOM   1049 N  ND1 . HIS   A 1 140 ? -11.238 -5.251  -0.751 1.00 81.98  ? 436 HIS   A ND1 1 
ATOM   1050 C  CD2 . HIS   A 1 140 ? -12.033 -3.633  -1.989 1.00 81.39  ? 436 HIS   A CD2 1 
ATOM   1051 C  CE1 . HIS   A 1 140 ? -10.221 -4.475  -1.085 1.00 87.74  ? 436 HIS   A CE1 1 
ATOM   1052 N  NE2 . HIS   A 1 140 ? -10.677 -3.488  -1.838 1.00 85.57  ? 436 HIS   A NE2 1 
ATOM   1053 N  N   . GLY   A 1 141 ? -16.241 -6.737  0.135  1.00 59.00  ? 437 GLY   A N   1 
ATOM   1054 C  CA  . GLY   A 1 141 ? -17.672 -6.911  0.283  1.00 64.81  ? 437 GLY   A CA  1 
ATOM   1055 C  C   . GLY   A 1 141 ? -18.133 -6.723  1.707  1.00 63.26  ? 437 GLY   A C   1 
ATOM   1056 O  O   . GLY   A 1 141 ? -19.264 -6.296  1.942  1.00 71.17  ? 437 GLY   A O   1 
ATOM   1057 N  N   . MET   A 1 142 ? -17.270 -7.044  2.676  1.00 70.38  ? 438 MET   A N   1 
ATOM   1058 C  CA  . MET   A 1 142 ? -17.582 -6.755  4.074  1.00 55.26  ? 438 MET   A CA  1 
ATOM   1059 C  C   . MET   A 1 142 ? -17.665 -5.251  4.307  1.00 54.16  ? 438 MET   A C   1 
ATOM   1060 O  O   . MET   A 1 142 ? -18.630 -4.755  4.896  1.00 63.81  ? 438 MET   A O   1 
ATOM   1061 C  CB  . MET   A 1 142 ? -16.537 -7.394  4.999  1.00 53.81  ? 438 MET   A CB  1 
ATOM   1062 C  CG  . MET   A 1 142 ? -16.750 -8.869  5.250  1.00 55.62  ? 438 MET   A CG  1 
ATOM   1063 S  SD  . MET   A 1 142 ? -15.373 -9.672  6.104  1.00 61.36  ? 438 MET   A SD  1 
ATOM   1064 C  CE  . MET   A 1 142 ? -15.792 -9.318  7.799  1.00 61.36  ? 438 MET   A CE  1 
ATOM   1065 N  N   . PHE   A 1 143 ? -16.662 -4.509  3.836  1.00 55.48  ? 439 PHE   A N   1 
ATOM   1066 C  CA  . PHE   A 1 143 ? -16.686 -3.053  3.944  1.00 53.50  ? 439 PHE   A CA  1 
ATOM   1067 C  C   . PHE   A 1 143 ? -17.995 -2.489  3.409  1.00 61.67  ? 439 PHE   A C   1 
ATOM   1068 O  O   . PHE   A 1 143 ? -18.667 -1.692  4.074  1.00 59.45  ? 439 PHE   A O   1 
ATOM   1069 C  CB  . PHE   A 1 143 ? -15.485 -2.474  3.193  1.00 63.32  ? 439 PHE   A CB  1 
ATOM   1070 C  CG  . PHE   A 1 143 ? -15.417 -0.979  3.215  1.00 74.03  ? 439 PHE   A CG  1 
ATOM   1071 C  CD1 . PHE   A 1 143 ? -15.245 -0.259  2.039  1.00 81.67  ? 439 PHE   A CD1 1 
ATOM   1072 C  CD2 . PHE   A 1 143 ? -15.536 -0.291  4.415  1.00 71.43  ? 439 PHE   A CD2 1 
ATOM   1073 C  CE1 . PHE   A 1 143 ? -15.179 1.125   2.064  1.00 86.77  ? 439 PHE   A CE1 1 
ATOM   1074 C  CE2 . PHE   A 1 143 ? -15.471 1.084   4.444  1.00 75.87  ? 439 PHE   A CE2 1 
ATOM   1075 C  CZ  . PHE   A 1 143 ? -15.297 1.796   3.267  1.00 78.74  ? 439 PHE   A CZ  1 
ATOM   1076 N  N   . ASN   A 1 144 ? -18.390 -2.937  2.214  1.00 60.79  ? 440 ASN   A N   1 
ATOM   1077 C  CA  . ASN   A 1 144 ? -19.622 -2.463  1.603  1.00 60.95  ? 440 ASN   A CA  1 
ATOM   1078 C  C   . ASN   A 1 144 ? -20.836 -2.796  2.458  1.00 62.96  ? 440 ASN   A C   1 
ATOM   1079 O  O   . ASN   A 1 144 ? -21.710 -1.950  2.668  1.00 77.08  ? 440 ASN   A O   1 
ATOM   1080 C  CB  . ASN   A 1 144 ? -19.780 -3.080  0.219  1.00 61.22  ? 440 ASN   A CB  1 
ATOM   1081 C  CG  . ASN   A 1 144 ? -20.839 -2.399  -0.567 1.00 63.39  ? 440 ASN   A CG  1 
ATOM   1082 O  OD1 . ASN   A 1 144 ? -20.754 -1.195  -0.775 1.00 57.95  ? 440 ASN   A OD1 1 
ATOM   1083 N  ND2 . ASN   A 1 144 ? -21.870 -3.139  -0.969 1.00 62.43  ? 440 ASN   A ND2 1 
ATOM   1084 N  N   . TYR   A 1 145 ? -20.921 -4.038  2.939  1.00 59.39  ? 441 TYR   A N   1 
ATOM   1085 C  CA  . TYR   A 1 145 ? -22.051 -4.420  3.778  1.00 60.49  ? 441 TYR   A CA  1 
ATOM   1086 C  C   . TYR   A 1 145 ? -22.063 -3.625  5.078  1.00 57.61  ? 441 TYR   A C   1 
ATOM   1087 O  O   . TYR   A 1 145 ? -23.132 -3.241  5.573  1.00 65.44  ? 441 TYR   A O   1 
ATOM   1088 C  CB  . TYR   A 1 145 ? -22.003 -5.920  4.058  1.00 55.32  ? 441 TYR   A CB  1 
ATOM   1089 C  CG  . TYR   A 1 145 ? -22.863 -6.782  3.152  1.00 50.42  ? 441 TYR   A CG  1 
ATOM   1090 C  CD1 . TYR   A 1 145 ? -22.291 -7.787  2.377  1.00 45.07  ? 441 TYR   A CD1 1 
ATOM   1091 C  CD2 . TYR   A 1 145 ? -24.242 -6.623  3.107  1.00 51.63  ? 441 TYR   A CD2 1 
ATOM   1092 C  CE1 . TYR   A 1 145 ? -23.068 -8.592  1.552  1.00 51.06  ? 441 TYR   A CE1 1 
ATOM   1093 C  CE2 . TYR   A 1 145 ? -25.027 -7.422  2.296  1.00 52.80  ? 441 TYR   A CE2 1 
ATOM   1094 C  CZ  . TYR   A 1 145 ? -24.434 -8.409  1.522  1.00 58.67  ? 441 TYR   A CZ  1 
ATOM   1095 O  OH  . TYR   A 1 145 ? -25.223 -9.212  0.712  1.00 65.24  ? 441 TYR   A OH  1 
ATOM   1096 N  N   . ILE   A 1 146 ? -20.882 -3.359  5.644  1.00 60.69  ? 442 ILE   A N   1 
ATOM   1097 C  CA  . ILE   A 1 146 ? -20.806 -2.599  6.890  1.00 51.81  ? 442 ILE   A CA  1 
ATOM   1098 C  C   . ILE   A 1 146 ? -21.203 -1.148  6.651  1.00 62.09  ? 442 ILE   A C   1 
ATOM   1099 O  O   . ILE   A 1 146 ? -21.855 -0.528  7.496  1.00 62.57  ? 442 ILE   A O   1 
ATOM   1100 C  CB  . ILE   A 1 146 ? -19.394 -2.707  7.498  1.00 52.24  ? 442 ILE   A CB  1 
ATOM   1101 C  CG1 . ILE   A 1 146 ? -19.064 -4.160  7.850  1.00 49.72  ? 442 ILE   A CG1 1 
ATOM   1102 C  CG2 . ILE   A 1 146 ? -19.245 -1.802  8.706  1.00 57.27  ? 442 ILE   A CG2 1 
ATOM   1103 C  CD1 . ILE   A 1 146 ? -18.052 -4.297  8.962  1.00 52.82  ? 442 ILE   A CD1 1 
ATOM   1104 N  N   . CYS   A 1 147 ? -20.861 -0.600  5.476  1.00 67.19  ? 443 CYS   A N   1 
ATOM   1105 C  CA  . CYS   A 1 147 ? -21.135 0.809   5.204  1.00 61.50  ? 443 CYS   A CA  1 
ATOM   1106 C  C   . CYS   A 1 147 ? -22.634 1.070   5.143  1.00 58.77  ? 443 CYS   A C   1 
ATOM   1107 O  O   . CYS   A 1 147 ? -23.137 2.020   5.752  1.00 59.85  ? 443 CYS   A O   1 
ATOM   1108 C  CB  . CYS   A 1 147 ? -20.474 1.239   3.889  1.00 66.80  ? 443 CYS   A CB  1 
ATOM   1109 S  SG  . CYS   A 1 147 ? -18.794 1.878   4.002  1.00 70.02  ? 443 CYS   A SG  1 
ATOM   1110 N  N   . ASN   A 1 148 ? -23.364 0.227   4.413  1.00 49.91  ? 444 ASN   A N   1 
ATOM   1111 C  CA  . ASN   A 1 148 ? -24.810 0.379   4.315  1.00 56.53  ? 444 ASN   A CA  1 
ATOM   1112 C  C   . ASN   A 1 148 ? -25.478 0.123   5.650  1.00 56.00  ? 444 ASN   A C   1 
ATOM   1113 O  O   . ASN   A 1 148 ? -26.565 0.650   5.909  1.00 59.02  ? 444 ASN   A O   1 
ATOM   1114 C  CB  . ASN   A 1 148 ? -25.383 -0.580  3.269  1.00 64.53  ? 444 ASN   A CB  1 
ATOM   1115 C  CG  . ASN   A 1 148 ? -24.793 -0.378  1.882  1.00 64.47  ? 444 ASN   A CG  1 
ATOM   1116 O  OD1 . ASN   A 1 148 ? -24.280 0.695   1.544  1.00 68.05  ? 444 ASN   A OD1 1 
ATOM   1117 N  ND2 . ASN   A 1 148 ? -24.881 -1.413  1.072  1.00 52.95  ? 444 ASN   A ND2 1 
ATOM   1118 N  N   . HIS   A 1 149 ? -24.859 -0.703  6.497  1.00 52.93  ? 445 HIS   A N   1 
ATOM   1119 C  CA  . HIS   A 1 149 ? -25.368 -0.878  7.854  1.00 53.00  ? 445 HIS   A CA  1 
ATOM   1120 C  C   . HIS   A 1 149 ? -25.235 0.420   8.646  1.00 53.32  ? 445 HIS   A C   1 
ATOM   1121 O  O   . HIS   A 1 149 ? -26.217 0.912   9.216  1.00 50.99  ? 445 HIS   A O   1 
ATOM   1122 C  CB  . HIS   A 1 149 ? -24.644 -2.048  8.537  1.00 53.36  ? 445 HIS   A CB  1 
ATOM   1123 C  CG  . HIS   A 1 149 ? -24.966 -2.221  10.004 1.00 47.71  ? 445 HIS   A CG  1 
ATOM   1124 N  ND1 . HIS   A 1 149 ? -25.126 -3.462  10.584 1.00 44.77  ? 445 HIS   A ND1 1 
ATOM   1125 C  CD2 . HIS   A 1 149 ? -25.115 -1.322  11.008 1.00 50.14  ? 445 HIS   A CD2 1 
ATOM   1126 C  CE1 . HIS   A 1 149 ? -25.381 -3.319  11.877 1.00 51.13  ? 445 HIS   A CE1 1 
ATOM   1127 N  NE2 . HIS   A 1 149 ? -25.381 -2.028  12.160 1.00 48.83  ? 445 HIS   A NE2 1 
ATOM   1128 N  N   . VAL   A 1 150 ? -24.023 0.991   8.687  1.00 52.76  ? 446 VAL   A N   1 
ATOM   1129 C  CA  . VAL   A 1 150 ? -23.813 2.284   9.345  1.00 55.92  ? 446 VAL   A CA  1 
ATOM   1130 C  C   . VAL   A 1 150 ? -24.819 3.311   8.837  1.00 61.72  ? 446 VAL   A C   1 
ATOM   1131 O  O   . VAL   A 1 150 ? -25.554 3.927   9.613  1.00 65.34  ? 446 VAL   A O   1 
ATOM   1132 C  CB  . VAL   A 1 150 ? -22.372 2.780   9.121  1.00 59.28  ? 446 VAL   A CB  1 
ATOM   1133 C  CG1 . VAL   A 1 150 ? -22.229 4.244   9.559  1.00 59.20  ? 446 VAL   A CG1 1 
ATOM   1134 C  CG2 . VAL   A 1 150 ? -21.383 1.901   9.845  1.00 52.72  ? 446 VAL   A CG2 1 
ATOM   1135 N  N   . LYS   A 1 151 ? -24.879 3.493   7.517  1.00 60.62  ? 447 LYS   A N   1 
ATOM   1136 C  CA  . LYS   A 1 151 ? -25.736 4.532   6.944  1.00 66.85  ? 447 LYS   A CA  1 
ATOM   1137 C  C   . LYS   A 1 151 ? -27.202 4.289   7.279  1.00 69.00  ? 447 LYS   A C   1 
ATOM   1138 O  O   . LYS   A 1 151 ? -27.947 5.234   7.574  1.00 75.84  ? 447 LYS   A O   1 
ATOM   1139 C  CB  . LYS   A 1 151 ? -25.538 4.607   5.418  1.00 55.02  ? 447 LYS   A CB  1 
ATOM   1140 C  CG  . LYS   A 1 151 ? -26.221 5.819   4.740  1.00 58.56  ? 447 LYS   A CG  1 
ATOM   1141 C  CD  . LYS   A 1 151 ? -25.625 6.083   3.359  1.00 60.68  ? 447 LYS   A CD  1 
ATOM   1142 C  CE  . LYS   A 1 151 ? -25.959 7.489   2.800  1.00 71.89  ? 447 LYS   A CE  1 
ATOM   1143 N  NZ  . LYS   A 1 151 ? -25.694 7.617   1.325  1.00 76.45  ? 447 LYS   A NZ  1 
ATOM   1144 N  N   . TYR   A 1 152 ? -27.639 3.029   7.239  1.00 60.64  ? 448 TYR   A N   1 
ATOM   1145 C  CA  . TYR   A 1 152 ? -29.050 2.756   7.470  1.00 60.73  ? 448 TYR   A CA  1 
ATOM   1146 C  C   . TYR   A 1 152 ? -29.418 2.970   8.934  1.00 56.59  ? 448 TYR   A C   1 
ATOM   1147 O  O   . TYR   A 1 152 ? -30.455 3.578   9.235  1.00 56.53  ? 448 TYR   A O   1 
ATOM   1148 C  CB  . TYR   A 1 152 ? -29.396 1.337   7.026  1.00 52.50  ? 448 TYR   A CB  1 
ATOM   1149 C  CG  . TYR   A 1 152 ? -30.717 0.865   7.596  1.00 60.60  ? 448 TYR   A CG  1 
ATOM   1150 C  CD1 . TYR   A 1 152 ? -31.901 1.106   6.912  1.00 72.23  ? 448 TYR   A CD1 1 
ATOM   1151 C  CD2 . TYR   A 1 152 ? -30.788 0.204   8.821  1.00 55.88  ? 448 TYR   A CD2 1 
ATOM   1152 C  CE1 . TYR   A 1 152 ? -33.117 0.699   7.420  1.00 75.18  ? 448 TYR   A CE1 1 
ATOM   1153 C  CE2 . TYR   A 1 152 ? -32.008 -0.204  9.334  1.00 56.49  ? 448 TYR   A CE2 1 
ATOM   1154 C  CZ  . TYR   A 1 152 ? -33.169 0.050   8.628  1.00 63.64  ? 448 TYR   A CZ  1 
ATOM   1155 O  OH  . TYR   A 1 152 ? -34.394 -0.348  9.109  1.00 72.79  ? 448 TYR   A OH  1 
ATOM   1156 N  N   . ALA   A 1 153 ? -28.574 2.480   9.851  1.00 54.43  ? 449 ALA   A N   1 
ATOM   1157 C  CA  . ALA   A 1 153 ? -28.873 2.547   11.273 1.00 61.07  ? 449 ALA   A CA  1 
ATOM   1158 C  C   . ALA   A 1 153 ? -28.667 3.944   11.841 1.00 69.93  ? 449 ALA   A C   1 
ATOM   1159 O  O   . ALA   A 1 153 ? -29.161 4.239   12.939 1.00 74.64  ? 449 ALA   A O   1 
ATOM   1160 C  CB  . ALA   A 1 153 ? -28.001 1.545   12.035 1.00 55.76  ? 449 ALA   A CB  1 
ATOM   1161 N  N   . THR   A 1 154 ? -27.912 4.787   11.144 1.00 60.52  ? 450 THR   A N   1 
ATOM   1162 C  CA  . THR   A 1 154 ? -27.719 6.163   11.583 1.00 67.95  ? 450 THR   A CA  1 
ATOM   1163 C  C   . THR   A 1 154 ? -28.926 7.021   11.225 1.00 77.27  ? 450 THR   A C   1 
ATOM   1164 O  O   . THR   A 1 154 ? -29.405 7.802   12.053 1.00 88.92  ? 450 THR   A O   1 
ATOM   1165 C  CB  . THR   A 1 154 ? -26.440 6.727   10.970 1.00 62.14  ? 450 THR   A CB  1 
ATOM   1166 O  OG1 . THR   A 1 154 ? -25.313 6.056   11.547 1.00 70.02  ? 450 THR   A OG1 1 
ATOM   1167 C  CG2 . THR   A 1 154 ? -26.324 8.207   11.232 1.00 66.43  ? 450 THR   A CG2 1 
ATOM   1168 N  N   . ASN   A 1 155 ? -29.430 6.881   9.995  1.00 75.06  ? 451 ASN   A N   1 
ATOM   1169 C  CA  . ASN   A 1 155 ? -30.729 7.431   9.588  1.00 68.42  ? 451 ASN   A CA  1 
ATOM   1170 C  C   . ASN   A 1 155 ? -30.878 8.900   9.971  1.00 67.13  ? 451 ASN   A C   1 
ATOM   1171 O  O   . ASN   A 1 155 ? -31.913 9.330   10.488 1.00 72.52  ? 451 ASN   A O   1 
ATOM   1172 C  CB  . ASN   A 1 155 ? -31.872 6.584   10.171 1.00 70.59  ? 451 ASN   A CB  1 
ATOM   1173 C  CG  . ASN   A 1 155 ? -33.248 6.978   9.634  1.00 79.45  ? 451 ASN   A CG  1 
ATOM   1174 O  OD1 . ASN   A 1 155 ? -33.372 7.489   8.524  1.00 81.03  ? 451 ASN   A OD1 1 
ATOM   1175 N  ND2 . ASN   A 1 155 ? -34.286 6.725   10.423 1.00 83.17  ? 451 ASN   A ND2 1 
ATOM   1176 N  N   . LYS   A 1 156 ? -29.846 9.693   9.671  1.00 73.26  ? 452 LYS   A N   1 
ATOM   1177 C  CA  . LYS   A 1 156 ? -29.873 11.140  9.883  1.00 74.34  ? 452 LYS   A CA  1 
ATOM   1178 C  C   . LYS   A 1 156 ? -29.973 11.484  11.373 1.00 82.02  ? 452 LYS   A C   1 
ATOM   1179 O  O   . LYS   A 1 156 ? -30.580 12.492  11.745 1.00 86.95  ? 452 LYS   A O   1 
ATOM   1180 C  CB  . LYS   A 1 156 ? -31.023 11.821  9.125  1.00 80.64  ? 452 LYS   A CB  1 
ATOM   1181 C  CG  . LYS   A 1 156 ? -30.974 11.793  7.594  1.00 90.36  ? 452 LYS   A CG  1 
ATOM   1182 C  CD  . LYS   A 1 156 ? -32.067 12.687  7.024  1.00 91.19  ? 452 LYS   A CD  1 
ATOM   1183 C  CE  . LYS   A 1 156 ? -32.298 12.395  5.561  1.00 106.56 ? 452 LYS   A CE  1 
ATOM   1184 N  NZ  . LYS   A 1 156 ? -31.157 12.854  4.722  1.00 113.58 ? 452 LYS   A NZ  1 
ATOM   1185 N  N   . GLY   A 1 157 ? -29.401 10.635  12.226 1.00 71.67  ? 453 GLY   A N   1 
ATOM   1186 C  CA  . GLY   A 1 157 ? -29.486 10.785  13.660 1.00 75.36  ? 453 GLY   A CA  1 
ATOM   1187 C  C   . GLY   A 1 157 ? -30.684 10.111  14.287 1.00 84.53  ? 453 GLY   A C   1 
ATOM   1188 O  O   . GLY   A 1 157 ? -30.688 9.873   15.518 1.00 79.70  ? 453 GLY   A O   1 
ATOM   1189 N  N   . ASN   A 1 158 ? -31.701 9.799   13.481 1.00 78.59  ? 454 ASN   A N   1 
ATOM   1190 C  CA  . ASN   A 1 158 ? -32.875 9.079   13.962 1.00 85.18  ? 454 ASN   A CA  1 
ATOM   1191 C  C   . ASN   A 1 158 ? -32.552 7.589   13.918 1.00 86.11  ? 454 ASN   A C   1 
ATOM   1192 O  O   . ASN   A 1 158 ? -32.981 6.853   13.030 1.00 87.00  ? 454 ASN   A O   1 
ATOM   1193 C  CB  . ASN   A 1 158 ? -34.097 9.446   13.131 1.00 80.62  ? 454 ASN   A CB  1 
ATOM   1194 C  CG  . ASN   A 1 158 ? -35.347 8.717   13.575 1.00 91.87  ? 454 ASN   A CG  1 
ATOM   1195 O  OD1 . ASN   A 1 158 ? -35.363 8.068   14.622 1.00 102.75 ? 454 ASN   A OD1 1 
ATOM   1196 N  ND2 . ASN   A 1 158 ? -36.409 8.825   12.782 1.00 97.82  ? 454 ASN   A ND2 1 
ATOM   1197 N  N   . LEU   A 1 159 ? -31.791 7.138   14.921 1.00 84.60  ? 455 LEU   A N   1 
ATOM   1198 C  CA  . LEU   A 1 159 ? -31.116 5.845   14.840 1.00 76.02  ? 455 LEU   A CA  1 
ATOM   1199 C  C   . LEU   A 1 159 ? -32.107 4.686   14.809 1.00 68.90  ? 455 LEU   A C   1 
ATOM   1200 O  O   . LEU   A 1 159 ? -33.214 4.761   15.353 1.00 67.19  ? 455 LEU   A O   1 
ATOM   1201 C  CB  . LEU   A 1 159 ? -30.153 5.652   16.014 1.00 70.45  ? 455 LEU   A CB  1 
ATOM   1202 C  CG  . LEU   A 1 159 ? -28.753 6.284   16.068 1.00 71.09  ? 455 LEU   A CG  1 
ATOM   1203 C  CD1 . LEU   A 1 159 ? -28.649 7.517   15.217 1.00 72.91  ? 455 LEU   A CD1 1 
ATOM   1204 C  CD2 . LEU   A 1 159 ? -28.363 6.629   17.523 1.00 69.98  ? 455 LEU   A CD2 1 
ATOM   1205 N  N   . ARG   A 1 160 ? -31.679 3.597   14.169 1.00 59.78  ? 456 ARG   A N   1 
ATOM   1206 C  CA  . ARG   A 1 160 ? -32.489 2.405   13.978 1.00 55.76  ? 456 ARG   A CA  1 
ATOM   1207 C  C   . ARG   A 1 160 ? -31.662 1.180   14.312 1.00 50.28  ? 456 ARG   A C   1 
ATOM   1208 O  O   . ARG   A 1 160 ? -30.469 1.112   13.992 1.00 59.08  ? 456 ARG   A O   1 
ATOM   1209 C  CB  . ARG   A 1 160 ? -33.008 2.308   12.523 1.00 55.37  ? 456 ARG   A CB  1 
ATOM   1210 C  CG  . ARG   A 1 160 ? -33.971 3.421   12.165 1.00 60.45  ? 456 ARG   A CG  1 
ATOM   1211 C  CD  . ARG   A 1 160 ? -34.517 3.319   10.724 1.00 64.17  ? 456 ARG   A CD  1 
ATOM   1212 N  NE  . ARG   A 1 160 ? -33.516 3.628   9.722  1.00 65.65  ? 456 ARG   A NE  1 
ATOM   1213 C  CZ  . ARG   A 1 160 ? -33.801 3.784   8.432  1.00 71.98  ? 456 ARG   A CZ  1 
ATOM   1214 N  NH1 . ARG   A 1 160 ? -35.057 3.673   8.010  1.00 76.68  ? 456 ARG   A NH1 1 
ATOM   1215 N  NH2 . ARG   A 1 160 ? -32.841 4.061   7.564  1.00 69.10  ? 456 ARG   A NH2 1 
ATOM   1216 N  N   . SER   A 1 161 ? -32.298 0.211   14.950 1.00 56.81  ? 457 SER   A N   1 
ATOM   1217 C  CA  . SER   A 1 161 ? -31.569 -0.962  15.400 1.00 60.54  ? 457 SER   A CA  1 
ATOM   1218 C  C   . SER   A 1 161 ? -31.335 -1.865  14.202 1.00 54.91  ? 457 SER   A C   1 
ATOM   1219 O  O   . SER   A 1 161 ? -32.245 -2.063  13.385 1.00 58.42  ? 457 SER   A O   1 
ATOM   1220 C  CB  . SER   A 1 161 ? -32.342 -1.697  16.502 1.00 59.12  ? 457 SER   A CB  1 
ATOM   1221 O  OG  . SER   A 1 161 ? -32.903 -0.803  17.475 1.00 50.10  ? 457 SER   A OG  1 
ATOM   1222 N  N   . ALA   A 1 162 ? -30.116 -2.402  14.086 1.00 53.54  ? 458 ALA   A N   1 
ATOM   1223 C  CA  . ALA   A 1 162 ? -29.782 -3.249  12.945 1.00 52.05  ? 458 ALA   A CA  1 
ATOM   1224 C  C   . ALA   A 1 162 ? -28.674 -4.236  13.293 1.00 49.58  ? 458 ALA   A C   1 
ATOM   1225 O  O   . ALA   A 1 162 ? -27.948 -4.082  14.276 1.00 60.45  ? 458 ALA   A O   1 
ATOM   1226 C  CB  . ALA   A 1 162 ? -29.371 -2.408  11.718 1.00 45.48  ? 458 ALA   A CB  1 
ATOM   1227 N  N   . ILE   A 1 163 ? -28.551 -5.258  12.447 1.00 44.65  ? 459 ILE   A N   1 
ATOM   1228 C  CA  . ILE   A 1 163 ? -27.510 -6.278  12.548 1.00 44.02  ? 459 ILE   A CA  1 
ATOM   1229 C  C   . ILE   A 1 163 ? -27.198 -6.783  11.136 1.00 46.83  ? 459 ILE   A C   1 
ATOM   1230 O  O   . ILE   A 1 163 ? -28.102 -6.959  10.312 1.00 46.28  ? 459 ILE   A O   1 
ATOM   1231 C  CB  . ILE   A 1 163 ? -27.954 -7.428  13.476 1.00 39.05  ? 459 ILE   A CB  1 
ATOM   1232 C  CG1 . ILE   A 1 163 ? -26.861 -8.510  13.577 1.00 38.10  ? 459 ILE   A CG1 1 
ATOM   1233 C  CG2 . ILE   A 1 163 ? -29.284 -8.004  12.997 1.00 45.42  ? 459 ILE   A CG2 1 
ATOM   1234 C  CD1 . ILE   A 1 163 ? -27.117 -9.575  14.679 1.00 37.27  ? 459 ILE   A CD1 1 
ATOM   1235 N  N   . THR   A 1 164 ? -25.913 -7.005  10.854 1.00 49.35  ? 460 THR   A N   1 
ATOM   1236 C  CA  . THR   A 1 164 ? -25.442 -7.546  9.584  1.00 53.78  ? 460 THR   A CA  1 
ATOM   1237 C  C   . THR   A 1 164 ? -24.740 -8.873  9.861  1.00 58.97  ? 460 THR   A C   1 
ATOM   1238 O  O   . THR   A 1 164 ? -23.740 -8.903  10.584 1.00 66.96  ? 460 THR   A O   1 
ATOM   1239 C  CB  . THR   A 1 164 ? -24.493 -6.570  8.895  1.00 53.01  ? 460 THR   A CB  1 
ATOM   1240 O  OG1 . THR   A 1 164 ? -25.192 -5.357  8.575  1.00 53.46  ? 460 THR   A OG1 1 
ATOM   1241 C  CG2 . THR   A 1 164 ? -23.951 -7.187  7.591  1.00 40.75  ? 460 THR   A CG2 1 
ATOM   1242 N  N   . ILE   A 1 165 ? -25.248 -9.963  9.284  1.00 53.62  ? 461 ILE   A N   1 
ATOM   1243 C  CA  . ILE   A 1 165 ? -24.828 -11.321 9.629  1.00 46.16  ? 461 ILE   A CA  1 
ATOM   1244 C  C   . ILE   A 1 165 ? -24.017 -11.891 8.471  1.00 51.05  ? 461 ILE   A C   1 
ATOM   1245 O  O   . ILE   A 1 165 ? -24.563 -12.135 7.398  1.00 48.62  ? 461 ILE   A O   1 
ATOM   1246 C  CB  . ILE   A 1 165 ? -26.038 -12.205 9.950  1.00 44.90  ? 461 ILE   A CB  1 
ATOM   1247 C  CG1 . ILE   A 1 165 ? -26.716 -11.754 11.261 1.00 49.54  ? 461 ILE   A CG1 1 
ATOM   1248 C  CG2 . ILE   A 1 165 ? -25.625 -13.642 10.067 1.00 55.22  ? 461 ILE   A CG2 1 
ATOM   1249 C  CD1 . ILE   A 1 165 ? -28.079 -12.362 11.423 1.00 48.42  ? 461 ILE   A CD1 1 
ATOM   1250 N  N   . PHE   A 1 166 ? -22.729 -12.114 8.687  1.00 52.52  ? 462 PHE   A N   1 
ATOM   1251 C  CA  . PHE   A 1 166 ? -21.805 -12.608 7.679  1.00 45.29  ? 462 PHE   A CA  1 
ATOM   1252 C  C   . PHE   A 1 166 ? -21.776 -14.132 7.682  1.00 60.19  ? 462 PHE   A C   1 
ATOM   1253 O  O   . PHE   A 1 166 ? -22.410 -14.764 8.536  1.00 54.48  ? 462 PHE   A O   1 
ATOM   1254 C  CB  . PHE   A 1 166 ? -20.424 -11.990 7.906  1.00 42.93  ? 462 PHE   A CB  1 
ATOM   1255 C  CG  . PHE   A 1 166 ? -20.345 -10.539 7.494  1.00 49.11  ? 462 PHE   A CG  1 
ATOM   1256 C  CD1 . PHE   A 1 166 ? -20.345 -10.190 6.153  1.00 46.33  ? 462 PHE   A CD1 1 
ATOM   1257 C  CD2 . PHE   A 1 166 ? -20.331 -9.521  8.447  1.00 43.74  ? 462 PHE   A CD2 1 
ATOM   1258 C  CE1 . PHE   A 1 166 ? -20.288 -8.852  5.756  1.00 48.96  ? 462 PHE   A CE1 1 
ATOM   1259 C  CE2 . PHE   A 1 166 ? -20.277 -8.176  8.063  1.00 45.11  ? 462 PHE   A CE2 1 
ATOM   1260 C  CZ  . PHE   A 1 166 ? -20.255 -7.840  6.706  1.00 46.04  ? 462 PHE   A CZ  1 
ATOM   1261 N  N   . PRO   A 1 167 ? -21.106 -14.761 6.691  1.00 59.22  ? 463 PRO   A N   1 
ATOM   1262 C  CA  . PRO   A 1 167 ? -21.204 -16.222 6.547  1.00 66.26  ? 463 PRO   A CA  1 
ATOM   1263 C  C   . PRO   A 1 167 ? -20.826 -16.970 7.823  1.00 66.22  ? 463 PRO   A C   1 
ATOM   1264 O  O   . PRO   A 1 167 ? -19.952 -16.553 8.584  1.00 58.39  ? 463 PRO   A O   1 
ATOM   1265 C  CB  . PRO   A 1 167 ? -20.236 -16.524 5.395  1.00 65.04  ? 463 PRO   A CB  1 
ATOM   1266 C  CG  . PRO   A 1 167 ? -20.303 -15.314 4.544  1.00 58.95  ? 463 PRO   A CG  1 
ATOM   1267 C  CD  . PRO   A 1 167 ? -20.349 -14.178 5.565  1.00 61.94  ? 463 PRO   A CD  1 
ATOM   1268 N  N   . GLN   A 1 168 ? -21.502 -18.088 8.057  1.00 69.14  ? 464 GLN   A N   1 
ATOM   1269 C  CA  . GLN   A 1 168 ? -21.295 -18.789 9.311  1.00 57.79  ? 464 GLN   A CA  1 
ATOM   1270 C  C   . GLN   A 1 168 ? -19.963 -19.530 9.284  1.00 62.74  ? 464 GLN   A C   1 
ATOM   1271 O  O   . GLN   A 1 168 ? -19.387 -19.789 8.226  1.00 66.44  ? 464 GLN   A O   1 
ATOM   1272 C  CB  . GLN   A 1 168 ? -22.439 -19.760 9.585  1.00 49.30  ? 464 GLN   A CB  1 
ATOM   1273 C  CG  . GLN   A 1 168 ? -22.391 -20.988 8.713  1.00 53.11  ? 464 GLN   A CG  1 
ATOM   1274 C  CD  . GLN   A 1 168 ? -23.779 -21.528 8.388  1.00 53.92  ? 464 GLN   A CD  1 
ATOM   1275 O  OE1 . GLN   A 1 168 ? -24.790 -20.825 8.541  1.00 56.84  ? 464 GLN   A OE1 1 
ATOM   1276 N  NE2 . GLN   A 1 168 ? -23.835 -22.786 7.952  1.00 55.89  ? 464 GLN   A NE2 1 
ATOM   1277 N  N   . ARG   A 1 169 ? -19.470 -19.861 10.477 1.00 59.82  ? 465 ARG   A N   1 
ATOM   1278 C  CA  . ARG   A 1 169 ? -18.219 -20.594 10.592 1.00 58.15  ? 465 ARG   A CA  1 
ATOM   1279 C  C   . ARG   A 1 169 ? -18.410 -22.002 10.055 1.00 65.92  ? 465 ARG   A C   1 
ATOM   1280 O  O   . ARG   A 1 169 ? -19.482 -22.591 10.199 1.00 69.61  ? 465 ARG   A O   1 
ATOM   1281 C  CB  . ARG   A 1 169 ? -17.752 -20.636 12.050 1.00 69.30  ? 465 ARG   A CB  1 
ATOM   1282 C  CG  . ARG   A 1 169 ? -16.383 -21.270 12.226 1.00 78.41  ? 465 ARG   A CG  1 
ATOM   1283 C  CD  . ARG   A 1 169 ? -16.046 -21.532 13.681 1.00 77.94  ? 465 ARG   A CD  1 
ATOM   1284 N  NE  . ARG   A 1 169 ? -15.269 -20.453 14.285 1.00 79.38  ? 465 ARG   A NE  1 
ATOM   1285 C  CZ  . ARG   A 1 169 ? -15.734 -19.626 15.215 1.00 78.44  ? 465 ARG   A CZ  1 
ATOM   1286 N  NH1 . ARG   A 1 169 ? -16.975 -19.766 15.666 1.00 78.84  ? 465 ARG   A NH1 1 
ATOM   1287 N  NH2 . ARG   A 1 169 ? -14.956 -18.663 15.702 1.00 75.37  ? 465 ARG   A NH2 1 
ATOM   1288 N  N   . THR   A 1 170 ? -17.367 -22.530 9.401  1.00 69.83  ? 466 THR   A N   1 
ATOM   1289 C  CA  . THR   A 1 170 ? -17.414 -23.861 8.811  1.00 64.49  ? 466 THR   A CA  1 
ATOM   1290 C  C   . THR   A 1 170 ? -16.284 -24.680 9.436  1.00 71.47  ? 466 THR   A C   1 
ATOM   1291 O  O   . THR   A 1 170 ? -16.448 -25.206 10.547 1.00 83.93  ? 466 THR   A O   1 
ATOM   1292 C  CB  . THR   A 1 170 ? -17.318 -23.809 7.273  1.00 77.72  ? 466 THR   A CB  1 
ATOM   1293 O  OG1 . THR   A 1 170 ? -16.183 -23.029 6.877  1.00 79.03  ? 466 THR   A OG1 1 
ATOM   1294 C  CG2 . THR   A 1 170 ? -18.589 -23.225 6.648  1.00 76.86  ? 466 THR   A CG2 1 
ATOM   1295 N  N   . ASP   A 1 171 ? -15.138 -24.804 8.765  1.00 80.85  ? 467 ASP   A N   1 
ATOM   1296 C  CA  . ASP   A 1 171 ? -14.045 -25.594 9.327  1.00 89.33  ? 467 ASP   A CA  1 
ATOM   1297 C  C   . ASP   A 1 171 ? -13.503 -24.970 10.606 1.00 87.56  ? 467 ASP   A C   1 
ATOM   1298 O  O   . ASP   A 1 171 ? -13.140 -25.687 11.543 1.00 90.86  ? 467 ASP   A O   1 
ATOM   1299 C  CB  . ASP   A 1 171 ? -12.923 -25.749 8.305  1.00 104.58 ? 467 ASP   A CB  1 
ATOM   1300 C  CG  . ASP   A 1 171 ? -12.188 -24.445 8.043  1.00 112.95 ? 467 ASP   A CG  1 
ATOM   1301 O  OD1 . ASP   A 1 171 ? -12.842 -23.378 8.046  1.00 113.27 ? 467 ASP   A OD1 1 
ATOM   1302 O  OD2 . ASP   A 1 171 ? -10.956 -24.483 7.845  1.00 119.57 ? 467 ASP   A OD2 1 
ATOM   1303 N  N   . GLY   A 1 172 ? -13.433 -23.638 10.665 1.00 88.37  ? 468 GLY   A N   1 
ATOM   1304 C  CA  . GLY   A 1 172 ? -12.793 -22.924 11.758 1.00 88.94  ? 468 GLY   A CA  1 
ATOM   1305 C  C   . GLY   A 1 172 ? -11.640 -22.036 11.324 1.00 95.97  ? 468 GLY   A C   1 
ATOM   1306 O  O   . GLY   A 1 172 ? -11.359 -21.034 11.986 1.00 91.20  ? 468 GLY   A O   1 
ATOM   1307 N  N   . LYS   A 1 173 ? -10.955 -22.390 10.232 1.00 100.85 ? 469 LYS   A N   1 
ATOM   1308 C  CA  . LYS   A 1 173 ? -9.898  -21.545 9.681  1.00 105.57 ? 469 LYS   A CA  1 
ATOM   1309 C  C   . LYS   A 1 173 ? -10.396 -20.663 8.540  1.00 102.03 ? 469 LYS   A C   1 
ATOM   1310 O  O   . LYS   A 1 173 ? -9.587  -20.038 7.842  1.00 101.30 ? 469 LYS   A O   1 
ATOM   1311 C  CB  . LYS   A 1 173 ? -8.705  -22.393 9.214  1.00 116.65 ? 469 LYS   A CB  1 
ATOM   1312 C  CG  . LYS   A 1 173 ? -7.389  -21.606 9.157  1.00 125.46 ? 469 LYS   A CG  1 
ATOM   1313 C  CD  . LYS   A 1 173 ? -6.329  -22.233 8.258  1.00 132.55 ? 469 LYS   A CD  1 
ATOM   1314 C  CE  . LYS   A 1 173 ? -5.228  -21.216 7.945  1.00 131.96 ? 469 LYS   A CE  1 
ATOM   1315 N  NZ  . LYS   A 1 173 ? -4.019  -21.831 7.331  1.00 134.87 ? 469 LYS   A NZ  1 
ATOM   1316 N  N   . HIS   A 1 174 ? -11.710 -20.590 8.339  1.00 96.84  ? 470 HIS   A N   1 
ATOM   1317 C  CA  . HIS   A 1 174 ? -12.304 -19.766 7.288  1.00 95.39  ? 470 HIS   A CA  1 
ATOM   1318 C  C   . HIS   A 1 174 ? -13.351 -18.857 7.913  1.00 90.56  ? 470 HIS   A C   1 
ATOM   1319 O  O   . HIS   A 1 174 ? -14.506 -18.806 7.495  1.00 91.35  ? 470 HIS   A O   1 
ATOM   1320 C  CB  . HIS   A 1 174 ? -12.906 -20.619 6.188  1.00 97.12  ? 470 HIS   A CB  1 
ATOM   1321 C  CG  . HIS   A 1 174 ? -11.890 -21.445 5.473  1.00 104.62 ? 470 HIS   A CG  1 
ATOM   1322 N  ND1 . HIS   A 1 174 ? -11.953 -22.819 5.411  1.00 109.54 ? 470 HIS   A ND1 1 
ATOM   1323 C  CD2 . HIS   A 1 174 ? -10.762 -21.089 4.815  1.00 111.29 ? 470 HIS   A CD2 1 
ATOM   1324 C  CE1 . HIS   A 1 174 ? -10.915 -23.274 4.733  1.00 118.22 ? 470 HIS   A CE1 1 
ATOM   1325 N  NE2 . HIS   A 1 174 ? -10.177 -22.244 4.359  1.00 117.29 ? 470 HIS   A NE2 1 
ATOM   1326 N  N   . ASP   A 1 175 ? -12.936 -18.144 8.950  1.00 82.52  ? 471 ASP   A N   1 
ATOM   1327 C  CA  . ASP   A 1 175 ? -13.828 -17.293 9.719  1.00 76.14  ? 471 ASP   A CA  1 
ATOM   1328 C  C   . ASP   A 1 175 ? -13.861 -15.892 9.133  1.00 75.75  ? 471 ASP   A C   1 
ATOM   1329 O  O   . ASP   A 1 175 ? -12.825 -15.354 8.725  1.00 79.55  ? 471 ASP   A O   1 
ATOM   1330 C  CB  . ASP   A 1 175 ? -13.397 -17.242 11.182 1.00 75.32  ? 471 ASP   A CB  1 
ATOM   1331 C  CG  . ASP   A 1 175 ? -13.598 -18.554 11.871 1.00 79.58  ? 471 ASP   A CG  1 
ATOM   1332 O  OD1 . ASP   A 1 175 ? -13.754 -19.567 11.164 1.00 88.62  ? 471 ASP   A OD1 1 
ATOM   1333 O  OD2 . ASP   A 1 175 ? -13.615 -18.579 13.112 1.00 81.75  ? 471 ASP   A OD2 1 
ATOM   1334 N  N   . PHE   A 1 176 ? -15.058 -15.327 9.064  1.00 71.24  ? 472 PHE   A N   1 
ATOM   1335 C  CA  . PHE   A 1 176 ? -15.213 -13.900 8.849  1.00 63.07  ? 472 PHE   A CA  1 
ATOM   1336 C  C   . PHE   A 1 176 ? -15.165 -13.228 10.211 1.00 62.69  ? 472 PHE   A C   1 
ATOM   1337 O  O   . PHE   A 1 176 ? -15.925 -13.597 11.112 1.00 54.53  ? 472 PHE   A O   1 
ATOM   1338 C  CB  . PHE   A 1 176 ? -16.526 -13.607 8.134  1.00 56.62  ? 472 PHE   A CB  1 
ATOM   1339 C  CG  . PHE   A 1 176 ? -16.546 -14.061 6.705  1.00 60.54  ? 472 PHE   A CG  1 
ATOM   1340 C  CD1 . PHE   A 1 176 ? -16.620 -15.407 6.396  1.00 55.35  ? 472 PHE   A CD1 1 
ATOM   1341 C  CD2 . PHE   A 1 176 ? -16.484 -13.140 5.676  1.00 63.13  ? 472 PHE   A CD2 1 
ATOM   1342 C  CE1 . PHE   A 1 176 ? -16.638 -15.831 5.069  1.00 68.90  ? 472 PHE   A CE1 1 
ATOM   1343 C  CE2 . PHE   A 1 176 ? -16.496 -13.553 4.365  1.00 67.90  ? 472 PHE   A CE2 1 
ATOM   1344 C  CZ  . PHE   A 1 176 ? -16.571 -14.902 4.060  1.00 65.36  ? 472 PHE   A CZ  1 
ATOM   1345 N  N   . ARG   A 1 177 ? -14.245 -12.287 10.380 1.00 62.80  ? 473 ARG   A N   1 
ATOM   1346 C  CA  . ARG   A 1 177 ? -14.129 -11.549 11.629 1.00 60.35  ? 473 ARG   A CA  1 
ATOM   1347 C  C   . ARG   A 1 177 ? -13.927 -10.081 11.310 1.00 65.43  ? 473 ARG   A C   1 
ATOM   1348 O  O   . ARG   A 1 177 ? -13.083 -9.736  10.478 1.00 73.52  ? 473 ARG   A O   1 
ATOM   1349 C  CB  . ARG   A 1 177 ? -12.961 -12.062 12.479 1.00 62.34  ? 473 ARG   A CB  1 
ATOM   1350 C  CG  . ARG   A 1 177 ? -13.107 -13.480 12.969 1.00 62.12  ? 473 ARG   A CG  1 
ATOM   1351 C  CD  . ARG   A 1 177 ? -14.196 -13.576 14.021 1.00 72.48  ? 473 ARG   A CD  1 
ATOM   1352 N  NE  . ARG   A 1 177 ? -14.062 -12.577 15.081 1.00 70.64  ? 473 ARG   A NE  1 
ATOM   1353 C  CZ  . ARG   A 1 177 ? -13.270 -12.714 16.141 1.00 71.75  ? 473 ARG   A CZ  1 
ATOM   1354 N  NH1 . ARG   A 1 177 ? -12.527 -13.807 16.269 1.00 71.97  ? 473 ARG   A NH1 1 
ATOM   1355 N  NH2 . ARG   A 1 177 ? -13.220 -11.757 17.069 1.00 63.99  ? 473 ARG   A NH2 1 
ATOM   1356 N  N   . VAL   A 1 178 ? -14.724 -9.226  11.936 1.00 64.19  ? 474 VAL   A N   1 
ATOM   1357 C  CA  . VAL   A 1 178 ? -14.352 -7.826  12.101 1.00 57.48  ? 474 VAL   A CA  1 
ATOM   1358 C  C   . VAL   A 1 178 ? -13.386 -7.788  13.276 1.00 68.18  ? 474 VAL   A C   1 
ATOM   1359 O  O   . VAL   A 1 178 ? -13.711 -8.269  14.367 1.00 61.54  ? 474 VAL   A O   1 
ATOM   1360 C  CB  . VAL   A 1 178 ? -15.585 -6.943  12.356 1.00 56.14  ? 474 VAL   A CB  1 
ATOM   1361 C  CG1 . VAL   A 1 178 ? -15.200 -5.477  12.402 1.00 64.57  ? 474 VAL   A CG1 1 
ATOM   1362 C  CG2 . VAL   A 1 178 ? -16.667 -7.199  11.292 1.00 47.20  ? 474 VAL   A CG2 1 
ATOM   1363 N  N   . TRP   A 1 179 ? -12.177 -7.278  13.044 1.00 72.66  ? 475 TRP   A N   1 
ATOM   1364 C  CA  . TRP   A 1 179 ? -11.197 -7.237  14.124 1.00 70.27  ? 475 TRP   A CA  1 
ATOM   1365 C  C   . TRP   A 1 179 ? -11.450 -6.073  15.075 1.00 72.09  ? 475 TRP   A C   1 
ATOM   1366 O  O   . TRP   A 1 179 ? -11.061 -6.138  16.250 1.00 59.66  ? 475 TRP   A O   1 
ATOM   1367 C  CB  . TRP   A 1 179 ? -9.781  -7.160  13.550 1.00 68.83  ? 475 TRP   A CB  1 
ATOM   1368 C  CG  . TRP   A 1 179 ? -9.299  -8.455  13.016 1.00 65.87  ? 475 TRP   A CG  1 
ATOM   1369 C  CD1 . TRP   A 1 179 ? -10.052 -9.425  12.424 1.00 72.27  ? 475 TRP   A CD1 1 
ATOM   1370 C  CD2 . TRP   A 1 179 ? -7.956  -8.941  13.028 1.00 68.52  ? 475 TRP   A CD2 1 
ATOM   1371 N  NE1 . TRP   A 1 179 ? -9.257  -10.482 12.049 1.00 76.49  ? 475 TRP   A NE1 1 
ATOM   1372 C  CE2 . TRP   A 1 179 ? -7.965  -10.210 12.414 1.00 79.78  ? 475 TRP   A CE2 1 
ATOM   1373 C  CE3 . TRP   A 1 179 ? -6.743  -8.421  13.480 1.00 64.41  ? 475 TRP   A CE3 1 
ATOM   1374 C  CZ2 . TRP   A 1 179 ? -6.810  -10.968 12.250 1.00 84.14  ? 475 TRP   A CZ2 1 
ATOM   1375 C  CZ3 . TRP   A 1 179 ? -5.601  -9.175  13.327 1.00 73.87  ? 475 TRP   A CZ3 1 
ATOM   1376 C  CH2 . TRP   A 1 179 ? -5.641  -10.436 12.711 1.00 81.42  ? 475 TRP   A CH2 1 
ATOM   1377 N  N   . ASN   A 1 180 ? -12.092 -5.015  14.587 1.00 66.13  ? 476 ASN   A N   1 
ATOM   1378 C  CA  . ASN   A 1 180 ? -12.547 -3.928  15.440 1.00 66.15  ? 476 ASN   A CA  1 
ATOM   1379 C  C   . ASN   A 1 180 ? -13.478 -4.451  16.526 1.00 69.05  ? 476 ASN   A C   1 
ATOM   1380 O  O   . ASN   A 1 180 ? -14.210 -5.427  16.317 1.00 59.27  ? 476 ASN   A O   1 
ATOM   1381 C  CB  . ASN   A 1 180 ? -13.271 -2.894  14.588 1.00 58.98  ? 476 ASN   A CB  1 
ATOM   1382 C  CG  . ASN   A 1 180 ? -12.363 -2.256  13.579 1.00 67.97  ? 476 ASN   A CG  1 
ATOM   1383 O  OD1 . ASN   A 1 180 ? -11.915 -2.905  12.632 1.00 85.75  ? 476 ASN   A OD1 1 
ATOM   1384 N  ND2 . ASN   A 1 180 ? -12.075 -0.977  13.771 1.00 73.18  ? 476 ASN   A ND2 1 
ATOM   1385 N  N   . SER   A 1 181 ? -13.455 -3.791  17.701 1.00 63.31  ? 477 SER   A N   1 
ATOM   1386 C  CA  . SER   A 1 181 ? -14.373 -4.193  18.765 1.00 58.11  ? 477 SER   A CA  1 
ATOM   1387 C  C   . SER   A 1 181 ? -15.728 -3.511  18.620 1.00 59.37  ? 477 SER   A C   1 
ATOM   1388 O  O   . SER   A 1 181 ? -16.739 -4.036  19.104 1.00 49.17  ? 477 SER   A O   1 
ATOM   1389 C  CB  . SER   A 1 181 ? -13.785 -3.895  20.156 1.00 59.24  ? 477 SER   A CB  1 
ATOM   1390 O  OG  . SER   A 1 181 ? -13.476 -2.524  20.336 1.00 62.89  ? 477 SER   A OG  1 
ATOM   1391 N  N   . GLN   A 1 182 ? -15.758 -2.341  17.980 1.00 64.77  ? 478 GLN   A N   1 
ATOM   1392 C  CA  . GLN   A 1 182 ? -16.976 -1.636  17.601 1.00 62.66  ? 478 GLN   A CA  1 
ATOM   1393 C  C   . GLN   A 1 182 ? -16.681 -0.954  16.284 1.00 59.27  ? 478 GLN   A C   1 
ATOM   1394 O  O   . GLN   A 1 182 ? -15.616 -0.349  16.142 1.00 65.49  ? 478 GLN   A O   1 
ATOM   1395 C  CB  . GLN   A 1 182 ? -17.405 -0.555  18.609 1.00 70.54  ? 478 GLN   A CB  1 
ATOM   1396 C  CG  . GLN   A 1 182 ? -17.602 -0.944  20.056 1.00 75.09  ? 478 GLN   A CG  1 
ATOM   1397 C  CD  . GLN   A 1 182 ? -17.725 0.295   20.953 1.00 77.50  ? 478 GLN   A CD  1 
ATOM   1398 O  OE1 . GLN   A 1 182 ? -18.238 1.349   20.526 1.00 64.11  ? 478 GLN   A OE1 1 
ATOM   1399 N  NE2 . GLN   A 1 182 ? -17.238 0.178   22.196 1.00 71.94  ? 478 GLN   A NE2 1 
ATOM   1400 N  N   . LEU   A 1 183 ? -17.618 -1.044  15.342 1.00 59.49  ? 479 LEU   A N   1 
ATOM   1401 C  CA  . LEU   A 1 183 ? -17.495 -0.423  14.029 1.00 55.53  ? 479 LEU   A CA  1 
ATOM   1402 C  C   . LEU   A 1 183 ? -16.869 0.965   14.100 1.00 61.78  ? 479 LEU   A C   1 
ATOM   1403 O  O   . LEU   A 1 183 ? -15.971 1.287   13.316 1.00 61.58  ? 479 LEU   A O   1 
ATOM   1404 C  CB  . LEU   A 1 183 ? -18.869 -0.344  13.363 1.00 57.21  ? 479 LEU   A CB  1 
ATOM   1405 C  CG  . LEU   A 1 183 ? -19.611 -1.663  13.047 1.00 58.07  ? 479 LEU   A CG  1 
ATOM   1406 C  CD1 . LEU   A 1 183 ? -20.792 -1.419  12.067 1.00 40.17  ? 479 LEU   A CD1 1 
ATOM   1407 C  CD2 . LEU   A 1 183 ? -18.663 -2.720  12.490 1.00 64.80  ? 479 LEU   A CD2 1 
ATOM   1408 N  N   . ILE   A 1 184 ? -17.294 1.781   15.068 1.00 63.12  ? 480 ILE   A N   1 
ATOM   1409 C  CA  . ILE   A 1 184 ? -16.839 3.163   15.199 1.00 52.84  ? 480 ILE   A CA  1 
ATOM   1410 C  C   . ILE   A 1 184 ? -16.238 3.357   16.590 1.00 69.63  ? 480 ILE   A C   1 
ATOM   1411 O  O   . ILE   A 1 184 ? -16.955 3.285   17.595 1.00 65.74  ? 480 ILE   A O   1 
ATOM   1412 C  CB  . ILE   A 1 184 ? -17.985 4.149   14.938 1.00 54.52  ? 480 ILE   A CB  1 
ATOM   1413 C  CG1 . ILE   A 1 184 ? -18.402 4.063   13.456 1.00 63.44  ? 480 ILE   A CG1 1 
ATOM   1414 C  CG2 . ILE   A 1 184 ? -17.569 5.564   15.273 1.00 61.67  ? 480 ILE   A CG2 1 
ATOM   1415 C  CD1 . ILE   A 1 184 ? -19.571 4.921   13.104 1.00 62.63  ? 480 ILE   A CD1 1 
ATOM   1416 N  N   . ARG   A 1 185 ? -14.923 3.586   16.641 1.00 73.34  ? 481 ARG   A N   1 
ATOM   1417 C  CA  . ARG   A 1 185 ? -14.191 3.860   17.867 1.00 71.00  ? 481 ARG   A CA  1 
ATOM   1418 C  C   . ARG   A 1 185 ? -13.116 4.902   17.589 1.00 80.17  ? 481 ARG   A C   1 
ATOM   1419 O  O   . ARG   A 1 185 ? -12.634 5.024   16.462 1.00 87.64  ? 481 ARG   A O   1 
ATOM   1420 C  CB  . ARG   A 1 185 ? -13.529 2.605   18.446 1.00 72.50  ? 481 ARG   A CB  1 
ATOM   1421 C  CG  . ARG   A 1 185 ? -14.479 1.492   18.823 1.00 76.41  ? 481 ARG   A CG  1 
ATOM   1422 C  CD  . ARG   A 1 185 ? -13.939 0.682   20.016 1.00 71.23  ? 481 ARG   A CD  1 
ATOM   1423 N  NE  . ARG   A 1 185 ? -13.904 1.466   21.244 1.00 75.80  ? 481 ARG   A NE  1 
ATOM   1424 C  CZ  . ARG   A 1 185 ? -13.677 0.944   22.448 1.00 76.67  ? 481 ARG   A CZ  1 
ATOM   1425 N  NH1 . ARG   A 1 185 ? -13.464 -0.363  22.582 1.00 63.55  ? 481 ARG   A NH1 1 
ATOM   1426 N  NH2 . ARG   A 1 185 ? -13.661 1.729   23.516 1.00 81.61  ? 481 ARG   A NH2 1 
ATOM   1427 N  N   . TYR   A 1 186 ? -12.729 5.640   18.633 1.00 70.94  ? 482 TYR   A N   1 
ATOM   1428 C  CA  . TYR   A 1 186 ? -11.644 6.600   18.519 1.00 76.81  ? 482 TYR   A CA  1 
ATOM   1429 C  C   . TYR   A 1 186 ? -10.305 5.958   18.852 1.00 82.11  ? 482 TYR   A C   1 
ATOM   1430 O  O   . TYR   A 1 186 ? -10.204 5.057   19.695 1.00 73.22  ? 482 TYR   A O   1 
ATOM   1431 C  CB  . TYR   A 1 186 ? -11.871 7.805   19.431 1.00 88.60  ? 482 TYR   A CB  1 
ATOM   1432 C  CG  . TYR   A 1 186 ? -13.143 8.543   19.118 1.00 93.41  ? 482 TYR   A CG  1 
ATOM   1433 C  CD1 . TYR   A 1 186 ? -14.166 8.635   20.051 1.00 91.64  ? 482 TYR   A CD1 1 
ATOM   1434 C  CD2 . TYR   A 1 186 ? -13.340 9.121   17.870 1.00 90.10  ? 482 TYR   A CD2 1 
ATOM   1435 C  CE1 . TYR   A 1 186 ? -15.340 9.309   19.758 1.00 95.12  ? 482 TYR   A CE1 1 
ATOM   1436 C  CE2 . TYR   A 1 186 ? -14.505 9.795   17.566 1.00 88.97  ? 482 TYR   A CE2 1 
ATOM   1437 C  CZ  . TYR   A 1 186 ? -15.505 9.880   18.507 1.00 91.16  ? 482 TYR   A CZ  1 
ATOM   1438 O  OH  . TYR   A 1 186 ? -16.674 10.541  18.202 1.00 84.22  ? 482 TYR   A OH  1 
ATOM   1439 N  N   . ALA   A 1 187 ? -9.268  6.483   18.213 1.00 82.63  ? 483 ALA   A N   1 
ATOM   1440 C  CA  . ALA   A 1 187 ? -7.944  5.891   18.206 1.00 94.62  ? 483 ALA   A CA  1 
ATOM   1441 C  C   . ALA   A 1 187 ? -7.282  6.004   19.568 1.00 94.00  ? 483 ALA   A C   1 
ATOM   1442 O  O   . ALA   A 1 187 ? -7.652  6.830   20.403 1.00 94.75  ? 483 ALA   A O   1 
ATOM   1443 C  CB  . ALA   A 1 187 ? -7.063  6.573   17.156 1.00 102.82 ? 483 ALA   A CB  1 
ATOM   1444 N  N   . GLY   A 1 188 ? -6.276  5.160   19.775 1.00 99.80  ? 484 GLY   A N   1 
ATOM   1445 C  CA  . GLY   A 1 188 ? -5.501  5.191   20.996 1.00 106.57 ? 484 GLY   A CA  1 
ATOM   1446 C  C   . GLY   A 1 188 ? -4.019  5.348   20.747 1.00 109.32 ? 484 GLY   A C   1 
ATOM   1447 O  O   . GLY   A 1 188 ? -3.386  4.475   20.148 1.00 108.72 ? 484 GLY   A O   1 
ATOM   1448 N  N   . TYR   A 1 189 ? -3.450  6.463   21.196 1.00 115.10 ? 485 TYR   A N   1 
ATOM   1449 C  CA  . TYR   A 1 189 ? -2.016  6.695   21.089 1.00 121.73 ? 485 TYR   A CA  1 
ATOM   1450 C  C   . TYR   A 1 189 ? -1.476  7.071   22.457 1.00 121.37 ? 485 TYR   A C   1 
ATOM   1451 O  O   . TYR   A 1 189 ? -1.927  8.054   23.053 1.00 118.32 ? 485 TYR   A O   1 
ATOM   1452 C  CB  . TYR   A 1 189 ? -1.676  7.805   20.088 1.00 126.67 ? 485 TYR   A CB  1 
ATOM   1453 C  CG  . TYR   A 1 189 ? -2.518  7.866   18.842 1.00 117.16 ? 485 TYR   A CG  1 
ATOM   1454 C  CD1 . TYR   A 1 189 ? -3.607  8.722   18.768 1.00 115.12 ? 485 TYR   A CD1 1 
ATOM   1455 C  CD2 . TYR   A 1 189 ? -2.203  7.103   17.726 1.00 119.47 ? 485 TYR   A CD2 1 
ATOM   1456 C  CE1 . TYR   A 1 189 ? -4.369  8.808   17.628 1.00 117.56 ? 485 TYR   A CE1 1 
ATOM   1457 C  CE2 . TYR   A 1 189 ? -2.965  7.179   16.577 1.00 116.39 ? 485 TYR   A CE2 1 
ATOM   1458 C  CZ  . TYR   A 1 189 ? -4.043  8.035   16.536 1.00 114.42 ? 485 TYR   A CZ  1 
ATOM   1459 O  OH  . TYR   A 1 189 ? -4.814  8.126   15.412 1.00 112.83 ? 485 TYR   A OH  1 
ATOM   1460 N  N   . LYS   A 1 190 ? -0.504  6.306   22.945 1.00 122.19 ? 486 LYS   A N   1 
ATOM   1461 C  CA  . LYS   A 1 190 ? 0.281   6.777   24.071 1.00 132.05 ? 486 LYS   A CA  1 
ATOM   1462 C  C   . LYS   A 1 190 ? 1.205   7.899   23.598 1.00 140.25 ? 486 LYS   A C   1 
ATOM   1463 O  O   . LYS   A 1 190 ? 1.170   8.322   22.441 1.00 146.54 ? 486 LYS   A O   1 
ATOM   1464 C  CB  . LYS   A 1 190 ? 1.057   5.628   24.710 1.00 134.13 ? 486 LYS   A CB  1 
ATOM   1465 C  CG  . LYS   A 1 190 ? 2.022   4.916   23.781 1.00 137.41 ? 486 LYS   A CG  1 
ATOM   1466 C  CD  . LYS   A 1 190 ? 1.629   3.457   23.616 1.00 132.34 ? 486 LYS   A CD  1 
ATOM   1467 C  CE  . LYS   A 1 190 ? 2.846   2.561   23.470 1.00 134.80 ? 486 LYS   A CE  1 
ATOM   1468 N  NZ  . LYS   A 1 190 ? 2.467   1.121   23.402 1.00 127.98 ? 486 LYS   A NZ  1 
ATOM   1469 N  N   . GLN   A 1 191 ? 2.044   8.393   24.499 1.00 142.11 ? 487 GLN   A N   1 
ATOM   1470 C  CA  . GLN   A 1 191 ? 2.827   9.584   24.192 1.00 146.15 ? 487 GLN   A CA  1 
ATOM   1471 C  C   . GLN   A 1 191 ? 4.317   9.319   24.393 1.00 151.72 ? 487 GLN   A C   1 
ATOM   1472 O  O   . GLN   A 1 191 ? 4.689   8.229   24.846 1.00 150.76 ? 487 GLN   A O   1 
ATOM   1473 C  CB  . GLN   A 1 191 ? 2.342   10.750  25.060 1.00 148.54 ? 487 GLN   A CB  1 
ATOM   1474 C  CG  . GLN   A 1 191 ? 1.078   11.406  24.533 1.00 143.73 ? 487 GLN   A CG  1 
ATOM   1475 C  CD  . GLN   A 1 191 ? 1.227   11.872  23.088 1.00 147.00 ? 487 GLN   A CD  1 
ATOM   1476 O  OE1 . GLN   A 1 191 ? 2.014   12.770  22.792 1.00 157.39 ? 487 GLN   A OE1 1 
ATOM   1477 N  NE2 . GLN   A 1 191 ? 0.474   11.256  22.184 1.00 140.68 ? 487 GLN   A NE2 1 
ATOM   1478 N  N   . PRO   A 1 192 ? 5.205   10.260  24.042 1.00 157.10 ? 488 PRO   A N   1 
ATOM   1479 C  CA  . PRO   A 1 192 ? 6.610   10.096  24.451 1.00 163.60 ? 488 PRO   A CA  1 
ATOM   1480 C  C   . PRO   A 1 192 ? 6.781   10.114  25.957 1.00 163.84 ? 488 PRO   A C   1 
ATOM   1481 O  O   . PRO   A 1 192 ? 7.621   9.384   26.497 1.00 167.35 ? 488 PRO   A O   1 
ATOM   1482 C  CB  . PRO   A 1 192 ? 7.311   11.288  23.782 1.00 173.98 ? 488 PRO   A CB  1 
ATOM   1483 C  CG  . PRO   A 1 192 ? 6.228   12.278  23.533 1.00 172.94 ? 488 PRO   A CG  1 
ATOM   1484 C  CD  . PRO   A 1 192 ? 5.036   11.444  23.181 1.00 163.34 ? 488 PRO   A CD  1 
ATOM   1485 N  N   . ASP   A 1 193 ? 5.990   10.925  26.654 1.00 163.02 ? 489 ASP   A N   1 
ATOM   1486 C  CA  . ASP   A 1 193 ? 6.046   11.017  28.106 1.00 158.09 ? 489 ASP   A CA  1 
ATOM   1487 C  C   . ASP   A 1 193 ? 5.268   9.914   28.803 1.00 150.60 ? 489 ASP   A C   1 
ATOM   1488 O  O   . ASP   A 1 193 ? 5.094   9.981   30.023 1.00 148.80 ? 489 ASP   A O   1 
ATOM   1489 C  CB  . ASP   A 1 193 ? 5.519   12.377  28.565 1.00 160.36 ? 489 ASP   A CB  1 
ATOM   1490 C  CG  . ASP   A 1 193 ? 4.148   12.684  28.004 1.00 155.47 ? 489 ASP   A CG  1 
ATOM   1491 O  OD1 . ASP   A 1 193 ? 4.034   12.867  26.770 1.00 154.70 ? 489 ASP   A OD1 1 
ATOM   1492 O  OD2 . ASP   A 1 193 ? 3.184   12.720  28.797 1.00 149.24 ? 489 ASP   A OD2 1 
ATOM   1493 N  N   . GLY   A 1 194 ? 4.792   8.916   28.071 1.00 148.63 ? 490 GLY   A N   1 
ATOM   1494 C  CA  . GLY   A 1 194 ? 4.074   7.793   28.649 1.00 147.69 ? 490 GLY   A CA  1 
ATOM   1495 C  C   . GLY   A 1 194 ? 2.559   7.886   28.642 1.00 148.77 ? 490 GLY   A C   1 
ATOM   1496 O  O   . GLY   A 1 194 ? 1.884   6.872   28.445 1.00 150.15 ? 490 GLY   A O   1 
ATOM   1497 N  N   . SER   A 1 195 ? 2.010   9.081   28.847 1.00 146.00 ? 491 SER   A N   1 
ATOM   1498 C  CA  . SER   A 1 195 ? 0.563   9.261   28.935 1.00 139.71 ? 491 SER   A CA  1 
ATOM   1499 C  C   . SER   A 1 195 ? -0.078  8.959   27.575 1.00 139.80 ? 491 SER   A C   1 
ATOM   1500 O  O   . SER   A 1 195 ? 0.587   8.559   26.616 1.00 143.10 ? 491 SER   A O   1 
ATOM   1501 C  CB  . SER   A 1 195 ? 0.232   10.662  29.437 1.00 135.53 ? 491 SER   A CB  1 
ATOM   1502 O  OG  . SER   A 1 195 ? 0.668   11.651  28.526 1.00 141.79 ? 491 SER   A OG  1 
ATOM   1503 N  N   . THR   A 1 196 ? -1.394  9.154   27.475 1.00 138.57 ? 492 THR   A N   1 
ATOM   1504 C  CA  . THR   A 1 196 ? -2.143  8.656   26.326 1.00 135.71 ? 492 THR   A CA  1 
ATOM   1505 C  C   . THR   A 1 196 ? -3.087  9.715   25.770 1.00 134.46 ? 492 THR   A C   1 
ATOM   1506 O  O   . THR   A 1 196 ? -3.860  10.321  26.518 1.00 137.86 ? 492 THR   A O   1 
ATOM   1507 C  CB  . THR   A 1 196 ? -2.931  7.394   26.710 1.00 131.19 ? 492 THR   A CB  1 
ATOM   1508 O  OG1 . THR   A 1 196 ? -2.015  6.338   27.036 1.00 131.30 ? 492 THR   A OG1 1 
ATOM   1509 C  CG2 . THR   A 1 196 ? -3.837  6.945   25.566 1.00 125.88 ? 492 THR   A CG2 1 
ATOM   1510 N  N   . LEU   A 1 197 ? -3.020  9.923   24.455 1.00 129.83 ? 493 LEU   A N   1 
ATOM   1511 C  CA  . LEU   A 1 197 ? -3.989  10.719  23.713 1.00 121.99 ? 493 LEU   A CA  1 
ATOM   1512 C  C   . LEU   A 1 197 ? -5.022  9.795   23.078 1.00 108.43 ? 493 LEU   A C   1 
ATOM   1513 O  O   . LEU   A 1 197 ? -4.695  8.688   22.634 1.00 103.02 ? 493 LEU   A O   1 
ATOM   1514 C  CB  . LEU   A 1 197 ? -3.297  11.562  22.631 1.00 123.93 ? 493 LEU   A CB  1 
ATOM   1515 C  CG  . LEU   A 1 197 ? -4.056  12.526  21.704 1.00 124.16 ? 493 LEU   A CG  1 
ATOM   1516 C  CD1 . LEU   A 1 197 ? -4.948  13.509  22.448 1.00 126.35 ? 493 LEU   A CD1 1 
ATOM   1517 C  CD2 . LEU   A 1 197 ? -3.070  13.286  20.828 1.00 128.67 ? 493 LEU   A CD2 1 
ATOM   1518 N  N   . GLY   A 1 198 ? -6.270  10.246  23.054 1.00 102.15 ? 494 GLY   A N   1 
ATOM   1519 C  CA  . GLY   A 1 198 ? -7.329  9.503   22.388 1.00 102.76 ? 494 GLY   A CA  1 
ATOM   1520 C  C   . GLY   A 1 198 ? -8.007  8.550   23.341 1.00 100.15 ? 494 GLY   A C   1 
ATOM   1521 O  O   . GLY   A 1 198 ? -8.309  8.913   24.483 1.00 111.81 ? 494 GLY   A O   1 
ATOM   1522 N  N   . ASP   A 1 199 ? -8.233  7.323   22.886 1.00 84.43  ? 495 ASP   A N   1 
ATOM   1523 C  CA  . ASP   A 1 199 ? -8.869  6.322   23.731 1.00 84.48  ? 495 ASP   A CA  1 
ATOM   1524 C  C   . ASP   A 1 199 ? -7.840  5.309   24.217 1.00 88.77  ? 495 ASP   A C   1 
ATOM   1525 O  O   . ASP   A 1 199 ? -7.391  4.465   23.425 1.00 76.46  ? 495 ASP   A O   1 
ATOM   1526 C  CB  . ASP   A 1 199 ? -9.993  5.620   22.973 1.00 80.32  ? 495 ASP   A CB  1 
ATOM   1527 C  CG  . ASP   A 1 199 ? -10.936 4.895   23.890 1.00 86.15  ? 495 ASP   A CG  1 
ATOM   1528 O  OD1 . ASP   A 1 199 ? -10.586 4.713   25.082 1.00 85.14  ? 495 ASP   A OD1 1 
ATOM   1529 O  OD2 . ASP   A 1 199 ? -12.034 4.512   23.426 1.00 81.95  ? 495 ASP   A OD2 1 
ATOM   1530 N  N   . PRO   A 1 200 ? -7.441  5.344   25.495 1.00 90.13  ? 496 PRO   A N   1 
ATOM   1531 C  CA  . PRO   A 1 200 ? -6.481  4.341   25.994 1.00 92.29  ? 496 PRO   A CA  1 
ATOM   1532 C  C   . PRO   A 1 200 ? -6.982  2.908   25.891 1.00 82.21  ? 496 PRO   A C   1 
ATOM   1533 O  O   . PRO   A 1 200 ? -6.165  1.978   25.904 1.00 80.07  ? 496 PRO   A O   1 
ATOM   1534 C  CB  . PRO   A 1 200 ? -6.267  4.749   27.464 1.00 98.16  ? 496 PRO   A CB  1 
ATOM   1535 C  CG  . PRO   A 1 200 ? -6.719  6.181   27.554 1.00 99.34  ? 496 PRO   A CG  1 
ATOM   1536 C  CD  . PRO   A 1 200 ? -7.822  6.320   26.532 1.00 91.86  ? 496 PRO   A CD  1 
ATOM   1537 N  N   . ALA   A 1 201 ? -8.297  2.696   25.801 1.00 82.18  ? 497 ALA   A N   1 
ATOM   1538 C  CA  . ALA   A 1 201 ? -8.820  1.350   25.592 1.00 87.72  ? 497 ALA   A CA  1 
ATOM   1539 C  C   . ALA   A 1 201 ? -8.255  0.708   24.331 1.00 85.48  ? 497 ALA   A C   1 
ATOM   1540 O  O   . ALA   A 1 201 ? -8.094  -0.516  24.281 1.00 81.48  ? 497 ALA   A O   1 
ATOM   1541 C  CB  . ALA   A 1 201 ? -10.348 1.384   25.506 1.00 89.20  ? 497 ALA   A CB  1 
ATOM   1542 N  N   . ASN   A 1 202 ? -7.921  1.512   23.323 1.00 91.31  ? 498 ASN   A N   1 
ATOM   1543 C  CA  . ASN   A 1 202 ? -7.722  1.025   21.963 1.00 94.47  ? 498 ASN   A CA  1 
ATOM   1544 C  C   . ASN   A 1 202 ? -6.259  0.984   21.538 1.00 98.85  ? 498 ASN   A C   1 
ATOM   1545 O  O   . ASN   A 1 202 ? -5.980  0.700   20.371 1.00 100.61 ? 498 ASN   A O   1 
ATOM   1546 C  CB  . ASN   A 1 202 ? -8.509  1.895   20.981 1.00 89.47  ? 498 ASN   A CB  1 
ATOM   1547 C  CG  . ASN   A 1 202 ? -10.012 1.755   21.142 1.00 83.07  ? 498 ASN   A CG  1 
ATOM   1548 O  OD1 . ASN   A 1 202 ? -10.515 0.665   21.397 1.00 78.51  ? 498 ASN   A OD1 1 
ATOM   1549 N  ND2 . ASN   A 1 202 ? -10.740 2.859   20.965 1.00 87.01  ? 498 ASN   A ND2 1 
ATOM   1550 N  N   . VAL   A 1 203 ? -5.318  1.240   22.453 1.00 92.63  ? 499 VAL   A N   1 
ATOM   1551 C  CA  . VAL   A 1 203 ? -3.937  1.502   22.048 1.00 93.02  ? 499 VAL   A CA  1 
ATOM   1552 C  C   . VAL   A 1 203 ? -3.327  0.291   21.356 1.00 94.96  ? 499 VAL   A C   1 
ATOM   1553 O  O   . VAL   A 1 203 ? -2.596  0.434   20.370 1.00 105.85 ? 499 VAL   A O   1 
ATOM   1554 C  CB  . VAL   A 1 203 ? -3.089  1.946   23.255 1.00 97.90  ? 499 VAL   A CB  1 
ATOM   1555 C  CG1 . VAL   A 1 203 ? -1.675  2.257   22.803 1.00 110.83 ? 499 VAL   A CG1 1 
ATOM   1556 C  CG2 . VAL   A 1 203 ? -3.706  3.155   23.908 1.00 93.71  ? 499 VAL   A CG2 1 
ATOM   1557 N  N   . GLN   A 1 204 ? -3.613  -0.919  21.843 1.00 86.34  ? 500 GLN   A N   1 
ATOM   1558 C  CA  . GLN   A 1 204 ? -3.096  -2.100  21.154 1.00 94.92  ? 500 GLN   A CA  1 
ATOM   1559 C  C   . GLN   A 1 204 ? -3.679  -2.207  19.751 1.00 99.67  ? 500 GLN   A C   1 
ATOM   1560 O  O   . GLN   A 1 204 ? -2.952  -2.456  18.780 1.00 100.87 ? 500 GLN   A O   1 
ATOM   1561 C  CB  . GLN   A 1 204 ? -3.389  -3.377  21.939 1.00 97.53  ? 500 GLN   A CB  1 
ATOM   1562 C  CG  . GLN   A 1 204 ? -2.727  -4.607  21.306 1.00 106.39 ? 500 GLN   A CG  1 
ATOM   1563 C  CD  . GLN   A 1 204 ? -3.199  -5.927  21.895 1.00 114.14 ? 500 GLN   A CD  1 
ATOM   1564 O  OE1 . GLN   A 1 204 ? -4.267  -6.009  22.503 1.00 111.31 ? 500 GLN   A OE1 1 
ATOM   1565 N  NE2 . GLN   A 1 204 ? -2.399  -6.974  21.709 1.00 121.79 ? 500 GLN   A NE2 1 
ATOM   1566 N  N   . PHE   A 1 205 ? -4.998  -2.026  19.627 1.00 95.83  ? 501 PHE   A N   1 
ATOM   1567 C  CA  . PHE   A 1 205 ? -5.637  -2.088  18.314 1.00 91.20  ? 501 PHE   A CA  1 
ATOM   1568 C  C   . PHE   A 1 205 ? -5.079  -1.017  17.384 1.00 96.36  ? 501 PHE   A C   1 
ATOM   1569 O  O   . PHE   A 1 205 ? -4.747  -1.298  16.225 1.00 93.48  ? 501 PHE   A O   1 
ATOM   1570 C  CB  . PHE   A 1 205 ? -7.157  -1.947  18.454 1.00 85.50  ? 501 PHE   A CB  1 
ATOM   1571 C  CG  . PHE   A 1 205 ? -7.907  -2.118  17.158 1.00 96.50  ? 501 PHE   A CG  1 
ATOM   1572 C  CD1 . PHE   A 1 205 ? -8.129  -3.386  16.630 1.00 101.25 ? 501 PHE   A CD1 1 
ATOM   1573 C  CD2 . PHE   A 1 205 ? -8.397  -1.014  16.464 1.00 98.84  ? 501 PHE   A CD2 1 
ATOM   1574 C  CE1 . PHE   A 1 205 ? -8.820  -3.550  15.427 1.00 98.88  ? 501 PHE   A CE1 1 
ATOM   1575 C  CE2 . PHE   A 1 205 ? -9.091  -1.175  15.269 1.00 100.06 ? 501 PHE   A CE2 1 
ATOM   1576 C  CZ  . PHE   A 1 205 ? -9.297  -2.443  14.750 1.00 97.24  ? 501 PHE   A CZ  1 
ATOM   1577 N  N   . THR   A 1 206 ? -4.964  0.222   17.877 1.00 93.01  ? 502 THR   A N   1 
ATOM   1578 C  CA  . THR   A 1 206 ? -4.448  1.304   17.045 1.00 97.15  ? 502 THR   A CA  1 
ATOM   1579 C  C   . THR   A 1 206 ? -3.049  0.981   16.530 1.00 105.84 ? 502 THR   A C   1 
ATOM   1580 O  O   . THR   A 1 206 ? -2.708  1.314   15.386 1.00 103.32 ? 502 THR   A O   1 
ATOM   1581 C  CB  . THR   A 1 206 ? -4.450  2.620   17.826 1.00 94.03  ? 502 THR   A CB  1 
ATOM   1582 O  OG1 . THR   A 1 206 ? -5.791  2.945   18.213 1.00 91.92  ? 502 THR   A OG1 1 
ATOM   1583 C  CG2 . THR   A 1 206 ? -3.886  3.760   16.981 1.00 100.93 ? 502 THR   A CG2 1 
ATOM   1584 N  N   . GLU   A 1 207 ? -2.233  0.307   17.350 1.00 107.78 ? 503 GLU   A N   1 
ATOM   1585 C  CA  . GLU   A 1 207 ? -0.907  -0.092  16.891 1.00 120.52 ? 503 GLU   A CA  1 
ATOM   1586 C  C   . GLU   A 1 207 ? -0.999  -1.170  15.818 1.00 117.51 ? 503 GLU   A C   1 
ATOM   1587 O  O   . GLU   A 1 207 ? -0.188  -1.192  14.884 1.00 123.33 ? 503 GLU   A O   1 
ATOM   1588 C  CB  . GLU   A 1 207 ? -0.054  -0.558  18.070 1.00 130.63 ? 503 GLU   A CB  1 
ATOM   1589 C  CG  . GLU   A 1 207 ? 0.908   0.510   18.582 1.00 147.31 ? 503 GLU   A CG  1 
ATOM   1590 C  CD  . GLU   A 1 207 ? 0.580   0.989   19.990 1.00 155.36 ? 503 GLU   A CD  1 
ATOM   1591 O  OE1 . GLU   A 1 207 ? 0.166   0.157   20.826 1.00 155.38 ? 503 GLU   A OE1 1 
ATOM   1592 O  OE2 . GLU   A 1 207 ? 0.740   2.200   20.261 1.00 161.08 ? 503 GLU   A OE2 1 
ATOM   1593 N  N   . ILE   A 1 208 ? -1.990  -2.060  15.924 1.00 106.50 ? 504 ILE   A N   1 
ATOM   1594 C  CA  . ILE   A 1 208 ? -2.192  -3.080  14.893 1.00 98.10  ? 504 ILE   A CA  1 
ATOM   1595 C  C   . ILE   A 1 208 ? -2.570  -2.431  13.564 1.00 96.12  ? 504 ILE   A C   1 
ATOM   1596 O  O   . ILE   A 1 208 ? -1.983  -2.737  12.519 1.00 96.10  ? 504 ILE   A O   1 
ATOM   1597 C  CB  . ILE   A 1 208 ? -3.249  -4.103  15.348 1.00 84.75  ? 504 ILE   A CB  1 
ATOM   1598 C  CG1 . ILE   A 1 208 ? -2.655  -5.079  16.369 1.00 80.49  ? 504 ILE   A CG1 1 
ATOM   1599 C  CG2 . ILE   A 1 208 ? -3.797  -4.866  14.167 1.00 78.95  ? 504 ILE   A CG2 1 
ATOM   1600 C  CD1 . ILE   A 1 208 ? -3.627  -6.153  16.828 1.00 84.56  ? 504 ILE   A CD1 1 
ATOM   1601 N  N   . CYS   A 1 209 ? -3.563  -1.530  13.579 1.00 90.18  ? 505 CYS   A N   1 
ATOM   1602 C  CA  . CYS   A 1 209 ? -3.909  -0.794  12.362 1.00 88.32  ? 505 CYS   A CA  1 
ATOM   1603 C  C   . CYS   A 1 209 ? -2.695  -0.073  11.799 1.00 100.43 ? 505 CYS   A C   1 
ATOM   1604 O  O   . CYS   A 1 209 ? -2.458  -0.093  10.583 1.00 109.66 ? 505 CYS   A O   1 
ATOM   1605 C  CB  . CYS   A 1 209 ? -5.035  0.213   12.624 1.00 83.82  ? 505 CYS   A CB  1 
ATOM   1606 S  SG  . CYS   A 1 209 ? -6.651  -0.512  13.039 1.00 88.93  ? 505 CYS   A SG  1 
ATOM   1607 N  N   . ILE   A 1 210 ? -1.909  0.570   12.666 1.00 104.10 ? 506 ILE   A N   1 
ATOM   1608 C  CA  . ILE   A 1 210 ? -0.693  1.222   12.190 1.00 114.25 ? 506 ILE   A CA  1 
ATOM   1609 C  C   . ILE   A 1 210 ? 0.304   0.183   11.677 1.00 120.24 ? 506 ILE   A C   1 
ATOM   1610 O  O   . ILE   A 1 210 ? 1.032   0.435   10.706 1.00 109.53 ? 506 ILE   A O   1 
ATOM   1611 C  CB  . ILE   A 1 210 ? -0.098  2.111   13.301 1.00 105.27 ? 506 ILE   A CB  1 
ATOM   1612 C  CG1 . ILE   A 1 210 ? -1.008  3.310   13.580 1.00 103.53 ? 506 ILE   A CG1 1 
ATOM   1613 C  CG2 . ILE   A 1 210 ? 1.274   2.630   12.903 1.00 113.43 ? 506 ILE   A CG2 1 
ATOM   1614 C  CD1 . ILE   A 1 210 ? -0.494  4.206   14.713 1.00 120.83 ? 506 ILE   A CD1 1 
ATOM   1615 N  N   . GLN   A 1 211 ? 0.338   -1.002  12.303 1.00 115.99 ? 507 GLN   A N   1 
ATOM   1616 C  CA  . GLN   A 1 211 ? 1.196   -2.083  11.820 1.00 118.11 ? 507 GLN   A CA  1 
ATOM   1617 C  C   . GLN   A 1 211 ? 0.831   -2.482  10.395 1.00 109.16 ? 507 GLN   A C   1 
ATOM   1618 O  O   . GLN   A 1 211 ? 1.714   -2.752  9.571  1.00 108.96 ? 507 GLN   A O   1 
ATOM   1619 C  CB  . GLN   A 1 211 ? 1.100   -3.291  12.757 1.00 121.24 ? 507 GLN   A CB  1 
ATOM   1620 C  CG  . GLN   A 1 211 ? 2.103   -3.289  13.917 1.00 133.44 ? 507 GLN   A CG  1 
ATOM   1621 C  CD  . GLN   A 1 211 ? 3.317   -4.173  13.650 1.00 142.17 ? 507 GLN   A CD  1 
ATOM   1622 O  OE1 . GLN   A 1 211 ? 3.213   -5.199  12.972 1.00 142.07 ? 507 GLN   A OE1 1 
ATOM   1623 N  NE2 . GLN   A 1 211 ? 4.475   -3.776  14.181 1.00 146.66 ? 507 GLN   A NE2 1 
ATOM   1624 N  N   . GLN   A 1 212 ? -0.469  -2.533  10.087 1.00 105.21 ? 508 GLN   A N   1 
ATOM   1625 C  CA  . GLN   A 1 212 ? -0.950  -2.812  8.737  1.00 96.69  ? 508 GLN   A CA  1 
ATOM   1626 C  C   . GLN   A 1 212 ? -0.980  -1.567  7.853  1.00 101.18 ? 508 GLN   A C   1 
ATOM   1627 O  O   . GLN   A 1 212 ? -1.683  -1.551  6.830  1.00 97.03  ? 508 GLN   A O   1 
ATOM   1628 C  CB  . GLN   A 1 212 ? -2.341  -3.457  8.784  1.00 89.57  ? 508 GLN   A CB  1 
ATOM   1629 C  CG  . GLN   A 1 212 ? -2.401  -4.801  9.513  1.00 94.88  ? 508 GLN   A CG  1 
ATOM   1630 C  CD  . GLN   A 1 212 ? -1.426  -5.835  8.963  1.00 105.07 ? 508 GLN   A CD  1 
ATOM   1631 O  OE1 . GLN   A 1 212 ? -1.048  -5.796  7.791  1.00 112.89 ? 508 GLN   A OE1 1 
ATOM   1632 N  NE2 . GLN   A 1 212 ? -1.014  -6.766  9.817  1.00 107.59 ? 508 GLN   A NE2 1 
ATOM   1633 N  N   . GLY   A 1 213 ? -0.247  -0.525  8.234  1.00 104.18 ? 509 GLY   A N   1 
ATOM   1634 C  CA  . GLY   A 1 213 ? -0.075  0.630   7.386  1.00 114.33 ? 509 GLY   A CA  1 
ATOM   1635 C  C   . GLY   A 1 213 ? -1.062  1.757   7.576  1.00 113.09 ? 509 GLY   A C   1 
ATOM   1636 O  O   . GLY   A 1 213 ? -1.093  2.668   6.745  1.00 114.98 ? 509 GLY   A O   1 
ATOM   1637 N  N   . TRP   A 1 214 ? -1.875  1.735   8.627  1.00 115.13 ? 510 TRP   A N   1 
ATOM   1638 C  CA  . TRP   A 1 214 ? -2.718  2.894   8.889  1.00 116.65 ? 510 TRP   A CA  1 
ATOM   1639 C  C   . TRP   A 1 214 ? -1.829  4.084   9.200  1.00 123.47 ? 510 TRP   A C   1 
ATOM   1640 O  O   . TRP   A 1 214 ? -0.905  3.991   10.015 1.00 124.49 ? 510 TRP   A O   1 
ATOM   1641 C  CB  . TRP   A 1 214 ? -3.690  2.641   10.046 1.00 108.40 ? 510 TRP   A CB  1 
ATOM   1642 C  CG  . TRP   A 1 214 ? -4.739  3.718   10.204 1.00 106.15 ? 510 TRP   A CG  1 
ATOM   1643 C  CD1 . TRP   A 1 214 ? -5.634  4.118   9.266  1.00 100.81 ? 510 TRP   A CD1 1 
ATOM   1644 C  CD2 . TRP   A 1 214 ? -4.999  4.518   11.372 1.00 112.72 ? 510 TRP   A CD2 1 
ATOM   1645 N  NE1 . TRP   A 1 214 ? -6.439  5.111   9.763  1.00 98.73  ? 510 TRP   A NE1 1 
ATOM   1646 C  CE2 . TRP   A 1 214 ? -6.069  5.379   11.054 1.00 108.11 ? 510 TRP   A CE2 1 
ATOM   1647 C  CE3 . TRP   A 1 214 ? -4.432  4.591   12.650 1.00 118.45 ? 510 TRP   A CE3 1 
ATOM   1648 C  CZ2 . TRP   A 1 214 ? -6.585  6.300   11.963 1.00 113.81 ? 510 TRP   A CZ2 1 
ATOM   1649 C  CZ3 . TRP   A 1 214 ? -4.947  5.513   13.558 1.00 116.94 ? 510 TRP   A CZ3 1 
ATOM   1650 C  CH2 . TRP   A 1 214 ? -6.015  6.351   13.209 1.00 115.30 ? 510 TRP   A CH2 1 
ATOM   1651 N  N   . LYS   A 1 215 ? -2.084  5.189   8.515  1.00 124.84 ? 511 LYS   A N   1 
ATOM   1652 C  CA  . LYS   A 1 215 ? -1.372  6.430   8.772  1.00 131.02 ? 511 LYS   A CA  1 
ATOM   1653 C  C   . LYS   A 1 215 ? -2.167  7.204   9.819  1.00 124.06 ? 511 LYS   A C   1 
ATOM   1654 O  O   . LYS   A 1 215 ? -3.275  7.675   9.545  1.00 119.42 ? 511 LYS   A O   1 
ATOM   1655 C  CB  . LYS   A 1 215 ? -1.198  7.207   7.473  1.00 139.81 ? 511 LYS   A CB  1 
ATOM   1656 C  CG  . LYS   A 1 215 ? -0.749  6.327   6.301  1.00 143.23 ? 511 LYS   A CG  1 
ATOM   1657 C  CD  . LYS   A 1 215 ? 0.769   6.119   6.256  1.00 151.66 ? 511 LYS   A CD  1 
ATOM   1658 C  CE  . LYS   A 1 215 ? 1.171   4.698   6.629  1.00 149.90 ? 511 LYS   A CE  1 
ATOM   1659 N  NZ  . LYS   A 1 215 ? 2.568   4.375   6.213  1.00 156.83 ? 511 LYS   A NZ  1 
ATOM   1660 N  N   . ALA   A 1 216 ? -1.614  7.306   11.025 1.00 122.11 ? 512 ALA   A N   1 
ATOM   1661 C  CA  . ALA   A 1 216 ? -2.369  7.836   12.154 1.00 111.01 ? 512 ALA   A CA  1 
ATOM   1662 C  C   . ALA   A 1 216 ? -2.406  9.359   12.100 1.00 117.30 ? 512 ALA   A C   1 
ATOM   1663 O  O   . ALA   A 1 216 ? -1.365  9.991   11.890 1.00 124.28 ? 512 ALA   A O   1 
ATOM   1664 C  CB  . ALA   A 1 216 ? -1.751  7.373   13.468 1.00 111.33 ? 512 ALA   A CB  1 
ATOM   1665 N  N   . PRO   A 1 217 ? -3.580  9.982   12.263 1.00 115.24 ? 513 PRO   A N   1 
ATOM   1666 C  CA  . PRO   A 1 217 ? -3.628  11.446  12.392 1.00 124.62 ? 513 PRO   A CA  1 
ATOM   1667 C  C   . PRO   A 1 217 ? -3.311  11.923  13.804 1.00 137.17 ? 513 PRO   A C   1 
ATOM   1668 O  O   . PRO   A 1 217 ? -3.616  13.070  14.149 1.00 141.85 ? 513 PRO   A O   1 
ATOM   1669 C  CB  . PRO   A 1 217 ? -5.075  11.787  12.005 1.00 118.47 ? 513 PRO   A CB  1 
ATOM   1670 C  CG  . PRO   A 1 217 ? -5.614  10.549  11.325 1.00 111.07 ? 513 PRO   A CG  1 
ATOM   1671 C  CD  . PRO   A 1 217 ? -4.915  9.418   12.012 1.00 107.90 ? 513 PRO   A CD  1 
ATOM   1672 N  N   . ARG   A 1 218 ? -2.702  11.039  14.610 1.00 138.83 ? 514 ARG   A N   1 
ATOM   1673 C  CA  . ARG   A 1 218 ? -2.312  11.238  16.010 1.00 136.65 ? 514 ARG   A CA  1 
ATOM   1674 C  C   . ARG   A 1 218 ? -2.956  12.437  16.697 1.00 132.98 ? 514 ARG   A C   1 
ATOM   1675 O  O   . ARG   A 1 218 ? -2.267  13.384  17.093 1.00 137.88 ? 514 ARG   A O   1 
ATOM   1676 C  CB  . ARG   A 1 218 ? -0.788  11.337  16.121 1.00 147.59 ? 514 ARG   A CB  1 
ATOM   1677 C  CG  . ARG   A 1 218 ? -0.101  9.999   15.916 1.00 147.60 ? 514 ARG   A CG  1 
ATOM   1678 C  CD  . ARG   A 1 218 ? 1.309   9.947   16.499 1.00 154.70 ? 514 ARG   A CD  1 
ATOM   1679 N  NE  . ARG   A 1 218 ? 1.536   8.710   17.247 1.00 149.66 ? 514 ARG   A NE  1 
ATOM   1680 C  CZ  . ARG   A 1 218 ? 1.597   7.497   16.702 1.00 150.43 ? 514 ARG   A CZ  1 
ATOM   1681 N  NH1 . ARG   A 1 218 ? 1.801   6.434   17.466 1.00 148.33 ? 514 ARG   A NH1 1 
ATOM   1682 N  NH2 . ARG   A 1 218 ? 1.444   7.338   15.394 1.00 154.37 ? 514 ARG   A NH2 1 
ATOM   1683 N  N   . GLY   A 1 219 ? -4.278  12.398  16.836 1.00 116.31 ? 515 GLY   A N   1 
ATOM   1684 C  CA  . GLY   A 1 219 ? -5.032  13.337  17.633 1.00 124.43 ? 515 GLY   A CA  1 
ATOM   1685 C  C   . GLY   A 1 219 ? -5.870  12.606  18.668 1.00 116.78 ? 515 GLY   A C   1 
ATOM   1686 O  O   . GLY   A 1 219 ? -5.555  11.492  19.081 1.00 106.85 ? 515 GLY   A O   1 
ATOM   1687 N  N   . ARG   A 1 220 ? -6.972  13.245  19.056 1.00 117.73 ? 516 ARG   A N   1 
ATOM   1688 C  CA  . ARG   A 1 220 ? -7.874  12.706  20.066 1.00 121.14 ? 516 ARG   A CA  1 
ATOM   1689 C  C   . ARG   A 1 220 ? -8.930  11.794  19.470 1.00 119.96 ? 516 ARG   A C   1 
ATOM   1690 O  O   . ARG   A 1 220 ? -8.809  10.565  19.509 1.00 124.55 ? 516 ARG   A O   1 
ATOM   1691 C  CB  . ARG   A 1 220 ? -8.575  13.840  20.809 1.00 131.19 ? 516 ARG   A CB  1 
ATOM   1692 C  CG  . ARG   A 1 220 ? -9.463  13.366  21.931 1.00 127.60 ? 516 ARG   A CG  1 
ATOM   1693 C  CD  . ARG   A 1 220 ? -8.764  13.545  23.254 1.00 132.16 ? 516 ARG   A CD  1 
ATOM   1694 N  NE  . ARG   A 1 220 ? -9.372  14.617  24.034 1.00 136.89 ? 516 ARG   A NE  1 
ATOM   1695 C  CZ  . ARG   A 1 220 ? -9.195  14.779  25.339 1.00 138.25 ? 516 ARG   A CZ  1 
ATOM   1696 N  NH1 . ARG   A 1 220 ? -8.421  13.939  26.012 1.00 136.59 ? 516 ARG   A NH1 1 
ATOM   1697 N  NH2 . ARG   A 1 220 ? -9.797  15.774  25.971 1.00 142.54 ? 516 ARG   A NH2 1 
ATOM   1698 N  N   . PHE   A 1 221 ? -9.978  12.404  18.925 1.00 115.21 ? 517 PHE   A N   1 
ATOM   1699 C  CA  . PHE   A 1 221 ? -11.140 11.678  18.418 1.00 106.11 ? 517 PHE   A CA  1 
ATOM   1700 C  C   . PHE   A 1 221 ? -10.935 11.301  16.945 1.00 107.60 ? 517 PHE   A C   1 
ATOM   1701 O  O   . PHE   A 1 221 ? -11.688 11.687  16.048 1.00 109.77 ? 517 PHE   A O   1 
ATOM   1702 C  CB  . PHE   A 1 221 ? -12.407 12.509  18.624 1.00 103.73 ? 517 PHE   A CB  1 
ATOM   1703 C  CG  . PHE   A 1 221 ? -12.617 13.000  20.061 1.00 99.32  ? 517 PHE   A CG  1 
ATOM   1704 C  CD1 . PHE   A 1 221 ? -12.542 14.347  20.366 1.00 96.46  ? 517 PHE   A CD1 1 
ATOM   1705 C  CD2 . PHE   A 1 221 ? -12.917 12.112  21.088 1.00 86.18  ? 517 PHE   A CD2 1 
ATOM   1706 C  CE1 . PHE   A 1 221 ? -12.749 14.804  21.663 1.00 105.26 ? 517 PHE   A CE1 1 
ATOM   1707 C  CE2 . PHE   A 1 221 ? -13.133 12.569  22.382 1.00 91.65  ? 517 PHE   A CE2 1 
ATOM   1708 C  CZ  . PHE   A 1 221 ? -13.041 13.905  22.677 1.00 92.89  ? 517 PHE   A CZ  1 
ATOM   1709 N  N   . ASP   A 1 222 ? -9.871  10.531  16.712 1.00 108.53 ? 518 ASP   A N   1 
ATOM   1710 C  CA  . ASP   A 1 222 ? -9.577  9.980   15.397 1.00 104.08 ? 518 ASP   A CA  1 
ATOM   1711 C  C   . ASP   A 1 222 ? -10.353 8.679   15.207 1.00 103.98 ? 518 ASP   A C   1 
ATOM   1712 O  O   . ASP   A 1 222 ? -10.172 7.723   15.975 1.00 95.82  ? 518 ASP   A O   1 
ATOM   1713 C  CB  . ASP   A 1 222 ? -8.077  9.733   15.243 1.00 103.33 ? 518 ASP   A CB  1 
ATOM   1714 C  CG  . ASP   A 1 222 ? -7.258  11.009  15.324 1.00 108.93 ? 518 ASP   A CG  1 
ATOM   1715 O  OD1 . ASP   A 1 222 ? -7.852  12.087  15.539 1.00 110.82 ? 518 ASP   A OD1 1 
ATOM   1716 O  OD2 . ASP   A 1 222 ? -6.017  10.935  15.170 1.00 105.71 ? 518 ASP   A OD2 1 
ATOM   1717 N  N   . VAL   A 1 223 ? -11.207 8.643   14.182 1.00 95.22  ? 519 VAL   A N   1 
ATOM   1718 C  CA  . VAL   A 1 223 ? -12.030 7.469   13.909 1.00 90.03  ? 519 VAL   A CA  1 
ATOM   1719 C  C   . VAL   A 1 223 ? -11.149 6.384   13.308 1.00 89.06  ? 519 VAL   A C   1 
ATOM   1720 O  O   . VAL   A 1 223 ? -10.555 6.570   12.236 1.00 89.13  ? 519 VAL   A O   1 
ATOM   1721 C  CB  . VAL   A 1 223 ? -13.190 7.819   12.965 1.00 89.95  ? 519 VAL   A CB  1 
ATOM   1722 C  CG1 . VAL   A 1 223 ? -14.154 6.647   12.832 1.00 80.77  ? 519 VAL   A CG1 1 
ATOM   1723 C  CG2 . VAL   A 1 223 ? -13.913 9.078   13.428 1.00 93.28  ? 519 VAL   A CG2 1 
ATOM   1724 N  N   . LEU   A 1 224 ? -11.078 5.239   13.978 1.00 80.27  ? 520 LEU   A N   1 
ATOM   1725 C  CA  . LEU   A 1 224 ? -10.248 4.153   13.494 1.00 83.64  ? 520 LEU   A CA  1 
ATOM   1726 C  C   . LEU   A 1 224 ? -10.802 3.560   12.198 1.00 83.06  ? 520 LEU   A C   1 
ATOM   1727 O  O   . LEU   A 1 224 ? -12.001 3.638   11.924 1.00 75.89  ? 520 LEU   A O   1 
ATOM   1728 C  CB  . LEU   A 1 224 ? -10.150 3.057   14.541 1.00 67.95  ? 520 LEU   A CB  1 
ATOM   1729 C  CG  . LEU   A 1 224 ? -9.451  3.457   15.849 1.00 75.97  ? 520 LEU   A CG  1 
ATOM   1730 C  CD1 . LEU   A 1 224 ? -10.189 2.755   16.962 1.00 65.81  ? 520 LEU   A CD1 1 
ATOM   1731 C  CD2 . LEU   A 1 224 ? -7.973  3.084   15.837 1.00 74.03  ? 520 LEU   A CD2 1 
ATOM   1732 N  N   . PRO   A 1 225 ? -9.950  2.939   11.395 1.00 81.47  ? 521 PRO   A N   1 
ATOM   1733 C  CA  . PRO   A 1 225 ? -10.430 2.262   10.191 1.00 89.80  ? 521 PRO   A CA  1 
ATOM   1734 C  C   . PRO   A 1 225 ? -10.904 0.851   10.505 1.00 87.72  ? 521 PRO   A C   1 
ATOM   1735 O  O   . PRO   A 1 225 ? -10.557 0.259   11.532 1.00 91.42  ? 521 PRO   A O   1 
ATOM   1736 C  CB  . PRO   A 1 225 ? -9.184  2.235   9.296  1.00 96.90  ? 521 PRO   A CB  1 
ATOM   1737 C  CG  . PRO   A 1 225 ? -8.064  2.116   10.280 1.00 94.67  ? 521 PRO   A CG  1 
ATOM   1738 C  CD  . PRO   A 1 225 ? -8.478  2.936   11.474 1.00 92.52  ? 521 PRO   A CD  1 
ATOM   1739 N  N   . LEU   A 1 226 ? -11.721 0.323   9.596  1.00 83.39  ? 522 LEU   A N   1 
ATOM   1740 C  CA  . LEU   A 1 226 ? -12.186 -1.051  9.723  1.00 74.71  ? 522 LEU   A CA  1 
ATOM   1741 C  C   . LEU   A 1 226 ? -11.065 -2.025  9.391  1.00 73.42  ? 522 LEU   A C   1 
ATOM   1742 O  O   . LEU   A 1 226 ? -10.369 -1.864  8.384  1.00 76.41  ? 522 LEU   A O   1 
ATOM   1743 C  CB  . LEU   A 1 226 ? -13.377 -1.304  8.807  1.00 68.22  ? 522 LEU   A CB  1 
ATOM   1744 C  CG  . LEU   A 1 226 ? -14.755 -0.786  9.210  1.00 68.55  ? 522 LEU   A CG  1 
ATOM   1745 C  CD1 . LEU   A 1 226 ? -15.741 -0.929  8.030  1.00 57.73  ? 522 LEU   A CD1 1 
ATOM   1746 C  CD2 . LEU   A 1 226 ? -15.247 -1.523  10.454 1.00 66.12  ? 522 LEU   A CD2 1 
ATOM   1747 N  N   . LEU   A 1 227 ? -10.884 -3.032  10.250 1.00 64.21  ? 523 LEU   A N   1 
ATOM   1748 C  CA  . LEU   A 1 227 ? -9.987  -4.149  9.980  1.00 69.51  ? 523 LEU   A CA  1 
ATOM   1749 C  C   . LEU   A 1 227 ? -10.855 -5.379  9.752  1.00 66.32  ? 523 LEU   A C   1 
ATOM   1750 O  O   . LEU   A 1 227 ? -11.449 -5.906  10.694 1.00 72.95  ? 523 LEU   A O   1 
ATOM   1751 C  CB  . LEU   A 1 227 ? -9.006  -4.369  11.125 1.00 72.59  ? 523 LEU   A CB  1 
ATOM   1752 C  CG  . LEU   A 1 227 ? -7.500  -4.450  10.840 1.00 77.31  ? 523 LEU   A CG  1 
ATOM   1753 C  CD1 . LEU   A 1 227 ? -6.887  -5.579  11.660 1.00 81.85  ? 523 LEU   A CD1 1 
ATOM   1754 C  CD2 . LEU   A 1 227 ? -7.154  -4.609  9.368  1.00 74.27  ? 523 LEU   A CD2 1 
ATOM   1755 N  N   . LEU   A 1 228 ? -10.921 -5.840  8.504  1.00 69.41  ? 524 LEU   A N   1 
ATOM   1756 C  CA  . LEU   A 1 228 ? -11.885 -6.851  8.089  1.00 67.41  ? 524 LEU   A CA  1 
ATOM   1757 C  C   . LEU   A 1 228 ? -11.159 -8.078  7.557  1.00 71.81  ? 524 LEU   A C   1 
ATOM   1758 O  O   . LEU   A 1 228 ? -10.428 -7.988  6.561  1.00 75.94  ? 524 LEU   A O   1 
ATOM   1759 C  CB  . LEU   A 1 228 ? -12.830 -6.293  7.020  1.00 68.03  ? 524 LEU   A CB  1 
ATOM   1760 C  CG  . LEU   A 1 228 ? -13.507 -4.992  7.441  1.00 65.29  ? 524 LEU   A CG  1 
ATOM   1761 C  CD1 . LEU   A 1 228 ? -14.416 -4.469  6.352  1.00 60.43  ? 524 LEU   A CD1 1 
ATOM   1762 C  CD2 . LEU   A 1 228 ? -14.252 -5.151  8.778  1.00 61.23  ? 524 LEU   A CD2 1 
ATOM   1763 N  N   . GLN   A 1 229 ? -11.392 -9.217  8.208  1.00 65.14  ? 525 GLN   A N   1 
ATOM   1764 C  CA  . GLN   A 1 229 ? -10.924 -10.527 7.773  1.00 72.47  ? 525 GLN   A CA  1 
ATOM   1765 C  C   . GLN   A 1 229 ? -12.095 -11.304 7.179  1.00 77.32  ? 525 GLN   A C   1 
ATOM   1766 O  O   . GLN   A 1 229 ? -13.140 -11.447 7.826  1.00 80.01  ? 525 GLN   A O   1 
ATOM   1767 C  CB  . GLN   A 1 229 ? -10.310 -11.299 8.943  1.00 68.58  ? 525 GLN   A CB  1 
ATOM   1768 C  CG  . GLN   A 1 229 ? -10.397 -12.813 8.816  1.00 61.45  ? 525 GLN   A CG  1 
ATOM   1769 C  CD  . GLN   A 1 229 ? -9.992  -13.535 10.089 1.00 68.80  ? 525 GLN   A CD  1 
ATOM   1770 O  OE1 . GLN   A 1 229 ? -10.094 -12.989 11.193 1.00 69.11  ? 525 GLN   A OE1 1 
ATOM   1771 N  NE2 . GLN   A 1 229 ? -9.527  -14.774 9.941  1.00 69.73  ? 525 GLN   A NE2 1 
ATOM   1772 N  N   . ALA   A 1 230 ? -11.909 -11.808 5.957  1.00 65.19  ? 526 ALA   A N   1 
ATOM   1773 C  CA  . ALA   A 1 230 ? -12.936 -12.523 5.205  1.00 70.83  ? 526 ALA   A CA  1 
ATOM   1774 C  C   . ALA   A 1 230 ? -12.467 -13.936 4.882  1.00 72.67  ? 526 ALA   A C   1 
ATOM   1775 O  O   . ALA   A 1 230 ? -11.361 -14.122 4.361  1.00 67.47  ? 526 ALA   A O   1 
ATOM   1776 C  CB  . ALA   A 1 230 ? -13.268 -11.800 3.894  1.00 70.61  ? 526 ALA   A CB  1 
ATOM   1777 N  N   . ASN   A 1 231 ? -13.329 -14.918 5.155  1.00 74.28  ? 527 ASN   A N   1 
ATOM   1778 C  CA  . ASN   A 1 231 ? -13.060 -16.336 4.903  1.00 76.58  ? 527 ASN   A CA  1 
ATOM   1779 C  C   . ASN   A 1 231 ? -11.658 -16.732 5.356  1.00 76.49  ? 527 ASN   A C   1 
ATOM   1780 O  O   . ASN   A 1 231 ? -10.865 -17.289 4.595  1.00 75.06  ? 527 ASN   A O   1 
ATOM   1781 C  CB  . ASN   A 1 231 ? -13.274 -16.689 3.430  1.00 83.83  ? 527 ASN   A CB  1 
ATOM   1782 C  CG  . ASN   A 1 231 ? -13.592 -18.159 3.230  1.00 90.33  ? 527 ASN   A CG  1 
ATOM   1783 O  OD1 . ASN   A 1 231 ? -14.376 -18.741 3.985  1.00 95.73  ? 527 ASN   A OD1 1 
ATOM   1784 N  ND2 . ASN   A 1 231 ? -12.972 -18.771 2.229  1.00 91.19  ? 527 ASN   A ND2 1 
ATOM   1785 N  N   . GLY   A 1 232 ? -11.351 -16.419 6.614  1.00 78.38  ? 528 GLY   A N   1 
ATOM   1786 C  CA  . GLY   A 1 232 ? -10.095 -16.821 7.219  1.00 86.34  ? 528 GLY   A CA  1 
ATOM   1787 C  C   . GLY   A 1 232 ? -8.849  -16.133 6.705  1.00 93.00  ? 528 GLY   A C   1 
ATOM   1788 O  O   . GLY   A 1 232 ? -7.750  -16.475 7.152  1.00 100.32 ? 528 GLY   A O   1 
ATOM   1789 N  N   . ASN   A 1 233 ? -8.977  -15.168 5.799  1.00 94.01  ? 529 ASN   A N   1 
ATOM   1790 C  CA  . ASN   A 1 233 ? -7.824  -14.529 5.178  1.00 97.06  ? 529 ASN   A CA  1 
ATOM   1791 C  C   . ASN   A 1 233 ? -7.280  -13.392 6.044  1.00 96.43  ? 529 ASN   A C   1 
ATOM   1792 O  O   . ASN   A 1 233 ? -7.928  -12.926 6.983  1.00 96.32  ? 529 ASN   A O   1 
ATOM   1793 C  CB  . ASN   A 1 233 ? -8.193  -14.013 3.786  1.00 94.21  ? 529 ASN   A CB  1 
ATOM   1794 C  CG  . ASN   A 1 233 ? -8.205  -15.117 2.735  1.00 94.39  ? 529 ASN   A CG  1 
ATOM   1795 O  OD1 . ASN   A 1 233 ? -7.239  -15.280 1.993  1.00 105.40 ? 529 ASN   A OD1 1 
ATOM   1796 N  ND2 . ASN   A 1 233 ? -9.296  -15.877 2.668  1.00 87.48  ? 529 ASN   A ND2 1 
ATOM   1797 N  N   . ASP   A 1 234 ? -6.063  -12.958 5.724  1.00 98.60  ? 530 ASP   A N   1 
ATOM   1798 C  CA  . ASP   A 1 234 ? -5.459  -11.849 6.453  1.00 100.94 ? 530 ASP   A CA  1 
ATOM   1799 C  C   . ASP   A 1 234 ? -6.343  -10.610 6.321  1.00 94.53  ? 530 ASP   A C   1 
ATOM   1800 O  O   . ASP   A 1 234 ? -6.854  -10.334 5.225  1.00 100.62 ? 530 ASP   A O   1 
ATOM   1801 C  CB  . ASP   A 1 234 ? -4.046  -11.558 5.936  1.00 107.13 ? 530 ASP   A CB  1 
ATOM   1802 C  CG  . ASP   A 1 234 ? -3.095  -12.726 6.140  1.00 118.09 ? 530 ASP   A CG  1 
ATOM   1803 O  OD1 . ASP   A 1 234 ? -1.952  -12.671 5.637  1.00 128.08 ? 530 ASP   A OD1 1 
ATOM   1804 O  OD2 . ASP   A 1 234 ? -3.493  -13.708 6.796  1.00 128.45 ? 530 ASP   A OD2 1 
ATOM   1805 N  N   . PRO   A 1 235 ? -6.569  -9.861  7.396  1.00 80.89  ? 531 PRO   A N   1 
ATOM   1806 C  CA  . PRO   A 1 235 ? -7.500  -8.731  7.330  1.00 78.25  ? 531 PRO   A CA  1 
ATOM   1807 C  C   . PRO   A 1 235 ? -6.882  -7.523  6.648  1.00 83.92  ? 531 PRO   A C   1 
ATOM   1808 O  O   . PRO   A 1 235 ? -5.667  -7.424  6.471  1.00 92.46  ? 531 PRO   A O   1 
ATOM   1809 C  CB  . PRO   A 1 235 ? -7.793  -8.437  8.807  1.00 69.57  ? 531 PRO   A CB  1 
ATOM   1810 C  CG  . PRO   A 1 235 ? -6.544  -8.819  9.474  1.00 75.62  ? 531 PRO   A CG  1 
ATOM   1811 C  CD  . PRO   A 1 235 ? -6.065  -10.055 8.771  1.00 80.05  ? 531 PRO   A CD  1 
ATOM   1812 N  N   . GLU   A 1 236 ? -7.753  -6.585  6.278  1.00 82.32  ? 532 GLU   A N   1 
ATOM   1813 C  CA  . GLU   A 1 236 ? -7.378  -5.484  5.396  1.00 89.65  ? 532 GLU   A CA  1 
ATOM   1814 C  C   . GLU   A 1 236 ? -8.076  -4.206  5.836  1.00 78.47  ? 532 GLU   A C   1 
ATOM   1815 O  O   . GLU   A 1 236 ? -9.209  -4.236  6.311  1.00 74.82  ? 532 GLU   A O   1 
ATOM   1816 C  CB  . GLU   A 1 236 ? -7.736  -5.792  3.928  1.00 92.79  ? 532 GLU   A CB  1 
ATOM   1817 C  CG  . GLU   A 1 236 ? -6.996  -6.985  3.323  1.00 101.68 ? 532 GLU   A CG  1 
ATOM   1818 C  CD  . GLU   A 1 236 ? -7.842  -7.757  2.320  1.00 106.65 ? 532 GLU   A CD  1 
ATOM   1819 O  OE1 . GLU   A 1 236 ? -8.530  -7.120  1.487  1.00 103.19 ? 532 GLU   A OE1 1 
ATOM   1820 O  OE2 . GLU   A 1 236 ? -7.822  -9.009  2.376  1.00 108.64 ? 532 GLU   A OE2 1 
ATOM   1821 N  N   . LEU   A 1 237 ? -7.404  -3.080  5.636  1.00 80.97  ? 533 LEU   A N   1 
ATOM   1822 C  CA  . LEU   A 1 237 ? -7.867  -1.806  6.168  1.00 81.38  ? 533 LEU   A CA  1 
ATOM   1823 C  C   . LEU   A 1 237 ? -8.806  -1.093  5.207  1.00 83.06  ? 533 LEU   A C   1 
ATOM   1824 O  O   . LEU   A 1 237 ? -8.540  -1.009  4.007  1.00 90.29  ? 533 LEU   A O   1 
ATOM   1825 C  CB  . LEU   A 1 237 ? -6.674  -0.907  6.481  1.00 85.51  ? 533 LEU   A CB  1 
ATOM   1826 C  CG  . LEU   A 1 237 ? -5.952  -1.311  7.765  1.00 91.91  ? 533 LEU   A CG  1 
ATOM   1827 C  CD1 . LEU   A 1 237 ? -4.610  -0.617  7.829  1.00 103.13 ? 533 LEU   A CD1 1 
ATOM   1828 C  CD2 . LEU   A 1 237 ? -6.800  -0.985  8.984  1.00 82.75  ? 533 LEU   A CD2 1 
ATOM   1829 N  N   . PHE   A 1 238 ? -9.903  -0.570  5.751  1.00 79.64  ? 534 PHE   A N   1 
ATOM   1830 C  CA  . PHE   A 1 238 ? -10.829 0.270   5.003  1.00 84.09  ? 534 PHE   A CA  1 
ATOM   1831 C  C   . PHE   A 1 238 ? -11.359 1.350   5.932  1.00 82.52  ? 534 PHE   A C   1 
ATOM   1832 O  O   . PHE   A 1 238 ? -11.810 1.045   7.041  1.00 76.39  ? 534 PHE   A O   1 
ATOM   1833 C  CB  . PHE   A 1 238 ? -12.010 -0.525  4.438  1.00 77.75  ? 534 PHE   A CB  1 
ATOM   1834 C  CG  . PHE   A 1 238 ? -11.637 -1.846  3.852  1.00 82.73  ? 534 PHE   A CG  1 
ATOM   1835 C  CD1 . PHE   A 1 238 ? -11.554 -2.976  4.652  1.00 88.31  ? 534 PHE   A CD1 1 
ATOM   1836 C  CD2 . PHE   A 1 238 ? -11.391 -1.970  2.496  1.00 80.90  ? 534 PHE   A CD2 1 
ATOM   1837 C  CE1 . PHE   A 1 238 ? -11.218 -4.207  4.104  1.00 91.01  ? 534 PHE   A CE1 1 
ATOM   1838 C  CE2 . PHE   A 1 238 ? -11.055 -3.191  1.950  1.00 83.73  ? 534 PHE   A CE2 1 
ATOM   1839 C  CZ  . PHE   A 1 238 ? -10.971 -4.312  2.748  1.00 80.31  ? 534 PHE   A CZ  1 
ATOM   1840 N  N   . GLN   A 1 239 ? -11.344 2.594   5.461  1.00 89.36  ? 535 GLN   A N   1 
ATOM   1841 C  CA  . GLN   A 1 239 ? -11.817 3.734   6.237  1.00 92.49  ? 535 GLN   A CA  1 
ATOM   1842 C  C   . GLN   A 1 239 ? -13.244 4.082   5.822  1.00 89.10  ? 535 GLN   A C   1 
ATOM   1843 O  O   . GLN   A 1 239 ? -13.479 4.531   4.693  1.00 96.18  ? 535 GLN   A O   1 
ATOM   1844 C  CB  . GLN   A 1 239 ? -10.893 4.933   6.047  1.00 108.25 ? 535 GLN   A CB  1 
ATOM   1845 C  CG  . GLN   A 1 239 ? -11.459 6.231   6.590  1.00 116.39 ? 535 GLN   A CG  1 
ATOM   1846 C  CD  . GLN   A 1 239 ? -11.383 7.360   5.581  1.00 119.36 ? 535 GLN   A CD  1 
ATOM   1847 O  OE1 . GLN   A 1 239 ? -12.400 7.939   5.207  1.00 118.45 ? 535 GLN   A OE1 1 
ATOM   1848 N  NE2 . GLN   A 1 239 ? -10.174 7.679   5.136  1.00 123.42 ? 535 GLN   A NE2 1 
ATOM   1849 N  N   . ILE   A 1 240 ? -14.182 3.874   6.741  1.00 89.57  ? 536 ILE   A N   1 
ATOM   1850 C  CA  . ILE   A 1 240 ? -15.568 4.344   6.683  1.00 86.32  ? 536 ILE   A CA  1 
ATOM   1851 C  C   . ILE   A 1 240 ? -15.589 5.774   6.161  1.00 92.39  ? 536 ILE   A C   1 
ATOM   1852 O  O   . ILE   A 1 240 ? -14.912 6.636   6.740  1.00 94.40  ? 536 ILE   A O   1 
ATOM   1853 C  CB  . ILE   A 1 240 ? -16.228 4.282   8.075  1.00 74.94  ? 536 ILE   A CB  1 
ATOM   1854 C  CG1 . ILE   A 1 240 ? -16.102 2.883   8.681  1.00 75.20  ? 536 ILE   A CG1 1 
ATOM   1855 C  CG2 . ILE   A 1 240 ? -17.683 4.731   8.017  1.00 62.11  ? 536 ILE   A CG2 1 
ATOM   1856 C  CD1 . ILE   A 1 240 ? -15.163 2.837   9.883  1.00 83.19  ? 536 ILE   A CD1 1 
ATOM   1857 N  N   . PRO   A 1 241 ? -16.330 6.084   5.097  1.00 84.27  ? 537 PRO   A N   1 
ATOM   1858 C  CA  . PRO   A 1 241 ? -16.350 7.463   4.601  1.00 95.39  ? 537 PRO   A CA  1 
ATOM   1859 C  C   . PRO   A 1 241 ? -16.827 8.407   5.689  1.00 84.83  ? 537 PRO   A C   1 
ATOM   1860 O  O   . PRO   A 1 241 ? -17.866 8.170   6.327  1.00 82.34  ? 537 PRO   A O   1 
ATOM   1861 C  CB  . PRO   A 1 241 ? -17.322 7.412   3.406  1.00 97.65  ? 537 PRO   A CB  1 
ATOM   1862 C  CG  . PRO   A 1 241 ? -17.355 5.967   3.010  1.00 93.92  ? 537 PRO   A CG  1 
ATOM   1863 C  CD  . PRO   A 1 241 ? -17.211 5.209   4.308  1.00 86.39  ? 537 PRO   A CD  1 
ATOM   1864 N  N   . PRO   A 1 242 ? -16.063 9.465   5.949  1.00 86.29  ? 538 PRO   A N   1 
ATOM   1865 C  CA  . PRO   A 1 242 ? -16.336 10.311  7.123  1.00 83.19  ? 538 PRO   A CA  1 
ATOM   1866 C  C   . PRO   A 1 242 ? -17.748 10.843  7.159  1.00 89.58  ? 538 PRO   A C   1 
ATOM   1867 O  O   . PRO   A 1 242 ? -18.323 10.975  8.242  1.00 78.14  ? 538 PRO   A O   1 
ATOM   1868 C  CB  . PRO   A 1 242 ? -15.317 11.444  6.966  1.00 86.62  ? 538 PRO   A CB  1 
ATOM   1869 C  CG  . PRO   A 1 242 ? -14.213 10.847  6.156  1.00 87.14  ? 538 PRO   A CG  1 
ATOM   1870 C  CD  . PRO   A 1 242 ? -14.886 9.917   5.194  1.00 86.93  ? 538 PRO   A CD  1 
ATOM   1871 N  N   . GLU   A 1 243 ? -18.337 11.124  5.995  1.00 86.38  ? 539 GLU   A N   1 
ATOM   1872 C  CA  . GLU   A 1 243 ? -19.713 11.599  5.953  1.00 88.99  ? 539 GLU   A CA  1 
ATOM   1873 C  C   . GLU   A 1 243 ? -20.682 10.595  6.564  1.00 85.85  ? 539 GLU   A C   1 
ATOM   1874 O  O   . GLU   A 1 243 ? -21.766 10.988  7.010  1.00 84.42  ? 539 GLU   A O   1 
ATOM   1875 C  CB  . GLU   A 1 243 ? -20.114 11.916  4.502  1.00 94.17  ? 539 GLU   A CB  1 
ATOM   1876 C  CG  . GLU   A 1 243 ? -20.159 10.704  3.579  1.00 95.12  ? 539 GLU   A CG  1 
ATOM   1877 C  CD  . GLU   A 1 243 ? -18.917 10.558  2.696  1.00 96.57  ? 539 GLU   A CD  1 
ATOM   1878 O  OE1 . GLU   A 1 243 ? -17.794 10.760  3.219  1.00 91.62  ? 539 GLU   A OE1 1 
ATOM   1879 O  OE2 . GLU   A 1 243 ? -19.065 10.247  1.478  1.00 93.37  ? 539 GLU   A OE2 1 
ATOM   1880 N  N   . LEU   A 1 244 ? -20.300 9.316   6.619  1.00 75.31  ? 540 LEU   A N   1 
ATOM   1881 C  CA  . LEU   A 1 244 ? -21.109 8.275   7.235  1.00 76.25  ? 540 LEU   A CA  1 
ATOM   1882 C  C   . LEU   A 1 244 ? -20.928 8.178   8.744  1.00 69.58  ? 540 LEU   A C   1 
ATOM   1883 O  O   . LEU   A 1 244 ? -21.722 7.492   9.404  1.00 65.34  ? 540 LEU   A O   1 
ATOM   1884 C  CB  . LEU   A 1 244 ? -20.765 6.920   6.622  1.00 75.27  ? 540 LEU   A CB  1 
ATOM   1885 C  CG  . LEU   A 1 244 ? -21.194 6.760   5.155  1.00 72.26  ? 540 LEU   A CG  1 
ATOM   1886 C  CD1 . LEU   A 1 244 ? -20.853 5.370   4.682  1.00 68.92  ? 540 LEU   A CD1 1 
ATOM   1887 C  CD2 . LEU   A 1 244 ? -22.683 7.018   5.085  1.00 69.32  ? 540 LEU   A CD2 1 
ATOM   1888 N  N   . VAL   A 1 245 ? -19.913 8.822   9.310  1.00 81.74  ? 541 VAL   A N   1 
ATOM   1889 C  CA  . VAL   A 1 245 ? -19.658 8.755   10.750 1.00 78.58  ? 541 VAL   A CA  1 
ATOM   1890 C  C   . VAL   A 1 245 ? -20.244 10.019  11.369 1.00 76.53  ? 541 VAL   A C   1 
ATOM   1891 O  O   . VAL   A 1 245 ? -19.677 11.110  11.254 1.00 81.07  ? 541 VAL   A O   1 
ATOM   1892 C  CB  . VAL   A 1 245 ? -18.170 8.596   11.069 1.00 81.62  ? 541 VAL   A CB  1 
ATOM   1893 C  CG1 . VAL   A 1 245 ? -17.932 8.617   12.614 1.00 76.61  ? 541 VAL   A CG1 1 
ATOM   1894 C  CG2 . VAL   A 1 245 ? -17.668 7.307   10.482 1.00 76.88  ? 541 VAL   A CG2 1 
ATOM   1895 N  N   . LEU   A 1 246 ? -21.392 9.863   12.023 1.00 75.57  ? 542 LEU   A N   1 
ATOM   1896 C  CA  . LEU   A 1 246 ? -22.073 10.974  12.661 1.00 78.49  ? 542 LEU   A CA  1 
ATOM   1897 C  C   . LEU   A 1 246 ? -21.498 11.180  14.057 1.00 71.42  ? 542 LEU   A C   1 
ATOM   1898 O  O   . LEU   A 1 246 ? -21.366 10.228  14.829 1.00 74.13  ? 542 LEU   A O   1 
ATOM   1899 C  CB  . LEU   A 1 246 ? -23.574 10.701  12.743 1.00 74.84  ? 542 LEU   A CB  1 
ATOM   1900 C  CG  . LEU   A 1 246 ? -24.391 11.640  13.646 1.00 75.95  ? 542 LEU   A CG  1 
ATOM   1901 C  CD1 . LEU   A 1 246 ? -24.570 13.015  13.021 1.00 77.29  ? 542 LEU   A CD1 1 
ATOM   1902 C  CD2 . LEU   A 1 246 ? -25.742 10.998  13.985 1.00 76.11  ? 542 LEU   A CD2 1 
ATOM   1903 N  N   . GLU   A 1 247 ? -21.151 12.418  14.370 1.00 82.96  ? 543 GLU   A N   1 
ATOM   1904 C  CA  . GLU   A 1 247 ? -20.630 12.772  15.681 1.00 90.46  ? 543 GLU   A CA  1 
ATOM   1905 C  C   . GLU   A 1 247 ? -21.451 13.914  16.270 1.00 94.81  ? 543 GLU   A C   1 
ATOM   1906 O  O   . GLU   A 1 247 ? -22.014 14.740  15.540 1.00 94.78  ? 543 GLU   A O   1 
ATOM   1907 C  CB  . GLU   A 1 247 ? -19.143 13.147  15.587 1.00 97.86  ? 543 GLU   A CB  1 
ATOM   1908 C  CG  . GLU   A 1 247 ? -18.264 12.018  15.048 1.00 94.43  ? 543 GLU   A CG  1 
ATOM   1909 C  CD  . GLU   A 1 247 ? -16.835 12.457  14.790 1.00 106.01 ? 543 GLU   A CD  1 
ATOM   1910 O  OE1 . GLU   A 1 247 ? -16.623 13.622  14.387 1.00 111.39 ? 543 GLU   A OE1 1 
ATOM   1911 O  OE2 . GLU   A 1 247 ? -15.919 11.640  15.001 1.00 106.11 ? 543 GLU   A OE2 1 
ATOM   1912 N  N   . VAL   A 1 248 ? -21.513 13.944  17.600 1.00 92.10  ? 544 VAL   A N   1 
ATOM   1913 C  CA  . VAL   A 1 248 ? -22.294 14.905  18.370 1.00 96.58  ? 544 VAL   A CA  1 
ATOM   1914 C  C   . VAL   A 1 248 ? -21.328 15.715  19.225 1.00 101.02 ? 544 VAL   A C   1 
ATOM   1915 O  O   . VAL   A 1 248 ? -20.605 15.141  20.048 1.00 86.25  ? 544 VAL   A O   1 
ATOM   1916 C  CB  . VAL   A 1 248 ? -23.344 14.223  19.265 1.00 94.80  ? 544 VAL   A CB  1 
ATOM   1917 C  CG1 . VAL   A 1 248 ? -23.929 15.240  20.263 1.00 101.20 ? 544 VAL   A CG1 1 
ATOM   1918 C  CG2 . VAL   A 1 248 ? -24.443 13.580  18.428 1.00 93.12  ? 544 VAL   A CG2 1 
ATOM   1919 N  N   . PRO   A 1 249 ? -21.278 17.042  19.064 1.00 103.67 ? 545 PRO   A N   1 
ATOM   1920 C  CA  . PRO   A 1 249 ? -20.411 17.877  19.908 1.00 104.18 ? 545 PRO   A CA  1 
ATOM   1921 C  C   . PRO   A 1 249 ? -21.082 18.157  21.245 1.00 109.60 ? 545 PRO   A C   1 
ATOM   1922 O  O   . PRO   A 1 249 ? -22.240 18.582  21.294 1.00 111.73 ? 545 PRO   A O   1 
ATOM   1923 C  CB  . PRO   A 1 249 ? -20.252 19.163  19.084 1.00 107.17 ? 545 PRO   A CB  1 
ATOM   1924 C  CG  . PRO   A 1 249 ? -21.530 19.244  18.310 1.00 111.05 ? 545 PRO   A CG  1 
ATOM   1925 C  CD  . PRO   A 1 249 ? -21.924 17.824  17.987 1.00 107.25 ? 545 PRO   A CD  1 
ATOM   1926 N  N   . ILE   A 1 250 ? -20.348 17.926  22.333 1.00 111.27 ? 546 ILE   A N   1 
ATOM   1927 C  CA  . ILE   A 1 250 ? -20.919 17.996  23.673 1.00 100.27 ? 546 ILE   A CA  1 
ATOM   1928 C  C   . ILE   A 1 250 ? -20.826 19.420  24.210 1.00 109.58 ? 546 ILE   A C   1 
ATOM   1929 O  O   . ILE   A 1 250 ? -19.727 19.953  24.420 1.00 110.12 ? 546 ILE   A O   1 
ATOM   1930 C  CB  . ILE   A 1 250 ? -20.237 17.007  24.634 1.00 99.06  ? 546 ILE   A CB  1 
ATOM   1931 C  CG1 . ILE   A 1 250 ? -19.977 15.647  23.952 1.00 90.75  ? 546 ILE   A CG1 1 
ATOM   1932 C  CG2 . ILE   A 1 250 ? -21.079 16.860  25.892 1.00 99.83  ? 546 ILE   A CG2 1 
ATOM   1933 C  CD1 . ILE   A 1 250 ? -21.185 15.034  23.255 1.00 86.24  ? 546 ILE   A CD1 1 
ATOM   1934 N  N   . ARG   A 1 251 ? -21.987 20.015  24.486 1.00 116.74 ? 547 ARG   A N   1 
ATOM   1935 C  CA  . ARG   A 1 251 ? -22.096 21.291  25.179 1.00 123.15 ? 547 ARG   A CA  1 
ATOM   1936 C  C   . ARG   A 1 251 ? -23.068 21.151  26.344 1.00 121.50 ? 547 ARG   A C   1 
ATOM   1937 O  O   . ARG   A 1 251 ? -23.913 20.254  26.362 1.00 123.02 ? 547 ARG   A O   1 
ATOM   1938 C  CB  . ARG   A 1 251 ? -22.577 22.410  24.239 1.00 128.42 ? 547 ARG   A CB  1 
ATOM   1939 C  CG  . ARG   A 1 251 ? -24.032 22.277  23.742 1.00 129.53 ? 547 ARG   A CG  1 
ATOM   1940 C  CD  . ARG   A 1 251 ? -24.181 21.369  22.488 1.00 128.68 ? 547 ARG   A CD  1 
ATOM   1941 N  NE  . ARG   A 1 251 ? -25.349 21.715  21.672 1.00 123.05 ? 547 ARG   A NE  1 
ATOM   1942 C  CZ  . ARG   A 1 251 ? -25.823 20.977  20.672 1.00 119.46 ? 547 ARG   A CZ  1 
ATOM   1943 N  NH1 . ARG   A 1 251 ? -26.884 21.393  19.992 1.00 121.89 ? 547 ARG   A NH1 1 
ATOM   1944 N  NH2 . ARG   A 1 251 ? -25.244 19.827  20.346 1.00 106.35 ? 547 ARG   A NH2 1 
ATOM   1945 N  N   . HIS   A 1 252 ? -22.955 22.063  27.321 1.00 120.22 ? 548 HIS   A N   1 
ATOM   1946 C  CA  . HIS   A 1 252 ? -23.879 22.091  28.444 1.00 122.53 ? 548 HIS   A CA  1 
ATOM   1947 C  C   . HIS   A 1 252 ? -24.913 23.192  28.271 1.00 127.73 ? 548 HIS   A C   1 
ATOM   1948 O  O   . HIS   A 1 252 ? -24.651 24.210  27.621 1.00 131.46 ? 548 HIS   A O   1 
ATOM   1949 C  CB  . HIS   A 1 252 ? -23.130 22.295  29.765 1.00 121.23 ? 548 HIS   A CB  1 
ATOM   1950 C  CG  . HIS   A 1 252 ? -23.888 21.796  30.957 1.00 126.32 ? 548 HIS   A CG  1 
ATOM   1951 N  ND1 . HIS   A 1 252 ? -24.698 22.604  31.730 1.00 130.30 ? 548 HIS   A ND1 1 
ATOM   1952 C  CD2 . HIS   A 1 252 ? -23.984 20.554  31.489 1.00 120.35 ? 548 HIS   A CD2 1 
ATOM   1953 C  CE1 . HIS   A 1 252 ? -25.249 21.882  32.690 1.00 123.62 ? 548 HIS   A CE1 1 
ATOM   1954 N  NE2 . HIS   A 1 252 ? -24.836 20.634  32.560 1.00 118.36 ? 548 HIS   A NE2 1 
ATOM   1955 N  N   . PRO   A 1 253 ? -26.117 23.010  28.833 1.00 129.22 ? 549 PRO   A N   1 
ATOM   1956 C  CA  . PRO   A 1 253 ? -27.127 24.079  28.774 1.00 132.65 ? 549 PRO   A CA  1 
ATOM   1957 C  C   . PRO   A 1 253 ? -26.835 25.273  29.667 1.00 141.69 ? 549 PRO   A C   1 
ATOM   1958 O  O   . PRO   A 1 253 ? -27.534 26.292  29.559 1.00 145.23 ? 549 PRO   A O   1 
ATOM   1959 C  CB  . PRO   A 1 253 ? -28.420 23.371  29.224 1.00 127.56 ? 549 PRO   A CB  1 
ATOM   1960 C  CG  . PRO   A 1 253 ? -27.967 22.183  29.974 1.00 120.70 ? 549 PRO   A CG  1 
ATOM   1961 C  CD  . PRO   A 1 253 ? -26.689 21.748  29.336 1.00 117.61 ? 549 PRO   A CD  1 
ATOM   1962 N  N   . LYS   A 1 254 ? -25.838 25.183  30.546 1.00 147.26 ? 550 LYS   A N   1 
ATOM   1963 C  CA  . LYS   A 1 254 ? -25.536 26.270  31.467 1.00 145.43 ? 550 LYS   A CA  1 
ATOM   1964 C  C   . LYS   A 1 254 ? -24.082 26.705  31.347 1.00 148.35 ? 550 LYS   A C   1 
ATOM   1965 O  O   . LYS   A 1 254 ? -23.793 27.889  31.157 1.00 156.17 ? 550 LYS   A O   1 
ATOM   1966 C  CB  . LYS   A 1 254 ? -25.835 25.844  32.901 1.00 147.44 ? 550 LYS   A CB  1 
ATOM   1967 C  CG  . LYS   A 1 254 ? -27.106 25.035  33.061 1.00 143.68 ? 550 LYS   A CG  1 
ATOM   1968 C  CD  . LYS   A 1 254 ? -28.344 25.887  32.881 1.00 146.38 ? 550 LYS   A CD  1 
ATOM   1969 C  CE  . LYS   A 1 254 ? -29.595 25.083  33.179 1.00 142.56 ? 550 LYS   A CE  1 
ATOM   1970 N  NZ  . LYS   A 1 254 ? -30.817 25.933  33.206 1.00 149.24 ? 550 LYS   A NZ  1 
ATOM   1971 N  N   . PHE   A 1 255 ? -23.163 25.752  31.452 1.00 142.60 ? 551 PHE   A N   1 
ATOM   1972 C  CA  . PHE   A 1 255 ? -21.733 26.047  31.524 1.00 145.29 ? 551 PHE   A CA  1 
ATOM   1973 C  C   . PHE   A 1 255 ? -21.182 26.258  30.118 1.00 151.58 ? 551 PHE   A C   1 
ATOM   1974 O  O   . PHE   A 1 255 ? -20.836 25.310  29.414 1.00 140.63 ? 551 PHE   A O   1 
ATOM   1975 C  CB  . PHE   A 1 255 ? -21.007 24.922  32.250 1.00 146.21 ? 551 PHE   A CB  1 
ATOM   1976 C  CG  . PHE   A 1 255 ? -21.628 24.555  33.582 1.00 147.63 ? 551 PHE   A CG  1 
ATOM   1977 C  CD1 . PHE   A 1 255 ? -22.382 23.401  33.719 1.00 142.27 ? 551 PHE   A CD1 1 
ATOM   1978 C  CD2 . PHE   A 1 255 ? -21.467 25.370  34.686 1.00 142.63 ? 551 PHE   A CD2 1 
ATOM   1979 C  CE1 . PHE   A 1 255 ? -22.955 23.065  34.941 1.00 136.76 ? 551 PHE   A CE1 1 
ATOM   1980 C  CE2 . PHE   A 1 255 ? -22.041 25.038  35.912 1.00 143.03 ? 551 PHE   A CE2 1 
ATOM   1981 C  CZ  . PHE   A 1 255 ? -22.785 23.885  36.030 1.00 137.97 ? 551 PHE   A CZ  1 
ATOM   1982 N  N   . ASP   A 1 256 ? -21.087 27.522  29.695 1.00 161.09 ? 552 ASP   A N   1 
ATOM   1983 C  CA  . ASP   A 1 256 ? -20.592 27.801  28.349 1.00 165.26 ? 552 ASP   A CA  1 
ATOM   1984 C  C   . ASP   A 1 256 ? -19.100 27.531  28.202 1.00 160.94 ? 552 ASP   A C   1 
ATOM   1985 O  O   . ASP   A 1 256 ? -18.608 27.484  27.072 1.00 160.71 ? 552 ASP   A O   1 
ATOM   1986 C  CB  . ASP   A 1 256 ? -20.905 29.244  27.947 1.00 180.18 ? 552 ASP   A CB  1 
ATOM   1987 C  CG  . ASP   A 1 256 ? -22.229 29.367  27.207 1.00 184.94 ? 552 ASP   A CG  1 
ATOM   1988 O  OD1 . ASP   A 1 256 ? -23.258 29.629  27.866 1.00 186.70 ? 552 ASP   A OD1 1 
ATOM   1989 O  OD2 . ASP   A 1 256 ? -22.241 29.189  25.966 1.00 184.74 ? 552 ASP   A OD2 1 
ATOM   1990 N  N   . TRP   A 1 257 ? -18.369 27.345  29.302 1.00 159.47 ? 553 TRP   A N   1 
ATOM   1991 C  CA  . TRP   A 1 257 ? -17.008 26.838  29.177 1.00 157.40 ? 553 TRP   A CA  1 
ATOM   1992 C  C   . TRP   A 1 257 ? -16.969 25.368  28.791 1.00 145.56 ? 553 TRP   A C   1 
ATOM   1993 O  O   . TRP   A 1 257 ? -15.876 24.799  28.682 1.00 143.83 ? 553 TRP   A O   1 
ATOM   1994 C  CB  . TRP   A 1 257 ? -16.248 27.041  30.481 1.00 157.87 ? 553 TRP   A CB  1 
ATOM   1995 C  CG  . TRP   A 1 257 ? -16.999 26.535  31.676 1.00 158.35 ? 553 TRP   A CG  1 
ATOM   1996 C  CD1 . TRP   A 1 257 ? -17.832 27.256  32.481 1.00 161.39 ? 553 TRP   A CD1 1 
ATOM   1997 C  CD2 . TRP   A 1 257 ? -16.998 25.197  32.197 1.00 147.50 ? 553 TRP   A CD2 1 
ATOM   1998 N  NE1 . TRP   A 1 257 ? -18.344 26.454  33.473 1.00 155.31 ? 553 TRP   A NE1 1 
ATOM   1999 C  CE2 . TRP   A 1 257 ? -17.847 25.186  33.321 1.00 147.66 ? 553 TRP   A CE2 1 
ATOM   2000 C  CE3 . TRP   A 1 257 ? -16.362 24.010  31.823 1.00 139.04 ? 553 TRP   A CE3 1 
ATOM   2001 C  CZ2 . TRP   A 1 257 ? -18.076 24.038  34.071 1.00 137.56 ? 553 TRP   A CZ2 1 
ATOM   2002 C  CZ3 . TRP   A 1 257 ? -16.593 22.867  32.579 1.00 132.15 ? 553 TRP   A CZ3 1 
ATOM   2003 C  CH2 . TRP   A 1 257 ? -17.439 22.894  33.685 1.00 135.23 ? 553 TRP   A CH2 1 
ATOM   2004 N  N   . PHE   A 1 258 ? -18.129 24.741  28.597 1.00 140.13 ? 554 PHE   A N   1 
ATOM   2005 C  CA  . PHE   A 1 258 ? -18.154 23.324  28.256 1.00 138.08 ? 554 PHE   A CA  1 
ATOM   2006 C  C   . PHE   A 1 258 ? -17.553 23.070  26.881 1.00 133.34 ? 554 PHE   A C   1 
ATOM   2007 O  O   . PHE   A 1 258 ? -16.790 22.115  26.706 1.00 129.47 ? 554 PHE   A O   1 
ATOM   2008 C  CB  . PHE   A 1 258 ? -19.580 22.790  28.314 1.00 134.84 ? 554 PHE   A CB  1 
ATOM   2009 C  CG  . PHE   A 1 258 ? -19.688 21.496  29.020 1.00 119.19 ? 554 PHE   A CG  1 
ATOM   2010 C  CD1 . PHE   A 1 258 ? -19.795 21.465  30.390 1.00 123.61 ? 554 PHE   A CD1 1 
ATOM   2011 C  CD2 . PHE   A 1 258 ? -19.652 20.301  28.319 1.00 116.27 ? 554 PHE   A CD2 1 
ATOM   2012 C  CE1 . PHE   A 1 258 ? -19.873 20.262  31.077 1.00 114.08 ? 554 PHE   A CE1 1 
ATOM   2013 C  CE2 . PHE   A 1 258 ? -19.735 19.087  28.981 1.00 113.21 ? 554 PHE   A CE2 1 
ATOM   2014 C  CZ  . PHE   A 1 258 ? -19.844 19.070  30.380 1.00 107.18 ? 554 PHE   A CZ  1 
ATOM   2015 N  N   . LYS   A 1 259 ? -17.881 23.906  25.895 1.00 134.81 ? 555 LYS   A N   1 
ATOM   2016 C  CA  . LYS   A 1 259 ? -17.375 23.671  24.544 1.00 135.27 ? 555 LYS   A CA  1 
ATOM   2017 C  C   . LYS   A 1 259 ? -15.851 23.696  24.517 1.00 140.16 ? 555 LYS   A C   1 
ATOM   2018 O  O   . LYS   A 1 259 ? -15.223 22.910  23.797 1.00 133.38 ? 555 LYS   A O   1 
ATOM   2019 C  CB  . LYS   A 1 259 ? -17.958 24.701  23.571 1.00 144.19 ? 555 LYS   A CB  1 
ATOM   2020 C  CG  . LYS   A 1 259 ? -18.760 25.806  24.247 1.00 153.78 ? 555 LYS   A CG  1 
ATOM   2021 C  CD  . LYS   A 1 259 ? -19.597 26.604  23.257 1.00 160.17 ? 555 LYS   A CD  1 
ATOM   2022 C  CE  . LYS   A 1 259 ? -20.761 27.260  23.975 1.00 162.29 ? 555 LYS   A CE  1 
ATOM   2023 N  NZ  . LYS   A 1 259 ? -21.541 26.233  24.731 1.00 145.09 ? 555 LYS   A NZ  1 
ATOM   2024 N  N   . ASP   A 1 260 ? -15.237 24.567  25.326 1.00 147.56 ? 556 ASP   A N   1 
ATOM   2025 C  CA  . ASP   A 1 260 ? -13.781 24.678  25.345 1.00 149.98 ? 556 ASP   A CA  1 
ATOM   2026 C  C   . ASP   A 1 260 ? -13.127 23.357  25.729 1.00 141.66 ? 556 ASP   A C   1 
ATOM   2027 O  O   . ASP   A 1 260 ? -12.013 23.062  25.275 1.00 141.36 ? 556 ASP   A O   1 
ATOM   2028 C  CB  . ASP   A 1 260 ? -13.356 25.794  26.301 1.00 157.83 ? 556 ASP   A CB  1 
ATOM   2029 C  CG  . ASP   A 1 260 ? -13.948 27.150  25.921 1.00 164.47 ? 556 ASP   A CG  1 
ATOM   2030 O  OD1 . ASP   A 1 260 ? -14.634 27.235  24.883 1.00 161.29 ? 556 ASP   A OD1 1 
ATOM   2031 O  OD2 . ASP   A 1 260 ? -13.733 28.132  26.668 1.00 172.70 ? 556 ASP   A OD2 1 
ATOM   2032 N  N   . LEU   A 1 261 ? -13.810 22.553  26.554 1.00 140.82 ? 557 LEU   A N   1 
ATOM   2033 C  CA  . LEU   A 1 261 ? -13.382 21.180  26.811 1.00 135.17 ? 557 LEU   A CA  1 
ATOM   2034 C  C   . LEU   A 1 261 ? -13.158 20.414  25.514 1.00 139.13 ? 557 LEU   A C   1 
ATOM   2035 O  O   . LEU   A 1 261 ? -12.307 19.520  25.461 1.00 141.23 ? 557 LEU   A O   1 
ATOM   2036 C  CB  . LEU   A 1 261 ? -14.415 20.453  27.677 1.00 123.60 ? 557 LEU   A CB  1 
ATOM   2037 C  CG  . LEU   A 1 261 ? -14.555 20.873  29.147 1.00 128.67 ? 557 LEU   A CG  1 
ATOM   2038 C  CD1 . LEU   A 1 261 ? -15.671 20.093  29.857 1.00 122.46 ? 557 LEU   A CD1 1 
ATOM   2039 C  CD2 . LEU   A 1 261 ? -13.236 20.687  29.884 1.00 125.84 ? 557 LEU   A CD2 1 
ATOM   2040 N  N   . GLY   A 1 262 ? -13.908 20.740  24.467 1.00 134.69 ? 558 GLY   A N   1 
ATOM   2041 C  CA  . GLY   A 1 262 ? -13.625 20.206  23.148 1.00 137.88 ? 558 GLY   A CA  1 
ATOM   2042 C  C   . GLY   A 1 262 ? -13.886 18.725  22.985 1.00 129.65 ? 558 GLY   A C   1 
ATOM   2043 O  O   . GLY   A 1 262 ? -13.127 18.042  22.284 1.00 129.73 ? 558 GLY   A O   1 
ATOM   2044 N  N   . LEU   A 1 263 ? -14.949 18.212  23.598 1.00 122.58 ? 559 LEU   A N   1 
ATOM   2045 C  CA  . LEU   A 1 263 ? -15.267 16.795  23.533 1.00 113.16 ? 559 LEU   A CA  1 
ATOM   2046 C  C   . LEU   A 1 263 ? -16.404 16.540  22.549 1.00 107.73 ? 559 LEU   A C   1 
ATOM   2047 O  O   . LEU   A 1 263 ? -17.149 17.449  22.173 1.00 101.03 ? 559 LEU   A O   1 
ATOM   2048 C  CB  . LEU   A 1 263 ? -15.620 16.264  24.927 1.00 106.54 ? 559 LEU   A CB  1 
ATOM   2049 C  CG  . LEU   A 1 263 ? -14.502 16.538  25.935 1.00 106.65 ? 559 LEU   A CG  1 
ATOM   2050 C  CD1 . LEU   A 1 263 ? -15.010 16.410  27.353 1.00 99.74  ? 559 LEU   A CD1 1 
ATOM   2051 C  CD2 . LEU   A 1 263 ? -13.303 15.624  25.708 1.00 99.61  ? 559 LEU   A CD2 1 
ATOM   2052 N  N   . LYS   A 1 264 ? -16.528 15.277  22.145 1.00 105.46 ? 560 LYS   A N   1 
ATOM   2053 C  CA  . LYS   A 1 264 ? -17.492 14.838  21.144 1.00 104.56 ? 560 LYS   A CA  1 
ATOM   2054 C  C   . LYS   A 1 264 ? -17.504 13.319  21.112 1.00 102.49 ? 560 LYS   A C   1 
ATOM   2055 O  O   . LYS   A 1 264 ? -16.509 12.674  21.457 1.00 104.02 ? 560 LYS   A O   1 
ATOM   2056 C  CB  . LYS   A 1 264 ? -17.157 15.377  19.747 1.00 103.44 ? 560 LYS   A CB  1 
ATOM   2057 C  CG  . LYS   A 1 264 ? -15.804 14.913  19.206 1.00 104.51 ? 560 LYS   A CG  1 
ATOM   2058 C  CD  . LYS   A 1 264 ? -15.736 15.023  17.667 1.00 114.04 ? 560 LYS   A CD  1 
ATOM   2059 C  CE  . LYS   A 1 264 ? -14.294 15.092  17.138 1.00 116.97 ? 560 LYS   A CE  1 
ATOM   2060 N  NZ  . LYS   A 1 264 ? -14.208 15.351  15.666 1.00 115.19 ? 560 LYS   A NZ  1 
ATOM   2061 N  N   . TRP   A 1 265 ? -18.630 12.760  20.675 1.00 93.88  ? 561 TRP   A N   1 
ATOM   2062 C  CA  . TRP   A 1 265 ? -18.792 11.314  20.615 1.00 86.81  ? 561 TRP   A CA  1 
ATOM   2063 C  C   . TRP   A 1 265 ? -19.586 10.956  19.366 1.00 87.29  ? 561 TRP   A C   1 
ATOM   2064 O  O   . TRP   A 1 265 ? -20.334 11.780  18.829 1.00 92.64  ? 561 TRP   A O   1 
ATOM   2065 C  CB  . TRP   A 1 265 ? -19.489 10.753  21.864 1.00 79.25  ? 561 TRP   A CB  1 
ATOM   2066 C  CG  . TRP   A 1 265 ? -19.158 9.315   22.103 1.00 77.48  ? 561 TRP   A CG  1 
ATOM   2067 C  CD1 . TRP   A 1 265 ? -19.983 8.230   21.935 1.00 79.07  ? 561 TRP   A CD1 1 
ATOM   2068 C  CD2 . TRP   A 1 265 ? -17.898 8.795   22.531 1.00 80.64  ? 561 TRP   A CD2 1 
ATOM   2069 N  NE1 . TRP   A 1 265 ? -19.312 7.068   22.246 1.00 73.85  ? 561 TRP   A NE1 1 
ATOM   2070 C  CE2 . TRP   A 1 265 ? -18.030 7.387   22.617 1.00 77.35  ? 561 TRP   A CE2 1 
ATOM   2071 C  CE3 . TRP   A 1 265 ? -16.670 9.382   22.856 1.00 77.36  ? 561 TRP   A CE3 1 
ATOM   2072 C  CZ2 . TRP   A 1 265 ? -16.976 6.557   23.013 1.00 66.09  ? 561 TRP   A CZ2 1 
ATOM   2073 C  CZ3 . TRP   A 1 265 ? -15.625 8.557   23.248 1.00 76.90  ? 561 TRP   A CZ3 1 
ATOM   2074 C  CH2 . TRP   A 1 265 ? -15.789 7.158   23.331 1.00 64.30  ? 561 TRP   A CH2 1 
ATOM   2075 N  N   . TYR   A 1 266 ? -19.409 9.718   18.911 1.00 73.04  ? 562 TYR   A N   1 
ATOM   2076 C  CA  . TYR   A 1 266 ? -20.119 9.212   17.747 1.00 79.55  ? 562 TYR   A CA  1 
ATOM   2077 C  C   . TYR   A 1 266 ? -21.515 8.729   18.130 1.00 76.84  ? 562 TYR   A C   1 
ATOM   2078 O  O   . TYR   A 1 266 ? -21.744 8.218   19.233 1.00 67.66  ? 562 TYR   A O   1 
ATOM   2079 C  CB  . TYR   A 1 266 ? -19.331 8.077   17.098 1.00 78.26  ? 562 TYR   A CB  1 
ATOM   2080 C  CG  . TYR   A 1 266 ? -18.827 7.017   18.066 1.00 78.72  ? 562 TYR   A CG  1 
ATOM   2081 C  CD1 . TYR   A 1 266 ? -19.595 5.903   18.368 1.00 74.96  ? 562 TYR   A CD1 1 
ATOM   2082 C  CD2 . TYR   A 1 266 ? -17.568 7.117   18.645 1.00 68.57  ? 562 TYR   A CD2 1 
ATOM   2083 C  CE1 . TYR   A 1 266 ? -19.132 4.936   19.233 1.00 79.05  ? 562 TYR   A CE1 1 
ATOM   2084 C  CE2 . TYR   A 1 266 ? -17.102 6.152   19.501 1.00 71.80  ? 562 TYR   A CE2 1 
ATOM   2085 C  CZ  . TYR   A 1 266 ? -17.884 5.070   19.805 1.00 74.66  ? 562 TYR   A CZ  1 
ATOM   2086 O  OH  . TYR   A 1 266 ? -17.413 4.109   20.660 1.00 79.78  ? 562 TYR   A OH  1 
ATOM   2087 N  N   . GLY   A 1 267 ? -22.459 8.899   17.198 1.00 70.25  ? 563 GLY   A N   1 
ATOM   2088 C  CA  . GLY   A 1 267 ? -23.839 8.564   17.501 1.00 64.30  ? 563 GLY   A CA  1 
ATOM   2089 C  C   . GLY   A 1 267 ? -24.089 7.080   17.674 1.00 72.19  ? 563 GLY   A C   1 
ATOM   2090 O  O   . GLY   A 1 267 ? -24.940 6.680   18.477 1.00 86.72  ? 563 GLY   A O   1 
ATOM   2091 N  N   . LEU   A 1 268 ? -23.331 6.243   16.971 1.00 62.40  ? 564 LEU   A N   1 
ATOM   2092 C  CA  . LEU   A 1 268 ? -23.768 4.881   16.681 1.00 60.21  ? 564 LEU   A CA  1 
ATOM   2093 C  C   . LEU   A 1 268 ? -22.967 3.867   17.478 1.00 58.94  ? 564 LEU   A C   1 
ATOM   2094 O  O   . LEU   A 1 268 ? -21.777 3.651   17.177 1.00 56.76  ? 564 LEU   A O   1 
ATOM   2095 C  CB  . LEU   A 1 268 ? -23.649 4.597   15.175 1.00 68.92  ? 564 LEU   A CB  1 
ATOM   2096 C  CG  . LEU   A 1 268 ? -24.194 3.244   14.703 1.00 65.16  ? 564 LEU   A CG  1 
ATOM   2097 C  CD1 . LEU   A 1 268 ? -25.723 3.203   14.669 1.00 65.95  ? 564 LEU   A CD1 1 
ATOM   2098 C  CD2 . LEU   A 1 268 ? -23.622 2.868   13.349 1.00 63.54  ? 564 LEU   A CD2 1 
ATOM   2099 N  N   . PRO   A 1 269 ? -23.585 3.204   18.506 1.00 52.68  ? 565 PRO   A N   1 
ATOM   2100 C  CA  . PRO   A 1 269 ? -22.907 2.105   19.207 1.00 50.44  ? 565 PRO   A CA  1 
ATOM   2101 C  C   . PRO   A 1 269 ? -23.089 0.798   18.462 1.00 51.04  ? 565 PRO   A C   1 
ATOM   2102 O  O   . PRO   A 1 269 ? -24.226 0.337   18.309 1.00 60.96  ? 565 PRO   A O   1 
ATOM   2103 C  CB  . PRO   A 1 269 ? -23.616 2.055   20.565 1.00 45.86  ? 565 PRO   A CB  1 
ATOM   2104 C  CG  . PRO   A 1 269 ? -25.008 2.619   20.308 1.00 58.40  ? 565 PRO   A CG  1 
ATOM   2105 C  CD  . PRO   A 1 269 ? -24.967 3.403   18.987 1.00 55.65  ? 565 PRO   A CD  1 
ATOM   2106 N  N   . ALA   A 1 270 ? -22.006 0.166   18.023 1.00 55.40  ? 566 ALA   A N   1 
ATOM   2107 C  CA  . ALA   A 1 270 ? -22.136 -0.972  17.105 1.00 57.86  ? 566 ALA   A CA  1 
ATOM   2108 C  C   . ALA   A 1 270 ? -21.074 -1.999  17.478 1.00 54.08  ? 566 ALA   A C   1 
ATOM   2109 O  O   . ALA   A 1 270 ? -19.895 -1.834  17.152 1.00 49.67  ? 566 ALA   A O   1 
ATOM   2110 C  CB  . ALA   A 1 270 ? -22.009 -0.530  15.654 1.00 63.16  ? 566 ALA   A CB  1 
ATOM   2111 N  N   . VAL   A 1 271 ? -21.495 -3.027  18.202 1.00 48.02  ? 567 VAL   A N   1 
ATOM   2112 C  CA  . VAL   A 1 271 ? -20.581 -4.051  18.675 1.00 55.87  ? 567 VAL   A CA  1 
ATOM   2113 C  C   . VAL   A 1 271 ? -20.287 -5.016  17.540 1.00 52.30  ? 567 VAL   A C   1 
ATOM   2114 O  O   . VAL   A 1 271 ? -21.203 -5.622  16.969 1.00 64.79  ? 567 VAL   A O   1 
ATOM   2115 C  CB  . VAL   A 1 271 ? -21.177 -4.783  19.888 1.00 50.06  ? 567 VAL   A CB  1 
ATOM   2116 C  CG1 . VAL   A 1 271 ? -20.547 -6.153  20.024 1.00 51.49  ? 567 VAL   A CG1 1 
ATOM   2117 C  CG2 . VAL   A 1 271 ? -20.989 -3.931  21.156 1.00 47.60  ? 567 VAL   A CG2 1 
ATOM   2118 N  N   . SER   A 1 272 ? -19.005 -5.189  17.228 1.00 50.47  ? 568 SER   A N   1 
ATOM   2119 C  CA  . SER   A 1 272 ? -18.600 -5.986  16.076 1.00 48.77  ? 568 SER   A CA  1 
ATOM   2120 C  C   . SER   A 1 272 ? -17.750 -7.209  16.395 1.00 52.35  ? 568 SER   A C   1 
ATOM   2121 O  O   . SER   A 1 272 ? -17.316 -7.891  15.461 1.00 55.48  ? 568 SER   A O   1 
ATOM   2122 C  CB  . SER   A 1 272 ? -17.829 -5.098  15.100 1.00 58.87  ? 568 SER   A CB  1 
ATOM   2123 O  OG  . SER   A 1 272 ? -16.772 -4.456  15.790 1.00 56.44  ? 568 SER   A OG  1 
ATOM   2124 N  N   . ASN   A 1 273 ? -17.491 -7.517  17.671 1.00 47.17  ? 569 ASN   A N   1 
ATOM   2125 C  CA  . ASN   A 1 273 ? -16.498 -8.528  18.012 1.00 51.13  ? 569 ASN   A CA  1 
ATOM   2126 C  C   . ASN   A 1 273 ? -17.106 -9.775  18.632 1.00 57.46  ? 569 ASN   A C   1 
ATOM   2127 O  O   . ASN   A 1 273 ? -16.361 -10.612 19.154 1.00 58.84  ? 569 ASN   A O   1 
ATOM   2128 C  CB  . ASN   A 1 273 ? -15.446 -7.948  18.965 1.00 62.22  ? 569 ASN   A CB  1 
ATOM   2129 C  CG  . ASN   A 1 273 ? -16.054 -7.396  20.258 1.00 63.05  ? 569 ASN   A CG  1 
ATOM   2130 O  OD1 . ASN   A 1 273 ? -17.245 -7.583  20.547 1.00 51.65  ? 569 ASN   A OD1 1 
ATOM   2131 N  ND2 . ASN   A 1 273 ? -15.223 -6.727  21.051 1.00 71.91  ? 569 ASN   A ND2 1 
ATOM   2132 N  N   . MET   A 1 274 ? -18.429 -9.915  18.596 1.00 54.69  ? 570 MET   A N   1 
ATOM   2133 C  CA  . MET   A 1 274 ? -19.123 -10.985 19.293 1.00 45.61  ? 570 MET   A CA  1 
ATOM   2134 C  C   . MET   A 1 274 ? -19.626 -12.048 18.329 1.00 53.36  ? 570 MET   A C   1 
ATOM   2135 O  O   . MET   A 1 274 ? -19.668 -11.865 17.112 1.00 63.99  ? 570 MET   A O   1 
ATOM   2136 C  CB  . MET   A 1 274 ? -20.278 -10.431 20.138 1.00 47.95  ? 570 MET   A CB  1 
ATOM   2137 C  CG  . MET   A 1 274 ? -19.786 -9.824  21.497 1.00 46.68  ? 570 MET   A CG  1 
ATOM   2138 S  SD  . MET   A 1 274 ? -21.145 -9.118  22.427 1.00 52.90  ? 570 MET   A SD  1 
ATOM   2139 C  CE  . MET   A 1 274 ? -21.879 -10.568 23.160 1.00 45.24  ? 570 MET   A CE  1 
ATOM   2140 N  N   . LEU   A 1 275 ? -20.016 -13.170 18.918 1.00 47.18  ? 571 LEU   A N   1 
ATOM   2141 C  CA  . LEU   A 1 275 ? -20.432 -14.353 18.205 1.00 49.63  ? 571 LEU   A CA  1 
ATOM   2142 C  C   . LEU   A 1 275 ? -21.932 -14.520 18.373 1.00 56.82  ? 571 LEU   A C   1 
ATOM   2143 O  O   . LEU   A 1 275 ? -22.441 -14.478 19.495 1.00 60.78  ? 571 LEU   A O   1 
ATOM   2144 C  CB  . LEU   A 1 275 ? -19.681 -15.576 18.722 1.00 47.30  ? 571 LEU   A CB  1 
ATOM   2145 C  CG  . LEU   A 1 275 ? -19.714 -16.757 17.754 1.00 64.85  ? 571 LEU   A CG  1 
ATOM   2146 C  CD1 . LEU   A 1 275 ? -18.356 -17.419 17.714 1.00 74.59  ? 571 LEU   A CD1 1 
ATOM   2147 C  CD2 . LEU   A 1 275 ? -20.774 -17.731 18.201 1.00 72.01  ? 571 LEU   A CD2 1 
ATOM   2148 N  N   . LEU   A 1 276 ? -22.627 -14.680 17.253 1.00 49.28  ? 572 LEU   A N   1 
ATOM   2149 C  CA  . LEU   A 1 276 ? -24.049 -14.992 17.203 1.00 54.98  ? 572 LEU   A CA  1 
ATOM   2150 C  C   . LEU   A 1 276 ? -24.209 -16.502 17.049 1.00 58.57  ? 572 LEU   A C   1 
ATOM   2151 O  O   . LEU   A 1 276 ? -23.511 -17.127 16.242 1.00 65.34  ? 572 LEU   A O   1 
ATOM   2152 C  CB  . LEU   A 1 276 ? -24.724 -14.265 16.028 1.00 59.34  ? 572 LEU   A CB  1 
ATOM   2153 C  CG  . LEU   A 1 276 ? -26.179 -14.616 15.697 1.00 58.39  ? 572 LEU   A CG  1 
ATOM   2154 C  CD1 . LEU   A 1 276 ? -27.050 -14.542 16.926 1.00 63.26  ? 572 LEU   A CD1 1 
ATOM   2155 C  CD2 . LEU   A 1 276 ? -26.727 -13.683 14.684 1.00 47.20  ? 572 LEU   A CD2 1 
ATOM   2156 N  N   . GLU   A 1 277 ? -25.136 -17.082 17.811 1.00 41.68  ? 573 GLU   A N   1 
ATOM   2157 C  CA  . GLU   A 1 277 ? -25.371 -18.522 17.824 1.00 55.27  ? 573 GLU   A CA  1 
ATOM   2158 C  C   . GLU   A 1 277 ? -26.838 -18.796 17.539 1.00 56.85  ? 573 GLU   A C   1 
ATOM   2159 O  O   . GLU   A 1 277 ? -27.719 -18.313 18.258 1.00 51.73  ? 573 GLU   A O   1 
ATOM   2160 C  CB  . GLU   A 1 277 ? -24.979 -19.126 19.168 1.00 57.19  ? 573 GLU   A CB  1 
ATOM   2161 C  CG  . GLU   A 1 277 ? -23.967 -20.230 19.093 1.00 71.83  ? 573 GLU   A CG  1 
ATOM   2162 C  CD  . GLU   A 1 277 ? -24.371 -21.416 19.927 1.00 87.06  ? 573 GLU   A CD  1 
ATOM   2163 O  OE1 . GLU   A 1 277 ? -25.443 -21.994 19.636 1.00 86.20  ? 573 GLU   A OE1 1 
ATOM   2164 O  OE2 . GLU   A 1 277 ? -23.627 -21.752 20.878 1.00 95.54  ? 573 GLU   A OE2 1 
ATOM   2165 N  N   . ILE   A 1 278 ? -27.103 -19.568 16.495 1.00 56.80  ? 574 ILE   A N   1 
ATOM   2166 C  CA  . ILE   A 1 278 ? -28.464 -19.942 16.129 1.00 58.49  ? 574 ILE   A CA  1 
ATOM   2167 C  C   . ILE   A 1 278 ? -28.443 -21.401 15.719 1.00 63.21  ? 574 ILE   A C   1 
ATOM   2168 O  O   . ILE   A 1 278 ? -27.563 -21.821 14.962 1.00 68.68  ? 574 ILE   A O   1 
ATOM   2169 C  CB  . ILE   A 1 278 ? -29.029 -19.072 14.992 1.00 55.02  ? 574 ILE   A CB  1 
ATOM   2170 C  CG1 . ILE   A 1 278 ? -29.012 -17.588 15.390 1.00 62.09  ? 574 ILE   A CG1 1 
ATOM   2171 C  CG2 . ILE   A 1 278 ? -30.433 -19.493 14.695 1.00 56.32  ? 574 ILE   A CG2 1 
ATOM   2172 C  CD1 . ILE   A 1 278 ? -29.249 -16.639 14.232 1.00 61.68  ? 574 ILE   A CD1 1 
ATOM   2173 N  N   . GLY   A 1 279 ? -29.386 -22.180 16.245 1.00 63.11  ? 575 GLY   A N   1 
ATOM   2174 C  CA  . GLY   A 1 279 ? -29.459 -23.595 15.940 1.00 65.20  ? 575 GLY   A CA  1 
ATOM   2175 C  C   . GLY   A 1 279 ? -28.133 -24.327 16.001 1.00 65.96  ? 575 GLY   A C   1 
ATOM   2176 O  O   . GLY   A 1 279 ? -27.959 -25.324 15.305 1.00 62.55  ? 575 GLY   A O   1 
ATOM   2177 N  N   . GLY   A 1 280 ? -27.197 -23.867 16.838 1.00 70.21  ? 576 GLY   A N   1 
ATOM   2178 C  CA  . GLY   A 1 280 ? -25.877 -24.478 16.871 1.00 70.20  ? 576 GLY   A CA  1 
ATOM   2179 C  C   . GLY   A 1 280 ? -24.966 -24.104 15.720 1.00 67.44  ? 576 GLY   A C   1 
ATOM   2180 O  O   . GLY   A 1 280 ? -23.878 -24.674 15.595 1.00 74.46  ? 576 GLY   A O   1 
ATOM   2181 N  N   . LEU   A 1 281 ? -25.390 -23.189 14.864 1.00 65.07  ? 577 LEU   A N   1 
ATOM   2182 C  CA  . LEU   A 1 281 ? -24.530 -22.583 13.855 1.00 70.16  ? 577 LEU   A CA  1 
ATOM   2183 C  C   . LEU   A 1 281 ? -23.916 -21.303 14.416 1.00 68.12  ? 577 LEU   A C   1 
ATOM   2184 O  O   . LEU   A 1 281 ? -24.565 -20.559 15.153 1.00 66.18  ? 577 LEU   A O   1 
ATOM   2185 C  CB  . LEU   A 1 281 ? -25.322 -22.266 12.585 1.00 68.23  ? 577 LEU   A CB  1 
ATOM   2186 C  CG  . LEU   A 1 281 ? -25.662 -23.404 11.628 1.00 73.14  ? 577 LEU   A CG  1 
ATOM   2187 C  CD1 . LEU   A 1 281 ? -26.579 -22.896 10.517 1.00 67.04  ? 577 LEU   A CD1 1 
ATOM   2188 C  CD2 . LEU   A 1 281 ? -24.392 -24.017 11.055 1.00 80.99  ? 577 LEU   A CD2 1 
ATOM   2189 N  N   . GLU   A 1 282 ? -22.662 -21.040 14.046 1.00 65.17  ? 578 GLU   A N   1 
ATOM   2190 C  CA  . GLU   A 1 282 ? -21.871 -19.988 14.677 1.00 62.93  ? 578 GLU   A CA  1 
ATOM   2191 C  C   . GLU   A 1 282 ? -21.484 -18.917 13.666 1.00 54.80  ? 578 GLU   A C   1 
ATOM   2192 O  O   . GLU   A 1 282 ? -20.785 -19.202 12.685 1.00 58.38  ? 578 GLU   A O   1 
ATOM   2193 C  CB  . GLU   A 1 282 ? -20.624 -20.579 15.336 1.00 68.94  ? 578 GLU   A CB  1 
ATOM   2194 C  CG  . GLU   A 1 282 ? -20.953 -21.648 16.372 1.00 77.65  ? 578 GLU   A CG  1 
ATOM   2195 C  CD  . GLU   A 1 282 ? -19.748 -22.062 17.180 1.00 85.95  ? 578 GLU   A CD  1 
ATOM   2196 O  OE1 . GLU   A 1 282 ? -18.639 -22.089 16.605 1.00 88.47  ? 578 GLU   A OE1 1 
ATOM   2197 O  OE2 . GLU   A 1 282 ? -19.911 -22.355 18.388 1.00 88.92  ? 578 GLU   A OE2 1 
ATOM   2198 N  N   . PHE   A 1 283 ? -21.901 -17.679 13.940 1.00 55.33  ? 579 PHE   A N   1 
ATOM   2199 C  CA  . PHE   A 1 283 ? -21.631 -16.507 13.105 1.00 59.17  ? 579 PHE   A CA  1 
ATOM   2200 C  C   . PHE   A 1 283 ? -20.606 -15.618 13.813 1.00 54.23  ? 579 PHE   A C   1 
ATOM   2201 O  O   . PHE   A 1 283 ? -20.960 -14.816 14.681 1.00 67.44  ? 579 PHE   A O   1 
ATOM   2202 C  CB  . PHE   A 1 283 ? -22.925 -15.749 12.817 1.00 57.29  ? 579 PHE   A CB  1 
ATOM   2203 C  CG  . PHE   A 1 283 ? -23.930 -16.554 12.024 1.00 60.61  ? 579 PHE   A CG  1 
ATOM   2204 C  CD1 . PHE   A 1 283 ? -24.914 -17.290 12.667 1.00 56.74  ? 579 PHE   A CD1 1 
ATOM   2205 C  CD2 . PHE   A 1 283 ? -23.877 -16.584 10.646 1.00 63.28  ? 579 PHE   A CD2 1 
ATOM   2206 C  CE1 . PHE   A 1 283 ? -25.833 -18.042 11.952 1.00 60.76  ? 579 PHE   A CE1 1 
ATOM   2207 C  CE2 . PHE   A 1 283 ? -24.801 -17.328 9.901  1.00 63.15  ? 579 PHE   A CE2 1 
ATOM   2208 C  CZ  . PHE   A 1 283 ? -25.781 -18.057 10.550 1.00 66.36  ? 579 PHE   A CZ  1 
ATOM   2209 N  N   . SER   A 1 284 ? -19.337 -15.748 13.410 1.00 56.25  ? 580 SER   A N   1 
ATOM   2210 C  CA  . SER   A 1 284 ? -18.208 -15.052 14.030 1.00 55.05  ? 580 SER   A CA  1 
ATOM   2211 C  C   . SER   A 1 284 ? -18.161 -13.559 13.718 1.00 61.95  ? 580 SER   A C   1 
ATOM   2212 O  O   . SER   A 1 284 ? -17.422 -12.818 14.376 1.00 67.86  ? 580 SER   A O   1 
ATOM   2213 C  CB  . SER   A 1 284 ? -16.913 -15.705 13.555 1.00 60.12  ? 580 SER   A CB  1 
ATOM   2214 O  OG  . SER   A 1 284 ? -16.960 -15.857 12.150 1.00 68.02  ? 580 SER   A OG  1 
ATOM   2215 N  N   . ALA   A 1 285 ? -18.891 -13.104 12.707 1.00 69.43  ? 581 ALA   A N   1 
ATOM   2216 C  CA  . ALA   A 1 285 ? -18.981 -11.685 12.392 1.00 62.48  ? 581 ALA   A CA  1 
ATOM   2217 C  C   . ALA   A 1 285 ? -20.449 -11.332 12.251 1.00 58.67  ? 581 ALA   A C   1 
ATOM   2218 O  O   . ALA   A 1 285 ? -21.125 -11.824 11.340 1.00 61.55  ? 581 ALA   A O   1 
ATOM   2219 C  CB  . ALA   A 1 285 ? -18.200 -11.337 11.117 1.00 50.25  ? 581 ALA   A CB  1 
ATOM   2220 N  N   . CYS   A 1 286 ? -20.936 -10.491 13.149 1.00 46.89  ? 582 CYS   A N   1 
ATOM   2221 C  CA  . CYS   A 1 286 ? -22.353 -10.167 13.217 1.00 39.94  ? 582 CYS   A CA  1 
ATOM   2222 C  C   . CYS   A 1 286 ? -22.588 -8.788  13.827 1.00 48.59  ? 582 CYS   A C   1 
ATOM   2223 O  O   . CYS   A 1 286 ? -23.355 -8.671  14.794 1.00 58.08  ? 582 CYS   A O   1 
ATOM   2224 C  CB  . CYS   A 1 286 ? -23.087 -11.220 14.038 1.00 53.48  ? 582 CYS   A CB  1 
ATOM   2225 S  SG  . CYS   A 1 286 ? -22.350 -11.359 15.693 1.00 48.26  ? 582 CYS   A SG  1 
ATOM   2226 N  N   . PRO   A 1 287 ? -21.987 -7.723  13.283 1.00 52.10  ? 583 PRO   A N   1 
ATOM   2227 C  CA  . PRO   A 1 287 ? -22.060 -6.422  13.960 1.00 41.33  ? 583 PRO   A CA  1 
ATOM   2228 C  C   . PRO   A 1 287 ? -23.502 -5.953  14.122 1.00 49.46  ? 583 PRO   A C   1 
ATOM   2229 O  O   . PRO   A 1 287 ? -24.343 -6.140  13.232 1.00 47.88  ? 583 PRO   A O   1 
ATOM   2230 C  CB  . PRO   A 1 287 ? -21.255 -5.502  13.038 1.00 45.23  ? 583 PRO   A CB  1 
ATOM   2231 C  CG  . PRO   A 1 287 ? -21.415 -6.140  11.676 1.00 50.76  ? 583 PRO   A CG  1 
ATOM   2232 C  CD  . PRO   A 1 287 ? -21.368 -7.609  11.946 1.00 53.37  ? 583 PRO   A CD  1 
ATOM   2233 N  N   . PHE   A 1 288 ? -23.790 -5.372  15.297 1.00 48.53  ? 584 PHE   A N   1 
ATOM   2234 C  CA  . PHE   A 1 288 ? -25.138 -4.947  15.645 1.00 46.82  ? 584 PHE   A CA  1 
ATOM   2235 C  C   . PHE   A 1 288 ? -25.126 -3.592  16.346 1.00 53.77  ? 584 PHE   A C   1 
ATOM   2236 O  O   . PHE   A 1 288 ? -24.248 -3.300  17.169 1.00 42.83  ? 584 PHE   A O   1 
ATOM   2237 C  CB  . PHE   A 1 288 ? -25.843 -6.006  16.517 1.00 53.88  ? 584 PHE   A CB  1 
ATOM   2238 C  CG  . PHE   A 1 288 ? -25.128 -6.359  17.813 1.00 55.34  ? 584 PHE   A CG  1 
ATOM   2239 C  CD1 . PHE   A 1 288 ? -25.247 -5.552  18.936 1.00 47.19  ? 584 PHE   A CD1 1 
ATOM   2240 C  CD2 . PHE   A 1 288 ? -24.401 -7.537  17.929 1.00 51.39  ? 584 PHE   A CD2 1 
ATOM   2241 C  CE1 . PHE   A 1 288 ? -24.622 -5.893  20.130 1.00 41.17  ? 584 PHE   A CE1 1 
ATOM   2242 C  CE2 . PHE   A 1 288 ? -23.769 -7.880  19.138 1.00 36.23  ? 584 PHE   A CE2 1 
ATOM   2243 C  CZ  . PHE   A 1 288 ? -23.892 -7.045  20.213 1.00 44.93  ? 584 PHE   A CZ  1 
ATOM   2244 N  N   . SER   A 1 289 ? -26.116 -2.763  16.016 1.00 54.90  ? 585 SER   A N   1 
ATOM   2245 C  CA  . SER   A 1 289 ? -26.169 -1.404  16.525 1.00 64.12  ? 585 SER   A CA  1 
ATOM   2246 C  C   . SER   A 1 289 ? -27.546 -1.091  17.104 1.00 61.13  ? 585 SER   A C   1 
ATOM   2247 O  O   . SER   A 1 289 ? -28.569 -1.653  16.684 1.00 51.39  ? 585 SER   A O   1 
ATOM   2248 C  CB  . SER   A 1 289 ? -25.806 -0.384  15.419 1.00 72.88  ? 585 SER   A CB  1 
ATOM   2249 O  OG  . SER   A 1 289 ? -26.853 -0.207  14.478 1.00 72.77  ? 585 SER   A OG  1 
ATOM   2250 N  N   . GLY   A 1 290 ? -27.548 -0.184  18.090 1.00 48.71  ? 586 GLY   A N   1 
ATOM   2251 C  CA  . GLY   A 1 290 ? -28.766 0.443   18.566 1.00 54.20  ? 586 GLY   A CA  1 
ATOM   2252 C  C   . GLY   A 1 290 ? -28.557 1.935   18.757 1.00 62.85  ? 586 GLY   A C   1 
ATOM   2253 O  O   . GLY   A 1 290 ? -28.042 2.600   17.861 1.00 50.48  ? 586 GLY   A O   1 
ATOM   2254 N  N   . TRP   A 1 291 ? -28.935 2.482   19.914 1.00 55.24  ? 587 TRP   A N   1 
ATOM   2255 C  CA  . TRP   A 1 291 ? -28.583 3.849   20.272 1.00 61.51  ? 587 TRP   A CA  1 
ATOM   2256 C  C   . TRP   A 1 291 ? -28.002 3.847   21.678 1.00 70.15  ? 587 TRP   A C   1 
ATOM   2257 O  O   . TRP   A 1 291 ? -28.149 2.881   22.421 1.00 71.26  ? 587 TRP   A O   1 
ATOM   2258 C  CB  . TRP   A 1 291 ? -29.785 4.809   20.197 1.00 63.94  ? 587 TRP   A CB  1 
ATOM   2259 C  CG  . TRP   A 1 291 ? -31.033 4.290   20.803 1.00 71.97  ? 587 TRP   A CG  1 
ATOM   2260 C  CD1 . TRP   A 1 291 ? -31.377 4.317   22.133 1.00 77.59  ? 587 TRP   A CD1 1 
ATOM   2261 C  CD2 . TRP   A 1 291 ? -32.115 3.648   20.123 1.00 78.10  ? 587 TRP   A CD2 1 
ATOM   2262 N  NE1 . TRP   A 1 291 ? -32.609 3.737   22.314 1.00 79.88  ? 587 TRP   A NE1 1 
ATOM   2263 C  CE2 . TRP   A 1 291 ? -33.085 3.317   21.098 1.00 81.47  ? 587 TRP   A CE2 1 
ATOM   2264 C  CE3 . TRP   A 1 291 ? -32.362 3.317   18.785 1.00 78.31  ? 587 TRP   A CE3 1 
ATOM   2265 C  CZ2 . TRP   A 1 291 ? -34.278 2.668   20.776 1.00 84.67  ? 587 TRP   A CZ2 1 
ATOM   2266 C  CZ3 . TRP   A 1 291 ? -33.548 2.680   18.466 1.00 79.80  ? 587 TRP   A CZ3 1 
ATOM   2267 C  CH2 . TRP   A 1 291 ? -34.491 2.360   19.453 1.00 84.54  ? 587 TRP   A CH2 1 
ATOM   2268 N  N   . TYR   A 1 292 ? -27.337 4.939   22.033 1.00 72.01  ? 588 TYR   A N   1 
ATOM   2269 C  CA  . TYR   A 1 292 ? -26.660 5.014   23.317 1.00 69.24  ? 588 TYR   A CA  1 
ATOM   2270 C  C   . TYR   A 1 292 ? -27.639 5.272   24.457 1.00 67.19  ? 588 TYR   A C   1 
ATOM   2271 O  O   . TYR   A 1 292 ? -28.582 6.063   24.331 1.00 65.61  ? 588 TYR   A O   1 
ATOM   2272 C  CB  . TYR   A 1 292 ? -25.608 6.124   23.290 1.00 73.54  ? 588 TYR   A CB  1 
ATOM   2273 C  CG  . TYR   A 1 292 ? -24.213 5.670   22.931 1.00 71.14  ? 588 TYR   A CG  1 
ATOM   2274 C  CD1 . TYR   A 1 292 ? -23.607 6.075   21.743 1.00 69.35  ? 588 TYR   A CD1 1 
ATOM   2275 C  CD2 . TYR   A 1 292 ? -23.496 4.850   23.790 1.00 61.63  ? 588 TYR   A CD2 1 
ATOM   2276 C  CE1 . TYR   A 1 292 ? -22.314 5.675   21.425 1.00 66.77  ? 588 TYR   A CE1 1 
ATOM   2277 C  CE2 . TYR   A 1 292 ? -22.211 4.444   23.482 1.00 65.88  ? 588 TYR   A CE2 1 
ATOM   2278 C  CZ  . TYR   A 1 292 ? -21.630 4.845   22.285 1.00 64.46  ? 588 TYR   A CZ  1 
ATOM   2279 O  OH  . TYR   A 1 292 ? -20.350 4.432   21.999 1.00 61.73  ? 588 TYR   A OH  1 
ATOM   2280 N  N   . MET   A 1 293 ? -27.413 4.594   25.575 1.00 61.32  ? 589 MET   A N   1 
ATOM   2281 C  CA  . MET   A 1 293 ? -27.845 5.138   26.852 1.00 62.67  ? 589 MET   A CA  1 
ATOM   2282 C  C   . MET   A 1 293 ? -26.793 6.150   27.297 1.00 64.77  ? 589 MET   A C   1 
ATOM   2283 O  O   . MET   A 1 293 ? -25.592 5.890   27.197 1.00 64.36  ? 589 MET   A O   1 
ATOM   2284 C  CB  . MET   A 1 293 ? -28.043 4.020   27.891 1.00 49.58  ? 589 MET   A CB  1 
ATOM   2285 C  CG  . MET   A 1 293 ? -28.591 4.511   29.268 1.00 50.98  ? 589 MET   A CG  1 
ATOM   2286 S  SD  . MET   A 1 293 ? -28.982 3.160   30.398 1.00 57.05  ? 589 MET   A SD  1 
ATOM   2287 C  CE  . MET   A 1 293 ? -27.370 2.411   30.689 1.00 65.86  ? 589 MET   A CE  1 
ATOM   2288 N  N   . GLY   A 1 294 ? -27.243 7.318   27.739 1.00 68.64  ? 590 GLY   A N   1 
ATOM   2289 C  CA  . GLY   A 1 294 ? -26.357 8.408   28.124 1.00 65.19  ? 590 GLY   A CA  1 
ATOM   2290 C  C   . GLY   A 1 294 ? -25.125 8.016   28.926 1.00 72.40  ? 590 GLY   A C   1 
ATOM   2291 O  O   . GLY   A 1 294 ? -24.009 8.434   28.594 1.00 62.99  ? 590 GLY   A O   1 
ATOM   2292 N  N   . THR   A 1 295 ? -25.308 7.172   29.948 1.00 76.67  ? 591 THR   A N   1 
ATOM   2293 C  CA  . THR   A 1 295 ? -24.222 6.871   30.884 1.00 69.24  ? 591 THR   A CA  1 
ATOM   2294 C  C   . THR   A 1 295 ? -23.002 6.255   30.200 1.00 65.66  ? 591 THR   A C   1 
ATOM   2295 O  O   . THR   A 1 295 ? -21.863 6.529   30.598 1.00 62.96  ? 591 THR   A O   1 
ATOM   2296 C  CB  . THR   A 1 295 ? -24.722 5.956   32.005 1.00 59.22  ? 591 THR   A CB  1 
ATOM   2297 O  OG1 . THR   A 1 295 ? -24.933 4.617   31.550 1.00 60.37  ? 591 THR   A OG1 1 
ATOM   2298 C  CG2 . THR   A 1 295 ? -26.012 6.489   32.575 1.00 78.88  ? 591 THR   A CG2 1 
ATOM   2299 N  N   . GLU   A 1 296 ? -23.202 5.404   29.190 1.00 61.74  ? 592 GLU   A N   1 
ATOM   2300 C  CA  . GLU   A 1 296 ? -22.031 4.749   28.613 1.00 56.85  ? 592 GLU   A CA  1 
ATOM   2301 C  C   . GLU   A 1 296 ? -21.022 5.765   28.125 1.00 59.89  ? 592 GLU   A C   1 
ATOM   2302 O  O   . GLU   A 1 296 ? -19.813 5.530   28.200 1.00 76.94  ? 592 GLU   A O   1 
ATOM   2303 C  CB  . GLU   A 1 296 ? -22.398 3.854   27.453 1.00 55.89  ? 592 GLU   A CB  1 
ATOM   2304 C  CG  . GLU   A 1 296 ? -23.356 2.741   27.711 1.00 48.76  ? 592 GLU   A CG  1 
ATOM   2305 C  CD  . GLU   A 1 296 ? -23.723 2.146   26.329 1.00 61.90  ? 592 GLU   A CD  1 
ATOM   2306 O  OE1 . GLU   A 1 296 ? -22.828 1.507   25.704 1.00 41.31  ? 592 GLU   A OE1 1 
ATOM   2307 O  OE2 . GLU   A 1 296 ? -24.850 2.404   25.840 1.00 58.04  ? 592 GLU   A OE2 1 
ATOM   2308 N  N   . ILE   A 1 297 ? -21.503 6.901   27.634 1.00 67.92  ? 593 ILE   A N   1 
ATOM   2309 C  CA  . ILE   A 1 297 ? -20.623 7.992   27.247 1.00 75.52  ? 593 ILE   A CA  1 
ATOM   2310 C  C   . ILE   A 1 297 ? -20.205 8.806   28.459 1.00 74.04  ? 593 ILE   A C   1 
ATOM   2311 O  O   . ILE   A 1 297 ? -19.014 9.054   28.676 1.00 78.82  ? 593 ILE   A O   1 
ATOM   2312 C  CB  . ILE   A 1 297 ? -21.323 8.889   26.215 1.00 72.02  ? 593 ILE   A CB  1 
ATOM   2313 C  CG1 . ILE   A 1 297 ? -21.596 8.115   24.942 1.00 64.69  ? 593 ILE   A CG1 1 
ATOM   2314 C  CG2 . ILE   A 1 297 ? -20.488 10.109  25.928 1.00 76.49  ? 593 ILE   A CG2 1 
ATOM   2315 C  CD1 . ILE   A 1 297 ? -22.562 8.826   24.049 1.00 65.40  ? 593 ILE   A CD1 1 
ATOM   2316 N  N   . GLY   A 1 298 ? -21.188 9.280   29.229 1.00 73.82  ? 594 GLY   A N   1 
ATOM   2317 C  CA  . GLY   A 1 298 ? -20.907 10.280  30.248 1.00 82.80  ? 594 GLY   A CA  1 
ATOM   2318 C  C   . GLY   A 1 298 ? -20.141 9.734   31.435 1.00 81.38  ? 594 GLY   A C   1 
ATOM   2319 O  O   . GLY   A 1 298 ? -19.251 10.406  31.969 1.00 74.49  ? 594 GLY   A O   1 
ATOM   2320 N  N   . VAL   A 1 299 ? -20.464 8.508   31.856 1.00 80.83  ? 595 VAL   A N   1 
ATOM   2321 C  CA  . VAL   A 1 299 ? -19.832 7.902   33.028 1.00 75.84  ? 595 VAL   A CA  1 
ATOM   2322 C  C   . VAL   A 1 299 ? -18.633 7.045   32.634 1.00 75.51  ? 595 VAL   A C   1 
ATOM   2323 O  O   . VAL   A 1 299 ? -17.514 7.254   33.116 1.00 85.84  ? 595 VAL   A O   1 
ATOM   2324 C  CB  . VAL   A 1 299 ? -20.830 7.042   33.825 1.00 71.04  ? 595 VAL   A CB  1 
ATOM   2325 C  CG1 . VAL   A 1 299 ? -20.202 6.616   35.135 1.00 70.85  ? 595 VAL   A CG1 1 
ATOM   2326 C  CG2 . VAL   A 1 299 ? -22.144 7.774   34.054 1.00 65.60  ? 595 VAL   A CG2 1 
ATOM   2327 N  N   . ARG   A 1 300 ? -18.871 6.049   31.780 1.00 67.31  ? 596 ARG   A N   1 
ATOM   2328 C  CA  . ARG   A 1 300 ? -17.852 5.057   31.446 1.00 67.18  ? 596 ARG   A CA  1 
ATOM   2329 C  C   . ARG   A 1 300 ? -16.808 5.598   30.460 1.00 76.50  ? 596 ARG   A C   1 
ATOM   2330 O  O   . ARG   A 1 300 ? -15.609 5.613   30.771 1.00 75.11  ? 596 ARG   A O   1 
ATOM   2331 C  CB  . ARG   A 1 300 ? -18.528 3.786   30.911 1.00 56.61  ? 596 ARG   A CB  1 
ATOM   2332 C  CG  . ARG   A 1 300 ? -19.575 3.198   31.856 1.00 57.63  ? 596 ARG   A CG  1 
ATOM   2333 C  CD  . ARG   A 1 300 ? -19.009 3.050   33.322 1.00 59.36  ? 596 ARG   A CD  1 
ATOM   2334 N  NE  . ARG   A 1 300 ? -17.750 2.296   33.342 1.00 49.42  ? 596 ARG   A NE  1 
ATOM   2335 C  CZ  . ARG   A 1 300 ? -17.643 1.008   32.997 1.00 51.09  ? 596 ARG   A CZ  1 
ATOM   2336 N  NH1 . ARG   A 1 300 ? -18.718 0.309   32.622 1.00 56.84  ? 596 ARG   A NH1 1 
ATOM   2337 N  NH2 . ARG   A 1 300 ? -16.458 0.411   33.043 1.00 59.21  ? 596 ARG   A NH2 1 
ATOM   2338 N  N   . ASP   A 1 301 ? -17.231 6.042   29.263 1.00 70.56  ? 597 ASP   A N   1 
ATOM   2339 C  CA  . ASP   A 1 301 ? -16.249 6.511   28.277 1.00 69.75  ? 597 ASP   A CA  1 
ATOM   2340 C  C   . ASP   A 1 301 ? -15.468 7.719   28.792 1.00 73.21  ? 597 ASP   A C   1 
ATOM   2341 O  O   . ASP   A 1 301 ? -14.241 7.796   28.638 1.00 69.54  ? 597 ASP   A O   1 
ATOM   2342 C  CB  . ASP   A 1 301 ? -16.916 6.881   26.941 1.00 67.08  ? 597 ASP   A CB  1 
ATOM   2343 C  CG  . ASP   A 1 301 ? -17.464 5.694   26.191 1.00 65.91  ? 597 ASP   A CG  1 
ATOM   2344 O  OD1 . ASP   A 1 301 ? -16.847 4.594   26.176 1.00 56.75  ? 597 ASP   A OD1 1 
ATOM   2345 O  OD2 . ASP   A 1 301 ? -18.550 5.866   25.598 1.00 80.86  ? 597 ASP   A OD2 1 
ATOM   2346 N  N   . TYR   A 1 302 ? -16.159 8.683   29.393 1.00 71.23  ? 598 TYR   A N   1 
ATOM   2347 C  CA  . TYR   A 1 302 ? -15.540 9.956   29.733 1.00 72.38  ? 598 TYR   A CA  1 
ATOM   2348 C  C   . TYR   A 1 302 ? -14.858 9.956   31.107 1.00 84.69  ? 598 TYR   A C   1 
ATOM   2349 O  O   . TYR   A 1 302 ? -13.898 10.713  31.315 1.00 81.13  ? 598 TYR   A O   1 
ATOM   2350 C  CB  . TYR   A 1 302 ? -16.598 11.068  29.677 1.00 80.99  ? 598 TYR   A CB  1 
ATOM   2351 C  CG  . TYR   A 1 302 ? -16.896 11.614  28.286 1.00 94.15  ? 598 TYR   A CG  1 
ATOM   2352 C  CD1 . TYR   A 1 302 ? -18.092 12.277  28.019 1.00 99.64  ? 598 TYR   A CD1 1 
ATOM   2353 C  CD2 . TYR   A 1 302 ? -15.979 11.480  27.252 1.00 96.30  ? 598 TYR   A CD2 1 
ATOM   2354 C  CE1 . TYR   A 1 302 ? -18.368 12.787  26.756 1.00 98.06  ? 598 TYR   A CE1 1 
ATOM   2355 C  CE2 . TYR   A 1 302 ? -16.247 11.991  25.988 1.00 102.09 ? 598 TYR   A CE2 1 
ATOM   2356 C  CZ  . TYR   A 1 302 ? -17.440 12.644  25.751 1.00 102.23 ? 598 TYR   A CZ  1 
ATOM   2357 O  OH  . TYR   A 1 302 ? -17.708 13.153  24.503 1.00 101.80 ? 598 TYR   A OH  1 
ATOM   2358 N  N   . CYS   A 1 303 ? -15.306 9.114   32.042 1.00 70.39  ? 599 CYS   A N   1 
ATOM   2359 C  CA  . CYS   A 1 303 ? -14.840 9.197   33.419 1.00 73.12  ? 599 CYS   A CA  1 
ATOM   2360 C  C   . CYS   A 1 303 ? -14.247 7.919   34.002 1.00 78.82  ? 599 CYS   A C   1 
ATOM   2361 O  O   . CYS   A 1 303 ? -13.767 7.966   35.144 1.00 86.41  ? 599 CYS   A O   1 
ATOM   2362 C  CB  . CYS   A 1 303 ? -15.981 9.652   34.334 1.00 80.99  ? 599 CYS   A CB  1 
ATOM   2363 S  SG  . CYS   A 1 303 ? -16.661 11.249  33.944 1.00 83.23  ? 599 CYS   A SG  1 
ATOM   2364 N  N   . ASP   A 1 304 ? -14.279 6.785   33.296 1.00 77.39  ? 600 ASP   A N   1 
ATOM   2365 C  CA  . ASP   A 1 304 ? -13.441 5.665   33.709 1.00 85.05  ? 600 ASP   A CA  1 
ATOM   2366 C  C   . ASP   A 1 304 ? -12.017 6.167   33.908 1.00 92.91  ? 600 ASP   A C   1 
ATOM   2367 O  O   . ASP   A 1 304 ? -11.527 7.004   33.145 1.00 99.38  ? 600 ASP   A O   1 
ATOM   2368 C  CB  . ASP   A 1 304 ? -13.436 4.550   32.664 1.00 88.97  ? 600 ASP   A CB  1 
ATOM   2369 C  CG  . ASP   A 1 304 ? -14.383 3.404   32.982 1.00 82.35  ? 600 ASP   A CG  1 
ATOM   2370 O  OD1 . ASP   A 1 304 ? -15.416 3.615   33.654 1.00 79.76  ? 600 ASP   A OD1 1 
ATOM   2371 O  OD2 . ASP   A 1 304 ? -14.081 2.281   32.527 1.00 74.19  ? 600 ASP   A OD2 1 
ATOM   2372 N  N   . ASN   A 1 305 ? -11.358 5.676   34.956 1.00 91.66  ? 601 ASN   A N   1 
ATOM   2373 C  CA  . ASN   A 1 305 ? -9.976  6.079   35.199 1.00 91.90  ? 601 ASN   A CA  1 
ATOM   2374 C  C   . ASN   A 1 305 ? -9.061  5.644   34.064 1.00 86.24  ? 601 ASN   A C   1 
ATOM   2375 O  O   . ASN   A 1 305 ? -8.077  6.328   33.757 1.00 80.18  ? 601 ASN   A O   1 
ATOM   2376 C  CB  . ASN   A 1 305 ? -9.482  5.499   36.524 1.00 91.22  ? 601 ASN   A CB  1 
ATOM   2377 C  CG  . ASN   A 1 305 ? -9.679  6.449   37.683 1.00 100.84 ? 601 ASN   A CG  1 
ATOM   2378 O  OD1 . ASN   A 1 305 ? -9.719  7.667   37.502 1.00 108.23 ? 601 ASN   A OD1 1 
ATOM   2379 N  ND2 . ASN   A 1 305 ? -9.784  5.898   38.889 1.00 100.92 ? 601 ASN   A ND2 1 
ATOM   2380 N  N   . SER   A 1 306 ? -9.359  4.506   33.443 1.00 82.35  ? 602 SER   A N   1 
ATOM   2381 C  CA  . SER   A 1 306 ? -8.543  3.969   32.373 1.00 86.10  ? 602 SER   A CA  1 
ATOM   2382 C  C   . SER   A 1 306 ? -9.083  4.342   30.998 1.00 85.89  ? 602 SER   A C   1 
ATOM   2383 O  O   . SER   A 1 306 ? -8.589  3.832   29.986 1.00 76.26  ? 602 SER   A O   1 
ATOM   2384 C  CB  . SER   A 1 306 ? -8.438  2.454   32.516 1.00 84.10  ? 602 SER   A CB  1 
ATOM   2385 O  OG  . SER   A 1 306 ? -9.710  1.865   32.325 1.00 83.69  ? 602 SER   A OG  1 
ATOM   2386 N  N   . ARG   A 1 307 ? -10.085 5.224   30.939 1.00 89.98  ? 603 ARG   A N   1 
ATOM   2387 C  CA  . ARG   A 1 307 ? -10.595 5.725   29.669 1.00 90.77  ? 603 ARG   A CA  1 
ATOM   2388 C  C   . ARG   A 1 307 ? -10.281 7.218   29.547 1.00 91.65  ? 603 ARG   A C   1 
ATOM   2389 O  O   . ARG   A 1 307 ? -9.132  7.608   29.775 1.00 102.87 ? 603 ARG   A O   1 
ATOM   2390 C  CB  . ARG   A 1 307 ? -12.084 5.403   29.546 1.00 84.74  ? 603 ARG   A CB  1 
ATOM   2391 C  CG  . ARG   A 1 307 ? -12.353 3.890   29.618 1.00 83.89  ? 603 ARG   A CG  1 
ATOM   2392 C  CD  . ARG   A 1 307 ? -11.863 3.132   28.382 1.00 81.41  ? 603 ARG   A CD  1 
ATOM   2393 N  NE  . ARG   A 1 307 ? -12.257 3.835   27.181 1.00 74.37  ? 603 ARG   A NE  1 
ATOM   2394 C  CZ  . ARG   A 1 307 ? -13.502 3.884   26.731 1.00 72.43  ? 603 ARG   A CZ  1 
ATOM   2395 N  NH1 . ARG   A 1 307 ? -14.466 3.242   27.366 1.00 61.31  ? 603 ARG   A NH1 1 
ATOM   2396 N  NH2 . ARG   A 1 307 ? -13.786 4.561   25.628 1.00 85.47  ? 603 ARG   A NH2 1 
ATOM   2397 N  N   . TYR   A 1 308 ? -11.259 8.071   29.202 1.00 86.55  ? 604 TYR   A N   1 
ATOM   2398 C  CA  . TYR   A 1 308 ? -10.913 9.466   28.895 1.00 80.87  ? 604 TYR   A CA  1 
ATOM   2399 C  C   . TYR   A 1 308 ? -10.521 10.261  30.132 1.00 95.23  ? 604 TYR   A C   1 
ATOM   2400 O  O   . TYR   A 1 308 ? -9.693  11.175  30.034 1.00 99.03  ? 604 TYR   A O   1 
ATOM   2401 C  CB  . TYR   A 1 308 ? -12.055 10.166  28.167 1.00 80.37  ? 604 TYR   A CB  1 
ATOM   2402 C  CG  . TYR   A 1 308 ? -11.907 10.022  26.664 1.00 88.05  ? 604 TYR   A CG  1 
ATOM   2403 C  CD1 . TYR   A 1 308 ? -12.043 8.785   26.062 1.00 81.54  ? 604 TYR   A CD1 1 
ATOM   2404 C  CD2 . TYR   A 1 308 ? -11.593 11.108  25.865 1.00 96.93  ? 604 TYR   A CD2 1 
ATOM   2405 C  CE1 . TYR   A 1 308 ? -11.893 8.630   24.712 1.00 87.78  ? 604 TYR   A CE1 1 
ATOM   2406 C  CE2 . TYR   A 1 308 ? -11.436 10.960  24.488 1.00 98.07  ? 604 TYR   A CE2 1 
ATOM   2407 C  CZ  . TYR   A 1 308 ? -11.591 9.715   23.926 1.00 95.05  ? 604 TYR   A CZ  1 
ATOM   2408 O  OH  . TYR   A 1 308 ? -11.449 9.518   22.570 1.00 96.65  ? 604 TYR   A OH  1 
ATOM   2409 N  N   . ASN   A 1 309 ? -11.120 9.958   31.284 1.00 87.52  ? 605 ASN   A N   1 
ATOM   2410 C  CA  . ASN   A 1 309 ? -10.621 10.422  32.580 1.00 97.75  ? 605 ASN   A CA  1 
ATOM   2411 C  C   . ASN   A 1 309 ? -10.659 11.952  32.677 1.00 107.48 ? 605 ASN   A C   1 
ATOM   2412 O  O   . ASN   A 1 309 ? -9.641  12.623  32.880 1.00 119.86 ? 605 ASN   A O   1 
ATOM   2413 C  CB  . ASN   A 1 309 ? -9.209  9.879   32.812 1.00 99.04  ? 605 ASN   A CB  1 
ATOM   2414 C  CG  . ASN   A 1 309 ? -8.814  9.882   34.252 1.00 94.22  ? 605 ASN   A CG  1 
ATOM   2415 O  OD1 . ASN   A 1 309 ? -9.652  9.725   35.146 1.00 87.24  ? 605 ASN   A OD1 1 
ATOM   2416 N  ND2 . ASN   A 1 309 ? -7.521  10.055  34.498 1.00 98.91  ? 605 ASN   A ND2 1 
ATOM   2417 N  N   . ILE   A 1 310 ? -11.869 12.498  32.540 1.00 101.49 ? 606 ILE   A N   1 
ATOM   2418 C  CA  . ILE   A 1 310 ? -12.052 13.940  32.463 1.00 106.17 ? 606 ILE   A CA  1 
ATOM   2419 C  C   . ILE   A 1 310 ? -12.582 14.538  33.752 1.00 106.63 ? 606 ILE   A C   1 
ATOM   2420 O  O   . ILE   A 1 310 ? -12.777 15.759  33.813 1.00 108.63 ? 606 ILE   A O   1 
ATOM   2421 C  CB  . ILE   A 1 310 ? -12.992 14.316  31.305 1.00 107.35 ? 606 ILE   A CB  1 
ATOM   2422 C  CG1 . ILE   A 1 310 ? -14.442 14.137  31.753 1.00 105.95 ? 606 ILE   A CG1 1 
ATOM   2423 C  CG2 . ILE   A 1 310 ? -12.695 13.464  30.091 1.00 91.97  ? 606 ILE   A CG2 1 
ATOM   2424 C  CD1 . ILE   A 1 310 ? -15.435 14.214  30.637 1.00 89.59  ? 606 ILE   A CD1 1 
ATOM   2425 N  N   . LEU   A 1 311 ? -12.855 13.720  34.775 1.00 107.43 ? 607 LEU   A N   1 
ATOM   2426 C  CA  . LEU   A 1 311 ? -13.276 14.265  36.061 1.00 99.23  ? 607 LEU   A CA  1 
ATOM   2427 C  C   . LEU   A 1 311 ? -12.296 15.322  36.543 1.00 109.87 ? 607 LEU   A C   1 
ATOM   2428 O  O   . LEU   A 1 311 ? -12.698 16.333  37.129 1.00 107.30 ? 607 LEU   A O   1 
ATOM   2429 C  CB  . LEU   A 1 311 ? -13.406 13.144  37.100 1.00 91.54  ? 607 LEU   A CB  1 
ATOM   2430 C  CG  . LEU   A 1 311 ? -14.657 12.264  37.083 1.00 85.40  ? 607 LEU   A CG  1 
ATOM   2431 C  CD1 . LEU   A 1 311 ? -14.523 11.144  38.111 1.00 85.64  ? 607 LEU   A CD1 1 
ATOM   2432 C  CD2 . LEU   A 1 311 ? -15.922 13.072  37.337 1.00 86.57  ? 607 LEU   A CD2 1 
ATOM   2433 N  N   . GLU   A 1 312 ? -11.003 15.108  36.277 1.00 121.83 ? 608 GLU   A N   1 
ATOM   2434 C  CA  . GLU   A 1 312 ? -9.965  16.082  36.611 1.00 143.26 ? 608 GLU   A CA  1 
ATOM   2435 C  C   . GLU   A 1 312 ? -10.333 17.492  36.163 1.00 145.84 ? 608 GLU   A C   1 
ATOM   2436 O  O   . GLU   A 1 312 ? -10.333 18.433  36.964 1.00 148.80 ? 608 GLU   A O   1 
ATOM   2437 C  CB  . GLU   A 1 312 ? -8.643  15.659  35.963 1.00 154.27 ? 608 GLU   A CB  1 
ATOM   2438 C  CG  . GLU   A 1 312 ? -7.918  14.526  36.664 1.00 156.23 ? 608 GLU   A CG  1 
ATOM   2439 C  CD  . GLU   A 1 312 ? -7.037  15.018  37.801 1.00 163.99 ? 608 GLU   A CD  1 
ATOM   2440 O  OE1 . GLU   A 1 312 ? -7.348  16.078  38.388 1.00 165.87 ? 608 GLU   A OE1 1 
ATOM   2441 O  OE2 . GLU   A 1 312 ? -6.025  14.350  38.102 1.00 165.59 ? 608 GLU   A OE2 1 
ATOM   2442 N  N   . GLU   A 1 313 ? -10.651 17.652  34.879 1.00 142.57 ? 609 GLU   A N   1 
ATOM   2443 C  CA  . GLU   A 1 313 ? -10.792 18.987  34.307 1.00 145.40 ? 609 GLU   A CA  1 
ATOM   2444 C  C   . GLU   A 1 313 ? -12.159 19.591  34.593 1.00 138.91 ? 609 GLU   A C   1 
ATOM   2445 O  O   . GLU   A 1 313 ? -12.257 20.760  34.984 1.00 140.36 ? 609 GLU   A O   1 
ATOM   2446 C  CB  . GLU   A 1 313 ? -10.536 18.944  32.804 1.00 148.86 ? 609 GLU   A CB  1 
ATOM   2447 C  CG  . GLU   A 1 313 ? -9.106  19.284  32.420 1.00 160.41 ? 609 GLU   A CG  1 
ATOM   2448 C  CD  . GLU   A 1 313 ? -8.691  20.692  32.848 1.00 173.87 ? 609 GLU   A CD  1 
ATOM   2449 O  OE1 . GLU   A 1 313 ? -8.497  20.934  34.059 1.00 175.15 ? 609 GLU   A OE1 1 
ATOM   2450 O  OE2 . GLU   A 1 313 ? -8.557  21.566  31.964 1.00 180.35 ? 609 GLU   A OE2 1 
ATOM   2451 N  N   . VAL   A 1 314 ? -13.223 18.813  34.388 1.00 131.84 ? 610 VAL   A N   1 
ATOM   2452 C  CA  . VAL   A 1 314 ? -14.567 19.307  34.671 1.00 128.85 ? 610 VAL   A CA  1 
ATOM   2453 C  C   . VAL   A 1 314 ? -14.669 19.790  36.115 1.00 132.83 ? 610 VAL   A C   1 
ATOM   2454 O  O   . VAL   A 1 314 ? -15.328 20.798  36.403 1.00 124.35 ? 610 VAL   A O   1 
ATOM   2455 C  CB  . VAL   A 1 314 ? -15.603 18.216  34.351 1.00 117.98 ? 610 VAL   A CB  1 
ATOM   2456 C  CG1 . VAL   A 1 314 ? -17.011 18.721  34.611 1.00 117.41 ? 610 VAL   A CG1 1 
ATOM   2457 C  CG2 . VAL   A 1 314 ? -15.442 17.790  32.916 1.00 113.08 ? 610 VAL   A CG2 1 
ATOM   2458 N  N   . ALA   A 1 315 ? -14.007 19.093  37.041 1.00 132.57 ? 611 ALA   A N   1 
ATOM   2459 C  CA  . ALA   A 1 315 ? -13.973 19.561  38.422 1.00 138.22 ? 611 ALA   A CA  1 
ATOM   2460 C  C   . ALA   A 1 315 ? -13.381 20.960  38.502 1.00 142.97 ? 611 ALA   A C   1 
ATOM   2461 O  O   . ALA   A 1 315 ? -13.962 21.860  39.119 1.00 149.17 ? 611 ALA   A O   1 
ATOM   2462 C  CB  . ALA   A 1 315 ? -13.177 18.590  39.288 1.00 135.22 ? 611 ALA   A CB  1 
ATOM   2463 N  N   . LYS   A 1 316 ? -12.234 21.167  37.853 1.00 140.00 ? 612 LYS   A N   1 
ATOM   2464 C  CA  . LYS   A 1 316 ? -11.554 22.455  37.921 1.00 147.07 ? 612 LYS   A CA  1 
ATOM   2465 C  C   . LYS   A 1 316 ? -12.458 23.583  37.436 1.00 151.24 ? 612 LYS   A C   1 
ATOM   2466 O  O   . LYS   A 1 316 ? -12.745 24.529  38.177 1.00 153.54 ? 612 LYS   A O   1 
ATOM   2467 C  CB  . LYS   A 1 316 ? -10.264 22.405  37.102 1.00 145.84 ? 612 LYS   A CB  1 
ATOM   2468 C  CG  . LYS   A 1 316 ? -9.236  21.408  37.602 1.00 142.75 ? 612 LYS   A CG  1 
ATOM   2469 C  CD  . LYS   A 1 316 ? -7.876  21.687  36.989 1.00 148.14 ? 612 LYS   A CD  1 
ATOM   2470 C  CE  . LYS   A 1 316 ? -7.442  23.124  37.254 1.00 159.19 ? 612 LYS   A CE  1 
ATOM   2471 N  NZ  . LYS   A 1 316 ? -6.352  23.584  36.340 1.00 166.86 ? 612 LYS   A NZ  1 
ATOM   2472 N  N   . LYS   A 1 317 ? -12.941 23.482  36.195 1.00 144.44 ? 613 LYS   A N   1 
ATOM   2473 C  CA  . LYS   A 1 317 ? -13.668 24.583  35.569 1.00 149.50 ? 613 LYS   A CA  1 
ATOM   2474 C  C   . LYS   A 1 317 ? -14.965 24.947  36.289 1.00 149.24 ? 613 LYS   A C   1 
ATOM   2475 O  O   . LYS   A 1 317 ? -15.520 26.018  36.012 1.00 160.34 ? 613 LYS   A O   1 
ATOM   2476 C  CB  . LYS   A 1 317 ? -13.957 24.244  34.107 1.00 145.84 ? 613 LYS   A CB  1 
ATOM   2477 C  CG  . LYS   A 1 317 ? -12.833 24.584  33.149 1.00 149.99 ? 613 LYS   A CG  1 
ATOM   2478 C  CD  . LYS   A 1 317 ? -12.207 23.339  32.579 1.00 143.75 ? 613 LYS   A CD  1 
ATOM   2479 C  CE  . LYS   A 1 317 ? -11.017 23.681  31.700 1.00 148.51 ? 613 LYS   A CE  1 
ATOM   2480 N  NZ  . LYS   A 1 317 ? -10.581 22.507  30.883 1.00 143.06 ? 613 LYS   A NZ  1 
ATOM   2481 N  N   . MET   A 1 318 ? -15.467 24.093  37.182 1.00 144.29 ? 614 MET   A N   1 
ATOM   2482 C  CA  . MET   A 1 318 ? -16.560 24.459  38.075 1.00 146.08 ? 614 MET   A CA  1 
ATOM   2483 C  C   . MET   A 1 318 ? -16.077 25.121  39.350 1.00 150.27 ? 614 MET   A C   1 
ATOM   2484 O  O   . MET   A 1 318 ? -16.889 25.728  40.057 1.00 153.33 ? 614 MET   A O   1 
ATOM   2485 C  CB  . MET   A 1 318 ? -17.385 23.228  38.456 1.00 136.13 ? 614 MET   A CB  1 
ATOM   2486 C  CG  . MET   A 1 318 ? -18.086 22.581  37.288 1.00 139.28 ? 614 MET   A CG  1 
ATOM   2487 S  SD  . MET   A 1 318 ? -18.730 20.944  37.668 1.00 132.44 ? 614 MET   A SD  1 
ATOM   2488 C  CE  . MET   A 1 318 ? -19.913 21.298  38.969 1.00 125.08 ? 614 MET   A CE  1 
ATOM   2489 N  N   . ASP   A 1 319 ? -14.780 25.019  39.645 1.00 152.13 ? 615 ASP   A N   1 
ATOM   2490 C  CA  . ASP   A 1 319 ? -14.203 25.396  40.931 1.00 158.92 ? 615 ASP   A CA  1 
ATOM   2491 C  C   . ASP   A 1 319 ? -14.819 24.582  42.060 1.00 151.18 ? 615 ASP   A C   1 
ATOM   2492 O  O   . ASP   A 1 319 ? -15.702 25.069  42.775 1.00 153.24 ? 615 ASP   A O   1 
ATOM   2493 C  CB  . ASP   A 1 319 ? -14.376 26.889  41.199 1.00 170.07 ? 615 ASP   A CB  1 
ATOM   2494 C  CG  . ASP   A 1 319 ? -13.252 27.454  42.043 1.00 181.68 ? 615 ASP   A CG  1 
ATOM   2495 O  OD1 . ASP   A 1 319 ? -12.088 27.059  41.803 1.00 183.51 ? 615 ASP   A OD1 1 
ATOM   2496 O  OD2 . ASP   A 1 319 ? -13.527 28.288  42.935 1.00 187.64 ? 615 ASP   A OD2 1 
ATOM   2497 N  N   . LEU   A 1 320 ? -14.361 23.343  42.224 1.00 145.49 ? 616 LEU   A N   1 
ATOM   2498 C  CA  . LEU   A 1 320 ? -14.820 22.467  43.290 1.00 143.30 ? 616 LEU   A CA  1 
ATOM   2499 C  C   . LEU   A 1 320 ? -13.696 22.223  44.289 1.00 147.07 ? 616 LEU   A C   1 
ATOM   2500 O  O   . LEU   A 1 320 ? -12.511 22.367  43.972 1.00 149.32 ? 616 LEU   A O   1 
ATOM   2501 C  CB  . LEU   A 1 320 ? -15.324 21.132  42.729 1.00 130.55 ? 616 LEU   A CB  1 
ATOM   2502 C  CG  . LEU   A 1 320 ? -16.501 21.254  41.763 1.00 128.86 ? 616 LEU   A CG  1 
ATOM   2503 C  CD1 . LEU   A 1 320 ? -17.003 19.868  41.356 1.00 125.06 ? 616 LEU   A CD1 1 
ATOM   2504 C  CD2 . LEU   A 1 320 ? -17.621 22.085  42.366 1.00 132.09 ? 616 LEU   A CD2 1 
ATOM   2505 N  N   . ASP   A 1 321 ? -14.084 21.850  45.509 1.00 142.10 ? 617 ASP   A N   1 
ATOM   2506 C  CA  . ASP   A 1 321 ? -13.117 21.521  46.548 1.00 146.97 ? 617 ASP   A CA  1 
ATOM   2507 C  C   . ASP   A 1 321 ? -12.437 20.191  46.244 1.00 136.94 ? 617 ASP   A C   1 
ATOM   2508 O  O   . ASP   A 1 321 ? -12.874 19.144  46.729 1.00 128.26 ? 617 ASP   A O   1 
ATOM   2509 C  CB  . ASP   A 1 321 ? -13.806 21.481  47.920 1.00 152.72 ? 617 ASP   A CB  1 
ATOM   2510 C  CG  . ASP   A 1 321 ? -12.839 21.210  49.065 1.00 160.35 ? 617 ASP   A CG  1 
ATOM   2511 O  OD1 . ASP   A 1 321 ? -12.714 20.042  49.488 1.00 159.34 ? 617 ASP   A OD1 1 
ATOM   2512 O  OD2 . ASP   A 1 321 ? -12.198 22.165  49.545 1.00 169.56 ? 617 ASP   A OD2 1 
ATOM   2513 N  N   . MET   A 1 322 ? -11.363 20.218  45.453 1.00 136.26 ? 618 MET   A N   1 
ATOM   2514 C  CA  . MET   A 1 322 ? -10.635 19.002  45.106 1.00 137.35 ? 618 MET   A CA  1 
ATOM   2515 C  C   . MET   A 1 322 ? -9.617  18.581  46.168 1.00 143.55 ? 618 MET   A C   1 
ATOM   2516 O  O   . MET   A 1 322 ? -9.047  17.489  46.055 1.00 145.13 ? 618 MET   A O   1 
ATOM   2517 C  CB  . MET   A 1 322 ? -9.934  19.166  43.741 1.00 140.31 ? 618 MET   A CB  1 
ATOM   2518 C  CG  . MET   A 1 322 ? -10.853 18.956  42.529 1.00 137.54 ? 618 MET   A CG  1 
ATOM   2519 S  SD  . MET   A 1 322 ? -10.058 18.990  40.887 1.00 141.05 ? 618 MET   A SD  1 
ATOM   2520 C  CE  . MET   A 1 322 ? -8.786  17.736  41.072 1.00 144.70 ? 618 MET   A CE  1 
ATOM   2521 N  N   . ARG   A 1 323 ? -9.388  19.395  47.202 1.00 149.17 ? 619 ARG   A N   1 
ATOM   2522 C  CA  . ARG   A 1 323 ? -8.458  18.998  48.257 1.00 158.92 ? 619 ARG   A CA  1 
ATOM   2523 C  C   . ARG   A 1 323 ? -8.951  17.761  49.004 1.00 156.91 ? 619 ARG   A C   1 
ATOM   2524 O  O   . ARG   A 1 323 ? -8.154  16.886  49.363 1.00 158.14 ? 619 ARG   A O   1 
ATOM   2525 C  CB  . ARG   A 1 323 ? -8.251  20.151  49.239 1.00 168.17 ? 619 ARG   A CB  1 
ATOM   2526 C  CG  . ARG   A 1 323 ? -7.512  21.342  48.675 1.00 178.59 ? 619 ARG   A CG  1 
ATOM   2527 C  CD  . ARG   A 1 323 ? -8.056  22.620  49.277 1.00 188.00 ? 619 ARG   A CD  1 
ATOM   2528 N  NE  . ARG   A 1 323 ? -9.062  23.234  48.415 1.00 190.49 ? 619 ARG   A NE  1 
ATOM   2529 C  CZ  . ARG   A 1 323 ? -9.972  24.108  48.833 1.00 192.81 ? 619 ARG   A CZ  1 
ATOM   2530 N  NH1 . ARG   A 1 323 ? -10.014 24.458  50.116 1.00 191.15 ? 619 ARG   A NH1 1 
ATOM   2531 N  NH2 . ARG   A 1 323 ? -10.844 24.622  47.970 1.00 190.20 ? 619 ARG   A NH2 1 
ATOM   2532 N  N   . LYS   A 1 324 ? -10.255 17.672  49.250 1.00 148.12 ? 620 LYS   A N   1 
ATOM   2533 C  CA  . LYS   A 1 324 ? -10.839 16.626  50.077 1.00 133.76 ? 620 LYS   A CA  1 
ATOM   2534 C  C   . LYS   A 1 324 ? -11.587 15.619  49.213 1.00 124.51 ? 620 LYS   A C   1 
ATOM   2535 O  O   . LYS   A 1 324 ? -12.311 15.996  48.287 1.00 127.95 ? 620 LYS   A O   1 
ATOM   2536 C  CB  . LYS   A 1 324 ? -11.786 17.231  51.121 1.00 135.06 ? 620 LYS   A CB  1 
ATOM   2537 C  CG  . LYS   A 1 324 ? -11.275 17.182  52.557 1.00 140.63 ? 620 LYS   A CG  1 
ATOM   2538 C  CD  . LYS   A 1 324 ? -9.978  17.956  52.756 1.00 146.51 ? 620 LYS   A CD  1 
ATOM   2539 C  CE  . LYS   A 1 324 ? -9.432  17.732  54.158 1.00 148.38 ? 620 LYS   A CE  1 
ATOM   2540 N  NZ  . LYS   A 1 324 ? -8.073  18.308  54.330 1.00 156.52 ? 620 LYS   A NZ  1 
ATOM   2541 N  N   . THR   A 1 325 ? -11.398 14.334  49.517 1.00 111.27 ? 621 THR   A N   1 
ATOM   2542 C  CA  . THR   A 1 325 ? -12.146 13.288  48.827 1.00 105.13 ? 621 THR   A CA  1 
ATOM   2543 C  C   . THR   A 1 325 ? -13.637 13.362  49.152 1.00 112.73 ? 621 THR   A C   1 
ATOM   2544 O  O   . THR   A 1 325 ? -14.486 13.169  48.267 1.00 98.32  ? 621 THR   A O   1 
ATOM   2545 C  CB  . THR   A 1 325 ? -11.578 11.914  49.193 1.00 104.45 ? 621 THR   A CB  1 
ATOM   2546 O  OG1 . THR   A 1 325 ? -12.561 10.907  48.939 1.00 100.30 ? 621 THR   A OG1 1 
ATOM   2547 C  CG2 . THR   A 1 325 ? -11.174 11.852  50.676 1.00 113.84 ? 621 THR   A CG2 1 
ATOM   2548 N  N   . SER   A 1 326 ? -13.967 13.659  50.416 1.00 119.48 ? 622 SER   A N   1 
ATOM   2549 C  CA  . SER   A 1 326 ? -15.322 13.721  50.953 1.00 113.69 ? 622 SER   A CA  1 
ATOM   2550 C  C   . SER   A 1 326 ? -16.085 14.967  50.518 1.00 106.00 ? 622 SER   A C   1 
ATOM   2551 O  O   . SER   A 1 326 ? -17.227 15.158  50.949 1.00 105.75 ? 622 SER   A O   1 
ATOM   2552 C  CB  . SER   A 1 326 ? -15.271 13.644  52.485 1.00 103.86 ? 622 SER   A CB  1 
ATOM   2553 O  OG  . SER   A 1 326 ? -13.995 14.018  52.984 1.00 108.40 ? 622 SER   A OG  1 
ATOM   2554 N  N   . SER   A 1 327 ? -15.498 15.820  49.685 1.00 109.90 ? 623 SER   A N   1 
ATOM   2555 C  CA  . SER   A 1 327 ? -16.269 16.911  49.110 1.00 118.56 ? 623 SER   A CA  1 
ATOM   2556 C  C   . SER   A 1 327 ? -17.187 16.452  47.976 1.00 114.61 ? 623 SER   A C   1 
ATOM   2557 O  O   . SER   A 1 327 ? -18.050 17.230  47.558 1.00 110.65 ? 623 SER   A O   1 
ATOM   2558 C  CB  . SER   A 1 327 ? -15.322 17.997  48.602 1.00 127.77 ? 623 SER   A CB  1 
ATOM   2559 O  OG  . SER   A 1 327 ? -14.632 17.561  47.440 1.00 117.37 ? 623 SER   A OG  1 
ATOM   2560 N  N   . LEU   A 1 328 ? -17.016 15.223  47.469 1.00 112.89 ? 624 LEU   A N   1 
ATOM   2561 C  CA  . LEU   A 1 328 ? -17.814 14.660  46.352 1.00 103.25 ? 624 LEU   A CA  1 
ATOM   2562 C  C   . LEU   A 1 328 ? -17.711 15.489  45.075 1.00 108.72 ? 624 LEU   A C   1 
ATOM   2563 O  O   . LEU   A 1 328 ? -18.642 15.530  44.254 1.00 104.73 ? 624 LEU   A O   1 
ATOM   2564 C  CB  . LEU   A 1 328 ? -19.279 14.470  46.748 1.00 100.16 ? 624 LEU   A CB  1 
ATOM   2565 C  CG  . LEU   A 1 328 ? -19.427 13.664  48.049 1.00 93.28  ? 624 LEU   A CG  1 
ATOM   2566 C  CD1 . LEU   A 1 328 ? -20.868 13.267  48.288 1.00 90.68  ? 624 LEU   A CD1 1 
ATOM   2567 C  CD2 . LEU   A 1 328 ? -18.544 12.442  47.975 1.00 88.99  ? 624 LEU   A CD2 1 
ATOM   2568 N  N   . TRP   A 1 329 ? -16.559 16.123  44.876 1.00 110.91 ? 625 TRP   A N   1 
ATOM   2569 C  CA  . TRP   A 1 329 ? -16.341 16.862  43.642 1.00 111.01 ? 625 TRP   A CA  1 
ATOM   2570 C  C   . TRP   A 1 329 ? -16.424 15.943  42.426 1.00 108.74 ? 625 TRP   A C   1 
ATOM   2571 O  O   . TRP   A 1 329 ? -16.871 16.368  41.354 1.00 107.48 ? 625 TRP   A O   1 
ATOM   2572 C  CB  . TRP   A 1 329 ? -14.993 17.579  43.696 1.00 115.76 ? 625 TRP   A CB  1 
ATOM   2573 C  CG  . TRP   A 1 329 ? -13.827 16.653  43.865 1.00 113.62 ? 625 TRP   A CG  1 
ATOM   2574 C  CD1 . TRP   A 1 329 ? -13.260 16.261  45.031 1.00 119.66 ? 625 TRP   A CD1 1 
ATOM   2575 C  CD2 . TRP   A 1 329 ? -13.083 16.014  42.820 1.00 119.91 ? 625 TRP   A CD2 1 
ATOM   2576 N  NE1 . TRP   A 1 329 ? -12.207 15.409  44.786 1.00 120.06 ? 625 TRP   A NE1 1 
ATOM   2577 C  CE2 . TRP   A 1 329 ? -12.079 15.242  43.434 1.00 118.37 ? 625 TRP   A CE2 1 
ATOM   2578 C  CE3 . TRP   A 1 329 ? -13.172 16.018  41.425 1.00 107.49 ? 625 TRP   A CE3 1 
ATOM   2579 C  CZ2 . TRP   A 1 329 ? -11.167 14.484  42.701 1.00 116.91 ? 625 TRP   A CZ2 1 
ATOM   2580 C  CZ3 . TRP   A 1 329 ? -12.268 15.268  40.699 1.00 112.14 ? 625 TRP   A CZ3 1 
ATOM   2581 C  CH2 . TRP   A 1 329 ? -11.279 14.512  41.335 1.00 115.90 ? 625 TRP   A CH2 1 
ATOM   2582 N  N   . LYS   A 1 330 ? -16.000 14.679  42.576 1.00 104.70 ? 626 LYS   A N   1 
ATOM   2583 C  CA  . LYS   A 1 330 ? -16.108 13.715  41.480 1.00 99.56  ? 626 LYS   A CA  1 
ATOM   2584 C  C   . LYS   A 1 330 ? -17.564 13.451  41.122 1.00 90.93  ? 626 LYS   A C   1 
ATOM   2585 O  O   . LYS   A 1 330 ? -17.914 13.325  39.945 1.00 101.50 ? 626 LYS   A O   1 
ATOM   2586 C  CB  . LYS   A 1 330 ? -15.424 12.397  41.857 1.00 103.33 ? 626 LYS   A CB  1 
ATOM   2587 C  CG  . LYS   A 1 330 ? -13.908 12.386  41.746 1.00 103.67 ? 626 LYS   A CG  1 
ATOM   2588 C  CD  . LYS   A 1 330 ? -13.337 11.002  42.037 1.00 95.83  ? 626 LYS   A CD  1 
ATOM   2589 C  CE  . LYS   A 1 330 ? -11.846 10.936  41.727 1.00 91.55  ? 626 LYS   A CE  1 
ATOM   2590 N  NZ  . LYS   A 1 330 ? -11.226 9.638   42.128 1.00 86.16  ? 626 LYS   A NZ  1 
ATOM   2591 N  N   . ASP   A 1 331 ? -18.421 13.336  42.132 1.00 95.70  ? 627 ASP   A N   1 
ATOM   2592 C  CA  . ASP   A 1 331 ? -19.831 13.039  41.913 1.00 91.89  ? 627 ASP   A CA  1 
ATOM   2593 C  C   . ASP   A 1 331 ? -20.531 14.192  41.222 1.00 97.21  ? 627 ASP   A C   1 
ATOM   2594 O  O   . ASP   A 1 331 ? -21.227 13.999  40.216 1.00 103.17 ? 627 ASP   A O   1 
ATOM   2595 C  CB  . ASP   A 1 331 ? -20.498 12.739  43.250 1.00 93.42  ? 627 ASP   A CB  1 
ATOM   2596 C  CG  . ASP   A 1 331 ? -19.838 11.591  43.965 1.00 87.76  ? 627 ASP   A CG  1 
ATOM   2597 O  OD1 . ASP   A 1 331 ? -18.670 11.728  44.370 1.00 82.42  ? 627 ASP   A OD1 1 
ATOM   2598 O  OD2 . ASP   A 1 331 ? -20.480 10.541  44.087 1.00 75.89  ? 627 ASP   A OD2 1 
ATOM   2599 N  N   . GLN   A 1 332 ? -20.351 15.401  41.751 1.00 98.21  ? 628 GLN   A N   1 
ATOM   2600 C  CA  . GLN   A 1 332 ? -20.974 16.584  41.168 1.00 108.25 ? 628 GLN   A CA  1 
ATOM   2601 C  C   . GLN   A 1 332 ? -20.548 16.775  39.719 1.00 105.17 ? 628 GLN   A C   1 
ATOM   2602 O  O   . GLN   A 1 332 ? -21.382 17.026  38.840 1.00 100.54 ? 628 GLN   A O   1 
ATOM   2603 C  CB  . GLN   A 1 332 ? -20.614 17.811  41.997 1.00 116.56 ? 628 GLN   A CB  1 
ATOM   2604 C  CG  . GLN   A 1 332 ? -21.795 18.647  42.403 1.00 118.05 ? 628 GLN   A CG  1 
ATOM   2605 C  CD  . GLN   A 1 332 ? -21.482 19.492  43.621 1.00 123.48 ? 628 GLN   A CD  1 
ATOM   2606 O  OE1 . GLN   A 1 332 ? -20.318 19.667  43.989 1.00 121.01 ? 628 GLN   A OE1 1 
ATOM   2607 N  NE2 . GLN   A 1 332 ? -22.519 20.012  44.259 1.00 126.98 ? 628 GLN   A NE2 1 
ATOM   2608 N  N   . ALA   A 1 333 ? -19.246 16.660  39.451 1.00 99.37  ? 629 ALA   A N   1 
ATOM   2609 C  CA  . ALA   A 1 333 ? -18.760 16.802  38.085 1.00 106.40 ? 629 ALA   A CA  1 
ATOM   2610 C  C   . ALA   A 1 333 ? -19.255 15.680  37.179 1.00 105.57 ? 629 ALA   A C   1 
ATOM   2611 O  O   . ALA   A 1 333 ? -19.291 15.860  35.957 1.00 95.26  ? 629 ALA   A O   1 
ATOM   2612 C  CB  . ALA   A 1 333 ? -17.230 16.859  38.066 1.00 101.93 ? 629 ALA   A CB  1 
ATOM   2613 N  N   . LEU   A 1 334 ? -19.657 14.536  37.745 1.00 97.62  ? 630 LEU   A N   1 
ATOM   2614 C  CA  . LEU   A 1 334 ? -20.199 13.470  36.910 1.00 84.60  ? 630 LEU   A CA  1 
ATOM   2615 C  C   . LEU   A 1 334 ? -21.643 13.755  36.501 1.00 90.95  ? 630 LEU   A C   1 
ATOM   2616 O  O   . LEU   A 1 334 ? -22.036 13.446  35.365 1.00 100.73 ? 630 LEU   A O   1 
ATOM   2617 C  CB  . LEU   A 1 334 ? -20.106 12.124  37.615 1.00 77.46  ? 630 LEU   A CB  1 
ATOM   2618 C  CG  . LEU   A 1 334 ? -20.493 10.899  36.787 1.00 84.49  ? 630 LEU   A CG  1 
ATOM   2619 C  CD1 . LEU   A 1 334 ? -19.246 10.158  36.368 1.00 82.55  ? 630 LEU   A CD1 1 
ATOM   2620 C  CD2 . LEU   A 1 334 ? -21.426 9.983   37.547 1.00 81.95  ? 630 LEU   A CD2 1 
ATOM   2621 N  N   . VAL   A 1 335 ? -22.439 14.361  37.388 1.00 85.53  ? 631 VAL   A N   1 
ATOM   2622 C  CA  . VAL   A 1 335 ? -23.820 14.681  37.036 1.00 92.60  ? 631 VAL   A CA  1 
ATOM   2623 C  C   . VAL   A 1 335 ? -23.868 15.746  35.939 1.00 101.87 ? 631 VAL   A C   1 
ATOM   2624 O  O   . VAL   A 1 335 ? -24.663 15.637  34.996 1.00 104.04 ? 631 VAL   A O   1 
ATOM   2625 C  CB  . VAL   A 1 335 ? -24.621 15.103  38.282 1.00 94.15  ? 631 VAL   A CB  1 
ATOM   2626 C  CG1 . VAL   A 1 335 ? -25.926 15.760  37.860 1.00 99.62  ? 631 VAL   A CG1 1 
ATOM   2627 C  CG2 . VAL   A 1 335 ? -24.902 13.887  39.174 1.00 86.63  ? 631 VAL   A CG2 1 
ATOM   2628 N  N   . GLU   A 1 336 ? -23.004 16.772  36.024 1.00 100.16 ? 632 GLU   A N   1 
ATOM   2629 C  CA  . GLU   A 1 336 ? -22.979 17.820  34.997 1.00 109.42 ? 632 GLU   A CA  1 
ATOM   2630 C  C   . GLU   A 1 336 ? -22.623 17.254  33.630 1.00 101.74 ? 632 GLU   A C   1 
ATOM   2631 O  O   . GLU   A 1 336 ? -23.209 17.649  32.613 1.00 98.06  ? 632 GLU   A O   1 
ATOM   2632 C  CB  . GLU   A 1 336 ? -21.973 18.916  35.351 1.00 115.70 ? 632 GLU   A CB  1 
ATOM   2633 C  CG  . GLU   A 1 336 ? -22.008 19.401  36.765 1.00 129.05 ? 632 GLU   A CG  1 
ATOM   2634 C  CD  . GLU   A 1 336 ? -23.269 20.156  37.087 1.00 137.48 ? 632 GLU   A CD  1 
ATOM   2635 O  OE1 . GLU   A 1 336 ? -23.963 20.590  36.136 1.00 136.66 ? 632 GLU   A OE1 1 
ATOM   2636 O  OE2 . GLU   A 1 336 ? -23.561 20.297  38.300 1.00 140.39 ? 632 GLU   A OE2 1 
ATOM   2637 N  N   . ILE   A 1 337 ? -21.630 16.360  33.590 1.00 96.72  ? 633 ILE   A N   1 
ATOM   2638 C  CA  . ILE   A 1 337 ? -21.182 15.763  32.336 1.00 95.12  ? 633 ILE   A CA  1 
ATOM   2639 C  C   . ILE   A 1 337 ? -22.329 15.040  31.645 1.00 98.25  ? 633 ILE   A C   1 
ATOM   2640 O  O   . ILE   A 1 337 ? -22.504 15.145  30.425 1.00 89.47  ? 633 ILE   A O   1 
ATOM   2641 C  CB  . ILE   A 1 337 ? -19.983 14.832  32.608 1.00 86.53  ? 633 ILE   A CB  1 
ATOM   2642 C  CG1 . ILE   A 1 337 ? -18.743 15.673  32.937 1.00 96.15  ? 633 ILE   A CG1 1 
ATOM   2643 C  CG2 . ILE   A 1 337 ? -19.743 13.874  31.447 1.00 82.20  ? 633 ILE   A CG2 1 
ATOM   2644 C  CD1 . ILE   A 1 337 ? -17.548 14.874  33.425 1.00 94.67  ? 633 ILE   A CD1 1 
ATOM   2645 N  N   . ASN   A 1 338 ? -23.153 14.327  32.410 1.00 92.42  ? 634 ASN   A N   1 
ATOM   2646 C  CA  . ASN   A 1 338 ? -24.212 13.528  31.806 1.00 85.23  ? 634 ASN   A CA  1 
ATOM   2647 C  C   . ASN   A 1 338 ? -25.448 14.339  31.425 1.00 90.02  ? 634 ASN   A C   1 
ATOM   2648 O  O   . ASN   A 1 338 ? -26.208 13.894  30.553 1.00 85.29  ? 634 ASN   A O   1 
ATOM   2649 C  CB  . ASN   A 1 338 ? -24.597 12.384  32.741 1.00 82.87  ? 634 ASN   A CB  1 
ATOM   2650 C  CG  . ASN   A 1 338 ? -23.621 11.231  32.659 1.00 85.19  ? 634 ASN   A CG  1 
ATOM   2651 O  OD1 . ASN   A 1 338 ? -23.684 10.413  31.737 1.00 89.52  ? 634 ASN   A OD1 1 
ATOM   2652 N  ND2 . ASN   A 1 338 ? -22.689 11.179  33.602 1.00 73.41  ? 634 ASN   A ND2 1 
ATOM   2653 N  N   . ILE   A 1 339 ? -25.667 15.508  32.047 1.00 94.46  ? 635 ILE   A N   1 
ATOM   2654 C  CA  . ILE   A 1 339 ? -26.677 16.437  31.540 1.00 96.93  ? 635 ILE   A CA  1 
ATOM   2655 C  C   . ILE   A 1 339 ? -26.245 16.992  30.191 1.00 94.67  ? 635 ILE   A C   1 
ATOM   2656 O  O   . ILE   A 1 339 ? -27.085 17.294  29.336 1.00 103.28 ? 635 ILE   A O   1 
ATOM   2657 C  CB  . ILE   A 1 339 ? -26.935 17.577  32.546 1.00 107.92 ? 635 ILE   A CB  1 
ATOM   2658 C  CG1 . ILE   A 1 339 ? -27.525 17.035  33.849 1.00 95.14  ? 635 ILE   A CG1 1 
ATOM   2659 C  CG2 . ILE   A 1 339 ? -27.873 18.645  31.964 1.00 102.37 ? 635 ILE   A CG2 1 
ATOM   2660 C  CD1 . ILE   A 1 339 ? -27.686 18.092  34.928 1.00 105.37 ? 635 ILE   A CD1 1 
ATOM   2661 N  N   . ALA   A 1 340 ? -24.933 17.123  29.974 1.00 93.58  ? 636 ALA   A N   1 
ATOM   2662 C  CA  . ALA   A 1 340 ? -24.415 17.742  28.758 1.00 97.52  ? 636 ALA   A CA  1 
ATOM   2663 C  C   . ALA   A 1 340 ? -24.398 16.775  27.576 1.00 98.48  ? 636 ALA   A C   1 
ATOM   2664 O  O   . ALA   A 1 340 ? -24.655 17.178  26.430 1.00 96.33  ? 636 ALA   A O   1 
ATOM   2665 C  CB  . ALA   A 1 340 ? -23.014 18.283  29.021 1.00 99.55  ? 636 ALA   A CB  1 
ATOM   2666 N  N   . VAL   A 1 341 ? -24.055 15.512  27.823 1.00 95.04  ? 637 VAL   A N   1 
ATOM   2667 C  CA  . VAL   A 1 341 ? -24.144 14.506  26.771 1.00 92.61  ? 637 VAL   A CA  1 
ATOM   2668 C  C   . VAL   A 1 341 ? -25.576 14.410  26.278 1.00 100.27 ? 637 VAL   A C   1 
ATOM   2669 O  O   . VAL   A 1 341 ? -25.850 14.522  25.078 1.00 102.87 ? 637 VAL   A O   1 
ATOM   2670 C  CB  . VAL   A 1 341 ? -23.636 13.142  27.272 1.00 86.22  ? 637 VAL   A CB  1 
ATOM   2671 C  CG1 . VAL   A 1 341 ? -23.975 12.053  26.257 1.00 86.43  ? 637 VAL   A CG1 1 
ATOM   2672 C  CG2 . VAL   A 1 341 ? -22.143 13.184  27.517 1.00 86.94  ? 637 VAL   A CG2 1 
ATOM   2673 N  N   . LEU   A 1 342 ? -26.513 14.209  27.205 1.00 97.38  ? 638 LEU   A N   1 
ATOM   2674 C  CA  . LEU   A 1 342 ? -27.920 14.128  26.831 1.00 98.78  ? 638 LEU   A CA  1 
ATOM   2675 C  C   . LEU   A 1 342 ? -28.358 15.367  26.060 1.00 100.75 ? 638 LEU   A C   1 
ATOM   2676 O  O   . LEU   A 1 342 ? -28.940 15.260  24.977 1.00 93.18  ? 638 LEU   A O   1 
ATOM   2677 C  CB  . LEU   A 1 342 ? -28.788 13.943  28.074 1.00 99.18  ? 638 LEU   A CB  1 
ATOM   2678 C  CG  . LEU   A 1 342 ? -28.513 12.707  28.928 1.00 92.01  ? 638 LEU   A CG  1 
ATOM   2679 C  CD1 . LEU   A 1 342 ? -29.588 12.558  29.960 1.00 81.36  ? 638 LEU   A CD1 1 
ATOM   2680 C  CD2 . LEU   A 1 342 ? -28.427 11.468  28.060 1.00 92.22  ? 638 LEU   A CD2 1 
ATOM   2681 N  N   . TYR   A 1 343 ? -28.085 16.556  26.605 1.00 108.55 ? 639 TYR   A N   1 
ATOM   2682 C  CA  . TYR   A 1 343 ? -28.544 17.788  25.962 1.00 107.31 ? 639 TYR   A CA  1 
ATOM   2683 C  C   . TYR   A 1 343 ? -27.937 17.949  24.580 1.00 109.01 ? 639 TYR   A C   1 
ATOM   2684 O  O   . TYR   A 1 343 ? -28.620 18.373  23.642 1.00 104.16 ? 639 TYR   A O   1 
ATOM   2685 C  CB  . TYR   A 1 343 ? -28.211 19.002  26.834 1.00 117.38 ? 639 TYR   A CB  1 
ATOM   2686 C  CG  . TYR   A 1 343 ? -28.491 20.341  26.169 1.00 114.35 ? 639 TYR   A CG  1 
ATOM   2687 C  CD1 . TYR   A 1 343 ? -29.783 20.855  26.113 1.00 113.40 ? 639 TYR   A CD1 1 
ATOM   2688 C  CD2 . TYR   A 1 343 ? -27.460 21.102  25.634 1.00 116.37 ? 639 TYR   A CD2 1 
ATOM   2689 C  CE1 . TYR   A 1 343 ? -30.045 22.074  25.525 1.00 126.34 ? 639 TYR   A CE1 1 
ATOM   2690 C  CE2 . TYR   A 1 343 ? -27.713 22.329  25.034 1.00 127.72 ? 639 TYR   A CE2 1 
ATOM   2691 C  CZ  . TYR   A 1 343 ? -29.008 22.807  24.982 1.00 128.68 ? 639 TYR   A CZ  1 
ATOM   2692 O  OH  . TYR   A 1 343 ? -29.266 24.025  24.399 1.00 133.52 ? 639 TYR   A OH  1 
ATOM   2693 N  N   . SER   A 1 344 ? -26.656 17.618  24.428 1.00 109.55 ? 640 SER   A N   1 
ATOM   2694 C  CA  . SER   A 1 344 ? -26.025 17.739  23.117 1.00 99.58  ? 640 SER   A CA  1 
ATOM   2695 C  C   . SER   A 1 344 ? -26.690 16.812  22.113 1.00 99.80  ? 640 SER   A C   1 
ATOM   2696 O  O   . SER   A 1 344 ? -27.074 17.240  21.019 1.00 93.63  ? 640 SER   A O   1 
ATOM   2697 C  CB  . SER   A 1 344 ? -24.529 17.451  23.220 1.00 94.96  ? 640 SER   A CB  1 
ATOM   2698 O  OG  . SER   A 1 344 ? -23.947 18.273  24.227 1.00 102.64 ? 640 SER   A OG  1 
ATOM   2699 N  N   . PHE   A 1 345 ? -26.855 15.538  22.482 1.00 96.91  ? 641 PHE   A N   1 
ATOM   2700 C  CA  . PHE   A 1 345 ? -27.514 14.589  21.588 1.00 101.09 ? 641 PHE   A CA  1 
ATOM   2701 C  C   . PHE   A 1 345 ? -28.948 15.019  21.268 1.00 105.56 ? 641 PHE   A C   1 
ATOM   2702 O  O   . PHE   A 1 345 ? -29.366 14.987  20.105 1.00 97.41  ? 641 PHE   A O   1 
ATOM   2703 C  CB  . PHE   A 1 345 ? -27.494 13.183  22.201 1.00 89.49  ? 641 PHE   A CB  1 
ATOM   2704 C  CG  . PHE   A 1 345 ? -26.239 12.373  21.906 1.00 79.29  ? 641 PHE   A CG  1 
ATOM   2705 C  CD1 . PHE   A 1 345 ? -25.008 12.738  22.428 1.00 82.26  ? 641 PHE   A CD1 1 
ATOM   2706 C  CD2 . PHE   A 1 345 ? -26.310 11.217  21.135 1.00 72.24  ? 641 PHE   A CD2 1 
ATOM   2707 C  CE1 . PHE   A 1 345 ? -23.871 11.980  22.172 1.00 80.84  ? 641 PHE   A CE1 1 
ATOM   2708 C  CE2 . PHE   A 1 345 ? -25.174 10.450  20.886 1.00 71.43  ? 641 PHE   A CE2 1 
ATOM   2709 C  CZ  . PHE   A 1 345 ? -23.951 10.841  21.404 1.00 75.26  ? 641 PHE   A CZ  1 
ATOM   2710 N  N   . GLN   A 1 346 ? -29.716 15.435  22.283 1.00 103.91 ? 642 GLN   A N   1 
ATOM   2711 C  CA  . GLN   A 1 346 ? -31.120 15.777  22.049 1.00 105.04 ? 642 GLN   A CA  1 
ATOM   2712 C  C   . GLN   A 1 346 ? -31.263 17.008  21.164 1.00 105.63 ? 642 GLN   A C   1 
ATOM   2713 O  O   . GLN   A 1 346 ? -32.177 17.079  20.332 1.00 96.18  ? 642 GLN   A O   1 
ATOM   2714 C  CB  . GLN   A 1 346 ? -31.849 16.000  23.373 1.00 111.62 ? 642 GLN   A CB  1 
ATOM   2715 C  CG  . GLN   A 1 346 ? -32.160 14.731  24.147 1.00 116.70 ? 642 GLN   A CG  1 
ATOM   2716 C  CD  . GLN   A 1 346 ? -32.489 15.022  25.602 1.00 120.94 ? 642 GLN   A CD  1 
ATOM   2717 O  OE1 . GLN   A 1 346 ? -31.630 15.465  26.363 1.00 121.51 ? 642 GLN   A OE1 1 
ATOM   2718 N  NE2 . GLN   A 1 346 ? -33.739 14.793  25.988 1.00 121.32 ? 642 GLN   A NE2 1 
ATOM   2719 N  N   . SER   A 1 347 ? -30.376 17.992  21.328 1.00 110.68 ? 643 SER   A N   1 
ATOM   2720 C  CA  . SER   A 1 347 ? -30.502 19.238  20.582 1.00 112.18 ? 643 SER   A CA  1 
ATOM   2721 C  C   . SER   A 1 347 ? -30.147 19.081  19.103 1.00 118.07 ? 643 SER   A C   1 
ATOM   2722 O  O   . SER   A 1 347 ? -30.482 19.968  18.305 1.00 119.83 ? 643 SER   A O   1 
ATOM   2723 C  CB  . SER   A 1 347 ? -29.637 20.326  21.243 1.00 112.35 ? 643 SER   A CB  1 
ATOM   2724 O  OG  . SER   A 1 347 ? -30.160 20.757  22.503 1.00 112.83 ? 643 SER   A OG  1 
ATOM   2725 N  N   . ASP   A 1 348 ? -29.499 17.978  18.718 1.00 115.33 ? 644 ASP   A N   1 
ATOM   2726 C  CA  . ASP   A 1 348 ? -29.223 17.653  17.322 1.00 103.80 ? 644 ASP   A CA  1 
ATOM   2727 C  C   . ASP   A 1 348 ? -30.154 16.571  16.780 1.00 103.60 ? 644 ASP   A C   1 
ATOM   2728 O  O   . ASP   A 1 348 ? -29.944 16.083  15.660 1.00 90.72  ? 644 ASP   A O   1 
ATOM   2729 C  CB  . ASP   A 1 348 ? -27.761 17.217  17.151 1.00 96.25  ? 644 ASP   A CB  1 
ATOM   2730 C  CG  . ASP   A 1 348 ? -26.767 18.257  17.667 1.00 100.74 ? 644 ASP   A CG  1 
ATOM   2731 O  OD1 . ASP   A 1 348 ? -27.199 19.384  17.982 1.00 105.90 ? 644 ASP   A OD1 1 
ATOM   2732 O  OD2 . ASP   A 1 348 ? -25.554 17.952  17.754 1.00 97.33  ? 644 ASP   A OD2 1 
ATOM   2733 N  N   . LYS   A 1 349 ? -31.177 16.188  17.550 1.00 112.37 ? 645 LYS   A N   1 
ATOM   2734 C  CA  . LYS   A 1 349 ? -32.131 15.148  17.156 1.00 120.09 ? 645 LYS   A CA  1 
ATOM   2735 C  C   . LYS   A 1 349 ? -31.422 13.827  16.874 1.00 103.42 ? 645 LYS   A C   1 
ATOM   2736 O  O   . LYS   A 1 349 ? -31.793 13.084  15.967 1.00 91.44  ? 645 LYS   A O   1 
ATOM   2737 C  CB  . LYS   A 1 349 ? -32.973 15.579  15.949 1.00 136.03 ? 645 LYS   A CB  1 
ATOM   2738 C  CG  . LYS   A 1 349 ? -34.430 15.095  15.984 1.00 145.74 ? 645 LYS   A CG  1 
ATOM   2739 C  CD  . LYS   A 1 349 ? -35.156 15.574  17.251 1.00 155.10 ? 645 LYS   A CD  1 
ATOM   2740 C  CE  . LYS   A 1 349 ? -36.630 15.160  17.270 1.00 157.31 ? 645 LYS   A CE  1 
ATOM   2741 N  NZ  . LYS   A 1 349 ? -36.817 13.683  17.364 1.00 150.47 ? 645 LYS   A NZ  1 
ATOM   2742 N  N   . VAL   A 1 350 ? -30.387 13.530  17.655 1.00 102.30 ? 646 VAL   A N   1 
ATOM   2743 C  CA  . VAL   A 1 350 ? -29.717 12.236  17.598 1.00 88.08  ? 646 VAL   A CA  1 
ATOM   2744 C  C   . VAL   A 1 350 ? -30.243 11.381  18.740 1.00 87.33  ? 646 VAL   A C   1 
ATOM   2745 O  O   . VAL   A 1 350 ? -30.231 11.803  19.913 1.00 85.24  ? 646 VAL   A O   1 
ATOM   2746 C  CB  . VAL   A 1 350 ? -28.190 12.382  17.670 1.00 77.87  ? 646 VAL   A CB  1 
ATOM   2747 C  CG1 . VAL   A 1 350 ? -27.527 10.993  17.634 1.00 67.63  ? 646 VAL   A CG1 1 
ATOM   2748 C  CG2 . VAL   A 1 350 ? -27.699 13.284  16.542 1.00 85.52  ? 646 VAL   A CG2 1 
ATOM   2749 N  N   . THR   A 1 351 ? -30.685 10.174  18.394 1.00 71.34  ? 647 THR   A N   1 
ATOM   2750 C  CA  . THR   A 1 351 ? -31.383 9.318   19.340 1.00 76.61  ? 647 THR   A CA  1 
ATOM   2751 C  C   . THR   A 1 351 ? -30.478 8.969   20.508 1.00 77.00  ? 647 THR   A C   1 
ATOM   2752 O  O   . THR   A 1 351 ? -29.345 8.508   20.317 1.00 79.61  ? 647 THR   A O   1 
ATOM   2753 C  CB  . THR   A 1 351 ? -31.855 8.038   18.638 1.00 76.72  ? 647 THR   A CB  1 
ATOM   2754 O  OG1 . THR   A 1 351 ? -32.657 8.368   17.491 1.00 82.51  ? 647 THR   A OG1 1 
ATOM   2755 C  CG2 . THR   A 1 351 ? -32.649 7.149   19.607 1.00 70.52  ? 647 THR   A CG2 1 
ATOM   2756 N  N   . ILE   A 1 352 ? -30.992 9.169   21.721 1.00 79.71  ? 648 ILE   A N   1 
ATOM   2757 C  CA  . ILE   A 1 352 ? -30.265 8.809   22.926 1.00 66.20  ? 648 ILE   A CA  1 
ATOM   2758 C  C   . ILE   A 1 352 ? -31.301 8.600   24.031 1.00 75.49  ? 648 ILE   A C   1 
ATOM   2759 O  O   . ILE   A 1 352 ? -32.392 9.179   23.990 1.00 74.99  ? 648 ILE   A O   1 
ATOM   2760 C  CB  . ILE   A 1 352 ? -29.213 9.892   23.291 1.00 67.94  ? 648 ILE   A CB  1 
ATOM   2761 C  CG1 . ILE   A 1 352 ? -28.224 9.358   24.354 1.00 72.66  ? 648 ILE   A CG1 1 
ATOM   2762 C  CG2 . ILE   A 1 352 ? -29.877 11.137  23.867 1.00 75.78  ? 648 ILE   A CG2 1 
ATOM   2763 C  CD1 . ILE   A 1 352 ? -27.013 10.261  24.550 1.00 73.72  ? 648 ILE   A CD1 1 
ATOM   2764 N  N   . VAL   A 1 353 ? -30.974 7.752   25.008 1.00 71.88  ? 649 VAL   A N   1 
ATOM   2765 C  CA  . VAL   A 1 353 ? -31.865 7.501   26.143 1.00 68.78  ? 649 VAL   A CA  1 
ATOM   2766 C  C   . VAL   A 1 353 ? -31.099 7.772   27.433 1.00 74.52  ? 649 VAL   A C   1 
ATOM   2767 O  O   . VAL   A 1 353 ? -29.890 7.517   27.504 1.00 69.95  ? 649 VAL   A O   1 
ATOM   2768 C  CB  . VAL   A 1 353 ? -32.428 6.059   26.102 1.00 68.38  ? 649 VAL   A CB  1 
ATOM   2769 C  CG1 . VAL   A 1 353 ? -31.371 5.025   26.476 1.00 61.44  ? 649 VAL   A CG1 1 
ATOM   2770 C  CG2 . VAL   A 1 353 ? -33.662 5.923   26.990 1.00 71.45  ? 649 VAL   A CG2 1 
ATOM   2771 N  N   . ASP   A 1 354 ? -31.799 8.323   28.442 1.00 72.07  ? 650 ASP   A N   1 
ATOM   2772 C  CA  . ASP   A 1 354 ? -31.209 8.656   29.726 1.00 73.79  ? 650 ASP   A CA  1 
ATOM   2773 C  C   . ASP   A 1 354 ? -31.458 7.508   30.696 1.00 79.81  ? 650 ASP   A C   1 
ATOM   2774 O  O   . ASP   A 1 354 ? -32.445 6.779   30.574 1.00 84.61  ? 650 ASP   A O   1 
ATOM   2775 C  CB  . ASP   A 1 354 ? -31.771 9.974   30.272 1.00 69.09  ? 650 ASP   A CB  1 
ATOM   2776 C  CG  . ASP   A 1 354 ? -33.169 9.842   30.874 1.00 83.83  ? 650 ASP   A CG  1 
ATOM   2777 O  OD1 . ASP   A 1 354 ? -34.121 10.435  30.321 1.00 79.55  ? 650 ASP   A OD1 1 
ATOM   2778 O  OD2 . ASP   A 1 354 ? -33.317 9.189   31.928 1.00 78.79  ? 650 ASP   A OD2 1 
ATOM   2779 N  N   . HIS   A 1 355 ? -30.550 7.347   31.664 1.00 81.02  ? 651 HIS   A N   1 
ATOM   2780 C  CA  . HIS   A 1 355 ? -30.543 6.122   32.471 1.00 72.77  ? 651 HIS   A CA  1 
ATOM   2781 C  C   . HIS   A 1 355 ? -31.819 5.928   33.284 1.00 69.13  ? 651 HIS   A C   1 
ATOM   2782 O  O   . HIS   A 1 355 ? -32.118 4.801   33.697 1.00 72.03  ? 651 HIS   A O   1 
ATOM   2783 C  CB  . HIS   A 1 355 ? -29.330 6.093   33.404 1.00 77.90  ? 651 HIS   A CB  1 
ATOM   2784 C  CG  . HIS   A 1 355 ? -29.099 7.365   34.161 1.00 78.15  ? 651 HIS   A CG  1 
ATOM   2785 N  ND1 . HIS   A 1 355 ? -28.297 8.377   33.683 1.00 83.68  ? 651 HIS   A ND1 1 
ATOM   2786 C  CD2 . HIS   A 1 355 ? -29.529 7.772   35.380 1.00 80.86  ? 651 HIS   A CD2 1 
ATOM   2787 C  CE1 . HIS   A 1 355 ? -28.254 9.361   34.567 1.00 86.96  ? 651 HIS   A CE1 1 
ATOM   2788 N  NE2 . HIS   A 1 355 ? -28.997 9.022   35.604 1.00 83.01  ? 651 HIS   A NE2 1 
ATOM   2789 N  N   . HIS   A 1 356 ? -32.572 6.993   33.536 1.00 70.63  ? 652 HIS   A N   1 
ATOM   2790 C  CA  . HIS   A 1 356 ? -33.881 6.835   34.155 1.00 69.15  ? 652 HIS   A CA  1 
ATOM   2791 C  C   . HIS   A 1 356 ? -34.893 6.282   33.162 1.00 73.98  ? 652 HIS   A C   1 
ATOM   2792 O  O   . HIS   A 1 356 ? -35.555 5.272   33.436 1.00 68.91  ? 652 HIS   A O   1 
ATOM   2793 C  CB  . HIS   A 1 356 ? -34.341 8.169   34.716 1.00 77.15  ? 652 HIS   A CB  1 
ATOM   2794 C  CG  . HIS   A 1 356 ? -33.332 8.804   35.612 1.00 87.48  ? 652 HIS   A CG  1 
ATOM   2795 N  ND1 . HIS   A 1 356 ? -33.143 8.399   36.918 1.00 84.76  ? 652 HIS   A ND1 1 
ATOM   2796 C  CD2 . HIS   A 1 356 ? -32.433 9.790   35.385 1.00 90.62  ? 652 HIS   A CD2 1 
ATOM   2797 C  CE1 . HIS   A 1 356 ? -32.179 9.121   37.458 1.00 88.92  ? 652 HIS   A CE1 1 
ATOM   2798 N  NE2 . HIS   A 1 356 ? -31.735 9.974   36.551 1.00 89.32  ? 652 HIS   A NE2 1 
ATOM   2799 N  N   . SER   A 1 357 ? -35.001 6.913   31.980 1.00 69.89  ? 653 SER   A N   1 
ATOM   2800 C  CA  . SER   A 1 357 ? -36.034 6.510   31.037 1.00 79.17  ? 653 SER   A CA  1 
ATOM   2801 C  C   . SER   A 1 357 ? -35.812 5.094   30.520 1.00 64.81  ? 653 SER   A C   1 
ATOM   2802 O  O   . SER   A 1 357 ? -36.779 4.396   30.224 1.00 70.07  ? 653 SER   A O   1 
ATOM   2803 C  CB  . SER   A 1 357 ? -36.100 7.487   29.870 1.00 84.54  ? 653 SER   A CB  1 
ATOM   2804 O  OG  . SER   A 1 357 ? -37.211 7.161   29.062 1.00 91.31  ? 653 SER   A OG  1 
ATOM   2805 N  N   . ALA   A 1 358 ? -34.561 4.639   30.449 1.00 61.03  ? 654 ALA   A N   1 
ATOM   2806 C  CA  . ALA   A 1 358 ? -34.248 3.322   29.898 1.00 60.92  ? 654 ALA   A CA  1 
ATOM   2807 C  C   . ALA   A 1 358 ? -34.405 2.208   30.935 1.00 63.68  ? 654 ALA   A C   1 
ATOM   2808 O  O   . ALA   A 1 358 ? -34.815 1.086   30.604 1.00 55.85  ? 654 ALA   A O   1 
ATOM   2809 C  CB  . ALA   A 1 358 ? -32.825 3.336   29.341 1.00 56.79  ? 654 ALA   A CB  1 
ATOM   2810 N  N   . THR   A 1 359 ? -34.048 2.478   32.189 1.00 52.99  ? 655 THR   A N   1 
ATOM   2811 C  CA  . THR   A 1 359 ? -34.244 1.461   33.209 1.00 55.59  ? 655 THR   A CA  1 
ATOM   2812 C  C   . THR   A 1 359 ? -35.726 1.277   33.514 1.00 58.07  ? 655 THR   A C   1 
ATOM   2813 O  O   . THR   A 1 359 ? -36.159 0.162   33.833 1.00 57.48  ? 655 THR   A O   1 
ATOM   2814 C  CB  . THR   A 1 359 ? -33.444 1.812   34.467 1.00 61.21  ? 655 THR   A CB  1 
ATOM   2815 O  OG1 . THR   A 1 359 ? -33.751 3.143   34.883 1.00 63.30  ? 655 THR   A OG1 1 
ATOM   2816 C  CG2 . THR   A 1 359 ? -31.959 1.707   34.161 1.00 54.48  ? 655 THR   A CG2 1 
ATOM   2817 N  N   . GLU   A 1 360 ? -36.521 2.344   33.402 1.00 59.62  ? 656 GLU   A N   1 
ATOM   2818 C  CA  . GLU   A 1 360 ? -37.964 2.199   33.567 1.00 69.01  ? 656 GLU   A CA  1 
ATOM   2819 C  C   . GLU   A 1 360 ? -38.554 1.331   32.460 1.00 76.74  ? 656 GLU   A C   1 
ATOM   2820 O  O   . GLU   A 1 360 ? -39.422 0.491   32.714 1.00 81.45  ? 656 GLU   A O   1 
ATOM   2821 C  CB  . GLU   A 1 360 ? -38.644 3.570   33.585 1.00 75.73  ? 656 GLU   A CB  1 
ATOM   2822 C  CG  . GLU   A 1 360 ? -40.059 3.544   34.161 1.00 94.70  ? 656 GLU   A CG  1 
ATOM   2823 C  CD  . GLU   A 1 360 ? -41.024 4.470   33.438 1.00 113.30 ? 656 GLU   A CD  1 
ATOM   2824 O  OE1 . GLU   A 1 360 ? -42.212 4.098   33.297 1.00 120.24 ? 656 GLU   A OE1 1 
ATOM   2825 O  OE2 . GLU   A 1 360 ? -40.599 5.565   33.007 1.00 117.89 ? 656 GLU   A OE2 1 
ATOM   2826 N  N   . SER   A 1 361 ? -38.093 1.516   31.219 1.00 77.66  ? 657 SER   A N   1 
ATOM   2827 C  CA  A SER   A 1 361 ? -38.587 0.683   30.129 0.46 69.98  ? 657 SER   A CA  1 
ATOM   2828 C  CA  B SER   A 1 361 ? -38.581 0.681   30.125 0.54 69.94  ? 657 SER   A CA  1 
ATOM   2829 C  C   . SER   A 1 361 ? -38.214 -0.779  30.339 1.00 73.05  ? 657 SER   A C   1 
ATOM   2830 O  O   . SER   A 1 361 ? -39.004 -1.675  30.012 1.00 72.90  ? 657 SER   A O   1 
ATOM   2831 C  CB  A SER   A 1 361 ? -38.054 1.200   28.787 0.46 64.93  ? 657 SER   A CB  1 
ATOM   2832 C  CB  B SER   A 1 361 ? -38.025 1.173   28.784 0.54 64.85  ? 657 SER   A CB  1 
ATOM   2833 O  OG  A SER   A 1 361 ? -38.645 2.447   28.443 0.46 66.87  ? 657 SER   A OG  1 
ATOM   2834 O  OG  B SER   A 1 361 ? -36.731 0.640   28.528 0.54 54.66  ? 657 SER   A OG  1 
ATOM   2835 N  N   . PHE   A 1 362 ? -37.035 -1.035  30.906 1.00 72.82  ? 658 PHE   A N   1 
ATOM   2836 C  CA  . PHE   A 1 362 ? -36.616 -2.408  31.140 1.00 70.30  ? 658 PHE   A CA  1 
ATOM   2837 C  C   . PHE   A 1 362 ? -37.510 -3.107  32.156 1.00 63.77  ? 658 PHE   A C   1 
ATOM   2838 O  O   . PHE   A 1 362 ? -37.811 -4.297  32.001 1.00 55.23  ? 658 PHE   A O   1 
ATOM   2839 C  CB  . PHE   A 1 362 ? -35.170 -2.467  31.609 1.00 66.48  ? 658 PHE   A CB  1 
ATOM   2840 C  CG  . PHE   A 1 362 ? -34.688 -3.856  31.755 1.00 62.14  ? 658 PHE   A CG  1 
ATOM   2841 C  CD1 . PHE   A 1 362 ? -34.470 -4.633  30.625 1.00 57.97  ? 658 PHE   A CD1 1 
ATOM   2842 C  CD2 . PHE   A 1 362 ? -34.530 -4.427  32.998 1.00 65.17  ? 658 PHE   A CD2 1 
ATOM   2843 C  CE1 . PHE   A 1 362 ? -34.055 -5.930  30.739 1.00 48.40  ? 658 PHE   A CE1 1 
ATOM   2844 C  CE2 . PHE   A 1 362 ? -34.111 -5.735  33.119 1.00 64.60  ? 658 PHE   A CE2 1 
ATOM   2845 C  CZ  . PHE   A 1 362 ? -33.867 -6.489  31.991 1.00 57.95  ? 658 PHE   A CZ  1 
ATOM   2846 N  N   . ILE   A 1 363 ? -37.924 -2.399  33.213 1.00 66.36  ? 659 ILE   A N   1 
ATOM   2847 C  CA  . ILE   A 1 363 ? -38.882 -2.973  34.155 1.00 70.17  ? 659 ILE   A CA  1 
ATOM   2848 C  C   . ILE   A 1 363 ? -40.187 -3.294  33.442 1.00 68.41  ? 659 ILE   A C   1 
ATOM   2849 O  O   . ILE   A 1 363 ? -40.766 -4.374  33.626 1.00 66.35  ? 659 ILE   A O   1 
ATOM   2850 C  CB  . ILE   A 1 363 ? -39.122 -2.027  35.354 1.00 71.13  ? 659 ILE   A CB  1 
ATOM   2851 C  CG1 . ILE   A 1 363 ? -37.835 -1.805  36.164 1.00 64.36  ? 659 ILE   A CG1 1 
ATOM   2852 C  CG2 . ILE   A 1 363 ? -40.232 -2.584  36.248 1.00 68.73  ? 659 ILE   A CG2 1 
ATOM   2853 C  CD1 . ILE   A 1 363 ? -37.727 -2.639  37.414 1.00 59.82  ? 659 ILE   A CD1 1 
ATOM   2854 N  N   . LYS   A 1 364 ? -40.672 -2.356  32.622 1.00 78.17  ? 660 LYS   A N   1 
ATOM   2855 C  CA  . LYS   A 1 364 ? -41.840 -2.626  31.788 1.00 77.79  ? 660 LYS   A CA  1 
ATOM   2856 C  C   . LYS   A 1 364 ? -41.605 -3.835  30.895 1.00 75.23  ? 660 LYS   A C   1 
ATOM   2857 O  O   . LYS   A 1 364 ? -42.446 -4.740  30.823 1.00 74.05  ? 660 LYS   A O   1 
ATOM   2858 C  CB  . LYS   A 1 364 ? -42.182 -1.400  30.949 1.00 77.42  ? 660 LYS   A CB  1 
ATOM   2859 C  CG  . LYS   A 1 364 ? -43.518 -0.786  31.313 1.00 93.66  ? 660 LYS   A CG  1 
ATOM   2860 C  CD  . LYS   A 1 364 ? -44.518 -0.900  30.179 1.00 103.08 ? 660 LYS   A CD  1 
ATOM   2861 C  CE  . LYS   A 1 364 ? -45.921 -0.538  30.641 1.00 115.24 ? 660 LYS   A CE  1 
ATOM   2862 N  NZ  . LYS   A 1 364 ? -46.872 -0.570  29.496 1.00 120.70 ? 660 LYS   A NZ  1 
ATOM   2863 N  N   . HIS   A 1 365 ? -40.467 -3.856  30.194 1.00 76.76  ? 661 HIS   A N   1 
ATOM   2864 C  CA  . HIS   A 1 365 ? -40.112 -5.014  29.375 1.00 67.16  ? 661 HIS   A CA  1 
ATOM   2865 C  C   . HIS   A 1 365 ? -40.081 -6.282  30.206 1.00 71.00  ? 661 HIS   A C   1 
ATOM   2866 O  O   . HIS   A 1 365 ? -40.542 -7.341  29.765 1.00 71.81  ? 661 HIS   A O   1 
ATOM   2867 C  CB  . HIS   A 1 365 ? -38.750 -4.804  28.725 1.00 60.76  ? 661 HIS   A CB  1 
ATOM   2868 C  CG  . HIS   A 1 365 ? -38.227 -6.024  28.025 1.00 67.41  ? 661 HIS   A CG  1 
ATOM   2869 N  ND1 . HIS   A 1 365 ? -38.883 -6.603  26.959 1.00 60.93  ? 661 HIS   A ND1 1 
ATOM   2870 C  CD2 . HIS   A 1 365 ? -37.121 -6.778  28.241 1.00 64.07  ? 661 HIS   A CD2 1 
ATOM   2871 C  CE1 . HIS   A 1 365 ? -38.196 -7.653  26.543 1.00 63.77  ? 661 HIS   A CE1 1 
ATOM   2872 N  NE2 . HIS   A 1 365 ? -37.124 -7.783  27.303 1.00 60.31  ? 661 HIS   A NE2 1 
ATOM   2873 N  N   . MET   A 1 366 ? -39.519 -6.196  31.408 1.00 62.43  ? 662 MET   A N   1 
ATOM   2874 C  CA  . MET   A 1 366 ? -39.474 -7.363  32.270 1.00 60.99  ? 662 MET   A CA  1 
ATOM   2875 C  C   . MET   A 1 366 ? -40.882 -7.827  32.607 1.00 59.42  ? 662 MET   A C   1 
ATOM   2876 O  O   . MET   A 1 366 ? -41.166 -9.030  32.612 1.00 53.72  ? 662 MET   A O   1 
ATOM   2877 C  CB  . MET   A 1 366 ? -38.680 -7.034  33.541 1.00 63.66  ? 662 MET   A CB  1 
ATOM   2878 C  CG  . MET   A 1 366 ? -37.848 -8.182  34.067 1.00 62.97  ? 662 MET   A CG  1 
ATOM   2879 S  SD  . MET   A 1 366 ? -36.708 -7.610  35.342 1.00 71.33  ? 662 MET   A SD  1 
ATOM   2880 C  CE  . MET   A 1 366 ? -36.149 -9.194  35.986 1.00 77.55  ? 662 MET   A CE  1 
ATOM   2881 N  N   . GLU   A 1 367 ? -41.786 -6.878  32.869 1.00 64.12  ? 663 GLU   A N   1 
ATOM   2882 C  CA  . GLU   A 1 367 ? -43.166 -7.233  33.174 1.00 75.52  ? 663 GLU   A CA  1 
ATOM   2883 C  C   . GLU   A 1 367 ? -43.796 -7.999  32.023 1.00 85.08  ? 663 GLU   A C   1 
ATOM   2884 O  O   . GLU   A 1 367 ? -44.472 -9.013  32.236 1.00 91.19  ? 663 GLU   A O   1 
ATOM   2885 C  CB  . GLU   A 1 367 ? -43.978 -5.976  33.485 1.00 84.31  ? 663 GLU   A CB  1 
ATOM   2886 C  CG  . GLU   A 1 367 ? -43.587 -5.277  34.782 1.00 90.31  ? 663 GLU   A CG  1 
ATOM   2887 C  CD  . GLU   A 1 367 ? -44.399 -4.015  35.040 1.00 103.87 ? 663 GLU   A CD  1 
ATOM   2888 O  OE1 . GLU   A 1 367 ? -45.426 -3.800  34.349 1.00 108.31 ? 663 GLU   A OE1 1 
ATOM   2889 O  OE2 . GLU   A 1 367 ? -44.003 -3.236  35.937 1.00 106.87 ? 663 GLU   A OE2 1 
ATOM   2890 N  N   . ASN   A 1 368 ? -43.571 -7.534  30.795 1.00 78.85  ? 664 ASN   A N   1 
ATOM   2891 C  CA  . ASN   A 1 368 ? -44.120 -8.213  29.630 1.00 79.37  ? 664 ASN   A CA  1 
ATOM   2892 C  C   . ASN   A 1 368 ? -43.507 -9.597  29.445 1.00 79.07  ? 664 ASN   A C   1 
ATOM   2893 O  O   . ASN   A 1 368 ? -44.220 -10.558 29.127 1.00 81.68  ? 664 ASN   A O   1 
ATOM   2894 C  CB  . ASN   A 1 368 ? -43.897 -7.353  28.390 1.00 74.87  ? 664 ASN   A CB  1 
ATOM   2895 C  CG  . ASN   A 1 368 ? -44.600 -6.015  28.483 1.00 79.15  ? 664 ASN   A CG  1 
ATOM   2896 O  OD1 . ASN   A 1 368 ? -45.679 -5.901  29.072 1.00 95.02  ? 664 ASN   A OD1 1 
ATOM   2897 N  ND2 . ASN   A 1 368 ? -43.988 -4.994  27.914 1.00 69.06  ? 664 ASN   A ND2 1 
ATOM   2898 N  N   . GLU   A 1 369 ? -42.190 -9.724  29.643 1.00 70.39  ? 665 GLU   A N   1 
ATOM   2899 C  CA  . GLU   A 1 369 ? -41.538 -11.011 29.419 1.00 65.85  ? 665 GLU   A CA  1 
ATOM   2900 C  C   . GLU   A 1 369 ? -42.063 -12.073 30.384 1.00 77.62  ? 665 GLU   A C   1 
ATOM   2901 O  O   . GLU   A 1 369 ? -42.404 -13.184 29.966 1.00 83.83  ? 665 GLU   A O   1 
ATOM   2902 C  CB  . GLU   A 1 369 ? -40.021 -10.863 29.533 1.00 64.41  ? 665 GLU   A CB  1 
ATOM   2903 C  CG  . GLU   A 1 369 ? -39.364 -10.127 28.369 1.00 69.57  ? 665 GLU   A CG  1 
ATOM   2904 C  CD  . GLU   A 1 369 ? -39.254 -10.976 27.116 1.00 78.47  ? 665 GLU   A CD  1 
ATOM   2905 O  OE1 . GLU   A 1 369 ? -38.226 -11.672 26.948 1.00 87.62  ? 665 GLU   A OE1 1 
ATOM   2906 O  OE2 . GLU   A 1 369 ? -40.207 -10.951 26.307 1.00 69.49  ? 665 GLU   A OE2 1 
ATOM   2907 N  N   . TYR   A 1 370 ? -42.154 -11.746 31.680 1.00 76.26  ? 666 TYR   A N   1 
ATOM   2908 C  CA  . TYR   A 1 370 ? -42.731 -12.694 32.636 1.00 80.56  ? 666 TYR   A CA  1 
ATOM   2909 C  C   . TYR   A 1 370 ? -44.182 -13.028 32.292 1.00 85.51  ? 666 TYR   A C   1 
ATOM   2910 O  O   . TYR   A 1 370 ? -44.635 -14.151 32.552 1.00 82.68  ? 666 TYR   A O   1 
ATOM   2911 C  CB  . TYR   A 1 370 ? -42.625 -12.154 34.068 1.00 74.49  ? 666 TYR   A CB  1 
ATOM   2912 C  CG  . TYR   A 1 370 ? -41.240 -12.299 34.664 1.00 72.37  ? 666 TYR   A CG  1 
ATOM   2913 C  CD1 . TYR   A 1 370 ? -40.236 -11.390 34.363 1.00 69.12  ? 666 TYR   A CD1 1 
ATOM   2914 C  CD2 . TYR   A 1 370 ? -40.932 -13.347 35.528 1.00 75.42  ? 666 TYR   A CD2 1 
ATOM   2915 C  CE1 . TYR   A 1 370 ? -38.961 -11.512 34.906 1.00 65.45  ? 666 TYR   A CE1 1 
ATOM   2916 C  CE2 . TYR   A 1 370 ? -39.649 -13.480 36.073 1.00 74.51  ? 666 TYR   A CE2 1 
ATOM   2917 C  CZ  . TYR   A 1 370 ? -38.667 -12.560 35.752 1.00 72.94  ? 666 TYR   A CZ  1 
ATOM   2918 O  OH  . TYR   A 1 370 ? -37.391 -12.674 36.276 1.00 74.55  ? 666 TYR   A OH  1 
ATOM   2919 N  N   . ARG   A 1 371 ? -44.914 -12.086 31.681 1.00 91.32  ? 667 ARG   A N   1 
ATOM   2920 C  CA  . ARG   A 1 371 ? -46.301 -12.344 31.292 1.00 102.68 ? 667 ARG   A CA  1 
ATOM   2921 C  C   . ARG   A 1 371 ? -46.391 -13.359 30.145 1.00 102.75 ? 667 ARG   A C   1 
ATOM   2922 O  O   . ARG   A 1 371 ? -46.963 -14.444 30.307 1.00 106.23 ? 667 ARG   A O   1 
ATOM   2923 C  CB  . ARG   A 1 371 ? -46.982 -11.028 30.903 1.00 111.69 ? 667 ARG   A CB  1 
ATOM   2924 C  CG  . ARG   A 1 371 ? -48.406 -11.170 30.377 1.00 122.27 ? 667 ARG   A CG  1 
ATOM   2925 C  CD  . ARG   A 1 371 ? -48.913 -9.867  29.763 1.00 129.05 ? 667 ARG   A CD  1 
ATOM   2926 N  NE  . ARG   A 1 371 ? -48.075 -9.386  28.659 1.00 129.27 ? 667 ARG   A NE  1 
ATOM   2927 C  CZ  . ARG   A 1 371 ? -48.242 -9.707  27.372 1.00 129.26 ? 667 ARG   A CZ  1 
ATOM   2928 N  NH1 . ARG   A 1 371 ? -49.219 -10.527 27.000 1.00 131.92 ? 667 ARG   A NH1 1 
ATOM   2929 N  NH2 . ARG   A 1 371 ? -47.426 -9.206  26.448 1.00 123.15 ? 667 ARG   A NH2 1 
ATOM   2930 N  N   . CYS   A 1 372 ? -45.816 -13.033 28.979 1.00 95.64  ? 668 CYS   A N   1 
ATOM   2931 C  CA  . CYS   A 1 372 ? -46.035 -13.776 27.738 1.00 97.59  ? 668 CYS   A CA  1 
ATOM   2932 C  C   . CYS   A 1 372 ? -44.883 -14.717 27.380 1.00 87.03  ? 668 CYS   A C   1 
ATOM   2933 O  O   . CYS   A 1 372 ? -44.783 -15.146 26.223 1.00 88.90  ? 668 CYS   A O   1 
ATOM   2934 C  CB  . CYS   A 1 372 ? -46.288 -12.796 26.585 1.00 105.09 ? 668 CYS   A CB  1 
ATOM   2935 S  SG  . CYS   A 1 372 ? -44.851 -11.777 26.099 1.00 110.57 ? 668 CYS   A SG  1 
ATOM   2936 N  N   . ARG   A 1 373 ? -44.017 -15.046 28.341 1.00 72.00  ? 669 ARG   A N   1 
ATOM   2937 C  CA  . ARG   A 1 373 ? -42.843 -15.882 28.100 1.00 70.89  ? 669 ARG   A CA  1 
ATOM   2938 C  C   . ARG   A 1 373 ? -42.401 -16.594 29.379 1.00 77.95  ? 669 ARG   A C   1 
ATOM   2939 O  O   . ARG   A 1 373 ? -41.649 -17.574 29.325 1.00 73.63  ? 669 ARG   A O   1 
ATOM   2940 C  CB  . ARG   A 1 373 ? -41.689 -15.041 27.542 1.00 68.32  ? 669 ARG   A CB  1 
ATOM   2941 C  CG  . ARG   A 1 373 ? -40.593 -15.852 26.869 1.00 71.85  ? 669 ARG   A CG  1 
ATOM   2942 C  CD  . ARG   A 1 373 ? -39.332 -15.026 26.595 1.00 70.67  ? 669 ARG   A CD  1 
ATOM   2943 N  NE  . ARG   A 1 373 ? -38.478 -15.691 25.610 1.00 71.25  ? 669 ARG   A NE  1 
ATOM   2944 C  CZ  . ARG   A 1 373 ? -37.211 -15.371 25.361 1.00 64.24  ? 669 ARG   A CZ  1 
ATOM   2945 N  NH1 . ARG   A 1 373 ? -36.611 -14.387 26.036 1.00 49.22  ? 669 ARG   A NH1 1 
ATOM   2946 N  NH2 . ARG   A 1 373 ? -36.537 -16.052 24.437 1.00 57.41  ? 669 ARG   A NH2 1 
ATOM   2947 N  N   . GLY   A 1 374 ? -42.852 -16.100 30.534 1.00 82.95  ? 670 GLY   A N   1 
ATOM   2948 C  CA  . GLY   A 1 374 ? -42.574 -16.760 31.797 1.00 81.45  ? 670 GLY   A CA  1 
ATOM   2949 C  C   . GLY   A 1 374 ? -41.253 -16.408 32.447 1.00 82.82  ? 670 GLY   A C   1 
ATOM   2950 O  O   . GLY   A 1 374 ? -40.837 -17.094 33.390 1.00 86.49  ? 670 GLY   A O   1 
ATOM   2951 N  N   . GLY   A 1 375 ? -40.583 -15.360 31.991 1.00 70.20  ? 671 GLY   A N   1 
ATOM   2952 C  CA  . GLY   A 1 375 ? -39.307 -14.988 32.564 1.00 65.17  ? 671 GLY   A CA  1 
ATOM   2953 C  C   . GLY   A 1 375 ? -38.575 -14.023 31.661 1.00 63.12  ? 671 GLY   A C   1 
ATOM   2954 O  O   . GLY   A 1 375 ? -39.044 -13.663 30.586 1.00 59.76  ? 671 GLY   A O   1 
ATOM   2955 N  N   . CYS   A 1 376 ? -37.396 -13.630 32.121 1.00 53.76  ? 672 CYS   A N   1 
ATOM   2956 C  CA  . CYS   A 1 376 ? -36.549 -12.681 31.419 1.00 51.31  ? 672 CYS   A CA  1 
ATOM   2957 C  C   . CYS   A 1 376 ? -35.148 -12.767 32.003 1.00 54.85  ? 672 CYS   A C   1 
ATOM   2958 O  O   . CYS   A 1 376 ? -34.906 -12.231 33.087 1.00 45.26  ? 672 CYS   A O   1 
ATOM   2959 C  CB  . CYS   A 1 376 ? -37.114 -11.257 31.542 1.00 47.01  ? 672 CYS   A CB  1 
ATOM   2960 S  SG  . CYS   A 1 376 ? -36.189 -9.931  30.715 1.00 57.34  ? 672 CYS   A SG  1 
ATOM   2961 N  N   . PRO   A 1 377 ? -34.208 -13.456 31.359 1.00 56.25  ? 673 PRO   A N   1 
ATOM   2962 C  CA  . PRO   A 1 377 ? -32.831 -13.443 31.873 1.00 51.01  ? 673 PRO   A CA  1 
ATOM   2963 C  C   . PRO   A 1 377 ? -32.350 -12.016 32.056 1.00 53.28  ? 673 PRO   A C   1 
ATOM   2964 O  O   . PRO   A 1 377 ? -32.657 -11.127 31.255 1.00 46.68  ? 673 PRO   A O   1 
ATOM   2965 C  CB  . PRO   A 1 377 ? -32.029 -14.181 30.791 1.00 54.01  ? 673 PRO   A CB  1 
ATOM   2966 C  CG  . PRO   A 1 377 ? -32.959 -14.335 29.631 1.00 48.22  ? 673 PRO   A CG  1 
ATOM   2967 C  CD  . PRO   A 1 377 ? -34.350 -14.298 30.163 1.00 51.25  ? 673 PRO   A CD  1 
ATOM   2968 N  N   . ALA   A 1 378 ? -31.617 -11.788 33.141 1.00 50.28  ? 674 ALA   A N   1 
ATOM   2969 C  CA  . ALA   A 1 378 ? -31.196 -10.428 33.462 1.00 48.28  ? 674 ALA   A CA  1 
ATOM   2970 C  C   . ALA   A 1 378 ? -29.985 -10.464 34.386 1.00 50.38  ? 674 ALA   A C   1 
ATOM   2971 O  O   . ALA   A 1 378 ? -29.917 -11.290 35.294 1.00 46.82  ? 674 ALA   A O   1 
ATOM   2972 C  CB  . ALA   A 1 378 ? -32.346 -9.622  34.083 1.00 40.87  ? 674 ALA   A CB  1 
ATOM   2973 N  N   . ASP   A 1 379 ? -29.022 -9.595  34.118 1.00 44.08  ? 675 ASP   A N   1 
ATOM   2974 C  CA  . ASP   A 1 379 ? -27.766 -9.550  34.847 1.00 45.59  ? 675 ASP   A CA  1 
ATOM   2975 C  C   . ASP   A 1 379 ? -27.743 -8.202  35.551 1.00 56.43  ? 675 ASP   A C   1 
ATOM   2976 O  O   . ASP   A 1 379 ? -27.435 -7.168  34.946 1.00 56.72  ? 675 ASP   A O   1 
ATOM   2977 C  CB  . ASP   A 1 379 ? -26.579 -9.736  33.919 1.00 42.30  ? 675 ASP   A CB  1 
ATOM   2978 C  CG  . ASP   A 1 379 ? -25.251 -9.767  34.643 1.00 55.22  ? 675 ASP   A CG  1 
ATOM   2979 O  OD1 . ASP   A 1 379 ? -24.296 -10.291 34.020 1.00 49.80  ? 675 ASP   A OD1 1 
ATOM   2980 O  OD2 . ASP   A 1 379 ? -25.150 -9.281  35.801 1.00 54.74  ? 675 ASP   A OD2 1 
ATOM   2981 N  N   . TRP   A 1 380 ? -28.105 -8.234  36.828 1.00 46.54  ? 676 TRP   A N   1 
ATOM   2982 C  CA  . TRP   A 1 380 ? -28.171 -7.035  37.660 1.00 39.72  ? 676 TRP   A CA  1 
ATOM   2983 C  C   . TRP   A 1 380 ? -26.862 -6.262  37.637 1.00 40.18  ? 676 TRP   A C   1 
ATOM   2984 O  O   . TRP   A 1 380 ? -26.875 -5.025  37.546 1.00 42.67  ? 676 TRP   A O   1 
ATOM   2985 C  CB  . TRP   A 1 380 ? -28.527 -7.457  39.081 1.00 43.75  ? 676 TRP   A CB  1 
ATOM   2986 C  CG  . TRP   A 1 380 ? -28.982 -6.363  40.043 1.00 38.04  ? 676 TRP   A CG  1 
ATOM   2987 C  CD1 . TRP   A 1 380 ? -30.266 -6.121  40.417 1.00 46.64  ? 676 TRP   A CD1 1 
ATOM   2988 C  CD2 . TRP   A 1 380 ? -28.174 -5.403  40.752 1.00 39.92  ? 676 TRP   A CD2 1 
ATOM   2989 N  NE1 . TRP   A 1 380 ? -30.320 -5.093  41.311 1.00 51.90  ? 676 TRP   A NE1 1 
ATOM   2990 C  CE2 . TRP   A 1 380 ? -29.050 -4.632  41.544 1.00 45.87  ? 676 TRP   A CE2 1 
ATOM   2991 C  CE3 . TRP   A 1 380 ? -26.799 -5.144  40.827 1.00 44.66  ? 676 TRP   A CE3 1 
ATOM   2992 C  CZ2 . TRP   A 1 380 ? -28.596 -3.609  42.413 1.00 44.05  ? 676 TRP   A CZ2 1 
ATOM   2993 C  CZ3 . TRP   A 1 380 ? -26.350 -4.121  41.683 1.00 45.84  ? 676 TRP   A CZ3 1 
ATOM   2994 C  CH2 . TRP   A 1 380 ? -27.246 -3.367  42.453 1.00 44.54  ? 676 TRP   A CH2 1 
ATOM   2995 N  N   . VAL   A 1 381 ? -25.722 -6.967  37.732 1.00 44.27  ? 677 VAL   A N   1 
ATOM   2996 C  CA  . VAL   A 1 381 ? -24.419 -6.296  37.720 1.00 40.83  ? 677 VAL   A CA  1 
ATOM   2997 C  C   . VAL   A 1 381 ? -24.284 -5.379  36.519 1.00 52.79  ? 677 VAL   A C   1 
ATOM   2998 O  O   . VAL   A 1 381 ? -23.658 -4.312  36.607 1.00 45.55  ? 677 VAL   A O   1 
ATOM   2999 C  CB  . VAL   A 1 381 ? -23.276 -7.328  37.772 1.00 47.84  ? 677 VAL   A CB  1 
ATOM   3000 C  CG1 . VAL   A 1 381 ? -21.970 -6.672  37.443 1.00 46.35  ? 677 VAL   A CG1 1 
ATOM   3001 C  CG2 . VAL   A 1 381 ? -23.176 -7.971  39.186 1.00 42.24  ? 677 VAL   A CG2 1 
ATOM   3002 N  N   . TRP   A 1 382 ? -24.888 -5.760  35.389 1.00 53.56  ? 678 TRP   A N   1 
ATOM   3003 C  CA  . TRP   A 1 382 ? -24.831 -4.984  34.159 1.00 52.44  ? 678 TRP   A CA  1 
ATOM   3004 C  C   . TRP   A 1 382 ? -26.059 -4.118  33.922 1.00 49.53  ? 678 TRP   A C   1 
ATOM   3005 O  O   . TRP   A 1 382 ? -25.933 -3.044  33.330 1.00 51.15  ? 678 TRP   A O   1 
ATOM   3006 C  CB  . TRP   A 1 382 ? -24.631 -5.915  32.961 1.00 50.49  ? 678 TRP   A CB  1 
ATOM   3007 C  CG  . TRP   A 1 382 ? -23.191 -6.317  32.778 1.00 60.73  ? 678 TRP   A CG  1 
ATOM   3008 C  CD1 . TRP   A 1 382 ? -22.418 -7.041  33.647 1.00 55.87  ? 678 TRP   A CD1 1 
ATOM   3009 C  CD2 . TRP   A 1 382 ? -22.357 -6.025  31.646 1.00 60.16  ? 678 TRP   A CD2 1 
ATOM   3010 N  NE1 . TRP   A 1 382 ? -21.153 -7.208  33.129 1.00 64.99  ? 678 TRP   A NE1 1 
ATOM   3011 C  CE2 . TRP   A 1 382 ? -21.093 -6.598  31.899 1.00 66.50  ? 678 TRP   A CE2 1 
ATOM   3012 C  CE3 . TRP   A 1 382 ? -22.563 -5.346  30.445 1.00 53.31  ? 678 TRP   A CE3 1 
ATOM   3013 C  CZ2 . TRP   A 1 382 ? -20.039 -6.500  30.994 1.00 65.77  ? 678 TRP   A CZ2 1 
ATOM   3014 C  CZ3 . TRP   A 1 382 ? -21.515 -5.255  29.541 1.00 64.85  ? 678 TRP   A CZ3 1 
ATOM   3015 C  CH2 . TRP   A 1 382 ? -20.272 -5.835  29.819 1.00 68.99  ? 678 TRP   A CH2 1 
ATOM   3016 N  N   . ILE   A 1 383 ? -27.237 -4.516  34.396 1.00 48.11  ? 679 ILE   A N   1 
ATOM   3017 C  CA  . ILE   A 1 383 ? -28.425 -3.698  34.143 1.00 45.35  ? 679 ILE   A CA  1 
ATOM   3018 C  C   . ILE   A 1 383 ? -28.377 -2.387  34.947 1.00 54.32  ? 679 ILE   A C   1 
ATOM   3019 O  O   . ILE   A 1 383 ? -28.795 -1.342  34.443 1.00 49.19  ? 679 ILE   A O   1 
ATOM   3020 C  CB  . ILE   A 1 383 ? -29.698 -4.521  34.438 1.00 51.35  ? 679 ILE   A CB  1 
ATOM   3021 C  CG1 . ILE   A 1 383 ? -29.817 -5.708  33.463 1.00 50.50  ? 679 ILE   A CG1 1 
ATOM   3022 C  CG2 . ILE   A 1 383 ? -30.954 -3.632  34.438 1.00 41.09  ? 679 ILE   A CG2 1 
ATOM   3023 C  CD1 . ILE   A 1 383 ? -30.408 -5.351  32.096 1.00 60.36  ? 679 ILE   A CD1 1 
ATOM   3024 N  N   . VAL   A 1 384 ? -27.869 -2.405  36.192 1.00 42.76  ? 680 VAL   A N   1 
ATOM   3025 C  CA  . VAL   A 1 384 ? -27.879 -1.163  36.995 1.00 49.16  ? 680 VAL   A CA  1 
ATOM   3026 C  C   . VAL   A 1 384 ? -26.976 -0.127  36.337 1.00 46.64  ? 680 VAL   A C   1 
ATOM   3027 O  O   . VAL   A 1 384 ? -25.815 -0.438  36.007 1.00 48.89  ? 680 VAL   A O   1 
ATOM   3028 C  CB  . VAL   A 1 384 ? -27.433 -1.438  38.432 1.00 46.72  ? 680 VAL   A CB  1 
ATOM   3029 C  CG1 . VAL   A 1 384 ? -27.424 -0.130  39.256 1.00 41.16  ? 680 VAL   A CG1 1 
ATOM   3030 C  CG2 . VAL   A 1 384 ? -28.349 -2.423  39.066 1.00 63.63  ? 680 VAL   A CG2 1 
ATOM   3031 N  N   . PRO   A 1 385 ? -27.453 1.084   36.073 1.00 54.79  ? 681 PRO   A N   1 
ATOM   3032 C  CA  . PRO   A 1 385 ? -26.573 2.107   35.484 1.00 55.82  ? 681 PRO   A CA  1 
ATOM   3033 C  C   . PRO   A 1 385 ? -25.355 2.334   36.366 1.00 57.10  ? 681 PRO   A C   1 
ATOM   3034 O  O   . PRO   A 1 385 ? -25.394 2.034   37.568 1.00 66.99  ? 681 PRO   A O   1 
ATOM   3035 C  CB  . PRO   A 1 385 ? -27.466 3.361   35.416 1.00 64.28  ? 681 PRO   A CB  1 
ATOM   3036 C  CG  . PRO   A 1 385 ? -28.854 2.834   35.401 1.00 67.67  ? 681 PRO   A CG  1 
ATOM   3037 C  CD  . PRO   A 1 385 ? -28.839 1.561   36.214 1.00 55.04  ? 681 PRO   A CD  1 
ATOM   3038 N  N   . PRO   A 1 386 ? -24.246 2.855   35.798 1.00 54.42  ? 682 PRO   A N   1 
ATOM   3039 C  CA  . PRO   A 1 386 ? -23.018 3.067   36.582 1.00 62.15  ? 682 PRO   A CA  1 
ATOM   3040 C  C   . PRO   A 1 386 ? -22.988 4.362   37.394 1.00 67.12  ? 682 PRO   A C   1 
ATOM   3041 O  O   . PRO   A 1 386 ? -21.926 4.802   37.860 1.00 63.48  ? 682 PRO   A O   1 
ATOM   3042 C  CB  . PRO   A 1 386 ? -21.929 3.070   35.508 1.00 63.82  ? 682 PRO   A CB  1 
ATOM   3043 C  CG  . PRO   A 1 386 ? -22.610 3.634   34.277 1.00 61.16  ? 682 PRO   A CG  1 
ATOM   3044 C  CD  . PRO   A 1 386 ? -24.065 3.199   34.366 1.00 61.97  ? 682 PRO   A CD  1 
ATOM   3045 N  N   . MET   A 1 387 ? -24.147 4.988   37.576 1.00 73.26  ? 683 MET   A N   1 
ATOM   3046 C  CA  . MET   A 1 387 ? -24.269 6.155   38.434 1.00 75.74  ? 683 MET   A CA  1 
ATOM   3047 C  C   . MET   A 1 387 ? -25.713 6.223   38.888 1.00 74.29  ? 683 MET   A C   1 
ATOM   3048 O  O   . MET   A 1 387 ? -26.601 5.660   38.243 1.00 68.49  ? 683 MET   A O   1 
ATOM   3049 C  CB  . MET   A 1 387 ? -23.878 7.461   37.729 1.00 85.02  ? 683 MET   A CB  1 
ATOM   3050 C  CG  . MET   A 1 387 ? -24.957 8.003   36.796 1.00 91.22  ? 683 MET   A CG  1 
ATOM   3051 S  SD  . MET   A 1 387 ? -24.557 9.518   35.872 1.00 86.48  ? 683 MET   A SD  1 
ATOM   3052 C  CE  . MET   A 1 387 ? -24.869 10.791  37.087 1.00 74.99  ? 683 MET   A CE  1 
ATOM   3053 N  N   . SER   A 1 388 ? -25.935 6.898   40.020 1.00 68.70  ? 684 SER   A N   1 
ATOM   3054 C  CA  . SER   A 1 388 ? -27.285 7.080   40.560 1.00 63.81  ? 684 SER   A CA  1 
ATOM   3055 C  C   . SER   A 1 388 ? -28.042 5.754   40.697 1.00 67.95  ? 684 SER   A C   1 
ATOM   3056 O  O   . SER   A 1 388 ? -29.276 5.721   40.632 1.00 71.18  ? 684 SER   A O   1 
ATOM   3057 C  CB  . SER   A 1 388 ? -28.078 8.059   39.694 1.00 71.13  ? 684 SER   A CB  1 
ATOM   3058 O  OG  . SER   A 1 388 ? -27.432 9.314   39.607 1.00 80.91  ? 684 SER   A OG  1 
ATOM   3059 N  N   . GLY   A 1 389 ? -27.300 4.654   40.849 1.00 57.49  ? 685 GLY   A N   1 
ATOM   3060 C  CA  . GLY   A 1 389 ? -27.844 3.313   40.957 1.00 60.10  ? 685 GLY   A CA  1 
ATOM   3061 C  C   . GLY   A 1 389 ? -29.243 3.168   41.525 1.00 64.62  ? 685 GLY   A C   1 
ATOM   3062 O  O   . GLY   A 1 389 ? -30.172 2.822   40.794 1.00 65.10  ? 685 GLY   A O   1 
ATOM   3063 N  N   . SER   A 1 390 ? -29.415 3.437   42.820 1.00 62.19  ? 686 SER   A N   1 
ATOM   3064 C  CA  . SER   A 1 390 ? -30.666 3.140   43.511 1.00 57.25  ? 686 SER   A CA  1 
ATOM   3065 C  C   . SER   A 1 390 ? -31.729 4.222   43.360 1.00 69.04  ? 686 SER   A C   1 
ATOM   3066 O  O   . SER   A 1 390 ? -32.821 4.069   43.922 1.00 71.90  ? 686 SER   A O   1 
ATOM   3067 C  CB  . SER   A 1 390 ? -30.415 2.870   45.013 1.00 55.77  ? 686 SER   A CB  1 
ATOM   3068 O  OG  . SER   A 1 390 ? -29.731 3.938   45.620 1.00 57.23  ? 686 SER   A OG  1 
ATOM   3069 N  N   . ILE   A 1 391 ? -31.464 5.306   42.630 1.00 78.50  ? 687 ILE   A N   1 
ATOM   3070 C  CA  . ILE   A 1 391 ? -32.576 6.186   42.281 1.00 72.08  ? 687 ILE   A CA  1 
ATOM   3071 C  C   . ILE   A 1 391 ? -33.117 5.787   40.910 1.00 62.03  ? 687 ILE   A C   1 
ATOM   3072 O  O   . ILE   A 1 391 ? -33.943 6.507   40.339 1.00 70.30  ? 687 ILE   A O   1 
ATOM   3073 C  CB  . ILE   A 1 391 ? -32.209 7.684   42.324 1.00 73.59  ? 687 ILE   A CB  1 
ATOM   3074 C  CG1 . ILE   A 1 391 ? -31.233 8.066   41.213 1.00 82.60  ? 687 ILE   A CG1 1 
ATOM   3075 C  CG2 . ILE   A 1 391 ? -31.703 8.102   43.705 1.00 73.36  ? 687 ILE   A CG2 1 
ATOM   3076 C  CD1 . ILE   A 1 391 ? -30.972 9.568   41.139 1.00 85.16  ? 687 ILE   A CD1 1 
ATOM   3077 N  N   . THR   A 1 392 ? -32.649 4.633   40.364 1.00 65.17  ? 688 THR   A N   1 
ATOM   3078 C  CA  . THR   A 1 392 ? -33.258 3.976   39.201 1.00 68.28  ? 688 THR   A CA  1 
ATOM   3079 C  C   . THR   A 1 392 ? -33.944 2.681   39.630 1.00 69.99  ? 688 THR   A C   1 
ATOM   3080 O  O   . THR   A 1 392 ? -33.441 1.973   40.517 1.00 66.30  ? 688 THR   A O   1 
ATOM   3081 C  CB  . THR   A 1 392 ? -32.254 3.657   38.067 1.00 69.31  ? 688 THR   A CB  1 
ATOM   3082 O  OG1 . THR   A 1 392 ? -31.381 2.589   38.448 1.00 64.75  ? 688 THR   A OG1 1 
ATOM   3083 C  CG2 . THR   A 1 392 ? -31.433 4.886   37.682 1.00 73.84  ? 688 THR   A CG2 1 
ATOM   3084 N  N   . PRO   A 1 393 ? -35.098 2.359   39.036 1.00 73.40  ? 689 PRO   A N   1 
ATOM   3085 C  CA  . PRO   A 1 393 ? -35.913 1.261   39.569 1.00 65.96  ? 689 PRO   A CA  1 
ATOM   3086 C  C   . PRO   A 1 393 ? -35.291 -0.105  39.395 1.00 57.72  ? 689 PRO   A C   1 
ATOM   3087 O  O   . PRO   A 1 393 ? -35.669 -1.024  40.141 1.00 65.52  ? 689 PRO   A O   1 
ATOM   3088 C  CB  . PRO   A 1 393 ? -37.223 1.385   38.785 1.00 82.05  ? 689 PRO   A CB  1 
ATOM   3089 C  CG  . PRO   A 1 393 ? -36.800 1.970   37.477 1.00 82.16  ? 689 PRO   A CG  1 
ATOM   3090 C  CD  . PRO   A 1 393 ? -35.687 2.935   37.808 1.00 78.99  ? 689 PRO   A CD  1 
ATOM   3091 N  N   . VAL   A 1 394 ? -34.335 -0.278  38.473 1.00 53.90  ? 690 VAL   A N   1 
ATOM   3092 C  CA  . VAL   A 1 394 ? -33.761 -1.609  38.293 1.00 48.38  ? 690 VAL   A CA  1 
ATOM   3093 C  C   . VAL   A 1 394 ? -32.903 -2.020  39.495 1.00 50.76  ? 690 VAL   A C   1 
ATOM   3094 O  O   . VAL   A 1 394 ? -32.754 -3.221  39.763 1.00 62.06  ? 690 VAL   A O   1 
ATOM   3095 C  CB  . VAL   A 1 394 ? -32.950 -1.701  36.988 1.00 51.00  ? 690 VAL   A CB  1 
ATOM   3096 C  CG1 . VAL   A 1 394 ? -33.863 -1.483  35.747 1.00 56.43  ? 690 VAL   A CG1 1 
ATOM   3097 C  CG2 . VAL   A 1 394 ? -31.801 -0.710  36.994 1.00 60.94  ? 690 VAL   A CG2 1 
ATOM   3098 N  N   . PHE   A 1 395 ? -32.324 -1.048  40.229 1.00 51.69  ? 691 PHE   A N   1 
ATOM   3099 C  CA  . PHE   A 1 395 ? -31.564 -1.358  41.453 1.00 50.15  ? 691 PHE   A CA  1 
ATOM   3100 C  C   . PHE   A 1 395 ? -32.370 -2.215  42.416 1.00 59.49  ? 691 PHE   A C   1 
ATOM   3101 O  O   . PHE   A 1 395 ? -31.810 -3.058  43.149 1.00 50.14  ? 691 PHE   A O   1 
ATOM   3102 C  CB  . PHE   A 1 395 ? -31.143 -0.045  42.146 1.00 53.66  ? 691 PHE   A CB  1 
ATOM   3103 C  CG  . PHE   A 1 395 ? -30.357 -0.218  43.455 1.00 56.92  ? 691 PHE   A CG  1 
ATOM   3104 C  CD1 . PHE   A 1 395 ? -28.974 -0.061  43.481 1.00 49.97  ? 691 PHE   A CD1 1 
ATOM   3105 C  CD2 . PHE   A 1 395 ? -31.006 -0.479  44.659 1.00 60.69  ? 691 PHE   A CD2 1 
ATOM   3106 C  CE1 . PHE   A 1 395 ? -28.253 -0.209  44.660 1.00 61.93  ? 691 PHE   A CE1 1 
ATOM   3107 C  CE2 . PHE   A 1 395 ? -30.287 -0.613  45.848 1.00 62.29  ? 691 PHE   A CE2 1 
ATOM   3108 C  CZ  . PHE   A 1 395 ? -28.911 -0.467  45.841 1.00 63.30  ? 691 PHE   A CZ  1 
ATOM   3109 N  N   . HIS   A 1 396 ? -33.682 -1.997  42.440 1.00 63.79  ? 692 HIS   A N   1 
ATOM   3110 C  CA  . HIS   A 1 396 ? -34.562 -2.530  43.461 1.00 65.21  ? 692 HIS   A CA  1 
ATOM   3111 C  C   . HIS   A 1 396 ? -35.258 -3.806  43.028 1.00 58.68  ? 692 HIS   A C   1 
ATOM   3112 O  O   . HIS   A 1 396 ? -36.141 -4.298  43.743 1.00 58.76  ? 692 HIS   A O   1 
ATOM   3113 C  CB  . HIS   A 1 396 ? -35.583 -1.464  43.832 1.00 72.48  ? 692 HIS   A CB  1 
ATOM   3114 C  CG  . HIS   A 1 396 ? -34.963 -0.191  44.317 1.00 74.43  ? 692 HIS   A CG  1 
ATOM   3115 N  ND1 . HIS   A 1 396 ? -34.206 -0.129  45.466 1.00 66.89  ? 692 HIS   A ND1 1 
ATOM   3116 C  CD2 . HIS   A 1 396 ? -34.969 1.062   43.801 1.00 71.68  ? 692 HIS   A CD2 1 
ATOM   3117 C  CE1 . HIS   A 1 396 ? -33.787 1.113   45.648 1.00 69.60  ? 692 HIS   A CE1 1 
ATOM   3118 N  NE2 . HIS   A 1 396 ? -34.226 1.851   44.645 1.00 73.68  ? 692 HIS   A NE2 1 
ATOM   3119 N  N   . GLN   A 1 397 ? -34.852 -4.364  41.888 1.00 61.37  ? 693 GLN   A N   1 
ATOM   3120 C  CA  . GLN   A 1 397 ? -35.549 -5.443  41.206 1.00 61.37  ? 693 GLN   A CA  1 
ATOM   3121 C  C   . GLN   A 1 397 ? -34.654 -6.673  41.239 1.00 58.90  ? 693 GLN   A C   1 
ATOM   3122 O  O   . GLN   A 1 397 ? -33.599 -6.687  40.597 1.00 54.92  ? 693 GLN   A O   1 
ATOM   3123 C  CB  . GLN   A 1 397 ? -35.861 -5.036  39.757 1.00 60.76  ? 693 GLN   A CB  1 
ATOM   3124 C  CG  . GLN   A 1 397 ? -36.580 -6.089  38.931 1.00 48.93  ? 693 GLN   A CG  1 
ATOM   3125 C  CD  . GLN   A 1 397 ? -38.012 -6.293  39.378 1.00 66.05  ? 693 GLN   A CD  1 
ATOM   3126 O  OE1 . GLN   A 1 397 ? -38.820 -5.352  39.383 1.00 72.16  ? 693 GLN   A OE1 1 
ATOM   3127 N  NE2 . GLN   A 1 397 ? -38.339 -7.526  39.764 1.00 70.66  ? 693 GLN   A NE2 1 
ATOM   3128 N  N   . GLU   A 1 398 ? -35.060 -7.696  41.989 1.00 49.66  ? 694 GLU   A N   1 
ATOM   3129 C  CA  . GLU   A 1 398 ? -34.400 -8.988  41.883 1.00 57.22  ? 694 GLU   A CA  1 
ATOM   3130 C  C   . GLU   A 1 398 ? -34.494 -9.508  40.450 1.00 56.60  ? 694 GLU   A C   1 
ATOM   3131 O  O   . GLU   A 1 398 ? -35.521 -9.364  39.784 1.00 60.75  ? 694 GLU   A O   1 
ATOM   3132 C  CB  . GLU   A 1 398 ? -35.024 -9.984  42.864 1.00 43.19  ? 694 GLU   A CB  1 
ATOM   3133 C  CG  . GLU   A 1 398 ? -34.897 -9.521  44.311 1.00 63.70  ? 694 GLU   A CG  1 
ATOM   3134 C  CD  . GLU   A 1 398 ? -35.565 -10.450 45.292 1.00 66.54  ? 694 GLU   A CD  1 
ATOM   3135 O  OE1 . GLU   A 1 398 ? -35.409 -10.233 46.508 1.00 70.73  ? 694 GLU   A OE1 1 
ATOM   3136 O  OE2 . GLU   A 1 398 ? -36.249 -11.395 44.843 1.00 72.04  ? 694 GLU   A OE2 1 
ATOM   3137 N  N   . MET   A 1 399 ? -33.405 -10.094 39.969 1.00 58.38  ? 695 MET   A N   1 
ATOM   3138 C  CA  . MET   A 1 399 ? -33.332 -10.589 38.598 1.00 57.06  ? 695 MET   A CA  1 
ATOM   3139 C  C   . MET   A 1 399 ? -32.645 -11.937 38.592 1.00 57.34  ? 695 MET   A C   1 
ATOM   3140 O  O   . MET   A 1 399 ? -31.589 -12.099 39.210 1.00 66.79  ? 695 MET   A O   1 
ATOM   3141 C  CB  . MET   A 1 399 ? -32.543 -9.641  37.676 1.00 55.55  ? 695 MET   A CB  1 
ATOM   3142 C  CG  . MET   A 1 399 ? -33.106 -8.244  37.489 1.00 59.14  ? 695 MET   A CG  1 
ATOM   3143 S  SD  . MET   A 1 399 ? -31.839 -7.167  36.788 1.00 50.94  ? 695 MET   A SD  1 
ATOM   3144 C  CE  . MET   A 1 399 ? -32.680 -5.602  36.789 1.00 37.05  ? 695 MET   A CE  1 
ATOM   3145 N  N   . LEU   A 1 400 ? -33.229 -12.893 37.875 1.00 52.90  ? 696 LEU   A N   1 
ATOM   3146 C  CA  . LEU   A 1 400 ? -32.622 -14.202 37.687 1.00 53.04  ? 696 LEU   A CA  1 
ATOM   3147 C  C   . LEU   A 1 400 ? -31.786 -14.208 36.415 1.00 58.19  ? 696 LEU   A C   1 
ATOM   3148 O  O   . LEU   A 1 400 ? -32.316 -13.960 35.329 1.00 49.87  ? 696 LEU   A O   1 
ATOM   3149 C  CB  . LEU   A 1 400 ? -33.695 -15.276 37.583 1.00 56.22  ? 696 LEU   A CB  1 
ATOM   3150 C  CG  . LEU   A 1 400 ? -34.434 -15.660 38.843 1.00 60.97  ? 696 LEU   A CG  1 
ATOM   3151 C  CD1 . LEU   A 1 400 ? -35.489 -16.655 38.446 1.00 65.42  ? 696 LEU   A CD1 1 
ATOM   3152 C  CD2 . LEU   A 1 400 ? -33.462 -16.250 39.853 1.00 56.32  ? 696 LEU   A CD2 1 
ATOM   3153 N  N   . ASN   A 1 401 ? -30.494 -14.500 36.539 1.00 56.20  ? 697 ASN   A N   1 
ATOM   3154 C  CA  . ASN   A 1 401 ? -29.647 -14.641 35.363 1.00 56.13  ? 697 ASN   A CA  1 
ATOM   3155 C  C   . ASN   A 1 401 ? -29.542 -16.106 34.957 1.00 54.52  ? 697 ASN   A C   1 
ATOM   3156 O  O   . ASN   A 1 401 ? -29.442 -16.992 35.813 1.00 42.68  ? 697 ASN   A O   1 
ATOM   3157 C  CB  . ASN   A 1 401 ? -28.250 -14.065 35.596 1.00 58.86  ? 697 ASN   A CB  1 
ATOM   3158 C  CG  . ASN   A 1 401 ? -27.540 -13.744 34.281 1.00 55.07  ? 697 ASN   A CG  1 
ATOM   3159 O  OD1 . ASN   A 1 401 ? -28.195 -13.581 33.257 1.00 54.89  ? 697 ASN   A OD1 1 
ATOM   3160 N  ND2 . ASN   A 1 401 ? -26.208 -13.671 34.299 1.00 38.98  ? 697 ASN   A ND2 1 
ATOM   3161 N  N   . TYR   A 1 402 ? -29.592 -16.353 33.643 1.00 54.78  ? 698 TYR   A N   1 
ATOM   3162 C  CA  . TYR   A 1 402 ? -29.397 -17.674 33.063 1.00 42.25  ? 698 TYR   A CA  1 
ATOM   3163 C  C   . TYR   A 1 402 ? -29.253 -17.520 31.540 1.00 56.43  ? 698 TYR   A C   1 
ATOM   3164 O  O   . TYR   A 1 402 ? -29.620 -16.493 30.962 1.00 53.62  ? 698 TYR   A O   1 
ATOM   3165 C  CB  . TYR   A 1 402 ? -30.545 -18.624 33.423 1.00 53.03  ? 698 TYR   A CB  1 
ATOM   3166 C  CG  . TYR   A 1 402 ? -31.938 -18.054 33.244 1.00 57.83  ? 698 TYR   A CG  1 
ATOM   3167 C  CD1 . TYR   A 1 402 ? -32.579 -18.125 32.014 1.00 65.15  ? 698 TYR   A CD1 1 
ATOM   3168 C  CD2 . TYR   A 1 402 ? -32.614 -17.441 34.306 1.00 55.33  ? 698 TYR   A CD2 1 
ATOM   3169 C  CE1 . TYR   A 1 402 ? -33.851 -17.611 31.829 1.00 63.42  ? 698 TYR   A CE1 1 
ATOM   3170 C  CE2 . TYR   A 1 402 ? -33.894 -16.925 34.136 1.00 60.13  ? 698 TYR   A CE2 1 
ATOM   3171 C  CZ  . TYR   A 1 402 ? -34.507 -17.014 32.881 1.00 65.57  ? 698 TYR   A CZ  1 
ATOM   3172 O  OH  . TYR   A 1 402 ? -35.775 -16.507 32.672 1.00 61.13  ? 698 TYR   A OH  1 
ATOM   3173 N  N   . ARG   A 1 403 ? -28.689 -18.543 30.907 1.00 47.66  ? 699 ARG   A N   1 
ATOM   3174 C  CA  . ARG   A 1 403 ? -28.285 -18.474 29.504 1.00 60.55  ? 699 ARG   A CA  1 
ATOM   3175 C  C   . ARG   A 1 403 ? -29.316 -19.200 28.646 1.00 64.17  ? 699 ARG   A C   1 
ATOM   3176 O  O   . ARG   A 1 403 ? -29.458 -20.425 28.729 1.00 73.02  ? 699 ARG   A O   1 
ATOM   3177 C  CB  . ARG   A 1 403 ? -26.894 -19.077 29.302 1.00 68.06  ? 699 ARG   A CB  1 
ATOM   3178 C  CG  . ARG   A 1 403 ? -25.769 -18.446 30.129 1.00 72.05  ? 699 ARG   A CG  1 
ATOM   3179 C  CD  . ARG   A 1 403 ? -25.419 -17.022 29.688 1.00 83.43  ? 699 ARG   A CD  1 
ATOM   3180 N  NE  . ARG   A 1 403 ? -24.548 -16.966 28.509 1.00 96.56  ? 699 ARG   A NE  1 
ATOM   3181 C  CZ  . ARG   A 1 403 ? -23.770 -15.925 28.203 1.00 102.20 ? 699 ARG   A CZ  1 
ATOM   3182 N  NH1 . ARG   A 1 403 ? -23.739 -14.852 28.988 1.00 96.54  ? 699 ARG   A NH1 1 
ATOM   3183 N  NH2 . ARG   A 1 403 ? -23.010 -15.953 27.113 1.00 99.12  ? 699 ARG   A NH2 1 
ATOM   3184 N  N   . LEU   A 1 404 ? -30.034 -18.450 27.827 1.00 66.10  ? 700 LEU   A N   1 
ATOM   3185 C  CA  . LEU   A 1 404 ? -30.876 -19.031 26.794 1.00 60.96  ? 700 LEU   A CA  1 
ATOM   3186 C  C   . LEU   A 1 404 ? -30.193 -18.905 25.432 1.00 68.01  ? 700 LEU   A C   1 
ATOM   3187 O  O   . LEU   A 1 404 ? -29.193 -18.200 25.265 1.00 68.97  ? 700 LEU   A O   1 
ATOM   3188 C  CB  . LEU   A 1 404 ? -32.250 -18.356 26.762 1.00 55.63  ? 700 LEU   A CB  1 
ATOM   3189 C  CG  . LEU   A 1 404 ? -33.130 -18.327 28.007 1.00 59.37  ? 700 LEU   A CG  1 
ATOM   3190 C  CD1 . LEU   A 1 404 ? -34.406 -17.545 27.704 1.00 52.37  ? 700 LEU   A CD1 1 
ATOM   3191 C  CD2 . LEU   A 1 404 ? -33.438 -19.740 28.541 1.00 61.28  ? 700 LEU   A CD2 1 
ATOM   3192 N  N   . THR   A 1 405 ? -30.758 -19.601 24.451 1.00 64.81  ? 701 THR   A N   1 
ATOM   3193 C  CA  . THR   A 1 405 ? -30.262 -19.617 23.084 1.00 60.83  ? 701 THR   A CA  1 
ATOM   3194 C  C   . THR   A 1 405 ? -31.463 -19.550 22.149 1.00 57.47  ? 701 THR   A C   1 
ATOM   3195 O  O   . THR   A 1 405 ? -32.540 -20.044 22.504 1.00 52.34  ? 701 THR   A O   1 
ATOM   3196 C  CB  . THR   A 1 405 ? -29.423 -20.880 22.831 1.00 63.20  ? 701 THR   A CB  1 
ATOM   3197 O  OG1 . THR   A 1 405 ? -28.746 -20.771 21.582 1.00 71.39  ? 701 THR   A OG1 1 
ATOM   3198 C  CG2 . THR   A 1 405 ? -30.291 -22.135 22.851 1.00 60.56  ? 701 THR   A CG2 1 
ATOM   3199 N  N   . PRO   A 1 406 ? -31.332 -18.908 20.958 1.00 57.50  ? 702 PRO   A N   1 
ATOM   3200 C  CA  . PRO   A 1 406 ? -30.230 -18.174 20.314 1.00 57.20  ? 702 PRO   A CA  1 
ATOM   3201 C  C   . PRO   A 1 406 ? -29.582 -17.110 21.210 1.00 59.09  ? 702 PRO   A C   1 
ATOM   3202 O  O   . PRO   A 1 406 ? -30.265 -16.558 22.080 1.00 58.57  ? 702 PRO   A O   1 
ATOM   3203 C  CB  . PRO   A 1 406 ? -30.916 -17.509 19.100 1.00 51.54  ? 702 PRO   A CB  1 
ATOM   3204 C  CG  . PRO   A 1 406 ? -32.064 -18.402 18.762 1.00 53.61  ? 702 PRO   A CG  1 
ATOM   3205 C  CD  . PRO   A 1 406 ? -32.528 -18.986 20.086 1.00 58.30  ? 702 PRO   A CD  1 
ATOM   3206 N  N   . SER   A 1 407 ? -28.298 -16.813 21.004 1.00 57.89  ? 703 SER   A N   1 
ATOM   3207 C  CA  . SER   A 1 407 ? -27.604 -15.974 21.973 1.00 56.02  ? 703 SER   A CA  1 
ATOM   3208 C  C   . SER   A 1 407 ? -26.384 -15.310 21.355 1.00 52.18  ? 703 SER   A C   1 
ATOM   3209 O  O   . SER   A 1 407 ? -25.770 -15.854 20.429 1.00 60.30  ? 703 SER   A O   1 
ATOM   3210 C  CB  . SER   A 1 407 ? -27.151 -16.799 23.174 1.00 48.03  ? 703 SER   A CB  1 
ATOM   3211 O  OG  . SER   A 1 407 ? -26.013 -17.559 22.804 1.00 51.27  ? 703 SER   A OG  1 
ATOM   3212 N  N   . PHE   A 1 408 ? -26.028 -14.144 21.906 1.00 55.77  ? 704 PHE   A N   1 
ATOM   3213 C  CA  . PHE   A 1 408 ? -24.758 -13.493 21.614 1.00 59.02  ? 704 PHE   A CA  1 
ATOM   3214 C  C   . PHE   A 1 408 ? -23.728 -13.933 22.653 1.00 57.50  ? 704 PHE   A C   1 
ATOM   3215 O  O   . PHE   A 1 408 ? -24.023 -13.970 23.850 1.00 60.88  ? 704 PHE   A O   1 
ATOM   3216 C  CB  . PHE   A 1 408 ? -24.890 -11.968 21.636 1.00 46.50  ? 704 PHE   A CB  1 
ATOM   3217 C  CG  . PHE   A 1 408 ? -25.661 -11.388 20.483 1.00 50.26  ? 704 PHE   A CG  1 
ATOM   3218 C  CD1 . PHE   A 1 408 ? -26.985 -11.005 20.643 1.00 45.63  ? 704 PHE   A CD1 1 
ATOM   3219 C  CD2 . PHE   A 1 408 ? -25.053 -11.202 19.231 1.00 47.35  ? 704 PHE   A CD2 1 
ATOM   3220 C  CE1 . PHE   A 1 408 ? -27.695 -10.455 19.574 1.00 51.40  ? 704 PHE   A CE1 1 
ATOM   3221 C  CE2 . PHE   A 1 408 ? -25.756 -10.651 18.163 1.00 42.35  ? 704 PHE   A CE2 1 
ATOM   3222 C  CZ  . PHE   A 1 408 ? -27.077 -10.284 18.328 1.00 46.78  ? 704 PHE   A CZ  1 
ATOM   3223 N  N   . GLU   A 1 409 ? -22.524 -14.262 22.189 1.00 49.28  ? 705 GLU   A N   1 
ATOM   3224 C  CA  . GLU   A 1 409 ? -21.463 -14.772 23.031 1.00 50.89  ? 705 GLU   A CA  1 
ATOM   3225 C  C   . GLU   A 1 409 ? -20.187 -13.989 22.771 1.00 56.04  ? 705 GLU   A C   1 
ATOM   3226 O  O   . GLU   A 1 409 ? -20.021 -13.343 21.729 1.00 57.93  ? 705 GLU   A O   1 
ATOM   3227 C  CB  . GLU   A 1 409 ? -21.211 -16.270 22.793 1.00 45.18  ? 705 GLU   A CB  1 
ATOM   3228 C  CG  . GLU   A 1 409 ? -22.440 -17.165 22.913 1.00 61.02  ? 705 GLU   A CG  1 
ATOM   3229 C  CD  . GLU   A 1 409 ? -22.930 -17.309 24.345 1.00 66.51  ? 705 GLU   A CD  1 
ATOM   3230 O  OE1 . GLU   A 1 409 ? -22.167 -16.955 25.275 1.00 70.48  ? 705 GLU   A OE1 1 
ATOM   3231 O  OE2 . GLU   A 1 409 ? -24.078 -17.770 24.535 1.00 66.49  ? 705 GLU   A OE2 1 
ATOM   3232 N  N   . TYR   A 1 410 ? -19.297 -14.037 23.755 1.00 48.70  ? 706 TYR   A N   1 
ATOM   3233 C  CA  . TYR   A 1 410 ? -17.977 -13.465 23.592 1.00 47.68  ? 706 TYR   A CA  1 
ATOM   3234 C  C   . TYR   A 1 410 ? -17.092 -14.447 22.850 1.00 53.18  ? 706 TYR   A C   1 
ATOM   3235 O  O   . TYR   A 1 410 ? -17.335 -15.660 22.835 1.00 65.57  ? 706 TYR   A O   1 
ATOM   3236 C  CB  . TYR   A 1 410 ? -17.349 -13.121 24.955 1.00 42.52  ? 706 TYR   A CB  1 
ATOM   3237 C  CG  . TYR   A 1 410 ? -18.101 -12.039 25.696 1.00 49.72  ? 706 TYR   A CG  1 
ATOM   3238 C  CD1 . TYR   A 1 410 ? -19.078 -12.370 26.634 1.00 58.54  ? 706 TYR   A CD1 1 
ATOM   3239 C  CD2 . TYR   A 1 410 ? -17.857 -10.687 25.447 1.00 56.53  ? 706 TYR   A CD2 1 
ATOM   3240 C  CE1 . TYR   A 1 410 ? -19.790 -11.392 27.315 1.00 65.40  ? 706 TYR   A CE1 1 
ATOM   3241 C  CE2 . TYR   A 1 410 ? -18.568 -9.695  26.127 1.00 71.24  ? 706 TYR   A CE2 1 
ATOM   3242 C  CZ  . TYR   A 1 410 ? -19.530 -10.060 27.066 1.00 67.58  ? 706 TYR   A CZ  1 
ATOM   3243 O  OH  . TYR   A 1 410 ? -20.250 -9.102  27.730 1.00 58.42  ? 706 TYR   A OH  1 
ATOM   3244 N  N   . GLN   A 1 411 ? -16.040 -13.919 22.250 1.00 46.53  ? 707 GLN   A N   1 
ATOM   3245 C  CA  . GLN   A 1 411 ? -15.061 -14.739 21.554 1.00 47.20  ? 707 GLN   A CA  1 
ATOM   3246 C  C   . GLN   A 1 411 ? -13.716 -14.053 21.676 1.00 52.71  ? 707 GLN   A C   1 
ATOM   3247 O  O   . GLN   A 1 411 ? -13.648 -12.833 21.877 1.00 57.76  ? 707 GLN   A O   1 
ATOM   3248 C  CB  . GLN   A 1 411 ? -15.449 -14.928 20.080 1.00 62.49  ? 707 GLN   A CB  1 
ATOM   3249 C  CG  . GLN   A 1 411 ? -15.306 -13.676 19.271 1.00 66.94  ? 707 GLN   A CG  1 
ATOM   3250 C  CD  . GLN   A 1 411 ? -15.938 -13.800 17.907 1.00 74.95  ? 707 GLN   A CD  1 
ATOM   3251 O  OE1 . GLN   A 1 411 ? -16.086 -14.903 17.372 1.00 79.95  ? 707 GLN   A OE1 1 
ATOM   3252 N  NE2 . GLN   A 1 411 ? -16.328 -12.667 17.338 1.00 69.02  ? 707 GLN   A NE2 1 
ATOM   3253 N  N   . PRO   A 1 412 ? -12.622 -14.809 21.602 1.00 62.25  ? 708 PRO   A N   1 
ATOM   3254 C  CA  . PRO   A 1 412 ? -11.292 -14.207 21.756 1.00 69.24  ? 708 PRO   A CA  1 
ATOM   3255 C  C   . PRO   A 1 412 ? -10.974 -13.224 20.639 1.00 75.72  ? 708 PRO   A C   1 
ATOM   3256 O  O   . PRO   A 1 412 ? -11.507 -13.297 19.527 1.00 73.16  ? 708 PRO   A O   1 
ATOM   3257 C  CB  . PRO   A 1 412 ? -10.340 -15.408 21.714 1.00 70.62  ? 708 PRO   A CB  1 
ATOM   3258 C  CG  . PRO   A 1 412 ? -11.133 -16.502 21.050 1.00 78.75  ? 708 PRO   A CG  1 
ATOM   3259 C  CD  . PRO   A 1 412 ? -12.554 -16.272 21.476 1.00 71.04  ? 708 PRO   A CD  1 
ATOM   3260 N  N   . ASP   A 1 413 ? -10.086 -12.287 20.963 1.00 80.14  ? 709 ASP   A N   1 
ATOM   3261 C  CA  . ASP   A 1 413 ? -9.621  -11.337 19.968 1.00 85.09  ? 709 ASP   A CA  1 
ATOM   3262 C  C   . ASP   A 1 413 ? -8.941  -12.089 18.826 1.00 88.70  ? 709 ASP   A C   1 
ATOM   3263 O  O   . ASP   A 1 413 ? -8.137  -13.000 19.068 1.00 88.61  ? 709 ASP   A O   1 
ATOM   3264 C  CB  . ASP   A 1 413 ? -8.658  -10.328 20.593 1.00 88.91  ? 709 ASP   A CB  1 
ATOM   3265 C  CG  . ASP   A 1 413 ? -9.360  -9.335  21.512 1.00 88.81  ? 709 ASP   A CG  1 
ATOM   3266 O  OD1 . ASP   A 1 413 ? -10.593 -9.155  21.387 1.00 83.50  ? 709 ASP   A OD1 1 
ATOM   3267 O  OD2 . ASP   A 1 413 ? -8.669  -8.723  22.353 1.00 88.22  ? 709 ASP   A OD2 1 
ATOM   3268 N  N   . PRO   A 1 414 ? -9.245  -11.748 17.573 1.00 95.53  ? 710 PRO   A N   1 
ATOM   3269 C  CA  . PRO   A 1 414 ? -8.750  -12.564 16.452 1.00 99.14  ? 710 PRO   A CA  1 
ATOM   3270 C  C   . PRO   A 1 414 ? -7.238  -12.563 16.297 1.00 103.43 ? 710 PRO   A C   1 
ATOM   3271 O  O   . PRO   A 1 414 ? -6.696  -13.524 15.736 1.00 113.92 ? 710 PRO   A O   1 
ATOM   3272 C  CB  . PRO   A 1 414 ? -9.441  -11.943 15.226 1.00 99.24  ? 710 PRO   A CB  1 
ATOM   3273 C  CG  . PRO   A 1 414 ? -9.819  -10.562 15.653 1.00 101.08 ? 710 PRO   A CG  1 
ATOM   3274 C  CD  . PRO   A 1 414 ? -10.106 -10.639 17.128 1.00 98.03  ? 710 PRO   A CD  1 
ATOM   3275 N  N   . TRP   A 1 415 ? -6.535  -11.537 16.769 1.00 100.59 ? 711 TRP   A N   1 
ATOM   3276 C  CA  . TRP   A 1 415 ? -5.088  -11.509 16.589 1.00 102.47 ? 711 TRP   A CA  1 
ATOM   3277 C  C   . TRP   A 1 415 ? -4.343  -12.393 17.584 1.00 101.54 ? 711 TRP   A C   1 
ATOM   3278 O  O   . TRP   A 1 415 ? -3.111  -12.481 17.502 1.00 104.53 ? 711 TRP   A O   1 
ATOM   3279 C  CB  . TRP   A 1 415 ? -4.559  -10.071 16.672 1.00 102.29 ? 711 TRP   A CB  1 
ATOM   3280 C  CG  . TRP   A 1 415 ? -4.868  -9.360  17.948 1.00 97.04  ? 711 TRP   A CG  1 
ATOM   3281 C  CD1 . TRP   A 1 415 ? -4.087  -9.303  19.071 1.00 97.45  ? 711 TRP   A CD1 1 
ATOM   3282 C  CD2 . TRP   A 1 415 ? -6.039  -8.586  18.233 1.00 88.82  ? 711 TRP   A CD2 1 
ATOM   3283 N  NE1 . TRP   A 1 415 ? -4.705  -8.546  20.035 1.00 88.51  ? 711 TRP   A NE1 1 
ATOM   3284 C  CE2 . TRP   A 1 415 ? -5.904  -8.094  19.547 1.00 85.48  ? 711 TRP   A CE2 1 
ATOM   3285 C  CE3 . TRP   A 1 415 ? -7.190  -8.265  17.507 1.00 87.17  ? 711 TRP   A CE3 1 
ATOM   3286 C  CZ2 . TRP   A 1 415 ? -6.874  -7.295  20.145 1.00 83.11  ? 711 TRP   A CZ2 1 
ATOM   3287 C  CZ3 . TRP   A 1 415 ? -8.151  -7.475  18.098 1.00 79.75  ? 711 TRP   A CZ3 1 
ATOM   3288 C  CH2 . TRP   A 1 415 ? -7.990  -7.001  19.410 1.00 82.00  ? 711 TRP   A CH2 1 
ATOM   3289 N  N   . ASN   A 1 416 ? -5.047  -13.045 18.513 1.00 90.58  ? 712 ASN   A N   1 
ATOM   3290 C  CA  . ASN   A 1 416 ? -4.425  -14.055 19.358 1.00 93.32  ? 712 ASN   A CA  1 
ATOM   3291 C  C   . ASN   A 1 416 ? -4.513  -15.450 18.761 1.00 97.60  ? 712 ASN   A C   1 
ATOM   3292 O  O   . ASN   A 1 416 ? -3.697  -16.311 19.108 1.00 99.49  ? 712 ASN   A O   1 
ATOM   3293 C  CB  . ASN   A 1 416 ? -5.075  -14.064 20.743 1.00 95.51  ? 712 ASN   A CB  1 
ATOM   3294 C  CG  . ASN   A 1 416 ? -5.194  -12.677 21.337 1.00 102.36 ? 712 ASN   A CG  1 
ATOM   3295 O  OD1 . ASN   A 1 416 ? -4.330  -11.820 21.121 1.00 109.79 ? 712 ASN   A OD1 1 
ATOM   3296 N  ND2 . ASN   A 1 416 ? -6.270  -12.442 22.088 1.00 97.53  ? 712 ASN   A ND2 1 
ATOM   3297 N  N   . THR   A 1 417 ? -5.473  -15.682 17.866 1.00 95.90  ? 713 THR   A N   1 
ATOM   3298 C  CA  . THR   A 1 417 ? -5.738  -16.995 17.292 1.00 101.20 ? 713 THR   A CA  1 
ATOM   3299 C  C   . THR   A 1 417 ? -5.244  -17.146 15.862 1.00 102.20 ? 713 THR   A C   1 
ATOM   3300 O  O   . THR   A 1 417 ? -4.799  -18.237 15.485 1.00 106.89 ? 713 THR   A O   1 
ATOM   3301 C  CB  . THR   A 1 417 ? -7.246  -17.275 17.316 1.00 100.27 ? 713 THR   A CB  1 
ATOM   3302 O  OG1 . THR   A 1 417 ? -7.951  -16.070 17.650 1.00 94.95  ? 713 THR   A OG1 1 
ATOM   3303 C  CG2 . THR   A 1 417 ? -7.583  -18.363 18.331 1.00 101.41 ? 713 THR   A CG2 1 
ATOM   3304 N  N   . HIS   A 1 418 ? -5.301  -16.071 15.075 1.00 100.87 ? 714 HIS   A N   1 
ATOM   3305 C  CA  . HIS   A 1 418 ? -5.169  -16.152 13.624 1.00 101.88 ? 714 HIS   A CA  1 
ATOM   3306 C  C   . HIS   A 1 418 ? -3.841  -16.770 13.197 1.00 107.38 ? 714 HIS   A C   1 
ATOM   3307 O  O   . HIS   A 1 418 ? -2.769  -16.345 13.636 1.00 107.29 ? 714 HIS   A O   1 
ATOM   3308 C  CB  . HIS   A 1 418 ? -5.319  -14.753 13.022 1.00 98.28  ? 714 HIS   A CB  1 
ATOM   3309 C  CG  . HIS   A 1 418 ? -5.341  -14.730 11.524 1.00 98.53  ? 714 HIS   A CG  1 
ATOM   3310 N  ND1 . HIS   A 1 418 ? -6.021  -15.665 10.774 1.00 99.84  ? 714 HIS   A ND1 1 
ATOM   3311 C  CD2 . HIS   A 1 418 ? -4.783  -13.870 10.639 1.00 100.66 ? 714 HIS   A CD2 1 
ATOM   3312 C  CE1 . HIS   A 1 418 ? -5.874  -15.386 9.489  1.00 98.45  ? 714 HIS   A CE1 1 
ATOM   3313 N  NE2 . HIS   A 1 418 ? -5.128  -14.301 9.380  1.00 98.52  ? 714 HIS   A NE2 1 
ATOM   3314 N  N   . VAL   A 1 419 ? -3.925  -17.776 12.330 1.00 112.51 ? 715 VAL   A N   1 
ATOM   3315 C  CA  . VAL   A 1 419 ? -2.747  -18.337 11.679 1.00 120.30 ? 715 VAL   A CA  1 
ATOM   3316 C  C   . VAL   A 1 419 ? -2.383  -17.421 10.516 1.00 121.49 ? 715 VAL   A C   1 
ATOM   3317 O  O   . VAL   A 1 419 ? -3.162  -17.259 9.571  1.00 113.41 ? 715 VAL   A O   1 
ATOM   3318 C  CB  . VAL   A 1 419 ? -3.007  -19.776 11.215 1.00 120.19 ? 715 VAL   A CB  1 
ATOM   3319 C  CG1 . VAL   A 1 419 ? -2.033  -20.174 10.120 1.00 125.76 ? 715 VAL   A CG1 1 
ATOM   3320 C  CG2 . VAL   A 1 419 ? -2.905  -20.736 12.405 1.00 115.28 ? 715 VAL   A CG2 1 
ATOM   3321 N  N   . TRP   A 1 420 ? -1.199  -16.816 10.589 1.00 132.04 ? 716 TRP   A N   1 
ATOM   3322 C  CA  . TRP   A 1 420 ? -0.887  -15.619 9.824  1.00 140.48 ? 716 TRP   A CA  1 
ATOM   3323 C  C   . TRP   A 1 420 ? 0.393   -15.792 9.016  1.00 165.31 ? 716 TRP   A C   1 
ATOM   3324 O  O   . TRP   A 1 420 ? 1.334   -16.450 9.470  1.00 169.83 ? 716 TRP   A O   1 
ATOM   3325 C  CB  . TRP   A 1 420 ? -0.757  -14.426 10.775 1.00 134.82 ? 716 TRP   A CB  1 
ATOM   3326 C  CG  . TRP   A 1 420 ? -1.240  -13.162 10.194 1.00 132.64 ? 716 TRP   A CG  1 
ATOM   3327 C  CD1 . TRP   A 1 420 ? -1.519  -12.928 8.888  1.00 136.48 ? 716 TRP   A CD1 1 
ATOM   3328 C  CD2 . TRP   A 1 420 ? -1.515  -11.944 10.890 1.00 127.75 ? 716 TRP   A CD2 1 
ATOM   3329 N  NE1 . TRP   A 1 420 ? -1.946  -11.636 8.717  1.00 135.47 ? 716 TRP   A NE1 1 
ATOM   3330 C  CE2 . TRP   A 1 420 ? -1.954  -11.008 9.933  1.00 128.29 ? 716 TRP   A CE2 1 
ATOM   3331 C  CE3 . TRP   A 1 420 ? -1.429  -11.551 12.225 1.00 123.10 ? 716 TRP   A CE3 1 
ATOM   3332 C  CZ2 . TRP   A 1 420 ? -2.306  -9.706  10.267 1.00 122.16 ? 716 TRP   A CZ2 1 
ATOM   3333 C  CZ3 . TRP   A 1 420 ? -1.778  -10.258 12.554 1.00 122.91 ? 716 TRP   A CZ3 1 
ATOM   3334 C  CH2 . TRP   A 1 420 ? -2.213  -9.350  11.579 1.00 121.23 ? 716 TRP   A CH2 1 
ATOM   3335 N  N   . LYS   A 1 421 ? 0.419   -15.205 7.813  1.00 79.99  ? 717 LYS   A N   1 
ATOM   3336 C  CA  . LYS   A 1 421 ? 1.634   -15.165 6.985  1.00 89.65  ? 717 LYS   A CA  1 
ATOM   3337 C  C   . LYS   A 1 421 ? 1.802   -13.815 6.278  1.00 97.63  ? 717 LYS   A C   1 
ATOM   3338 O  O   . LYS   A 1 421 ? 1.439   -13.643 5.107  1.00 96.74  ? 717 LYS   A O   1 
ATOM   3339 C  CB  . LYS   A 1 421 ? 1.639   -16.289 5.936  1.00 84.20  ? 717 LYS   A CB  1 
ATOM   3340 C  CG  . LYS   A 1 421 ? 0.588   -17.357 6.129  1.00 85.57  ? 717 LYS   A CG  1 
ATOM   3341 C  CD  . LYS   A 1 421 ? -0.548  -17.162 5.158  1.00 93.43  ? 717 LYS   A CD  1 
ATOM   3342 C  CE  . LYS   A 1 421 ? -1.641  -18.190 5.386  1.00 101.50 ? 717 LYS   A CE  1 
ATOM   3343 N  NZ  . LYS   A 1 421 ? -2.446  -18.404 4.145  1.00 105.72 ? 717 LYS   A NZ  1 
HETATM 3344 C  CHA . HEM   B 2 .   ? -25.237 -4.337  26.302 1.00 55.76  ? 801 HEM   A CHA 1 
HETATM 3345 C  CHB . HEM   B 2 .   ? -28.329 -0.668  25.715 1.00 64.18  ? 801 HEM   A CHB 1 
HETATM 3346 C  CHC . HEM   B 2 .   ? -29.555 -2.367  21.283 1.00 54.00  ? 801 HEM   A CHC 1 
HETATM 3347 C  CHD . HEM   B 2 .   ? -27.223 -6.486  22.363 1.00 48.99  ? 801 HEM   A CHD 1 
HETATM 3348 C  C1A . HEM   B 2 .   ? -25.846 -3.100  26.472 1.00 55.23  ? 801 HEM   A C1A 1 
HETATM 3349 C  C2A . HEM   B 2 .   ? -25.482 -2.029  27.397 1.00 63.91  ? 801 HEM   A C2A 1 
HETATM 3350 C  C3A . HEM   B 2 .   ? -26.335 -1.019  27.221 1.00 63.24  ? 801 HEM   A C3A 1 
HETATM 3351 C  C4A . HEM   B 2 .   ? -27.281 -1.411  26.194 1.00 60.40  ? 801 HEM   A C4A 1 
HETATM 3352 C  CMA . HEM   B 2 .   ? -26.326 0.317   28.002 1.00 54.37  ? 801 HEM   A CMA 1 
HETATM 3353 C  CAA . HEM   B 2 .   ? -24.298 -2.024  28.393 1.00 56.92  ? 801 HEM   A CAA 1 
HETATM 3354 C  CBA . HEM   B 2 .   ? -23.086 -1.850  27.476 1.00 51.59  ? 801 HEM   A CBA 1 
HETATM 3355 C  CGA . HEM   B 2 .   ? -21.814 -1.894  28.261 1.00 54.10  ? 801 HEM   A CGA 1 
HETATM 3356 O  O1A . HEM   B 2 .   ? -21.831 -1.419  29.429 1.00 46.97  ? 801 HEM   A O1A 1 
HETATM 3357 O  O2A . HEM   B 2 .   ? -20.796 -2.388  27.716 1.00 52.78  ? 801 HEM   A O2A 1 
HETATM 3358 C  C1B . HEM   B 2 .   ? -28.901 -0.820  24.477 1.00 64.74  ? 801 HEM   A C1B 1 
HETATM 3359 C  C2B . HEM   B 2 .   ? -29.824 0.123   23.900 1.00 62.38  ? 801 HEM   A C2B 1 
HETATM 3360 C  C3B . HEM   B 2 .   ? -30.183 -0.341  22.695 1.00 64.11  ? 801 HEM   A C3B 1 
HETATM 3361 C  C4B . HEM   B 2 .   ? -29.478 -1.587  22.433 1.00 61.87  ? 801 HEM   A C4B 1 
HETATM 3362 C  CMB . HEM   B 2 .   ? -30.312 1.408   24.606 1.00 61.59  ? 801 HEM   A CMB 1 
HETATM 3363 C  CAB . HEM   B 2 .   ? -31.166 0.379   21.751 1.00 67.35  ? 801 HEM   A CAB 1 
HETATM 3364 C  CBB . HEM   B 2 .   ? -31.978 -0.323  20.957 1.00 76.69  ? 801 HEM   A CBB 1 
HETATM 3365 C  C1C . HEM   B 2 .   ? -29.015 -3.631  21.156 1.00 47.22  ? 801 HEM   A C1C 1 
HETATM 3366 C  C2C . HEM   B 2 .   ? -29.079 -4.494  19.990 1.00 51.74  ? 801 HEM   A C2C 1 
HETATM 3367 C  C3C . HEM   B 2 .   ? -28.409 -5.619  20.291 1.00 51.91  ? 801 HEM   A C3C 1 
HETATM 3368 C  C4C . HEM   B 2 .   ? -27.941 -5.523  21.669 1.00 55.34  ? 801 HEM   A C4C 1 
HETATM 3369 C  CMC . HEM   B 2 .   ? -29.759 -4.072  18.657 1.00 54.62  ? 801 HEM   A CMC 1 
HETATM 3370 C  CAC . HEM   B 2 .   ? -28.167 -6.895  19.469 1.00 51.64  ? 801 HEM   A CAC 1 
HETATM 3371 C  CBC . HEM   B 2 .   ? -29.007 -7.254  18.497 1.00 46.60  ? 801 HEM   A CBC 1 
HETATM 3372 C  C1D . HEM   B 2 .   ? -26.509 -6.286  23.528 1.00 46.69  ? 801 HEM   A C1D 1 
HETATM 3373 C  C2D . HEM   B 2 .   ? -25.710 -7.269  24.210 1.00 46.83  ? 801 HEM   A C2D 1 
HETATM 3374 C  C3D . HEM   B 2 .   ? -25.160 -6.683  25.306 1.00 47.67  ? 801 HEM   A C3D 1 
HETATM 3375 C  C4D . HEM   B 2 .   ? -25.578 -5.298  25.342 1.00 49.86  ? 801 HEM   A C4D 1 
HETATM 3376 C  CMD . HEM   B 2 .   ? -25.572 -8.737  23.723 1.00 45.45  ? 801 HEM   A CMD 1 
HETATM 3377 C  CAD . HEM   B 2 .   ? -24.238 -7.342  26.363 1.00 50.78  ? 801 HEM   A CAD 1 
HETATM 3378 C  CBD . HEM   B 2 .   ? -22.971 -7.846  25.686 1.00 58.46  ? 801 HEM   A CBD 1 
HETATM 3379 C  CGD . HEM   B 2 .   ? -21.885 -6.866  25.968 1.00 58.32  ? 801 HEM   A CGD 1 
HETATM 3380 O  O1D . HEM   B 2 .   ? -20.832 -7.309  26.522 1.00 63.76  ? 801 HEM   A O1D 1 
HETATM 3381 O  O2D . HEM   B 2 .   ? -22.102 -5.659  25.678 1.00 63.81  ? 801 HEM   A O2D 1 
HETATM 3382 N  NA  . HEM   B 2 .   ? -26.954 -2.675  25.763 1.00 57.19  ? 801 HEM   A NA  1 
HETATM 3383 N  NB  . HEM   B 2 .   ? -28.706 -1.858  23.559 1.00 58.69  ? 801 HEM   A NB  1 
HETATM 3384 N  NC  . HEM   B 2 .   ? -28.330 -4.296  22.143 1.00 52.95  ? 801 HEM   A NC  1 
HETATM 3385 N  ND  . HEM   B 2 .   ? -26.400 -5.087  24.227 1.00 44.26  ? 801 HEM   A ND  1 
HETATM 3386 FE FE  . HEM   B 2 .   ? -27.893 -3.769  24.195 1.00 51.41  ? 801 HEM   A FE  1 
HETATM 3387 N  N1  . H4B   C 3 .   ? -21.908 -3.099  33.654 1.00 53.02  ? 802 H4B   A N1  1 
HETATM 3388 C  C2  . H4B   C 3 .   ? -21.897 -2.565  32.409 1.00 52.40  ? 802 H4B   A C2  1 
HETATM 3389 N  N2  . H4B   C 3 .   ? -23.061 -2.157  31.840 1.00 47.28  ? 802 H4B   A N2  1 
HETATM 3390 N  N3  . H4B   C 3 .   ? -20.731 -2.433  31.739 1.00 48.37  ? 802 H4B   A N3  1 
HETATM 3391 C  C4  . H4B   C 3 .   ? -19.563 -2.846  32.280 1.00 57.02  ? 802 H4B   A C4  1 
HETATM 3392 O  O4  . H4B   C 3 .   ? -18.495 -2.733  31.625 1.00 49.67  ? 802 H4B   A O4  1 
HETATM 3393 C  C4A . H4B   C 3 .   ? -19.561 -3.398  33.557 1.00 56.77  ? 802 H4B   A C4A 1 
HETATM 3394 C  C8A . H4B   C 3 .   ? -20.758 -3.508  34.237 1.00 60.43  ? 802 H4B   A C8A 1 
HETATM 3395 N  N5  . H4B   C 3 .   ? -18.430 -3.823  34.160 1.00 54.01  ? 802 H4B   A N5  1 
HETATM 3396 N  N8  . H4B   C 3 .   ? -20.796 -4.033  35.500 1.00 57.79  ? 802 H4B   A N8  1 
HETATM 3397 C  C6  . H4B   C 3 .   ? -18.558 -4.830  35.223 1.00 52.33  ? 802 H4B   A C6  1 
HETATM 3398 C  C7  . H4B   C 3 .   ? -19.597 -4.400  36.233 1.00 60.04  ? 802 H4B   A C7  1 
HETATM 3399 C  C9  . H4B   C 3 .   ? -17.238 -5.059  35.947 1.00 46.02  ? 802 H4B   A C9  1 
HETATM 3400 O  O9  . H4B   C 3 .   ? -16.869 -3.772  36.428 1.00 45.82  ? 802 H4B   A O9  1 
HETATM 3401 C  C10 . H4B   C 3 .   ? -17.399 -6.073  37.087 1.00 43.03  ? 802 H4B   A C10 1 
HETATM 3402 C  C11 . H4B   C 3 .   ? -16.150 -6.237  37.951 1.00 45.75  ? 802 H4B   A C11 1 
HETATM 3403 O  O10 . H4B   C 3 .   ? -17.737 -7.364  36.535 1.00 48.70  ? 802 H4B   A O10 1 
HETATM 3404 ZN ZN  . ZN    D 4 .   ? -24.394 -16.545 41.001 0.46 55.39  ? 803 ZN    A ZN  1 
HETATM 3405 C  C14 . A1AZ9 E 5 .   ? -19.523 -0.935  23.952 1.00 68.80  ? 804 A1AZ9 A C14 1 
HETATM 3406 C  C13 . A1AZ9 E 5 .   ? -20.084 0.242   23.521 1.00 69.47  ? 804 A1AZ9 A C13 1 
HETATM 3407 C  C12 . A1AZ9 E 5 .   ? -21.435 0.268   23.290 1.00 61.00  ? 804 A1AZ9 A C12 1 
HETATM 3408 C  C11 . A1AZ9 E 5 .   ? -22.227 -0.850  23.467 1.00 56.45  ? 804 A1AZ9 A C11 1 
HETATM 3409 C  C15 . A1AZ9 E 5 .   ? -20.305 -2.056  24.139 1.00 58.12  ? 804 A1AZ9 A C15 1 
HETATM 3410 C  C16 . A1AZ9 E 5 .   ? -21.673 -2.057  23.900 1.00 54.27  ? 804 A1AZ9 A C16 1 
HETATM 3411 C  C17 . A1AZ9 E 5 .   ? -19.534 -3.249  24.574 1.00 62.15  ? 804 A1AZ9 A C17 1 
HETATM 3412 C  C19 . A1AZ9 E 5 .   ? -19.126 -5.098  25.737 1.00 76.97  ? 804 A1AZ9 A C19 1 
HETATM 3413 C  C20 . A1AZ9 E 5 .   ? -18.093 -4.362  26.565 1.00 77.74  ? 804 A1AZ9 A C20 1 
HETATM 3414 C  C02 . A1AZ9 E 5 .   ? -25.726 0.428   23.443 1.00 57.66  ? 804 A1AZ9 A C02 1 
HETATM 3415 C  C03 . A1AZ9 E 5 .   ? -26.308 -0.384  22.470 1.00 49.45  ? 804 A1AZ9 A C03 1 
HETATM 3416 C  C04 . A1AZ9 E 5 .   ? -25.541 -1.340  21.817 1.00 55.20  ? 804 A1AZ9 A C04 1 
HETATM 3417 C  C05 . A1AZ9 E 5 .   ? -24.209 -1.493  22.163 1.00 54.17  ? 804 A1AZ9 A C05 1 
HETATM 3418 C  C06 . A1AZ9 E 5 .   ? -23.670 -0.685  23.150 1.00 48.48  ? 804 A1AZ9 A C06 1 
HETATM 3419 C  C07 . A1AZ9 E 5 .   ? -26.126 -2.219  20.730 1.00 53.65  ? 804 A1AZ9 A C07 1 
HETATM 3420 F  F12 . A1AZ9 E 5 .   ? -21.998 1.406   22.891 1.00 80.88  ? 804 A1AZ9 A F12 1 
HETATM 3421 F  F13 . A1AZ9 E 5 .   ? -19.328 1.342   23.344 1.00 77.51  ? 804 A1AZ9 A F13 1 
HETATM 3422 F  F21 . A1AZ9 E 5 .   ? -17.003 -5.183  26.610 1.00 85.86  ? 804 A1AZ9 A F21 1 
HETATM 3423 N  N01 . A1AZ9 E 5 .   ? -24.422 0.269   23.766 1.00 62.15  ? 804 A1AZ9 A N01 1 
HETATM 3424 N  N02 . A1AZ9 E 5 .   ? -26.466 1.361   24.095 1.00 63.26  ? 804 A1AZ9 A N02 1 
HETATM 3425 N  N18 . A1AZ9 E 5 .   ? -20.237 -4.196  25.416 1.00 70.55  ? 804 A1AZ9 A N18 1 
HETATM 3426 O  O   . HOH   F 6 .   ? -16.181 -30.033 18.848 1.00 70.06  ? 901 HOH   A O   1 
HETATM 3427 O  O   . HOH   F 6 .   ? -2.274  -15.433 6.976  1.00 70.38  ? 902 HOH   A O   1 
HETATM 3428 O  O   . HOH   F 6 .   ? -7.907  14.082  16.505 1.00 62.25  ? 903 HOH   A O   1 
HETATM 3429 O  O   . HOH   F 6 .   ? -26.357 -34.709 13.944 1.00 67.58  ? 904 HOH   A O   1 
HETATM 3430 O  O   . HOH   F 6 .   ? -24.909 5.627   0.393  1.00 52.09  ? 905 HOH   A O   1 
HETATM 3431 O  O   . HOH   F 6 .   ? -21.621 -14.968 -2.871 1.00 50.39  ? 906 HOH   A O   1 
HETATM 3432 O  O   . HOH   F 6 .   ? 0.066   4.362   21.026 1.00 97.74  ? 907 HOH   A O   1 
HETATM 3433 O  O   . HOH   F 6 .   ? -25.348 -4.061  6.019  1.00 48.28  ? 908 HOH   A O   1 
HETATM 3434 O  O   . HOH   F 6 .   ? -29.737 -16.056 28.113 1.00 53.38  ? 909 HOH   A O   1 
HETATM 3435 O  O   . HOH   F 6 .   ? -14.641 -21.038 9.426  1.00 52.44  ? 910 HOH   A O   1 
HETATM 3436 O  O   . HOH   F 6 .   ? -28.143 -13.244 24.045 1.00 75.59  ? 911 HOH   A O   1 
HETATM 3437 O  O   . HOH   F 6 .   ? -29.598 -13.090 40.308 1.00 77.84  ? 912 HOH   A O   1 
HETATM 3438 O  O   . HOH   F 6 .   ? -16.919 -19.523 7.829  1.00 74.79  ? 913 HOH   A O   1 
HETATM 3439 O  O   . HOH   F 6 .   ? -24.818 -12.170 32.412 1.00 58.29  ? 914 HOH   A O   1 
HETATM 3440 O  O   . HOH   F 6 .   ? -23.998 -3.314  -2.366 1.00 57.96  ? 915 HOH   A O   1 
HETATM 3441 O  O   . HOH   F 6 .   ? -21.741 -13.819 27.730 1.00 69.06  ? 916 HOH   A O   1 
HETATM 3442 O  O   . HOH   F 6 .   ? -22.002 -10.679 35.559 1.00 61.61  ? 917 HOH   A O   1 
HETATM 3443 O  O   . HOH   F 6 .   ? -24.707 -11.105 37.644 1.00 60.23  ? 918 HOH   A O   1 
HETATM 3444 O  O   . HOH   F 6 .   ? -32.036 -23.625 2.320  1.00 62.47  ? 919 HOH   A O   1 
HETATM 3445 O  O   . HOH   F 6 .   ? -17.572 -16.989 9.823  1.00 75.76  ? 920 HOH   A O   1 
HETATM 3446 O  O   . HOH   F 6 .   ? -18.510 -1.975  29.047 1.00 43.51  ? 921 HOH   A O   1 
HETATM 3447 O  O   . HOH   F 6 .   ? -18.972 3.424   24.382 1.00 49.62  ? 922 HOH   A O   1 
HETATM 3448 O  O   . HOH   F 6 .   ? -27.355 -2.781  29.862 1.00 53.62  ? 923 HOH   A O   1 
HETATM 3449 O  O   . HOH   F 6 .   ? -22.031 1.337   30.245 1.00 56.10  ? 924 HOH   A O   1 
HETATM 3450 O  O   . HOH   F 6 .   ? -23.299 -0.722  34.591 1.00 46.81  ? 925 HOH   A O   1 
HETATM 3451 O  O   . HOH   F 6 .   ? -28.026 24.012  21.639 1.00 73.47  ? 926 HOH   A O   1 
HETATM 3452 O  O   . HOH   F 6 .   ? -17.164 -18.554 21.864 1.00 84.38  ? 927 HOH   A O   1 
HETATM 3453 O  O   . HOH   F 6 .   ? -9.399  -17.785 10.905 1.00 65.25  ? 928 HOH   A O   1 
HETATM 3454 O  O   . HOH   F 6 .   ? -23.847 -14.373 36.286 1.00 73.04  ? 929 HOH   A O   1 
HETATM 3455 O  O   . HOH   F 6 .   ? -28.582 -11.035 38.239 1.00 66.58  ? 930 HOH   A O   1 
HETATM 3456 O  O   . HOH   F 6 .   ? -29.218 22.939  18.426 1.00 68.61  ? 931 HOH   A O   1 
HETATM 3457 O  O   . HOH   F 6 .   ? -19.879 -35.892 19.192 1.00 84.28  ? 932 HOH   A O   1 
HETATM 3458 O  O   . HOH   F 6 .   ? -46.226 -15.796 19.107 1.00 64.99  ? 933 HOH   A O   1 
HETATM 3459 O  O   . HOH   F 6 .   ? -25.094 0.401   32.217 1.00 47.73  ? 934 HOH   A O   1 
HETATM 3460 O  O   . HOH   F 6 .   ? -27.810 -15.836 1.554  1.00 60.91  ? 935 HOH   A O   1 
HETATM 3461 O  O   . HOH   F 6 .   ? -36.121 -7.633  9.545  1.00 69.80  ? 936 HOH   A O   1 
HETATM 3462 O  O   . HOH   F 6 .   ? -28.550 -13.931 0.390  1.00 85.50  ? 937 HOH   A O   1 
HETATM 3463 O  O   . HOH   F 6 .   ? -44.309 -12.761 22.202 1.00 80.94  ? 938 HOH   A O   1 
HETATM 3464 O  O   . HOH   F 6 .   ? -17.504 0.908   28.690 1.00 56.96  ? 939 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   ? 1.7559 1.7079 1.4079 -0.5493 0.0155  0.0990  299 ARG A N   
2    C CA  . ARG A 3   ? 1.7792 1.6916 1.4348 -0.5446 0.0007  0.0895  299 ARG A CA  
3    C C   . ARG A 3   ? 1.6434 1.6883 1.3945 -0.5188 0.0036  0.0797  299 ARG A C   
4    O O   . ARG A 3   ? 1.6881 1.7098 1.4615 -0.4889 -0.0078 0.0694  299 ARG A O   
5    C CB  . ARG A 3   ? 1.9210 1.7759 1.5030 -0.5911 -0.0082 0.0892  299 ARG A CB  
6    C CG  . ARG A 3   ? 1.9973 1.7731 1.5543 -0.5804 -0.0243 0.0797  299 ARG A CG  
7    C CD  . ARG A 3   ? 2.0818 1.7107 1.5852 -0.5402 -0.0359 0.0779  299 ARG A CD  
8    N NE  . ARG A 3   ? 2.0185 1.6721 1.5915 -0.4846 -0.0379 0.0712  299 ARG A NE  
9    C CZ  . ARG A 3   ? 2.0021 1.6269 1.5911 -0.4483 -0.0491 0.0599  299 ARG A CZ  
10   N NH1 . ARG A 3   ? 2.0698 1.6258 1.6032 -0.4721 -0.0585 0.0562  299 ARG A NH1 
11   N NH2 . ARG A 3   ? 1.9023 1.5706 1.5601 -0.3836 -0.0504 0.0514  299 ARG A NH2 
12   N N   . PHE A 4   ? 1.4779 1.6616 1.2807 -0.5273 0.0192  0.0833  300 PHE A N   
13   C CA  . PHE A 4   ? 1.3072 1.6275 1.1910 -0.5069 0.0232  0.0763  300 PHE A CA  
14   C C   . PHE A 4   ? 1.2728 1.6698 1.2109 -0.4446 0.0351  0.0730  300 PHE A C   
15   O O   . PHE A 4   ? 1.4040 1.9147 1.3661 -0.4534 0.0509  0.0783  300 PHE A O   
16   C CB  . PHE A 4   ? 1.2626 1.6640 1.1376 -0.5503 0.0248  0.0783  300 PHE A CB  
17   C CG  . PHE A 4   ? 1.3385 1.6306 1.1243 -0.6030 0.0136  0.0813  300 PHE A CG  
18   C CD1 . PHE A 4   ? 1.3269 1.5910 1.0518 -0.6437 0.0181  0.0899  300 PHE A CD1 
19   C CD2 . PHE A 4   ? 1.3673 1.5797 1.1237 -0.6092 -0.0016 0.0750  300 PHE A CD2 
20   C CE1 . PHE A 4   ? 1.4118 1.5687 1.0450 -0.6899 0.0070  0.0919  300 PHE A CE1 
21   C CE2 . PHE A 4   ? 1.4687 1.5743 1.1329 -0.6524 -0.0114 0.0771  300 PHE A CE2 
22   C CZ  . PHE A 4   ? 1.5300 1.6061 1.1306 -0.6929 -0.0076 0.0855  300 PHE A CZ  
23   N N   . LEU A 5   ? 1.1333 1.4691 1.0869 -0.3815 0.0271  0.0639  301 LEU A N   
24   C CA  . LEU A 5   ? 0.9662 1.2995 0.9314 -0.3295 0.0336  0.0618  301 LEU A CA  
25   C C   . LEU A 5   ? 0.9008 1.3531 0.9243 -0.2863 0.0443  0.0564  301 LEU A C   
26   O O   . LEU A 5   ? 0.8809 1.4081 0.9450 -0.2790 0.0431  0.0520  301 LEU A O   
27   C CB  . LEU A 5   ? 0.8544 1.0806 0.8103 -0.2855 0.0189  0.0542  301 LEU A CB  
28   C CG  . LEU A 5   ? 0.9170 1.0177 0.8131 -0.3078 0.0059  0.0572  301 LEU A CG  
29   C CD1 . LEU A 5   ? 0.9892 1.0360 0.9010 -0.2669 -0.0088 0.0472  301 LEU A CD1 
30   C CD2 . LEU A 5   ? 0.9208 0.9534 0.7658 -0.3090 0.0078  0.0646  301 LEU A CD2 
31   N N   . LYS A 6   ? 0.8133 1.2734 0.8333 -0.2525 0.0539  0.0564  302 LYS A N   
32   C CA  . LYS A 6   ? 0.7627 1.3141 0.8192 -0.2024 0.0648  0.0508  302 LYS A CA  
33   C C   . LYS A 6   ? 0.7342 1.2148 0.7924 -0.1426 0.0557  0.0406  302 LYS A C   
34   O O   . LYS A 6   ? 0.6840 1.0684 0.7114 -0.1386 0.0481  0.0404  302 LYS A O   
35   C CB  . LYS A 6   ? 0.9188 1.5344 0.9608 -0.2087 0.0841  0.0578  302 LYS A CB  
36   C CG  . LYS A 6   ? 0.9940 1.6796 1.0255 -0.2786 0.0945  0.0702  302 LYS A CG  
37   C CD  . LYS A 6   ? 0.9772 1.7905 1.0546 -0.2926 0.0972  0.0699  302 LYS A CD  
38   C CE  . LYS A 6   ? 1.0002 1.8751 1.0604 -0.3714 0.1033  0.0817  302 LYS A CE  
39   N NZ  . LYS A 6   ? 0.9883 1.9122 1.0272 -0.3795 0.1186  0.0884  302 LYS A NZ  
40   N N   . VAL A 7   ? 0.7527 1.2804 0.8423 -0.0980 0.0553  0.0325  303 VAL A N   
41   C CA  . VAL A 7   ? 0.7062 1.1743 0.7892 -0.0444 0.0485  0.0233  303 VAL A CA  
42   C C   . VAL A 7   ? 0.7506 1.2910 0.8373 0.0038  0.0616  0.0192  303 VAL A C   
43   O O   . VAL A 7   ? 0.7976 1.4422 0.9112 0.0104  0.0699  0.0203  303 VAL A O   
44   C CB  . VAL A 7   ? 0.7034 1.1276 0.8040 -0.0328 0.0325  0.0169  303 VAL A CB  
45   C CG1 . VAL A 7   ? 0.7796 1.1499 0.8753 -0.0772 0.0218  0.0207  303 VAL A CG1 
46   C CG2 . VAL A 7   ? 0.6327 1.1408 0.7656 -0.0123 0.0349  0.0139  303 VAL A CG2 
47   N N   . LYS A 8   ? 0.6904 1.1759 0.7453 0.0390  0.0629  0.0143  304 LYS A N   
48   C CA  . LYS A 8   ? 0.6624 1.1972 0.7025 0.0885  0.0765  0.0100  304 LYS A CA  
49   C C   . LYS A 8   ? 0.6075 1.0752 0.6260 0.1408  0.0667  -0.0007 304 LYS A C   
50   O O   . LYS A 8   ? 0.6845 1.0602 0.6938 0.1330  0.0507  -0.0039 304 LYS A O   
51   C CB  . LYS A 8   ? 0.7244 1.2446 0.7294 0.0842  0.0877  0.0130  304 LYS A CB  
52   C CG  . LYS A 8   ? 0.7677 1.3309 0.7471 0.1399  0.1030  0.0074  304 LYS A CG  
53   C CD  . LYS A 8   ? 0.8890 1.4633 0.8393 0.1275  0.1175  0.0124  304 LYS A CD  
54   C CE  . LYS A 8   ? 0.9347 1.5260 0.8468 0.1913  0.1308  0.0042  304 LYS A CE  
55   N NZ  . LYS A 8   ? 1.0409 1.6578 0.9257 0.1808  0.1474  0.0093  304 LYS A NZ  
56   N N   . ASN A 9   ? 0.5843 1.1003 0.5901 0.1944  0.0763  -0.0058 305 ASN A N   
57   C CA  . ASN A 9   ? 0.6979 1.1347 0.6589 0.2477  0.0694  -0.0158 305 ASN A CA  
58   C C   . ASN A 9   ? 0.7619 1.1792 0.6715 0.2809  0.0809  -0.0200 305 ASN A C   
59   O O   . ASN A 9   ? 0.7809 1.2937 0.6942 0.3020  0.0991  -0.0180 305 ASN A O   
60   C CB  . ASN A 9   ? 0.7958 1.2823 0.7652 0.2931  0.0694  -0.0193 305 ASN A CB  
61   C CG  . ASN A 9   ? 0.8541 1.2373 0.7618 0.3456  0.0605  -0.0290 305 ASN A CG  
62   O OD1 . ASN A 9   ? 0.8831 1.2095 0.7331 0.3765  0.0648  -0.0348 305 ASN A OD1 
63   N ND2 . ASN A 9   ? 0.7132 1.0646 0.6250 0.3533  0.0479  -0.0305 305 ASN A ND2 
64   N N   . TRP A 10  ? 0.8128 1.1128 0.6736 0.2838  0.0705  -0.0257 306 TRP A N   
65   C CA  . TRP A 10  ? 1.0241 1.2882 0.8278 0.3107  0.0790  -0.0306 306 TRP A CA  
66   C C   . TRP A 10  ? 1.1177 1.3351 0.8567 0.3797  0.0805  -0.0417 306 TRP A C   
67   O O   . TRP A 10  ? 1.1851 1.3493 0.8617 0.4066  0.0852  -0.0481 306 TRP A O   
68   C CB  . TRP A 10  ? 1.0277 1.1928 0.8072 0.2732  0.0658  -0.0306 306 TRP A CB  
69   C CG  . TRP A 10  ? 0.9628 1.1624 0.7885 0.2146  0.0654  -0.0197 306 TRP A CG  
70   C CD1 . TRP A 10  ? 0.8859 1.0765 0.7533 0.1737  0.0526  -0.0144 306 TRP A CD1 
71   C CD2 . TRP A 10  ? 0.9198 1.1600 0.7439 0.1927  0.0785  -0.0125 306 TRP A CD2 
72   N NE1 . TRP A 10  ? 0.8325 1.0457 0.7180 0.1301  0.0559  -0.0049 306 TRP A NE1 
73   C CE2 . TRP A 10  ? 0.9072 1.1502 0.7666 0.1382  0.0716  -0.0028 306 TRP A CE2 
74   C CE3 . TRP A 10  ? 0.9043 1.1740 0.6944 0.2148  0.0957  -0.0132 306 TRP A CE3 
75   C CZ2 . TRP A 10  ? 0.8727 1.1387 0.7292 0.1028  0.0804  0.0070  306 TRP A CZ2 
76   C CZ3 . TRP A 10  ? 0.9255 1.2295 0.7204 0.1771  0.1056  -0.0032 306 TRP A CZ3 
77   C CH2 . TRP A 10  ? 0.8896 1.1873 0.7150 0.1206  0.0974  0.0072  306 TRP A CH2 
78   N N   . GLU A 11  ? 1.0868 1.3133 0.8307 0.4099  0.0758  -0.0442 307 GLU A N   
79   C CA  . GLU A 11  ? 1.1541 1.3567 0.8342 0.4856  0.0805  -0.0532 307 GLU A CA  
80   C C   . GLU A 11  ? 1.1582 1.5098 0.8689 0.5279  0.1008  -0.0505 307 GLU A C   
81   O O   . GLU A 11  ? 1.3173 1.6689 0.9812 0.5701  0.1040  -0.0503 307 GLU A O   
82   C CB  . GLU A 11  ? 1.1232 1.2437 0.7784 0.5001  0.0632  -0.0569 307 GLU A CB  
83   C CG  . GLU A 11  ? 1.2490 1.2637 0.8009 0.5635  0.0585  -0.0659 307 GLU A CG  
84   C CD  . GLU A 11  ? 1.3891 1.3547 0.9221 0.5748  0.0422  -0.0630 307 GLU A CD  
85   O OE1 . GLU A 11  ? 1.4133 1.3670 0.8943 0.6185  0.0385  -0.0595 307 GLU A OE1 
86   O OE2 . GLU A 11  ? 1.3828 1.3213 0.9484 0.5415  0.0331  -0.0639 307 GLU A OE2 
87   N N   . THR A 12  ? 1.0447 1.5142 0.8377 0.4933  0.1036  -0.0412 308 THR A N   
88   C CA  . THR A 12  ? 1.0277 1.6313 0.8564 0.5088  0.1090  -0.0328 308 THR A CA  
89   C C   . THR A 12  ? 1.0227 1.7570 0.9069 0.4658  0.1255  -0.0238 308 THR A C   
90   O O   . THR A 12  ? 1.0248 1.8713 0.9346 0.4708  0.1273  -0.0162 308 THR A O   
91   C CB  . THR A 12  ? 1.0400 1.6761 0.9084 0.5005  0.0961  -0.0291 308 THR A CB  
92   O OG1 . THR A 12  ? 0.9356 1.6326 0.8775 0.4376  0.0991  -0.0242 308 THR A OG1 
93   C CG2 . THR A 12  ? 1.0817 1.5789 0.8978 0.5257  0.0800  -0.0366 308 THR A CG2 
94   N N   . ASP A 13  ? 1.0492 1.7646 0.9455 0.4174  0.1342  -0.0228 309 ASP A N   
95   C CA  . ASP A 13  ? 1.1035 1.9240 1.0431 0.3623  0.1483  -0.0118 309 ASP A CA  
96   C C   . ASP A 13  ? 1.0838 2.0147 1.0930 0.3173  0.1458  -0.0025 309 ASP A C   
97   O O   . ASP A 13  ? 1.1313 2.1607 1.1701 0.2746  0.1532  0.0077  309 ASP A O   
98   C CB  . ASP A 13  ? 1.2101 2.0975 1.1275 0.3906  0.1618  -0.0095 309 ASP A CB  
99   C CG  . ASP A 13  ? 1.2926 2.0965 1.1507 0.4035  0.1718  -0.0155 309 ASP A CG  
100  O OD1 . ASP A 13  ? 1.2896 2.0866 1.1558 0.3464  0.1772  -0.0086 309 ASP A OD1 
101  O OD2 . ASP A 13  ? 1.3535 2.0769 1.1508 0.4623  0.1666  -0.0248 309 ASP A OD2 
102  N N   . VAL A 14  ? 0.9646 1.8623 0.9929 0.3184  0.1300  -0.0050 310 VAL A N   
103  C CA  . VAL A 14  ? 0.8707 1.8522 0.9564 0.2723  0.1232  0.0028  310 VAL A CA  
104  C C   . VAL A 14  ? 0.9112 1.8397 1.0167 0.1930  0.1159  0.0091  310 VAL A C   
105  O O   . VAL A 14  ? 1.0481 1.8432 1.1258 0.1823  0.1041  0.0060  310 VAL A O   
106  C CB  . VAL A 14  ? 0.7113 1.6643 0.7976 0.3073  0.1059  -0.0020 310 VAL A CB  
107  C CG1 . VAL A 14  ? 0.6439 1.6382 0.7817 0.2513  0.0958  0.0037  310 VAL A CG1 
108  C CG2 . VAL A 14  ? 0.7252 1.7289 0.7852 0.3617  0.1032  -0.0019 310 VAL A CG2 
109  N N   . VAL A 15  ? 0.8212 1.8455 0.9662 0.1345  0.1201  0.0187  311 VAL A N   
110  C CA  . VAL A 15  ? 0.7810 1.7428 0.9313 0.0585  0.1106  0.0254  311 VAL A CA  
111  C C   . VAL A 15  ? 0.8001 1.8224 0.9906 0.0210  0.1017  0.0288  311 VAL A C   
112  O O   . VAL A 15  ? 0.8616 1.9883 1.0705 0.0279  0.1029  0.0305  311 VAL A O   
113  C CB  . VAL A 15  ? 0.8045 1.7932 0.9401 0.0086  0.1244  0.0352  311 VAL A CB  
114  C CG1 . VAL A 15  ? 0.8074 1.6970 0.9292 -0.0593 0.1121  0.0413  311 VAL A CG1 
115  C CG2 . VAL A 15  ? 0.8771 1.8255 0.9729 0.0518  0.1350  0.0313  311 VAL A CG2 
116  N N   . LEU A 16  ? 0.7162 1.6390 0.9037 -0.0172 0.0853  0.0288  312 LEU A N   
117  C CA  . LEU A 16  ? 0.7039 1.6607 0.9193 -0.0582 0.0751  0.0311  312 LEU A CA  
118  C C   . LEU A 16  ? 0.7340 1.6063 0.9278 -0.1278 0.0676  0.0369  312 LEU A C   
119  O O   . LEU A 16  ? 0.7259 1.4819 0.8882 -0.1266 0.0627  0.0358  312 LEU A O   
120  C CB  . LEU A 16  ? 0.6581 1.5701 0.8848 -0.0166 0.0604  0.0225  312 LEU A CB  
121  C CG  . LEU A 16  ? 0.7422 1.7499 0.9851 0.0487  0.0663  0.0183  312 LEU A CG  
122  C CD1 . LEU A 16  ? 0.7298 1.6777 0.9726 0.0890  0.0515  0.0109  312 LEU A CD1 
123  C CD2 . LEU A 16  ? 0.8044 1.9111 1.0527 0.0235  0.0663  0.0238  312 LEU A CD2 
124  N N   . THR A 17  ? 0.6929 1.6229 0.8973 -0.1878 0.0659  0.0432  313 THR A N   
125  C CA  . THR A 17  ? 0.6879 1.5304 0.8581 -0.2551 0.0581  0.0489  313 THR A CA  
126  C C   . THR A 17  ? 0.7961 1.5614 0.9676 -0.2589 0.0394  0.0427  313 THR A C   
127  O O   . THR A 17  ? 0.8202 1.6531 1.0235 -0.2545 0.0342  0.0394  313 THR A O   
128  C CB  . THR A 17  ? 0.7385 1.6445 0.8917 -0.3190 0.0622  0.0576  313 THR A CB  
129  O OG1 . THR A 17  ? 0.7218 1.7128 0.8759 -0.3041 0.0774  0.0614  313 THR A OG1 
130  C CG2 . THR A 17  ? 0.8020 1.5976 0.9008 -0.3848 0.0568  0.0646  313 THR A CG2 
131  N N   . ASP A 18  ? 0.7804 1.4099 0.9157 -0.2655 0.0296  0.0412  314 ASP A N   
132  C CA  . ASP A 18  ? 0.7531 1.3018 0.8833 -0.2659 0.0132  0.0351  314 ASP A CA  
133  C C   . ASP A 18  ? 0.8350 1.3290 0.9212 -0.3338 0.0068  0.0406  314 ASP A C   
134  O O   . ASP A 18  ? 0.9056 1.3197 0.9433 -0.3577 0.0077  0.0462  314 ASP A O   
135  C CB  . ASP A 18  ? 0.7193 1.1615 0.8370 -0.2211 0.0060  0.0293  314 ASP A CB  
136  C CG  . ASP A 18  ? 0.6772 1.0631 0.8016 -0.2065 -0.0085 0.0218  314 ASP A CG  
137  O OD1 . ASP A 18  ? 0.5934 0.9235 0.6904 -0.2420 -0.0169 0.0224  314 ASP A OD1 
138  O OD2 . ASP A 18  ? 0.6512 1.0443 0.8016 -0.1598 -0.0111 0.0154  314 ASP A OD2 
139  N N   . THR A 19  ? 0.8213 1.3547 0.9170 -0.3655 -0.0001 0.0392  315 THR A N   
140  C CA  . THR A 19  ? 0.8407 1.2975 0.8826 -0.4262 -0.0096 0.0417  315 THR A CA  
141  C C   . THR A 19  ? 0.8229 1.2016 0.8579 -0.4101 -0.0251 0.0324  315 THR A C   
142  O O   . THR A 19  ? 0.7752 1.0519 0.7510 -0.4443 -0.0342 0.0324  315 THR A O   
143  C CB  . THR A 19  ? 0.8107 1.3364 0.8370 -0.4618 -0.0070 0.0455  315 THR A CB  
144  O OG1 . THR A 19  ? 0.8249 1.4875 0.9088 -0.4280 0.0014  0.0446  315 THR A OG1 
145  C CG2 . THR A 19  ? 0.7639 1.2573 0.7310 -0.5104 -0.0010 0.0551  315 THR A CG2 
146  N N   . LEU A 20  ? 0.6953 1.1110 0.7810 -0.3551 -0.0276 0.0247  316 LEU A N   
147  C CA  . LEU A 20  ? 0.7741 1.1280 0.8575 -0.3362 -0.0404 0.0160  316 LEU A CA  
148  C C   . LEU A 20  ? 0.8464 1.0645 0.8834 -0.3222 -0.0469 0.0136  316 LEU A C   
149  O O   . LEU A 20  ? 0.9609 1.1111 0.9732 -0.3231 -0.0574 0.0078  316 LEU A O   
150  C CB  . LEU A 20  ? 0.7287 1.1423 0.8687 -0.2777 -0.0400 0.0102  316 LEU A CB  
151  C CG  . LEU A 20  ? 0.6678 1.0459 0.8152 -0.2572 -0.0512 0.0020  316 LEU A CG  
152  C CD1 . LEU A 20  ? 0.7014 1.1244 0.8461 -0.3002 -0.0579 0.0012  316 LEU A CD1 
153  C CD2 . LEU A 20  ? 0.5791 0.9952 0.7686 -0.1986 -0.0497 -0.0018 316 LEU A CD2 
154  N N   . HIS A 21  ? 0.8297 1.0110 0.8526 -0.3058 -0.0412 0.0177  317 HIS A N   
155  C CA  . HIS A 21  ? 0.7518 0.8175 0.7322 -0.2863 -0.0479 0.0161  317 HIS A CA  
156  C C   . HIS A 21  ? 0.8272 0.7959 0.7318 -0.3290 -0.0552 0.0184  317 HIS A C   
157  O O   . HIS A 21  ? 0.8862 0.7566 0.7502 -0.3067 -0.0632 0.0154  317 HIS A O   
158  C CB  . HIS A 21  ? 0.6704 0.7266 0.6491 -0.2640 -0.0408 0.0209  317 HIS A CB  
159  C CG  . HIS A 21  ? 0.7160 0.7729 0.6574 -0.3078 -0.0327 0.0310  317 HIS A CG  
160  N ND1 . HIS A 21  ? 0.7754 0.9360 0.7469 -0.3249 -0.0200 0.0361  317 HIS A ND1 
161  C CD2 . HIS A 21  ? 0.8539 0.8200 0.7248 -0.3381 -0.0353 0.0375  317 HIS A CD2 
162  C CE1 . HIS A 21  ? 0.8984 1.0378 0.8235 -0.3684 -0.0141 0.0457  317 HIS A CE1 
163  N NE2 . HIS A 21  ? 0.9423 0.9575 0.8025 -0.3786 -0.0238 0.0471  317 HIS A NE2 
164  N N   . LEU A 22  ? 0.8980 0.8907 0.7770 -0.3894 -0.0533 0.0237  318 LEU A N   
165  C CA  . LEU A 22  ? 1.1534 1.0367 0.9454 -0.4344 -0.0621 0.0252  318 LEU A CA  
166  C C   . LEU A 22  ? 1.2014 1.0356 0.9796 -0.4228 -0.0741 0.0147  318 LEU A C   
167  O O   . LEU A 22  ? 1.3044 1.0146 1.0049 -0.4271 -0.0832 0.0123  318 LEU A O   
168  C CB  . LEU A 22  ? 1.2234 1.1527 0.9891 -0.4944 -0.0558 0.0335  318 LEU A CB  
169  C CG  . LEU A 22  ? 1.2494 1.2428 1.0301 -0.5092 -0.0422 0.0438  318 LEU A CG  
170  C CD1 . LEU A 22  ? 1.3204 1.3843 1.0841 -0.5566 -0.0360 0.0501  318 LEU A CD1 
171  C CD2 . LEU A 22  ? 1.2588 1.1369 0.9766 -0.5058 -0.0428 0.0497  318 LEU A CD2 
172  N N   . LYS A 23  ? 1.0372 0.9618 0.8834 -0.4043 -0.0744 0.0084  319 LYS A N   
173  C CA  . LYS A 23  ? 1.0697 0.9538 0.9085 -0.3858 -0.0846 -0.0019 319 LYS A CA  
174  C C   . LYS A 23  ? 1.0654 0.8950 0.9122 -0.3199 -0.0870 -0.0077 319 LYS A C   
175  O O   . LYS A 23  ? 1.0492 0.8469 0.8899 -0.2985 -0.0939 -0.0162 319 LYS A O   
176  C CB  . LYS A 23  ? 0.8468 0.8463 0.7523 -0.3870 -0.0846 -0.0057 319 LYS A CB  
177  C CG  . LYS A 23  ? 0.8846 0.9544 0.7849 -0.4367 -0.0809 0.0003  319 LYS A CG  
178  C CD  . LYS A 23  ? 1.1372 1.1146 0.9529 -0.4728 -0.0874 0.0000  319 LYS A CD  
179  C CE  . LYS A 23  ? 1.2107 1.2079 1.0343 -0.4731 -0.0950 -0.0073 319 LYS A CE  
180  N NZ  . LYS A 23  ? 1.2475 1.3737 1.1155 -0.4918 -0.0901 -0.0026 319 LYS A NZ  
181  N N   . SER A 24  ? 1.0400 0.8650 0.8995 -0.2895 -0.0815 -0.0033 320 SER A N   
182  C CA  . SER A 24  ? 1.0676 0.8528 0.9344 -0.2322 -0.0846 -0.0079 320 SER A CA  
183  C C   . SER A 24  ? 1.2349 0.9029 1.0246 -0.2238 -0.0939 -0.0122 320 SER A C   
184  O O   . SER A 24  ? 1.2048 0.7886 0.9174 -0.2541 -0.0970 -0.0080 320 SER A O   
185  C CB  . SER A 24  ? 1.1218 0.9151 1.0021 -0.2103 -0.0790 -0.0017 320 SER A CB  
186  O OG  . SER A 24  ? 1.2252 0.9859 1.1087 -0.1607 -0.0836 -0.0055 320 SER A OG  
187  N N   . THR A 25  ? 1.3704 1.0306 1.1746 -0.1817 -0.0982 -0.0204 321 THR A N   
188  C CA  . THR A 25  ? 1.5741 1.1320 1.3065 -0.1620 -0.1065 -0.0264 321 THR A CA  
189  C C   . THR A 25  ? 1.4732 1.0110 1.2067 -0.1032 -0.1082 -0.0273 321 THR A C   
190  O O   . THR A 25  ? 1.3889 0.8398 1.0535 -0.0891 -0.1127 -0.0248 321 THR A O   
191  C CB  . THR A 25  ? 1.6074 1.1756 1.3461 -0.1633 -0.1101 -0.0359 321 THR A CB  
192  O OG1 . THR A 25  ? 1.6966 1.1848 1.3811 -0.1235 -0.1161 -0.0436 321 THR A OG1 
193  C CG2 . THR A 25  ? 1.4778 1.1608 1.3116 -0.1474 -0.1049 -0.0377 321 THR A CG2 
194  N N   . LEU A 26  ? 1.3899 1.0092 1.1975 -0.0707 -0.1051 -0.0299 322 LEU A N   
195  C CA  . LEU A 26  ? 1.3217 0.9444 1.1388 -0.0189 -0.1074 -0.0312 322 LEU A CA  
196  C C   . LEU A 26  ? 1.2996 0.9220 1.1166 -0.0138 -0.1067 -0.0230 322 LEU A C   
197  O O   . LEU A 26  ? 1.3358 0.9508 1.1425 -0.0488 -0.1032 -0.0163 322 LEU A O   
198  C CB  . LEU A 26  ? 1.1829 0.8947 1.0747 0.0012  -0.1043 -0.0352 322 LEU A CB  
199  C CG  . LEU A 26  ? 1.0788 0.8046 0.9798 -0.0039 -0.1041 -0.0426 322 LEU A CG  
200  C CD1 . LEU A 26  ? 0.9716 0.7888 0.9478 -0.0014 -0.0995 -0.0428 322 LEU A CD1 
201  C CD2 . LEU A 26  ? 0.9740 0.6480 0.8276 0.0333  -0.1086 -0.0500 322 LEU A CD2 
202  N N   . GLU A 27  ? 1.2270 0.8652 1.0560 0.0297  -0.1101 -0.0233 323 GLU A N   
203  C CA  . GLU A 27  ? 1.1564 0.7907 0.9791 0.0411  -0.1119 -0.0163 323 GLU A CA  
204  C C   . GLU A 27  ? 1.1201 0.8470 1.0173 0.0508  -0.1095 -0.0156 323 GLU A C   
205  O O   . GLU A 27  ? 1.1046 0.8894 1.0490 0.0585  -0.1080 -0.0204 323 GLU A O   
206  C CB  . GLU A 27  ? 1.1991 0.7664 0.9577 0.0849  -0.1207 -0.0165 323 GLU A CB  
207  C CG  . GLU A 27  ? 1.4265 0.8762 1.0894 0.0762  -0.1245 -0.0169 323 GLU A CG  
208  C CD  . GLU A 27  ? 1.6932 1.0617 1.2779 0.1213  -0.1336 -0.0145 323 GLU A CD  
209  O OE1 . GLU A 27  ? 1.6905 1.1024 1.3007 0.1516  -0.1368 -0.0106 323 GLU A OE1 
210  O OE2 . GLU A 27  ? 1.8434 1.1012 1.3352 0.1273  -0.1385 -0.0165 323 GLU A OE2 
211  N N   . THR A 28  ? 1.0234 0.7558 0.9222 0.0479  -0.1097 -0.0093 324 THR A N   
212  C CA  . THR A 28  ? 0.9340 0.7373 0.8888 0.0468  -0.1076 -0.0081 324 THR A CA  
213  C C   . THR A 28  ? 0.9355 0.7642 0.8972 0.0796  -0.1160 -0.0076 324 THR A C   
214  O O   . THR A 28  ? 0.8957 0.7871 0.9031 0.0808  -0.1165 -0.0093 324 THR A O   
215  C CB  . THR A 28  ? 0.9078 0.7073 0.8594 0.0193  -0.1015 -0.0021 324 THR A CB  
216  O OG1 . THR A 28  ? 0.9398 0.6780 0.8354 0.0241  -0.1055 0.0038  324 THR A OG1 
217  C CG2 . THR A 28  ? 0.8802 0.6828 0.8360 -0.0151 -0.0929 -0.0022 324 THR A CG2 
218  N N   . GLY A 29  ? 1.0375 0.8190 0.9502 0.1052  -0.1233 -0.0049 325 GLY A N   
219  C CA  . GLY A 29  ? 1.0506 0.8631 0.9667 0.1360  -0.1326 -0.0030 325 GLY A CA  
220  C C   . GLY A 29  ? 1.1222 0.9090 1.0137 0.1295  -0.1352 0.0041  325 GLY A C   
221  O O   . GLY A 29  ? 1.2917 1.0789 1.1619 0.1595  -0.1453 0.0070  325 GLY A O   
222  N N   . CYS A 30  ? 1.0357 0.8057 0.9285 0.0932  -0.1264 0.0070  326 CYS A N   
223  C CA  . CYS A 30  ? 0.9851 0.7226 0.8459 0.0846  -0.1266 0.0142  326 CYS A CA  
224  C C   . CYS A 30  ? 1.0559 0.7006 0.8400 0.0893  -0.1290 0.0195  326 CYS A C   
225  O O   . CYS A 30  ? 0.9835 0.5833 0.7399 0.0821  -0.1265 0.0175  326 CYS A O   
226  C CB  . CYS A 30  ? 0.7834 0.5416 0.6689 0.0473  -0.1146 0.0154  326 CYS A CB  
227  S SG  . CYS A 30  ? 0.7912 0.6317 0.7468 0.0404  -0.1113 0.0088  326 CYS A SG  
228  N N   . THR A 31  ? 1.0877 0.6967 0.8296 0.1012  -0.1350 0.0264  327 THR A N   
229  C CA  . THR A 31  ? 1.1394 0.6464 0.7950 0.0995  -0.1369 0.0338  327 THR A CA  
230  C C   . THR A 31  ? 1.2166 0.7101 0.8570 0.0643  -0.1290 0.0419  327 THR A C   
231  O O   . THR A 31  ? 1.2052 0.7664 0.8996 0.0495  -0.1230 0.0406  327 THR A O   
232  C CB  . THR A 31  ? 1.1134 0.5796 0.7167 0.1531  -0.1521 0.0360  327 THR A CB  
233  O OG1 . THR A 31  ? 1.0967 0.6112 0.7208 0.1693  -0.1592 0.0392  327 THR A OG1 
234  C CG2 . THR A 31  ? 1.1177 0.6197 0.7444 0.1922  -0.1581 0.0274  327 THR A CG2 
235  N N   . GLU A 32  ? 1.4141 0.8145 0.9731 0.0506  -0.1288 0.0505  328 GLU A N   
236  C CA  . GLU A 32  ? 1.4840 0.8727 1.0216 0.0198  -0.1213 0.0595  328 GLU A CA  
237  C C   . GLU A 32  ? 1.4860 0.9094 1.0382 0.0480  -0.1288 0.0614  328 GLU A C   
238  O O   . GLU A 32  ? 1.4011 0.8353 0.9508 0.0258  -0.1215 0.0668  328 GLU A O   
239  C CB  . GLU A 32  ? 1.6808 0.9519 1.1145 -0.0011 -0.1214 0.0699  328 GLU A CB  
240  C CG  . GLU A 32  ? 1.8448 1.0873 1.2592 -0.0529 -0.1111 0.0703  328 GLU A CG  
241  C CD  . GLU A 32  ? 2.0208 1.1740 1.3724 -0.0381 -0.1205 0.0669  328 GLU A CD  
242  O OE1 . GLU A 32  ? 2.1595 1.2132 1.4233 -0.0739 -0.1196 0.0736  328 GLU A OE1 
243  O OE2 . GLU A 32  ? 2.0051 1.1856 1.3897 0.0078  -0.1286 0.0575  328 GLU A OE2 
244  N N   . HIS A 33  ? 1.4219 0.8717 0.9906 0.0950  -0.1432 0.0568  329 HIS A N   
245  C CA  . HIS A 33  ? 1.3241 0.8043 0.8969 0.1224  -0.1543 0.0589  329 HIS A CA  
246  C C   . HIS A 33  ? 1.2190 0.8035 0.8726 0.1353  -0.1594 0.0499  329 HIS A C   
247  O O   . HIS A 33  ? 1.2576 0.8771 0.9177 0.1528  -0.1702 0.0509  329 HIS A O   
248  C CB  . HIS A 33  ? 1.5447 0.9592 1.0450 0.1698  -0.1705 0.0644  329 HIS A CB  
249  C CG  . HIS A 33  ? 1.7997 1.0904 1.2019 0.1577  -0.1678 0.0737  329 HIS A CG  
250  N ND1 . HIS A 33  ? 1.9111 1.1328 1.2703 0.1560  -0.1660 0.0720  329 HIS A ND1 
251  C CD2 . HIS A 33  ? 1.9004 1.1180 1.2318 0.1418  -0.1667 0.0852  329 HIS A CD2 
252  C CE1 . HIS A 33  ? 2.0307 1.1369 1.2925 0.1371  -0.1647 0.0822  329 HIS A CE1 
253  N NE2 . HIS A 33  ? 2.0236 1.1269 1.2678 0.1280  -0.1646 0.0909  329 HIS A NE2 
254  N N   . ILE A 34  ? 1.1423 0.7749 0.8520 0.1241  -0.1528 0.0417  330 ILE A N   
255  C CA  . ILE A 34  ? 0.9858 0.7085 0.7640 0.1274  -0.1565 0.0341  330 ILE A CA  
256  C C   . ILE A 34  ? 0.9338 0.6855 0.7593 0.0991  -0.1432 0.0278  330 ILE A C   
257  O O   . ILE A 34  ? 0.9303 0.6482 0.7441 0.0896  -0.1357 0.0274  330 ILE A O   
258  C CB  . ILE A 34  ? 1.0208 0.7843 0.8097 0.1691  -0.1713 0.0312  330 ILE A CB  
259  C CG1 . ILE A 34  ? 0.8797 0.7378 0.7298 0.1625  -0.1769 0.0257  330 ILE A CG1 
260  C CG2 . ILE A 34  ? 1.1064 0.8545 0.8952 0.1817  -0.1677 0.0269  330 ILE A CG2 
261  C CD1 . ILE A 34  ? 0.8262 0.7432 0.6824 0.2000  -0.1939 0.0257  330 ILE A CD1 
262  N N   . CYS A 35  ? 0.9276 0.7373 0.7997 0.0852  -0.1414 0.0230  331 CYS A N   
263  C CA  . CYS A 35  ? 0.7741 0.6137 0.6885 0.0643  -0.1307 0.0172  331 CYS A CA  
264  C C   . CYS A 35  ? 0.8130 0.7132 0.7691 0.0710  -0.1384 0.0114  331 CYS A C   
265  O O   . CYS A 35  ? 0.7146 0.6447 0.6745 0.0746  -0.1486 0.0112  331 CYS A O   
266  C CB  . CYS A 35  ? 0.6728 0.5126 0.5902 0.0400  -0.1192 0.0174  331 CYS A CB  
267  S SG  . CYS A 35  ? 0.7344 0.6151 0.6966 0.0247  -0.1098 0.0103  331 CYS A SG  
268  N N   . MET A 36  ? 0.9219 0.8403 0.9052 0.0692  -0.1340 0.0071  332 MET A N   
269  C CA  . MET A 36  ? 0.8814 0.8569 0.9008 0.0731  -0.1397 0.0026  332 MET A CA  
270  C C   . MET A 36  ? 0.7669 0.7592 0.8152 0.0497  -0.1311 -0.0016 332 MET A C   
271  O O   . MET A 36  ? 0.6291 0.6598 0.7037 0.0477  -0.1329 -0.0048 332 MET A O   
272  C CB  . MET A 36  ? 0.9696 0.9516 0.9882 0.0987  -0.1430 0.0014  332 MET A CB  
273  C CG  . MET A 36  ? 1.0939 1.0395 1.0689 0.1291  -0.1507 0.0056  332 MET A CG  
274  S SD  . MET A 36  ? 1.1621 1.1675 1.1452 0.1721  -0.1633 0.0039  332 MET A SD  
275  C CE  . MET A 36  ? 1.1931 1.1261 1.1048 0.2128  -0.1716 0.0097  332 MET A CE  
276  N N   . GLY A 37  ? 0.6396 0.6060 0.6799 0.0342  -0.1216 -0.0013 333 GLY A N   
277  C CA  . GLY A 37  ? 0.7338 0.7090 0.7927 0.0204  -0.1131 -0.0049 333 GLY A CA  
278  C C   . GLY A 37  ? 0.6308 0.6267 0.6979 0.0105  -0.1183 -0.0079 333 GLY A C   
279  O O   . GLY A 37  ? 0.6840 0.6750 0.7544 0.0026  -0.1122 -0.0105 333 GLY A O   
280  N N   . SER A 38  ? 0.5210 0.5382 0.5851 0.0100  -0.1305 -0.0073 334 SER A N   
281  C CA  . SER A 38  ? 0.6278 0.6678 0.6949 -0.0080 -0.1379 -0.0094 334 SER A CA  
282  C C   . SER A 38  ? 0.6010 0.6984 0.6918 -0.0062 -0.1466 -0.0086 334 SER A C   
283  O O   . SER A 38  ? 0.6388 0.7660 0.7316 -0.0279 -0.1538 -0.0091 334 SER A O   
284  C CB  . SER A 38  ? 0.6725 0.6964 0.7099 -0.0198 -0.1456 -0.0096 334 SER A CB  
285  O OG  . SER A 38  ? 0.6854 0.7388 0.7219 -0.0120 -0.1575 -0.0067 334 SER A OG  
286  N N   . ILE A 39  ? 0.5621 0.6748 0.6645 0.0185  -0.1461 -0.0073 335 ILE A N   
287  C CA  . ILE A 39  ? 0.6277 0.7988 0.7539 0.0279  -0.1504 -0.0076 335 ILE A CA  
288  C C   . ILE A 39  ? 0.6086 0.7814 0.7520 0.0165  -0.1414 -0.0102 335 ILE A C   
289  O O   . ILE A 39  ? 0.5646 0.6952 0.7047 0.0199  -0.1317 -0.0116 335 ILE A O   
290  C CB  . ILE A 39  ? 0.5800 0.7509 0.6996 0.0653  -0.1522 -0.0065 335 ILE A CB  
291  C CG1 . ILE A 39  ? 0.5282 0.6887 0.6229 0.0799  -0.1618 -0.0028 335 ILE A CG1 
292  C CG2 . ILE A 39  ? 0.5916 0.8297 0.7330 0.0823  -0.1556 -0.0076 335 ILE A CG2 
293  C CD1 . ILE A 39  ? 0.5694 0.7854 0.6703 0.0638  -0.1746 -0.0015 335 ILE A CD1 
294  N N   . MET A 40  ? 0.6243 0.8506 0.7846 0.0007  -0.1449 -0.0102 336 MET A N   
295  C CA  . MET A 40  ? 0.6388 0.8607 0.8076 -0.0160 -0.1374 -0.0115 336 MET A CA  
296  C C   . MET A 40  ? 0.7632 0.9923 0.9476 0.0075  -0.1300 -0.0137 336 MET A C   
297  O O   . MET A 40  ? 0.7394 0.9367 0.9238 0.0034  -0.1219 -0.0154 336 MET A O   
298  C CB  . MET A 40  ? 0.6013 0.8744 0.7749 -0.0474 -0.1434 -0.0095 336 MET A CB  
299  C CG  . MET A 40  ? 0.8722 1.1376 1.0467 -0.0669 -0.1365 -0.0096 336 MET A CG  
300  S SD  . MET A 40  ? 1.0860 1.2878 1.2174 -0.1073 -0.1388 -0.0084 336 MET A SD  
301  C CE  . MET A 40  ? 1.0398 1.3066 1.1660 -0.1528 -0.1497 -0.0042 336 MET A CE  
302  N N   . LEU A 41  ? 0.8726 1.1415 1.0651 0.0350  -0.1333 -0.0140 337 LEU A N   
303  C CA  . LEU A 41  ? 0.9051 1.1797 1.1034 0.0593  -0.1273 -0.0171 337 LEU A CA  
304  C C   . LEU A 41  ? 1.0433 1.3061 1.2232 0.0999  -0.1311 -0.0180 337 LEU A C   
305  O O   . LEU A 41  ? 1.1305 1.4500 1.3156 0.1268  -0.1354 -0.0183 337 LEU A O   
306  C CB  . LEU A 41  ? 0.8744 1.2239 1.0957 0.0526  -0.1262 -0.0170 337 LEU A CB  
307  C CG  . LEU A 41  ? 0.8827 1.2566 1.1127 0.0087  -0.1261 -0.0140 337 LEU A CG  
308  C CD1 . LEU A 41  ? 0.8459 1.3152 1.0969 0.0032  -0.1270 -0.0122 337 LEU A CD1 
309  C CD2 . LEU A 41  ? 0.8759 1.1940 1.0986 -0.0068 -0.1178 -0.0152 337 LEU A CD2 
310  N N   . PRO A 42  ? 1.0872 1.2768 1.2399 0.1066  -0.1295 -0.0180 338 PRO A N   
311  C CA  . PRO A 42  ? 1.1315 1.2888 1.2503 0.1429  -0.1343 -0.0177 338 PRO A CA  
312  C C   . PRO A 42  ? 1.2057 1.3305 1.3023 0.1688  -0.1299 -0.0224 338 PRO A C   
313  O O   . PRO A 42  ? 1.0794 1.2136 1.1918 0.1583  -0.1232 -0.0261 338 PRO A O   
314  C CB  . PRO A 42  ? 1.1471 1.2357 1.2407 0.1276  -0.1333 -0.0146 338 PRO A CB  
315  C CG  . PRO A 42  ? 1.1172 1.2054 1.2344 0.0889  -0.1262 -0.0147 338 PRO A CG  
316  C CD  . PRO A 42  ? 1.0759 1.2102 1.2226 0.0807  -0.1231 -0.0177 338 PRO A CD  
317  N N   . SER A 43  ? 1.2673 1.3450 1.3182 0.2042  -0.1347 -0.0224 339 SER A N   
318  C CA  . SER A 43  ? 1.3493 1.3701 1.3577 0.2310  -0.1323 -0.0275 339 SER A CA  
319  C C   . SER A 43  ? 1.4452 1.3611 1.3875 0.2380  -0.1355 -0.0252 339 SER A C   
320  O O   . SER A 43  ? 1.5330 1.4005 1.4192 0.2801  -0.1405 -0.0269 339 SER A O   
321  C CB  . SER A 43  ? 1.3274 1.4017 1.3316 0.2816  -0.1358 -0.0310 339 SER A CB  
322  O OG  . SER A 43  ? 1.2576 1.3877 1.2969 0.2747  -0.1286 -0.0356 339 SER A OG  
323  N N   . VAL A 52  ? 1.8859 1.7226 1.5025 0.5453  -0.0816 -0.1215 348 VAL A N   
324  C CA  . VAL A 52  ? 1.9406 1.6881 1.5122 0.5290  -0.0819 -0.1312 348 VAL A CA  
325  C C   . VAL A 52  ? 2.0462 1.6539 1.5611 0.4933  -0.0929 -0.1320 348 VAL A C   
326  O O   . VAL A 52  ? 2.1750 1.7437 1.6655 0.4953  -0.0995 -0.1249 348 VAL A O   
327  C CB  . VAL A 52  ? 1.9140 1.6303 1.4099 0.5739  -0.0796 -0.1371 348 VAL A CB  
328  C CG1 . VAL A 52  ? 2.0047 1.5914 1.3882 0.5989  -0.0903 -0.1361 348 VAL A CG1 
329  C CG2 . VAL A 52  ? 1.8274 1.5144 1.3129 0.5556  -0.0754 -0.1471 348 VAL A CG2 
330  N N   . ALA A 53  ? 1.9407 1.4785 1.4341 0.4554  -0.0949 -0.1402 349 ALA A N   
331  C CA  . ALA A 53  ? 1.8394 1.2525 1.2768 0.4073  -0.1051 -0.1403 349 ALA A CA  
332  C C   . ALA A 53  ? 1.9154 1.2210 1.2583 0.3979  -0.1092 -0.1471 349 ALA A C   
333  O O   . ALA A 53  ? 1.9345 1.2572 1.2882 0.3883  -0.1055 -0.1566 349 ALA A O   
334  C CB  . ALA A 53  ? 1.6157 1.0806 1.1357 0.3381  -0.1053 -0.1346 349 ALA A CB  
335  N N   . THR A 54  ? 1.9064 1.1006 1.1535 0.3986  -0.1174 -0.1415 350 THR A N   
336  C CA  . THR A 54  ? 1.9286 1.0168 1.0727 0.3989  -0.1224 -0.1448 350 THR A CA  
337  C C   . THR A 54  ? 1.9884 0.9987 1.1032 0.3226  -0.1293 -0.1463 350 THR A C   
338  O O   . THR A 54  ? 1.9476 0.9824 1.1164 0.2695  -0.1309 -0.1444 350 THR A O   
339  C CB  . THR A 54  ? 1.9645 0.9658 1.0081 0.4362  -0.1292 -0.1371 350 THR A CB  
340  O OG1 . THR A 54  ? 2.0548 0.9706 1.0565 0.3866  -0.1373 -0.1287 350 THR A OG1 
341  C CG2 . THR A 54  ? 1.8495 0.9426 0.9316 0.5005  -0.1244 -0.1337 350 THR A CG2 
342  N N   . LYS A 55  ? 2.1230 1.0419 1.1478 0.3162  -0.1343 -0.1487 351 LYS A N   
343  C CA  . LYS A 55  ? 2.2027 1.0679 1.2038 0.2420  -0.1406 -0.1502 351 LYS A CA  
344  C C   . LYS A 55  ? 2.2382 1.0131 1.1763 0.1905  -0.1494 -0.1382 351 LYS A C   
345  O O   . LYS A 55  ? 2.1451 0.9103 1.0902 0.1179  -0.1537 -0.1363 351 LYS A O   
346  C CB  . LYS A 55  ? 2.2773 1.0884 1.2113 0.2511  -0.1424 -0.1575 351 LYS A CB  
347  C CG  . LYS A 55  ? 2.4044 1.1409 1.2396 0.3169  -0.1439 -0.1551 351 LYS A CG  
348  C CD  . LYS A 55  ? 2.4912 1.1676 1.2584 0.3174  -0.1465 -0.1622 351 LYS A CD  
349  C CE  . LYS A 55  ? 2.5993 1.2412 1.2932 0.3999  -0.1450 -0.1629 351 LYS A CE  
350  N NZ  . LYS A 55  ? 2.7740 1.2622 1.3228 0.3969  -0.1560 -0.1585 351 LYS A NZ  
351  N N   . ASP A 56  ? 2.3693 1.0866 1.2457 0.2253  -0.1520 -0.1295 352 ASP A N   
352  C CA  . ASP A 56  ? 2.4668 1.1058 1.2853 0.1764  -0.1589 -0.1173 352 ASP A CA  
353  C C   . ASP A 56  ? 2.2512 0.9691 1.1668 0.1256  -0.1560 -0.1134 352 ASP A C   
354  O O   . ASP A 56  ? 2.2693 0.9696 1.1792 0.0527  -0.1595 -0.1074 352 ASP A O   
355  C CB  . ASP A 56  ? 2.6635 1.2354 1.4009 0.2314  -0.1623 -0.1101 352 ASP A CB  
356  C CG  . ASP A 56  ? 2.8420 1.3529 1.4898 0.2962  -0.1648 -0.1146 352 ASP A CG  
357  O OD1 . ASP A 56  ? 2.9788 1.3781 1.5201 0.2751  -0.1720 -0.1126 352 ASP A OD1 
358  O OD2 . ASP A 56  ? 2.8318 1.4116 1.5154 0.3675  -0.1594 -0.1194 352 ASP A OD2 
359  N N   . GLN A 57  ? 2.0655 0.8788 1.0718 0.1636  -0.1495 -0.1162 353 GLN A N   
360  C CA  . GLN A 57  ? 1.9592 0.8458 1.0550 0.1246  -0.1471 -0.1124 353 GLN A CA  
361  C C   . GLN A 57  ? 1.8411 0.7956 1.0097 0.0721  -0.1463 -0.1192 353 GLN A C   
362  O O   . GLN A 57  ? 1.6996 0.7032 0.9267 0.0242  -0.1466 -0.1144 353 GLN A O   
363  C CB  . GLN A 57  ? 1.9131 0.8804 1.0786 0.1841  -0.1415 -0.1132 353 GLN A CB  
364  C CG  . GLN A 57  ? 2.0930 1.0365 1.2035 0.2610  -0.1409 -0.1131 353 GLN A CG  
365  C CD  . GLN A 57  ? 2.0815 1.1419 1.2742 0.3205  -0.1330 -0.1191 353 GLN A CD  
366  O OE1 . GLN A 57  ? 1.9668 1.1133 1.2486 0.3062  -0.1279 -0.1248 353 GLN A OE1 
367  N NE2 . GLN A 57  ? 2.1783 1.2479 1.3385 0.3861  -0.1322 -0.1175 353 GLN A NE2 
368  N N   . LEU A 58  ? 1.8401 0.8010 1.0029 0.0808  -0.1460 -0.1298 354 LEU A N   
369  C CA  . LEU A 58  ? 1.7390 0.7811 0.9782 0.0463  -0.1458 -0.1383 354 LEU A CA  
370  C C   . LEU A 58  ? 1.8261 0.8594 1.0552 -0.0366 -0.1523 -0.1331 354 LEU A C   
371  O O   . LEU A 58  ? 1.6858 0.8036 0.9907 -0.0768 -0.1538 -0.1341 354 LEU A O   
372  C CB  . LEU A 58  ? 1.7358 0.7962 0.9731 0.0900  -0.1423 -0.1516 354 LEU A CB  
373  C CG  . LEU A 58  ? 1.5615 0.7542 0.9089 0.0951  -0.1357 -0.1549 354 LEU A CG  
374  C CD1 . LEU A 58  ? 1.4608 0.7500 0.8904 0.1412  -0.1255 -0.1462 354 LEU A CD1 
375  C CD2 . LEU A 58  ? 1.5818 0.7767 0.9082 0.1196  -0.1334 -0.1673 354 LEU A CD2 
376  N N   . PHE A 59  ? 1.9622 0.9028 1.0987 -0.0628 -0.1567 -0.1262 355 PHE A N   
377  C CA  . PHE A 59  ? 2.0399 0.9913 1.1727 -0.1420 -0.1618 -0.1201 355 PHE A CA  
378  C C   . PHE A 59  ? 2.0210 1.0157 1.1929 -0.1919 -0.1607 -0.1071 355 PHE A C   
379  O O   . PHE A 59  ? 2.0384 1.1138 1.2661 -0.2468 -0.1619 -0.1038 355 PHE A O   
380  C CB  . PHE A 59  ? 2.2462 1.0866 1.2635 -0.1618 -0.1676 -0.1161 355 PHE A CB  
381  C CG  . PHE A 59  ? 2.3612 1.2253 1.3766 -0.2429 -0.1726 -0.1096 355 PHE A CG  
382  C CD1 . PHE A 59  ? 2.3352 1.2750 1.4043 -0.2668 -0.1749 -0.1173 355 PHE A CD1 
383  C CD2 . PHE A 59  ? 2.4830 1.3026 1.4433 -0.2946 -0.1748 -0.0951 355 PHE A CD2 
384  C CE1 . PHE A 59  ? 2.3461 1.3237 1.4184 -0.3377 -0.1795 -0.1102 355 PHE A CE1 
385  C CE2 . PHE A 59  ? 2.5129 1.3689 1.4736 -0.3684 -0.1783 -0.0881 355 PHE A CE2 
386  C CZ  . PHE A 59  ? 2.4485 1.3876 1.4681 -0.3885 -0.1807 -0.0955 355 PHE A CZ  
387  N N   . PRO A 60  ? 2.0135 0.9633 1.1563 -0.1745 -0.1585 -0.0986 356 PRO A N   
388  C CA  . PRO A 60  ? 1.8372 0.8445 1.0304 -0.2170 -0.1556 -0.0873 356 PRO A CA  
389  C C   . PRO A 60  ? 1.6144 0.7505 0.9279 -0.2242 -0.1527 -0.0913 356 PRO A C   
390  O O   . PRO A 60  ? 1.5465 0.7622 0.9097 -0.2786 -0.1521 -0.0846 356 PRO A O   
391  C CB  . PRO A 60  ? 1.8860 0.8298 1.0379 -0.1739 -0.1537 -0.0817 356 PRO A CB  
392  C CG  . PRO A 60  ? 2.0902 0.9178 1.1314 -0.1391 -0.1580 -0.0836 356 PRO A CG  
393  C CD  . PRO A 60  ? 2.1404 0.9830 1.1916 -0.1215 -0.1593 -0.0967 356 PRO A CD  
394  N N   . LEU A 61  ? 1.5185 0.6814 0.8764 -0.1677 -0.1513 -0.1016 357 LEU A N   
395  C CA  . LEU A 61  ? 1.3726 0.6658 0.8465 -0.1654 -0.1470 -0.1006 357 LEU A CA  
396  C C   . LEU A 61  ? 1.3663 0.7334 0.8823 -0.2018 -0.1500 -0.1039 357 LEU A C   
397  O O   . LEU A 61  ? 1.2184 0.6902 0.8106 -0.2332 -0.1476 -0.0959 357 LEU A O   
398  C CB  . LEU A 61  ? 1.3202 0.6540 0.8408 -0.0908 -0.1390 -0.1030 357 LEU A CB  
399  C CG  . LEU A 61  ? 1.4125 0.6824 0.8911 -0.0449 -0.1375 -0.1006 357 LEU A CG  
400  C CD1 . LEU A 61  ? 1.3249 0.6408 0.8401 0.0268  -0.1311 -0.1045 357 LEU A CD1 
401  C CD2 . LEU A 61  ? 1.4098 0.7172 0.9288 -0.0677 -0.1345 -0.0876 357 LEU A CD2 
402  N N   . ALA A 62  ? 1.3389 0.6531 0.8021 -0.1938 -0.1556 -0.1157 358 ALA A N   
403  C CA  . ALA A 62  ? 1.2332 0.6067 0.7228 -0.2300 -0.1608 -0.1194 358 ALA A CA  
404  C C   . ALA A 62  ? 1.3802 0.7882 0.8711 -0.2978 -0.1626 -0.1078 358 ALA A C   
405  O O   . ALA A 62  ? 1.3367 0.8539 0.8970 -0.3267 -0.1638 -0.1041 358 ALA A O   
406  C CB  . ALA A 62  ? 1.4196 0.7151 0.8360 -0.2105 -0.1650 -0.1321 358 ALA A CB  
407  N N   . LYS A 63  ? 1.4877 0.8115 0.9020 -0.3182 -0.1613 -0.0998 359 LYS A N   
408  C CA  . LYS A 63  ? 1.5014 0.8549 0.9057 -0.3813 -0.1611 -0.0869 359 LYS A CA  
409  C C   . LYS A 63  ? 1.4951 0.9620 0.9858 -0.4008 -0.1553 -0.0772 359 LYS A C   
410  O O   . LYS A 63  ? 1.5159 1.0861 1.0582 -0.4358 -0.1547 -0.0716 359 LYS A O   
411  C CB  . LYS A 63  ? 1.4429 0.6727 0.7382 -0.3952 -0.1615 -0.0792 359 LYS A CB  
412  C CG  . LYS A 63  ? 1.5992 0.8484 0.8666 -0.4643 -0.1617 -0.0658 359 LYS A CG  
413  C CD  . LYS A 63  ? 1.7877 0.9016 0.9338 -0.4774 -0.1635 -0.0578 359 LYS A CD  
414  C CE  . LYS A 63  ? 1.9192 1.0250 1.0061 -0.5491 -0.1668 -0.0474 359 LYS A CE  
415  N NZ  . LYS A 63  ? 1.8575 1.1039 1.0266 -0.5949 -0.1614 -0.0386 359 LYS A NZ  
416  N N   . GLU A 64  ? 1.4075 0.8584 0.9122 -0.3744 -0.1506 -0.0746 360 GLU A N   
417  C CA  . GLU A 64  ? 1.3576 0.9095 0.9385 -0.3889 -0.1442 -0.0652 360 GLU A CA  
418  C C   . GLU A 64  ? 1.2574 0.9379 0.9372 -0.3799 -0.1446 -0.0684 360 GLU A C   
419  O O   . GLU A 64  ? 1.1597 0.9476 0.8957 -0.4043 -0.1401 -0.0598 360 GLU A O   
420  C CB  . GLU A 64  ? 1.4169 0.9189 0.9911 -0.3558 -0.1406 -0.0636 360 GLU A CB  
421  C CG  . GLU A 64  ? 1.3968 0.9962 1.0524 -0.3577 -0.1343 -0.0562 360 GLU A CG  
422  C CD  . GLU A 64  ? 1.4943 1.0611 1.1615 -0.3021 -0.1300 -0.0561 360 GLU A CD  
423  O OE1 . GLU A 64  ? 1.5495 1.0076 1.1474 -0.2717 -0.1337 -0.0616 360 GLU A OE1 
424  O OE2 . GLU A 64  ? 1.4193 1.0747 1.1641 -0.2818 -0.1216 -0.0495 360 GLU A OE2 
425  N N   . PHE A 65  ? 1.1851 0.8577 0.8816 -0.3419 -0.1498 -0.0802 361 PHE A N   
426  C CA  . PHE A 65  ? 0.9959 0.7909 0.7831 -0.3224 -0.1471 -0.0789 361 PHE A CA  
427  C C   . PHE A 65  ? 0.9894 0.8434 0.7815 -0.3633 -0.1535 -0.0790 361 PHE A C   
428  O O   . PHE A 65  ? 0.9534 0.9233 0.8125 -0.3692 -0.1502 -0.0716 361 PHE A O   
429  C CB  . PHE A 65  ? 0.8912 0.6746 0.6971 -0.2614 -0.1434 -0.0855 361 PHE A CB  
430  C CG  . PHE A 65  ? 0.7463 0.6316 0.6225 -0.2463 -0.1427 -0.0847 361 PHE A CG  
431  C CD1 . PHE A 65  ? 0.8083 0.7825 0.7606 -0.2235 -0.1351 -0.0762 361 PHE A CD1 
432  C CD2 . PHE A 65  ? 0.9230 0.8071 0.7802 -0.2542 -0.1505 -0.0925 361 PHE A CD2 
433  C CE1 . PHE A 65  ? 0.8007 0.8537 0.8038 -0.2071 -0.1354 -0.0748 361 PHE A CE1 
434  C CE2 . PHE A 65  ? 0.7770 0.7490 0.6919 -0.2385 -0.1507 -0.0907 361 PHE A CE2 
435  C CZ  . PHE A 65  ? 0.7064 0.7598 0.6921 -0.2140 -0.1432 -0.0815 361 PHE A CZ  
436  N N   . LEU A 66  ? 1.0095 0.7884 0.7320 -0.3787 -0.1590 -0.0850 362 LEU A N   
437  C CA  . LEU A 66  ? 1.0355 0.8711 0.7626 -0.4096 -0.1628 -0.0830 362 LEU A CA  
438  C C   . LEU A 66  ? 1.1614 1.0628 0.9008 -0.4525 -0.1574 -0.0691 362 LEU A C   
439  O O   . LEU A 66  ? 1.1233 1.1210 0.9000 -0.4694 -0.1584 -0.0647 362 LEU A O   
440  C CB  . LEU A 66  ? 1.2079 0.9376 0.8469 -0.4203 -0.1697 -0.0914 362 LEU A CB  
441  C CG  . LEU A 66  ? 1.1924 0.8813 0.8181 -0.3819 -0.1756 -0.1064 362 LEU A CG  
442  C CD1 . LEU A 66  ? 1.2954 0.9090 0.8421 -0.4013 -0.1817 -0.1119 362 LEU A CD1 
443  C CD2 . LEU A 66  ? 0.9984 0.8036 0.7104 -0.3625 -0.1780 -0.1079 362 LEU A CD2 
444  N N   . ASP A 67  ? 1.3304 1.1831 1.0351 -0.4686 -0.1516 -0.0619 363 ASP A N   
445  C CA  . ASP A 67  ? 1.3167 1.2308 1.0245 -0.5119 -0.1458 -0.0487 363 ASP A CA  
446  C C   . ASP A 67  ? 1.0764 1.1261 0.8786 -0.4946 -0.1381 -0.0424 363 ASP A C   
447  O O   . ASP A 67  ? 0.9817 1.1302 0.8114 -0.5176 -0.1350 -0.0347 363 ASP A O   
448  C CB  . ASP A 67  ? 1.4160 1.2288 1.0477 -0.5344 -0.1425 -0.0424 363 ASP A CB  
449  C CG  . ASP A 67  ? 1.6633 1.3656 1.1892 -0.5692 -0.1492 -0.0426 363 ASP A CG  
450  O OD1 . ASP A 67  ? 1.7838 1.5153 1.2802 -0.6215 -0.1492 -0.0336 363 ASP A OD1 
451  O OD2 . ASP A 67  ? 1.7616 1.3489 1.2294 -0.5431 -0.1544 -0.0515 363 ASP A OD2 
452  N N   . GLN A 68  ? 1.0041 1.0607 0.8521 -0.4518 -0.1350 -0.0453 364 GLN A N   
453  C CA  . GLN A 68  ? 0.9838 1.1604 0.9134 -0.4296 -0.1275 -0.0392 364 GLN A CA  
454  C C   . GLN A 68  ? 0.9685 1.2331 0.9519 -0.4045 -0.1313 -0.0421 364 GLN A C   
455  O O   . GLN A 68  ? 0.9304 1.3020 0.9632 -0.3946 -0.1257 -0.0353 364 GLN A O   
456  C CB  . GLN A 68  ? 0.8558 1.0097 0.8115 -0.3950 -0.1232 -0.0400 364 GLN A CB  
457  C CG  . GLN A 68  ? 0.9334 1.0269 0.8883 -0.3595 -0.1306 -0.0509 364 GLN A CG  
458  C CD  . GLN A 68  ? 0.9294 0.9869 0.8976 -0.3219 -0.1238 -0.0493 364 GLN A CD  
459  O OE1 . GLN A 68  ? 0.9314 1.0411 0.9567 -0.2767 -0.1175 -0.0473 364 GLN A OE1 
460  N NE2 . GLN A 68  ? 0.8963 0.8558 0.8050 -0.3329 -0.1233 -0.0489 364 GLN A NE2 
461  N N   . TYR A 69  ? 1.0325 1.2513 1.0001 -0.3919 -0.1406 -0.0519 365 TYR A N   
462  C CA  . TYR A 69  ? 0.8907 1.1862 0.9005 -0.3698 -0.1452 -0.0538 365 TYR A CA  
463  C C   . TYR A 69  ? 0.8882 1.2435 0.8887 -0.4038 -0.1470 -0.0489 365 TYR A C   
464  O O   . TYR A 69  ? 0.8180 1.2735 0.8644 -0.3863 -0.1460 -0.0446 365 TYR A O   
465  C CB  . TYR A 69  ? 0.8827 1.1137 0.8720 -0.3508 -0.1547 -0.0657 365 TYR A CB  
466  C CG  . TYR A 69  ? 0.8542 1.1479 0.8670 -0.3388 -0.1613 -0.0674 365 TYR A CG  
467  C CD1 . TYR A 69  ? 0.7884 1.1781 0.8627 -0.3032 -0.1583 -0.0613 365 TYR A CD1 
468  C CD2 . TYR A 69  ? 0.9154 1.1648 0.8811 -0.3606 -0.1705 -0.0748 365 TYR A CD2 
469  C CE1 . TYR A 69  ? 0.8163 1.2567 0.9052 -0.2895 -0.1648 -0.0618 365 TYR A CE1 
470  C CE2 . TYR A 69  ? 1.0003 1.3067 0.9853 -0.3501 -0.1772 -0.0760 365 TYR A CE2 
471  C CZ  . TYR A 69  ? 0.9420 1.3444 0.9891 -0.3145 -0.1746 -0.0691 365 TYR A CZ  
472  O OH  . TYR A 69  ? 0.9684 1.4212 1.0281 -0.3012 -0.1818 -0.0694 365 TYR A OH  
473  N N   . TYR A 70  ? 1.0257 1.3181 0.9611 -0.4514 -0.1500 -0.0490 366 TYR A N   
474  C CA  . TYR A 70  ? 1.1359 1.4899 1.0595 -0.4897 -0.1521 -0.0434 366 TYR A CA  
475  C C   . TYR A 70  ? 1.1788 1.6239 1.1273 -0.5068 -0.1418 -0.0314 366 TYR A C   
476  O O   . TYR A 70  ? 1.2356 1.7855 1.2107 -0.5139 -0.1410 -0.0260 366 TYR A O   
477  C CB  . TYR A 70  ? 1.2630 1.5156 1.1000 -0.5368 -0.1591 -0.0467 366 TYR A CB  
478  C CG  . TYR A 70  ? 1.2274 1.4354 1.0462 -0.5228 -0.1701 -0.0581 366 TYR A CG  
479  C CD1 . TYR A 70  ? 1.2175 1.3172 1.0037 -0.4965 -0.1737 -0.0693 366 TYR A CD1 
480  C CD2 . TYR A 70  ? 1.2234 1.5024 1.0571 -0.5328 -0.1767 -0.0581 366 TYR A CD2 
481  C CE1 . TYR A 70  ? 1.1988 1.2607 0.9652 -0.4817 -0.1829 -0.0806 366 TYR A CE1 
482  C CE2 . TYR A 70  ? 1.2189 1.4577 1.0343 -0.5193 -0.1870 -0.0688 366 TYR A CE2 
483  C CZ  . TYR A 70  ? 1.2013 1.3314 0.9823 -0.4941 -0.1897 -0.0802 366 TYR A CZ  
484  O OH  . TYR A 70  ? 1.2027 1.2943 0.9612 -0.4793 -0.1988 -0.0916 366 TYR A OH  
485  N N   . SER A 71  ? 1.1721 1.5819 1.1104 -0.5114 -0.1339 -0.0273 367 SER A N   
486  C CA  . SER A 71  ? 1.1402 1.6439 1.1104 -0.5159 -0.1230 -0.0171 367 SER A CA  
487  C C   . SER A 71  ? 1.0229 1.6363 1.0689 -0.4630 -0.1193 -0.0165 367 SER A C   
488  O O   . SER A 71  ? 1.0468 1.7687 1.1171 -0.4654 -0.1143 -0.0098 367 SER A O   
489  C CB  . SER A 71  ? 1.1496 1.5909 1.1021 -0.5181 -0.1158 -0.0143 367 SER A CB  
490  O OG  . SER A 71  ? 1.1810 1.6993 1.1441 -0.5368 -0.1057 -0.0042 367 SER A OG  
491  N N   . SER A 72  ? 0.9250 1.5087 1.0010 -0.4140 -0.1223 -0.0234 368 SER A N   
492  C CA  . SER A 72  ? 0.8499 1.5156 0.9853 -0.3589 -0.1186 -0.0219 368 SER A CA  
493  C C   . SER A 72  ? 0.9192 1.6739 1.0709 -0.3528 -0.1226 -0.0202 368 SER A C   
494  O O   . SER A 72  ? 0.9712 1.8209 1.1549 -0.3264 -0.1161 -0.0147 368 SER A O   
495  C CB  . SER A 72  ? 0.7915 1.3975 0.9433 -0.3154 -0.1227 -0.0290 368 SER A CB  
496  O OG  . SER A 72  ? 0.7939 1.4439 0.9729 -0.2773 -0.1277 -0.0307 368 SER A OG  
497  N N   . ILE A 73  ? 0.8896 1.6147 1.0153 -0.3749 -0.1333 -0.0252 369 ILE A N   
498  C CA  . ILE A 73  ? 0.9171 1.7242 1.0582 -0.3665 -0.1385 -0.0240 369 ILE A CA  
499  C C   . ILE A 73  ? 0.9911 1.8722 1.1148 -0.4153 -0.1359 -0.0168 369 ILE A C   
500  O O   . ILE A 73  ? 1.0439 1.9884 1.1685 -0.4245 -0.1416 -0.0158 369 ILE A O   
501  C CB  . ILE A 73  ? 1.0169 1.7664 1.1386 -0.3666 -0.1517 -0.0325 369 ILE A CB  
502  C CG1 . ILE A 73  ? 1.0671 1.7206 1.1279 -0.4214 -0.1574 -0.0374 369 ILE A CG1 
503  C CG2 . ILE A 73  ? 0.9955 1.6970 1.1384 -0.3145 -0.1538 -0.0381 369 ILE A CG2 
504  C CD1 . ILE A 73  ? 1.0923 1.6715 1.1273 -0.4157 -0.1694 -0.0480 369 ILE A CD1 
505  N N   . LYS A 74  ? 1.0735 1.9508 1.1797 -0.4477 -0.1274 -0.0113 370 LYS A N   
506  C CA  . LYS A 74  ? 1.1977 2.1479 1.2831 -0.4980 -0.1231 -0.0029 370 LYS A CA  
507  C C   . LYS A 74  ? 1.3156 2.2222 1.3436 -0.5615 -0.1323 -0.0034 370 LYS A C   
508  O O   . LYS A 74  ? 1.4462 2.4184 1.4514 -0.6096 -0.1306 0.0040  370 LYS A O   
509  C CB  . LYS A 74  ? 1.2053 2.3018 1.3321 -0.4704 -0.1185 0.0025  370 LYS A CB  
510  C CG  . LYS A 74  ? 1.1615 2.2947 1.3366 -0.3993 -0.1104 0.0024  370 LYS A CG  
511  C CD  . LYS A 74  ? 1.1538 2.3850 1.3416 -0.3965 -0.0981 0.0102  370 LYS A CD  
512  C CE  . LYS A 74  ? 1.1426 2.3492 1.3562 -0.3442 -0.0892 0.0093  370 LYS A CE  
513  N NZ  . LYS A 74  ? 1.1073 2.3668 1.3548 -0.2703 -0.0871 0.0080  370 LYS A NZ  
514  N N   . ARG A 75  ? 1.2044 2.0016 1.2029 -0.5637 -0.1421 -0.0121 371 ARG A N   
515  C CA  . ARG A 75  ? 1.1507 1.8783 1.0802 -0.6229 -0.1508 -0.0134 371 ARG A CA  
516  C C   . ARG A 75  ? 1.2887 1.8694 1.1570 -0.6439 -0.1511 -0.0166 371 ARG A C   
517  O O   . ARG A 75  ? 1.2371 1.7121 1.0668 -0.6420 -0.1597 -0.0256 371 ARG A O   
518  C CB  . ARG A 75  ? 1.0725 1.7915 1.0039 -0.6094 -0.1630 -0.0215 371 ARG A CB  
519  C CG  . ARG A 75  ? 1.0821 1.9396 1.0696 -0.5819 -0.1635 -0.0182 371 ARG A CG  
520  C CD  . ARG A 75  ? 1.0517 1.9080 1.0873 -0.5120 -0.1665 -0.0251 371 ARG A CD  
521  N NE  . ARG A 75  ? 1.0345 1.9080 1.0688 -0.5067 -0.1786 -0.0300 371 ARG A NE  
522  C CZ  . ARG A 75  ? 1.1086 1.8885 1.0983 -0.5273 -0.1894 -0.0385 371 ARG A CZ  
523  N NH1 . ARG A 75  ? 1.1080 1.9120 1.0983 -0.5207 -0.2005 -0.0428 371 ARG A NH1 
524  N NH2 . ARG A 75  ? 1.1155 1.7751 1.0548 -0.5521 -0.1892 -0.0432 371 ARG A NH2 
525  N N   . PHE A 76  ? 1.3658 1.9404 1.2218 -0.6607 -0.1417 -0.0094 372 PHE A N   
526  C CA  . PHE A 76  ? 1.4534 1.8929 1.2435 -0.6824 -0.1410 -0.0100 372 PHE A CA  
527  C C   . PHE A 76  ? 1.6153 1.9787 1.3120 -0.7474 -0.1483 -0.0075 372 PHE A C   
528  O O   . PHE A 76  ? 1.6895 2.1189 1.3642 -0.7984 -0.1470 0.0018  372 PHE A O   
529  C CB  . PHE A 76  ? 1.4966 1.9686 1.2993 -0.6861 -0.1292 -0.0015 372 PHE A CB  
530  C CG  . PHE A 76  ? 1.5116 1.8496 1.2577 -0.6930 -0.1275 -0.0019 372 PHE A CG  
531  C CD1 . PHE A 76  ? 1.5420 1.7357 1.2104 -0.7067 -0.1358 -0.0075 372 PHE A CD1 
532  C CD2 . PHE A 76  ? 1.5661 1.9236 1.3324 -0.6830 -0.1174 0.0036  372 PHE A CD2 
533  C CE1 . PHE A 76  ? 1.5871 1.6588 1.1983 -0.7068 -0.1342 -0.0073 372 PHE A CE1 
534  C CE2 . PHE A 76  ? 1.6033 1.8413 1.3164 -0.6874 -0.1161 0.0040  372 PHE A CE2 
535  C CZ  . PHE A 76  ? 1.6508 1.7453 1.2852 -0.6978 -0.1247 -0.0013 372 PHE A CZ  
536  N N   . GLY A 77  ? 1.6913 1.9158 1.3276 -0.7453 -0.1561 -0.0157 373 GLY A N   
537  C CA  . GLY A 77  ? 1.8489 1.9702 1.3791 -0.8025 -0.1628 -0.0132 373 GLY A CA  
538  C C   . GLY A 77  ? 1.9039 2.0647 1.4151 -0.8379 -0.1717 -0.0134 373 GLY A C   
539  O O   . GLY A 77  ? 1.9968 2.0754 1.4135 -0.8920 -0.1776 -0.0098 373 GLY A O   
540  N N   . SER A 78  ? 1.7704 2.0488 1.3621 -0.8091 -0.1734 -0.0170 374 SER A N   
541  C CA  . SER A 78  ? 1.7392 2.0606 1.3175 -0.8386 -0.1827 -0.0177 374 SER A CA  
542  C C   . SER A 78  ? 1.7506 1.9329 1.2596 -0.8387 -0.1938 -0.0285 374 SER A C   
543  O O   . SER A 78  ? 1.7833 1.8386 1.2522 -0.8146 -0.1934 -0.0350 374 SER A O   
544  C CB  . SER A 78  ? 1.6363 2.1040 1.3143 -0.7950 -0.1825 -0.0198 374 SER A CB  
545  O OG  . SER A 78  ? 1.5430 1.9925 1.2767 -0.7253 -0.1808 -0.0288 374 SER A OG  
546  N N   . LYS A 79  ? 1.6507 1.8571 1.1419 -0.8642 -0.2036 -0.0307 375 LYS A N   
547  C CA  . LYS A 79  ? 1.6534 1.7347 1.0786 -0.8614 -0.2144 -0.0420 375 LYS A CA  
548  C C   . LYS A 79  ? 1.5461 1.5923 1.0169 -0.7871 -0.2152 -0.0562 375 LYS A C   
549  O O   . LYS A 79  ? 1.4901 1.4009 0.8989 -0.7700 -0.2189 -0.0660 375 LYS A O   
550  C CB  . LYS A 79  ? 1.6675 1.8041 1.0806 -0.8975 -0.2249 -0.0421 375 LYS A CB  
551  C CG  . LYS A 79  ? 1.6636 1.6695 0.9983 -0.9001 -0.2365 -0.0536 375 LYS A CG  
552  C CD  . LYS A 79  ? 1.9362 1.8475 1.1516 -0.9751 -0.2416 -0.0461 375 LYS A CD  
553  C CE  . LYS A 79  ? 1.9278 1.6924 1.0536 -0.9727 -0.2524 -0.0576 375 LYS A CE  
554  N NZ  . LYS A 79  ? 1.9630 1.5904 1.0547 -0.9178 -0.2488 -0.0676 375 LYS A NZ  
555  N N   . ALA A 80  ? 1.4880 1.6536 1.0608 -0.7411 -0.2115 -0.0571 376 ALA A N   
556  C CA  . ALA A 80  ? 1.4961 1.6351 1.1101 -0.6747 -0.2119 -0.0689 376 ALA A CA  
557  C C   . ALA A 80  ? 1.5286 1.5605 1.1136 -0.6534 -0.2050 -0.0717 376 ALA A C   
558  O O   . ALA A 80  ? 1.5684 1.4911 1.1106 -0.6268 -0.2084 -0.0832 376 ALA A O   
559  C CB  . ALA A 80  ? 1.4537 1.7356 1.1724 -0.6324 -0.2084 -0.0659 376 ALA A CB  
560  N N   . HIS A 81  ? 1.4966 1.5589 1.0999 -0.6636 -0.1951 -0.0613 377 HIS A N   
561  C CA  . HIS A 81  ? 1.4803 1.4457 1.0560 -0.6439 -0.1889 -0.0627 377 HIS A CA  
562  C C   . HIS A 81  ? 1.4820 1.2860 0.9429 -0.6655 -0.1935 -0.0665 377 HIS A C   
563  O O   . HIS A 81  ? 1.4486 1.1505 0.8781 -0.6269 -0.1936 -0.0757 377 HIS A O   
564  C CB  . HIS A 81  ? 1.5118 1.5351 1.1134 -0.6616 -0.1783 -0.0497 377 HIS A CB  
565  C CG  . HIS A 81  ? 1.5989 1.5289 1.1733 -0.6423 -0.1723 -0.0500 377 HIS A CG  
566  N ND1 . HIS A 81  ? 1.6161 1.4540 1.1764 -0.5961 -0.1744 -0.0615 377 HIS A ND1 
567  C CD2 . HIS A 81  ? 1.6334 1.5509 1.1899 -0.6620 -0.1645 -0.0401 377 HIS A CD2 
568  C CE1 . HIS A 81  ? 1.6254 1.3988 1.1619 -0.5864 -0.1683 -0.0585 377 HIS A CE1 
569  N NE2 . HIS A 81  ? 1.6366 1.4536 1.1697 -0.6265 -0.1625 -0.0455 377 HIS A NE2 
570  N N   . MET A 82  ? 1.5691 1.3464 0.9603 -0.7252 -0.1973 -0.0588 378 MET A N   
571  C CA  . MET A 82  ? 1.7952 1.4098 1.0645 -0.7450 -0.2023 -0.0608 378 MET A CA  
572  C C   . MET A 82  ? 1.8460 1.3804 1.0891 -0.7024 -0.2093 -0.0768 378 MET A C   
573  O O   . MET A 82  ? 1.9366 1.3552 1.1307 -0.6638 -0.2078 -0.0838 378 MET A O   
574  C CB  . MET A 82  ? 2.0174 1.6265 1.2158 -0.8203 -0.2071 -0.0500 378 MET A CB  
575  C CG  . MET A 82  ? 2.2050 1.8090 1.3670 -0.8639 -0.2004 -0.0350 378 MET A CG  
576  S SD  . MET A 82  ? 2.3654 1.8224 1.4717 -0.8224 -0.1950 -0.0366 378 MET A SD  
577  C CE  . MET A 82  ? 2.5276 1.7886 1.4908 -0.8222 -0.2055 -0.0434 378 MET A CE  
578  N N   . ASP A 83  ? 1.7363 1.3359 1.0115 -0.7049 -0.2165 -0.0829 379 ASP A N   
579  C CA  . ASP A 83  ? 1.7204 1.2438 0.9618 -0.6686 -0.2231 -0.0984 379 ASP A CA  
580  C C   . ASP A 83  ? 1.6454 1.1636 0.9370 -0.5982 -0.2180 -0.1094 379 ASP A C   
581  O O   . ASP A 83  ? 1.7774 1.1857 1.0111 -0.5612 -0.2186 -0.1205 379 ASP A O   
582  C CB  . ASP A 83  ? 1.7501 1.3559 1.0220 -0.6845 -0.2321 -0.1024 379 ASP A CB  
583  C CG  . ASP A 83  ? 1.8544 1.4126 1.0397 -0.7488 -0.2399 -0.0965 379 ASP A CG  
584  O OD1 . ASP A 83  ? 1.8336 1.5008 1.0529 -0.7936 -0.2424 -0.0871 379 ASP A OD1 
585  O OD2 . ASP A 83  ? 1.9579 1.3683 1.0360 -0.7539 -0.2432 -0.1004 379 ASP A OD2 
586  N N   . ARG A 84  ? 1.4908 1.1262 0.8847 -0.5775 -0.2124 -0.1060 380 ARG A N   
587  C CA  . ARG A 84  ? 1.5059 1.1394 0.9444 -0.5164 -0.2080 -0.1152 380 ARG A CA  
588  C C   . ARG A 84  ? 1.5422 1.0627 0.9267 -0.4949 -0.2015 -0.1157 380 ARG A C   
589  O O   . ARG A 84  ? 1.6472 1.1199 1.0286 -0.4432 -0.1991 -0.1263 380 ARG A O   
590  C CB  . ARG A 84  ? 1.3899 1.1672 0.9410 -0.5013 -0.2040 -0.1091 380 ARG A CB  
591  C CG  . ARG A 84  ? 1.3025 1.0806 0.8972 -0.4457 -0.1996 -0.1160 380 ARG A CG  
592  C CD  . ARG A 84  ? 1.2658 1.0899 0.8962 -0.4134 -0.2052 -0.1253 380 ARG A CD  
593  N NE  . ARG A 84  ? 1.2219 1.0192 0.8674 -0.3649 -0.2016 -0.1330 380 ARG A NE  
594  C CZ  . ARG A 84  ? 1.1512 0.8502 0.7360 -0.3350 -0.2021 -0.1464 380 ARG A CZ  
595  N NH1 . ARG A 84  ? 1.2409 0.8583 0.7480 -0.3475 -0.2057 -0.1531 380 ARG A NH1 
596  N NH2 . ARG A 84  ? 0.9923 0.6817 0.5988 -0.2846 -0.1946 -0.1497 380 ARG A NH2 
597  N N   . LEU A 85  ? 1.4476 0.9255 0.7852 -0.5323 -0.1986 -0.1039 381 LEU A N   
598  C CA  . LEU A 85  ? 1.5073 0.8657 0.7786 -0.5105 -0.1940 -0.1033 381 LEU A CA  
599  C C   . LEU A 85  ? 1.6700 0.8837 0.8304 -0.4943 -0.1987 -0.1113 381 LEU A C   
600  O O   . LEU A 85  ? 1.6619 0.8020 0.7950 -0.4376 -0.1959 -0.1205 381 LEU A O   
601  C CB  . LEU A 85  ? 1.6444 0.9981 0.8903 -0.5566 -0.1901 -0.0872 381 LEU A CB  
602  C CG  . LEU A 85  ? 1.6253 0.8945 0.8371 -0.5245 -0.1841 -0.0851 381 LEU A CG  
603  C CD1 . LEU A 85  ? 1.4828 0.8566 0.7947 -0.5105 -0.1765 -0.0808 381 LEU A CD1 
604  C CD2 . LEU A 85  ? 1.8505 1.0144 0.9522 -0.5657 -0.1854 -0.0733 381 LEU A CD2 
605  N N   . GLU A 86  ? 1.8341 1.0072 0.9257 -0.5421 -0.2057 -0.1074 382 GLU A N   
606  C CA  . GLU A 86  ? 2.0400 1.0779 1.0229 -0.5271 -0.2110 -0.1148 382 GLU A CA  
607  C C   . GLU A 86  ? 1.9694 1.0137 0.9814 -0.4662 -0.2108 -0.1322 382 GLU A C   
608  O O   . GLU A 86  ? 2.0123 0.9515 0.9579 -0.4158 -0.2089 -0.1400 382 GLU A O   
609  C CB  . GLU A 86  ? 2.3046 1.3268 1.2281 -0.5927 -0.2198 -0.1090 382 GLU A CB  
610  C CG  . GLU A 86  ? 2.5776 1.4493 1.3743 -0.5845 -0.2263 -0.1144 382 GLU A CG  
611  C CD  . GLU A 86  ? 2.8587 1.5832 1.5316 -0.5941 -0.2264 -0.1037 382 GLU A CD  
612  O OE1 . GLU A 86  ? 3.0127 1.6011 1.5726 -0.5766 -0.2313 -0.1072 382 GLU A OE1 
613  O OE2 . GLU A 86  ? 2.8739 1.6164 1.5569 -0.6174 -0.2220 -0.0915 382 GLU A OE2 
614  N N   . GLU A 87  ? 1.6686 0.8396 0.7771 -0.4669 -0.2123 -0.1375 383 GLU A N   
615  C CA  . GLU A 87  ? 1.6294 0.8156 0.7648 -0.4140 -0.2120 -0.1533 383 GLU A CA  
616  C C   . GLU A 87  ? 1.6102 0.7715 0.7626 -0.3489 -0.2029 -0.1594 383 GLU A C   
617  O O   . GLU A 87  ? 1.6295 0.7228 0.7371 -0.2962 -0.1998 -0.1708 383 GLU A O   
618  C CB  . GLU A 87  ? 1.5584 0.8906 0.7934 -0.4289 -0.2162 -0.1543 383 GLU A CB  
619  C CG  . GLU A 87  ? 1.6101 0.9725 0.8792 -0.3777 -0.2156 -0.1684 383 GLU A CG  
620  C CD  . GLU A 87  ? 1.5589 1.0571 0.9127 -0.3934 -0.2219 -0.1667 383 GLU A CD  
621  O OE1 . GLU A 87  ? 1.3613 0.9623 0.7972 -0.4026 -0.2202 -0.1569 383 GLU A OE1 
622  O OE2 . GLU A 87  ? 1.6232 1.1239 0.9577 -0.3933 -0.2285 -0.1745 383 GLU A OE2 
623  N N   . VAL A 88  ? 1.4876 0.7056 0.7023 -0.3499 -0.1978 -0.1515 384 VAL A N   
624  C CA  . VAL A 88  ? 1.5005 0.7065 0.7377 -0.2904 -0.1898 -0.1568 384 VAL A CA  
625  C C   . VAL A 88  ? 1.7012 0.7732 0.8417 -0.2563 -0.1860 -0.1565 384 VAL A C   
626  O O   . VAL A 88  ? 1.7334 0.7681 0.8570 -0.1919 -0.1803 -0.1656 384 VAL A O   
627  C CB  . VAL A 88  ? 1.4250 0.7243 0.7505 -0.3028 -0.1864 -0.1476 384 VAL A CB  
628  C CG1 . VAL A 88  ? 1.4435 0.7077 0.7724 -0.2472 -0.1790 -0.1509 384 VAL A CG1 
629  C CG2 . VAL A 88  ? 1.3825 0.8144 0.8037 -0.3123 -0.1898 -0.1488 384 VAL A CG2 
630  N N   . ASN A 89  ? 1.8414 0.8442 0.9146 -0.2967 -0.1890 -0.1447 385 ASN A N   
631  C CA  . ASN A 89  ? 2.0025 0.8673 0.9661 -0.2672 -0.1881 -0.1419 385 ASN A CA  
632  C C   . ASN A 89  ? 2.0649 0.8555 0.9597 -0.2247 -0.1896 -0.1536 385 ASN A C   
633  O O   . ASN A 89  ? 2.1030 0.8321 0.9557 -0.1578 -0.1847 -0.1581 385 ASN A O   
634  C CB  . ASN A 89  ? 2.1590 0.9619 1.0499 -0.3308 -0.1935 -0.1267 385 ASN A CB  
635  C CG  . ASN A 89  ? 2.3147 0.9899 1.1046 -0.3037 -0.1927 -0.1190 385 ASN A CG  
636  O OD1 . ASN A 89  ? 2.2044 0.8824 1.0187 -0.2557 -0.1867 -0.1189 385 ASN A OD1 
637  N ND2 . ASN A 89  ? 2.4370 0.9978 1.1070 -0.3346 -0.1997 -0.1117 385 ASN A ND2 
638  N N   . LYS A 90  ? 1.9954 0.7995 0.8804 -0.2601 -0.1961 -0.1581 386 LYS A N   
639  C CA  . LYS A 90  ? 2.2106 0.9460 1.0288 -0.2227 -0.1973 -0.1692 386 LYS A CA  
640  C C   . LYS A 90  ? 2.1523 0.9405 1.0256 -0.1497 -0.1882 -0.1829 386 LYS A C   
641  O O   . LYS A 90  ? 2.2278 0.9484 1.0412 -0.0886 -0.1837 -0.1891 386 LYS A O   
642  C CB  . LYS A 90  ? 2.3251 1.0817 1.1347 -0.2781 -0.2065 -0.1716 386 LYS A CB  
643  C CG  . LYS A 90  ? 2.4251 1.1108 1.1531 -0.3479 -0.2154 -0.1584 386 LYS A CG  
644  C CD  . LYS A 90  ? 2.4148 1.1449 1.1492 -0.4023 -0.2245 -0.1610 386 LYS A CD  
645  C CE  . LYS A 90  ? 2.5469 1.1952 1.1831 -0.4711 -0.2333 -0.1482 386 LYS A CE  
646  N NZ  . LYS A 90  ? 2.4950 1.2036 1.1460 -0.5288 -0.2425 -0.1491 386 LYS A NZ  
647  N N   . GLU A 91  ? 1.9800 0.8921 0.9636 -0.1538 -0.1853 -0.1865 387 GLU A N   
648  C CA  . GLU A 91  ? 1.8895 0.8558 0.9220 -0.0892 -0.1761 -0.1980 387 GLU A CA  
649  C C   . GLU A 91  ? 1.9228 0.8650 0.9519 -0.0284 -0.1665 -0.1958 387 GLU A C   
650  O O   . GLU A 91  ? 1.8625 0.8263 0.9029 0.0374  -0.1569 -0.2040 387 GLU A O   
651  C CB  . GLU A 91  ? 1.7997 0.8966 0.9395 -0.1126 -0.1778 -0.2004 387 GLU A CB  
652  C CG  . GLU A 91  ? 1.7234 0.8769 0.9014 -0.0561 -0.1700 -0.2126 387 GLU A CG  
653  C CD  . GLU A 91  ? 1.6418 0.9255 0.9256 -0.0755 -0.1716 -0.2086 387 GLU A CD  
654  O OE1 . GLU A 91  ? 1.5497 0.9116 0.8974 -0.0279 -0.1576 -0.2049 387 GLU A OE1 
655  O OE2 . GLU A 91  ? 1.5889 0.9215 0.9110 -0.1347 -0.1819 -0.2006 387 GLU A OE2 
656  N N   . ILE A 92  ? 1.9528 0.8590 0.9672 -0.0482 -0.1683 -0.1837 388 ILE A N   
657  C CA  . ILE A 92  ? 1.9250 0.8026 0.9264 0.0102  -0.1610 -0.1800 388 ILE A CA  
658  C C   . ILE A 92  ? 2.1837 0.9406 1.0694 0.0505  -0.1620 -0.1775 388 ILE A C   
659  O O   . ILE A 92  ? 2.2896 1.0349 1.1602 0.1191  -0.1555 -0.1772 388 ILE A O   
660  C CB  . ILE A 92  ? 1.7660 0.6586 0.7997 -0.0237 -0.1625 -0.1678 388 ILE A CB  
661  C CG1 . ILE A 92  ? 1.5577 0.5703 0.7022 -0.0613 -0.1629 -0.1690 388 ILE A CG1 
662  C CG2 . ILE A 92  ? 1.8662 0.7436 0.8954 0.0400  -0.1557 -0.1644 388 ILE A CG2 
663  C CD1 . ILE A 92  ? 1.4717 0.5139 0.6597 -0.0861 -0.1624 -0.1573 388 ILE A CD1 
664  N N   . GLU A 93  ? 2.2679 0.9372 1.0681 0.0107  -0.1708 -0.1746 389 GLU A N   
665  C CA  . GLU A 93  ? 2.4728 1.0269 1.1571 0.0556  -0.1727 -0.1745 389 GLU A CA  
666  C C   . GLU A 93  ? 2.4440 1.0358 1.1434 0.1167  -0.1651 -0.1881 389 GLU A C   
667  O O   . GLU A 93  ? 2.3677 0.9444 1.0388 0.1924  -0.1588 -0.1891 389 GLU A O   
668  C CB  . GLU A 93  ? 2.6494 1.1003 1.2350 -0.0054 -0.1844 -0.1687 389 GLU A CB  
669  C CG  . GLU A 93  ? 2.7448 1.1747 1.3184 -0.0799 -0.1910 -0.1544 389 GLU A CG  
670  C CD  . GLU A 93  ? 2.8654 1.2019 1.3591 -0.0564 -0.1923 -0.1422 389 GLU A CD  
671  O OE1 . GLU A 93  ? 2.9276 1.2092 1.3668 0.0193  -0.1899 -0.1444 389 GLU A OE1 
672  O OE2 . GLU A 93  ? 2.9000 1.2234 1.3839 -0.1127 -0.1958 -0.1300 389 GLU A OE2 
673  N N   . SER A 94  ? 2.4877 1.1399 1.2345 0.0846  -0.1656 -0.1976 390 SER A N   
674  C CA  . SER A 94  ? 2.5161 1.2019 1.2700 0.1292  -0.1589 -0.2103 390 SER A CA  
675  C C   . SER A 94  ? 2.4394 1.2242 1.2698 0.1975  -0.1444 -0.2150 390 SER A C   
676  O O   . SER A 94  ? 2.4764 1.2473 1.2712 0.2682  -0.1369 -0.2166 390 SER A O   
677  C CB  . SER A 94  ? 2.5224 1.2639 1.3195 0.0706  -0.1642 -0.2177 390 SER A CB  
678  O OG  . SER A 94  ? 2.5146 1.3455 1.3708 0.1087  -0.1545 -0.2291 390 SER A OG  
679  N N   . THR A 95  ? 2.3763 1.2656 1.3096 0.1768  -0.1410 -0.2158 391 THR A N   
680  C CA  . THR A 95  ? 2.3101 1.3072 1.3232 0.2312  -0.1272 -0.2199 391 THR A CA  
681  C C   . THR A 95  ? 2.1421 1.1582 1.1835 0.2610  -0.1231 -0.2110 391 THR A C   
682  O O   . THR A 95  ? 2.0055 1.1167 1.1132 0.3066  -0.1114 -0.2122 391 THR A O   
683  C CB  . THR A 95  ? 2.3414 1.4419 1.4442 0.1946  -0.1268 -0.2262 391 THR A CB  
684  O OG1 . THR A 95  ? 2.4657 1.5365 1.5484 0.1252  -0.1401 -0.2274 391 THR A OG1 
685  C CG2 . THR A 95  ? 2.2990 1.4837 1.4380 0.2448  -0.1130 -0.2347 391 THR A CG2 
686  N N   . SER A 96  ? 2.1604 1.0947 1.1534 0.2345  -0.1321 -0.2009 392 SER A N   
687  C CA  . SER A 96  ? 2.2158 1.1661 1.2363 0.2515  -0.1303 -0.1916 392 SER A CA  
688  C C   . SER A 96  ? 2.0826 1.1389 1.2128 0.2266  -0.1270 -0.1930 392 SER A C   
689  O O   . SER A 96  ? 2.0793 1.1829 1.2549 0.2555  -0.1220 -0.1879 392 SER A O   
690  C CB  . SER A 96  ? 2.3451 1.3098 1.3473 0.3363  -0.1221 -0.1890 392 SER A CB  
691  O OG  . SER A 96  ? 2.3170 1.3995 1.3935 0.3780  -0.1092 -0.1960 392 SER A OG  
692  N N   . THR A 97  ? 1.9534 1.0487 1.1235 0.1743  -0.1314 -0.1992 393 THR A N   
693  C CA  . THR A 97  ? 1.7143 0.9187 0.9919 0.1431  -0.1304 -0.1946 393 THR A CA  
694  C C   . THR A 97  ? 1.6590 0.8808 0.9520 0.0736  -0.1402 -0.1944 393 THR A C   
695  O O   . THR A 97  ? 1.7921 0.9247 1.0012 0.0461  -0.1498 -0.2019 393 THR A O   
696  C CB  . THR A 97  ? 1.5636 0.8979 0.9330 0.1904  -0.1147 -0.1899 393 THR A CB  
697  O OG1 . THR A 97  ? 1.4796 0.9270 0.9620 0.1568  -0.1119 -0.1746 393 THR A OG1 
698  C CG2 . THR A 97  ? 1.5648 0.9220 0.9246 0.2015  -0.1107 -0.1992 393 THR A CG2 
699  N N   . TYR A 98  ? 1.4053 0.7510 0.8090 0.0453  -0.1371 -0.1823 394 TYR A N   
700  C CA  . TYR A 98  ? 1.4891 0.8670 0.9112 -0.0116 -0.1467 -0.1818 394 TYR A CA  
701  C C   . TYR A 98  ? 1.3376 0.8555 0.8767 -0.0125 -0.1393 -0.1700 394 TYR A C   
702  O O   . TYR A 98  ? 1.2074 0.7889 0.8071 0.0240  -0.1272 -0.1627 394 TYR A O   
703  C CB  . TYR A 98  ? 1.5018 0.8313 0.8905 -0.0770 -0.1603 -0.1786 394 TYR A CB  
704  C CG  . TYR A 98  ? 1.3916 0.7905 0.8580 -0.0934 -0.1567 -0.1634 394 TYR A CG  
705  C CD1 . TYR A 98  ? 1.3165 0.8175 0.8624 -0.1349 -0.1597 -0.1534 394 TYR A CD1 
706  C CD2 . TYR A 98  ? 1.4405 0.8048 0.8979 -0.0625 -0.1505 -0.1594 394 TYR A CD2 
707  C CE1 . TYR A 98  ? 1.2377 0.8005 0.8497 -0.1449 -0.1553 -0.1404 394 TYR A CE1 
708  C CE2 . TYR A 98  ? 1.2673 0.6917 0.7911 -0.0766 -0.1471 -0.1463 394 TYR A CE2 
709  C CZ  . TYR A 98  ? 1.2113 0.7334 0.8116 -0.1178 -0.1489 -0.1371 394 TYR A CZ  
710  O OH  . TYR A 98  ? 1.1342 0.7132 0.7951 -0.1275 -0.1447 -0.1249 394 TYR A OH  
711  N N   . GLN A 99  ? 1.2119 0.7743 0.7754 -0.0553 -0.1479 -0.1681 395 GLN A N   
712  C CA  . GLN A 99  ? 1.0700 0.7474 0.7247 -0.0555 -0.1434 -0.1579 395 GLN A CA  
713  C C   . GLN A 99  ? 0.9613 0.6932 0.6603 -0.1050 -0.1529 -0.1485 395 GLN A C   
714  O O   . GLN A 99  ? 0.9572 0.6550 0.6128 -0.1505 -0.1660 -0.1527 395 GLN A O   
715  C CB  . GLN A 99  ? 1.0520 0.7437 0.6917 -0.0465 -0.1441 -0.1649 395 GLN A CB  
716  C CG  . GLN A 99  ? 1.0515 0.7243 0.6661 0.0083  -0.1308 -0.1720 395 GLN A CG  
717  C CD  . GLN A 99  ? 1.1627 0.9136 0.8513 0.0419  -0.1155 -0.1607 395 GLN A CD  
718  O OE1 . GLN A 99  ? 1.2044 0.9411 0.8787 0.0833  -0.1052 -0.1637 395 GLN A OE1 
719  N NE2 . GLN A 99  ? 1.1634 0.9964 0.9258 0.0246  -0.1149 -0.1478 395 GLN A NE2 
720  N N   . LEU A 100 ? 0.8285 0.6467 0.6093 -0.0964 -0.1463 -0.1357 396 LEU A N   
721  C CA  . LEU A 100 ? 0.6900 0.5742 0.5177 -0.1318 -0.1532 -0.1263 396 LEU A CA  
722  C C   . LEU A 100 ? 0.8149 0.7563 0.6587 -0.1468 -0.1619 -0.1259 396 LEU A C   
723  O O   . LEU A 100 ? 0.8105 0.7694 0.6632 -0.1200 -0.1576 -0.1266 396 LEU A O   
724  C CB  . LEU A 100 ? 0.6131 0.5577 0.5113 -0.1106 -0.1431 -0.1139 396 LEU A CB  
725  C CG  . LEU A 100 ? 0.7367 0.6346 0.6232 -0.0971 -0.1361 -0.1131 396 LEU A CG  
726  C CD1 . LEU A 100 ? 0.7457 0.6988 0.6956 -0.0735 -0.1263 -0.1023 396 LEU A CD1 
727  C CD2 . LEU A 100 ? 0.6736 0.5360 0.5281 -0.1382 -0.1441 -0.1133 396 LEU A CD2 
728  N N   . LYS A 101 ? 0.7710 0.7474 0.6173 -0.1904 -0.1744 -0.1240 397 LYS A N   
729  C CA  . LYS A 101 ? 0.9111 0.9681 0.7891 -0.1986 -0.1830 -0.1201 397 LYS A CA  
730  C C   . LYS A 101 ? 0.8798 1.0107 0.8283 -0.1648 -0.1744 -0.1074 397 LYS A C   
731  O O   . LYS A 101 ? 0.8295 0.9634 0.8071 -0.1512 -0.1649 -0.1010 397 LYS A O   
732  C CB  . LYS A 101 ? 0.9812 1.0809 0.8542 -0.2521 -0.1979 -0.1195 397 LYS A CB  
733  C CG  . LYS A 101 ? 1.0893 1.1029 0.8827 -0.2971 -0.2071 -0.1305 397 LYS A CG  
734  C CD  . LYS A 101 ? 1.1282 1.1118 0.8692 -0.3099 -0.2187 -0.1414 397 LYS A CD  
735  C CE  . LYS A 101 ? 1.2712 1.1212 0.9245 -0.3013 -0.2162 -0.1551 397 LYS A CE  
736  N NZ  . LYS A 101 ? 1.3830 1.2066 0.9896 -0.2999 -0.2244 -0.1660 397 LYS A NZ  
737  N N   . ASP A 102 ? 0.7412 0.9238 0.7090 -0.1508 -0.1786 -0.1037 398 ASP A N   
738  C CA  . ASP A 102 ? 0.6608 0.9007 0.6802 -0.1197 -0.1726 -0.0914 398 ASP A CA  
739  C C   . ASP A 102 ? 0.6447 0.9406 0.7017 -0.1299 -0.1739 -0.0837 398 ASP A C   
740  O O   . ASP A 102 ? 0.6101 0.9151 0.6974 -0.1060 -0.1642 -0.0760 398 ASP A O   
741  C CB  . ASP A 102 ? 0.8650 1.1496 0.8877 -0.1067 -0.1806 -0.0880 398 ASP A CB  
742  C CG  . ASP A 102 ? 0.8827 1.1201 0.8741 -0.0893 -0.1756 -0.0927 398 ASP A CG  
743  O OD1 . ASP A 102 ? 0.8733 1.0650 0.8593 -0.0719 -0.1619 -0.0937 398 ASP A OD1 
744  O OD2 . ASP A 102 ? 1.0319 1.2856 1.0043 -0.0928 -0.1855 -0.0949 398 ASP A OD2 
745  N N   . THR A 103 ? 0.6489 0.9877 0.7025 -0.1670 -0.1859 -0.0857 399 THR A N   
746  C CA  . THR A 103 ? 0.7045 1.1059 0.7919 -0.1803 -0.1859 -0.0787 399 THR A CA  
747  C C   . THR A 103 ? 0.7712 1.1185 0.8578 -0.1812 -0.1738 -0.0781 399 THR A C   
748  O O   . THR A 103 ? 0.7390 1.1142 0.8605 -0.1592 -0.1654 -0.0702 399 THR A O   
749  C CB  . THR A 103 ? 0.7221 1.1554 0.7945 -0.2232 -0.1940 -0.0794 399 THR A CB  
750  O OG1 . THR A 103 ? 0.7745 1.1263 0.7887 -0.2584 -0.1998 -0.0910 399 THR A OG1 
751  C CG2 . THR A 103 ? 0.6062 1.1073 0.6920 -0.2095 -0.2007 -0.0746 399 THR A CG2 
752  N N   . GLU A 104 ? 0.7971 1.0599 0.8368 -0.2027 -0.1732 -0.0867 400 GLU A N   
753  C CA  . GLU A 104 ? 0.7128 0.9197 0.7433 -0.2027 -0.1636 -0.0862 400 GLU A CA  
754  C C   . GLU A 104 ? 0.7228 0.9119 0.7790 -0.1554 -0.1506 -0.0820 400 GLU A C   
755  O O   . GLU A 104 ? 0.7378 0.9190 0.8095 -0.1483 -0.1428 -0.0773 400 GLU A O   
756  C CB  . GLU A 104 ? 0.7531 0.8609 0.7138 -0.2269 -0.1671 -0.0969 400 GLU A CB  
757  C CG  . GLU A 104 ? 0.8223 0.9307 0.7410 -0.2782 -0.1823 -0.1031 400 GLU A CG  
758  C CD  . GLU A 104 ? 1.0194 1.0080 0.8516 -0.2962 -0.1865 -0.1150 400 GLU A CD  
759  O OE1 . GLU A 104 ? 1.0927 1.0581 0.8801 -0.3418 -0.1941 -0.1169 400 GLU A OE1 
760  O OE2 . GLU A 104 ? 1.0569 0.9761 0.8667 -0.2559 -0.1780 -0.1200 400 GLU A OE2 
761  N N   . LEU A 105 ? 0.7019 0.8851 0.7595 -0.1266 -0.1484 -0.0832 401 LEU A N   
762  C CA  . LEU A 105 ? 0.7040 0.8771 0.7830 -0.0901 -0.1368 -0.0783 401 LEU A CA  
763  C C   . LEU A 105 ? 0.6081 0.8362 0.7299 -0.0756 -0.1339 -0.0675 401 LEU A C   
764  O O   . LEU A 105 ? 0.5069 0.7232 0.6438 -0.0617 -0.1256 -0.0632 401 LEU A O   
765  C CB  . LEU A 105 ? 0.6568 0.8168 0.7228 -0.0697 -0.1347 -0.0808 401 LEU A CB  
766  C CG  . LEU A 105 ? 0.6604 0.8079 0.7391 -0.0410 -0.1227 -0.0765 401 LEU A CG  
767  C CD1 . LEU A 105 ? 0.6652 0.7626 0.7208 -0.0337 -0.1159 -0.0833 401 LEU A CD1 
768  C CD2 . LEU A 105 ? 0.7397 0.8987 0.8132 -0.0272 -0.1215 -0.0745 401 LEU A CD2 
769  N N   . ILE A 106 ? 0.5351 0.8227 0.6718 -0.0760 -0.1415 -0.0636 402 ILE A N   
770  C CA  . ILE A 106 ? 0.4831 0.8193 0.6495 -0.0539 -0.1397 -0.0543 402 ILE A CA  
771  C C   . ILE A 106 ? 0.5345 0.8942 0.7186 -0.0668 -0.1366 -0.0518 402 ILE A C   
772  O O   . ILE A 106 ? 0.4916 0.8544 0.6914 -0.0461 -0.1296 -0.0461 402 ILE A O   
773  C CB  . ILE A 106 ? 0.5014 0.8982 0.6723 -0.0450 -0.1500 -0.0513 402 ILE A CB  
774  C CG1 . ILE A 106 ? 0.4878 0.8527 0.6370 -0.0292 -0.1512 -0.0520 402 ILE A CG1 
775  C CG2 . ILE A 106 ? 0.5195 0.9666 0.7114 -0.0152 -0.1492 -0.0424 402 ILE A CG2 
776  C CD1 . ILE A 106 ? 0.4805 0.8964 0.6247 -0.0207 -0.1636 -0.0499 402 ILE A CD1 
777  N N   . TYR A 107 ? 0.5374 0.9087 0.7126 -0.1042 -0.1418 -0.0561 403 TYR A N   
778  C CA  . TYR A 107 ? 0.5729 0.9613 0.7582 -0.1230 -0.1379 -0.0534 403 TYR A CA  
779  C C   . TYR A 107 ? 0.6652 0.9840 0.8420 -0.1138 -0.1280 -0.0536 403 TYR A C   
780  O O   . TYR A 107 ? 0.5556 0.8870 0.7515 -0.0998 -0.1210 -0.0481 403 TYR A O   
781  C CB  . TYR A 107 ? 0.6516 1.0512 0.8153 -0.1741 -0.1461 -0.0577 403 TYR A CB  
782  C CG  . TYR A 107 ? 0.7287 1.1311 0.8906 -0.2029 -0.1416 -0.0546 403 TYR A CG  
783  C CD1 . TYR A 107 ? 0.7573 1.2335 0.9397 -0.2097 -0.1367 -0.0467 403 TYR A CD1 
784  C CD2 . TYR A 107 ? 0.8443 1.1573 0.9736 -0.2123 -0.1365 -0.0574 403 TYR A CD2 
785  C CE1 . TYR A 107 ? 0.8006 1.2735 0.9755 -0.2348 -0.1293 -0.0425 403 TYR A CE1 
786  C CE2 . TYR A 107 ? 0.8601 1.1681 0.9807 -0.2394 -0.1325 -0.0536 403 TYR A CE2 
787  C CZ  . TYR A 107 ? 0.8391 1.2310 0.9844 -0.2545 -0.1293 -0.0462 403 TYR A CZ  
788  O OH  . TYR A 107 ? 0.8289 1.2100 0.9600 -0.2799 -0.1223 -0.0411 403 TYR A OH  
789  N N   . GLY A 108 ? 0.7133 0.9601 0.8582 -0.1186 -0.1278 -0.0603 404 GLY A N   
790  C CA  . GLY A 108 ? 0.6334 0.8225 0.7688 -0.1065 -0.1200 -0.0606 404 GLY A CA  
791  C C   . GLY A 108 ? 0.5804 0.7796 0.7432 -0.0726 -0.1126 -0.0548 404 GLY A C   
792  O O   . GLY A 108 ? 0.5207 0.7075 0.6909 -0.0660 -0.1069 -0.0515 404 GLY A O   
793  N N   . ALA A 109 ? 0.4972 0.7146 0.6687 -0.0536 -0.1134 -0.0532 405 ALA A N   
794  C CA  . ALA A 109 ? 0.5661 0.7811 0.7505 -0.0280 -0.1075 -0.0474 405 ALA A CA  
795  C C   . ALA A 109 ? 0.6021 0.8494 0.8044 -0.0191 -0.1059 -0.0410 405 ALA A C   
796  O O   . ALA A 109 ? 0.6151 0.8442 0.8210 -0.0103 -0.1004 -0.0379 405 ALA A O   
797  C CB  . ALA A 109 ? 0.5340 0.7528 0.7119 -0.0145 -0.1094 -0.0462 405 ALA A CB  
798  N N   . LYS A 110 ? 0.5748 0.8745 0.7863 -0.0194 -0.1108 -0.0391 406 LYS A N   
799  C CA  . LYS A 110 ? 0.5309 0.8684 0.7560 -0.0037 -0.1082 -0.0336 406 LYS A CA  
800  C C   . LYS A 110 ? 0.5341 0.8667 0.7656 -0.0189 -0.1026 -0.0335 406 LYS A C   
801  O O   . LYS A 110 ? 0.5491 0.8836 0.7847 -0.0016 -0.0972 -0.0296 406 LYS A O   
802  C CB  . LYS A 110 ? 0.5287 0.9412 0.7649 -0.0008 -0.1147 -0.0320 406 LYS A CB  
803  C CG  . LYS A 110 ? 0.4671 0.8856 0.6928 0.0268  -0.1203 -0.0297 406 LYS A CG  
804  C CD  . LYS A 110 ? 0.4305 0.9338 0.6681 0.0301  -0.1287 -0.0285 406 LYS A CD  
805  C CE  . LYS A 110 ? 0.5374 1.0424 0.7579 0.0647  -0.1351 -0.0250 406 LYS A CE  
806  N NZ  . LYS A 110 ? 0.5426 1.1260 0.7702 0.0746  -0.1395 -0.0221 406 LYS A NZ  
807  N N   . HIS A 111 ? 0.4653 0.7815 0.6887 -0.0506 -0.1040 -0.0377 407 HIS A N   
808  C CA  . HIS A 111 ? 0.5693 0.8773 0.7909 -0.0685 -0.0994 -0.0365 407 HIS A CA  
809  C C   . HIS A 111 ? 0.6025 0.8470 0.8133 -0.0589 -0.0946 -0.0369 407 HIS A C   
810  O O   . HIS A 111 ? 0.6344 0.8731 0.8460 -0.0608 -0.0898 -0.0340 407 HIS A O   
811  C CB  . HIS A 111 ? 0.5126 0.8221 0.7171 -0.1099 -0.1043 -0.0397 407 HIS A CB  
812  C CG  . HIS A 111 ? 0.4681 0.8634 0.6892 -0.1278 -0.1076 -0.0369 407 HIS A CG  
813  N ND1 . HIS A 111 ? 0.4475 0.8886 0.6771 -0.1471 -0.1030 -0.0322 407 HIS A ND1 
814  C CD2 . HIS A 111 ? 0.3732 0.8283 0.6059 -0.1267 -0.1147 -0.0374 407 HIS A CD2 
815  C CE1 . HIS A 111 ? 0.4283 0.9550 0.6736 -0.1572 -0.1059 -0.0299 407 HIS A CE1 
816  N NE2 . HIS A 111 ? 0.4314 0.9641 0.6776 -0.1431 -0.1132 -0.0328 407 HIS A NE2 
817  N N   . ALA A 112 ? 0.5455 0.7502 0.7467 -0.0478 -0.0957 -0.0401 408 ALA A N   
818  C CA  . ALA A 112 ? 0.5326 0.6984 0.7298 -0.0344 -0.0917 -0.0395 408 ALA A CA  
819  C C   . ALA A 112 ? 0.6131 0.7915 0.8227 -0.0166 -0.0881 -0.0341 408 ALA A C   
820  O O   . ALA A 112 ? 0.7678 0.9290 0.9760 -0.0138 -0.0851 -0.0322 408 ALA A O   
821  C CB  . ALA A 112 ? 0.5130 0.6551 0.7010 -0.0251 -0.0927 -0.0433 408 ALA A CB  
822  N N   . TRP A 113 ? 0.4736 0.6756 0.6878 -0.0030 -0.0892 -0.0318 409 TRP A N   
823  C CA  . TRP A 113 ? 0.4724 0.6755 0.6839 0.0164  -0.0867 -0.0272 409 TRP A CA  
824  C C   . TRP A 113 ? 0.4879 0.7182 0.7067 0.0161  -0.0830 -0.0256 409 TRP A C   
825  O O   . TRP A 113 ? 0.5913 0.8015 0.8043 0.0209  -0.0793 -0.0241 409 TRP A O   
826  C CB  . TRP A 113 ? 0.4165 0.6337 0.6203 0.0350  -0.0899 -0.0250 409 TRP A CB  
827  C CG  . TRP A 113 ? 0.4556 0.6540 0.6392 0.0599  -0.0884 -0.0209 409 TRP A CG  
828  C CD1 . TRP A 113 ? 0.5873 0.7574 0.7597 0.0640  -0.0847 -0.0197 409 TRP A CD1 
829  C CD2 . TRP A 113 ? 0.4993 0.6956 0.6603 0.0865  -0.0916 -0.0177 409 TRP A CD2 
830  N NE1 . TRP A 113 ? 0.5398 0.6847 0.6802 0.0903  -0.0852 -0.0168 409 TRP A NE1 
831  C CE2 . TRP A 113 ? 0.4944 0.6519 0.6251 0.1065  -0.0894 -0.0151 409 TRP A CE2 
832  C CE3 . TRP A 113 ? 0.5238 0.7424 0.6810 0.0972  -0.0969 -0.0167 409 TRP A CE3 
833  C CZ2 . TRP A 113 ? 0.4922 0.6237 0.5825 0.1391  -0.0922 -0.0117 409 TRP A CZ2 
834  C CZ3 . TRP A 113 ? 0.6045 0.8049 0.7269 0.1306  -0.0999 -0.0125 409 TRP A CZ3 
835  C CH2 . TRP A 113 ? 0.6503 0.8032 0.7365 0.1526  -0.0974 -0.0100 409 TRP A CH2 
836  N N   . ARG A 114 ? 0.3699 0.6516 0.6003 0.0079  -0.0841 -0.0257 410 ARG A N   
837  C CA  . ARG A 114 ? 0.4402 0.7657 0.6796 0.0032  -0.0794 -0.0235 410 ARG A CA  
838  C C   . ARG A 114 ? 0.5065 0.7970 0.7392 -0.0126 -0.0750 -0.0231 410 ARG A C   
839  O O   . ARG A 114 ? 0.5026 0.8061 0.7349 -0.0045 -0.0691 -0.0204 410 ARG A O   
840  C CB  . ARG A 114 ? 0.3634 0.7499 0.6151 -0.0212 -0.0827 -0.0240 410 ARG A CB  
841  C CG  . ARG A 114 ? 0.4566 0.9138 0.7211 -0.0262 -0.0772 -0.0204 410 ARG A CG  
842  C CD  . ARG A 114 ? 0.4553 0.9833 0.7312 -0.0586 -0.0817 -0.0202 410 ARG A CD  
843  N NE  . ARG A 114 ? 0.4442 1.0663 0.7378 -0.0567 -0.0758 -0.0158 410 ARG A NE  
844  C CZ  . ARG A 114 ? 0.4485 1.1246 0.7402 -0.0810 -0.0745 -0.0133 410 ARG A CZ  
845  N NH1 . ARG A 114 ? 0.4029 1.1473 0.6987 -0.0738 -0.0649 -0.0086 410 ARG A NH1 
846  N NH2 . ARG A 114 ? 0.5469 1.2096 0.8287 -0.1118 -0.0827 -0.0159 410 ARG A NH2 
847  N N   . ASN A 115 ? 0.4393 0.6834 0.6621 -0.0304 -0.0779 -0.0259 411 ASN A N   
848  C CA  . ASN A 115 ? 0.4493 0.6553 0.6589 -0.0433 -0.0757 -0.0253 411 ASN A CA  
849  C C   . ASN A 115 ? 0.4999 0.6656 0.7040 -0.0250 -0.0752 -0.0250 411 ASN A C   
850  O O   . ASN A 115 ? 0.4895 0.6234 0.6813 -0.0307 -0.0748 -0.0244 411 ASN A O   
851  C CB  . ASN A 115 ? 0.3343 0.5049 0.5245 -0.0665 -0.0801 -0.0287 411 ASN A CB  
852  C CG  . ASN A 115 ? 0.4542 0.6577 0.6406 -0.0965 -0.0823 -0.0290 411 ASN A CG  
853  O OD1 . ASN A 115 ? 0.5072 0.7687 0.7082 -0.1047 -0.0788 -0.0252 411 ASN A OD1 
854  N ND2 . ASN A 115 ? 0.5246 0.6943 0.6880 -0.1135 -0.0883 -0.0337 411 ASN A ND2 
855  N N   . ALA A 116 ? 0.4186 0.5830 0.6261 -0.0057 -0.0761 -0.0249 412 ALA A N   
856  C CA  . ALA A 116 ? 0.5036 0.6346 0.7030 0.0032  -0.0771 -0.0244 412 ALA A CA  
857  C C   . ALA A 116 ? 0.4872 0.6125 0.6782 0.0103  -0.0737 -0.0219 412 ALA A C   
858  O O   . ALA A 116 ? 0.5073 0.6362 0.6899 0.0259  -0.0720 -0.0208 412 ALA A O   
859  C CB  . ALA A 116 ? 0.3655 0.4907 0.5611 0.0130  -0.0796 -0.0242 412 ALA A CB  
860  N N   . SER A 117 ? 0.5602 0.6706 0.7464 0.0021  -0.0730 -0.0212 413 SER A N   
861  C CA  . SER A 117 ? 0.6561 0.7647 0.8325 0.0074  -0.0688 -0.0190 413 SER A CA  
862  C C   . SER A 117 ? 0.6004 0.6826 0.7605 0.0197  -0.0710 -0.0191 413 SER A C   
863  O O   . SER A 117 ? 0.6118 0.6898 0.7565 0.0309  -0.0673 -0.0185 413 SER A O   
864  C CB  . SER A 117 ? 0.6932 0.7861 0.8618 -0.0054 -0.0683 -0.0173 413 SER A CB  
865  O OG  . SER A 117 ? 0.7089 0.7738 0.8721 -0.0053 -0.0745 -0.0182 413 SER A OG  
866  N N   . ARG A 118 ? 0.4247 0.4895 0.5826 0.0165  -0.0768 -0.0199 414 ARG A N   
867  C CA  . ARG A 118 ? 0.3768 0.4121 0.5109 0.0184  -0.0803 -0.0195 414 ARG A CA  
868  C C   . ARG A 118 ? 0.5481 0.5673 0.6611 0.0299  -0.0801 -0.0193 414 ARG A C   
869  O O   . ARG A 118 ? 0.4878 0.4679 0.5676 0.0276  -0.0839 -0.0187 414 ARG A O   
870  C CB  . ARG A 118 ? 0.4892 0.5225 0.6276 0.0042  -0.0867 -0.0192 414 ARG A CB  
871  C CG  . ARG A 118 ? 0.5779 0.6200 0.7263 0.0010  -0.0888 -0.0191 414 ARG A CG  
872  C CD  . ARG A 118 ? 0.5979 0.6541 0.7516 -0.0071 -0.0955 -0.0186 414 ARG A CD  
873  N NE  . ARG A 118 ? 0.5433 0.6027 0.6956 -0.0046 -0.0995 -0.0179 414 ARG A NE  
874  C CZ  . ARG A 118 ? 0.6457 0.7312 0.8054 -0.0046 -0.1057 -0.0173 414 ARG A CZ  
875  N NH1 . ARG A 118 ? 0.6203 0.7360 0.7920 -0.0099 -0.1072 -0.0176 414 ARG A NH1 
876  N NH2 . ARG A 118 ? 0.7003 0.7870 0.8541 0.0026  -0.1104 -0.0162 414 ARG A NH2 
877  N N   . CYS A 119 ? 0.5757 0.6202 0.7000 0.0418  -0.0769 -0.0194 415 CYS A N   
878  C CA  . CYS A 119 ? 0.6084 0.6366 0.7085 0.0586  -0.0779 -0.0185 415 CYS A CA  
879  C C   . CYS A 119 ? 0.5208 0.5516 0.6003 0.0878  -0.0733 -0.0189 415 CYS A C   
880  O O   . CYS A 119 ? 0.6031 0.6871 0.7077 0.0962  -0.0682 -0.0191 415 CYS A O   
881  C CB  . CYS A 119 ? 0.5503 0.6102 0.6730 0.0575  -0.0789 -0.0184 415 CYS A CB  
882  S SG  . CYS A 119 ? 0.6083 0.6497 0.6973 0.0836  -0.0812 -0.0162 415 CYS A SG  
883  N N   . VAL A 120 ? 0.5924 0.5663 0.6206 0.1034  -0.0753 -0.0190 416 VAL A N   
884  C CA  . VAL A 120 ? 0.6536 0.6242 0.6515 0.1411  -0.0705 -0.0202 416 VAL A CA  
885  C C   . VAL A 120 ? 0.6498 0.6435 0.6416 0.1719  -0.0706 -0.0189 416 VAL A C   
886  O O   . VAL A 120 ? 0.6219 0.6510 0.6079 0.2077  -0.0654 -0.0197 416 VAL A O   
887  C CB  . VAL A 120 ? 0.7516 0.6373 0.6816 0.1495  -0.0735 -0.0217 416 VAL A CB  
888  C CG1 . VAL A 120 ? 0.8113 0.6240 0.6905 0.1424  -0.0818 -0.0197 416 VAL A CG1 
889  C CG2 . VAL A 120 ? 0.7118 0.5938 0.6058 0.1953  -0.0670 -0.0244 416 VAL A CG2 
890  N N   . GLY A 121 ? 0.7188 0.7031 0.7138 0.1604  -0.0763 -0.0168 417 GLY A N   
891  C CA  . GLY A 121 ? 0.5988 0.5949 0.5786 0.1914  -0.0785 -0.0150 417 GLY A CA  
892  C C   . GLY A 121 ? 0.6000 0.6909 0.6365 0.1920  -0.0767 -0.0149 417 GLY A C   
893  O O   . GLY A 121 ? 0.7815 0.8901 0.8109 0.2132  -0.0805 -0.0131 417 GLY A O   
894  N N   . ARG A 122 ? 0.5407 0.6891 0.6263 0.1680  -0.0720 -0.0164 418 ARG A N   
895  C CA  . ARG A 122 ? 0.5107 0.7356 0.6442 0.1514  -0.0724 -0.0164 418 ARG A CA  
896  C C   . ARG A 122 ? 0.5671 0.8676 0.7087 0.1826  -0.0714 -0.0153 418 ARG A C   
897  O O   . ARG A 122 ? 0.5496 0.9158 0.7256 0.1661  -0.0738 -0.0151 418 ARG A O   
898  C CB  . ARG A 122 ? 0.4397 0.6926 0.6073 0.1169  -0.0680 -0.0175 418 ARG A CB  
899  C CG  . ARG A 122 ? 0.4770 0.6800 0.6479 0.0860  -0.0711 -0.0187 418 ARG A CG  
900  C CD  . ARG A 122 ? 0.5642 0.7843 0.7565 0.0587  -0.0679 -0.0193 418 ARG A CD  
901  N NE  . ARG A 122 ? 0.5408 0.7398 0.7198 0.0631  -0.0633 -0.0187 418 ARG A NE  
902  C CZ  . ARG A 122 ? 0.5440 0.7562 0.7325 0.0447  -0.0592 -0.0179 418 ARG A CZ  
903  N NH1 . ARG A 122 ? 0.2705 0.5102 0.4763 0.0193  -0.0597 -0.0176 418 ARG A NH1 
904  N NH2 . ARG A 122 ? 0.6485 0.8399 0.8218 0.0498  -0.0553 -0.0172 418 ARG A NH2 
905  N N   . ILE A 123 ? 0.5506 0.8465 0.6581 0.2281  -0.0685 -0.0148 419 ILE A N   
906  C CA  . ILE A 123 ? 0.5200 0.9031 0.6362 0.2652  -0.0674 -0.0136 419 ILE A CA  
907  C C   . ILE A 123 ? 0.7023 1.1059 0.8217 0.2726  -0.0769 -0.0118 419 ILE A C   
908  O O   . ILE A 123 ? 0.6142 1.0961 0.7491 0.2793  -0.0751 -0.0107 419 ILE A O   
909  C CB  . ILE A 123 ? 0.6472 1.0011 0.7103 0.3234  -0.0633 -0.0141 419 ILE A CB  
910  C CG1 . ILE A 123 ? 0.6967 1.1438 0.7662 0.3452  -0.0546 -0.0135 419 ILE A CG1 
911  C CG2 . ILE A 123 ? 0.6404 0.8874 0.6363 0.3511  -0.0714 -0.0132 419 ILE A CG2 
912  C CD1 . ILE A 123 ? 0.7643 1.1684 0.7631 0.4020  -0.0521 -0.0146 419 ILE A CD1 
913  N N   . GLN A 124 ? 0.7307 1.0528 0.8274 0.2575  -0.0833 -0.0113 420 GLN A N   
914  C CA  . GLN A 124 ? 0.7867 1.1115 0.8780 0.2627  -0.0921 -0.0092 420 GLN A CA  
915  C C   . GLN A 124 ? 0.6511 1.0055 0.7875 0.2122  -0.0951 -0.0109 420 GLN A C   
916  O O   . GLN A 124 ? 0.6352 0.9788 0.7648 0.2093  -0.1021 -0.0099 420 GLN A O   
917  C CB  . GLN A 124 ? 0.9631 1.1747 0.9905 0.2769  -0.0965 -0.0067 420 GLN A CB  
918  C CG  . GLN A 124 ? 1.1255 1.2849 1.0858 0.3327  -0.0965 -0.0052 420 GLN A CG  
919  C CD  . GLN A 124 ? 1.2547 1.4037 1.1725 0.3747  -0.1041 -0.0014 420 GLN A CD  
920  O OE1 . GLN A 124 ? 1.2015 1.3822 1.1421 0.3613  -0.1108 0.0007  420 GLN A OE1 
921  N NE2 . GLN A 124 ? 1.3673 1.4644 1.2164 0.4157  -0.0997 -0.0021 420 GLN A NE2 
922  N N   . TRP A 125 ? 0.5478 0.9327 0.7221 0.1743  -0.0901 -0.0136 421 TRP A N   
923  C CA  . TRP A 125 ? 0.4658 0.8470 0.6649 0.1285  -0.0927 -0.0163 421 TRP A CA  
924  C C   . TRP A 125 ? 0.4859 0.9242 0.7008 0.1219  -0.1005 -0.0168 421 TRP A C   
925  O O   . TRP A 125 ? 0.6270 1.0378 0.8423 0.0985  -0.1047 -0.0190 421 TRP A O   
926  C CB  . TRP A 125 ? 0.3817 0.7826 0.6065 0.0942  -0.0870 -0.0183 421 TRP A CB  
927  C CG  . TRP A 125 ? 0.4456 0.9412 0.6964 0.0858  -0.0860 -0.0176 421 TRP A CG  
928  C CD1 . TRP A 125 ? 0.4714 1.0255 0.7281 0.1070  -0.0798 -0.0153 421 TRP A CD1 
929  C CD2 . TRP A 125 ? 0.4250 0.9740 0.6964 0.0508  -0.0915 -0.0192 421 TRP A CD2 
930  N NE1 . TRP A 125 ? 0.5362 1.1705 0.8130 0.0822  -0.0782 -0.0140 421 TRP A NE1 
931  C CE2 . TRP A 125 ? 0.4861 1.1145 0.7700 0.0457  -0.0862 -0.0163 421 TRP A CE2 
932  C CE3 . TRP A 125 ? 0.2830 0.8073 0.5529 0.0216  -0.0986 -0.0226 421 TRP A CE3 
933  C CZ2 . TRP A 125 ? 0.5182 1.1908 0.8080 0.0073  -0.0876 -0.0160 421 TRP A CZ2 
934  C CZ3 . TRP A 125 ? 0.3676 0.9484 0.6488 -0.0136 -0.1036 -0.0239 421 TRP A CZ3 
935  C CH2 . TRP A 125 ? 0.4479 1.0910 0.7341 -0.0223 -0.0969 -0.0198 421 TRP A CH2 
936  N N   . SER A 126 ? 0.4581 0.9815 0.6850 0.1427  -0.1028 -0.0150 422 SER A N   
937  C CA  . SER A 126 ? 0.5510 1.1206 0.7854 0.1305  -0.1089 -0.0149 422 SER A CA  
938  C C   . SER A 126 ? 0.6331 1.1742 0.8384 0.1646  -0.1167 -0.0126 422 SER A C   
939  O O   . SER A 126 ? 0.7576 1.3239 0.9660 0.1526  -0.1232 -0.0131 422 SER A O   
940  C CB  . SER A 126 ? 0.5999 1.2492 0.8438 0.1287  -0.1025 -0.0129 422 SER A CB  
941  O OG  . SER A 126 ? 0.5820 1.2440 0.8009 0.1804  -0.0989 -0.0099 422 SER A OG  
942  N N   . LYS A 127 ? 0.7030 1.1863 0.8725 0.2062  -0.1169 -0.0096 423 LYS A N   
943  C CA  . LYS A 127 ? 0.7025 1.1378 0.8295 0.2378  -0.1246 -0.0058 423 LYS A CA  
944  C C   . LYS A 127 ? 0.7398 1.0796 0.8481 0.2072  -0.1224 -0.0063 423 LYS A C   
945  O O   . LYS A 127 ? 0.6104 0.8706 0.6835 0.2136  -0.1181 -0.0043 423 LYS A O   
946  C CB  . LYS A 127 ? 0.7755 1.1715 0.8506 0.2902  -0.1208 -0.0020 423 LYS A CB  
947  C CG  . LYS A 127 ? 0.9120 1.3577 0.9713 0.3202  -0.1194 -0.0008 423 LYS A CG  
948  C CD  . LYS A 127 ? 0.9975 1.3643 0.9869 0.3629  -0.1252 0.0035  423 LYS A CD  
949  C CE  . LYS A 127 ? 1.1113 1.5341 1.0868 0.3934  -0.1252 0.0036  423 LYS A CE  
950  N NZ  . LYS A 127 ? 1.3126 1.6575 1.2204 0.4276  -0.1324 0.0078  423 LYS A NZ  
951  N N   . LEU A 128 ? 0.6586 1.0104 0.7883 0.1724  -0.1254 -0.0094 424 LEU A N   
952  C CA  . LEU A 128 ? 0.5751 0.8590 0.6957 0.1428  -0.1218 -0.0107 424 LEU A CA  
953  C C   . LEU A 128 ? 0.5287 0.8197 0.6459 0.1318  -0.1282 -0.0116 424 LEU A C   
954  O O   . LEU A 128 ? 0.6027 0.9548 0.7456 0.1189  -0.1336 -0.0156 424 LEU A O   
955  C CB  . LEU A 128 ? 0.3409 0.6279 0.4941 0.1072  -0.1152 -0.0162 424 LEU A CB  
956  C CG  . LEU A 128 ? 0.4192 0.6558 0.5689 0.0803  -0.1114 -0.0185 424 LEU A CG  
957  C CD1 . LEU A 128 ? 0.4200 0.5931 0.5402 0.0857  -0.1070 -0.0139 424 LEU A CD1 
958  C CD2 . LEU A 128 ? 0.2757 0.5256 0.4537 0.0520  -0.1078 -0.0247 424 LEU A CD2 
959  N N   . GLN A 129 ? 0.7055 0.9337 0.7870 0.1332  -0.1276 -0.0077 425 GLN A N   
960  C CA  . GLN A 129 ? 0.6710 0.8977 0.7409 0.1255  -0.1325 -0.0076 425 GLN A CA  
961  C C   . GLN A 129 ? 0.6869 0.8972 0.7730 0.0895  -0.1260 -0.0132 425 GLN A C   
962  O O   . GLN A 129 ? 0.7443 0.9107 0.8209 0.0784  -0.1184 -0.0115 425 GLN A O   
963  C CB  . GLN A 129 ? 0.7387 0.9052 0.7520 0.1478  -0.1350 0.0013  425 GLN A CB  
964  C CG  . GLN A 129 ? 0.7187 0.8789 0.7138 0.1403  -0.1392 0.0026  425 GLN A CG  
965  C CD  . GLN A 129 ? 0.8023 1.0337 0.8179 0.1495  -0.1497 -0.0011 425 GLN A CD  
966  O OE1 . GLN A 129 ? 0.7874 1.0702 0.8151 0.1743  -0.1559 -0.0006 425 GLN A OE1 
967  N NE2 . GLN A 129 ? 0.8673 1.1079 0.8857 0.1289  -0.1518 -0.0050 425 GLN A NE2 
968  N N   . VAL A 130 ? 0.6473 0.8941 0.7538 0.0721  -0.1294 -0.0203 426 VAL A N   
969  C CA  . VAL A 130 ? 0.5318 0.7616 0.6463 0.0462  -0.1236 -0.0270 426 VAL A CA  
970  C C   . VAL A 130 ? 0.6029 0.8170 0.6927 0.0446  -0.1246 -0.0266 426 VAL A C   
971  O O   . VAL A 130 ? 0.4980 0.7371 0.5814 0.0475  -0.1333 -0.0283 426 VAL A O   
972  C CB  . VAL A 130 ? 0.5989 0.8602 0.7366 0.0261  -0.1265 -0.0360 426 VAL A CB  
973  C CG1 . VAL A 130 ? 0.5281 0.7584 0.6609 0.0087  -0.1207 -0.0437 426 VAL A CG1 
974  C CG2 . VAL A 130 ? 0.5880 0.8700 0.7477 0.0256  -0.1249 -0.0351 426 VAL A CG2 
975  N N   . PHE A 131 ? 0.6099 0.7893 0.6856 0.0382  -0.1159 -0.0242 427 PHE A N   
976  C CA  . PHE A 131 ? 0.6411 0.8102 0.6944 0.0332  -0.1138 -0.0243 427 PHE A CA  
977  C C   . PHE A 131 ? 0.6098 0.7855 0.6755 0.0198  -0.1081 -0.0349 427 PHE A C   
978  O O   . PHE A 131 ? 0.5078 0.6773 0.5853 0.0145  -0.0996 -0.0364 427 PHE A O   
979  C CB  . PHE A 131 ? 0.5147 0.6479 0.5382 0.0317  -0.1073 -0.0139 427 PHE A CB  
980  C CG  . PHE A 131 ? 0.5737 0.6797 0.5645 0.0497  -0.1142 -0.0036 427 PHE A CG  
981  C CD1 . PHE A 131 ? 0.6122 0.7251 0.5821 0.0672  -0.1241 -0.0012 427 PHE A CD1 
982  C CD2 . PHE A 131 ? 0.6902 0.7604 0.6654 0.0524  -0.1119 0.0032  427 PHE A CD2 
983  C CE1 . PHE A 131 ? 0.6647 0.7480 0.5963 0.0926  -0.1312 0.0083  427 PHE A CE1 
984  C CE2 . PHE A 131 ? 0.7499 0.7815 0.6818 0.0750  -0.1186 0.0119  427 PHE A CE2 
985  C CZ  . PHE A 131 ? 0.7612 0.7985 0.6700 0.0980  -0.1281 0.0147  427 PHE A CZ  
986  N N   . ASP A 132 ? 0.6575 0.8437 0.7147 0.0167  -0.1138 -0.0426 428 ASP A N   
987  C CA  . ASP A 132 ? 0.5575 0.7363 0.6099 0.0094  -0.1099 -0.0542 428 ASP A CA  
988  C C   . ASP A 132 ? 0.6261 0.7977 0.6589 0.0130  -0.0997 -0.0532 428 ASP A C   
989  O O   . ASP A 132 ? 0.7158 0.8876 0.7254 0.0144  -0.1022 -0.0521 428 ASP A O   
990  C CB  . ASP A 132 ? 0.5750 0.7600 0.6152 0.0006  -0.1214 -0.0632 428 ASP A CB  
991  C CG  . ASP A 132 ? 0.6182 0.7760 0.6361 -0.0045 -0.1184 -0.0763 428 ASP A CG  
992  O OD1 . ASP A 132 ? 0.5499 0.7006 0.5479 -0.0178 -0.1286 -0.0849 428 ASP A OD1 
993  O OD2 . ASP A 132 ? 0.5981 0.7411 0.6133 0.0053  -0.1068 -0.0784 428 ASP A OD2 
994  N N   . ALA A 133 ? 0.6437 0.8159 0.6854 0.0145  -0.0883 -0.0535 429 ALA A N   
995  C CA  . ALA A 133 ? 0.6171 0.7996 0.6444 0.0171  -0.0767 -0.0528 429 ALA A CA  
996  C C   . ALA A 133 ? 0.6026 0.7843 0.6208 0.0290  -0.0711 -0.0660 429 ALA A C   
997  O O   . ALA A 133 ? 0.6739 0.8782 0.6900 0.0369  -0.0590 -0.0663 429 ALA A O   
998  C CB  . ALA A 133 ? 0.5726 0.7690 0.6124 0.0095  -0.0677 -0.0420 429 ALA A CB  
999  N N   . ARG A 134 ? 0.5913 0.7470 0.5988 0.0305  -0.0800 -0.0768 430 ARG A N   
1000 C CA  . ARG A 134 ? 0.6583 0.7927 0.6401 0.0455  -0.0761 -0.0903 430 ARG A CA  
1001 C C   . ARG A 134 ? 0.7065 0.8395 0.6526 0.0563  -0.0711 -0.0969 430 ARG A C   
1002 O O   . ARG A 134 ? 0.7147 0.8256 0.6299 0.0758  -0.0667 -0.1090 430 ARG A O   
1003 C CB  . ARG A 134 ? 0.6464 0.7394 0.6131 0.0367  -0.0882 -0.0993 430 ARG A CB  
1004 C CG  . ARG A 134 ? 0.6912 0.7841 0.6882 0.0300  -0.0903 -0.0942 430 ARG A CG  
1005 C CD  . ARG A 134 ? 0.7268 0.7830 0.7059 0.0121  -0.1022 -0.1009 430 ARG A CD  
1006 N NE  . ARG A 134 ? 0.7815 0.8540 0.7628 -0.0097 -0.1138 -0.0991 430 ARG A NE  
1007 C CZ  . ARG A 134 ? 0.8029 0.8541 0.7602 -0.0332 -0.1256 -0.1057 430 ARG A CZ  
1008 N NH1 . ARG A 134 ? 0.8649 0.8611 0.7853 -0.0396 -0.1273 -0.1146 430 ARG A NH1 
1009 N NH2 . ARG A 134 ? 0.7466 0.8312 0.7109 -0.0512 -0.1365 -0.1031 430 ARG A NH2 
1010 N N   . ASP A 135 ? 0.6332 0.7844 0.5757 0.0476  -0.0713 -0.0896 431 ASP A N   
1011 C CA  . ASP A 135 ? 0.7298 0.8855 0.6387 0.0580  -0.0641 -0.0945 431 ASP A CA  
1012 C C   . ASP A 135 ? 0.7334 0.9360 0.6532 0.0647  -0.0464 -0.0864 431 ASP A C   
1013 O O   . ASP A 135 ? 0.7799 0.9978 0.6740 0.0744  -0.0371 -0.0894 431 ASP A O   
1014 C CB  . ASP A 135 ? 0.7459 0.8938 0.6355 0.0448  -0.0747 -0.0915 431 ASP A CB  
1015 C CG  . ASP A 135 ? 0.8125 0.9806 0.7226 0.0317  -0.0766 -0.0740 431 ASP A CG  
1016 O OD1 . ASP A 135 ? 0.8075 0.9699 0.7005 0.0262  -0.0866 -0.0702 431 ASP A OD1 
1017 O OD2 . ASP A 135 ? 0.8368 1.0212 0.7724 0.0279  -0.0693 -0.0640 431 ASP A OD2 
1018 N N   . CYS A 136 ? 0.6980 0.9272 0.6531 0.0575  -0.0418 -0.0765 432 CYS A N   
1019 C CA  . CYS A 136 ? 0.7438 1.0263 0.7112 0.0531  -0.0267 -0.0667 432 CYS A CA  
1020 C C   . CYS A 136 ? 0.7857 1.1039 0.7467 0.0816  -0.0134 -0.0767 432 CYS A C   
1021 O O   . CYS A 136 ? 0.8181 1.1128 0.7731 0.1056  -0.0165 -0.0889 432 CYS A O   
1022 C CB  . CYS A 136 ? 0.6534 0.9484 0.6548 0.0356  -0.0280 -0.0553 432 CYS A CB  
1023 S SG  . CYS A 136 ? 0.6785 1.0317 0.6885 0.0105  -0.0141 -0.0392 432 CYS A SG  
1024 N N   . THR A 137 ? 0.7586 1.1337 0.7149 0.0804  0.0017  -0.0713 433 THR A N   
1025 C CA  . THR A 137 ? 0.6686 1.0941 0.6175 0.1138  0.0162  -0.0804 433 THR A CA  
1026 C C   . THR A 137 ? 0.6761 1.1974 0.6523 0.1034  0.0320  -0.0691 433 THR A C   
1027 O O   . THR A 137 ? 0.7113 1.2919 0.6891 0.1364  0.0440  -0.0760 433 THR A O   
1028 C CB  . THR A 137 ? 0.7445 1.1569 0.6476 0.1331  0.0217  -0.0905 433 THR A CB  
1029 O OG1 . THR A 137 ? 0.6929 1.1301 0.5891 0.1038  0.0276  -0.0779 433 THR A OG1 
1030 C CG2 . THR A 137 ? 0.7120 1.0342 0.5813 0.1401  0.0051  -0.1033 433 THR A CG2 
1031 N N   . THR A 138 ? 0.6315 1.1703 0.6233 0.0593  0.0320  -0.0520 434 THR A N   
1032 C CA  . THR A 138 ? 0.6492 1.2797 0.6587 0.0362  0.0464  -0.0396 434 THR A CA  
1033 C C   . THR A 138 ? 0.5201 1.1415 0.5520 -0.0043 0.0384  -0.0259 434 THR A C   
1034 O O   . THR A 138 ? 0.6370 1.1797 0.6633 -0.0170 0.0240  -0.0233 434 THR A O   
1035 C CB  . THR A 138 ? 0.7904 1.4493 0.7714 0.0123  0.0582  -0.0306 434 THR A CB  
1036 O OG1 . THR A 138 ? 0.8836 1.4590 0.8373 -0.0141 0.0464  -0.0230 434 THR A OG1 
1037 C CG2 . THR A 138 ? 0.7741 1.4632 0.7315 0.0536  0.0705  -0.0439 434 THR A CG2 
1038 N N   . ALA A 139 ? 0.5568 1.2644 0.6111 -0.0247 0.0480  -0.0172 435 ALA A N   
1039 C CA  . ALA A 139 ? 0.6284 1.3259 0.6920 -0.0711 0.0411  -0.0032 435 ALA A CA  
1040 C C   . ALA A 139 ? 0.7587 1.3894 0.7817 -0.1139 0.0370  0.0103  435 ALA A C   
1041 O O   . ALA A 139 ? 0.8061 1.3685 0.8190 -0.1366 0.0247  0.0173  435 ALA A O   
1042 C CB  . ALA A 139 ? 0.6233 1.4367 0.7121 -0.0927 0.0523  0.0043  435 ALA A CB  
1043 N N   . HIS A 140 ? 0.8359 1.4811 0.8291 -0.1219 0.0470  0.0141  436 HIS A N   
1044 C CA  . HIS A 140 ? 0.7545 1.3273 0.6985 -0.1572 0.0424  0.0272  436 HIS A CA  
1045 C C   . HIS A 140 ? 0.6658 1.1346 0.5954 -0.1338 0.0251  0.0216  436 HIS A C   
1046 O O   . HIS A 140 ? 0.7358 1.1305 0.6341 -0.1561 0.0146  0.0320  436 HIS A O   
1047 C CB  . HIS A 140 ? 0.7653 1.3746 0.6791 -0.1644 0.0567  0.0311  436 HIS A CB  
1048 C CG  . HIS A 140 ? 0.7945 1.4931 0.7037 -0.2106 0.0727  0.0448  436 HIS A CG  
1049 N ND1 . HIS A 140 ? 0.7820 1.5968 0.7360 -0.2065 0.0837  0.0416  436 HIS A ND1 
1050 C CD2 . HIS A 140 ? 0.8458 1.5388 0.7077 -0.2642 0.0795  0.0626  436 HIS A CD2 
1051 C CE1 . HIS A 140 ? 0.8350 1.7236 0.7750 -0.2587 0.0967  0.0567  436 HIS A CE1 
1052 N NE2 . HIS A 140 ? 0.8529 1.6643 0.7343 -0.2973 0.0948  0.0699  436 HIS A NE2 
1053 N N   . GLY A 141 ? 0.6114 1.0737 0.5566 -0.0890 0.0218  0.0052  437 GLY A N   
1054 C CA  . GLY A 141 ? 0.7138 1.0960 0.6524 -0.0700 0.0049  -0.0007 437 GLY A CA  
1055 C C   . GLY A 141 ? 0.6963 1.0481 0.6592 -0.0721 -0.0064 -0.0001 437 GLY A C   
1056 O O   . GLY A 141 ? 0.8217 1.1102 0.7722 -0.0701 -0.0198 0.0021  437 GLY A O   
1057 N N   . MET A 142 ? 0.7585 1.1603 0.7551 -0.0732 -0.0010 -0.0020 438 MET A N   
1058 C CA  . MET A 142 ? 0.5695 0.9447 0.5853 -0.0796 -0.0106 0.0000  438 MET A CA  
1059 C C   . MET A 142 ? 0.5807 0.9129 0.5642 -0.1185 -0.0147 0.0160  438 MET A C   
1060 O O   . MET A 142 ? 0.7286 0.9955 0.7005 -0.1163 -0.0267 0.0183  438 MET A O   
1061 C CB  . MET A 142 ? 0.5158 0.9588 0.5700 -0.0726 -0.0044 -0.0047 438 MET A CB  
1062 C CG  . MET A 142 ? 0.5296 0.9782 0.6055 -0.0285 -0.0061 -0.0210 438 MET A CG  
1063 S SD  . MET A 142 ? 0.5619 1.0972 0.6724 -0.0093 0.0023  -0.0261 438 MET A SD  
1064 C CE  . MET A 142 ? 0.5668 1.0663 0.6983 -0.0222 -0.0104 -0.0224 438 MET A CE  
1065 N N   . PHE A 143 ? 0.5934 0.9594 0.5552 -0.1548 -0.0047 0.0275  439 PHE A N   
1066 C CA  . PHE A 143 ? 0.6039 0.9125 0.5162 -0.1971 -0.0088 0.0435  439 PHE A CA  
1067 C C   . PHE A 143 ? 0.7539 0.9678 0.6214 -0.1833 -0.0201 0.0467  439 PHE A C   
1068 O O   . PHE A 143 ? 0.7598 0.9002 0.5990 -0.1868 -0.0312 0.0521  439 PHE A O   
1069 C CB  . PHE A 143 ? 0.7194 1.0800 0.6065 -0.2412 0.0049  0.0554  439 PHE A CB  
1070 C CG  . PHE A 143 ? 0.9010 1.1909 0.7208 -0.2923 0.0008  0.0730  439 PHE A CG  
1071 C CD1 . PHE A 143 ? 1.0252 1.2907 0.7870 -0.3208 0.0067  0.0852  439 PHE A CD1 
1072 C CD2 . PHE A 143 ? 0.8906 1.1281 0.6955 -0.3118 -0.0093 0.0772  439 PHE A CD2 
1073 C CE1 . PHE A 143 ? 1.1431 1.3260 0.8276 -0.3698 0.0020  0.1021  439 PHE A CE1 
1074 C CE2 . PHE A 143 ? 0.9999 1.1551 0.7278 -0.3588 -0.0141 0.0927  439 PHE A CE2 
1075 C CZ  . PHE A 143 ? 1.0680 1.1913 0.7324 -0.3884 -0.0088 0.1055  439 PHE A CZ  
1076 N N   . ASN A 144 ? 0.7444 0.9619 0.6034 -0.1628 -0.0180 0.0426  440 ASN A N   
1077 C CA  . ASN A 144 ? 0.7852 0.9271 0.6034 -0.1460 -0.0296 0.0456  440 ASN A CA  
1078 C C   . ASN A 144 ? 0.8138 0.9224 0.6559 -0.1128 -0.0438 0.0371  440 ASN A C   
1079 O O   . ASN A 144 ? 1.0272 1.0683 0.8332 -0.1061 -0.0550 0.0437  440 ASN A O   
1080 C CB  . ASN A 144 ? 0.7831 0.9480 0.5951 -0.1291 -0.0253 0.0403  440 ASN A CB  
1081 C CG  . ASN A 144 ? 0.8510 0.9463 0.6114 -0.1187 -0.0367 0.0470  440 ASN A CG  
1082 O OD1 . ASN A 144 ? 0.8204 0.8596 0.5220 -0.1422 -0.0382 0.0623  440 ASN A OD1 
1083 N ND2 . ASN A 144 ? 0.8342 0.9283 0.6098 -0.0840 -0.0462 0.0361  440 ASN A ND2 
1084 N N   . TYR A 145 ? 0.7348 0.8895 0.6323 -0.0900 -0.0433 0.0226  441 TYR A N   
1085 C CA  . TYR A 145 ? 0.7482 0.8806 0.6694 -0.0645 -0.0554 0.0150  441 TYR A CA  
1086 C C   . TYR A 145 ? 0.7239 0.8238 0.6412 -0.0752 -0.0596 0.0214  441 TYR A C   
1087 O O   . TYR A 145 ? 0.8402 0.8985 0.7478 -0.0581 -0.0703 0.0222  441 TYR A O   
1088 C CB  . TYR A 145 ? 0.6515 0.8297 0.6208 -0.0450 -0.0533 -0.0006 441 TYR A CB  
1089 C CG  . TYR A 145 ? 0.5900 0.7680 0.5579 -0.0238 -0.0592 -0.0106 441 TYR A CG  
1090 C CD1 . TYR A 145 ? 0.5104 0.7204 0.4818 -0.0160 -0.0513 -0.0203 441 TYR A CD1 
1091 C CD2 . TYR A 145 ? 0.6172 0.7666 0.5779 -0.0108 -0.0730 -0.0110 441 TYR A CD2 
1092 C CE1 . TYR A 145 ? 0.5924 0.7939 0.5538 -0.0009 -0.0580 -0.0305 441 TYR A CE1 
1093 C CE2 . TYR A 145 ? 0.6308 0.7861 0.5892 0.0020  -0.0801 -0.0202 441 TYR A CE2 
1094 C CZ  . TYR A 145 ? 0.6991 0.8746 0.6553 0.0044  -0.0730 -0.0302 441 TYR A CZ  
1095 O OH  . TYR A 145 ? 0.7872 0.9597 0.7320 0.0131  -0.0815 -0.0402 441 TYR A OH  
1096 N N   . ILE A 146 ? 0.7535 0.8764 0.6759 -0.1031 -0.0514 0.0260  442 ILE A N   
1097 C CA  . ILE A 146 ? 0.6559 0.7443 0.5682 -0.1175 -0.0558 0.0314  442 ILE A CA  
1098 C C   . ILE A 146 ? 0.8384 0.8424 0.6785 -0.1310 -0.0621 0.0446  442 ILE A C   
1099 O O   . ILE A 146 ? 0.8708 0.8180 0.6885 -0.1214 -0.0708 0.0466  442 ILE A O   
1100 C CB  . ILE A 146 ? 0.6356 0.7793 0.5702 -0.1476 -0.0469 0.0330  442 ILE A CB  
1101 C CG1 . ILE A 146 ? 0.5589 0.7745 0.5559 -0.1237 -0.0423 0.0196  442 ILE A CG1 
1102 C CG2 . ILE A 146 ? 0.7207 0.8218 0.6333 -0.1701 -0.0525 0.0394  442 ILE A CG2 
1103 C CD1 . ILE A 146 ? 0.5734 0.8354 0.5982 -0.1393 -0.0393 0.0195  442 ILE A CD1 
1104 N N   . CYS A 147 ? 0.9230 0.9116 0.7183 -0.1496 -0.0580 0.0537  443 CYS A N   
1105 C CA  . CYS A 147 ? 0.9107 0.8048 0.6212 -0.1643 -0.0641 0.0676  443 CYS A CA  
1106 C C   . CYS A 147 ? 0.9033 0.7391 0.5906 -0.1183 -0.0773 0.0660  443 CYS A C   
1107 O O   . CYS A 147 ? 0.9607 0.7174 0.5959 -0.1105 -0.0858 0.0717  443 CYS A O   
1108 C CB  . CYS A 147 ? 0.9934 0.8857 0.6590 -0.1942 -0.0563 0.0782  443 CYS A CB  
1109 S SG  . CYS A 147 ? 1.0350 0.9517 0.6738 -0.2659 -0.0442 0.0904  443 CYS A SG  
1110 N N   . ASN A 148 ? 0.7659 0.6427 0.4879 -0.0862 -0.0796 0.0578  444 ASN A N   
1111 C CA  . ASN A 148 ? 0.8643 0.7104 0.5731 -0.0423 -0.0926 0.0559  444 ASN A CA  
1112 C C   . ASN A 148 ? 0.8429 0.6967 0.5882 -0.0196 -0.0981 0.0484  444 ASN A C   
1113 O O   . ASN A 148 ? 0.9023 0.7190 0.6213 0.0141  -0.1083 0.0500  444 ASN A O   
1114 C CB  . ASN A 148 ? 0.9366 0.8366 0.6784 -0.0214 -0.0946 0.0478  444 ASN A CB  
1115 C CG  . ASN A 148 ? 0.9498 0.8452 0.6544 -0.0399 -0.0888 0.0546  444 ASN A CG  
1116 O OD1 . ASN A 148 ? 1.0367 0.8735 0.6753 -0.0626 -0.0864 0.0683  444 ASN A OD1 
1117 N ND2 . ASN A 148 ? 0.7735 0.7252 0.5132 -0.0318 -0.0866 0.0452  444 ASN A ND2 
1118 N N   . HIS A 149 ? 0.7673 0.6728 0.5711 -0.0341 -0.0912 0.0402  445 HIS A N   
1119 C CA  . HIS A 149 ? 0.7578 0.6657 0.5902 -0.0182 -0.0950 0.0344  445 HIS A CA  
1120 C C   . HIS A 149 ? 0.8085 0.6371 0.5804 -0.0258 -0.0982 0.0434  445 HIS A C   
1121 O O   . HIS A 149 ? 0.7990 0.5900 0.5485 0.0059  -0.1060 0.0435  445 HIS A O   
1122 C CB  . HIS A 149 ? 0.7184 0.6917 0.6174 -0.0321 -0.0874 0.0247  445 HIS A CB  
1123 C CG  . HIS A 149 ? 0.6378 0.6119 0.5629 -0.0228 -0.0899 0.0200  445 HIS A CG  
1124 N ND1 . HIS A 149 ? 0.5637 0.5902 0.5470 -0.0145 -0.0884 0.0095  445 HIS A ND1 
1125 C CD2 . HIS A 149 ? 0.6959 0.6193 0.5897 -0.0217 -0.0934 0.0245  445 HIS A CD2 
1126 C CE1 . HIS A 149 ? 0.6457 0.6601 0.6371 -0.0091 -0.0904 0.0083  445 HIS A CE1 
1127 N NE2 . HIS A 149 ? 0.6541 0.6080 0.5931 -0.0120 -0.0933 0.0167  445 HIS A NE2 
1128 N N   . VAL A 150 ? 0.8203 0.6239 0.5605 -0.0683 -0.0923 0.0509  446 VAL A N   
1129 C CA  . VAL A 150 ? 0.9157 0.6278 0.5810 -0.0843 -0.0964 0.0599  446 VAL A CA  
1130 C C   . VAL A 150 ? 1.0460 0.6682 0.6307 -0.0520 -0.1061 0.0672  446 VAL A C   
1131 O O   . VAL A 150 ? 1.1241 0.6873 0.6711 -0.0225 -0.1134 0.0671  446 VAL A O   
1132 C CB  . VAL A 150 ? 0.9723 0.6750 0.6051 -0.1443 -0.0894 0.0689  446 VAL A CB  
1133 C CG1 . VAL A 150 ? 1.0451 0.6290 0.5750 -0.1670 -0.0959 0.0798  446 VAL A CG1 
1134 C CG2 . VAL A 150 ? 0.8354 0.6267 0.5411 -0.1693 -0.0817 0.0621  446 VAL A CG2 
1135 N N   . LYS A 151 ? 1.0458 0.6576 0.6000 -0.0521 -0.1063 0.0736  447 LYS A N   
1136 C CA  . LYS A 151 ? 1.1848 0.7048 0.6506 -0.0200 -0.1164 0.0824  447 LYS A CA  
1137 C C   . LYS A 151 ? 1.1970 0.7374 0.6872 0.0443  -0.1255 0.0750  447 LYS A C   
1138 O O   . LYS A 151 ? 1.3340 0.7944 0.7531 0.0811  -0.1344 0.0795  447 LYS A O   
1139 C CB  . LYS A 151 ? 1.0448 0.5637 0.4821 -0.0311 -0.1148 0.0901  447 LYS A CB  
1140 C CG  . LYS A 151 ? 1.1639 0.5710 0.4901 -0.0033 -0.1257 0.1023  447 LYS A CG  
1141 C CD  . LYS A 151 ? 1.2126 0.6001 0.4927 -0.0346 -0.1216 0.1132  447 LYS A CD  
1142 C CE  . LYS A 151 ? 1.4477 0.6934 0.5905 -0.0223 -0.1315 0.1290  447 LYS A CE  
1143 N NZ  . LYS A 151 ? 1.5217 0.7581 0.6248 -0.0391 -0.1293 0.1390  447 LYS A NZ  
1144 N N   . TYR A 152 ? 1.0241 0.6711 0.6087 0.0586  -0.1236 0.0637  448 TYR A N   
1145 C CA  . TYR A 152 ? 1.0043 0.6881 0.6149 0.1125  -0.1322 0.0575  448 TYR A CA  
1146 C C   . TYR A 152 ? 0.9548 0.6248 0.5705 0.1309  -0.1328 0.0533  448 TYR A C   
1147 O O   . TYR A 152 ? 0.9755 0.6178 0.5545 0.1797  -0.1407 0.0545  448 TYR A O   
1148 C CB  . TYR A 152 ? 0.8336 0.6276 0.5337 0.1129  -0.1307 0.0470  448 TYR A CB  
1149 C CG  . TYR A 152 ? 0.9021 0.7553 0.6452 0.1533  -0.1375 0.0395  448 TYR A CG  
1150 C CD1 . TYR A 152 ? 1.0491 0.9209 0.7745 0.1953  -0.1485 0.0415  448 TYR A CD1 
1151 C CD2 . TYR A 152 ? 0.8095 0.7054 0.6084 0.1486  -0.1330 0.0313  448 TYR A CD2 
1152 C CE1 . TYR A 152 ? 1.0495 0.9915 0.8154 0.2292  -0.1545 0.0356  448 TYR A CE1 
1153 C CE2 . TYR A 152 ? 0.7847 0.7413 0.6202 0.1806  -0.1381 0.0257  448 TYR A CE2 
1154 C CZ  . TYR A 152 ? 0.8710 0.8555 0.6915 0.2197  -0.1486 0.0279  448 TYR A CZ  
1155 O OH  . TYR A 152 ? 0.9482 1.0102 0.8074 0.2487  -0.1534 0.0231  448 TYR A OH  
1156 N N   . ALA A 153 ? 0.9059 0.5980 0.5642 0.0958  -0.1247 0.0482  449 ALA A N   
1157 C CA  . ALA A 153 ? 0.9880 0.6748 0.6575 0.1100  -0.1245 0.0433  449 ALA A CA  
1158 C C   . ALA A 153 ? 1.1722 0.7410 0.7438 0.1132  -0.1281 0.0507  449 ALA A C   
1159 O O   . ALA A 153 ? 1.2433 0.7903 0.8025 0.1390  -0.1297 0.0471  449 ALA A O   
1160 C CB  . ALA A 153 ? 0.8768 0.6233 0.6187 0.0724  -0.1159 0.0359  449 ALA A CB  
1161 N N   . THR A 154 ? 1.1049 0.5933 0.6014 0.0841  -0.1289 0.0608  450 THR A N   
1162 C CA  . THR A 154 ? 1.2809 0.6365 0.6643 0.0824  -0.1340 0.0686  450 THR A CA  
1163 C C   . THR A 154 ? 1.4483 0.7342 0.7533 0.1476  -0.1441 0.0728  450 THR A C   
1164 O O   . THR A 154 ? 1.6436 0.8520 0.8828 0.1816  -0.1489 0.0723  450 THR A O   
1165 C CB  . THR A 154 ? 1.2465 0.5422 0.5724 0.0188  -0.1312 0.0791  450 THR A CB  
1166 O OG1 . THR A 154 ? 1.3023 0.6641 0.6940 -0.0353 -0.1228 0.0750  450 THR A OG1 
1167 C CG2 . THR A 154 ? 1.3996 0.5375 0.5870 0.0139  -0.1386 0.0885  450 THR A CG2 
1168 N N   . ASN A 155 ? 1.4104 0.7238 0.7178 0.1693  -0.1477 0.0767  451 ASN A N   
1169 C CA  . ASN A 155 ? 1.3520 0.6387 0.6089 0.2418  -0.1582 0.0792  451 ASN A CA  
1170 C C   . ASN A 155 ? 1.4239 0.5698 0.5569 0.2643  -0.1614 0.0810  451 ASN A C   
1171 O O   . ASN A 155 ? 1.4929 0.6459 0.6166 0.3194  -0.1604 0.0693  451 ASN A O   
1172 C CB  . ASN A 155 ? 1.3095 0.7153 0.6574 0.2894  -0.1586 0.0680  451 ASN A CB  
1173 C CG  . ASN A 155 ? 1.4245 0.8481 0.7462 0.3612  -0.1672 0.0680  451 ASN A CG  
1174 O OD1 . ASN A 155 ? 1.4722 0.8603 0.7462 0.3684  -0.1703 0.0725  451 ASN A OD1 
1175 N ND2 . ASN A 155 ? 1.4286 0.9312 0.8005 0.4013  -0.1635 0.0566  451 ASN A ND2 
1176 N N   . LYS A 156 ? 1.5632 0.6044 0.6158 0.2118  -0.1596 0.0877  452 LYS A N   
1177 C CA  . LYS A 156 ? 1.6556 0.5723 0.5966 0.2174  -0.1592 0.0802  452 LYS A CA  
1178 C C   . LYS A 156 ? 1.7679 0.6550 0.6934 0.2276  -0.1570 0.0685  452 LYS A C   
1179 O O   . LYS A 156 ? 1.8798 0.6962 0.7278 0.2664  -0.1577 0.0573  452 LYS A O   
1180 C CB  . LYS A 156 ? 1.7580 0.6540 0.6518 0.2824  -0.1627 0.0742  452 LYS A CB  
1181 C CG  . LYS A 156 ? 1.8843 0.7829 0.7661 0.2759  -0.1658 0.0842  452 LYS A CG  
1182 C CD  . LYS A 156 ? 1.9306 0.7876 0.7467 0.3404  -0.1695 0.0764  452 LYS A CD  
1183 C CE  . LYS A 156 ? 2.1075 1.0028 0.9386 0.3476  -0.1735 0.0854  452 LYS A CE  
1184 N NZ  . LYS A 156 ? 2.2471 1.0553 1.0130 0.2842  -0.1728 0.0967  452 LYS A NZ  
1185 N N   . GLY A 157 ? 1.5956 0.5371 0.5906 0.1953  -0.1544 0.0709  453 GLY A N   
1186 C CA  . GLY A 157 ? 1.6470 0.5757 0.6404 0.2037  -0.1522 0.0606  453 GLY A CA  
1187 C C   . GLY A 157 ? 1.7053 0.7322 0.7741 0.2683  -0.1502 0.0523  453 GLY A C   
1188 O O   . GLY A 157 ? 1.6294 0.6744 0.7245 0.2702  -0.1471 0.0458  453 GLY A O   
1189 N N   . ASN A 158 ? 1.5943 0.6923 0.6995 0.3177  -0.1515 0.0518  454 ASN A N   
1190 C CA  . ASN A 158 ? 1.6109 0.8275 0.7980 0.3707  -0.1487 0.0438  454 ASN A CA  
1191 C C   . ASN A 158 ? 1.5484 0.8750 0.8483 0.3451  -0.1505 0.0497  454 ASN A C   
1192 O O   . ASN A 158 ? 1.5114 0.9247 0.8695 0.3561  -0.1543 0.0525  454 ASN A O   
1193 C CB  . ASN A 158 ? 1.5463 0.7976 0.7193 0.4283  -0.1496 0.0394  454 ASN A CB  
1194 C CG  . ASN A 158 ? 1.6146 1.0032 0.8727 0.4738  -0.1454 0.0314  454 ASN A CG  
1195 O OD1 . ASN A 158 ? 1.7137 1.1593 1.0309 0.4671  -0.1409 0.0276  454 ASN A OD1 
1196 N ND2 . ASN A 158 ? 1.6694 1.1149 0.9326 0.5167  -0.1464 0.0288  454 ASN A ND2 
1197 N N   . LEU A 159 ? 1.5174 0.8468 0.8503 0.3070  -0.1468 0.0481  455 LEU A N   
1198 C CA  . LEU A 159 ? 1.3347 0.7728 0.7809 0.2522  -0.1391 0.0436  455 LEU A CA  
1199 C C   . LEU A 159 ? 1.1630 0.7419 0.7129 0.2793  -0.1369 0.0362  455 LEU A C   
1200 O O   . LEU A 159 ? 1.1283 0.7417 0.6827 0.3320  -0.1383 0.0325  455 LEU A O   
1201 C CB  . LEU A 159 ? 1.2626 0.6873 0.7268 0.2062  -0.1331 0.0394  455 LEU A CB  
1202 C CG  . LEU A 159 ? 1.3211 0.6550 0.7248 0.1445  -0.1331 0.0454  455 LEU A CG  
1203 C CD1 . LEU A 159 ? 1.4251 0.6352 0.7101 0.1468  -0.1403 0.0561  455 LEU A CD1 
1204 C CD2 . LEU A 159 ? 1.3327 0.6172 0.7089 0.1312  -0.1324 0.0409  455 LEU A CD2 
1205 N N   . ARG A 160 ? 0.9938 0.6546 0.6229 0.2405  -0.1333 0.0340  456 ARG A N   
1206 C CA  . ARG A 160 ? 0.8712 0.6566 0.5911 0.2513  -0.1324 0.0275  456 ARG A CA  
1207 C C   . ARG A 160 ? 0.7560 0.6001 0.5544 0.2002  -0.1246 0.0213  456 ARG A C   
1208 O O   . ARG A 160 ? 0.8787 0.6934 0.6726 0.1576  -0.1211 0.0235  456 ARG A O   
1209 C CB  . ARG A 160 ? 0.8559 0.6730 0.5750 0.2662  -0.1393 0.0310  456 ARG A CB  
1210 C CG  . ARG A 160 ? 0.9604 0.7324 0.6041 0.3274  -0.1486 0.0371  456 ARG A CG  
1211 C CD  . ARG A 160 ? 0.9957 0.8045 0.6381 0.3441  -0.1571 0.0410  456 ARG A CD  
1212 N NE  . ARG A 160 ? 1.0517 0.7910 0.6517 0.3080  -0.1570 0.0478  456 ARG A NE  
1213 C CZ  . ARG A 160 ? 1.1398 0.8801 0.7150 0.3205  -0.1645 0.0532  456 ARG A CZ  
1214 N NH1 . ARG A 160 ? 1.1716 0.9809 0.7609 0.3692  -0.1740 0.0523  456 ARG A NH1 
1215 N NH2 . ARG A 160 ? 1.1372 0.8159 0.6724 0.2840  -0.1625 0.0600  456 ARG A NH2 
1216 N N   . SER A 161 ? 0.7882 0.7166 0.6538 0.2055  -0.1218 0.0142  457 SER A N   
1217 C CA  . SER A 161 ? 0.7999 0.7719 0.7286 0.1638  -0.1152 0.0083  457 SER A CA  
1218 C C   . SER A 161 ? 0.7017 0.7186 0.6662 0.1414  -0.1160 0.0064  457 SER A C   
1219 O O   . SER A 161 ? 0.7289 0.7886 0.7022 0.1600  -0.1217 0.0061  457 SER A O   
1220 C CB  . SER A 161 ? 0.7447 0.7802 0.7215 0.1736  -0.1120 0.0023  457 SER A CB  
1221 O OG  . SER A 161 ? 0.6531 0.6579 0.5924 0.2083  -0.1117 0.0036  457 SER A OG  
1222 N N   . ALA A 162 ? 0.6805 0.6910 0.6626 0.1037  -0.1107 0.0048  458 ALA A N   
1223 C CA  . ALA A 162 ? 0.6418 0.6866 0.6491 0.0854  -0.1103 0.0020  458 ALA A CA  
1224 C C   . ALA A 162 ? 0.5926 0.6554 0.6359 0.0546  -0.1032 -0.0032 458 ALA A C   
1225 O O   . ALA A 162 ? 0.7363 0.7805 0.7801 0.0426  -0.0991 -0.0027 458 ALA A O   
1226 C CB  . ALA A 162 ? 0.5893 0.5911 0.5477 0.0835  -0.1124 0.0094  458 ALA A CB  
1227 N N   . ILE A 163 ? 0.5101 0.6083 0.5782 0.0446  -0.1026 -0.0086 459 ILE A N   
1228 C CA  . ILE A 163 ? 0.4878 0.6027 0.5818 0.0245  -0.0963 -0.0143 459 ILE A CA  
1229 C C   . ILE A 163 ? 0.5204 0.6486 0.6104 0.0190  -0.0956 -0.0171 459 ILE A C   
1230 O O   . ILE A 163 ? 0.5104 0.6516 0.5964 0.0278  -0.1017 -0.0189 459 ILE A O   
1231 C CB  . ILE A 163 ? 0.4048 0.5459 0.5331 0.0239  -0.0965 -0.0217 459 ILE A CB  
1232 C CG1 . ILE A 163 ? 0.3850 0.5337 0.5290 0.0115  -0.0911 -0.0277 459 ILE A CG1 
1233 C CG2 . ILE A 163 ? 0.4720 0.6435 0.6100 0.0306  -0.1032 -0.0256 459 ILE A CG2 
1234 C CD1 . ILE A 163 ? 0.3651 0.5211 0.5298 0.0095  -0.0912 -0.0332 459 ILE A CD1 
1235 N N   . THR A 164 ? 0.5512 0.6825 0.6414 0.0053  -0.0881 -0.0176 460 THR A N   
1236 C CA  . THR A 164 ? 0.6042 0.7504 0.6887 0.0021  -0.0849 -0.0212 460 THR A CA  
1237 C C   . THR A 164 ? 0.6554 0.8233 0.7620 0.0022  -0.0798 -0.0308 460 THR A C   
1238 O O   . THR A 164 ? 0.7495 0.9277 0.8669 -0.0026 -0.0740 -0.0297 460 THR A O   
1239 C CB  . THR A 164 ? 0.6071 0.7433 0.6638 -0.0110 -0.0790 -0.0124 460 THR A CB  
1240 O OG1 . THR A 164 ? 0.6370 0.7360 0.6581 -0.0072 -0.0851 -0.0033 460 THR A OG1 
1241 C CG2 . THR A 164 ? 0.4460 0.6050 0.4972 -0.0121 -0.0736 -0.0167 460 THR A CG2 
1242 N N   . ILE A 165 ? 0.5864 0.7580 0.6931 0.0083  -0.0830 -0.0401 461 ILE A N   
1243 C CA  . ILE A 165 ? 0.4895 0.6618 0.6026 0.0134  -0.0807 -0.0501 461 ILE A CA  
1244 C C   . ILE A 165 ? 0.5549 0.7346 0.6500 0.0208  -0.0747 -0.0561 461 ILE A C   
1245 O O   . ILE A 165 ? 0.5331 0.7051 0.6093 0.0209  -0.0785 -0.0602 461 ILE A O   
1246 C CB  . ILE A 165 ? 0.4779 0.6366 0.5914 0.0106  -0.0896 -0.0567 461 ILE A CB  
1247 C CG1 . ILE A 165 ? 0.5294 0.6903 0.6627 0.0065  -0.0928 -0.0512 461 ILE A CG1 
1248 C CG2 . ILE A 165 ? 0.6200 0.7584 0.7195 0.0154  -0.0884 -0.0672 461 ILE A CG2 
1249 C CD1 . ILE A 165 ? 0.5135 0.6779 0.6482 -0.0021 -0.1013 -0.0549 461 ILE A CD1 
1250 N N   . PHE A 166 ? 0.5654 0.7652 0.6651 0.0286  -0.0654 -0.0569 462 PHE A N   
1251 C CA  . PHE A 166 ? 0.4730 0.6917 0.5562 0.0414  -0.0570 -0.0624 462 PHE A CA  
1252 C C   . PHE A 166 ? 0.6772 0.8697 0.7400 0.0624  -0.0584 -0.0761 462 PHE A C   
1253 O O   . PHE A 166 ? 0.6160 0.7758 0.6782 0.0613  -0.0657 -0.0797 462 PHE A O   
1254 C CB  . PHE A 166 ? 0.4216 0.6898 0.5196 0.0392  -0.0463 -0.0552 462 PHE A CB  
1255 C CG  . PHE A 166 ? 0.4968 0.7765 0.5925 0.0142  -0.0442 -0.0423 462 PHE A CG  
1256 C CD1 . PHE A 166 ? 0.4681 0.7513 0.5410 0.0097  -0.0405 -0.0403 462 PHE A CD1 
1257 C CD2 . PHE A 166 ? 0.4267 0.7020 0.5331 -0.0051 -0.0468 -0.0321 462 PHE A CD2 
1258 C CE1 . PHE A 166 ? 0.5075 0.7873 0.5656 -0.0144 -0.0393 -0.0273 462 PHE A CE1 
1259 C CE2 . PHE A 166 ? 0.4533 0.7196 0.5411 -0.0291 -0.0461 -0.0201 462 PHE A CE2 
1260 C CZ  . PHE A 166 ? 0.4735 0.7402 0.5355 -0.0341 -0.0424 -0.0171 462 PHE A CZ  
1261 N N   . PRO A 167 ? 0.6714 0.8702 0.7083 0.0816  -0.0516 -0.0840 463 PRO A N   
1262 C CA  . PRO A 167 ? 0.7894 0.9410 0.7873 0.1033  -0.0546 -0.0983 463 PRO A CA  
1263 C C   . PRO A 167 ? 0.7943 0.9286 0.7930 0.1193  -0.0557 -0.1010 463 PRO A C   
1264 O O   . PRO A 167 ? 0.6703 0.8495 0.6986 0.1267  -0.0498 -0.0945 463 PRO A O   
1265 C CB  . PRO A 167 ? 0.7744 0.9496 0.7470 0.1283  -0.0435 -0.1045 463 PRO A CB  
1266 C CG  . PRO A 167 ? 0.6792 0.8929 0.6677 0.1067  -0.0398 -0.0947 463 PRO A CG  
1267 C CD  . PRO A 167 ? 0.6937 0.9341 0.7254 0.0831  -0.0413 -0.0806 463 PRO A CD  
1268 N N   . GLN A 168 ? 0.8668 0.9327 0.8274 0.1218  -0.0643 -0.1103 464 GLN A N   
1269 C CA  . GLN A 168 ? 0.7352 0.7719 0.6887 0.1339  -0.0669 -0.1115 464 GLN A CA  
1270 C C   . GLN A 168 ? 0.8044 0.8477 0.7317 0.1808  -0.0588 -0.1182 464 GLN A C   
1271 O O   . GLN A 168 ? 0.8562 0.9102 0.7580 0.2045  -0.0519 -0.1252 464 GLN A O   
1272 C CB  . GLN A 168 ? 0.6687 0.6243 0.5800 0.1161  -0.0788 -0.1180 464 GLN A CB  
1273 C CG  . GLN A 168 ? 0.7651 0.6507 0.6021 0.1340  -0.0813 -0.1324 464 GLN A CG  
1274 C CD  . GLN A 168 ? 0.8081 0.6325 0.6079 0.0957  -0.0943 -0.1373 464 GLN A CD  
1275 O OE1 . GLN A 168 ? 0.8213 0.6779 0.6605 0.0589  -0.1000 -0.1297 464 GLN A OE1 
1276 N NE2 . GLN A 168 ? 0.8897 0.6259 0.6080 0.1046  -0.0995 -0.1503 464 GLN A NE2 
1277 N N   . ARG A 169 ? 0.7663 0.8079 0.6987 0.1974  -0.0595 -0.1160 465 ARG A N   
1278 C CA  . ARG A 169 ? 0.7498 0.8034 0.6563 0.2492  -0.0532 -0.1218 465 ARG A CA  
1279 C C   . ARG A 169 ? 0.9092 0.8653 0.7302 0.2777  -0.0572 -0.1365 465 ARG A C   
1280 O O   . ARG A 169 ? 0.9984 0.8666 0.7797 0.2525  -0.0677 -0.1403 465 ARG A O   
1281 C CB  . ARG A 169 ? 0.8790 0.9479 0.8062 0.2599  -0.0556 -0.1155 465 ARG A CB  
1282 C CG  . ARG A 169 ? 0.9896 1.0923 0.8974 0.3186  -0.0497 -0.1198 465 ARG A CG  
1283 C CD  . ARG A 169 ? 0.9829 1.0821 0.8965 0.3327  -0.0553 -0.1149 465 ARG A CD  
1284 N NE  . ARG A 169 ? 0.9405 1.1509 0.9246 0.3216  -0.0512 -0.1036 465 ARG A NE  
1285 C CZ  . ARG A 169 ? 0.9101 1.1329 0.9375 0.2804  -0.0561 -0.0935 465 ARG A CZ  
1286 N NH1 . ARG A 169 ? 0.9466 1.0890 0.9601 0.2498  -0.0639 -0.0929 465 ARG A NH1 
1287 N NH2 . ARG A 169 ? 0.8219 1.1393 0.9025 0.2685  -0.0532 -0.0842 465 ARG A NH2 
1288 N N   . THR A 170 ? 0.9644 0.9370 0.7518 0.3293  -0.0486 -0.1448 466 THR A N   
1289 C CA  . THR A 170 ? 0.9623 0.8336 0.6543 0.3647  -0.0517 -0.1603 466 THR A CA  
1290 C C   . THR A 170 ? 1.0650 0.9311 0.7194 0.4314  -0.0485 -0.1647 466 THR A C   
1291 O O   . THR A 170 ? 1.2497 1.0582 0.8811 0.4356  -0.0570 -0.1626 466 THR A O   
1292 C CB  . THR A 170 ? 1.1334 1.0166 0.8029 0.3727  -0.0445 -0.1686 466 THR A CB  
1293 O OG1 . THR A 170 ? 1.0901 1.0990 0.8137 0.3956  -0.0294 -0.1633 466 THR A OG1 
1294 C CG2 . THR A 170 ? 1.1224 0.9881 0.8098 0.3110  -0.0516 -0.1659 466 THR A CG2 
1295 N N   . ASP A 171 ? 1.1658 1.0949 0.8113 0.4863  -0.0364 -0.1702 467 ASP A N   
1296 C CA  . ASP A 171 ? 1.2810 1.2187 0.8945 0.5411  -0.0365 -0.1668 467 ASP A CA  
1297 C C   . ASP A 171 ? 1.2062 1.2310 0.8898 0.5357  -0.0370 -0.1539 467 ASP A C   
1298 O O   . ASP A 171 ? 1.2711 1.2595 0.9215 0.5575  -0.0446 -0.1490 467 ASP A O   
1299 C CB  . ASP A 171 ? 1.4532 1.4639 1.0567 0.5803  -0.0262 -0.1659 467 ASP A CB  
1300 C CG  . ASP A 171 ? 1.4730 1.6472 1.1713 0.5656  -0.0126 -0.1575 467 ASP A CG  
1301 O OD1 . ASP A 171 ? 1.4444 1.6557 1.2036 0.5217  -0.0090 -0.1567 467 ASP A OD1 
1302 O OD2 . ASP A 171 ? 1.5234 1.7887 1.2310 0.5952  -0.0064 -0.1508 467 ASP A OD2 
1303 N N   . GLY A 172 ? 1.1481 1.2858 0.9237 0.5042  -0.0297 -0.1472 468 GLY A N   
1304 C CA  . GLY A 172 ? 1.1008 1.3342 0.9445 0.4915  -0.0301 -0.1332 468 GLY A CA  
1305 C C   . GLY A 172 ? 1.1209 1.5027 1.0230 0.4851  -0.0183 -0.1237 468 GLY A C   
1306 O O   . GLY A 172 ? 1.0106 1.4756 0.9790 0.4507  -0.0178 -0.1122 468 GLY A O   
1307 N N   . LYS A 173 ? 1.1826 1.5944 1.0548 0.5139  -0.0098 -0.1276 469 LYS A N   
1308 C CA  . LYS A 173 ? 1.1803 1.7304 1.1007 0.5023  0.0018  -0.1186 469 LYS A CA  
1309 C C   . LYS A 173 ? 1.1154 1.6964 1.0650 0.4683  0.0118  -0.1199 469 LYS A C   
1310 O O   . LYS A 173 ? 1.0637 1.7459 1.0394 0.4571  0.0224  -0.1131 469 LYS A O   
1311 C CB  . LYS A 173 ? 1.3246 1.9092 1.1985 0.5558  0.0048  -0.1200 469 LYS A CB  
1312 C CG  . LYS A 173 ? 1.3687 2.1066 1.2916 0.5439  0.0128  -0.1083 469 LYS A CG  
1313 C CD  . LYS A 173 ? 1.4542 2.2442 1.3377 0.5928  0.0181  -0.1102 469 LYS A CD  
1314 C CE  . LYS A 173 ? 1.3770 2.3228 1.3141 0.5646  0.0274  -0.0987 469 LYS A CE  
1315 N NZ  . LYS A 173 ? 1.4010 2.4189 1.3043 0.6161  0.0305  -0.0988 469 LYS A NZ  
1316 N N   . HIS A 174 ? 1.0805 1.5770 1.0220 0.4505  0.0084  -0.1286 470 HIS A N   
1317 C CA  . HIS A 174 ? 1.0563 1.5554 1.0128 0.4029  0.0129  -0.1253 470 HIS A CA  
1318 C C   . HIS A 174 ? 0.9954 1.4560 0.9894 0.3369  0.0019  -0.1144 470 HIS A C   
1319 O O   . HIS A 174 ? 1.0386 1.4183 1.0140 0.3076  -0.0053 -0.1166 470 HIS A O   
1320 C CB  . HIS A 174 ? 1.1333 1.5374 1.0196 0.4242  0.0126  -0.1399 470 HIS A CB  
1321 C CG  . HIS A 174 ? 1.2322 1.6692 1.0738 0.4910  0.0241  -0.1505 470 HIS A CG  
1322 N ND1 . HIS A 174 ? 1.3579 1.6870 1.1171 0.5343  0.0156  -0.1605 470 HIS A ND1 
1323 C CD2 . HIS A 174 ? 1.2732 1.8198 1.1354 0.4981  0.0354  -0.1421 470 HIS A CD2 
1324 C CE1 . HIS A 174 ? 1.4612 1.8357 1.1948 0.5721  0.0214  -0.1585 470 HIS A CE1 
1325 N NE2 . HIS A 174 ? 1.3833 1.8930 1.1801 0.5516  0.0335  -0.1481 470 HIS A NE2 
1326 N N   . ASP A 175 ? 0.8559 1.3788 0.9007 0.3158  0.0000  -0.1029 471 ASP A N   
1327 C CA  . ASP A 175 ? 0.7765 1.2643 0.8523 0.2619  -0.0100 -0.0930 471 ASP A CA  
1328 C C   . ASP A 175 ? 0.7432 1.2823 0.8525 0.2114  -0.0048 -0.0814 471 ASP A C   
1329 O O   . ASP A 175 ? 0.7518 1.3888 0.8818 0.2078  0.0062  -0.0756 471 ASP A O   
1330 C CB  . ASP A 175 ? 0.7480 1.2629 0.8510 0.2647  -0.0160 -0.0872 471 ASP A CB  
1331 C CG  . ASP A 175 ? 0.8413 1.2802 0.9023 0.3075  -0.0238 -0.0968 471 ASP A CG  
1332 O OD1 . ASP A 175 ? 0.9936 1.3732 1.0003 0.3431  -0.0227 -0.1087 471 ASP A OD1 
1333 O OD2 . ASP A 175 ? 0.8673 1.2970 0.9417 0.3045  -0.0316 -0.0924 471 ASP A OD2 
1334 N N   . PHE A 176 ? 0.7083 1.1812 0.8171 0.1734  -0.0126 -0.0777 472 PHE A N   
1335 C CA  . PHE A 176 ? 0.5883 1.0873 0.7208 0.1249  -0.0114 -0.0647 472 PHE A CA  
1336 C C   . PHE A 176 ? 0.5705 1.0788 0.7326 0.1004  -0.0180 -0.0556 472 PHE A C   
1337 O O   . PHE A 176 ? 0.4873 0.9367 0.6480 0.1037  -0.0278 -0.0583 472 PHE A O   
1338 C CB  . PHE A 176 ? 0.5373 0.9637 0.6503 0.1043  -0.0176 -0.0653 472 PHE A CB  
1339 C CG  . PHE A 176 ? 0.5991 1.0200 0.6810 0.1204  -0.0114 -0.0729 472 PHE A CG  
1340 C CD1 . PHE A 176 ? 0.5576 0.9402 0.6052 0.1594  -0.0121 -0.0875 472 PHE A CD1 
1341 C CD2 . PHE A 176 ? 0.6250 1.0704 0.7033 0.0961  -0.0054 -0.0653 472 PHE A CD2 
1342 C CE1 . PHE A 176 ? 0.7448 1.1165 0.7568 0.1748  -0.0068 -0.0956 472 PHE A CE1 
1343 C CE2 . PHE A 176 ? 0.6972 1.1380 0.7448 0.1111  0.0004  -0.0724 472 PHE A CE2 
1344 C CZ  . PHE A 176 ? 0.6874 1.0930 0.7030 0.1510  -0.0002 -0.0881 472 PHE A CZ  
1345 N N   . ARG A 177 ? 0.5395 1.1225 0.7239 0.0743  -0.0127 -0.0451 473 ARG A N   
1346 C CA  . ARG A 177 ? 0.4991 1.0894 0.7045 0.0463  -0.0196 -0.0365 473 ARG A CA  
1347 C C   . ARG A 177 ? 0.5574 1.1672 0.7616 -0.0056 -0.0172 -0.0233 473 ARG A C   
1348 O O   . ARG A 177 ? 0.6376 1.3148 0.8410 -0.0186 -0.0070 -0.0187 473 ARG A O   
1349 C CB  . ARG A 177 ? 0.4912 1.1592 0.7183 0.0685  -0.0183 -0.0375 473 ARG A CB  
1350 C CG  . ARG A 177 ? 0.5033 1.1378 0.7194 0.1213  -0.0224 -0.0491 473 ARG A CG  
1351 C CD  . ARG A 177 ? 0.6654 1.2114 0.8770 0.1131  -0.0344 -0.0497 473 ARG A CD  
1352 N NE  . ARG A 177 ? 0.6291 1.1922 0.8628 0.0771  -0.0400 -0.0398 473 ARG A NE  
1353 C CZ  . ARG A 177 ? 0.6216 1.2326 0.8718 0.0850  -0.0436 -0.0377 473 ARG A CZ  
1354 N NH1 . ARG A 177 ? 0.6122 1.2623 0.8601 0.1327  -0.0420 -0.0442 473 ARG A NH1 
1355 N NH2 . ARG A 177 ? 0.5172 1.1337 0.7804 0.0479  -0.0497 -0.0294 473 ARG A NH2 
1356 N N   . VAL A 178 ? 0.5654 1.1114 0.7621 -0.0345 -0.0261 -0.0173 474 VAL A N   
1357 C CA  . VAL A 178 ? 0.4812 1.0354 0.6674 -0.0849 -0.0268 -0.0043 474 VAL A CA  
1358 C C   . VAL A 178 ? 0.5887 1.2039 0.7979 -0.0952 -0.0294 -0.0016 474 VAL A C   
1359 O O   . VAL A 178 ? 0.5089 1.0990 0.7305 -0.0763 -0.0371 -0.0064 474 VAL A O   
1360 C CB  . VAL A 178 ? 0.5063 0.9614 0.6653 -0.1030 -0.0359 0.0000  474 VAL A CB  
1361 C CG1 . VAL A 178 ? 0.6276 1.0697 0.7561 -0.1544 -0.0370 0.0132  474 VAL A CG1 
1362 C CG2 . VAL A 178 ? 0.4164 0.8190 0.5581 -0.0836 -0.0359 -0.0044 474 VAL A CG2 
1363 N N   . TRP A 179 ? 0.6142 1.3173 0.8292 -0.1256 -0.0231 0.0061  475 TRP A N   
1364 C CA  . TRP A 179 ? 0.5517 1.3283 0.7899 -0.1380 -0.0269 0.0090  475 TRP A CA  
1365 C C   . TRP A 179 ? 0.6010 1.3207 0.8173 -0.1866 -0.0376 0.0172  475 TRP A C   
1366 O O   . TRP A 179 ? 0.4408 1.1640 0.6620 -0.1846 -0.0435 0.0169  475 TRP A O   
1367 C CB  . TRP A 179 ? 0.5053 1.3717 0.7383 -0.1474 -0.0151 0.0141  475 TRP A CB  
1368 C CG  . TRP A 179 ? 0.4434 1.3670 0.6923 -0.0890 -0.0064 0.0044  475 TRP A CG  
1369 C CD1 . TRP A 179 ? 0.5307 1.4283 0.7868 -0.0420 -0.0043 -0.0066 475 TRP A CD1 
1370 C CD2 . TRP A 179 ? 0.4471 1.4584 0.6977 -0.0690 0.0000  0.0041  475 TRP A CD2 
1371 N NE1 . TRP A 179 ? 0.5661 1.5185 0.8217 0.0073  0.0037  -0.0139 475 TRP A NE1 
1372 C CE2 . TRP A 179 ? 0.5837 1.6099 0.8376 -0.0069 0.0061  -0.0072 475 TRP A CE2 
1373 C CE3 . TRP A 179 ? 0.3744 1.4538 0.6190 -0.0974 0.0001  0.0122  475 TRP A CE3 
1374 C CZ2 . TRP A 179 ? 0.6146 1.7181 0.8643 0.0305  0.0121  -0.0105 475 TRP A CZ2 
1375 C CZ3 . TRP A 179 ? 0.4635 1.6320 0.7111 -0.0621 0.0058  0.0092  475 TRP A CZ3 
1376 C CH2 . TRP A 179 ? 0.5550 1.7341 0.8044 0.0029  0.0117  -0.0019 475 TRP A CH2 
1377 N N   . ASN A 180 ? 0.5667 1.2055 0.7406 -0.2212 -0.0388 0.0241  476 ASN A N   
1378 C CA  . ASN A 180 ? 0.6070 1.1624 0.7441 -0.2574 -0.0495 0.0301  476 ASN A CA  
1379 C C   . ASN A 180 ? 0.6601 1.1543 0.8091 -0.2203 -0.0581 0.0217  476 ASN A C   
1380 O O   . ASN A 180 ? 0.5355 1.0120 0.7044 -0.1732 -0.0563 0.0128  476 ASN A O   
1381 C CB  . ASN A 180 ? 0.5654 1.0288 0.6467 -0.2817 -0.0491 0.0371  476 ASN A CB  
1382 C CG  . ASN A 180 ? 0.6701 1.1834 0.7291 -0.3277 -0.0408 0.0476  476 ASN A CG  
1383 O OD1 . ASN A 180 ? 0.8614 1.4501 0.9465 -0.3111 -0.0298 0.0455  476 ASN A OD1 
1384 N ND2 . ASN A 180 ? 0.7696 1.2376 0.7732 -0.3876 -0.0457 0.0589  476 ASN A ND2 
1385 N N   . SER A 181 ? 0.6049 1.0645 0.7360 -0.2453 -0.0676 0.0247  477 SER A N   
1386 C CA  . SER A 181 ? 0.5566 0.9571 0.6942 -0.2134 -0.0747 0.0177  477 SER A CA  
1387 C C   . SER A 181 ? 0.6236 0.9122 0.7200 -0.2078 -0.0777 0.0182  477 SER A C   
1388 O O   . SER A 181 ? 0.5042 0.7526 0.6113 -0.1725 -0.0801 0.0116  477 SER A O   
1389 C CB  . SER A 181 ? 0.5660 0.9816 0.7031 -0.2354 -0.0837 0.0192  477 SER A CB  
1390 O OG  . SER A 181 ? 0.6430 1.0182 0.7285 -0.2911 -0.0890 0.0279  477 SER A OG  
1391 N N   . GLN A 182 ? 0.7254 0.9649 0.7705 -0.2421 -0.0779 0.0264  478 GLN A N   
1392 C CA  . GLN A 182 ? 0.7479 0.8866 0.7463 -0.2309 -0.0804 0.0280  478 GLN A CA  
1393 C C   . GLN A 182 ? 0.7207 0.8492 0.6821 -0.2577 -0.0757 0.0364  478 GLN A C   
1394 O O   . GLN A 182 ? 0.7977 0.9535 0.7371 -0.3065 -0.0746 0.0444  478 GLN A O   
1395 C CB  . GLN A 182 ? 0.8971 0.9441 0.8389 -0.2459 -0.0895 0.0308  478 GLN A CB  
1396 C CG  . GLN A 182 ? 0.9478 0.9943 0.9110 -0.2297 -0.0948 0.0244  478 GLN A CG  
1397 C CD  . GLN A 182 ? 1.0317 0.9878 0.9250 -0.2546 -0.1035 0.0279  478 GLN A CD  
1398 O OE1 . GLN A 182 ? 0.9156 0.7810 0.7393 -0.2617 -0.1060 0.0328  478 GLN A OE1 
1399 N NE2 . GLN A 182 ? 0.9519 0.9263 0.8554 -0.2665 -0.1089 0.0253  478 GLN A NE2 
1400 N N   . LEU A 183 ? 0.7385 0.8311 0.6906 -0.2293 -0.0736 0.0352  479 LEU A N   
1401 C CA  . LEU A 183 ? 0.7085 0.7814 0.6201 -0.2489 -0.0695 0.0434  479 LEU A CA  
1402 C C   . LEU A 183 ? 0.8310 0.8477 0.6687 -0.3052 -0.0729 0.0556  479 LEU A C   
1403 O O   . LEU A 183 ? 0.8222 0.8743 0.6433 -0.3456 -0.0669 0.0638  479 LEU A O   
1404 C CB  . LEU A 183 ? 0.7580 0.7669 0.6489 -0.2100 -0.0722 0.0415  479 LEU A CB  
1405 C CG  . LEU A 183 ? 0.7336 0.7885 0.6842 -0.1626 -0.0699 0.0303  479 LEU A CG  
1406 C CD1 . LEU A 183 ? 0.5324 0.5388 0.4552 -0.1361 -0.0729 0.0312  479 LEU A CD1 
1407 C CD2 . LEU A 183 ? 0.7709 0.9202 0.7710 -0.1641 -0.0606 0.0259  479 LEU A CD2 
1408 N N   . ILE A 184 ? 0.8938 0.8228 0.6817 -0.3111 -0.0823 0.0568  480 ILE A N   
1409 C CA  . ILE A 184 ? 0.8216 0.6673 0.5186 -0.3649 -0.0880 0.0678  480 ILE A CA  
1410 C C   . ILE A 184 ? 1.0332 0.8838 0.7286 -0.3934 -0.0946 0.0659  480 ILE A C   
1411 O O   . ILE A 184 ? 0.9977 0.8054 0.6946 -0.3608 -0.1006 0.0587  480 ILE A O   
1412 C CB  . ILE A 184 ? 0.9180 0.6253 0.5284 -0.3421 -0.0948 0.0715  480 ILE A CB  
1413 C CG1 . ILE A 184 ? 1.0330 0.7403 0.6370 -0.3240 -0.0894 0.0755  480 ILE A CG1 
1414 C CG2 . ILE A 184 ? 1.0824 0.6783 0.5825 -0.3949 -0.1027 0.0815  480 ILE A CG2 
1415 C CD1 . ILE A 184 ? 1.0903 0.6751 0.6143 -0.2907 -0.0967 0.0791  480 ILE A CD1 
1416 N N   . ARG A 185 ? 1.0606 0.9721 0.7539 -0.4549 -0.0935 0.0726  481 ARG A N   
1417 C CA  . ARG A 185 ? 1.0290 0.9541 0.7145 -0.4896 -0.1007 0.0721  481 ARG A CA  
1418 C C   . ARG A 185 ? 1.1701 1.0881 0.7878 -0.5428 -0.0992 0.0828  481 ARG A C   
1419 O O   . ARG A 185 ? 1.2553 1.2096 0.8651 -0.5647 -0.0918 0.0896  481 ARG A O   
1420 C CB  . ARG A 185 ? 0.9669 1.0336 0.7542 -0.4690 -0.0966 0.0644  481 ARG A CB  
1421 C CG  . ARG A 185 ? 0.9902 1.0711 0.8419 -0.4013 -0.0960 0.0524  481 ARG A CG  
1422 C CD  . ARG A 185 ? 0.8782 1.0393 0.7891 -0.3916 -0.0996 0.0457  481 ARG A CD  
1423 N NE  . ARG A 185 ? 0.9746 1.0692 0.8363 -0.4166 -0.1103 0.0463  481 ARG A NE  
1424 C CZ  . ARG A 185 ? 0.9620 1.0933 0.8577 -0.4011 -0.1145 0.0405  481 ARG A CZ  
1425 N NH1 . ARG A 185 ? 0.7363 0.9665 0.7119 -0.3651 -0.1109 0.0343  481 ARG A NH1 
1426 N NH2 . ARG A 185 ? 1.0651 1.1279 0.9078 -0.4191 -0.1222 0.0412  481 ARG A NH2 
1427 N N   . TYR A 186 ? 1.0851 0.9588 0.6514 -0.5654 -0.1071 0.0837  482 TYR A N   
1428 C CA  . TYR A 186 ? 1.1816 1.0554 0.6814 -0.6214 -0.1087 0.0927  482 TYR A CA  
1429 C C   . TYR A 186 ? 1.1754 1.2017 0.7426 -0.6389 -0.1033 0.0935  482 TYR A C   
1430 O O   . TYR A 186 ? 1.0145 1.1121 0.6554 -0.6096 -0.1025 0.0866  482 TYR A O   
1431 C CB  . TYR A 186 ? 1.4093 1.1521 0.8051 -0.6402 -0.1210 0.0938  482 TYR A CB  
1432 C CG  . TYR A 186 ? 1.5498 1.1355 0.8637 -0.6148 -0.1268 0.0923  482 TYR A CG  
1433 C CD1 . TYR A 186 ? 1.5638 1.0605 0.8574 -0.5736 -0.1334 0.0848  482 TYR A CD1 
1434 C CD2 . TYR A 186 ? 1.5460 1.0753 0.8020 -0.6263 -0.1255 0.0978  482 TYR A CD2 
1435 C CE1 . TYR A 186 ? 1.6798 1.0385 0.8957 -0.5396 -0.1381 0.0829  482 TYR A CE1 
1436 C CE2 . TYR A 186 ? 1.6055 0.9920 0.7829 -0.5942 -0.1310 0.0962  482 TYR A CE2 
1437 C CZ  . TYR A 186 ? 1.6670 0.9714 0.8252 -0.5478 -0.1370 0.0887  482 TYR A CZ  
1438 O OH  . TYR A 186 ? 1.6493 0.8214 0.7293 -0.5050 -0.1418 0.0862  482 TYR A OH  
1439 N N   . ALA A 187 ? 1.1789 1.2495 0.7113 -0.6867 -0.1008 0.1019  483 ALA A N   
1440 C CA  . ALA A 187 ? 1.2598 1.4851 0.8503 -0.7016 -0.0941 0.1040  483 ALA A CA  
1441 C C   . ALA A 187 ? 1.2433 1.4962 0.8320 -0.7172 -0.1008 0.1039  483 ALA A C   
1442 O O   . ALA A 187 ? 1.3116 1.4566 0.8319 -0.7338 -0.1113 0.1047  483 ALA A O   
1443 C CB  . ALA A 187 ? 1.3707 1.6260 0.9101 -0.7545 -0.0916 0.1131  483 ALA A CB  
1444 N N   . GLY A 188 ? 1.2444 1.6430 0.9046 -0.7092 -0.0947 0.1030  484 GLY A N   
1445 C CA  . GLY A 188 ? 1.3137 1.7583 0.9771 -0.7254 -0.1003 0.1040  484 GLY A CA  
1446 C C   . GLY A 188 ? 1.3106 1.8749 0.9683 -0.7695 -0.0975 0.1121  484 GLY A C   
1447 O O   . GLY A 188 ? 1.2387 1.9306 0.9614 -0.7470 -0.0877 0.1106  484 GLY A O   
1448 N N   . TYR A 189 ? 1.4249 1.9491 0.9992 -0.8323 -0.1064 0.1206  485 TYR A N   
1449 C CA  . TYR A 189 ? 1.4747 2.1149 1.0357 -0.8824 -0.1057 0.1291  485 TYR A CA  
1450 C C   . TYR A 189 ? 1.4785 2.1209 1.0123 -0.9119 -0.1149 0.1324  485 TYR A C   
1451 O O   . TYR A 189 ? 1.5111 2.0229 0.9616 -0.9431 -0.1254 0.1352  485 TYR A O   
1452 C CB  . TYR A 189 ? 1.5813 2.1802 1.0513 -0.9472 -0.1086 0.1382  485 TYR A CB  
1453 C CG  . TYR A 189 ? 1.4867 2.0179 0.9467 -0.9293 -0.1040 0.1358  485 TYR A CG  
1454 C CD1 . TYR A 189 ? 1.5449 1.9030 0.9261 -0.9346 -0.1116 0.1351  485 TYR A CD1 
1455 C CD2 . TYR A 189 ? 1.4595 2.0981 0.9817 -0.9067 -0.0923 0.1342  485 TYR A CD2 
1456 C CE1 . TYR A 189 ? 1.6010 1.8968 0.9688 -0.9191 -0.1079 0.1334  485 TYR A CE1 
1457 C CE2 . TYR A 189 ? 1.4450 2.0216 0.9558 -0.8935 -0.0881 0.1327  485 TYR A CE2 
1458 C CZ  . TYR A 189 ? 1.5022 1.9085 0.9367 -0.9009 -0.0960 0.1326  485 TYR A CZ  
1459 O OH  . TYR A 189 ? 1.5081 1.8509 0.9280 -0.8871 -0.0923 0.1315  485 TYR A OH  
1460 N N   . LYS A 190 ? 1.4190 2.2069 1.0170 -0.9007 -0.1112 0.1323  486 LYS A N   
1461 C CA  . LYS A 190 ? 1.5467 2.3601 1.1106 -0.9442 -0.1196 0.1383  486 LYS A CA  
1462 C C   . LYS A 190 ? 1.6759 2.5031 1.1500 -1.0296 -0.1240 0.1512  486 LYS A C   
1463 O O   . LYS A 190 ? 1.7746 2.5816 1.2118 -1.0527 -0.1215 0.1544  486 LYS A O   
1464 C CB  . LYS A 190 ? 1.4915 2.4584 1.1463 -0.9051 -0.1150 0.1343  486 LYS A CB  
1465 C CG  . LYS A 190 ? 1.4614 2.5910 1.1685 -0.8927 -0.1041 0.1357  486 LYS A CG  
1466 C CD  . LYS A 190 ? 1.3455 2.5318 1.1512 -0.8037 -0.0950 0.1237  486 LYS A CD  
1467 C CE  . LYS A 190 ? 1.2971 2.6656 1.1592 -0.7801 -0.0877 0.1238  486 LYS A CE  
1468 N NZ  . LYS A 190 ? 1.1696 2.5785 1.1145 -0.6905 -0.0803 0.1116  486 LYS A NZ  
1469 N N   . GLN A 191 ? 1.7009 2.5627 1.1359 -1.0800 -0.1315 0.1586  487 GLN A N   
1470 C CA  . GLN A 191 ? 1.7898 2.6416 1.1216 -1.1698 -0.1385 0.1712  487 GLN A CA  
1471 C C   . GLN A 191 ? 1.7898 2.8263 1.1485 -1.2045 -0.1364 0.1786  487 GLN A C   
1472 O O   . GLN A 191 ? 1.7045 2.8649 1.1589 -1.1532 -0.1300 0.1734  487 GLN A O   
1473 C CB  . GLN A 191 ? 1.9125 2.5964 1.1352 -1.2138 -0.1522 0.1751  487 GLN A CB  
1474 C CG  . GLN A 191 ? 1.9362 2.4341 1.0909 -1.2023 -0.1560 0.1712  487 GLN A CG  
1475 C CD  . GLN A 191 ? 1.9947 2.4869 1.1038 -1.2346 -0.1538 0.1751  487 GLN A CD  
1476 O OE1 . GLN A 191 ? 2.1546 2.6500 1.1754 -1.3115 -0.1604 0.1850  487 GLN A OE1 
1477 N NE2 . GLN A 191 ? 1.8981 2.3822 1.0648 -1.1784 -0.1450 0.1673  487 GLN A NE2 
1478 N N   . PRO A 192 ? 1.8767 2.9410 1.1513 -1.2894 -0.1420 0.1905  488 PRO A N   
1479 C CA  . PRO A 192 ? 1.8953 3.1335 1.1873 -1.3279 -0.1418 0.1986  488 PRO A CA  
1480 C C   . PRO A 192 ? 1.8999 3.1329 1.1925 -1.3335 -0.1488 0.1999  488 PRO A C   
1481 O O   . PRO A 192 ? 1.8700 3.2582 1.2302 -1.3169 -0.1452 0.2002  488 PRO A O   
1482 C CB  . PRO A 192 ? 2.0664 3.2972 1.2467 -1.4268 -0.1491 0.2111  488 PRO A CB  
1483 C CG  . PRO A 192 ? 2.1590 3.1714 1.2406 -1.4466 -0.1574 0.2101  488 PRO A CG  
1484 C CD  . PRO A 192 ? 2.0304 2.9839 1.1919 -1.3534 -0.1488 0.1969  488 PRO A CD  
1485 N N   . ASP A 193 ? 1.9739 3.0301 1.1899 -1.3536 -0.1591 0.2002  489 ASP A N   
1486 C CA  . ASP A 193 ? 1.9224 2.9535 1.1309 -1.3601 -0.1670 0.2008  489 ASP A CA  
1487 C C   . ASP A 193 ? 1.7954 2.8207 1.1060 -1.2674 -0.1630 0.1870  489 ASP A C   
1488 O O   . ASP A 193 ? 1.7899 2.7697 1.0942 -1.2648 -0.1706 0.1852  489 ASP A O   
1489 C CB  . ASP A 193 ? 2.0612 2.8975 1.1341 -1.4190 -0.1805 0.2067  489 ASP A CB  
1490 C CG  . ASP A 193 ? 2.0708 2.7287 1.1077 -1.3823 -0.1810 0.1990  489 ASP A CG  
1491 O OD1 . ASP A 193 ? 2.0710 2.7183 1.0885 -1.3892 -0.1769 0.1996  489 ASP A OD1 
1492 O OD2 . ASP A 193 ? 2.0361 2.5694 1.0651 -1.3448 -0.1856 0.1920  489 ASP A OD2 
1493 N N   . GLY A 194 ? 1.7276 2.7936 1.1262 -1.1939 -0.1521 0.1770  490 GLY A N   
1494 C CA  . GLY A 194 ? 1.6841 2.7503 1.1771 -1.1068 -0.1487 0.1636  490 GLY A CA  
1495 C C   . GLY A 194 ? 1.7593 2.6531 1.2403 -1.0648 -0.1507 0.1544  490 GLY A C   
1496 O O   . GLY A 194 ? 1.7463 2.6506 1.3082 -0.9905 -0.1441 0.1432  490 GLY A O   
1497 N N   . SER A 195 ? 1.8126 2.5470 1.1878 -1.1103 -0.1601 0.1589  491 SER A N   
1498 C CA  . SER A 195 ? 1.7959 2.3637 1.1488 -1.0707 -0.1631 0.1504  491 SER A CA  
1499 C C   . SER A 195 ? 1.7946 2.3442 1.1729 -1.0361 -0.1539 0.1461  491 SER A C   
1500 O O   . SER A 195 ? 1.7853 2.4499 1.2021 -1.0394 -0.1452 0.1488  491 SER A O   
1501 C CB  . SER A 195 ? 1.8423 2.2452 1.0621 -1.1267 -0.1756 0.1568  491 SER A CB  
1502 O OG  . SER A 195 ? 1.9635 2.3341 1.0900 -1.1919 -0.1774 0.1674  491 SER A OG  
1503 N N   . THR A 196 ? 1.8349 2.2405 1.1895 -1.0016 -0.1558 0.1391  492 THR A N   
1504 C CA  . THR A 196 ? 1.7888 2.1825 1.1852 -0.9564 -0.1470 0.1331  492 THR A CA  
1505 C C   . THR A 196 ? 1.8637 2.0858 1.1595 -0.9722 -0.1522 0.1344  492 THR A C   
1506 O O   . THR A 196 ? 1.9729 2.0593 1.2058 -0.9681 -0.1609 0.1319  492 THR A O   
1507 C CB  . THR A 196 ? 1.6884 2.1076 1.1888 -0.8753 -0.1422 0.1200  492 THR A CB  
1508 O OG1 . THR A 196 ? 1.6057 2.1871 1.1959 -0.8539 -0.1370 0.1181  492 THR A OG1 
1509 C CG2 . THR A 196 ? 1.6196 2.0095 1.1536 -0.8314 -0.1341 0.1141  492 THR A CG2 
1510 N N   . LEU A 197 ? 1.8088 2.0375 1.0866 -0.9867 -0.1471 0.1378  493 LEU A N   
1511 C CA  . LEU A 197 ? 1.7869 1.8646 0.9836 -0.9874 -0.1505 0.1371  493 LEU A CA  
1512 C C   . LEU A 197 ? 1.5878 1.6658 0.8661 -0.9163 -0.1415 0.1275  493 LEU A C   
1513 O O   . LEU A 197 ? 1.4409 1.6512 0.8223 -0.8851 -0.1309 0.1243  493 LEU A O   
1514 C CB  . LEU A 197 ? 1.8374 1.9153 0.9562 -1.0510 -0.1520 0.1463  493 LEU A CB  
1515 C CG  . LEU A 197 ? 1.9246 1.8517 0.9412 -1.0640 -0.1571 0.1466  493 LEU A CG  
1516 C CD1 . LEU A 197 ? 2.0518 1.7902 0.9587 -1.0620 -0.1694 0.1445  493 LEU A CD1 
1517 C CD2 . LEU A 197 ? 1.9964 1.9523 0.9402 -1.1381 -0.1602 0.1558  493 LEU A CD2 
1518 N N   . GLY A 198 ? 1.5751 1.5041 0.8020 -0.8893 -0.1461 0.1226  494 GLY A N   
1519 C CA  . GLY A 198 ? 1.5665 1.4824 0.8553 -0.8286 -0.1388 0.1147  494 GLY A CA  
1520 C C   . GLY A 198 ? 1.5009 1.4340 0.8705 -0.7702 -0.1378 0.1046  494 GLY A C   
1521 O O   . GLY A 198 ? 1.6843 1.5469 1.0172 -0.7676 -0.1461 0.1021  494 GLY A O   
1522 N N   . ASP A 199 ? 1.2356 1.2616 0.7107 -0.7241 -0.1282 0.0985  495 ASP A N   
1523 C CA  . ASP A 199 ? 1.2032 1.2512 0.7555 -0.6693 -0.1282 0.0878  495 ASP A CA  
1524 C C   . ASP A 199 ? 1.1770 1.3789 0.8170 -0.6610 -0.1238 0.0862  495 ASP A C   
1525 O O   . ASP A 199 ? 0.9622 1.2736 0.6695 -0.6435 -0.1142 0.0855  495 ASP A O   
1526 C CB  . ASP A 199 ? 1.1413 1.1699 0.7407 -0.6188 -0.1228 0.0807  495 ASP A CB  
1527 C CG  . ASP A 199 ? 1.2074 1.2130 0.8530 -0.5685 -0.1266 0.0694  495 ASP A CG  
1528 O OD1 . ASP A 199 ? 1.1816 1.2118 0.8417 -0.5679 -0.1317 0.0664  495 ASP A OD1 
1529 O OD2 . ASP A 199 ? 1.1622 1.1253 0.8262 -0.5313 -0.1253 0.0635  495 ASP A OD2 
1530 N N   . PRO A 200 ? 1.1910 1.4045 0.8291 -0.6690 -0.1308 0.0851  496 PRO A N   
1531 C CA  . PRO A 200 ? 1.1436 1.5012 0.8620 -0.6542 -0.1275 0.0831  496 PRO A CA  
1532 C C   . PRO A 200 ? 0.9632 1.3824 0.7779 -0.5871 -0.1219 0.0723  496 PRO A C   
1533 O O   . PRO A 200 ? 0.8736 1.4165 0.7524 -0.5664 -0.1168 0.0708  496 PRO A O   
1534 C CB  . PRO A 200 ? 1.2396 1.5643 0.9258 -0.6725 -0.1382 0.0831  496 PRO A CB  
1535 C CG  . PRO A 200 ? 1.3413 1.5192 0.9139 -0.7143 -0.1458 0.0888  496 PRO A CG  
1536 C CD  . PRO A 200 ? 1.2806 1.3736 0.8362 -0.6904 -0.1421 0.0859  496 PRO A CD  
1537 N N   . ALA A 201 ? 0.9891 1.3240 0.8095 -0.5514 -0.1234 0.0647  497 ALA A N   
1538 C CA  . ALA A 201 ? 1.0144 1.4017 0.9170 -0.4919 -0.1188 0.0551  497 ALA A CA  
1539 C C   . ALA A 201 ? 0.9388 1.4232 0.8857 -0.4799 -0.1068 0.0571  497 ALA A C   
1540 O O   . ALA A 201 ? 0.8387 1.4042 0.8530 -0.4340 -0.1022 0.0508  497 ALA A O   
1541 C CB  . ALA A 201 ? 1.0733 1.3528 0.9630 -0.4652 -0.1223 0.0484  497 ALA A CB  
1542 N N   . ASN A 202 ? 1.0310 1.5048 0.9335 -0.5193 -0.1021 0.0658  498 ASN A N   
1543 C CA  . ASN A 202 ? 1.0396 1.5769 0.9728 -0.5067 -0.0908 0.0668  498 ASN A CA  
1544 C C   . ASN A 202 ? 1.0529 1.7096 0.9935 -0.5308 -0.0839 0.0736  498 ASN A C   
1545 O O   . ASN A 202 ? 1.0517 1.7632 1.0080 -0.5257 -0.0743 0.0752  498 ASN A O   
1546 C CB  . ASN A 202 ? 1.0283 1.4663 0.9047 -0.5298 -0.0903 0.0713  498 ASN A CB  
1547 C CG  . ASN A 202 ? 0.9809 1.3179 0.8576 -0.4968 -0.0954 0.0639  498 ASN A CG  
1548 O OD1 . ASN A 202 ? 0.8911 1.2608 0.8313 -0.4484 -0.0948 0.0547  498 ASN A OD1 
1549 N ND2 . ASN A 202 ? 1.0990 1.3096 0.8972 -0.5212 -0.1011 0.0680  498 ASN A ND2 
1550 N N   . VAL A 203 ? 0.9625 1.6656 0.8916 -0.5564 -0.0887 0.0774  499 VAL A N   
1551 C CA  . VAL A 203 ? 0.9366 1.7442 0.8535 -0.5939 -0.0842 0.0859  499 VAL A CA  
1552 C C   . VAL A 203 ? 0.8958 1.8320 0.8801 -0.5480 -0.0730 0.0816  499 VAL A C   
1553 O O   . VAL A 203 ? 1.0133 2.0197 0.9887 -0.5684 -0.0658 0.0871  499 VAL A O   
1554 C CB  . VAL A 203 ? 0.9965 1.8335 0.8898 -0.6287 -0.0924 0.0906  499 VAL A CB  
1555 C CG1 . VAL A 203 ? 1.1277 2.0790 1.0043 -0.6721 -0.0885 0.1001  499 VAL A CG1 
1556 C CG2 . VAL A 203 ? 1.0153 1.7144 0.8310 -0.6712 -0.1035 0.0944  499 VAL A CG2 
1557 N N   . GLN A 204 ? 0.7567 1.7217 0.8020 -0.4845 -0.0720 0.0715  500 GLN A N   
1558 C CA  . GLN A 204 ? 0.8132 1.8833 0.9100 -0.4341 -0.0617 0.0665  500 GLN A CA  
1559 C C   . GLN A 204 ? 0.8806 1.9274 0.9790 -0.4230 -0.0530 0.0652  500 GLN A C   
1560 O O   . GLN A 204 ? 0.8651 1.9972 0.9704 -0.4201 -0.0439 0.0673  500 GLN A O   
1561 C CB  . GLN A 204 ? 0.8251 1.9080 0.9727 -0.3668 -0.0638 0.0558  500 GLN A CB  
1562 C CG  . GLN A 204 ? 0.8900 2.0763 1.0762 -0.3115 -0.0541 0.0506  500 GLN A CG  
1563 C CD  . GLN A 204 ? 0.9802 2.1533 1.2035 -0.2409 -0.0563 0.0395  500 GLN A CD  
1564 O OE1 . GLN A 204 ? 0.9737 2.0548 1.2007 -0.2297 -0.0637 0.0348  500 GLN A OE1 
1565 N NE2 . GLN A 204 ? 1.0402 2.3032 1.2842 -0.1923 -0.0506 0.0354  500 GLN A NE2 
1566 N N   . PHE A 205 ? 0.8717 1.8069 0.9623 -0.4161 -0.0560 0.0617  501 PHE A N   
1567 C CA  . PHE A 205 ? 0.8222 1.7306 0.9123 -0.4076 -0.0485 0.0609  501 PHE A CA  
1568 C C   . PHE A 205 ? 0.9016 1.8186 0.9410 -0.4668 -0.0450 0.0719  501 PHE A C   
1569 O O   . PHE A 205 ? 0.8428 1.8176 0.8915 -0.4599 -0.0354 0.0726  501 PHE A O   
1570 C CB  . PHE A 205 ? 0.7927 1.5798 0.8762 -0.3962 -0.0544 0.0564  501 PHE A CB  
1571 C CG  . PHE A 205 ? 0.9394 1.7008 1.0264 -0.3829 -0.0473 0.0550  501 PHE A CG  
1572 C CD1 . PHE A 205 ? 0.9672 1.7756 1.1041 -0.3254 -0.0402 0.0458  501 PHE A CD1 
1573 C CD2 . PHE A 205 ? 1.0130 1.6965 1.0458 -0.4273 -0.0484 0.0628  501 PHE A CD2 
1574 C CE1 . PHE A 205 ? 0.9432 1.7315 1.0822 -0.3144 -0.0338 0.0443  501 PHE A CE1 
1575 C CE2 . PHE A 205 ? 1.0347 1.6970 1.0700 -0.4159 -0.0421 0.0622  501 PHE A CE2 
1576 C CZ  . PHE A 205 ? 0.9609 1.6812 1.0527 -0.3607 -0.0346 0.0529  501 PHE A CZ  
1577 N N   . THR A 206 ? 0.8998 1.7554 0.8786 -0.5257 -0.0536 0.0802  502 THR A N   
1578 C CA  . THR A 206 ? 0.9748 1.8245 0.8919 -0.5868 -0.0527 0.0909  502 THR A CA  
1579 C C   . THR A 206 ? 1.0303 2.0256 0.9654 -0.5956 -0.0455 0.0943  502 THR A C   
1580 O O   . THR A 206 ? 0.9963 2.0205 0.9090 -0.6208 -0.0401 0.0993  502 THR A O   
1581 C CB  . THR A 206 ? 0.9920 1.7492 0.8316 -0.6458 -0.0648 0.0984  502 THR A CB  
1582 O OG1 . THR A 206 ? 1.0193 1.6379 0.8352 -0.6331 -0.0716 0.0948  502 THR A OG1 
1583 C CG2 . THR A 206 ? 1.1094 1.8522 0.8732 -0.7124 -0.0661 0.1091  502 THR A CG2 
1584 N N   . GLU A 207 ? 1.0102 2.1009 0.9842 -0.5729 -0.0457 0.0914  503 GLU A N   
1585 C CA  . GLU A 207 ? 1.1162 2.3545 1.1084 -0.5732 -0.0391 0.0940  503 GLU A CA  
1586 C C   . GLU A 207 ? 1.0431 2.3399 1.0820 -0.5154 -0.0274 0.0867  503 GLU A C   
1587 O O   . GLU A 207 ? 1.0875 2.4757 1.1229 -0.5262 -0.0209 0.0901  503 GLU A O   
1588 C CB  . GLU A 207 ? 1.2078 2.5297 1.2256 -0.5590 -0.0428 0.0928  503 GLU A CB  
1589 C CG  . GLU A 207 ? 1.4253 2.7810 1.3910 -0.6325 -0.0501 0.1040  503 GLU A CG  
1590 C CD  . GLU A 207 ? 1.5603 2.8376 1.5051 -0.6517 -0.0613 0.1049  503 GLU A CD  
1591 O OE1 . GLU A 207 ? 1.5488 2.8155 1.5394 -0.5985 -0.0628 0.0963  503 GLU A OE1 
1592 O OE2 . GLU A 207 ? 1.6737 2.8961 1.5504 -0.7204 -0.0693 0.1139  503 GLU A OE2 
1593 N N   . ILE A 208 ? 0.9080 2.1519 0.9865 -0.4551 -0.0251 0.0765  504 ILE A N   
1594 C CA  . ILE A 208 ? 0.7772 2.0591 0.8909 -0.3998 -0.0145 0.0689  504 ILE A CA  
1595 C C   . ILE A 208 ? 0.7738 2.0205 0.8578 -0.4321 -0.0093 0.0739  504 ILE A C   
1596 O O   . ILE A 208 ? 0.7449 2.0715 0.8350 -0.4232 -0.0007 0.0742  504 ILE A O   
1597 C CB  . ILE A 208 ? 0.6161 1.8359 0.7682 -0.3354 -0.0154 0.0571  504 ILE A CB  
1598 C CG1 . ILE A 208 ? 0.5313 1.8121 0.7150 -0.2885 -0.0180 0.0507  504 ILE A CG1 
1599 C CG2 . ILE A 208 ? 0.5373 1.7547 0.7079 -0.2922 -0.0058 0.0502  504 ILE A CG2 
1600 C CD1 . ILE A 208 ? 0.5931 1.8126 0.8073 -0.2259 -0.0202 0.0390  504 ILE A CD1 
1601 N N   . CYS A 209 ? 0.7514 1.8758 0.7991 -0.4680 -0.0149 0.0780  505 CYS A N   
1602 C CA  . CYS A 209 ? 0.7556 1.8360 0.7641 -0.5040 -0.0112 0.0843  505 CYS A CA  
1603 C C   . CYS A 209 ? 0.8958 2.0529 0.8673 -0.5586 -0.0105 0.0937  505 CYS A C   
1604 O O   . CYS A 209 ? 1.0004 2.1989 0.9673 -0.5638 -0.0027 0.0956  505 CYS A O   
1605 C CB  . CYS A 209 ? 0.7652 1.6960 0.7237 -0.5385 -0.0199 0.0886  505 CYS A CB  
1606 S SG  . CYS A 209 ? 0.8487 1.6857 0.8446 -0.4817 -0.0220 0.0784  505 CYS A SG  
1607 N N   . ILE A 210 ? 0.9442 2.1239 0.8872 -0.6018 -0.0190 0.0997  506 ILE A N   
1608 C CA  . ILE A 210 ? 1.0562 2.3212 0.9634 -0.6573 -0.0198 0.1085  506 ILE A CA  
1609 C C   . ILE A 210 ? 1.0618 2.4858 1.0209 -0.6159 -0.0102 0.1044  506 ILE A C   
1610 O O   . ILE A 210 ? 0.9063 2.4057 0.8496 -0.6433 -0.0064 0.1092  506 ILE A O   
1611 C CB  . ILE A 210 ? 0.9614 2.2154 0.8229 -0.7135 -0.0316 0.1156  506 ILE A CB  
1612 C CG1 . ILE A 210 ? 1.0190 2.1068 0.8076 -0.7598 -0.0418 0.1204  506 ILE A CG1 
1613 C CG2 . ILE A 210 ? 1.0376 2.4043 0.8681 -0.7691 -0.0329 0.1242  506 ILE A CG2 
1614 C CD1 . ILE A 210 ? 1.2653 2.3265 0.9993 -0.8143 -0.0540 0.1269  506 ILE A CD1 
1615 N N   . GLN A 211 ? 0.9726 2.4452 0.9891 -0.5476 -0.0068 0.0952  507 GLN A N   
1616 C CA  . GLN A 211 ? 0.9401 2.5493 0.9983 -0.4960 0.0017  0.0899  507 GLN A CA  
1617 C C   . GLN A 211 ? 0.8222 2.4351 0.8902 -0.4697 0.0120  0.0863  507 GLN A C   
1618 O O   . GLN A 211 ? 0.7808 2.5049 0.8543 -0.4636 0.0179  0.0873  507 GLN A O   
1619 C CB  . GLN A 211 ? 0.9579 2.5852 1.0636 -0.4228 0.0021  0.0795  507 GLN A CB  
1620 C CG  . GLN A 211 ? 1.0849 2.7920 1.1931 -0.4326 -0.0042 0.0826  507 GLN A CG  
1621 C CD  . GLN A 211 ? 1.1357 2.9988 1.2675 -0.3905 0.0013  0.0802  507 GLN A CD  
1622 O OE1 . GLN A 211 ? 1.1170 3.0071 1.2738 -0.3258 0.0090  0.0716  507 GLN A OE1 
1623 N NE2 . GLN A 211 ? 1.1624 3.1287 1.2813 -0.4265 -0.0031 0.0877  507 GLN A NE2 
1624 N N   . GLN A 212 ? 0.8105 2.3069 0.8801 -0.4532 0.0142  0.0821  508 GLN A N   
1625 C CA  . GLN A 212 ? 0.7050 2.1903 0.7784 -0.4339 0.0241  0.0794  508 GLN A CA  
1626 C C   . GLN A 212 ? 0.7921 2.2390 0.8133 -0.5063 0.0233  0.0904  508 GLN A C   
1627 O O   . GLN A 212 ? 0.7581 2.1564 0.7722 -0.5009 0.0303  0.0899  508 GLN A O   
1628 C CB  . GLN A 212 ? 0.6409 2.0252 0.7370 -0.3845 0.0268  0.0703  508 GLN A CB  
1629 C CG  . GLN A 212 ? 0.6849 2.0942 0.8260 -0.3084 0.0273  0.0579  508 GLN A CG  
1630 C CD  . GLN A 212 ? 0.7672 2.2957 0.9292 -0.2560 0.0350  0.0518  508 GLN A CD  
1631 O OE1 . GLN A 212 ? 0.8515 2.4325 1.0053 -0.2602 0.0428  0.0537  508 GLN A OE1 
1632 N NE2 . GLN A 212 ? 0.7784 2.3467 0.9629 -0.2046 0.0322  0.0446  508 GLN A NE2 
1633 N N   . GLY A 213 ? 0.8392 2.3013 0.8179 -0.5745 0.0145  0.1002  509 GLY A N   
1634 C CA  . GLY A 213 ? 0.9966 2.4306 0.9170 -0.6453 0.0122  0.1102  509 GLY A CA  
1635 C C   . GLY A 213 ? 1.0552 2.3271 0.9145 -0.6931 0.0036  0.1160  509 GLY A C   
1636 O O   . GLY A 213 ? 1.1132 2.3386 0.9170 -0.7452 0.0020  0.1232  509 GLY A O   
1637 N N   . TRP A 214 ? 1.1105 2.2907 0.9732 -0.6755 -0.0026 0.1127  510 TRP A N   
1638 C CA  . TRP A 214 ? 1.2048 2.2298 0.9977 -0.7210 -0.0128 0.1185  510 TRP A CA  
1639 C C   . TRP A 214 ? 1.3155 2.3387 1.0372 -0.7985 -0.0240 0.1276  510 TRP A C   
1640 O O   . TRP A 214 ? 1.2963 2.4035 1.0301 -0.8096 -0.0280 0.1284  510 TRP A O   
1641 C CB  . TRP A 214 ? 1.1239 2.0606 0.9341 -0.6868 -0.0182 0.1131  510 TRP A CB  
1642 C CG  . TRP A 214 ? 1.1762 1.9435 0.9134 -0.7184 -0.0279 0.1176  510 TRP A CG  
1643 C CD1 . TRP A 214 ? 1.1528 1.8248 0.8528 -0.7228 -0.0259 0.1205  510 TRP A CD1 
1644 C CD2 . TRP A 214 ? 1.3089 1.9786 0.9954 -0.7448 -0.0414 0.1197  510 TRP A CD2 
1645 N NE1 . TRP A 214 ? 1.2021 1.7207 0.8285 -0.7465 -0.0379 0.1238  510 TRP A NE1 
1646 C CE2 . TRP A 214 ? 1.3260 1.8396 0.9420 -0.7601 -0.0476 0.1229  510 TRP A CE2 
1647 C CE3 . TRP A 214 ? 1.3714 2.0683 1.0608 -0.7550 -0.0487 0.1192  510 TRP A CE3 
1648 C CZ2 . TRP A 214 ? 1.4653 1.8476 1.0112 -0.7811 -0.0610 0.1244  510 TRP A CZ2 
1649 C CZ3 . TRP A 214 ? 1.4170 1.9860 1.0401 -0.7807 -0.0614 0.1214  510 TRP A CZ3 
1650 C CH2 . TRP A 214 ? 1.4724 1.8850 1.0235 -0.7915 -0.0676 0.1234  510 TRP A CH2 
1651 N N   . LYS A 215 ? 1.3907 2.3190 1.0336 -0.8524 -0.0294 0.1343  511 LYS A N   
1652 C CA  . LYS A 215 ? 1.5070 2.4065 1.0645 -0.9315 -0.0421 0.1423  511 LYS A CA  
1653 C C   . LYS A 215 ? 1.4911 2.2351 0.9876 -0.9451 -0.0548 0.1428  511 LYS A C   
1654 O O   . LYS A 215 ? 1.4953 2.0953 0.9468 -0.9388 -0.0580 0.1424  511 LYS A O   
1655 C CB  . LYS A 215 ? 1.6479 2.5202 1.1442 -0.9814 -0.0420 0.1482  511 LYS A CB  
1656 C CG  . LYS A 215 ? 1.6251 2.6298 1.1873 -0.9519 -0.0268 0.1466  511 LYS A CG  
1657 C CD  . LYS A 215 ? 1.6655 2.8458 1.2509 -0.9777 -0.0257 0.1492  511 LYS A CD  
1658 C CE  . LYS A 215 ? 1.5628 2.8843 1.2485 -0.9047 -0.0155 0.1417  511 LYS A CE  
1659 N NZ  . LYS A 215 ? 1.5823 3.0831 1.2933 -0.9172 -0.0116 0.1440  511 LYS A NZ  
1660 N N   . ALA A 216 ? 1.4573 2.2310 0.9513 -0.9595 -0.0620 0.1435  512 ALA A N   
1661 C CA  . ALA A 216 ? 1.3758 2.0161 0.8260 -0.9594 -0.0725 0.1425  512 ALA A CA  
1662 C C   . ALA A 216 ? 1.5436 2.0491 0.8643 -1.0300 -0.0868 0.1488  512 ALA A C   
1663 O O   . ALA A 216 ? 1.6319 2.1879 0.9022 -1.0940 -0.0919 0.1551  512 ALA A O   
1664 C CB  . ALA A 216 ? 1.3387 2.0594 0.8320 -0.9485 -0.0744 0.1412  512 ALA A CB  
1665 N N   . PRO A 217 ? 1.5960 1.9284 0.8543 -1.0196 -0.0941 0.1467  513 PRO A N   
1666 C CA  . PRO A 217 ? 1.8082 1.9964 0.9303 -1.0802 -0.1095 0.1508  513 PRO A CA  
1667 C C   . PRO A 217 ? 1.9922 2.1483 1.0714 -1.1045 -0.1202 0.1524  513 PRO A C   
1668 O O   . PRO A 217 ? 2.1395 2.1480 1.1022 -1.1392 -0.1336 0.1537  513 PRO A O   
1669 C CB  . PRO A 217 ? 1.8010 1.8217 0.8786 -1.0434 -0.1119 0.1466  513 PRO A CB  
1670 C CG  . PRO A 217 ? 1.6445 1.7420 0.8335 -0.9796 -0.0964 0.1430  513 PRO A CG  
1671 C CD  . PRO A 217 ? 1.5136 1.7741 0.8122 -0.9540 -0.0881 0.1408  513 PRO A CD  
1672 N N   . ARG A 218 ? 1.9387 2.2288 1.1075 -1.0840 -0.1144 0.1519  514 ARG A N   
1673 C CA  . ARG A 218 ? 1.9158 2.2075 1.0690 -1.1000 -0.1218 0.1537  514 ARG A CA  
1674 C C   . ARG A 218 ? 1.9720 2.0767 1.0039 -1.1253 -0.1366 0.1544  514 ARG A C   
1675 O O   . ARG A 218 ? 2.0757 2.1487 1.0144 -1.1914 -0.1473 0.1609  514 ARG A O   
1676 C CB  . ARG A 218 ? 2.0075 2.4414 1.1587 -1.1585 -0.1226 0.1614  514 ARG A CB  
1677 C CG  . ARG A 218 ? 1.8999 2.5293 1.1788 -1.1176 -0.1086 0.1591  514 ARG A CG  
1678 C CD  . ARG A 218 ? 1.9384 2.7122 1.2271 -1.1592 -0.1102 0.1656  514 ARG A CD  
1679 N NE  . ARG A 218 ? 1.7986 2.6907 1.1972 -1.0983 -0.1017 0.1603  514 ARG A NE  
1680 C CZ  . ARG A 218 ? 1.7375 2.7421 1.2361 -1.0365 -0.0888 0.1540  514 ARG A CZ  
1681 N NH1 . ARG A 218 ? 1.6524 2.7477 1.2359 -0.9819 -0.0833 0.1485  514 ARG A NH1 
1682 N NH2 . ARG A 218 ? 1.7785 2.7991 1.2876 -1.0277 -0.0819 0.1527  514 ARG A NH2 
1683 N N   . GLY A 219 ? 1.8038 1.7844 0.8313 -1.0719 -0.1374 0.1476  515 GLY A N   
1684 C CA  . GLY A 219 ? 1.9982 1.8055 0.9240 -1.0741 -0.1501 0.1459  515 GLY A CA  
1685 C C   . GLY A 219 ? 1.8829 1.6757 0.8786 -1.0079 -0.1475 0.1389  515 GLY A C   
1686 O O   . GLY A 219 ? 1.6749 1.5994 0.7854 -0.9774 -0.1387 0.1367  515 GLY A O   
1687 N N   . ARG A 220 ? 1.9749 1.6027 0.8956 -0.9827 -0.1558 0.1342  516 ARG A N   
1688 C CA  . ARG A 220 ? 2.0131 1.6073 0.9824 -0.9225 -0.1554 0.1269  516 ARG A CA  
1689 C C   . ARG A 220 ? 1.9675 1.5707 1.0199 -0.8547 -0.1462 0.1198  516 ARG A C   
1690 O O   . ARG A 220 ? 1.9427 1.6726 1.1170 -0.8226 -0.1360 0.1169  516 ARG A O   
1691 C CB  . ARG A 220 ? 2.2424 1.6567 1.0854 -0.9229 -0.1687 0.1247  516 ARG A CB  
1692 C CG  . ARG A 220 ? 2.1947 1.5744 1.0793 -0.8644 -0.1692 0.1169  516 ARG A CG  
1693 C CD  . ARG A 220 ? 2.2496 1.6517 1.1202 -0.8943 -0.1750 0.1199  516 ARG A CD  
1694 N NE  . ARG A 220 ? 2.4061 1.6423 1.1526 -0.8926 -0.1870 0.1180  516 ARG A NE  
1695 C CZ  . ARG A 220 ? 2.4359 1.6539 1.1631 -0.8997 -0.1928 0.1182  516 ARG A CZ  
1696 N NH1 . ARG A 220 ? 2.3361 1.6923 1.1617 -0.9096 -0.1883 0.1199  516 ARG A NH1 
1697 N NH2 . ARG A 220 ? 2.5830 1.6436 1.1895 -0.8937 -0.2031 0.1162  516 ARG A NH2 
1698 N N   . PHE A 221 ? 1.9775 1.4425 0.9576 -0.8314 -0.1504 0.1167  517 PHE A N   
1699 C CA  . PHE A 221 ? 1.8471 1.2971 0.8875 -0.7669 -0.1436 0.1107  517 PHE A CA  
1700 C C   . PHE A 221 ? 1.8321 1.3469 0.9094 -0.7743 -0.1343 0.1145  517 PHE A C   
1701 O O   . PHE A 221 ? 1.9052 1.3315 0.9342 -0.7576 -0.1350 0.1142  517 PHE A O   
1702 C CB  . PHE A 221 ? 1.9085 1.1814 0.8514 -0.7298 -0.1526 0.1052  517 PHE A CB  
1703 C CG  . PHE A 221 ? 1.8947 1.0932 0.7858 -0.7224 -0.1618 0.1013  517 PHE A CG  
1704 C CD1 . PHE A 221 ? 1.9497 1.0165 0.6989 -0.7518 -0.1738 0.1022  517 PHE A CD1 
1705 C CD2 . PHE A 221 ? 1.6802 0.9355 0.6587 -0.6853 -0.1588 0.0959  517 PHE A CD2 
1706 C CE1 . PHE A 221 ? 2.1025 1.0983 0.7987 -0.7437 -0.1817 0.0991  517 PHE A CE1 
1707 C CE2 . PHE A 221 ? 1.7892 0.9748 0.7181 -0.6777 -0.1668 0.0923  517 PHE A CE2 
1708 C CZ  . PHE A 221 ? 1.8940 0.9522 0.6833 -0.7062 -0.1778 0.0945  517 PHE A CZ  
1709 N N   . ASP A 222 ? 1.7618 1.4371 0.9246 -0.7966 -0.1253 0.1180  518 ASP A N   
1710 C CA  . ASP A 222 ? 1.6589 1.4225 0.8733 -0.7990 -0.1144 0.1209  518 ASP A CA  
1711 C C   . ASP A 222 ? 1.6015 1.4241 0.9252 -0.7361 -0.1039 0.1155  518 ASP A C   
1712 O O   . ASP A 222 ? 1.4375 1.3533 0.8500 -0.7103 -0.0999 0.1106  518 ASP A O   
1713 C CB  . ASP A 222 ? 1.5868 1.5006 0.8386 -0.8445 -0.1094 0.1259  518 ASP A CB  
1714 C CG  . ASP A 222 ? 1.7121 1.5752 0.8516 -0.9159 -0.1204 0.1322  518 ASP A CG  
1715 O OD1 . ASP A 222 ? 1.8258 1.5301 0.8548 -0.9277 -0.1321 0.1316  518 ASP A OD1 
1716 O OD2 . ASP A 222 ? 1.6260 1.6078 0.7827 -0.9592 -0.1178 0.1372  518 ASP A OD2 
1717 N N   . VAL A 223 ? 1.5129 1.2794 0.8256 -0.7124 -0.1002 0.1163  519 VAL A N   
1718 C CA  . VAL A 223 ? 1.4025 1.2128 0.8054 -0.6576 -0.0914 0.1122  519 VAL A CA  
1719 C C   . VAL A 223 ? 1.3000 1.2820 0.8018 -0.6583 -0.0778 0.1121  519 VAL A C   
1720 O O   . VAL A 223 ? 1.2919 1.3154 0.7791 -0.6857 -0.0716 0.1178  519 VAL A O   
1721 C CB  . VAL A 223 ? 1.4573 1.1525 0.8078 -0.6331 -0.0918 0.1155  519 VAL A CB  
1722 C CG1 . VAL A 223 ? 1.3027 1.0301 0.7361 -0.5788 -0.0853 0.1121  519 VAL A CG1 
1723 C CG2 . VAL A 223 ? 1.5970 1.1183 0.8291 -0.6288 -0.1058 0.1146  519 VAL A CG2 
1724 N N   . LEU A 224 ? 1.1238 1.2036 0.7224 -0.6232 -0.0736 0.1044  520 LEU A N   
1725 C CA  . LEU A 224 ? 1.0837 1.3231 0.7710 -0.6103 -0.0612 0.1018  520 LEU A CA  
1726 C C   . LEU A 224 ? 1.0596 1.3190 0.7771 -0.5861 -0.0506 0.1022  520 LEU A C   
1727 O O   . LEU A 224 ? 1.0073 1.1720 0.7042 -0.5664 -0.0531 0.1027  520 LEU A O   
1728 C CB  . LEU A 224 ? 0.8296 1.1498 0.6024 -0.5691 -0.0610 0.0916  520 LEU A CB  
1729 C CG  . LEU A 224 ? 0.9349 1.2612 0.6903 -0.5905 -0.0693 0.0918  520 LEU A CG  
1730 C CD1 . LEU A 224 ? 0.7961 1.1053 0.5992 -0.5459 -0.0747 0.0818  520 LEU A CD1 
1731 C CD2 . LEU A 224 ? 0.8516 1.3192 0.6417 -0.6054 -0.0630 0.0938  520 LEU A CD2 
1732 N N   . PRO A 225 ? 0.9829 1.3660 0.7464 -0.5843 -0.0386 0.1021  521 PRO A N   
1733 C CA  . PRO A 225 ? 1.0675 1.4809 0.8636 -0.5574 -0.0268 0.1016  521 PRO A CA  
1734 C C   . PRO A 225 ? 0.9884 1.4688 0.8756 -0.4966 -0.0230 0.0889  521 PRO A C   
1735 O O   . PRO A 225 ? 1.0029 1.5346 0.9361 -0.4730 -0.0269 0.0806  521 PRO A O   
1736 C CB  . PRO A 225 ? 1.1203 1.6412 0.9205 -0.5800 -0.0167 0.1052  521 PRO A CB  
1737 C CG  . PRO A 225 ? 1.0565 1.6605 0.8800 -0.5886 -0.0209 0.1021  521 PRO A CG  
1738 C CD  . PRO A 225 ? 1.0812 1.5777 0.8564 -0.6098 -0.0355 0.1037  521 PRO A CD  
1739 N N   . LEU A 226 ? 0.9385 1.3940 0.8361 -0.4524 -0.0178 0.0840  522 LEU A N   
1740 C CA  . LEU A 226 ? 0.7920 1.2887 0.7579 -0.3806 -0.0161 0.0682  522 LEU A CA  
1741 C C   . LEU A 226 ? 0.7057 1.3529 0.7310 -0.3676 -0.0032 0.0638  522 LEU A C   
1742 O O   . LEU A 226 ? 0.7253 1.4363 0.7415 -0.3918 0.0089  0.0706  522 LEU A O   
1743 C CB  . LEU A 226 ? 0.7400 1.1620 0.6903 -0.3378 -0.0162 0.0633  522 LEU A CB  
1744 C CG  . LEU A 226 ? 0.8006 1.0915 0.7126 -0.3186 -0.0294 0.0622  522 LEU A CG  
1745 C CD1 . LEU A 226 ? 0.6863 0.9281 0.5789 -0.2861 -0.0286 0.0603  522 LEU A CD1 
1746 C CD2 . LEU A 226 ? 0.7549 1.0450 0.7126 -0.2808 -0.0370 0.0506  522 LEU A CD2 
1747 N N   . LEU A 227 ? 0.5516 1.2553 0.6328 -0.3269 -0.0056 0.0527  523 LEU A N   
1748 C CA  . LEU A 227 ? 0.5590 1.3904 0.6915 -0.2914 0.0052  0.0454  523 LEU A CA  
1749 C C   . LEU A 227 ? 0.5229 1.3192 0.6779 -0.2203 0.0051  0.0303  523 LEU A C   
1750 O O   . LEU A 227 ? 0.6165 1.3677 0.7876 -0.1895 -0.0046 0.0222  523 LEU A O   
1751 C CB  . LEU A 227 ? 0.5769 1.4574 0.7238 -0.2846 0.0006  0.0436  523 LEU A CB  
1752 C CG  . LEU A 227 ? 0.6015 1.5885 0.7474 -0.2909 0.0083  0.0468  523 LEU A CG  
1753 C CD1 . LEU A 227 ? 0.6262 1.6752 0.8086 -0.2379 0.0072  0.0373  523 LEU A CD1 
1754 C CD2 . LEU A 227 ? 0.5469 1.5882 0.6869 -0.2874 0.0216  0.0480  523 LEU A CD2 
1755 N N   . LEU A 228 ? 0.5585 1.3707 0.7080 -0.1970 0.0156  0.0266  524 LEU A N   
1756 C CA  . LEU A 228 ? 0.5520 1.3059 0.7035 -0.1403 0.0139  0.0131  524 LEU A CA  
1757 C C   . LEU A 228 ? 0.5706 1.4125 0.7454 -0.0920 0.0254  0.0025  524 LEU A C   
1758 O O   . LEU A 228 ? 0.6007 1.5147 0.7700 -0.0994 0.0390  0.0059  524 LEU A O   
1759 C CB  . LEU A 228 ? 0.6018 1.2712 0.7118 -0.1515 0.0133  0.0166  524 LEU A CB  
1760 C CG  . LEU A 228 ? 0.6098 1.1877 0.6834 -0.1934 0.0026  0.0278  524 LEU A CG  
1761 C CD1 . LEU A 228 ? 0.5892 1.0887 0.6183 -0.1967 0.0011  0.0317  524 LEU A CD1 
1762 C CD2 . LEU A 228 ? 0.5728 1.0929 0.6607 -0.1771 -0.0109 0.0224  524 LEU A CD2 
1763 N N   . GLN A 229 ? 0.4843 1.3131 0.6774 -0.0410 0.0202  -0.0101 525 GLN A N   
1764 C CA  . GLN A 229 ? 0.5591 1.4364 0.7581 0.0179  0.0282  -0.0229 525 GLN A CA  
1765 C C   . GLN A 229 ? 0.6639 1.4390 0.8350 0.0513  0.0238  -0.0348 525 GLN A C   
1766 O O   . GLN A 229 ? 0.7291 1.4151 0.8957 0.0527  0.0111  -0.0381 525 GLN A O   
1767 C CB  . GLN A 229 ? 0.4852 1.4100 0.7105 0.0523  0.0241  -0.0283 525 GLN A CB  
1768 C CG  . GLN A 229 ? 0.4069 1.3096 0.6183 0.1235  0.0249  -0.0444 525 GLN A CG  
1769 C CD  . GLN A 229 ? 0.4960 1.4026 0.7154 0.1555  0.0168  -0.0480 525 GLN A CD  
1770 O OE1 . GLN A 229 ? 0.4984 1.3924 0.7351 0.1257  0.0074  -0.0409 525 GLN A OE1 
1771 N NE2 . GLN A 229 ? 0.5173 1.4219 0.7101 0.2152  0.0193  -0.0584 525 GLN A NE2 
1772 N N   . ALA A 230 ? 0.5109 1.3043 0.6616 0.0762  0.0343  -0.0414 526 ALA A N   
1773 C CA  . ALA A 230 ? 0.6236 1.3271 0.7406 0.1020  0.0302  -0.0529 526 ALA A CA  
1774 C C   . ALA A 230 ? 0.6481 1.3668 0.7461 0.1645  0.0363  -0.0686 526 ALA A C   
1775 O O   . ALA A 230 ? 0.5503 1.3625 0.6506 0.1861  0.0507  -0.0695 526 ALA A O   
1776 C CB  . ALA A 230 ? 0.6333 1.3232 0.7265 0.0744  0.0356  -0.0472 526 ALA A CB  
1777 N N   . ASN A 231 ? 0.7085 1.3329 0.7808 0.1929  0.0255  -0.0807 527 ASN A N   
1778 C CA  . ASN A 231 ? 0.7580 1.3599 0.7920 0.2536  0.0281  -0.0970 527 ASN A CA  
1779 C C   . ASN A 231 ? 0.7178 1.4209 0.7676 0.2946  0.0380  -0.0979 527 ASN A C   
1780 O O   . ASN A 231 ? 0.6895 1.4448 0.7176 0.3378  0.0506  -0.1054 527 ASN A O   
1781 C CB  . ASN A 231 ? 0.8728 1.4491 0.8633 0.2681  0.0349  -0.1058 527 ASN A CB  
1782 C CG  . ASN A 231 ? 1.0041 1.4941 0.9341 0.3192  0.0301  -0.1244 527 ASN A CG  
1783 O OD1 . ASN A 231 ? 1.1075 1.5094 1.0205 0.3196  0.0161  -0.1293 527 ASN A OD1 
1784 N ND2 . ASN A 231 ? 1.0210 1.5324 0.9115 0.3618  0.0420  -0.1348 527 ASN A ND2 
1785 N N   . GLY A 232 ? 0.7181 1.4547 0.8052 0.2826  0.0320  -0.0901 528 GLY A N   
1786 C CA  . GLY A 232 ? 0.7845 1.6109 0.8852 0.3190  0.0365  -0.0894 528 GLY A CA  
1787 C C   . GLY A 232 ? 0.8250 1.7660 0.9426 0.2971  0.0465  -0.0774 528 GLY A C   
1788 O O   . GLY A 232 ? 0.9003 1.8967 1.0145 0.3176  0.0449  -0.0739 528 GLY A O   
1789 N N   . ASN A 233 ? 0.8204 1.7994 0.9521 0.2549  0.0562  -0.0707 529 ASN A N   
1790 C CA  . ASN A 233 ? 0.8223 1.9043 0.9614 0.2307  0.0655  -0.0595 529 ASN A CA  
1791 C C   . ASN A 233 ? 0.7846 1.9222 0.9572 0.1712  0.0606  -0.0432 529 ASN A C   
1792 O O   . ASN A 233 ? 0.7922 1.8839 0.9838 0.1425  0.0515  -0.0395 529 ASN A O   
1793 C CB  . ASN A 233 ? 0.7882 1.8758 0.9156 0.2091  0.0783  -0.0586 529 ASN A CB  
1794 C CG  . ASN A 233 ? 0.8142 1.8745 0.8977 0.2687  0.0851  -0.0735 529 ASN A CG  
1795 O OD1 . ASN A 233 ? 0.9352 2.0630 1.0066 0.2844  0.0921  -0.0713 529 ASN A OD1 
1796 N ND2 . ASN A 233 ? 0.7707 1.7280 0.8251 0.3008  0.0815  -0.0891 529 ASN A ND2 
1797 N N   . ASP A 234 ? 0.7790 2.0138 0.9536 0.1527  0.0656  -0.0339 530 ASP A N   
1798 C CA  . ASP A 234 ? 0.7856 2.0701 0.9793 0.0922  0.0609  -0.0193 530 ASP A CA  
1799 C C   . ASP A 234 ? 0.7198 1.9536 0.9184 0.0255  0.0607  -0.0098 530 ASP A C   
1800 O O   . ASP A 234 ? 0.8067 2.0231 0.9932 0.0135  0.0695  -0.0093 530 ASP A O   
1801 C CB  . ASP A 234 ? 0.8266 2.2280 1.0160 0.0795  0.0662  -0.0114 530 ASP A CB  
1802 C CG  . ASP A 234 ? 0.9487 2.4085 1.1298 0.1462  0.0648  -0.0190 530 ASP A CG  
1803 O OD1 . ASP A 234 ? 1.0419 2.6058 1.2189 0.1478  0.0688  -0.0143 530 ASP A OD1 
1804 O OD2 . ASP A 234 ? 1.1019 2.5024 1.2762 0.1974  0.0590  -0.0293 530 ASP A OD2 
1805 N N   . PRO A 235 ? 0.5536 1.7566 0.7632 -0.0165 0.0507  -0.0021 531 PRO A N   
1806 C CA  . PRO A 235 ? 0.5436 1.6816 0.7480 -0.0744 0.0480  0.0068  531 PRO A CA  
1807 C C   . PRO A 235 ? 0.6103 1.7862 0.7921 -0.1388 0.0532  0.0215  531 PRO A C   
1808 O O   . PRO A 235 ? 0.6915 1.9529 0.8687 -0.1477 0.0560  0.0258  531 PRO A O   
1809 C CB  . PRO A 235 ? 0.4452 1.5368 0.6613 -0.0905 0.0339  0.0090  531 PRO A CB  
1810 C CG  . PRO A 235 ? 0.4951 1.6609 0.7170 -0.0742 0.0323  0.0089  531 PRO A CG  
1811 C CD  . PRO A 235 ? 0.5349 1.7501 0.7564 -0.0093 0.0405  -0.0018 531 PRO A CD  
1812 N N   . GLU A 236 ? 0.6194 1.7267 0.7817 -0.1852 0.0531  0.0297  532 GLU A N   
1813 C CA  . GLU A 236 ? 0.7210 1.8381 0.8472 -0.2445 0.0587  0.0435  532 GLU A CA  
1814 C C   . GLU A 236 ? 0.6226 1.6436 0.7154 -0.3069 0.0494  0.0558  532 GLU A C   
1815 O O   . GLU A 236 ? 0.6007 1.5427 0.6992 -0.2985 0.0428  0.0532  532 GLU A O   
1816 C CB  . GLU A 236 ? 0.7634 1.8853 0.8768 -0.2266 0.0735  0.0411  532 GLU A CB  
1817 C CG  . GLU A 236 ? 0.8418 2.0485 0.9730 -0.1648 0.0826  0.0289  532 GLU A CG  
1818 C CD  . GLU A 236 ? 0.9179 2.0925 1.0419 -0.1189 0.0940  0.0179  532 GLU A CD  
1819 O OE1 . GLU A 236 ? 0.9032 2.0225 0.9949 -0.1491 0.0994  0.0248  532 GLU A OE1 
1820 O OE2 . GLU A 236 ? 0.9343 2.1215 1.0721 -0.0510 0.0951  0.0021  532 GLU A OE2 
1821 N N   . LEU A 237 ? 0.6676 1.6904 0.7187 -0.3686 0.0472  0.0689  533 LEU A N   
1822 C CA  . LEU A 237 ? 0.7233 1.6435 0.7254 -0.4272 0.0357  0.0802  533 LEU A CA  
1823 C C   . LEU A 237 ? 0.7937 1.6183 0.7441 -0.4545 0.0397  0.0899  533 LEU A C   
1824 O O   . LEU A 237 ? 0.8827 1.7344 0.8134 -0.4627 0.0505  0.0940  533 LEU A O   
1825 C CB  . LEU A 237 ? 0.7750 1.7306 0.7433 -0.4817 0.0290  0.0886  533 LEU A CB  
1826 C CG  . LEU A 237 ? 0.8256 1.8399 0.8266 -0.4661 0.0216  0.0832  533 LEU A CG  
1827 C CD1 . LEU A 237 ? 0.9537 2.0383 0.9263 -0.5159 0.0180  0.0909  533 LEU A CD1 
1828 C CD2 . LEU A 237 ? 0.7456 1.6596 0.7388 -0.4700 0.0095  0.0824  533 LEU A CD2 
1829 N N   . PHE A 238 ? 0.7996 1.5050 0.7214 -0.4649 0.0297  0.0937  534 PHE A N   
1830 C CA  . PHE A 238 ? 0.9249 1.4966 0.7735 -0.4768 0.0250  0.1014  534 PHE A CA  
1831 C C   . PHE A 238 ? 0.9658 1.4123 0.7573 -0.5088 0.0086  0.1084  534 PHE A C   
1832 O O   . PHE A 238 ? 0.8876 1.3075 0.7075 -0.4803 -0.0020 0.0992  534 PHE A O   
1833 C CB  . PHE A 238 ? 0.8577 1.3751 0.7212 -0.4056 0.0223  0.0886  534 PHE A CB  
1834 C CG  . PHE A 238 ? 0.8655 1.4896 0.7883 -0.3577 0.0348  0.0760  534 PHE A CG  
1835 C CD1 . PHE A 238 ? 0.8966 1.5760 0.8829 -0.3103 0.0330  0.0612  534 PHE A CD1 
1836 C CD2 . PHE A 238 ? 0.8361 1.4954 0.7422 -0.3571 0.0479  0.0785  534 PHE A CD2 
1837 C CE1 . PHE A 238 ? 0.8904 1.6514 0.9163 -0.2612 0.0437  0.0489  534 PHE A CE1 
1838 C CE2 . PHE A 238 ? 0.8277 1.5756 0.7781 -0.3084 0.0594  0.0656  534 PHE A CE2 
1839 C CZ  . PHE A 238 ? 0.7500 1.5445 0.7571 -0.2591 0.0570  0.0505  534 PHE A CZ  
1840 N N   . GLN A 239 ? 1.1103 1.4713 0.8136 -0.5649 0.0067  0.1243  535 GLN A N   
1841 C CA  . GLN A 239 ? 1.2214 1.4446 0.8480 -0.5960 -0.0087 0.1317  535 GLN A CA  
1842 C C   . GLN A 239 ? 1.2442 1.3236 0.8175 -0.5508 -0.0183 0.1305  535 GLN A C   
1843 O O   . GLN A 239 ? 1.3691 1.3989 0.8865 -0.5586 -0.0147 0.1394  535 GLN A O   
1844 C CB  . GLN A 239 ? 1.4547 1.6500 1.0084 -0.6542 -0.0162 0.1366  535 GLN A CB  
1845 C CG  . GLN A 239 ? 1.6476 1.6754 1.0994 -0.6763 -0.0335 0.1406  535 GLN A CG  
1846 C CD  . GLN A 239 ? 1.7480 1.6856 1.1016 -0.7127 -0.0373 0.1484  535 GLN A CD  
1847 O OE1 . GLN A 239 ? 1.8056 1.6064 1.0885 -0.6945 -0.0430 0.1532  535 GLN A OE1 
1848 N NE2 . GLN A 239 ? 1.7762 1.7908 1.1224 -0.7614 -0.0351 0.1494  535 GLN A NE2 
1849 N N   . ILE A 240 ? 1.2643 1.2844 0.8546 -0.5030 -0.0303 0.1199  536 ILE A N   
1850 C CA  . ILE A 240 ? 1.2856 1.1715 0.8225 -0.4601 -0.0423 0.1188  536 ILE A CA  
1851 C C   . ILE A 240 ? 1.4467 1.2047 0.8592 -0.5055 -0.0471 0.1361  536 ILE A C   
1852 O O   . ILE A 240 ? 1.5061 1.2211 0.8596 -0.5665 -0.0505 0.1454  536 ILE A O   
1853 C CB  . ILE A 240 ? 1.1508 0.9922 0.7043 -0.4287 -0.0541 0.1093  536 ILE A CB  
1854 C CG1 . ILE A 240 ? 1.0771 1.0372 0.7432 -0.3913 -0.0498 0.0938  536 ILE A CG1 
1855 C CG2 . ILE A 240 ? 1.0452 0.7665 0.5481 -0.3774 -0.0655 0.1077  536 ILE A CG2 
1856 C CD1 . ILE A 240 ? 1.1507 1.1653 0.8449 -0.4259 -0.0507 0.0926  536 ILE A CD1 
1857 N N   . PRO A 241 ? 1.3839 1.0726 0.7454 -0.4806 -0.0486 0.1412  537 PRO A N   
1858 C CA  . PRO A 241 ? 1.6146 1.1662 0.8437 -0.5217 -0.0540 0.1587  537 PRO A CA  
1859 C C   . PRO A 241 ? 1.5515 0.9683 0.7032 -0.5214 -0.0693 0.1596  537 PRO A C   
1860 O O   . PRO A 241 ? 1.5247 0.9063 0.6974 -0.4582 -0.0783 0.1493  537 PRO A O   
1861 C CB  . PRO A 241 ? 1.6664 1.1737 0.8703 -0.4708 -0.0559 0.1601  537 PRO A CB  
1862 C CG  . PRO A 241 ? 1.5303 1.1820 0.8562 -0.4299 -0.0462 0.1456  537 PRO A CG  
1863 C CD  . PRO A 241 ? 1.3815 1.1057 0.7950 -0.4146 -0.0471 0.1316  537 PRO A CD  
1864 N N   . PRO A 242 ? 1.6055 0.9762 0.6970 -0.5715 -0.0761 0.1552  538 PRO A N   
1865 C CA  . PRO A 242 ? 1.6210 0.8876 0.6521 -0.5676 -0.0910 0.1468  538 PRO A CA  
1866 C C   . PRO A 242 ? 1.7709 0.8989 0.7336 -0.5018 -0.1018 0.1450  538 PRO A C   
1867 O O   . PRO A 242 ? 1.6460 0.7235 0.5994 -0.4695 -0.1100 0.1376  538 PRO A O   
1868 C CB  . PRO A 242 ? 1.7028 0.9331 0.6551 -0.6347 -0.0969 0.1447  538 PRO A CB  
1869 C CG  . PRO A 242 ? 1.6406 1.0133 0.6571 -0.6795 -0.0833 0.1502  538 PRO A CG  
1870 C CD  . PRO A 242 ? 1.6048 1.0220 0.6760 -0.6346 -0.0711 0.1573  538 PRO A CD  
1871 N N   . GLU A 243 ? 1.7631 0.8378 0.6810 -0.4756 -0.1019 0.1508  539 GLU A N   
1872 C CA  . GLU A 243 ? 1.8533 0.8154 0.7127 -0.4025 -0.1125 0.1476  539 GLU A CA  
1873 C C   . GLU A 243 ? 1.7743 0.7816 0.7060 -0.3372 -0.1137 0.1469  539 GLU A C   
1874 O O   . GLU A 243 ? 1.7931 0.7251 0.6892 -0.2749 -0.1237 0.1399  539 GLU A O   
1875 C CB  . GLU A 243 ? 1.9473 0.8701 0.7605 -0.3846 -0.1119 0.1546  539 GLU A CB  
1876 C CG  . GLU A 243 ? 1.8944 0.9316 0.7882 -0.3728 -0.1011 0.1646  539 GLU A CG  
1877 C CD  . GLU A 243 ? 1.8808 0.9959 0.7925 -0.4422 -0.0876 0.1714  539 GLU A CD  
1878 O OE1 . GLU A 243 ? 1.8010 0.9561 0.7240 -0.5053 -0.0837 0.1684  539 GLU A OE1 
1879 O OE2 . GLU A 243 ? 1.8296 0.9735 0.7447 -0.4315 -0.0817 0.1785  539 GLU A OE2 
1880 N N   . LEU A 244 ? 1.5580 0.7029 0.6004 -0.3458 -0.1036 0.1477  540 LEU A N   
1881 C CA  . LEU A 244 ? 1.5048 0.7364 0.6559 -0.2814 -0.1045 0.1308  540 LEU A CA  
1882 C C   . LEU A 244 ? 1.4080 0.6475 0.5883 -0.2871 -0.1071 0.1221  540 LEU A C   
1883 O O   . LEU A 244 ? 1.3156 0.6015 0.5654 -0.2331 -0.1094 0.1094  540 LEU A O   
1884 C CB  . LEU A 244 ? 1.3991 0.7883 0.6724 -0.2785 -0.0927 0.1228  540 LEU A CB  
1885 C CG  . LEU A 244 ? 1.3613 0.7596 0.6249 -0.2563 -0.0908 0.1271  540 LEU A CG  
1886 C CD1 . LEU A 244 ? 1.2315 0.7770 0.6100 -0.2507 -0.0796 0.1167  540 LEU A CD1 
1887 C CD2 . LEU A 244 ? 1.3566 0.6886 0.5887 -0.1845 -0.1037 0.1242  540 LEU A CD2 
1888 N N   . VAL A 245 ? 1.5924 0.7921 0.7212 -0.3539 -0.1071 0.1288  541 VAL A N   
1889 C CA  . VAL A 245 ? 1.5422 0.7494 0.6942 -0.3644 -0.1105 0.1209  541 VAL A CA  
1890 C C   . VAL A 245 ? 1.6087 0.6575 0.6416 -0.3472 -0.1231 0.1196  541 VAL A C   
1891 O O   . VAL A 245 ? 1.7157 0.6986 0.6660 -0.3864 -0.1275 0.1164  541 VAL A O   
1892 C CB  . VAL A 245 ? 1.5438 0.8308 0.7266 -0.4442 -0.1039 0.1244  541 VAL A CB  
1893 C CG1 . VAL A 245 ? 1.4768 0.7612 0.6728 -0.4550 -0.1099 0.1164  541 VAL A CG1 
1894 C CG2 . VAL A 245 ? 1.3860 0.8420 0.6932 -0.4408 -0.0909 0.1190  541 VAL A CG2 
1895 N N   . LEU A 246 ? 1.6070 0.6196 0.6446 -0.2789 -0.1289 0.1139  542 LEU A N   
1896 C CA  . LEU A 246 ? 1.7116 0.6102 0.6603 -0.2415 -0.1383 0.1022  542 LEU A CA  
1897 C C   . LEU A 246 ? 1.6242 0.5191 0.5702 -0.2717 -0.1410 0.0936  542 LEU A C   
1898 O O   . LEU A 246 ? 1.6035 0.5774 0.6357 -0.2726 -0.1377 0.0927  542 LEU A O   
1899 C CB  . LEU A 246 ? 1.6644 0.5513 0.6277 -0.1498 -0.1419 0.0981  542 LEU A CB  
1900 C CG  . LEU A 246 ? 1.7319 0.5303 0.6237 -0.0998 -0.1484 0.0835  542 LEU A CG  
1901 C CD1 . LEU A 246 ? 1.8286 0.5103 0.5978 -0.0941 -0.1535 0.0789  542 LEU A CD1 
1902 C CD2 . LEU A 246 ? 1.6992 0.5446 0.6478 -0.0151 -0.1489 0.0785  542 LEU A CD2 
1903 N N   . GLU A 247 ? 1.8361 0.6376 0.6784 -0.2970 -0.1479 0.0872  543 GLU A N   
1904 C CA  . GLU A 247 ? 1.9436 0.7300 0.7632 -0.3243 -0.1525 0.0802  543 GLU A CA  
1905 C C   . GLU A 247 ? 2.0795 0.7363 0.7868 -0.2788 -0.1611 0.0692  543 GLU A C   
1906 O O   . GLU A 247 ? 2.1374 0.7044 0.7593 -0.2513 -0.1647 0.0666  543 GLU A O   
1907 C CB  . GLU A 247 ? 2.0355 0.8502 0.8324 -0.4133 -0.1535 0.0852  543 GLU A CB  
1908 C CG  . GLU A 247 ? 1.9053 0.8666 0.8160 -0.4554 -0.1431 0.0943  543 GLU A CG  
1909 C CD  . GLU A 247 ? 2.0466 1.0492 0.9322 -0.5369 -0.1434 0.0992  543 GLU A CD  
1910 O OE1 . GLU A 247 ? 2.1842 1.0907 0.9576 -0.5641 -0.1508 0.0989  543 GLU A OE1 
1911 O OE2 . GLU A 247 ? 1.9736 1.1084 0.9495 -0.5720 -0.1366 0.1026  543 GLU A OE2 
1912 N N   . VAL A 248 ? 2.0475 0.6978 0.7541 -0.2695 -0.1638 0.0624  544 VAL A N   
1913 C CA  . VAL A 248 ? 2.1733 0.7151 0.7810 -0.2227 -0.1702 0.0514  544 VAL A CA  
1914 C C   . VAL A 248 ? 2.2742 0.7628 0.8012 -0.2829 -0.1779 0.0507  544 VAL A C   
1915 O O   . VAL A 248 ? 2.0411 0.6042 0.6320 -0.3200 -0.1765 0.0538  544 VAL A O   
1916 C CB  . VAL A 248 ? 2.1153 0.6979 0.7888 -0.1514 -0.1661 0.0444  544 VAL A CB  
1917 C CG1 . VAL A 248 ? 2.2651 0.7464 0.8335 -0.1139 -0.1717 0.0336  544 VAL A CG1 
1918 C CG2 . VAL A 248 ? 2.0587 0.6862 0.7932 -0.0851 -0.1606 0.0453  544 VAL A CG2 
1919 N N   . PRO A 249 ? 2.3984 0.7590 0.7816 -0.2944 -0.1866 0.0472  545 PRO A N   
1920 C CA  . PRO A 249 ? 2.4562 0.7554 0.7468 -0.3512 -0.1956 0.0478  545 PRO A CA  
1921 C C   . PRO A 249 ? 2.5551 0.8025 0.8066 -0.3033 -0.1984 0.0397  545 PRO A C   
1922 O O   . PRO A 249 ? 2.6239 0.8001 0.8214 -0.2299 -0.1985 0.0305  545 PRO A O   
1923 C CB  . PRO A 249 ? 2.5866 0.7566 0.7287 -0.3751 -0.2043 0.0465  545 PRO A CB  
1924 C CG  . PRO A 249 ? 2.6545 0.7808 0.7842 -0.2947 -0.2008 0.0394  545 PRO A CG  
1925 C CD  . PRO A 249 ? 2.5046 0.7711 0.7993 -0.2621 -0.1892 0.0435  545 PRO A CD  
1926 N N   . ILE A 250 ? 2.5535 0.8424 0.8318 -0.3435 -0.2002 0.0434  546 ILE A N   
1927 C CA  . ILE A 250 ? 2.4292 0.6894 0.6913 -0.3011 -0.2012 0.0371  546 ILE A CA  
1928 C C   . ILE A 250 ? 2.6551 0.7648 0.7435 -0.3136 -0.2128 0.0350  546 ILE A C   
1929 O O   . ILE A 250 ? 2.6890 0.7737 0.7215 -0.3881 -0.2198 0.0428  546 ILE A O   
1930 C CB  . ILE A 250 ? 2.3371 0.7133 0.7135 -0.3329 -0.1975 0.0417  546 ILE A CB  
1931 C CG1 . ILE A 250 ? 2.1312 0.6529 0.6639 -0.3425 -0.1878 0.0460  546 ILE A CG1 
1932 C CG2 . ILE A 250 ? 2.3498 0.7106 0.7325 -0.2738 -0.1961 0.0335  546 ILE A CG2 
1933 C CD1 . ILE A 250 ? 2.0458 0.5918 0.6392 -0.2694 -0.1802 0.0404  546 ILE A CD1 
1934 N N   . ARG A 251 ? 2.8007 0.8207 0.8144 -0.2382 -0.2132 0.0252  547 ARG A N   
1935 C CA  . ARG A 251 ? 2.9688 0.8591 0.8512 -0.2316 -0.2195 0.0233  547 ARG A CA  
1936 C C   . ARG A 251 ? 2.9465 0.8327 0.8371 -0.1593 -0.2157 0.0158  547 ARG A C   
1937 O O   . ARG A 251 ? 2.9098 0.8753 0.8892 -0.1003 -0.2078 0.0101  547 ARG A O   
1938 C CB  . ARG A 251 ? 3.1153 0.8848 0.8793 -0.2068 -0.2229 0.0195  547 ARG A CB  
1939 C CG  . ARG A 251 ? 3.1270 0.8932 0.9015 -0.1075 -0.2163 0.0093  547 ARG A CG  
1940 C CD  . ARG A 251 ? 3.0547 0.9110 0.9237 -0.1017 -0.2108 0.0094  547 ARG A CD  
1941 N NE  . ARG A 251 ? 3.0107 0.8243 0.8405 -0.0244 -0.2079 0.0016  547 ARG A NE  
1942 C CZ  . ARG A 251 ? 2.9174 0.8011 0.8206 0.0046  -0.2026 -0.0004 547 ARG A CZ  
1943 N NH1 . ARG A 251 ? 2.9770 0.8193 0.8349 0.0763  -0.2007 -0.0072 547 ARG A NH1 
1944 N NH2 . ARG A 251 ? 2.6603 0.6720 0.7086 -0.0359 -0.1966 0.0084  547 ARG A NH2 
1945 N N   . HIS A 252 ? 2.9945 0.7864 0.7870 -0.1645 -0.2214 0.0160  548 HIS A N   
1946 C CA  . HIS A 252 ? 3.0326 0.8079 0.8151 -0.0956 -0.2179 0.0092  548 HIS A CA  
1947 C C   . HIS A 252 ? 3.1776 0.8348 0.8409 -0.0258 -0.2187 0.0020  548 HIS A C   
1948 O O   . HIS A 252 ? 3.2968 0.8479 0.8503 -0.0479 -0.2256 0.0036  548 HIS A O   
1949 C CB  . HIS A 252 ? 3.0323 0.7858 0.7878 -0.1413 -0.2234 0.0143  548 HIS A CB  
1950 C CG  . HIS A 252 ? 3.0698 0.8606 0.8691 -0.0829 -0.2177 0.0086  548 HIS A CG  
1951 N ND1 . HIS A 252 ? 3.1816 0.8810 0.8882 -0.0244 -0.2181 0.0031  548 HIS A ND1 
1952 C CD2 . HIS A 252 ? 2.9130 0.8233 0.8366 -0.0724 -0.2113 0.0077  548 HIS A CD2 
1953 C CE1 . HIS A 252 ? 3.0517 0.8182 0.8272 0.0179  -0.2115 -0.0008 548 HIS A CE1 
1954 N NE2 . HIS A 252 ? 2.8998 0.7916 0.8058 -0.0105 -0.2076 0.0016  548 HIS A NE2 
1955 N N   . PRO A 253 ? 3.1848 0.8606 0.8645 0.0609  -0.2117 -0.0059 549 PRO A N   
1956 C CA  . PRO A 253 ? 3.3030 0.8719 0.8652 0.1331  -0.2123 -0.0122 549 PRO A CA  
1957 C C   . PRO A 253 ? 3.5106 0.9414 0.9317 0.1184  -0.2211 -0.0104 549 PRO A C   
1958 O O   . PRO A 253 ? 3.6313 0.9532 0.9336 0.1708  -0.2237 -0.0146 549 PRO A O   
1959 C CB  . PRO A 253 ? 3.1824 0.8419 0.8222 0.2241  -0.2010 -0.0195 549 PRO A CB  
1960 C CG  . PRO A 253 ? 3.0161 0.7903 0.7797 0.1924  -0.1970 -0.0170 549 PRO A CG  
1961 C CD  . PRO A 253 ? 2.9497 0.7571 0.7617 0.1013  -0.2019 -0.0094 549 PRO A CD  
1962 N N   . LYS A 254 ? 3.5796 1.0100 1.0057 0.0506  -0.2263 -0.0041 550 LYS A N   
1963 C CA  . LYS A 254 ? 3.6445 0.9445 0.9366 0.0337  -0.2352 -0.0018 550 LYS A CA  
1964 C C   . LYS A 254 ? 3.7146 0.9658 0.9564 -0.0737 -0.2461 0.0079  550 LYS A C   
1965 O O   . LYS A 254 ? 3.9073 1.0207 1.0056 -0.0979 -0.2555 0.0099  550 LYS A O   
1966 C CB  . LYS A 254 ? 3.6440 0.9829 0.9750 0.0620  -0.2314 -0.0035 550 LYS A CB  
1967 C CG  . LYS A 254 ? 3.5321 0.9706 0.9564 0.1531  -0.2187 -0.0113 550 LYS A CG  
1968 C CD  . LYS A 254 ? 3.6251 0.9845 0.9523 0.2437  -0.2165 -0.0181 550 LYS A CD  
1969 C CE  . LYS A 254 ? 3.5081 0.9799 0.9287 0.3313  -0.2036 -0.0246 550 LYS A CE  
1970 N NZ  . LYS A 254 ? 3.6478 1.0517 0.9710 0.4237  -0.2014 -0.0303 550 LYS A NZ  
1971 N N   . PHE A 255 ? 3.5655 0.9313 0.9214 -0.1387 -0.2449 0.0142  551 PHE A N   
1972 C CA  . PHE A 255 ? 3.6167 0.9639 0.9397 -0.2430 -0.2542 0.0248  551 PHE A CA  
1973 C C   . PHE A 255 ? 3.7024 1.0454 1.0117 -0.2910 -0.2568 0.0287  551 PHE A C   
1974 O O   . PHE A 255 ? 3.4844 0.9478 0.9112 -0.3149 -0.2515 0.0312  551 PHE A O   
1975 C CB  . PHE A 255 ? 3.5415 1.0215 0.9925 -0.2869 -0.2515 0.0302  551 PHE A CB  
1976 C CG  . PHE A 255 ? 3.5441 1.0415 1.0237 -0.2348 -0.2476 0.0255  551 PHE A CG  
1977 C CD1 . PHE A 255 ? 3.3957 1.0078 1.0022 -0.1773 -0.2368 0.0195  551 PHE A CD1 
1978 C CD2 . PHE A 255 ? 3.5496 0.9454 0.9243 -0.2442 -0.2548 0.0271  551 PHE A CD2 
1979 C CE1 . PHE A 255 ? 3.3123 0.9415 0.9424 -0.1308 -0.2329 0.0151  551 PHE A CE1 
1980 C CE2 . PHE A 255 ? 3.5416 0.9527 0.9403 -0.1960 -0.2510 0.0227  551 PHE A CE2 
1981 C CZ  . PHE A 255 ? 3.3950 0.9247 0.9225 -0.1394 -0.2397 0.0166  551 PHE A CZ  
1982 N N   . ASP A 256 ? 3.9212 1.1197 1.0796 -0.3062 -0.2654 0.0293  552 ASP A N   
1983 C CA  . ASP A 256 ? 3.9876 1.1709 1.1204 -0.3515 -0.2682 0.0327  552 ASP A CA  
1984 C C   . ASP A 256 ? 3.8971 1.1490 1.0687 -0.4614 -0.2726 0.0445  552 ASP A C   
1985 O O   . ASP A 256 ? 3.8811 1.1598 1.0655 -0.5036 -0.2727 0.0481  552 ASP A O   
1986 C CB  . ASP A 256 ? 4.2977 1.2995 1.2487 -0.3378 -0.2768 0.0299  552 ASP A CB  
1987 C CG  . ASP A 256 ? 4.3739 1.3432 1.3097 -0.2408 -0.2709 0.0196  552 ASP A CG  
1988 O OD1 . ASP A 256 ? 4.4247 1.3471 1.3221 -0.1589 -0.2684 0.0123  552 ASP A OD1 
1989 O OD2 . ASP A 256 ? 4.3533 1.3493 1.3165 -0.2458 -0.2686 0.0191  552 ASP A OD2 
1990 N N   . TRP A 257 ? 3.8607 1.1471 1.0513 -0.5082 -0.2758 0.0508  553 TRP A N   
1991 C CA  . TRP A 257 ? 3.7763 1.1688 1.0353 -0.6038 -0.2774 0.0622  553 TRP A CA  
1992 C C   . TRP A 257 ? 3.5070 1.0778 0.9456 -0.5941 -0.2667 0.0625  553 TRP A C   
1993 O O   . TRP A 257 ? 3.4244 1.1048 0.9358 -0.6654 -0.2664 0.0719  553 TRP A O   
1994 C CB  . TRP A 257 ? 3.7958 1.1786 1.0239 -0.6545 -0.2841 0.0692  553 TRP A CB  
1995 C CG  . TRP A 257 ? 3.7785 1.1820 1.0562 -0.5890 -0.2796 0.0631  553 TRP A CG  
1996 C CD1 . TRP A 257 ? 3.8906 1.1717 1.0697 -0.5310 -0.2825 0.0565  553 TRP A CD1 
1997 C CD2 . TRP A 257 ? 3.5390 1.0931 0.9722 -0.5738 -0.2714 0.0631  553 TRP A CD2 
1998 N NE1 . TRP A 257 ? 3.7615 1.1118 1.0279 -0.4822 -0.2762 0.0522  553 TRP A NE1 
1999 C CE2 . TRP A 257 ? 3.5585 1.0725 0.9792 -0.5084 -0.2697 0.0560  553 TRP A CE2 
2000 C CE3 . TRP A 257 ? 3.3297 1.0465 0.9067 -0.6083 -0.2654 0.0684  553 TRP A CE3 
2001 C CZ2 . TRP A 257 ? 3.3516 0.9786 0.8965 -0.4795 -0.2627 0.0539  553 TRP A CZ2 
2002 C CZ3 . TRP A 257 ? 3.1661 0.9913 0.8638 -0.5778 -0.2589 0.0663  553 TRP A CZ3 
2003 C CH2 . TRP A 257 ? 3.2269 1.0046 0.9067 -0.5158 -0.2578 0.0590  553 TRP A CH2 
2004 N N   . PHE A 258 ? 3.4041 1.0084 0.9119 -0.5077 -0.2580 0.0529  554 PHE A N   
2005 C CA  . PHE A 258 ? 3.2707 1.0344 0.9412 -0.4963 -0.2484 0.0530  554 PHE A CA  
2006 C C   . PHE A 258 ? 3.1783 1.0011 0.8868 -0.5423 -0.2468 0.0580  554 PHE A C   
2007 O O   . PHE A 258 ? 3.0478 1.0051 0.8663 -0.5858 -0.2429 0.0647  554 PHE A O   
2008 C CB  . PHE A 258 ? 3.2078 0.9854 0.9302 -0.3944 -0.2401 0.0415  554 PHE A CB  
2009 C CG  . PHE A 258 ? 2.9223 0.8273 0.7792 -0.3758 -0.2334 0.0409  554 PHE A CG  
2010 C CD1 . PHE A 258 ? 2.9838 0.8778 0.8348 -0.3619 -0.2346 0.0398  554 PHE A CD1 
2011 C CD2 . PHE A 258 ? 2.8005 0.8323 0.7851 -0.3748 -0.2264 0.0417  554 PHE A CD2 
2012 C CE1 . PHE A 258 ? 2.7858 0.7928 0.7560 -0.3468 -0.2290 0.0391  554 PHE A CE1 
2013 C CE2 . PHE A 258 ? 2.6833 0.8285 0.7898 -0.3590 -0.2206 0.0411  554 PHE A CE2 
2014 C CZ  . PHE A 258 ? 2.6145 0.7460 0.7120 -0.3454 -0.2222 0.0396  554 PHE A CZ  
2015 N N   . LYS A 259 ? 3.2602 0.9852 0.8770 -0.5323 -0.2496 0.0549  555 LYS A N   
2016 C CA  . LYS A 259 ? 3.2375 1.0147 0.8874 -0.5726 -0.2476 0.0591  555 LYS A CA  
2017 C C   . LYS A 259 ? 3.2766 1.1158 0.9332 -0.6773 -0.2518 0.0716  555 LYS A C   
2018 O O   . LYS A 259 ? 3.1185 1.0797 0.8695 -0.7146 -0.2468 0.0771  555 LYS A O   
2019 C CB  . LYS A 259 ? 3.4347 1.0781 0.9655 -0.5469 -0.2513 0.0537  555 LYS A CB  
2020 C CG  . LYS A 259 ? 3.6533 1.1401 1.0496 -0.4949 -0.2570 0.0468  555 LYS A CG  
2021 C CD  . LYS A 259 ? 3.8054 1.1764 1.1038 -0.4456 -0.2585 0.0396  555 LYS A CD  
2022 C CE  . LYS A 259 ? 3.8967 1.1593 1.1102 -0.3595 -0.2595 0.0304  555 LYS A CE  
2023 N NZ  . LYS A 259 ? 3.6042 0.9704 0.9383 -0.2925 -0.2501 0.0251  555 LYS A NZ  
2024 N N   . ASP A 260 ? 3.4287 1.1915 0.9865 -0.7249 -0.2607 0.0765  556 ASP A N   
2025 C CA  . ASP A 260 ? 3.4408 1.2630 0.9946 -0.8261 -0.2651 0.0888  556 ASP A CA  
2026 C C   . ASP A 260 ? 3.2220 1.2291 0.9313 -0.8487 -0.2579 0.0950  556 ASP A C   
2027 O O   . ASP A 260 ? 3.1694 1.2795 0.9220 -0.9195 -0.2570 0.1044  556 ASP A O   
2028 C CB  . ASP A 260 ? 3.6244 1.3284 1.0439 -0.8664 -0.2763 0.0925  556 ASP A CB  
2029 C CG  . ASP A 260 ? 3.8286 1.3404 1.0802 -0.8464 -0.2843 0.0869  556 ASP A CG  
2030 O OD1 . ASP A 260 ? 3.8038 1.2795 1.0450 -0.8040 -0.2811 0.0805  556 ASP A OD1 
2031 O OD2 . ASP A 260 ? 4.0143 1.4078 1.1396 -0.8721 -0.2940 0.0891  556 ASP A OD2 
2032 N N   . LEU A 261 ? 3.1687 1.2216 0.9601 -0.7879 -0.2527 0.0897  557 LEU A N   
2033 C CA  . LEU A 261 ? 2.9893 1.2140 0.9326 -0.7950 -0.2450 0.0939  557 LEU A CA  
2034 C C   . LEU A 261 ? 2.9737 1.3064 1.0062 -0.8046 -0.2375 0.0960  557 LEU A C   
2035 O O   . LEU A 261 ? 2.9173 1.3979 1.0508 -0.8430 -0.2326 0.1035  557 LEU A O   
2036 C CB  . LEU A 261 ? 2.8171 1.0543 0.8250 -0.7161 -0.2404 0.0856  557 LEU A CB  
2037 C CG  . LEU A 261 ? 2.9218 1.0916 0.8753 -0.7055 -0.2458 0.0843  557 LEU A CG  
2038 C CD1 . LEU A 261 ? 2.8140 1.0031 0.8360 -0.6226 -0.2401 0.0748  557 LEU A CD1 
2039 C CD2 . LEU A 261 ? 2.8509 1.1018 0.8286 -0.7832 -0.2494 0.0959  557 LEU A CD2 
2040 N N   . GLY A 262 ? 2.9530 1.2163 0.9484 -0.7682 -0.2363 0.0894  558 GLY A N   
2041 C CA  . GLY A 262 ? 2.9448 1.2916 1.0023 -0.7859 -0.2306 0.0920  558 GLY A CA  
2042 C C   . GLY A 262 ? 2.7353 1.2299 0.9611 -0.7474 -0.2185 0.0907  558 GLY A C   
2043 O O   . GLY A 262 ? 2.6630 1.2854 0.9809 -0.7830 -0.2113 0.0969  558 GLY A O   
2044 N N   . LEU A 263 ? 2.6315 1.1171 0.9090 -0.6725 -0.2143 0.0822  559 LEU A N   
2045 C CA  . LEU A 263 ? 2.4122 1.0322 0.8551 -0.6326 -0.2021 0.0799  559 LEU A CA  
2046 C C   . LEU A 263 ? 2.3452 0.9378 0.8101 -0.5688 -0.1967 0.0731  559 LEU A C   
2047 O O   . LEU A 263 ? 2.3399 0.8037 0.6949 -0.5381 -0.2021 0.0675  559 LEU A O   
2048 C CB  . LEU A 263 ? 2.3021 0.9475 0.7985 -0.5977 -0.2010 0.0753  559 LEU A CB  
2049 C CG  . LEU A 263 ? 2.3035 0.9735 0.7751 -0.6597 -0.2068 0.0827  559 LEU A CG  
2050 C CD1 . LEU A 263 ? 2.2242 0.8659 0.6995 -0.6224 -0.2088 0.0768  559 LEU A CD1 
2051 C CD2 . LEU A 263 ? 2.1188 0.9578 0.7082 -0.7103 -0.2001 0.0904  559 LEU A CD2 
2052 N N   . LYS A 264 ? 2.2282 0.9446 0.8340 -0.5479 -0.1860 0.0736  560 LYS A N   
2053 C CA  . LYS A 264 ? 2.2037 0.9196 0.8495 -0.4940 -0.1797 0.0700  560 LYS A CA  
2054 C C   . LYS A 264 ? 2.0768 0.9365 0.8807 -0.4774 -0.1691 0.0710  560 LYS A C   
2055 O O   . LYS A 264 ? 2.0336 1.0050 0.9135 -0.5205 -0.1658 0.0755  560 LYS A O   
2056 C CB  . LYS A 264 ? 2.2174 0.9035 0.8094 -0.5264 -0.1804 0.0749  560 LYS A CB  
2057 C CG  . LYS A 264 ? 2.1691 0.9775 0.8241 -0.5989 -0.1757 0.0850  560 LYS A CG  
2058 C CD  . LYS A 264 ? 2.2935 1.1022 0.9372 -0.6127 -0.1722 0.0891  560 LYS A CD  
2059 C CE  . LYS A 264 ? 2.2999 1.1938 0.9507 -0.6944 -0.1707 0.0982  560 LYS A CE  
2060 N NZ  . LYS A 264 ? 2.2913 1.1715 0.9141 -0.7120 -0.1682 0.1017  560 LYS A NZ  
2061 N N   . TRP A 265 ? 1.9536 0.8113 0.8022 -0.4135 -0.1641 0.0666  561 TRP A N   
2062 C CA  . TRP A 265 ? 1.7783 0.7556 0.7643 -0.3937 -0.1555 0.0665  561 TRP A CA  
2063 C C   . TRP A 265 ? 1.7779 0.7528 0.7861 -0.3554 -0.1505 0.0691  561 TRP A C   
2064 O O   . TRP A 265 ? 1.9068 0.7825 0.8306 -0.3216 -0.1539 0.0677  561 TRP A O   
2065 C CB  . TRP A 265 ? 1.6641 0.6517 0.6953 -0.3470 -0.1557 0.0573  561 TRP A CB  
2066 C CG  . TRP A 265 ? 1.5528 0.6733 0.7177 -0.3536 -0.1498 0.0558  561 TRP A CG  
2067 C CD1 . TRP A 265 ? 1.5299 0.6971 0.7772 -0.3079 -0.1455 0.0512  561 TRP A CD1 
2068 C CD2 . TRP A 265 ? 1.5359 0.7640 0.7639 -0.4073 -0.1484 0.0580  561 TRP A CD2 
2069 N NE1 . TRP A 265 ? 1.3824 0.6827 0.7408 -0.3278 -0.1416 0.0478  561 TRP A NE1 
2070 C CE2 . TRP A 265 ? 1.4186 0.7546 0.7659 -0.3888 -0.1437 0.0522  561 TRP A CE2 
2071 C CE3 . TRP A 265 ? 1.4997 0.7473 0.6923 -0.4666 -0.1513 0.0640  561 TRP A CE3 
2072 C CZ2 . TRP A 265 ? 1.2041 0.6701 0.6370 -0.4205 -0.1413 0.0515  561 TRP A CZ2 
2073 C CZ3 . TRP A 265 ? 1.4199 0.8007 0.7011 -0.4981 -0.1480 0.0650  561 TRP A CZ3 
2074 C CH2 . TRP A 265 ? 1.1845 0.6737 0.5850 -0.4711 -0.1427 0.0583  561 TRP A CH2 
2075 N N   . TYR A 266 ? 1.5228 0.6095 0.6427 -0.3596 -0.1428 0.0726  562 TYR A N   
2076 C CA  . TYR A 266 ? 1.5922 0.6887 0.7417 -0.3256 -0.1380 0.0779  562 TYR A CA  
2077 C C   . TYR A 266 ? 1.5486 0.6391 0.7318 -0.2426 -0.1381 0.0699  562 TYR A C   
2078 O O   . TYR A 266 ? 1.4013 0.5335 0.6361 -0.2208 -0.1379 0.0602  562 TYR A O   
2079 C CB  . TYR A 266 ? 1.4898 0.7332 0.7504 -0.3569 -0.1285 0.0810  562 TYR A CB  
2080 C CG  . TYR A 266 ? 1.4181 0.7861 0.7868 -0.3607 -0.1252 0.0715  562 TYR A CG  
2081 C CD1 . TYR A 266 ? 1.3121 0.7594 0.7765 -0.2997 -0.1206 0.0607  562 TYR A CD1 
2082 C CD2 . TYR A 266 ? 1.2752 0.6836 0.6463 -0.4276 -0.1274 0.0743  562 TYR A CD2 
2083 C CE1 . TYR A 266 ? 1.3013 0.8496 0.8528 -0.3017 -0.1182 0.0532  562 TYR A CE1 
2084 C CE2 . TYR A 266 ? 1.2474 0.7685 0.7120 -0.4258 -0.1255 0.0664  562 TYR A CE2 
2085 C CZ  . TYR A 266 ? 1.2341 0.8178 0.7850 -0.3614 -0.1209 0.0559  562 TYR A CZ  
2086 O OH  . TYR A 266 ? 1.2381 0.9219 0.8713 -0.3583 -0.1197 0.0490  562 TYR A OH  
2087 N N   . GLY A 267 ? 1.4840 0.5416 0.6435 -0.1927 -0.1380 0.0726  563 GLY A N   
2088 C CA  . GLY A 267 ? 1.3940 0.4651 0.5839 -0.1106 -0.1380 0.0640  563 GLY A CA  
2089 C C   . GLY A 267 ? 1.3933 0.6215 0.7281 -0.0882 -0.1299 0.0547  563 GLY A C   
2090 O O   . GLY A 267 ? 1.5556 0.8120 0.9275 -0.0407 -0.1292 0.0460  563 GLY A O   
2091 N N   . LEU A 268 ? 1.2102 0.5388 0.6220 -0.1229 -0.1233 0.0563  564 LEU A N   
2092 C CA  . LEU A 268 ? 1.1020 0.5566 0.6289 -0.0932 -0.1167 0.0489  564 LEU A CA  
2093 C C   . LEU A 268 ? 1.0254 0.5757 0.6384 -0.1195 -0.1118 0.0424  564 LEU A C   
2094 O O   . LEU A 268 ? 0.9759 0.5714 0.6092 -0.1682 -0.1083 0.0460  564 LEU A O   
2095 C CB  . LEU A 268 ? 1.1942 0.6866 0.7379 -0.0994 -0.1131 0.0541  564 LEU A CB  
2096 C CG  . LEU A 268 ? 1.0758 0.6800 0.7201 -0.0685 -0.1080 0.0463  564 LEU A CG  
2097 C CD1 . LEU A 268 ? 1.0875 0.6855 0.7327 -0.0064 -0.1124 0.0422  564 LEU A CD1 
2098 C CD2 . LEU A 268 ? 1.0336 0.6833 0.6974 -0.0910 -0.1029 0.0505  564 LEU A CD2 
2099 N N   . PRO A 269 ? 0.9166 0.5048 0.5803 -0.0869 -0.1111 0.0333  565 PRO A N   
2100 C CA  . PRO A 269 ? 0.8307 0.5099 0.5759 -0.1041 -0.1069 0.0273  565 PRO A CA  
2101 C C   . PRO A 269 ? 0.7786 0.5539 0.6069 -0.0878 -0.1008 0.0229  565 PRO A C   
2102 O O   . PRO A 269 ? 0.8903 0.6826 0.7433 -0.0474 -0.1004 0.0186  565 PRO A O   
2103 C CB  . PRO A 269 ? 0.7779 0.4393 0.5253 -0.0749 -0.1089 0.0207  565 PRO A CB  
2104 C CG  . PRO A 269 ? 0.9683 0.5769 0.6737 -0.0242 -0.1110 0.0205  565 PRO A CG  
2105 C CD  . PRO A 269 ? 0.9707 0.5263 0.6176 -0.0301 -0.1136 0.0288  565 PRO A CD  
2106 N N   . ALA A 270 ? 0.7983 0.6393 0.6672 -0.1177 -0.0963 0.0236  566 ALA A N   
2107 C CA  . ALA A 270 ? 0.7856 0.6991 0.7136 -0.1019 -0.0908 0.0195  566 ALA A CA  
2108 C C   . ALA A 270 ? 0.6922 0.6851 0.6774 -0.1172 -0.0865 0.0153  566 ALA A C   
2109 O O   . ALA A 270 ? 0.6266 0.6512 0.6096 -0.1503 -0.0837 0.0198  566 ALA A O   
2110 C CB  . ALA A 270 ? 0.8670 0.7678 0.7651 -0.1118 -0.0889 0.0258  566 ALA A CB  
2111 N N   . VAL A 271 ? 0.5892 0.6147 0.6205 -0.0928 -0.0862 0.0075  567 VAL A N   
2112 C CA  . VAL A 271 ? 0.6516 0.7423 0.7289 -0.0973 -0.0835 0.0033  567 VAL A CA  
2113 C C   . VAL A 271 ? 0.5788 0.7220 0.6864 -0.0874 -0.0776 -0.0002 567 VAL A C   
2114 O O   . VAL A 271 ? 0.7351 0.8734 0.8532 -0.0639 -0.0771 -0.0048 567 VAL A O   
2115 C CB  . VAL A 271 ? 0.5695 0.6607 0.6719 -0.0753 -0.0857 -0.0028 567 VAL A CB  
2116 C CG1 . VAL A 271 ? 0.5533 0.7037 0.6993 -0.0653 -0.0829 -0.0084 567 VAL A CG1 
2117 C CG2 . VAL A 271 ? 0.5600 0.6142 0.6346 -0.0900 -0.0907 -0.0001 567 VAL A CG2 
2118 N N   . SER A 272 ? 0.5331 0.7315 0.6530 -0.1051 -0.0735 0.0017  568 SER A N   
2119 C CA  . SER A 272 ? 0.4889 0.7362 0.6280 -0.0942 -0.0666 -0.0016 568 SER A CA  
2120 C C   . SER A 272 ? 0.5002 0.8130 0.6758 -0.0763 -0.0634 -0.0080 568 SER A C   
2121 O O   . SER A 272 ? 0.5231 0.8764 0.7086 -0.0626 -0.0571 -0.0116 568 SER A O   
2122 C CB  . SER A 272 ? 0.6198 0.8830 0.7340 -0.1257 -0.0620 0.0069  568 SER A CB  
2123 O OG  . SER A 272 ? 0.5822 0.8725 0.6897 -0.1603 -0.0631 0.0132  568 SER A OG  
2124 N N   . ASN A 273 ? 0.4268 0.7486 0.6170 -0.0719 -0.0677 -0.0096 569 ASN A N   
2125 C CA  . ASN A 273 ? 0.4466 0.8332 0.6631 -0.0533 -0.0658 -0.0138 569 ASN A CA  
2126 C C   . ASN A 273 ? 0.5324 0.8928 0.7579 -0.0179 -0.0687 -0.0221 569 ASN A C   
2127 O O   . ASN A 273 ? 0.5331 0.9314 0.7711 0.0029  -0.0693 -0.0253 569 ASN A O   
2128 C CB  . ASN A 273 ? 0.5701 1.0015 0.7925 -0.0784 -0.0695 -0.0080 569 ASN A CB  
2129 C CG  . ASN A 273 ? 0.6039 0.9781 0.8134 -0.0900 -0.0779 -0.0063 569 ASN A CG  
2130 O OD1 . ASN A 273 ? 0.4830 0.7944 0.6850 -0.0739 -0.0799 -0.0098 569 ASN A OD1 
2131 N ND2 . ASN A 273 ? 0.7085 1.1101 0.9138 -0.1192 -0.0829 -0.0012 569 ASN A ND2 
2132 N N   . MET A 274 ? 0.5214 0.8199 0.7367 -0.0114 -0.0710 -0.0249 570 MET A N   
2133 C CA  . MET A 274 ? 0.4169 0.6829 0.6332 0.0106  -0.0743 -0.0309 570 MET A CA  
2134 C C   . MET A 274 ? 0.5241 0.7723 0.7310 0.0305  -0.0721 -0.0385 570 MET A C   
2135 O O   . MET A 274 ? 0.6581 0.9140 0.8593 0.0282  -0.0684 -0.0394 570 MET A O   
2136 C CB  . MET A 274 ? 0.4643 0.6830 0.6747 0.0000  -0.0786 -0.0284 570 MET A CB  
2137 C CG  . MET A 274 ? 0.4464 0.6689 0.6585 -0.0118 -0.0825 -0.0239 570 MET A CG  
2138 S SD  . MET A 274 ? 0.5477 0.7160 0.7464 -0.0178 -0.0856 -0.0219 570 MET A SD  
2139 C CE  . MET A 274 ? 0.4536 0.6064 0.6591 0.0014  -0.0862 -0.0271 570 MET A CE  
2140 N N   . LEU A 275 ? 0.4589 0.6765 0.6571 0.0474  -0.0751 -0.0438 571 LEU A N   
2141 C CA  . LEU A 275 ? 0.5075 0.6943 0.6838 0.0640  -0.0750 -0.0519 571 LEU A CA  
2142 C C   . LEU A 275 ? 0.6168 0.7577 0.7845 0.0494  -0.0792 -0.0528 571 LEU A C   
2143 O O   . LEU A 275 ? 0.6711 0.7958 0.8425 0.0418  -0.0820 -0.0498 571 LEU A O   
2144 C CB  . LEU A 275 ? 0.4869 0.6650 0.6451 0.0936  -0.0760 -0.0569 571 LEU A CB  
2145 C CG  . LEU A 275 ? 0.7326 0.8768 0.8544 0.1161  -0.0750 -0.0664 571 LEU A CG  
2146 C CD1 . LEU A 275 ? 0.8502 1.0242 0.9599 0.1554  -0.0720 -0.0702 571 LEU A CD1 
2147 C CD2 . LEU A 275 ? 0.8599 0.9287 0.9475 0.1108  -0.0810 -0.0703 571 LEU A CD2 
2148 N N   . LEU A 276 ? 0.5292 0.6574 0.6857 0.0444  -0.0794 -0.0565 572 LEU A N   
2149 C CA  . LEU A 276 ? 0.6142 0.7134 0.7613 0.0291  -0.0841 -0.0582 572 LEU A CA  
2150 C C   . LEU A 276 ? 0.6878 0.7403 0.7972 0.0348  -0.0872 -0.0665 572 LEU A C   
2151 O O   . LEU A 276 ? 0.7851 0.8264 0.8712 0.0527  -0.0855 -0.0730 572 LEU A O   
2152 C CB  . LEU A 276 ? 0.6625 0.7775 0.8146 0.0192  -0.0849 -0.0572 572 LEU A CB  
2153 C CG  . LEU A 276 ? 0.6570 0.7608 0.8008 0.0036  -0.0908 -0.0595 572 LEU A CG  
2154 C CD1 . LEU A 276 ? 0.7146 0.8195 0.8695 -0.0077 -0.0929 -0.0554 572 LEU A CD1 
2155 C CD2 . LEU A 276 ? 0.5048 0.6327 0.6560 0.0001  -0.0924 -0.0566 572 LEU A CD2 
2156 N N   . GLU A 277 ? 0.4884 0.5103 0.5850 0.0190  -0.0914 -0.0663 573 GLU A N   
2157 C CA  . GLU A 277 ? 0.6977 0.6578 0.7444 0.0166  -0.0956 -0.0729 573 GLU A CA  
2158 C C   . GLU A 277 ? 0.7247 0.6747 0.7606 -0.0178 -0.1011 -0.0737 573 GLU A C   
2159 O O   . GLU A 277 ? 0.6422 0.6200 0.7031 -0.0374 -0.1015 -0.0674 573 GLU A O   
2160 C CB  . GLU A 277 ? 0.7386 0.6660 0.7683 0.0249  -0.0962 -0.0706 573 GLU A CB  
2161 C CG  . GLU A 277 ? 0.9570 0.8340 0.9381 0.0562  -0.0970 -0.0769 573 GLU A CG  
2162 C CD  . GLU A 277 ? 1.1947 0.9935 1.1198 0.0481  -0.1022 -0.0776 573 GLU A CD  
2163 O OE1 . GLU A 277 ? 1.2086 0.9656 1.1009 0.0153  -0.1066 -0.0799 573 GLU A OE1 
2164 O OE2 . GLU A 277 ? 1.3127 1.0933 1.2240 0.0716  -0.1024 -0.0752 573 GLU A OE2 
2165 N N   . ILE A 278 ? 0.7486 0.6641 0.7454 -0.0252 -0.1055 -0.0816 574 ILE A N   
2166 C CA  . ILE A 278 ? 0.7768 0.6877 0.7580 -0.0633 -0.1126 -0.0830 574 ILE A CA  
2167 C C   . ILE A 278 ? 0.8906 0.7151 0.7959 -0.0726 -0.1186 -0.0923 574 ILE A C   
2168 O O   . ILE A 278 ? 0.9830 0.7709 0.8555 -0.0448 -0.1175 -0.1001 574 ILE A O   
2169 C CB  . ILE A 278 ? 0.7038 0.6713 0.7155 -0.0692 -0.1144 -0.0827 574 ILE A CB  
2170 C CG1 . ILE A 278 ? 0.7512 0.7858 0.8222 -0.0562 -0.1090 -0.0735 574 ILE A CG1 
2171 C CG2 . ILE A 278 ? 0.7216 0.6984 0.7197 -0.1094 -0.1231 -0.0837 574 ILE A CG2 
2172 C CD1 . ILE A 278 ? 0.7249 0.8022 0.8163 -0.0506 -0.1101 -0.0723 574 ILE A CD1 
2173 N N   . GLY A 279 ? 0.9128 0.7016 0.7834 -0.1115 -0.1246 -0.0914 575 GLY A N   
2174 C CA  . GLY A 279 ? 1.0024 0.6904 0.7843 -0.1279 -0.1319 -0.0997 575 GLY A CA  
2175 C C   . GLY A 279 ? 1.0567 0.6649 0.7847 -0.0819 -0.1294 -0.1061 575 GLY A C   
2176 O O   . GLY A 279 ? 1.0679 0.5910 0.7178 -0.0789 -0.1348 -0.1160 575 GLY A O   
2177 N N   . GLY A 280 ? 1.0902 0.7242 0.8533 -0.0444 -0.1221 -0.1008 576 GLY A N   
2178 C CA  . GLY A 280 ? 1.1225 0.7028 0.8420 0.0071  -0.1196 -0.1064 576 GLY A CA  
2179 C C   . GLY A 280 ? 1.0707 0.6865 0.8054 0.0464  -0.1144 -0.1131 576 GLY A C   
2180 O O   . GLY A 280 ? 1.1850 0.7647 0.8795 0.0936  -0.1120 -0.1191 576 GLY A O   
2181 N N   . LEU A 281 ? 0.9999 0.6859 0.7864 0.0300  -0.1126 -0.1122 577 LEU A N   
2182 C CA  . LEU A 281 ? 1.0383 0.7757 0.8516 0.0620  -0.1057 -0.1154 577 LEU A CA  
2183 C C   . LEU A 281 ? 0.9557 0.7846 0.8479 0.0743  -0.0978 -0.1052 577 LEU A C   
2184 O O   . LEU A 281 ? 0.9039 0.7696 0.8410 0.0488  -0.0987 -0.0964 577 LEU A O   
2185 C CB  . LEU A 281 ? 1.0064 0.7623 0.8238 0.0363  -0.1090 -0.1191 577 LEU A CB  
2186 C CG  . LEU A 281 ? 1.1237 0.7963 0.8590 0.0287  -0.1163 -0.1317 577 LEU A CG  
2187 C CD1 . LEU A 281 ? 1.0279 0.7381 0.7811 -0.0027 -0.1212 -0.1328 577 LEU A CD1 
2188 C CD2 . LEU A 281 ? 1.2522 0.8862 0.9387 0.0821  -0.1104 -0.1415 577 LEU A CD2 
2189 N N   . GLU A 282 ? 0.9016 0.7684 0.8061 0.1123  -0.0902 -0.1067 578 GLU A N   
2190 C CA  . GLU A 282 ? 0.8273 0.7716 0.7923 0.1222  -0.0838 -0.0975 578 GLU A CA  
2191 C C   . GLU A 282 ? 0.6883 0.7022 0.6917 0.1208  -0.0770 -0.0948 578 GLU A C   
2192 O O   . GLU A 282 ? 0.7372 0.7605 0.7207 0.1449  -0.0719 -0.1011 578 GLU A O   
2193 C CB  . GLU A 282 ? 0.9096 0.8527 0.8573 0.1647  -0.0811 -0.0990 578 GLU A CB  
2194 C CG  . GLU A 282 ? 1.0628 0.9255 0.9619 0.1682  -0.0882 -0.1005 578 GLU A CG  
2195 C CD  . GLU A 282 ? 1.1688 1.0401 1.0567 0.2128  -0.0870 -0.0997 578 GLU A CD  
2196 O OE1 . GLU A 282 ? 1.1855 1.1016 1.0743 0.2524  -0.0811 -0.1035 578 GLU A OE1 
2197 O OE2 . GLU A 282 ? 1.2202 1.0600 1.0983 0.2092  -0.0918 -0.0950 578 GLU A OE2 
2198 N N   . PHE A 283 ? 0.6639 0.7228 0.7157 0.0947  -0.0766 -0.0852 579 PHE A N   
2199 C CA  . PHE A 283 ? 0.6842 0.7982 0.7657 0.0866  -0.0713 -0.0800 579 PHE A CA  
2200 C C   . PHE A 283 ? 0.5911 0.7616 0.7079 0.0890  -0.0661 -0.0714 579 PHE A C   
2201 O O   . PHE A 283 ? 0.7479 0.9257 0.8888 0.0702  -0.0687 -0.0637 579 PHE A O   
2202 C CB  . PHE A 283 ? 0.6572 0.7678 0.7518 0.0571  -0.0765 -0.0755 579 PHE A CB  
2203 C CG  . PHE A 283 ? 0.7238 0.7935 0.7857 0.0482  -0.0831 -0.0834 579 PHE A CG  
2204 C CD1 . PHE A 283 ? 0.6932 0.7236 0.7391 0.0322  -0.0907 -0.0858 579 PHE A CD1 
2205 C CD2 . PHE A 283 ? 0.7628 0.8350 0.8065 0.0518  -0.0819 -0.0882 579 PHE A CD2 
2206 C CE1 . PHE A 283 ? 0.7672 0.7627 0.7787 0.0158  -0.0981 -0.0929 579 PHE A CE1 
2207 C CE2 . PHE A 283 ? 0.7854 0.8195 0.7945 0.0397  -0.0897 -0.0961 579 PHE A CE2 
2208 C CZ  . PHE A 283 ? 0.8441 0.8406 0.8367 0.0196  -0.0984 -0.0985 579 PHE A CZ  
2209 N N   . SER A 284 ? 0.6022 0.8163 0.7188 0.1113  -0.0587 -0.0731 580 SER A N   
2210 C CA  . SER A 284 ? 0.5551 0.8348 0.7018 0.1114  -0.0544 -0.0656 580 SER A CA  
2211 C C   . SER A 284 ? 0.6223 0.9390 0.7925 0.0777  -0.0517 -0.0553 580 SER A C   
2212 O O   . SER A 284 ? 0.6755 1.0363 0.8665 0.0643  -0.0505 -0.0478 580 SER A O   
2213 C CB  . SER A 284 ? 0.6060 0.9346 0.7435 0.1472  -0.0468 -0.0707 580 SER A CB  
2214 O OG  . SER A 284 ? 0.7128 1.0410 0.8307 0.1536  -0.0411 -0.0760 580 SER A OG  
2215 N N   . ALA A 285 ? 0.7270 1.0236 0.8874 0.0631  -0.0514 -0.0546 581 ALA A N   
2216 C CA  . ALA A 285 ? 0.6321 0.9422 0.7996 0.0329  -0.0503 -0.0443 581 ALA A CA  
2217 C C   . ALA A 285 ? 0.6046 0.8617 0.7628 0.0219  -0.0577 -0.0434 581 ALA A C   
2218 O O   . ALA A 285 ? 0.6534 0.8893 0.7961 0.0287  -0.0595 -0.0491 581 ALA A O   
2219 C CB  . ALA A 285 ? 0.4654 0.8186 0.6252 0.0292  -0.0411 -0.0422 581 ALA A CB  
2220 N N   . CYS A 286 ? 0.4590 0.6984 0.6240 0.0069  -0.0625 -0.0366 582 CYS A N   
2221 C CA  . CYS A 286 ? 0.3857 0.5872 0.5446 0.0033  -0.0695 -0.0357 582 CYS A CA  
2222 C C   . CYS A 286 ? 0.5025 0.6877 0.6558 -0.0111 -0.0720 -0.0261 582 CYS A C   
2223 O O   . CYS A 286 ? 0.6278 0.7934 0.7856 -0.0085 -0.0766 -0.0257 582 CYS A O   
2224 C CB  . CYS A 286 ? 0.5612 0.7436 0.7270 0.0127  -0.0742 -0.0423 582 CYS A CB  
2225 S SG  . CYS A 286 ? 0.4880 0.6767 0.6690 0.0143  -0.0737 -0.0405 582 CYS A SG  
2226 N N   . PRO A 287 ? 0.5523 0.7393 0.6880 -0.0268 -0.0692 -0.0183 583 PRO A N   
2227 C CA  . PRO A 287 ? 0.4332 0.5887 0.5484 -0.0419 -0.0722 -0.0096 583 PRO A CA  
2228 C C   . PRO A 287 ? 0.5547 0.6693 0.6552 -0.0280 -0.0790 -0.0087 583 PRO A C   
2229 O O   . PRO A 287 ? 0.5367 0.6495 0.6328 -0.0157 -0.0815 -0.0105 583 PRO A O   
2230 C CB  . PRO A 287 ? 0.4917 0.6482 0.5786 -0.0646 -0.0681 -0.0014 583 PRO A CB  
2231 C CG  . PRO A 287 ? 0.5543 0.7306 0.6438 -0.0530 -0.0648 -0.0055 583 PRO A CG  
2232 C CD  . PRO A 287 ? 0.5658 0.7733 0.6888 -0.0329 -0.0634 -0.0166 583 PRO A CD  
2233 N N   . PHE A 288 ? 0.5545 0.6424 0.6469 -0.0278 -0.0822 -0.0062 584 PHE A N   
2234 C CA  . PHE A 288 ? 0.5462 0.6066 0.6262 -0.0081 -0.0874 -0.0057 584 PHE A CA  
2235 C C   . PHE A 288 ? 0.6668 0.6731 0.7032 -0.0113 -0.0901 0.0010  584 PHE A C   
2236 O O   . PHE A 288 ? 0.5339 0.5296 0.5638 -0.0304 -0.0891 0.0027  584 PHE A O   
2237 C CB  . PHE A 288 ? 0.6152 0.7013 0.7307 0.0043  -0.0881 -0.0128 584 PHE A CB  
2238 C CG  . PHE A 288 ? 0.6272 0.7175 0.7580 -0.0043 -0.0860 -0.0144 584 PHE A CG  
2239 C CD1 . PHE A 288 ? 0.5396 0.6007 0.6528 -0.0038 -0.0876 -0.0113 584 PHE A CD1 
2240 C CD2 . PHE A 288 ? 0.5584 0.6784 0.7157 -0.0083 -0.0833 -0.0195 584 PHE A CD2 
2241 C CE1 . PHE A 288 ? 0.4572 0.5238 0.5831 -0.0116 -0.0869 -0.0127 584 PHE A CE1 
2242 C CE2 . PHE A 288 ? 0.3609 0.4862 0.5296 -0.0121 -0.0829 -0.0204 584 PHE A CE2 
2243 C CZ  . PHE A 288 ? 0.4836 0.5847 0.6387 -0.0156 -0.0849 -0.0168 584 PHE A CZ  
2244 N N   . SER A 289 ? 0.7051 0.6750 0.7058 0.0092  -0.0945 0.0045  585 SER A N   
2245 C CA  . SER A 289 ? 0.8658 0.7648 0.8059 0.0118  -0.0979 0.0105  585 SER A CA  
2246 C C   . SER A 289 ? 0.8361 0.7223 0.7642 0.0513  -0.1015 0.0088  585 SER A C   
2247 O O   . SER A 289 ? 0.6879 0.6198 0.6449 0.0751  -0.1028 0.0056  585 SER A O   
2248 C CB  . SER A 289 ? 1.0139 0.8607 0.8944 0.0003  -0.0999 0.0191  585 SER A CB  
2249 O OG  . SER A 289 ? 1.0189 0.8617 0.8842 0.0310  -0.1039 0.0206  585 SER A OG  
2250 N N   . GLY A 290 ? 0.7137 0.5411 0.5961 0.0572  -0.1032 0.0106  586 GLY A N   
2251 C CA  . GLY A 290 ? 0.8027 0.6042 0.6526 0.1009  -0.1061 0.0101  586 GLY A CA  
2252 C C   . GLY A 290 ? 0.9803 0.6730 0.7346 0.1064  -0.1107 0.0158  586 GLY A C   
2253 O O   . GLY A 290 ? 0.8577 0.4977 0.5625 0.0899  -0.1137 0.0225  586 GLY A O   
2254 N N   . TRP A 291 ? 0.9099 0.5603 0.6287 0.1278  -0.1113 0.0134  587 TRP A N   
2255 C CA  . TRP A 291 ? 1.0636 0.5938 0.6798 0.1264  -0.1162 0.0175  587 TRP A CA  
2256 C C   . TRP A 291 ? 1.1801 0.6914 0.7940 0.1047  -0.1148 0.0132  587 TRP A C   
2257 O O   . TRP A 291 ? 1.1446 0.7327 0.8304 0.1055  -0.1098 0.0073  587 TRP A O   
2258 C CB  . TRP A 291 ? 1.1389 0.6090 0.6817 0.1892  -0.1205 0.0186  587 TRP A CB  
2259 C CG  . TRP A 291 ? 1.1989 0.7462 0.7896 0.2397  -0.1166 0.0123  587 TRP A CG  
2260 C CD1 . TRP A 291 ? 1.2707 0.8181 0.8592 0.2588  -0.1128 0.0065  587 TRP A CD1 
2261 C CD2 . TRP A 291 ? 1.2252 0.8694 0.8729 0.2737  -0.1158 0.0114  587 TRP A CD2 
2262 N NE1 . TRP A 291 ? 1.2502 0.8931 0.8920 0.3020  -0.1085 0.0028  587 TRP A NE1 
2263 C CE2 . TRP A 291 ? 1.2368 0.9425 0.9162 0.3100  -0.1109 0.0057  587 TRP A CE2 
2264 C CE3 . TRP A 291 ? 1.2045 0.8929 0.8779 0.2744  -0.1190 0.0149  587 TRP A CE3 
2265 C CZ2 . TRP A 291 ? 1.2212 1.0372 0.9585 0.3421  -0.1095 0.0040  587 TRP A CZ2 
2266 C CZ3 . TRP A 291 ? 1.1709 0.9619 0.8993 0.3079  -0.1190 0.0125  587 TRP A CZ3 
2267 C CH2 . TRP A 291 ? 1.1981 1.0552 0.9588 0.3392  -0.1144 0.0074  587 TRP A CH2 
2268 N N   . TYR A 292 ? 1.2698 0.6730 0.7934 0.0823  -0.1201 0.0164  588 TYR A N   
2269 C CA  . TYR A 292 ? 1.2459 0.6258 0.7590 0.0544  -0.1208 0.0126  588 TYR A CA  
2270 C C   . TYR A 292 ? 1.2369 0.5918 0.7244 0.1045  -0.1195 0.0060  588 TYR A C   
2271 O O   . TYR A 292 ? 1.2596 0.5532 0.6800 0.1560  -0.1213 0.0060  588 TYR A O   
2272 C CB  . TYR A 292 ? 1.3694 0.6391 0.7859 0.0055  -0.1284 0.0185  588 TYR A CB  
2273 C CG  . TYR A 292 ? 1.3067 0.6298 0.7667 -0.0630 -0.1281 0.0227  588 TYR A CG  
2274 C CD1 . TYR A 292 ? 1.3018 0.6026 0.7306 -0.0976 -0.1296 0.0315  588 TYR A CD1 
2275 C CD2 . TYR A 292 ? 1.1377 0.5373 0.6666 -0.0908 -0.1262 0.0184  588 TYR A CD2 
2276 C CE1 . TYR A 292 ? 1.2347 0.5982 0.7039 -0.1584 -0.1280 0.0356  588 TYR A CE1 
2277 C CE2 . TYR A 292 ? 1.1583 0.6184 0.7263 -0.1467 -0.1261 0.0222  588 TYR A CE2 
2278 C CZ  . TYR A 292 ? 1.1532 0.6015 0.6945 -0.1799 -0.1263 0.0306  588 TYR A CZ  
2279 O OH  . TYR A 292 ? 1.0797 0.6033 0.6625 -0.2328 -0.1248 0.0344  588 TYR A OH  
2280 N N   . MET A 293 ? 1.1289 0.5339 0.6672 0.0928  -0.1160 0.0004  589 MET A N   
2281 C CA  . MET A 293 ? 1.1828 0.5309 0.6676 0.1198  -0.1162 -0.0052 589 MET A CA  
2282 C C   . MET A 293 ? 1.2790 0.5120 0.6698 0.0757  -0.1251 -0.0036 589 MET A C   
2283 O O   . MET A 293 ? 1.2587 0.5128 0.6739 0.0149  -0.1285 -0.0005 589 MET A O   
2284 C CB  . MET A 293 ? 0.9570 0.4000 0.5267 0.1231  -0.1092 -0.0110 589 MET A CB  
2285 C CG  . MET A 293 ? 1.0077 0.4028 0.5263 0.1558  -0.1074 -0.0174 589 MET A CG  
2286 S SD  . MET A 293 ? 1.0143 0.5238 0.6296 0.1617  -0.0977 -0.0224 589 MET A SD  
2287 C CE  . MET A 293 ? 1.0999 0.6386 0.7639 0.0905  -0.1030 -0.0206 589 MET A CE  
2288 N N   . GLY A 294 ? 1.4062 0.5178 0.6841 0.1061  -0.1295 -0.0057 590 GLY A N   
2289 C CA  . GLY A 294 ? 1.4303 0.4376 0.6090 0.0613  -0.1375 -0.0046 590 GLY A CA  
2290 C C   . GLY A 294 ? 1.5067 0.5324 0.7119 -0.0042 -0.1423 -0.0053 590 GLY A C   
2291 O O   . GLY A 294 ? 1.4035 0.4093 0.5805 -0.0668 -0.1483 0.0010  590 GLY A O   
2292 N N   . THR A 295 ? 1.5172 0.6082 0.7876 0.0089  -0.1381 -0.0121 591 THR A N   
2293 C CA  . THR A 295 ? 1.4088 0.5230 0.6991 -0.0455 -0.1433 -0.0139 591 THR A CA  
2294 C C   . THR A 295 ? 1.3127 0.5104 0.6718 -0.1076 -0.1458 -0.0073 591 THR A C   
2295 O O   . THR A 295 ? 1.2917 0.4748 0.6257 -0.1670 -0.1547 -0.0055 591 THR A O   
2296 C CB  . THR A 295 ? 1.2326 0.4247 0.5929 -0.0148 -0.1361 -0.0208 591 THR A CB  
2297 O OG1 . THR A 295 ? 1.1619 0.4878 0.6442 -0.0048 -0.1273 -0.0192 591 THR A OG1 
2298 C CG2 . THR A 295 ? 1.5206 0.6535 0.8231 0.0529  -0.1308 -0.0271 591 THR A CG2 
2299 N N   . GLU A 296 ? 1.2031 0.4948 0.6482 -0.0951 -0.1384 -0.0038 592 GLU A N   
2300 C CA  . GLU A 296 ? 1.0901 0.4689 0.6011 -0.1466 -0.1393 0.0013  592 GLU A CA  
2301 C C   . GLU A 296 ? 1.1774 0.4877 0.6103 -0.2071 -0.1482 0.0083  592 GLU A C   
2302 O O   . GLU A 296 ? 1.3653 0.7325 0.8257 -0.2626 -0.1524 0.0115  592 GLU A O   
2303 C CB  . GLU A 296 ? 1.0219 0.4878 0.6138 -0.1246 -0.1308 0.0037  592 GLU A CB  
2304 C CG  . GLU A 296 ? 0.8798 0.4220 0.5509 -0.0759 -0.1222 -0.0017 592 GLU A CG  
2305 C CD  . GLU A 296 ? 1.0099 0.6096 0.7324 -0.0611 -0.1165 0.0012  592 GLU A CD  
2306 O OE1 . GLU A 296 ? 0.7107 0.3759 0.4830 -0.0916 -0.1155 0.0040  592 GLU A OE1 
2307 O OE2 . GLU A 296 ? 0.9743 0.5514 0.6794 -0.0193 -0.1137 0.0009  592 GLU A OE2 
2308 N N   . ILE A 297 ? 1.3535 0.5430 0.6839 -0.1975 -0.1514 0.0113  593 ILE A N   
2309 C CA  . ILE A 297 ? 1.4955 0.6290 0.7448 -0.2495 -0.1564 0.0203  593 ILE A CA  
2310 C C   . ILE A 297 ? 1.5178 0.5980 0.6972 -0.2684 -0.1620 0.0197  593 ILE A C   
2311 O O   . ILE A 297 ? 1.5712 0.6810 0.7426 -0.3270 -0.1659 0.0261  593 ILE A O   
2312 C CB  . ILE A 297 ? 1.5069 0.5523 0.6774 -0.2217 -0.1554 0.0248  593 ILE A CB  
2313 C CG1 . ILE A 297 ? 1.3745 0.4733 0.6103 -0.2108 -0.1506 0.0282  593 ILE A CG1 
2314 C CG2 . ILE A 297 ? 1.6172 0.5985 0.6905 -0.2716 -0.1608 0.0329  593 ILE A CG2 
2315 C CD1 . ILE A 297 ? 1.4314 0.4525 0.6009 -0.1642 -0.1496 0.0311  593 ILE A CD1 
2316 N N   . GLY A 298 ? 1.5595 0.5627 0.6826 -0.2171 -0.1622 0.0128  594 GLY A N   
2317 C CA  . GLY A 298 ? 1.7297 0.6561 0.7601 -0.2316 -0.1683 0.0133  594 GLY A CA  
2318 C C   . GLY A 298 ? 1.6760 0.6625 0.7536 -0.2636 -0.1714 0.0113  594 GLY A C   
2319 O O   . GLY A 298 ? 1.6157 0.5761 0.6383 -0.3106 -0.1780 0.0173  594 GLY A O   
2320 N N   . VAL A 299 ? 1.6093 0.6767 0.7851 -0.2396 -0.1675 0.0030  595 VAL A N   
2321 C CA  . VAL A 299 ? 1.5108 0.6379 0.7328 -0.2622 -0.1711 -0.0006 595 VAL A CA  
2322 C C   . VAL A 299 ? 1.4355 0.6855 0.7479 -0.3125 -0.1727 0.0042  595 VAL A C   
2323 O O   . VAL A 299 ? 1.5567 0.8410 0.8640 -0.3601 -0.1776 0.0101  595 VAL A O   
2324 C CB  . VAL A 299 ? 1.4282 0.5740 0.6972 -0.2075 -0.1670 -0.0131 595 VAL A CB  
2325 C CG1 . VAL A 299 ? 1.4039 0.5906 0.6974 -0.2298 -0.1724 -0.0167 595 VAL A CG1 
2326 C CG2 . VAL A 299 ? 1.4157 0.4667 0.6101 -0.1440 -0.1616 -0.0176 595 VAL A CG2 
2327 N N   . ARG A 300 ? 1.2795 0.6028 0.6752 -0.2983 -0.1683 0.0018  596 ARG A N   
2328 C CA  . ARG A 300 ? 1.2021 0.6577 0.6927 -0.3313 -0.1686 0.0048  596 ARG A CA  
2329 C C   . ARG A 300 ? 1.3155 0.7998 0.7914 -0.3796 -0.1667 0.0172  596 ARG A C   
2330 O O   . ARG A 300 ? 1.2706 0.8216 0.7618 -0.4207 -0.1686 0.0232  596 ARG A O   
2331 C CB  . ARG A 300 ? 1.0086 0.5460 0.5961 -0.2846 -0.1595 0.0011  596 ARG A CB  
2332 C CG  . ARG A 300 ? 1.0129 0.5499 0.6267 -0.2275 -0.1538 -0.0065 596 ARG A CG  
2333 C CD  . ARG A 300 ? 1.0325 0.5804 0.6424 -0.2455 -0.1621 -0.0106 596 ARG A CD  
2334 N NE  . ARG A 300 ? 0.8481 0.5060 0.5234 -0.2816 -0.1671 -0.0071 596 ARG A NE  
2335 C CZ  . ARG A 300 ? 0.8029 0.5668 0.5714 -0.2583 -0.1602 -0.0063 596 ARG A CZ  
2336 N NH1 . ARG A 300 ? 0.8592 0.6329 0.6676 -0.2078 -0.1486 -0.0086 596 ARG A NH1 
2337 N NH2 . ARG A 300 ? 0.8575 0.7179 0.6745 -0.2852 -0.1656 -0.0034 596 ARG A NH2 
2338 N N   . ASP A 301 ? 1.2664 0.7041 0.7106 -0.3742 -0.1627 0.0213  597 ASP A N   
2339 C CA  . ASP A 301 ? 1.2511 0.7193 0.6799 -0.4211 -0.1603 0.0330  597 ASP A CA  
2340 C C   . ASP A 301 ? 1.3449 0.7554 0.6813 -0.4658 -0.1658 0.0411  597 ASP A C   
2341 O O   . ASP A 301 ? 1.2704 0.7529 0.6188 -0.5144 -0.1654 0.0494  597 ASP A O   
2342 C CB  . ASP A 301 ? 1.2473 0.6584 0.6429 -0.4066 -0.1564 0.0362  597 ASP A CB  
2343 C CG  . ASP A 301 ? 1.1790 0.6600 0.6653 -0.3759 -0.1514 0.0311  597 ASP A CG  
2344 O OD1 . ASP A 301 ? 0.9893 0.5959 0.5710 -0.3839 -0.1490 0.0294  597 ASP A OD1 
2345 O OD2 . ASP A 301 ? 1.3999 0.8129 0.8596 -0.3360 -0.1492 0.0293  597 ASP A OD2 
2346 N N   . TYR A 302 ? 1.3952 0.6772 0.6340 -0.4488 -0.1708 0.0389  598 TYR A N   
2347 C CA  . TYR A 302 ? 1.4720 0.6763 0.6018 -0.4914 -0.1774 0.0471  598 TYR A CA  
2348 C C   . TYR A 302 ? 1.6200 0.8486 0.7492 -0.5159 -0.1832 0.0470  598 TYR A C   
2349 O O   . TYR A 302 ? 1.5990 0.8153 0.6682 -0.5697 -0.1882 0.0564  598 TYR A O   
2350 C CB  . TYR A 302 ? 1.6725 0.7209 0.6837 -0.4573 -0.1808 0.0449  598 TYR A CB  
2351 C CG  . TYR A 302 ? 1.8725 0.8698 0.8351 -0.4552 -0.1789 0.0493  598 TYR A CG  
2352 C CD1 . TYR A 302 ? 2.0063 0.8887 0.8910 -0.4023 -0.1797 0.0443  598 TYR A CD1 
2353 C CD2 . TYR A 302 ? 1.8664 0.9343 0.8584 -0.5028 -0.1760 0.0582  598 TYR A CD2 
2354 C CE1 . TYR A 302 ? 2.0184 0.8523 0.8551 -0.3981 -0.1789 0.0475  598 TYR A CE1 
2355 C CE2 . TYR A 302 ? 1.9727 0.9902 0.9160 -0.5023 -0.1748 0.0618  598 TYR A CE2 
2356 C CZ  . TYR A 302 ? 2.0407 0.9381 0.9057 -0.4505 -0.1769 0.0564  598 TYR A CZ  
2357 O OH  . TYR A 302 ? 2.0694 0.9154 0.8833 -0.4476 -0.1765 0.0592  598 TYR A OH  
2358 N N   . CYS A 303 ? 1.4059 0.6706 0.5979 -0.4803 -0.1830 0.0369  599 CYS A N   
2359 C CA  . CYS A 303 ? 1.4442 0.7116 0.6225 -0.4963 -0.1893 0.0357  599 CYS A CA  
2360 C C   . CYS A 303 ? 1.4325 0.8369 0.7252 -0.4973 -0.1890 0.0312  599 CYS A C   
2361 O O   . CYS A 303 ? 1.5286 0.9427 0.8119 -0.5133 -0.1950 0.0307  599 CYS A O   
2362 C CB  . CYS A 303 ? 1.6047 0.7565 0.7159 -0.4499 -0.1918 0.0271  599 CYS A CB  
2363 S SG  . CYS A 303 ? 1.7412 0.7228 0.6984 -0.4391 -0.1945 0.0315  599 CYS A SG  
2364 N N   . ASP A 304 ? 1.3468 0.8529 0.7409 -0.4784 -0.1830 0.0279  600 ASP A N   
2365 C CA  . ASP A 304 ? 1.3654 1.0095 0.8568 -0.4843 -0.1835 0.0264  600 ASP A CA  
2366 C C   . ASP A 304 ? 1.4545 1.1499 0.9258 -0.5409 -0.1864 0.0373  600 ASP A C   
2367 O O   . ASP A 304 ? 1.5621 1.2335 0.9803 -0.5790 -0.1846 0.0473  600 ASP A O   
2368 C CB  . ASP A 304 ? 1.3489 1.0955 0.9359 -0.4637 -0.1762 0.0250  600 ASP A CB  
2369 C CG  . ASP A 304 ? 1.2367 1.0048 0.8874 -0.4123 -0.1763 0.0135  600 ASP A CG  
2370 O OD1 . ASP A 304 ? 1.2470 0.9256 0.8578 -0.3849 -0.1794 0.0058  600 ASP A OD1 
2371 O OD2 . ASP A 304 ? 1.0689 0.9446 0.8055 -0.3975 -0.1729 0.0126  600 ASP A OD2 
2372 N N   . ASN A 305 ? 1.4034 1.1677 0.9113 -0.5474 -0.1916 0.0355  601 ASN A N   
2373 C CA  . ASN A 305 ? 1.3908 1.2168 0.8843 -0.6005 -0.1946 0.0457  601 ASN A CA  
2374 C C   . ASN A 305 ? 1.2602 1.2051 0.8112 -0.6170 -0.1865 0.0528  601 ASN A C   
2375 O O   . ASN A 305 ? 1.1884 1.1578 0.7004 -0.6686 -0.1863 0.0639  601 ASN A O   
2376 C CB  . ASN A 305 ? 1.3494 1.2368 0.8797 -0.5968 -0.2020 0.0414  601 ASN A CB  
2377 C CG  . ASN A 305 ? 1.5378 1.3163 0.9775 -0.6166 -0.2112 0.0413  601 ASN A CG  
2378 O OD1 . ASN A 305 ? 1.6978 1.3750 1.0396 -0.6495 -0.2127 0.0485  601 ASN A OD1 
2379 N ND2 . ASN A 305 ? 1.5246 1.3202 0.9896 -0.5960 -0.2179 0.0336  601 ASN A ND2 
2380 N N   . SER A 306 ? 1.1569 1.1766 0.7953 -0.5743 -0.1798 0.0469  602 SER A N   
2381 C CA  . SER A 306 ? 1.1468 1.2821 0.8425 -0.5795 -0.1709 0.0522  602 SER A CA  
2382 C C   . SER A 306 ? 1.1674 1.2551 0.8409 -0.5801 -0.1634 0.0550  602 SER A C   
2383 O O   . SER A 306 ? 0.9999 1.1759 0.7217 -0.5772 -0.1548 0.0581  602 SER A O   
2384 C CB  . SER A 306 ? 1.0502 1.2972 0.8482 -0.5297 -0.1684 0.0445  602 SER A CB  
2385 O OG  . SER A 306 ? 1.0528 1.2507 0.8762 -0.4829 -0.1673 0.0353  602 SER A OG  
2386 N N   . ARG A 307 ? 1.2911 1.2395 0.8881 -0.5806 -0.1665 0.0540  603 ARG A N   
2387 C CA  . ARG A 307 ? 1.3327 1.2225 0.8936 -0.5835 -0.1612 0.0576  603 ARG A CA  
2388 C C   . ARG A 307 ? 1.4156 1.2077 0.8592 -0.6352 -0.1657 0.0678  603 ARG A C   
2389 O O   . ARG A 307 ? 1.5484 1.3898 0.9704 -0.6834 -0.1677 0.0763  603 ARG A O   
2390 C CB  . ARG A 307 ? 1.2795 1.0921 0.8480 -0.5317 -0.1609 0.0475  603 ARG A CB  
2391 C CG  . ARG A 307 ? 1.1997 1.1104 0.8775 -0.4859 -0.1576 0.0384  603 ARG A CG  
2392 C CD  . ARG A 307 ? 1.1101 1.1268 0.8561 -0.4809 -0.1480 0.0413  603 ARG A CD  
2393 N NE  . ARG A 307 ? 1.0579 1.0113 0.7564 -0.4939 -0.1439 0.0465  603 ARG A NE  
2394 C CZ  . ARG A 307 ? 1.0661 0.9379 0.7478 -0.4650 -0.1440 0.0417  603 ARG A CZ  
2395 N NH1 . ARG A 307 ? 0.9228 0.7729 0.6339 -0.4236 -0.1478 0.0315  603 ARG A NH1 
2396 N NH2 . ARG A 307 ? 1.2673 1.0803 0.8998 -0.4770 -0.1409 0.0474  603 ARG A NH2 
2397 N N   . TYR A 308 ? 1.4247 1.0785 0.7852 -0.6258 -0.1680 0.0672  604 TYR A N   
2398 C CA  . TYR A 308 ? 1.4242 0.9839 0.6646 -0.6743 -0.1728 0.0774  604 TYR A CA  
2399 C C   . TYR A 308 ? 1.6518 1.1514 0.8152 -0.7055 -0.1825 0.0805  604 TYR A C   
2400 O O   . TYR A 308 ? 1.7338 1.2105 0.8185 -0.7632 -0.1869 0.0910  604 TYR A O   
2401 C CB  . TYR A 308 ? 1.4880 0.9131 0.6525 -0.6486 -0.1734 0.0755  604 TYR A CB  
2402 C CG  . TYR A 308 ? 1.5644 1.0305 0.7506 -0.6572 -0.1662 0.0802  604 TYR A CG  
2403 C CD1 . TYR A 308 ? 1.4075 0.9818 0.7089 -0.6263 -0.1571 0.0757  604 TYR A CD1 
2404 C CD2 . TYR A 308 ? 1.7328 1.1299 0.8201 -0.6981 -0.1691 0.0888  604 TYR A CD2 
2405 C CE1 . TYR A 308 ? 1.4669 1.0807 0.7877 -0.6339 -0.1501 0.0801  604 TYR A CE1 
2406 C CE2 . TYR A 308 ? 1.7274 1.1646 0.8343 -0.7071 -0.1625 0.0927  604 TYR A CE2 
2407 C CZ  . TYR A 308 ? 1.6128 1.1598 0.8387 -0.6742 -0.1524 0.0886  604 TYR A CZ  
2408 O OH  . TYR A 308 ? 1.6118 1.2013 0.8591 -0.6811 -0.1452 0.0925  604 TYR A OH  
2409 N N   . ASN A 309 ? 1.5596 1.0287 0.7371 -0.6706 -0.1864 0.0716  605 ASN A N   
2410 C CA  . ASN A 309 ? 1.7134 1.1571 0.8437 -0.6983 -0.1949 0.0737  605 ASN A CA  
2411 C C   . ASN A 309 ? 1.9364 1.2324 0.9148 -0.7338 -0.2028 0.0815  605 ASN A C   
2412 O O   . ASN A 309 ? 2.1109 1.4118 1.0314 -0.7954 -0.2080 0.0920  605 ASN A O   
2413 C CB  . ASN A 309 ? 1.6575 1.2507 0.8550 -0.7393 -0.1941 0.0798  605 ASN A CB  
2414 C CG  . ASN A 309 ? 1.5962 1.1971 0.7869 -0.7514 -0.2020 0.0784  605 ASN A CG  
2415 O OD1 . ASN A 309 ? 1.5298 1.0687 0.7162 -0.7126 -0.2057 0.0688  605 ASN A OD1 
2416 N ND2 . ASN A 309 ? 1.6296 1.3108 0.8178 -0.8061 -0.2046 0.0878  605 ASN A ND2 
2417 N N   . ILE A 310 ? 1.9284 1.0909 0.8369 -0.6919 -0.2040 0.0759  606 ILE A N   
2418 C CA  . ILE A 310 ? 2.0899 1.0997 0.8444 -0.7138 -0.2117 0.0819  606 ILE A CA  
2419 C C   . ILE A 310 ? 2.1604 1.0582 0.8330 -0.6948 -0.2192 0.0779  606 ILE A C   
2420 O O   . ILE A 310 ? 2.2784 1.0377 0.8111 -0.7078 -0.2265 0.0822  606 ILE A O   
2421 C CB  . ILE A 310 ? 2.1467 1.0748 0.8573 -0.6783 -0.2086 0.0790  606 ILE A CB  
2422 C CG1 . ILE A 310 ? 2.1537 1.0083 0.8635 -0.5990 -0.2069 0.0664  606 ILE A CG1 
2423 C CG2 . ILE A 310 ? 1.8779 0.9247 0.6918 -0.6813 -0.1995 0.0803  606 ILE A CG2 
2424 C CD1 . ILE A 310 ? 1.9667 0.7726 0.6646 -0.5527 -0.2023 0.0618  606 ILE A CD1 
2425 N N   . LEU A 311 ? 2.1283 1.0765 0.8771 -0.6618 -0.2179 0.0692  607 LEU A N   
2426 C CA  . LEU A 311 ? 2.0829 0.9323 0.7551 -0.6463 -0.2246 0.0657  607 LEU A CA  
2427 C C   . LEU A 311 ? 2.2729 1.0656 0.8361 -0.7162 -0.2346 0.0780  607 LEU A C   
2428 O O   . LEU A 311 ? 2.3293 0.9818 0.7658 -0.7121 -0.2417 0.0793  607 LEU A O   
2429 C CB  . LEU A 311 ? 1.9210 0.8579 0.6992 -0.6164 -0.2226 0.0556  607 LEU A CB  
2430 C CG  . LEU A 311 ? 1.8147 0.7649 0.6652 -0.5400 -0.2151 0.0414  607 LEU A CG  
2431 C CD1 . LEU A 311 ? 1.7531 0.7991 0.7019 -0.5258 -0.2152 0.0328  607 LEU A CD1 
2432 C CD2 . LEU A 311 ? 1.9121 0.7165 0.6605 -0.4864 -0.2153 0.0359  607 LEU A CD2 
2433 N N   . GLU A 312 ? 2.3736 1.2755 0.9799 -0.7803 -0.2350 0.0876  608 GLU A N   
2434 C CA  . GLU A 312 ? 2.6916 1.5552 1.1966 -0.8566 -0.2442 0.1009  608 GLU A CA  
2435 C C   . GLU A 312 ? 2.8376 1.5292 1.1744 -0.8714 -0.2509 0.1070  608 GLU A C   
2436 O O   . GLU A 312 ? 2.9561 1.5280 1.1696 -0.8912 -0.2604 0.1112  608 GLU A O   
2437 C CB  . GLU A 312 ? 2.7571 1.7717 1.3327 -0.9164 -0.2409 0.1103  608 GLU A CB  
2438 C CG  . GLU A 312 ? 2.6841 1.8614 1.3907 -0.9194 -0.2384 0.1073  608 GLU A CG  
2439 C CD  . GLU A 312 ? 2.8014 1.9758 1.4538 -0.9750 -0.2481 0.1147  608 GLU A CD  
2440 O OE1 . GLU A 312 ? 2.9184 1.9439 1.4400 -0.9899 -0.2568 0.1180  608 GLU A OE1 
2441 O OE2 . GLU A 312 ? 2.7446 2.0659 1.4813 -1.0026 -0.2474 0.1174  608 GLU A OE2 
2442 N N   . GLU A 313 ? 2.8064 1.4798 1.1308 -0.8612 -0.2468 0.1072  609 GLU A N   
2443 C CA  . GLU A 313 ? 2.9472 1.4693 1.1080 -0.8852 -0.2545 0.1133  609 GLU A CA  
2444 C C   . GLU A 313 ? 2.9496 1.3122 1.0161 -0.8153 -0.2573 0.1042  609 GLU A C   
2445 O O   . GLU A 313 ? 3.0615 1.2828 0.9887 -0.8276 -0.2662 0.1053  609 GLU A O   
2446 C CB  . GLU A 313 ? 2.9695 1.5368 1.1495 -0.9044 -0.2499 0.1164  609 GLU A CB  
2447 C CG  . GLU A 313 ? 3.1029 1.7358 1.2564 -0.9974 -0.2534 0.1303  609 GLU A CG  
2448 C CD  . GLU A 313 ? 3.3758 1.8703 1.3602 -1.0543 -0.2663 0.1376  609 GLU A CD  
2449 O OE1 . GLU A 313 ? 3.4162 1.8761 1.3626 -1.0685 -0.2725 0.1401  609 GLU A OE1 
2450 O OE2 . GLU A 313 ? 3.5108 1.9319 1.4098 -1.0830 -0.2700 0.1385  609 GLU A OE2 
2451 N N   . VAL A 314 ? 2.8201 1.2132 0.9761 -0.7369 -0.2484 0.0918  610 VAL A N   
2452 C CA  . VAL A 314 ? 2.8523 1.1140 0.9293 -0.6622 -0.2494 0.0822  610 VAL A CA  
2453 C C   . VAL A 314 ? 2.9556 1.1352 0.9563 -0.6578 -0.2563 0.0824  610 VAL A C   
2454 O O   . VAL A 314 ? 2.9329 0.9730 0.8187 -0.6258 -0.2603 0.0770  610 VAL A O   
2455 C CB  . VAL A 314 ? 2.6467 0.9841 0.8520 -0.5840 -0.2377 0.0693  610 VAL A CB  
2456 C CG1 . VAL A 314 ? 2.7056 0.9232 0.8324 -0.5027 -0.2373 0.0594  610 VAL A CG1 
2457 C CG2 . VAL A 314 ? 2.5382 0.9489 0.8096 -0.5934 -0.2317 0.0706  610 VAL A CG2 
2458 N N   . ALA A 315 ? 2.8905 1.1683 0.9780 -0.6844 -0.2558 0.0837  611 ALA A N   
2459 C CA  . ALA A 315 ? 3.0116 1.2146 1.0255 -0.6894 -0.2631 0.0849  611 ALA A CA  
2460 C C   . ALA A 315 ? 3.1686 1.2437 1.0201 -0.7481 -0.2746 0.0948  611 ALA A C   
2461 O O   . ALA A 315 ? 3.3290 1.2676 1.0711 -0.7193 -0.2794 0.0896  611 ALA A O   
2462 C CB  . ALA A 315 ? 2.8869 1.2279 1.0230 -0.7189 -0.2618 0.0846  611 ALA A CB  
2463 N N   . LYS A 316 ? 3.1158 1.2416 0.9619 -0.8273 -0.2778 0.1058  612 LYS A N   
2464 C CA  . LYS A 316 ? 3.2863 1.3070 0.9946 -0.8914 -0.2884 0.1128  612 LYS A CA  
2465 C C   . LYS A 316 ? 3.4367 1.2906 1.0193 -0.8490 -0.2911 0.1046  612 LYS A C   
2466 O O   . LYS A 316 ? 3.5523 1.2683 1.0133 -0.8408 -0.2986 0.1025  612 LYS A O   
2467 C CB  . LYS A 316 ? 3.2297 1.3485 0.9631 -0.9778 -0.2893 0.1251  612 LYS A CB  
2468 C CG  . LYS A 316 ? 3.0978 1.3847 0.9415 -1.0251 -0.2871 0.1348  612 LYS A CG  
2469 C CD  . LYS A 316 ? 3.1452 1.5074 0.9760 -1.1184 -0.2899 0.1479  612 LYS A CD  
2470 C CE  . LYS A 316 ? 3.3865 1.6082 1.0539 -1.1774 -0.3025 0.1531  612 LYS A CE  
2471 N NZ  . LYS A 316 ? 3.4800 1.7466 1.1132 -1.2610 -0.3050 0.1634  612 LYS A NZ  
2472 N N   . LYS A 317 ? 3.3389 1.2023 0.9470 -0.8185 -0.2850 0.0998  613 LYS A N   
2473 C CA  . LYS A 317 ? 3.4943 1.2069 0.9792 -0.7860 -0.2880 0.0933  613 LYS A CA  
2474 C C   . LYS A 317 ? 3.5473 1.1485 0.9746 -0.6971 -0.2870 0.0817  613 LYS A C   
2475 O O   . LYS A 317 ? 3.7777 1.2361 1.0786 -0.6710 -0.2913 0.0772  613 LYS A O   
2476 C CB  . LYS A 317 ? 3.4134 1.1749 0.9531 -0.7669 -0.2809 0.0902  613 LYS A CB  
2477 C CG  . LYS A 317 ? 3.4635 1.2558 0.9797 -0.8527 -0.2846 0.1003  613 LYS A CG  
2478 C CD  . LYS A 317 ? 3.2714 1.2494 0.9409 -0.8783 -0.2763 0.1056  613 LYS A CD  
2479 C CE  . LYS A 317 ? 3.3254 1.3462 0.9713 -0.9664 -0.2795 0.1162  613 LYS A CE  
2480 N NZ  . LYS A 317 ? 3.1504 1.3451 0.9402 -0.9770 -0.2698 0.1197  613 LYS A NZ  
2481 N N   . MET A 318 ? 3.4354 1.0990 0.9481 -0.6490 -0.2814 0.0769  614 MET A N   
2482 C CA  . MET A 318 ? 3.5099 1.0767 0.9638 -0.5727 -0.2807 0.0673  614 MET A CA  
2483 C C   . MET A 318 ? 3.6217 1.1062 0.9816 -0.6086 -0.2905 0.0720  614 MET A C   
2484 O O   . MET A 318 ? 3.7260 1.0998 1.0002 -0.5533 -0.2919 0.0652  614 MET A O   
2485 C CB  . MET A 318 ? 3.3057 0.9760 0.8907 -0.5026 -0.2699 0.0592  614 MET A CB  
2486 C CG  . MET A 318 ? 3.2945 1.0333 0.9643 -0.4539 -0.2601 0.0530  614 MET A CG  
2487 S SD  . MET A 318 ? 3.1033 0.9887 0.9399 -0.3975 -0.2486 0.0466  614 MET A SD  
2488 C CE  . MET A 318 ? 3.0584 0.8586 0.8354 -0.3147 -0.2463 0.0365  614 MET A CE  
2489 N N   . ASP A 319 ? 3.6230 1.1620 0.9953 -0.6991 -0.2971 0.0838  615 ASP A N   
2490 C CA  . ASP A 319 ? 3.7456 1.2378 1.0547 -0.7408 -0.3061 0.0895  615 ASP A CA  
2491 C C   . ASP A 319 ? 3.6077 1.1453 0.9910 -0.6835 -0.3009 0.0830  615 ASP A C   
2492 O O   . ASP A 319 ? 3.6931 1.1262 1.0032 -0.6232 -0.3012 0.0751  615 ASP A O   
2493 C CB  . ASP A 319 ? 4.0128 1.3137 1.1354 -0.7458 -0.3164 0.0892  615 ASP A CB  
2494 C CG  . ASP A 319 ? 4.2008 1.4604 1.2419 -0.8343 -0.3288 0.1006  615 ASP A CG  
2495 O OD1 . ASP A 319 ? 4.1686 1.5363 1.2677 -0.9158 -0.3310 0.1116  615 ASP A OD1 
2496 O OD2 . ASP A 319 ? 4.3628 1.4857 1.2808 -0.8223 -0.3364 0.0990  615 ASP A OD2 
2497 N N   . LEU A 320 ? 3.4369 1.1298 0.9612 -0.7010 -0.2960 0.0863  616 LEU A N   
2498 C CA  . LEU A 320 ? 3.3659 1.1125 0.9662 -0.6563 -0.2917 0.0809  616 LEU A CA  
2499 C C   . LEU A 320 ? 3.3925 1.1897 1.0056 -0.7286 -0.2995 0.0913  616 LEU A C   
2500 O O   . LEU A 320 ? 3.4062 1.2514 1.0158 -0.8127 -0.3051 0.1032  616 LEU A O   
2501 C CB  . LEU A 320 ? 3.1087 0.9906 0.8610 -0.6094 -0.2799 0.0753  616 LEU A CB  
2502 C CG  . LEU A 320 ? 3.0996 0.9461 0.8506 -0.5342 -0.2715 0.0649  616 LEU A CG  
2503 C CD1 . LEU A 320 ? 2.9542 0.9374 0.8601 -0.4896 -0.2601 0.0582  616 LEU A CD1 
2504 C CD2 . LEU A 320 ? 3.2200 0.9316 0.8671 -0.4626 -0.2711 0.0552  616 LEU A CD2 
2505 N N   . ASP A 321 ? 3.3272 1.1176 0.9541 -0.6947 -0.2996 0.0867  617 ASP A N   
2506 C CA  . ASP A 321 ? 3.3558 1.2093 1.0190 -0.7521 -0.3060 0.0907  617 ASP A CA  
2507 C C   . ASP A 321 ? 3.0976 1.1563 0.9491 -0.7737 -0.2996 0.0863  617 ASP A C   
2508 O O   . ASP A 321 ? 2.9180 1.0668 0.8885 -0.7255 -0.2929 0.0731  617 ASP A O   
2509 C CB  . ASP A 321 ? 3.4567 1.2506 1.0952 -0.7008 -0.3067 0.0813  617 ASP A CB  
2510 C CG  . ASP A 321 ? 3.5244 1.3749 1.1933 -0.7578 -0.3147 0.0830  617 ASP A CG  
2511 O OD1 . ASP A 321 ? 3.4163 1.4068 1.2310 -0.7440 -0.3100 0.0725  617 ASP A OD1 
2512 O OD2 . ASP A 321 ? 3.7157 1.4691 1.2576 -0.8173 -0.3265 0.0947  617 ASP A OD2 
2513 N N   . MET A 322 ? 3.0563 1.1904 0.9306 -0.8451 -0.3017 0.0974  618 MET A N   
2514 C CA  . MET A 322 ? 2.9478 1.2788 0.9920 -0.8654 -0.2960 0.0946  618 MET A CA  
2515 C C   . MET A 322 ? 2.9778 1.4023 1.0740 -0.9147 -0.3028 0.0960  618 MET A C   
2516 O O   . MET A 322 ? 2.8942 1.4866 1.1333 -0.9214 -0.2988 0.0920  618 MET A O   
2517 C CB  . MET A 322 ? 2.9646 1.3499 1.0165 -0.9149 -0.2937 0.1055  618 MET A CB  
2518 C CG  . MET A 322 ? 2.9232 1.2982 1.0045 -0.8574 -0.2839 0.0995  618 MET A CG  
2519 S SD  . MET A 322 ? 2.9326 1.3870 1.0396 -0.9100 -0.2801 0.1100  618 MET A SD  
2520 C CE  . MET A 322 ? 2.8459 1.5290 1.1233 -0.9526 -0.2765 0.1113  618 MET A CE  
2521 N N   . ARG A 323 ? 3.1215 1.4424 1.1039 -0.9461 -0.3134 0.1011  619 ARG A N   
2522 C CA  . ARG A 323 ? 3.1994 1.6092 1.2298 -0.9907 -0.3209 0.1013  619 ARG A CA  
2523 C C   . ARG A 323 ? 3.0986 1.6030 1.2604 -0.9281 -0.3164 0.0837  619 ARG A C   
2524 O O   . ARG A 323 ? 3.0275 1.6817 1.2995 -0.9503 -0.3186 0.0808  619 ARG A O   
2525 C CB  . ARG A 323 ? 3.4186 1.6808 1.2904 -1.0318 -0.3336 0.1094  619 ARG A CB  
2526 C CG  . ARG A 323 ? 3.6241 1.8033 1.3584 -1.1120 -0.3411 0.1285  619 ARG A CG  
2527 C CD  . ARG A 323 ? 3.8800 1.8408 1.4225 -1.1095 -0.3500 0.1335  619 ARG A CD  
2528 N NE  . ARG A 323 ? 3.9840 1.8152 1.4384 -1.0584 -0.3453 0.1334  619 ARG A NE  
2529 C CZ  . ARG A 323 ? 4.1190 1.7695 1.4371 -1.0130 -0.3489 0.1302  619 ARG A CZ  
2530 N NH1 . ARG A 323 ? 4.1499 1.7180 1.3949 -1.0153 -0.3569 0.1298  619 ARG A NH1 
2531 N NH2 . ARG A 323 ? 4.1287 1.6954 1.4027 -0.9585 -0.3437 0.1216  619 ARG A NH2 
2532 N N   . LYS A 324 ? 3.0199 1.4410 1.1670 -0.8489 -0.3105 0.0718  620 LYS A N   
2533 C CA  . LYS A 324 ? 2.7846 1.2690 1.0288 -0.7897 -0.3068 0.0551  620 LYS A CA  
2534 C C   . LYS A 324 ? 2.6012 1.1684 0.9613 -0.7281 -0.2939 0.0451  620 LYS A C   
2535 O O   . LYS A 324 ? 2.6784 1.1810 1.0019 -0.6970 -0.2868 0.0467  620 LYS A O   
2536 C CB  . LYS A 324 ? 2.8855 1.2209 1.0252 -0.7443 -0.3087 0.0487  620 LYS A CB  
2537 C CG  . LYS A 324 ? 2.9595 1.2989 1.0850 -0.7699 -0.3191 0.0454  620 LYS A CG  
2538 C CD  . LYS A 324 ? 3.0620 1.3894 1.1155 -0.8640 -0.3321 0.0606  620 LYS A CD  
2539 C CE  . LYS A 324 ? 3.0730 1.4306 1.1341 -0.8882 -0.3429 0.0556  620 LYS A CE  
2540 N NZ  . LYS A 324 ? 3.1843 1.5650 1.1979 -0.9838 -0.3555 0.0701  620 LYS A NZ  
2541 N N   . THR A 325 ? 2.3412 1.0505 0.8362 -0.7110 -0.2920 0.0351  621 THR A N   
2542 C CA  . THR A 325 ? 2.2025 0.9874 0.8047 -0.6522 -0.2807 0.0250  621 THR A CA  
2543 C C   . THR A 325 ? 2.3452 1.0302 0.9078 -0.5748 -0.2728 0.0139  621 THR A C   
2544 O O   . THR A 325 ? 2.1580 0.8348 0.7430 -0.5293 -0.2627 0.0103  621 THR A O   
2545 C CB  . THR A 325 ? 2.0935 1.0427 0.8325 -0.6517 -0.2826 0.0175  621 THR A CB  
2546 O OG1 . THR A 325 ? 2.0007 0.9902 0.8198 -0.5850 -0.2730 0.0052  621 THR A OG1 
2547 C CG2 . THR A 325 ? 2.2176 1.1686 0.9392 -0.6664 -0.2932 0.0133  621 THR A CG2 
2548 N N   . SER A 326 ? 2.4756 1.0872 0.9771 -0.5585 -0.2769 0.0085  622 SER A N   
2549 C CA  . SER A 326 ? 2.4438 0.9708 0.9052 -0.4838 -0.2689 -0.0021 622 SER A CA  
2550 C C   . SER A 326 ? 2.4402 0.8152 0.7721 -0.4580 -0.2657 0.0041  622 SER A C   
2551 O O   . SER A 326 ? 2.4768 0.7781 0.7632 -0.3919 -0.2585 -0.0033 622 SER A O   
2552 C CB  . SER A 326 ? 2.3349 0.8405 0.7710 -0.4806 -0.2750 -0.0089 622 SER A CB  
2553 O OG  . SER A 326 ? 2.3965 0.9164 0.8059 -0.5550 -0.2890 -0.0003 622 SER A OG  
2554 N N   . SER A 327 ? 2.5267 0.8552 0.7937 -0.5057 -0.2708 0.0176  623 SER A N   
2555 C CA  . SER A 327 ? 2.7227 0.9132 0.8690 -0.4749 -0.2683 0.0231  623 SER A CA  
2556 C C   . SER A 327 ? 2.6402 0.8677 0.8467 -0.4178 -0.2560 0.0174  623 SER A C   
2557 O O   . SER A 327 ? 2.6552 0.7782 0.7710 -0.3737 -0.2527 0.0189  623 SER A O   
2558 C CB  . SER A 327 ? 2.8967 1.0177 0.9403 -0.5487 -0.2788 0.0398  623 SER A CB  
2559 O OG  . SER A 327 ? 2.7030 0.9285 0.8279 -0.5889 -0.2769 0.0453  623 SER A OG  
2560 N N   . LEU A 328 ? 2.5219 0.8939 0.8735 -0.4170 -0.2500 0.0112  624 LEU A N   
2561 C CA  . LEU A 328 ? 2.3606 0.7812 0.7813 -0.3691 -0.2386 0.0057  624 LEU A CA  
2562 C C   . LEU A 328 ? 2.4699 0.8342 0.8268 -0.3873 -0.2397 0.0161  624 LEU A C   
2563 O O   . LEU A 328 ? 2.4268 0.7706 0.7818 -0.3356 -0.2317 0.0124  624 LEU A O   
2564 C CB  . LEU A 328 ? 2.3354 0.7205 0.7498 -0.2810 -0.2278 -0.0061 624 LEU A CB  
2565 C CG  . LEU A 328 ? 2.2137 0.6488 0.6818 -0.2622 -0.2260 -0.0167 624 LEU A CG  
2566 C CD1 . LEU A 328 ? 2.1757 0.6090 0.6608 -0.1763 -0.2121 -0.0283 624 LEU A CD1 
2567 C CD2 . LEU A 328 ? 2.0681 0.6467 0.6665 -0.3032 -0.2287 -0.0194 624 LEU A CD2 
2568 N N   . TRP A 329 ? 2.5206 0.8671 0.8263 -0.4626 -0.2495 0.0290  625 TRP A N   
2569 C CA  . TRP A 329 ? 2.5577 0.8579 0.8024 -0.4884 -0.2510 0.0391  625 TRP A CA  
2570 C C   . TRP A 329 ? 2.4501 0.8654 0.8162 -0.4767 -0.2422 0.0355  625 TRP A C   
2571 O O   . TRP A 329 ? 2.4613 0.8327 0.7897 -0.4590 -0.2392 0.0376  625 TRP A O   
2572 C CB  . TRP A 329 ? 2.6466 0.9274 0.8245 -0.5789 -0.2623 0.0539  625 TRP A CB  
2573 C CG  . TRP A 329 ? 2.5272 0.9635 0.8263 -0.6335 -0.2636 0.0557  625 TRP A CG  
2574 C CD1 . TRP A 329 ? 2.5753 1.0618 0.9094 -0.6563 -0.2689 0.0535  625 TRP A CD1 
2575 C CD2 . TRP A 329 ? 2.5310 1.0960 0.9289 -0.6681 -0.2598 0.0599  625 TRP A CD2 
2576 N NE1 . TRP A 329 ? 2.4902 1.1326 0.9391 -0.7004 -0.2690 0.0559  625 TRP A NE1 
2577 C CE2 . TRP A 329 ? 2.4379 1.1317 0.9278 -0.7075 -0.2629 0.0602  625 TRP A CE2 
2578 C CE3 . TRP A 329 ? 2.3611 0.9463 0.7767 -0.6671 -0.2541 0.0632  625 TRP A CE3 
2579 C CZ2 . TRP A 329 ? 2.3337 1.1776 0.9307 -0.7420 -0.2598 0.0641  625 TRP A CZ2 
2580 C CZ3 . TRP A 329 ? 2.3363 1.0663 0.8583 -0.7049 -0.2507 0.0673  625 TRP A CZ3 
2581 C CH2 . TRP A 329 ? 2.3113 1.1702 0.9223 -0.7400 -0.2531 0.0679  625 TRP A CH2 
2582 N N   . LYS A 330 ? 2.3037 0.8636 0.8108 -0.4851 -0.2388 0.0299  626 LYS A N   
2583 C CA  . LYS A 330 ? 2.1635 0.8325 0.7869 -0.4708 -0.2305 0.0263  626 LYS A CA  
2584 C C   . LYS A 330 ? 2.0602 0.6983 0.6964 -0.3899 -0.2207 0.0154  626 LYS A C   
2585 O O   . LYS A 330 ? 2.1799 0.8346 0.8419 -0.3738 -0.2152 0.0156  626 LYS A O   
2586 C CB  . LYS A 330 ? 2.1148 0.9363 0.8748 -0.4884 -0.2300 0.0216  626 LYS A CB  
2587 C CG  . LYS A 330 ? 2.0827 0.9875 0.8686 -0.5650 -0.2364 0.0328  626 LYS A CG  
2588 C CD  . LYS A 330 ? 1.8849 0.9478 0.8085 -0.5678 -0.2357 0.0271  626 LYS A CD  
2589 C CE  . LYS A 330 ? 1.7841 0.9512 0.7432 -0.6354 -0.2397 0.0385  626 LYS A CE  
2590 N NZ  . LYS A 330 ? 1.6238 0.9439 0.7061 -0.6329 -0.2407 0.0333  626 LYS A NZ  
2591 N N   . ASP A 331 ? 2.1382 0.7389 0.7592 -0.3381 -0.2180 0.0059  627 ASP A N   
2592 C CA  . ASP A 331 ? 2.0891 0.6761 0.7262 -0.2584 -0.2072 -0.0045 627 ASP A CA  
2593 C C   . ASP A 331 ? 2.2323 0.7045 0.7569 -0.2276 -0.2065 -0.0004 627 ASP A C   
2594 O O   . ASP A 331 ? 2.2923 0.7820 0.8456 -0.1902 -0.1993 -0.0034 627 ASP A O   
2595 C CB  . ASP A 331 ? 2.1125 0.6882 0.7487 -0.2143 -0.2039 -0.0142 627 ASP A CB  
2596 C CG  . ASP A 331 ? 1.9705 0.6547 0.7093 -0.2418 -0.2059 -0.0194 627 ASP A CG  
2597 O OD1 . ASP A 331 ? 1.8984 0.6010 0.6322 -0.3037 -0.2160 -0.0126 627 ASP A OD1 
2598 O OD2 . ASP A 331 ? 1.7689 0.5234 0.5912 -0.2015 -0.1978 -0.0298 627 ASP A OD2 
2599 N N   . GLN A 332 ? 2.3297 0.6815 0.7205 -0.2425 -0.2148 0.0065  628 GLN A N   
2600 C CA  . GLN A 332 ? 2.5401 0.7692 0.8036 -0.2129 -0.2165 0.0104  628 GLN A CA  
2601 C C   . GLN A 332 ? 2.4964 0.7371 0.7627 -0.2461 -0.2179 0.0168  628 GLN A C   
2602 O O   . GLN A 332 ? 2.4555 0.6665 0.6980 -0.1992 -0.2133 0.0137  628 GLN A O   
2603 C CB  . GLN A 332 ? 2.7401 0.8354 0.8531 -0.2381 -0.2275 0.0184  628 GLN A CB  
2604 C CG  . GLN A 332 ? 2.8364 0.8149 0.8342 -0.1640 -0.2258 0.0148  628 GLN A CG  
2605 C CD  . GLN A 332 ? 2.9806 0.8504 0.8606 -0.1824 -0.2351 0.0201  628 GLN A CD  
2606 O OE1 . GLN A 332 ? 2.9580 0.8210 0.8187 -0.2591 -0.2448 0.0288  628 GLN A OE1 
2607 N NE2 . GLN A 332 ? 3.0710 0.8686 0.8853 -0.1114 -0.2307 0.0125  628 GLN A NE2 
2608 N N   . ALA A 333 ? 2.3967 0.6867 0.6920 -0.3263 -0.2241 0.0259  629 ALA A N   
2609 C CA  . ALA A 333 ? 2.4770 0.7874 0.7783 -0.3623 -0.2247 0.0327  629 ALA A CA  
2610 C C   . ALA A 333 ? 2.3852 0.8064 0.8194 -0.3274 -0.2140 0.0252  629 ALA A C   
2611 O O   . ALA A 333 ? 2.2577 0.6761 0.6858 -0.3316 -0.2125 0.0281  629 ALA A O   
2612 C CB  . ALA A 333 ? 2.4010 0.7599 0.7119 -0.4550 -0.2320 0.0446  629 ALA A CB  
2613 N N   . LEU A 334 ? 2.2165 0.7292 0.7636 -0.2937 -0.2069 0.0157  630 LEU A N   
2614 C CA  . LEU A 334 ? 1.9813 0.5889 0.6442 -0.2594 -0.1972 0.0089  630 LEU A CA  
2615 C C   . LEU A 334 ? 2.0924 0.6446 0.7186 -0.1800 -0.1900 0.0017  630 LEU A C   
2616 O O   . LEU A 334 ? 2.1912 0.7764 0.8596 -0.1607 -0.1847 0.0008  630 LEU A O   
2617 C CB  . LEU A 334 ? 1.8111 0.5329 0.5989 -0.2541 -0.1930 0.0011  630 LEU A CB  
2618 C CG  . LEU A 334 ? 1.8251 0.6504 0.7348 -0.2301 -0.1845 -0.0047 630 LEU A CG  
2619 C CD1 . LEU A 334 ? 1.7355 0.6689 0.7321 -0.2917 -0.1876 0.0010  630 LEU A CD1 
2620 C CD2 . LEU A 334 ? 1.7589 0.6247 0.7302 -0.1741 -0.1772 -0.0171 630 LEU A CD2 
2621 N N   . VAL A 335 ? 2.0770 0.5495 0.6233 -0.1319 -0.1896 -0.0028 631 VAL A N   
2622 C CA  . VAL A 335 ? 2.1923 0.6248 0.7013 -0.0518 -0.1822 -0.0092 631 VAL A CA  
2623 C C   . VAL A 335 ? 2.3728 0.7170 0.7809 -0.0546 -0.1873 -0.0037 631 VAL A C   
2624 O O   . VAL A 335 ? 2.3878 0.7492 0.8159 -0.0097 -0.1810 -0.0074 631 VAL A O   
2625 C CB  . VAL A 335 ? 2.2529 0.6279 0.6964 0.0014  -0.1801 -0.0144 631 VAL A CB  
2626 C CG1 . VAL A 335 ? 2.3635 0.6841 0.7375 0.0799  -0.1746 -0.0182 631 VAL A CG1 
2627 C CG2 . VAL A 335 ? 2.0865 0.5624 0.6425 0.0215  -0.1716 -0.0228 631 VAL A CG2 
2628 N N   . GLU A 336 ? 2.4196 0.6696 0.7162 -0.1092 -0.1988 0.0053  632 GLU A N   
2629 C CA  . GLU A 336 ? 2.6050 0.7606 0.7918 -0.1177 -0.2048 0.0100  632 GLU A CA  
2630 C C   . GLU A 336 ? 2.4546 0.6867 0.7243 -0.1447 -0.2016 0.0122  632 GLU A C   
2631 O O   . GLU A 336 ? 2.4333 0.6284 0.6643 -0.1131 -0.2002 0.0100  632 GLU A O   
2632 C CB  . GLU A 336 ? 2.7636 0.8127 0.8197 -0.1844 -0.2181 0.0204  632 GLU A CB  
2633 C CG  . GLU A 336 ? 2.9754 0.9603 0.9675 -0.1772 -0.2217 0.0197  632 GLU A CG  
2634 C CD  . GLU A 336 ? 3.1390 1.0354 1.0493 -0.0941 -0.2178 0.0107  632 GLU A CD  
2635 O OE1 . GLU A 336 ? 3.1510 1.0136 1.0277 -0.0527 -0.2147 0.0065  632 GLU A OE1 
2636 O OE2 . GLU A 336 ? 3.1964 1.0613 1.0764 -0.0692 -0.2177 0.0083  632 GLU A OE2 
2637 N N   . ILE A 337 ? 2.3195 0.6573 0.6980 -0.2032 -0.2009 0.0169  633 ILE A N   
2638 C CA  . ILE A 337 ? 2.2453 0.6632 0.7056 -0.2331 -0.1976 0.0206  633 ILE A CA  
2639 C C   . ILE A 337 ? 2.2415 0.7119 0.7799 -0.1641 -0.1873 0.0123  633 ILE A C   
2640 O O   . ILE A 337 ? 2.1319 0.5993 0.6683 -0.1590 -0.1858 0.0139  633 ILE A O   
2641 C CB  . ILE A 337 ? 2.0610 0.5968 0.6299 -0.2976 -0.1976 0.0260  633 ILE A CB  
2642 C CG1 . ILE A 337 ? 2.2258 0.7169 0.7107 -0.3748 -0.2078 0.0371  633 ILE A CG1 
2643 C CG2 . ILE A 337 ? 1.9322 0.5763 0.6149 -0.3100 -0.1911 0.0276  633 ILE A CG2 
2644 C CD1 . ILE A 337 ? 2.1357 0.7452 0.7161 -0.4339 -0.2082 0.0423  633 ILE A CD1 
2645 N N   . ASN A 338 ? 2.1305 0.6481 0.7331 -0.1098 -0.1801 0.0036  634 ASN A N   
2646 C CA  . ASN A 338 ? 1.9895 0.5735 0.6755 -0.0484 -0.1698 -0.0030 634 ASN A CA  
2647 C C   . ASN A 338 ? 2.1017 0.6140 0.7047 0.0233  -0.1672 -0.0077 634 ASN A C   
2648 O O   . ASN A 338 ? 2.0078 0.5687 0.6642 0.0651  -0.1603 -0.0101 634 ASN A O   
2649 C CB  . ASN A 338 ? 1.8957 0.5684 0.6845 -0.0216 -0.1625 -0.0102 634 ASN A CB  
2650 C CG  . ASN A 338 ? 1.8531 0.6279 0.7557 -0.0764 -0.1628 -0.0077 634 ASN A CG  
2651 O OD1 . ASN A 338 ? 1.8568 0.7022 0.8422 -0.0753 -0.1585 -0.0069 634 ASN A OD1 
2652 N ND2 . ASN A 338 ? 1.7007 0.4847 0.6037 -0.1246 -0.1687 -0.0061 634 ASN A ND2 
2653 N N   . ILE A 339 ? 2.2388 0.6394 0.7107 0.0397  -0.1729 -0.0086 635 ILE A N   
2654 C CA  . ILE A 339 ? 2.3294 0.6511 0.7024 0.1013  -0.1725 -0.0124 635 ILE A CA  
2655 C C   . ILE A 339 ? 2.3337 0.6069 0.6563 0.0696  -0.1781 -0.0078 635 ILE A C   
2656 O O   . ILE A 339 ? 2.4578 0.7132 0.7532 0.1199  -0.1752 -0.0115 635 ILE A O   
2657 C CB  . ILE A 339 ? 2.5554 0.7584 0.7866 0.1242  -0.1784 -0.0137 635 ILE A CB  
2658 C CG1 . ILE A 339 ? 2.3606 0.6141 0.6401 0.1654  -0.1712 -0.0188 635 ILE A CG1 
2659 C CG2 . ILE A 339 ? 2.5571 0.6660 0.6666 0.1853  -0.1798 -0.0175 635 ILE A CG2 
2660 C CD1 . ILE A 339 ? 2.5744 0.7123 0.7168 0.1841  -0.1774 -0.0182 635 ILE A CD1 
2661 N N   . ALA A 340 ? 2.3286 0.5874 0.6397 -0.0142 -0.1859 0.0007  636 ALA A N   
2662 C CA  . ALA A 340 ? 2.4164 0.6224 0.6664 -0.0529 -0.1917 0.0057  636 ALA A CA  
2663 C C   . ALA A 340 ? 2.3541 0.6633 0.7244 -0.0577 -0.1848 0.0078  636 ALA A C   
2664 O O   . ALA A 340 ? 2.3516 0.6253 0.6831 -0.0466 -0.1854 0.0078  636 ALA A O   
2665 C CB  . ALA A 340 ? 2.4779 0.6389 0.6656 -0.1431 -0.2020 0.0153  636 ALA A CB  
2666 N N   . VAL A 341 ? 2.2235 0.6546 0.7331 -0.0762 -0.1788 0.0098  637 VAL A N   
2667 C CA  . VAL A 341 ? 2.1227 0.6507 0.7456 -0.0734 -0.1720 0.0121  637 VAL A CA  
2668 C C   . VAL A 341 ? 2.2139 0.7481 0.8478 0.0118  -0.1654 0.0054  637 VAL A C   
2669 O O   . VAL A 341 ? 2.2504 0.7794 0.8788 0.0241  -0.1645 0.0075  637 VAL A O   
2670 C CB  . VAL A 341 ? 1.9550 0.6053 0.7155 -0.0994 -0.1672 0.0136  637 VAL A CB  
2671 C CG1 . VAL A 341 ? 1.8907 0.6327 0.7606 -0.0815 -0.1601 0.0154  637 VAL A CG1 
2672 C CG2 . VAL A 341 ? 1.9571 0.6269 0.7191 -0.1858 -0.1730 0.0217  637 VAL A CG2 
2673 N N   . LEU A 342 ? 2.1658 0.7187 0.8154 0.0717  -0.1602 -0.0023 638 LEU A N   
2674 C CA  . LEU A 342 ? 2.1702 0.7493 0.8336 0.1546  -0.1530 -0.0082 638 LEU A CA  
2675 C C   . LEU A 342 ? 2.2710 0.7469 0.8099 0.1820  -0.1576 -0.0101 638 LEU A C   
2676 O O   . LEU A 342 ? 2.1601 0.6612 0.7192 0.2136  -0.1548 -0.0097 638 LEU A O   
2677 C CB  . LEU A 342 ? 2.1615 0.7689 0.8381 0.2094  -0.1469 -0.0158 638 LEU A CB  
2678 C CG  . LEU A 342 ? 1.9990 0.7044 0.7925 0.1918  -0.1418 -0.0164 638 LEU A CG  
2679 C CD1 . LEU A 342 ? 1.8494 0.5889 0.6532 0.2554  -0.1339 -0.0239 638 LEU A CD1 
2680 C CD2 . LEU A 342 ? 1.9247 0.7357 0.8434 0.1805  -0.1375 -0.0123 638 LEU A CD2 
2681 N N   . TYR A 343 ? 2.4554 0.8104 0.8585 0.1707  -0.1654 -0.0119 639 TYR A N   
2682 C CA  . TYR A 343 ? 2.5228 0.7646 0.7899 0.2017  -0.1706 -0.0154 639 TYR A CA  
2683 C C   . TYR A 343 ? 2.5555 0.7750 0.8114 0.1581  -0.1747 -0.0100 639 TYR A C   
2684 O O   . TYR A 343 ? 2.5185 0.7072 0.7319 0.2005  -0.1742 -0.0132 639 TYR A O   
2685 C CB  . TYR A 343 ? 2.7467 0.8528 0.8606 0.1877  -0.1800 -0.0168 639 TYR A CB  
2686 C CG  . TYR A 343 ? 2.7995 0.7758 0.7694 0.2080  -0.1860 -0.0192 639 TYR A CG  
2687 C CD1 . TYR A 343 ? 2.8120 0.7635 0.7332 0.2964  -0.1815 -0.0262 639 TYR A CD1 
2688 C CD2 . TYR A 343 ? 2.8804 0.7683 0.7728 0.1377  -0.1951 -0.0132 639 TYR A CD2 
2689 C CE1 . TYR A 343 ? 3.0567 0.8906 0.8530 0.3173  -0.1866 -0.0278 639 TYR A CE1 
2690 C CE2 . TYR A 343 ? 3.1068 0.8735 0.8723 0.1552  -0.2001 -0.0150 639 TYR A CE2 
2691 C CZ  . TYR A 343 ? 3.1458 0.8816 0.8619 0.2465  -0.1961 -0.0225 639 TYR A CZ  
2692 O OH  . TYR A 343 ? 3.2932 0.9032 0.8767 0.2669  -0.2018 -0.0244 639 TYR A OH  
2693 N N   . SER A 344 ? 2.5433 0.7830 0.8362 0.0741  -0.1785 -0.0016 640 SER A N   
2694 C CA  . SER A 344 ? 2.4237 0.6510 0.7088 0.0282  -0.1815 0.0047  640 SER A CA  
2695 C C   . SER A 344 ? 2.3572 0.6820 0.7529 0.0670  -0.1732 0.0062  640 SER A C   
2696 O O   . SER A 344 ? 2.3059 0.5929 0.6587 0.0883  -0.1741 0.0058  640 SER A O   
2697 C CB  . SER A 344 ? 2.3441 0.6021 0.6616 -0.0683 -0.1855 0.0145  640 SER A CB  
2698 O OG  . SER A 344 ? 2.5021 0.6781 0.7197 -0.1035 -0.1938 0.0145  640 SER A OG  
2699 N N   . PHE A 345 ? 2.2334 0.6814 0.7672 0.0777  -0.1657 0.0082  641 PHE A N   
2700 C CA  . PHE A 345 ? 2.2195 0.7641 0.8574 0.1144  -0.1588 0.0111  641 PHE A CA  
2701 C C   . PHE A 345 ? 2.2928 0.8241 0.8938 0.2021  -0.1560 0.0035  641 PHE A C   
2702 O O   . PHE A 345 ? 2.1819 0.7273 0.7918 0.2242  -0.1553 0.0062  641 PHE A O   
2703 C CB  . PHE A 345 ? 1.9850 0.6532 0.7621 0.1132  -0.1525 0.0132  641 PHE A CB  
2704 C CG  . PHE A 345 ? 1.8127 0.5363 0.6635 0.0369  -0.1531 0.0232  641 PHE A CG  
2705 C CD1 . PHE A 345 ? 1.8737 0.5639 0.6880 -0.0352 -0.1579 0.0258  641 PHE A CD1 
2706 C CD2 . PHE A 345 ? 1.6563 0.4751 0.6133 0.0390  -0.1488 0.0302  641 PHE A CD2 
2707 C CE1 . PHE A 345 ? 1.8077 0.5689 0.6950 -0.1028 -0.1570 0.0343  641 PHE A CE1 
2708 C CE2 . PHE A 345 ? 1.6058 0.4804 0.6278 -0.0281 -0.1483 0.0388  641 PHE A CE2 
2709 C CZ  . PHE A 345 ? 1.6725 0.5243 0.6626 -0.0988 -0.1517 0.0401  641 PHE A CZ  
2710 N N   . GLN A 346 ? 2.2938 0.8030 0.8514 0.2533  -0.1541 -0.0055 642 GLN A N   
2711 C CA  . GLN A 346 ? 2.3139 0.8328 0.8444 0.3393  -0.1501 -0.0126 642 GLN A CA  
2712 C C   . GLN A 346 ? 2.4048 0.8058 0.8029 0.3538  -0.1564 -0.0154 642 GLN A C   
2713 O O   . GLN A 346 ? 2.2758 0.7029 0.6758 0.4083  -0.1539 -0.0174 642 GLN A O   
2714 C CB  . GLN A 346 ? 2.4055 0.9261 0.9094 0.3880  -0.1462 -0.0206 642 GLN A CB  
2715 C CG  . GLN A 346 ? 2.3797 1.0348 1.0196 0.3981  -0.1377 -0.0202 642 GLN A CG  
2716 C CD  . GLN A 346 ? 2.4525 1.0887 1.0539 0.4234  -0.1351 -0.0262 642 GLN A CD  
2717 O OE1 . GLN A 346 ? 2.5061 1.0629 1.0477 0.3796  -0.1409 -0.0258 642 GLN A OE1 
2718 N NE2 . GLN A 346 ? 2.4214 1.1345 1.0537 0.4927  -0.1268 -0.0310 642 GLN A NE2 
2719 N N   . SER A 347 ? 2.5516 0.8236 0.8303 0.3046  -0.1651 -0.0156 643 SER A N   
2720 C CA  . SER A 347 ? 2.6619 0.8044 0.7960 0.3177  -0.1720 -0.0196 643 SER A CA  
2721 C C   . SER A 347 ? 2.7260 0.8760 0.8841 0.2889  -0.1735 -0.0131 643 SER A C   
2722 O O   . SER A 347 ? 2.8125 0.8731 0.8675 0.3138  -0.1777 -0.0169 643 SER A O   
2723 C CB  . SER A 347 ? 2.7587 0.7594 0.7506 0.2680  -0.1821 -0.0212 643 SER A CB  
2724 O OG  . SER A 347 ? 2.7957 0.7610 0.7303 0.3099  -0.1818 -0.0272 643 SER A OG  
2725 N N   . ASP A 348 ? 2.6148 0.8664 0.9009 0.2402  -0.1701 -0.0029 644 ASP A N   
2726 C CA  . ASP A 348 ? 2.4468 0.7253 0.7719 0.2169  -0.1701 0.0055  644 ASP A CA  
2727 C C   . ASP A 348 ? 2.3576 0.7695 0.8094 0.2705  -0.1629 0.0089  644 ASP A C   
2728 O O   . ASP A 348 ? 2.1632 0.6176 0.6663 0.2523  -0.1626 0.0181  644 ASP A O   
2729 C CB  . ASP A 348 ? 2.3308 0.6284 0.6979 0.1201  -0.1720 0.0164  644 ASP A CB  
2730 C CG  . ASP A 348 ? 2.4668 0.6483 0.7124 0.0573  -0.1804 0.0144  644 ASP A CG  
2731 O OD1 . ASP A 348 ? 2.6148 0.6804 0.7285 0.0884  -0.1860 0.0051  644 ASP A OD1 
2732 O OD2 . ASP A 348 ? 2.4036 0.6131 0.6813 -0.0232 -0.1818 0.0224  644 ASP A OD2 
2733 N N   . LYS A 349 ? 2.4292 0.9114 0.9291 0.3339  -0.1574 0.0022  645 LYS A N   
2734 C CA  . LYS A 349 ? 2.4408 1.0620 1.0603 0.3830  -0.1514 0.0046  645 LYS A CA  
2735 C C   . LYS A 349 ? 2.1536 0.8747 0.9011 0.3325  -0.1497 0.0162  645 LYS A C   
2736 O O   . LYS A 349 ? 1.9486 0.7542 0.7716 0.3469  -0.1488 0.0226  645 LYS A O   
2737 C CB  . LYS A 349 ? 2.6575 1.2705 1.2405 0.4332  -0.1528 0.0036  645 LYS A CB  
2738 C CG  . LYS A 349 ? 2.7190 1.4502 1.3683 0.5116  -0.1471 -0.0013 645 LYS A CG  
2739 C CD  . LYS A 349 ? 2.8565 1.5767 1.4600 0.5604  -0.1428 -0.0126 645 LYS A CD  
2740 C CE  . LYS A 349 ? 2.8225 1.6689 1.4857 0.6349  -0.1362 -0.0171 645 LYS A CE  
2741 N NZ  . LYS A 349 ? 2.6294 1.6375 1.4505 0.6209  -0.1313 -0.0114 645 LYS A NZ  
2742 N N   . VAL A 350 ? 2.1360 0.8478 0.9031 0.2730  -0.1500 0.0191  646 VAL A N   
2743 C CA  . VAL A 350 ? 1.8855 0.6920 0.7692 0.2294  -0.1480 0.0290  646 VAL A CA  
2744 C C   . VAL A 350 ? 1.8179 0.7139 0.7861 0.2584  -0.1429 0.0236  646 VAL A C   
2745 O O   . VAL A 350 ? 1.8170 0.6748 0.7469 0.2620  -0.1418 0.0158  646 VAL A O   
2746 C CB  . VAL A 350 ? 1.7821 0.5368 0.6398 0.1411  -0.1510 0.0359  646 VAL A CB  
2747 C CG1 . VAL A 350 ? 1.5786 0.4360 0.5549 0.1010  -0.1482 0.0458  646 VAL A CG1 
2748 C CG2 . VAL A 350 ? 1.9375 0.6060 0.7060 0.1097  -0.1553 0.0404  646 VAL A CG2 
2749 N N   . THR A 351 ? 1.5388 0.5536 0.6181 0.2768  -0.1405 0.0279  647 THR A N   
2750 C CA  . THR A 351 ? 1.5447 0.6582 0.7078 0.3103  -0.1352 0.0219  647 THR A CA  
2751 C C   . THR A 351 ? 1.5480 0.6478 0.7297 0.2656  -0.1345 0.0211  647 THR A C   
2752 O O   . THR A 351 ? 1.5754 0.6682 0.7811 0.2058  -0.1375 0.0291  647 THR A O   
2753 C CB  . THR A 351 ? 1.4659 0.7083 0.7407 0.3248  -0.1352 0.0269  647 THR A CB  
2754 O OG1 . THR A 351 ? 1.5394 0.7986 0.7969 0.3615  -0.1369 0.0278  647 THR A OG1 
2755 C CG2 . THR A 351 ? 1.3216 0.6752 0.6825 0.3556  -0.1291 0.0194  647 THR A CG2 
2756 N N   . ILE A 352 ? 1.5851 0.6874 0.7561 0.2945  -0.1300 0.0115  648 ILE A N   
2757 C CA  . ILE A 352 ? 1.4091 0.5060 0.6004 0.2588  -0.1291 0.0091  648 ILE A CA  
2758 C C   . ILE A 352 ? 1.4988 0.6526 0.7169 0.3111  -0.1217 -0.0003 648 ILE A C   
2759 O O   . ILE A 352 ? 1.5029 0.6621 0.6843 0.3666  -0.1180 -0.0055 648 ILE A O   
2760 C CB  . ILE A 352 ? 1.5064 0.4807 0.5945 0.2076  -0.1346 0.0090  648 ILE A CB  
2761 C CG1 . ILE A 352 ? 1.5508 0.5355 0.6745 0.1553  -0.1354 0.0085  648 ILE A CG1 
2762 C CG2 . ILE A 352 ? 1.6683 0.5619 0.6490 0.2488  -0.1346 0.0003  648 ILE A CG2 
2763 C CD1 . ILE A 352 ? 1.6229 0.5157 0.6623 0.0891  -0.1422 0.0108  648 ILE A CD1 
2764 N N   . VAL A 353 ? 1.4163 0.6172 0.6976 0.2932  -0.1190 -0.0024 649 VAL A N   
2765 C CA  . VAL A 353 ? 1.3495 0.6070 0.6569 0.3351  -0.1107 -0.0105 649 VAL A CA  
2766 C C   . VAL A 353 ? 1.4567 0.6499 0.7248 0.3040  -0.1119 -0.0147 649 VAL A C   
2767 O O   . VAL A 353 ? 1.4071 0.5679 0.6828 0.2447  -0.1179 -0.0114 649 VAL A O   
2768 C CB  . VAL A 353 ? 1.2560 0.6549 0.6871 0.3494  -0.1054 -0.0100 649 VAL A CB  
2769 C CG1 . VAL A 353 ? 1.1248 0.5746 0.6349 0.2830  -0.1039 -0.0103 649 VAL A CG1 
2770 C CG2 . VAL A 353 ? 1.2621 0.7373 0.7155 0.3984  -0.0947 -0.0170 649 VAL A CG2 
2771 N N   . ASP A 354 ? 1.4463 0.6238 0.6683 0.3423  -0.1066 -0.0218 650 ASP A N   
2772 C CA  . ASP A 354 ? 1.5035 0.6202 0.6799 0.3193  -0.1082 -0.0261 650 ASP A CA  
2773 C C   . ASP A 354 ? 1.5191 0.7282 0.7849 0.3267  -0.1004 -0.0300 650 ASP A C   
2774 O O   . ASP A 354 ? 1.5208 0.8356 0.8584 0.3656  -0.0918 -0.0307 650 ASP A O   
2775 C CB  . ASP A 354 ? 1.5107 0.5437 0.5706 0.3571  -0.1083 -0.0305 650 ASP A CB  
2776 C CG  . ASP A 354 ? 1.6668 0.7734 0.7449 0.4260  -0.0973 -0.0354 650 ASP A CG  
2777 O OD1 . ASP A 354 ? 1.6247 0.7352 0.6627 0.4758  -0.0951 -0.0360 650 ASP A OD1 
2778 O OD2 . ASP A 354 ? 1.5690 0.7295 0.6954 0.4298  -0.0907 -0.0387 650 ASP A OD2 
2779 N N   . HIS A 355 ? 1.5486 0.7220 0.8080 0.2854  -0.1039 -0.0325 651 HIS A N   
2780 C CA  . HIS A 355 ? 1.3867 0.6439 0.7345 0.2804  -0.0982 -0.0358 651 HIS A CA  
2781 C C   . HIS A 355 ? 1.3131 0.6353 0.6781 0.3398  -0.0856 -0.0409 651 HIS A C   
2782 O O   . HIS A 355 ? 1.2833 0.7141 0.7394 0.3367  -0.0773 -0.0414 651 HIS A O   
2783 C CB  . HIS A 355 ? 1.4709 0.6855 0.8035 0.2219  -0.1046 -0.0379 651 HIS A CB  
2784 C CG  . HIS A 355 ? 1.5516 0.6506 0.7673 0.2205  -0.1101 -0.0409 651 HIS A CG  
2785 N ND1 . HIS A 355 ? 1.6781 0.6873 0.8140 0.1809  -0.1206 -0.0359 651 HIS A ND1 
2786 C CD2 . HIS A 355 ? 1.6101 0.6835 0.7788 0.2471  -0.1062 -0.0462 651 HIS A CD2 
2787 C CE1 . HIS A 355 ? 1.7777 0.7068 0.8196 0.1842  -0.1240 -0.0377 651 HIS A CE1 
2788 N NE2 . HIS A 355 ? 1.7102 0.6744 0.7696 0.2255  -0.1155 -0.0440 651 HIS A NE2 
2789 N N   . HIS A 356 ? 1.3726 0.6531 0.6581 0.3812  -0.0827 -0.0429 652 HIS A N   
2790 C CA  . HIS A 356 ? 1.3209 0.6813 0.6253 0.4375  -0.0699 -0.0459 652 HIS A CA  
2791 C C   . HIS A 356 ? 1.3201 0.7951 0.6957 0.4676  -0.0637 -0.0424 652 HIS A C   
2792 O O   . HIS A 356 ? 1.1876 0.7823 0.6483 0.4787  -0.0539 -0.0424 652 HIS A O   
2793 C CB  . HIS A 356 ? 1.4885 0.7653 0.6776 0.4742  -0.0707 -0.0482 652 HIS A CB  
2794 C CG  . HIS A 356 ? 1.6844 0.8448 0.7947 0.4391  -0.0791 -0.0503 652 HIS A CG  
2795 N ND1 . HIS A 356 ? 1.6428 0.8123 0.7654 0.4312  -0.0751 -0.0545 652 HIS A ND1 
2796 C CD2 . HIS A 356 ? 1.7958 0.8334 0.8140 0.4047  -0.0919 -0.0482 652 HIS A CD2 
2797 C CE1 . HIS A 356 ? 1.7590 0.8176 0.8018 0.3939  -0.0859 -0.0548 652 HIS A CE1 
2798 N NE2 . HIS A 356 ? 1.8119 0.7916 0.7905 0.3755  -0.0961 -0.0504 652 HIS A NE2 
2799 N N   . SER A 357 ? 1.2910 0.7331 0.6315 0.4759  -0.0698 -0.0390 653 SER A N   
2800 C CA  . SER A 357 ? 1.3540 0.9029 0.7513 0.5055  -0.0651 -0.0360 653 SER A CA  
2801 C C   . SER A 357 ? 1.0988 0.7499 0.6136 0.4735  -0.0644 -0.0324 653 SER A C   
2802 O O   . SER A 357 ? 1.1015 0.8756 0.6854 0.4902  -0.0575 -0.0309 653 SER A O   
2803 C CB  . SER A 357 ? 1.4672 0.9492 0.7958 0.5193  -0.0727 -0.0337 653 SER A CB  
2804 O OG  . SER A 357 ? 1.5012 1.0900 0.8781 0.5519  -0.0683 -0.0318 653 SER A OG  
2805 N N   . ALA A 358 ? 1.0597 0.6647 0.5943 0.4251  -0.0720 -0.0306 654 ALA A N   
2806 C CA  . ALA A 358 ? 0.9919 0.6915 0.6312 0.3837  -0.0721 -0.0268 654 ALA A CA  
2807 C C   . ALA A 358 ? 0.9726 0.7620 0.6848 0.3632  -0.0625 -0.0291 654 ALA A C   
2808 O O   . ALA A 358 ? 0.8091 0.7076 0.6055 0.3463  -0.0580 -0.0269 654 ALA A O   
2809 C CB  . ALA A 358 ? 0.9639 0.5975 0.5964 0.3225  -0.0815 -0.0236 654 ALA A CB  
2810 N N   . THR A 359 ? 0.8670 0.6049 0.5416 0.3603  -0.0601 -0.0334 655 THR A N   
2811 C CA  . THR A 359 ? 0.8535 0.6705 0.5882 0.3436  -0.0508 -0.0347 655 THR A CA  
2812 C C   . THR A 359 ? 0.8449 0.7594 0.6020 0.3934  -0.0386 -0.0355 655 THR A C   
2813 O O   . THR A 359 ? 0.7794 0.7963 0.6082 0.3735  -0.0305 -0.0335 655 THR A O   
2814 C CB  . THR A 359 ? 0.9677 0.7045 0.6536 0.3267  -0.0524 -0.0388 655 THR A CB  
2815 O OG1 . THR A 359 ? 1.0596 0.7014 0.6439 0.3742  -0.0535 -0.0437 655 THR A OG1 
2816 C CG2 . THR A 359 ? 0.9009 0.5811 0.5879 0.2673  -0.0641 -0.0367 655 THR A CG2 
2817 N N   . GLU A 360 ? 0.8953 0.7820 0.5881 0.4581  -0.0372 -0.0380 656 GLU A N   
2818 C CA  . GLU A 360 ? 0.9678 0.9684 0.6860 0.4908  -0.0254 -0.0369 656 GLU A CA  
2819 C C   . GLU A 360 ? 1.0004 1.1165 0.7991 0.4754  -0.0256 -0.0316 656 GLU A C   
2820 O O   . GLU A 360 ? 0.9993 1.2372 0.8584 0.4692  -0.0163 -0.0295 656 GLU A O   
2821 C CB  . GLU A 360 ? 1.1017 1.0481 0.7276 0.5398  -0.0256 -0.0384 656 GLU A CB  
2822 C CG  . GLU A 360 ? 1.3040 1.3558 0.9385 0.5781  -0.0138 -0.0375 656 GLU A CG  
2823 C CD  . GLU A 360 ? 1.5541 1.6141 1.1367 0.6249  -0.0163 -0.0359 656 GLU A CD  
2824 O OE1 . GLU A 360 ? 1.5872 1.7718 1.2096 0.6428  -0.0098 -0.0328 656 GLU A OE1 
2825 O OE2 . GLU A 360 ? 1.6799 1.6219 1.1776 0.6418  -0.0253 -0.0376 656 GLU A OE2 
2826 N N   . SER A 361 ? 1.0256 1.1035 0.8217 0.4641  -0.0366 -0.0292 657 SER A N   
2827 C CA  A SER A 361 ? 0.8710 1.0499 0.7381 0.4453  -0.0383 -0.0248 657 SER A CA  
2828 C CA  B SER A 361 ? 0.8706 1.0492 0.7378 0.4452  -0.0384 -0.0248 657 SER A CA  
2829 C C   . SER A 361 ? 0.8583 1.1080 0.8094 0.3947  -0.0367 -0.0232 657 SER A C   
2830 O O   . SER A 361 ? 0.7982 1.1615 0.8103 0.3788  -0.0329 -0.0205 657 SER A O   
2831 C CB  A SER A 361 ? 0.8378 0.9509 0.6785 0.4428  -0.0505 -0.0226 657 SER A CB  
2832 C CB  B SER A 361 ? 0.8362 0.9492 0.6784 0.4415  -0.0507 -0.0225 657 SER A CB  
2833 O OG  A SER A 361 ? 0.9035 0.9691 0.6680 0.4861  -0.0511 -0.0235 657 SER A OG  
2834 O OG  B SER A 361 ? 0.7160 0.7799 0.5810 0.3933  -0.0584 -0.0212 657 SER A OG  
2835 N N   . PHE A 362 ? 0.8827 1.0570 0.8272 0.3519  -0.0387 -0.0243 658 PHE A N   
2836 C CA  . PHE A 362 ? 0.8150 1.0337 0.8224 0.2938  -0.0366 -0.0225 658 PHE A CA  
2837 C C   . PHE A 362 ? 0.6919 1.0002 0.7308 0.2934  -0.0243 -0.0218 658 PHE A C   
2838 O O   . PHE A 362 ? 0.5406 0.9236 0.6341 0.2555  -0.0218 -0.0187 658 PHE A O   
2839 C CB  . PHE A 362 ? 0.8033 0.9299 0.7928 0.2566  -0.0419 -0.0237 658 PHE A CB  
2840 C CG  . PHE A 362 ? 0.7184 0.8802 0.7624 0.2057  -0.0414 -0.0217 658 PHE A CG  
2841 C CD1 . PHE A 362 ? 0.6434 0.8325 0.7267 0.1775  -0.0467 -0.0198 658 PHE A CD1 
2842 C CD2 . PHE A 362 ? 0.7535 0.9195 0.8034 0.1890  -0.0355 -0.0218 658 PHE A CD2 
2843 C CE1 . PHE A 362 ? 0.5029 0.7124 0.6236 0.1360  -0.0467 -0.0185 658 PHE A CE1 
2844 C CE2 . PHE A 362 ? 0.7258 0.9138 0.8149 0.1461  -0.0359 -0.0195 658 PHE A CE2 
2845 C CZ  . PHE A 362 ? 0.6247 0.8307 0.7463 0.1208  -0.0416 -0.0180 658 PHE A CZ  
2846 N N   . ILE A 363 ? 0.7420 1.0390 0.7405 0.3326  -0.0162 -0.0246 659 ILE A N   
2847 C CA  . ILE A 363 ? 0.7490 1.1428 0.7745 0.3361  -0.0024 -0.0233 659 ILE A CA  
2848 C C   . ILE A 363 ? 0.6684 1.1940 0.7370 0.3509  0.0016  -0.0200 659 ILE A C   
2849 O O   . ILE A 363 ? 0.5928 1.2158 0.7123 0.3145  0.0082  -0.0158 659 ILE A O   
2850 C CB  . ILE A 363 ? 0.7934 1.1499 0.7595 0.3847  0.0061  -0.0279 659 ILE A CB  
2851 C CG1 . ILE A 363 ? 0.7619 0.9967 0.6866 0.3611  0.0010  -0.0311 659 ILE A CG1 
2852 C CG2 . ILE A 363 ? 0.7135 1.1886 0.7094 0.3919  0.0225  -0.0258 659 ILE A CG2 
2853 C CD1 . ILE A 363 ? 0.6900 0.9492 0.6336 0.3300  0.0097  -0.0297 659 ILE A CD1 
2854 N N   . LYS A 364 ? 0.8078 1.3197 0.8425 0.3894  -0.0034 -0.0206 660 LYS A N   
2855 C CA  . LYS A 364 ? 0.7621 1.3713 0.8225 0.3851  -0.0030 -0.0167 660 LYS A CA  
2856 C C   . LYS A 364 ? 0.6941 1.3476 0.8165 0.3283  -0.0094 -0.0136 660 LYS A C   
2857 O O   . LYS A 364 ? 0.6343 1.3842 0.7950 0.2954  -0.0051 -0.0098 660 LYS A O   
2858 C CB  . LYS A 364 ? 0.7904 1.3556 0.7957 0.4324  -0.0094 -0.0181 660 LYS A CB  
2859 C CG  . LYS A 364 ? 0.9855 1.6145 0.9587 0.4763  -0.0021 -0.0174 660 LYS A CG  
2860 C CD  . LYS A 364 ? 1.0710 1.7838 1.0619 0.4786  -0.0058 -0.0143 660 LYS A CD  
2861 C CE  . LYS A 364 ? 1.2011 2.0063 1.1714 0.5166  0.0015  -0.0125 660 LYS A CE  
2862 N NZ  . LYS A 364 ? 1.2400 2.1248 1.2212 0.5228  -0.0030 -0.0101 660 LYS A NZ  
2863 N N   . HIS A 365 ? 0.7375 1.3163 0.8626 0.3146  -0.0207 -0.0149 661 HIS A N   
2864 C CA  . HIS A 365 ? 0.5895 1.1970 0.7652 0.2612  -0.0280 -0.0129 661 HIS A CA  
2865 C C   . HIS A 365 ? 0.6144 1.2594 0.8238 0.2090  -0.0212 -0.0108 661 HIS A C   
2866 O O   . HIS A 365 ? 0.5892 1.3033 0.8361 0.1666  -0.0225 -0.0080 661 HIS A O   
2867 C CB  . HIS A 365 ? 0.5527 1.0473 0.7088 0.2465  -0.0387 -0.0147 661 HIS A CB  
2868 C CG  . HIS A 365 ? 0.6238 1.1209 0.8165 0.1892  -0.0445 -0.0138 661 HIS A CG  
2869 N ND1 . HIS A 365 ? 0.5075 1.0762 0.7315 0.1736  -0.0496 -0.0125 661 HIS A ND1 
2870 C CD2 . HIS A 365 ? 0.6007 1.0360 0.7977 0.1474  -0.0466 -0.0146 661 HIS A CD2 
2871 C CE1 . HIS A 365 ? 0.5473 1.0877 0.7878 0.1247  -0.0542 -0.0131 661 HIS A CE1 
2872 N NE2 . HIS A 365 ? 0.5348 0.9966 0.7599 0.1111  -0.0521 -0.0142 661 HIS A NE2 
2873 N N   . MET A 366 ? 0.5326 1.1202 0.7193 0.2073  -0.0149 -0.0119 662 MET A N   
2874 C CA  . MET A 366 ? 0.5011 1.1088 0.7073 0.1590  -0.0084 -0.0089 662 MET A CA  
2875 C C   . MET A 366 ? 0.4277 1.1682 0.6619 0.1533  0.0022  -0.0047 662 MET A C   
2876 O O   . MET A 366 ? 0.3321 1.1176 0.5913 0.0989  0.0035  -0.0005 662 MET A O   
2877 C CB  . MET A 366 ? 0.5735 1.1000 0.7454 0.1662  -0.0040 -0.0108 662 MET A CB  
2878 C CG  . MET A 366 ? 0.5776 1.0589 0.7559 0.1138  -0.0055 -0.0085 662 MET A CG  
2879 S SD  . MET A 366 ? 0.7322 1.1106 0.8675 0.1263  -0.0055 -0.0115 662 MET A SD  
2880 C CE  . MET A 366 ? 0.8132 1.1736 0.9599 0.0691  -0.0056 -0.0066 662 MET A CE  
2881 N N   . GLU A 367 ? 0.4738 1.2686 0.6937 0.2064  0.0095  -0.0056 663 GLU A N   
2882 C CA  . GLU A 367 ? 0.5823 1.4785 0.8087 0.1953  0.0187  -0.0010 663 GLU A CA  
2883 C C   . GLU A 367 ? 0.6780 1.6271 0.9277 0.1547  0.0112  0.0022  663 GLU A C   
2884 O O   . GLU A 367 ? 0.7283 1.7428 0.9939 0.1062  0.0152  0.0072  663 GLU A O   
2885 C CB  . GLU A 367 ? 0.7008 1.6148 0.8877 0.2611  0.0238  -0.0029 663 GLU A CB  
2886 C CG  . GLU A 367 ? 0.8044 1.6701 0.9567 0.2997  0.0330  -0.0062 663 GLU A CG  
2887 C CD  . GLU A 367 ? 0.9917 1.8624 1.0923 0.3661  0.0359  -0.0083 663 GLU A CD  
2888 O OE1 . GLU A 367 ? 1.0262 1.9640 1.1251 0.3803  0.0329  -0.0058 663 GLU A OE1 
2889 O OE2 . GLU A 367 ? 1.0670 1.8708 1.1228 0.4047  0.0404  -0.0125 663 GLU A OE2 
2890 N N   . ASN A 368 ? 0.6118 1.5269 0.8572 0.1719  0.0002  -0.0005 664 ASN A N   
2891 C CA  . ASN A 368 ? 0.5984 1.5563 0.8612 0.1368  -0.0072 0.0014  664 ASN A CA  
2892 C C   . ASN A 368 ? 0.5950 1.5291 0.8800 0.0682  -0.0120 0.0028  664 ASN A C   
2893 O O   . ASN A 368 ? 0.6087 1.5934 0.9012 0.0215  -0.0127 0.0062  664 ASN A O   
2894 C CB  . ASN A 368 ? 0.5593 1.4770 0.8086 0.1729  -0.0173 -0.0018 664 ASN A CB  
2895 C CG  . ASN A 368 ? 0.6201 1.5534 0.8339 0.2396  -0.0137 -0.0029 664 ASN A CG  
2896 O OD1 . ASN A 368 ? 0.7972 1.8091 1.0041 0.2539  -0.0055 -0.0005 664 ASN A OD1 
2897 N ND2 . ASN A 368 ? 0.5283 1.3833 0.7123 0.2806  -0.0203 -0.0061 664 ASN A ND2 
2898 N N   . GLU A 369 ? 0.5109 1.3645 0.7991 0.0611  -0.0163 0.0002  665 GLU A N   
2899 C CA  . GLU A 369 ? 0.4617 1.2801 0.7602 0.0003  -0.0225 0.0008  665 GLU A CA  
2900 C C   . GLU A 369 ? 0.5994 1.4541 0.8959 -0.0491 -0.0137 0.0063  665 GLU A C   
2901 O O   . GLU A 369 ? 0.6783 1.5380 0.9688 -0.1025 -0.0173 0.0087  665 GLU A O   
2902 C CB  . GLU A 369 ? 0.4846 1.1918 0.7707 0.0072  -0.0283 -0.0030 665 GLU A CB  
2903 C CG  . GLU A 369 ? 0.5696 1.2240 0.8499 0.0361  -0.0388 -0.0073 665 GLU A CG  
2904 C CD  . GLU A 369 ? 0.6797 1.3317 0.9701 -0.0004 -0.0493 -0.0087 665 GLU A CD  
2905 O OE1 . GLU A 369 ? 0.8274 1.3971 1.1046 -0.0267 -0.0538 -0.0108 665 GLU A OE1 
2906 O OE2 . GLU A 369 ? 0.5406 1.2588 0.8411 -0.0005 -0.0518 -0.0077 665 GLU A OE2 
2907 N N   . TYR A 370 ? 0.5766 1.4509 0.8702 -0.0326 -0.0019 0.0084  666 TYR A N   
2908 C CA  . TYR A 370 ? 0.6212 1.5325 0.9073 -0.0797 0.0077  0.0149  666 TYR A CA  
2909 C C   . TYR A 370 ? 0.6562 1.6545 0.9383 -0.0989 0.0099  0.0189  666 TYR A C   
2910 O O   . TYR A 370 ? 0.6199 1.6331 0.8884 -0.1574 0.0115  0.0243  666 TYR A O   
2911 C CB  . TYR A 370 ? 0.5414 1.4652 0.8237 -0.0516 0.0215  0.0163  666 TYR A CB  
2912 C CG  . TYR A 370 ? 0.5689 1.3580 0.8226 -0.0537 0.0180  0.0141  666 TYR A CG  
2913 C CD1 . TYR A 370 ? 0.5610 1.2626 0.8025 -0.0096 0.0103  0.0074  666 TYR A CD1 
2914 C CD2 . TYR A 370 ? 0.6301 1.3743 0.8614 -0.1008 0.0215  0.0193  666 TYR A CD2 
2915 C CE1 . TYR A 370 ? 0.5612 1.1491 0.7764 -0.0127 0.0059  0.0056  666 TYR A CE1 
2916 C CE2 . TYR A 370 ? 0.6688 1.2915 0.8707 -0.0975 0.0167  0.0174  666 TYR A CE2 
2917 C CZ  . TYR A 370 ? 0.6737 1.2262 0.8715 -0.0537 0.0087  0.0104  666 TYR A CZ  
2918 O OH  . TYR A 370 ? 0.7370 1.1860 0.9094 -0.0518 0.0030  0.0088  666 TYR A OH  
2919 N N   . ARG A 371 ? 0.7103 1.7622 0.9971 -0.0522 0.0088  0.0166  667 ARG A N   
2920 C CA  . ARG A 371 ? 0.8236 1.9702 1.1077 -0.0678 0.0092  0.0204  667 ARG A CA  
2921 C C   . ARG A 371 ? 0.8299 1.9627 1.1114 -0.1213 -0.0016 0.0208  667 ARG A C   
2922 O O   . ARG A 371 ? 0.8695 2.0296 1.1373 -0.1796 -0.0011 0.0258  667 ARG A O   
2923 C CB  . ARG A 371 ? 0.9204 2.1199 1.2035 0.0007  0.0097  0.0178  667 ARG A CB  
2924 C CG  . ARG A 371 ? 1.0187 2.3267 1.3001 -0.0080 0.0087  0.0213  667 ARG A CG  
2925 C CD  . ARG A 371 ? 1.0961 2.4374 1.3699 0.0622  0.0065  0.0183  667 ARG A CD  
2926 N NE  . ARG A 371 ? 1.1256 2.3860 1.3999 0.0843  -0.0033 0.0131  667 ARG A NE  
2927 C CZ  . ARG A 371 ? 1.1213 2.3884 1.4018 0.0649  -0.0128 0.0124  667 ARG A CZ  
2928 N NH1 . ARG A 371 ? 1.1261 2.4752 1.4111 0.0215  -0.0142 0.0164  667 ARG A NH1 
2929 N NH2 . ARG A 371 ? 1.0696 2.2612 1.3484 0.0876  -0.0215 0.0080  667 ARG A NH2 
2930 N N   . CYS A 372 ? 0.7538 1.8382 1.0417 -0.1033 -0.0120 0.0157  668 CYS A N   
2931 C CA  . CYS A 372 ? 0.7815 1.8619 1.0647 -0.1412 -0.0224 0.0151  668 CYS A CA  
2932 C C   . CYS A 372 ? 0.6859 1.6620 0.9587 -0.1822 -0.0308 0.0124  668 CYS A C   
2933 O O   . CYS A 372 ? 0.7201 1.6710 0.9869 -0.2010 -0.0409 0.0096  668 CYS A O   
2934 C CB  . CYS A 372 ? 0.8658 1.9691 1.1581 -0.0934 -0.0287 0.0114  668 CYS A CB  
2935 S SG  . CYS A 372 ? 0.9666 1.9699 1.2648 -0.0412 -0.0354 0.0048  668 CYS A SG  
2936 N N   . ARG A 373 ? 0.5180 1.4330 0.7847 -0.1946 -0.0272 0.0129  669 ARG A N   
2937 C CA  . ARG A 373 ? 0.5441 1.3551 0.7943 -0.2265 -0.0356 0.0099  669 ARG A CA  
2938 C C   . ARG A 373 ? 0.6548 1.4220 0.8848 -0.2585 -0.0294 0.0140  669 ARG A C   
2939 O O   . ARG A 373 ? 0.6399 1.3184 0.8394 -0.2956 -0.0358 0.0133  669 ARG A O   
2940 C CB  . ARG A 373 ? 0.5235 1.2808 0.7913 -0.1821 -0.0429 0.0033  669 ARG A CB  
2941 C CG  . ARG A 373 ? 0.6059 1.2686 0.8554 -0.2096 -0.0545 -0.0015 669 ARG A CG  
2942 C CD  . ARG A 373 ? 0.6045 1.2137 0.8671 -0.1673 -0.0601 -0.0071 669 ARG A CD  
2943 N NE  . ARG A 373 ? 0.6469 1.1733 0.8870 -0.1828 -0.0705 -0.0125 669 ARG A NE  
2944 C CZ  . ARG A 373 ? 0.5891 1.0324 0.8194 -0.1536 -0.0730 -0.0167 669 ARG A CZ  
2945 N NH1 . ARG A 373 ? 0.4027 0.8267 0.6409 -0.1131 -0.0675 -0.0159 669 ARG A NH1 
2946 N NH2 . ARG A 373 ? 0.5305 0.9116 0.7391 -0.1667 -0.0812 -0.0217 669 ARG A NH2 
2947 N N   . GLY A 374 ? 0.6964 1.5190 0.9364 -0.2416 -0.0171 0.0183  670 GLY A N   
2948 C CA  . GLY A 374 ? 0.6958 1.4853 0.9138 -0.2737 -0.0098 0.0237  670 GLY A CA  
2949 C C   . GLY A 374 ? 0.7341 1.4549 0.9577 -0.2525 -0.0098 0.0214  670 GLY A C   
2950 O O   . GLY A 374 ? 0.8144 1.4688 1.0031 -0.2773 -0.0060 0.0256  670 GLY A O   
2951 N N   . GLY A 375 ? 0.5791 1.2694 0.8186 -0.1944 -0.0141 0.0146  671 GLY A N   
2952 C CA  . GLY A 375 ? 0.5569 1.1419 0.7773 -0.1620 -0.0151 0.0115  671 GLY A CA  
2953 C C   . GLY A 375 ? 0.5386 1.0882 0.7714 -0.1158 -0.0233 0.0043  671 GLY A C   
2954 O O   . GLY A 375 ? 0.4729 1.0714 0.7262 -0.1061 -0.0284 0.0019  671 GLY A O   
2955 N N   . CYS A 376 ? 0.4539 0.9181 0.6706 -0.0908 -0.0253 0.0016  672 CYS A N   
2956 C CA  . CYS A 376 ? 0.4361 0.8571 0.6565 -0.0528 -0.0323 -0.0040 672 CYS A CA  
2957 C C   . CYS A 376 ? 0.5192 0.8472 0.7177 -0.0479 -0.0360 -0.0054 672 CYS A C   
2958 O O   . CYS A 376 ? 0.4072 0.7185 0.5940 -0.0303 -0.0311 -0.0046 672 CYS A O   
2959 C CB  . CYS A 376 ? 0.3633 0.8308 0.5921 -0.0052 -0.0273 -0.0053 672 CYS A CB  
2960 S SG  . CYS A 376 ? 0.5178 0.9244 0.7363 0.0378  -0.0357 -0.0105 672 CYS A SG  
2961 N N   . PRO A 377 ? 0.5589 0.8296 0.7489 -0.0619 -0.0447 -0.0076 673 PRO A N   
2962 C CA  . PRO A 377 ? 0.5220 0.7212 0.6951 -0.0514 -0.0490 -0.0089 673 PRO A CA  
2963 C C   . PRO A 377 ? 0.5525 0.7437 0.7284 -0.0174 -0.0492 -0.0113 673 PRO A C   
2964 O O   . PRO A 377 ? 0.4580 0.6714 0.6440 0.0009  -0.0501 -0.0134 673 PRO A O   
2965 C CB  . PRO A 377 ? 0.5747 0.7346 0.7430 -0.0609 -0.0578 -0.0121 673 PRO A CB  
2966 C CG  . PRO A 377 ? 0.4817 0.6860 0.6643 -0.0735 -0.0589 -0.0135 673 PRO A CG  
2967 C CD  . PRO A 377 ? 0.4948 0.7659 0.6863 -0.0862 -0.0512 -0.0094 673 PRO A CD  
2968 N N   . ALA A 378 ? 0.5324 0.6865 0.6917 -0.0101 -0.0492 -0.0106 674 ALA A N   
2969 C CA  . ALA A 378 ? 0.5163 0.6524 0.6655 0.0158  -0.0501 -0.0130 674 ALA A CA  
2970 C C   . ALA A 378 ? 0.5650 0.6531 0.6961 0.0138  -0.0551 -0.0129 674 ALA A C   
2971 O O   . ALA A 378 ? 0.5262 0.6048 0.6482 0.0023  -0.0535 -0.0100 674 ALA A O   
2972 C CB  . ALA A 378 ? 0.4129 0.5847 0.5554 0.0360  -0.0408 -0.0126 674 ALA A CB  
2973 N N   . ASP A 379 ? 0.4973 0.5569 0.6206 0.0222  -0.0620 -0.0154 675 ASP A N   
2974 C CA  . ASP A 379 ? 0.5321 0.5587 0.6413 0.0177  -0.0692 -0.0154 675 ASP A CA  
2975 C C   . ASP A 379 ? 0.6876 0.6888 0.7675 0.0295  -0.0693 -0.0174 675 ASP A C   
2976 O O   . ASP A 379 ? 0.7021 0.6843 0.7688 0.0338  -0.0733 -0.0194 675 ASP A O   
2977 C CB  . ASP A 379 ? 0.4880 0.5103 0.6091 0.0108  -0.0777 -0.0163 675 ASP A CB  
2978 C CG  . ASP A 379 ? 0.6597 0.6673 0.7711 0.0060  -0.0861 -0.0158 675 ASP A CG  
2979 O OD1 . ASP A 379 ? 0.5830 0.6017 0.7074 0.0031  -0.0918 -0.0159 675 ASP A OD1 
2980 O OD2 . ASP A 379 ? 0.6667 0.6566 0.7567 0.0067  -0.0873 -0.0156 675 ASP A OD2 
2981 N N   . TRP A 380 ? 0.5706 0.5650 0.6326 0.0337  -0.0649 -0.0167 676 TRP A N   
2982 C CA  . TRP A 380 ? 0.5082 0.4697 0.5313 0.0472  -0.0645 -0.0196 676 TRP A CA  
2983 C C   . TRP A 380 ? 0.5353 0.4555 0.5358 0.0359  -0.0768 -0.0216 676 TRP A C   
2984 O O   . TRP A 380 ? 0.5922 0.4735 0.5554 0.0436  -0.0790 -0.0247 676 TRP A O   
2985 C CB  . TRP A 380 ? 0.5637 0.5259 0.5725 0.0488  -0.0588 -0.0182 676 TRP A CB  
2986 C CG  . TRP A 380 ? 0.5157 0.4495 0.4801 0.0692  -0.0542 -0.0219 676 TRP A CG  
2987 C CD1 . TRP A 380 ? 0.6189 0.5787 0.5743 0.0922  -0.0411 -0.0226 676 TRP A CD1 
2988 C CD2 . TRP A 380 ? 0.5742 0.4501 0.4923 0.0688  -0.0629 -0.0259 676 TRP A CD2 
2989 N NE1 . TRP A 380 ? 0.7171 0.6337 0.6211 0.1121  -0.0400 -0.0273 676 TRP A NE1 
2990 C CE2 . TRP A 380 ? 0.6692 0.5274 0.5462 0.0955  -0.0539 -0.0296 676 TRP A CE2 
2991 C CE3 . TRP A 380 ? 0.6497 0.4924 0.5548 0.0470  -0.0775 -0.0267 676 TRP A CE3 
2992 C CZ2 . TRP A 380 ? 0.6888 0.4808 0.5041 0.1007  -0.0598 -0.0350 676 TRP A CZ2 
2993 C CZ3 . TRP A 380 ? 0.7024 0.4883 0.5510 0.0457  -0.0842 -0.0311 676 TRP A CZ3 
2994 C CH2 . TRP A 380 ? 0.7127 0.4661 0.5135 0.0722  -0.0757 -0.0356 676 TRP A CH2 
2995 N N   . VAL A 381 ? 0.5791 0.5070 0.5958 0.0177  -0.0854 -0.0196 677 VAL A N   
2996 C CA  . VAL A 381 ? 0.5478 0.4558 0.5479 0.0008  -0.0977 -0.0206 677 VAL A CA  
2997 C C   . VAL A 381 ? 0.7061 0.6011 0.6986 -0.0041 -0.0998 -0.0217 677 VAL A C   
2998 O O   . VAL A 381 ? 0.6395 0.4971 0.5942 -0.0183 -0.1073 -0.0230 677 VAL A O   
2999 C CB  . VAL A 381 ? 0.6167 0.5568 0.6441 -0.0109 -0.1058 -0.0178 677 VAL A CB  
3000 C CG1 . VAL A 381 ? 0.5982 0.5433 0.6195 -0.0314 -0.1175 -0.0180 677 VAL A CG1 
3001 C CG2 . VAL A 381 ? 0.5511 0.4867 0.5671 -0.0077 -0.1075 -0.0162 677 VAL A CG2 
3002 N N   . TRP A 382 ? 0.6978 0.6180 0.7190 0.0047  -0.0937 -0.0208 678 TRP A N   
3003 C CA  . TRP A 382 ? 0.6900 0.5987 0.7036 0.0020  -0.0951 -0.0208 678 TRP A CA  
3004 C C   . TRP A 382 ? 0.6719 0.5533 0.6568 0.0264  -0.0886 -0.0224 678 TRP A C   
3005 O O   . TRP A 382 ? 0.7183 0.5585 0.6666 0.0258  -0.0921 -0.0226 678 TRP A O   
3006 C CB  . TRP A 382 ? 0.6355 0.5888 0.6942 -0.0019 -0.0940 -0.0192 678 TRP A CB  
3007 C CG  . TRP A 382 ? 0.7520 0.7288 0.8269 -0.0216 -0.1017 -0.0178 678 TRP A CG  
3008 C CD1 . TRP A 382 ? 0.6809 0.6762 0.7656 -0.0261 -0.1066 -0.0172 678 TRP A CD1 
3009 C CD2 . TRP A 382 ? 0.7370 0.7297 0.8192 -0.0364 -0.1052 -0.0165 678 TRP A CD2 
3010 N NE1 . TRP A 382 ? 0.7798 0.8094 0.8800 -0.0394 -0.1131 -0.0159 678 TRP A NE1 
3011 C CE2 . TRP A 382 ? 0.7985 0.8294 0.8987 -0.0480 -0.1115 -0.0154 678 TRP A CE2 
3012 C CE3 . TRP A 382 ? 0.6569 0.6386 0.7302 -0.0396 -0.1035 -0.0156 678 TRP A CE3 
3013 C CZ2 . TRP A 382 ? 0.7730 0.8403 0.8857 -0.0637 -0.1148 -0.0136 678 TRP A CZ2 
3014 C CZ3 . TRP A 382 ? 0.7910 0.7992 0.8737 -0.0587 -0.1066 -0.0135 678 TRP A CZ3 
3015 C CH2 . TRP A 382 ? 0.8206 0.8759 0.9249 -0.0709 -0.1115 -0.0126 678 TRP A CH2 
3016 N N   . ILE A 383 ? 0.6432 0.5468 0.6378 0.0486  -0.0795 -0.0232 679 ILE A N   
3017 C CA  . ILE A 383 ? 0.6205 0.5131 0.5894 0.0794  -0.0733 -0.0247 679 ILE A CA  
3018 C C   . ILE A 383 ? 0.7814 0.6023 0.6804 0.0931  -0.0757 -0.0280 679 ILE A C   
3019 O O   . ILE A 383 ? 0.7452 0.5239 0.6000 0.1145  -0.0763 -0.0292 679 ILE A O   
3020 C CB  . ILE A 383 ? 0.6652 0.6192 0.6666 0.0961  -0.0623 -0.0240 679 ILE A CB  
3021 C CG1 . ILE A 383 ? 0.6184 0.6270 0.6733 0.0800  -0.0616 -0.0213 679 ILE A CG1 
3022 C CG2 . ILE A 383 ? 0.5438 0.5008 0.5165 0.1360  -0.0552 -0.0258 679 ILE A CG2 
3023 C CD1 . ILE A 383 ? 0.7343 0.7618 0.7973 0.0927  -0.0619 -0.0211 679 ILE A CD1 
3024 N N   . VAL A 384 ? 0.6492 0.4471 0.5286 0.0824  -0.0781 -0.0297 680 VAL A N   
3025 C CA  . VAL A 384 ? 0.7818 0.5018 0.5841 0.0955  -0.0808 -0.0341 680 VAL A CA  
3026 C C   . VAL A 384 ? 0.7898 0.4401 0.5425 0.0739  -0.0924 -0.0340 680 VAL A C   
3027 O O   . VAL A 384 ? 0.8059 0.4699 0.5818 0.0347  -0.1010 -0.0311 680 VAL A O   
3028 C CB  . VAL A 384 ? 0.7581 0.4685 0.5486 0.0834  -0.0826 -0.0359 680 VAL A CB  
3029 C CG1 . VAL A 384 ? 0.7482 0.3673 0.4485 0.0955  -0.0864 -0.0418 680 VAL A CG1 
3030 C CG2 . VAL A 384 ? 0.9381 0.7110 0.7686 0.1007  -0.0703 -0.0347 680 VAL A CG2 
3031 N N   . PRO A 385 ? 0.9409 0.5183 0.6224 0.0979  -0.0931 -0.0364 681 PRO A N   
3032 C CA  . PRO A 385 ? 1.0013 0.4985 0.6213 0.0698  -0.1048 -0.0352 681 PRO A CA  
3033 C C   . PRO A 385 ? 1.0400 0.5002 0.6292 0.0250  -0.1159 -0.0364 681 PRO A C   
3034 O O   . PRO A 385 ? 1.1627 0.6303 0.7522 0.0292  -0.1146 -0.0399 681 PRO A O   
3035 C CB  . PRO A 385 ? 1.1689 0.5759 0.6975 0.1138  -0.1031 -0.0386 681 PRO A CB  
3036 C CG  . PRO A 385 ? 1.1737 0.6515 0.7459 0.1668  -0.0896 -0.0397 681 PRO A CG  
3037 C CD  . PRO A 385 ? 0.9578 0.5253 0.6081 0.1537  -0.0832 -0.0396 681 PRO A CD  
3038 N N   . PRO A 386 ? 1.0266 0.4529 0.5884 -0.0214 -0.1272 -0.0331 682 PRO A N   
3039 C CA  . PRO A 386 ? 1.1397 0.5464 0.6754 -0.0711 -0.1396 -0.0336 682 PRO A CA  
3040 C C   . PRO A 386 ? 1.2834 0.5653 0.7016 -0.0772 -0.1478 -0.0390 682 PRO A C   
3041 O O   . PRO A 386 ? 1.2622 0.5109 0.6389 -0.1282 -0.1611 -0.0390 682 PRO A O   
3042 C CB  . PRO A 386 ? 1.1432 0.5805 0.7010 -0.1193 -0.1467 -0.0270 682 PRO A CB  
3043 C CG  . PRO A 386 ? 1.1324 0.5283 0.6631 -0.0978 -0.1417 -0.0244 682 PRO A CG  
3044 C CD  . PRO A 386 ? 1.1260 0.5438 0.6848 -0.0333 -0.1287 -0.0278 682 PRO A CD  
3045 N N   . MET A 387 ? 1.4042 0.6166 0.7629 -0.0249 -0.1406 -0.0438 683 MET A N   
3046 C CA  . MET A 387 ? 1.5187 0.6029 0.7562 -0.0182 -0.1469 -0.0507 683 MET A CA  
3047 C C   . MET A 387 ? 1.5100 0.5825 0.7301 0.0573  -0.1331 -0.0566 683 MET A C   
3048 O O   . MET A 387 ? 1.3907 0.5367 0.6751 0.0976  -0.1211 -0.0540 683 MET A O   
3049 C CB  . MET A 387 ? 1.6898 0.6965 0.8440 -0.0409 -0.1527 -0.0413 683 MET A CB  
3050 C CG  . MET A 387 ? 1.7910 0.7624 0.9123 0.0125  -0.1447 -0.0397 683 MET A CG  
3051 S SD  . MET A 387 ? 1.8005 0.6728 0.8126 -0.0119 -0.1524 -0.0291 683 MET A SD  
3052 C CE  . MET A 387 ? 1.7349 0.4966 0.6176 0.0099  -0.1556 -0.0299 683 MET A CE  
3053 N N   . SER A 388 ? 1.4824 0.4972 0.6309 0.0735  -0.1327 -0.0596 684 SER A N   
3054 C CA  . SER A 388 ? 1.4293 0.4411 0.5539 0.1457  -0.1189 -0.0643 684 SER A CA  
3055 C C   . SER A 388 ? 1.4105 0.5342 0.6369 0.1786  -0.1051 -0.0684 684 SER A C   
3056 O O   . SER A 388 ? 1.4378 0.5950 0.6718 0.2397  -0.0913 -0.0701 684 SER A O   
3057 C CB  . SER A 388 ? 1.5552 0.5247 0.6229 0.1872  -0.1154 -0.0593 684 SER A CB  
3058 O OG  . SER A 388 ? 1.7470 0.6139 0.7132 0.1569  -0.1273 -0.0530 684 SER A OG  
3059 N N   . GLY A 389 ? 1.2170 0.4316 0.5356 0.1333  -0.1074 -0.0635 685 GLY A N   
3060 C CA  . GLY A 389 ? 1.1713 0.5142 0.5981 0.1464  -0.0947 -0.0598 685 GLY A CA  
3061 C C   . GLY A 389 ? 1.2155 0.5953 0.6446 0.2063  -0.0776 -0.0631 685 GLY A C   
3062 O O   . GLY A 389 ? 1.1838 0.6306 0.6593 0.2377  -0.0671 -0.0601 685 GLY A O   
3063 N N   . SER A 390 ? 1.2140 0.5568 0.5921 0.2219  -0.0745 -0.0693 686 SER A N   
3064 C CA  . SER A 390 ? 1.1287 0.5280 0.5186 0.2731  -0.0564 -0.0717 686 SER A CA  
3065 C C   . SER A 390 ? 1.3211 0.6690 0.6331 0.3410  -0.0486 -0.0779 686 SER A C   
3066 O O   . SER A 390 ? 1.3367 0.7408 0.6545 0.3893  -0.0323 -0.0802 686 SER A O   
3067 C CB  . SER A 390 ? 1.1190 0.5100 0.4901 0.2630  -0.0549 -0.0753 686 SER A CB  
3068 O OG  . SER A 390 ? 1.2138 0.4798 0.4808 0.2533  -0.0677 -0.0830 686 SER A OG  
3069 N N   . ILE A 391 ? 1.5011 0.7457 0.7359 0.3483  -0.0593 -0.0802 687 ILE A N   
3070 C CA  . ILE A 391 ? 1.4349 0.6785 0.6254 0.4049  -0.0527 -0.0761 687 ILE A CA  
3071 C C   . ILE A 391 ? 1.2602 0.5798 0.5167 0.4199  -0.0489 -0.0713 687 ILE A C   
3072 O O   . ILE A 391 ? 1.3752 0.6974 0.5986 0.4604  -0.0469 -0.0672 687 ILE A O   
3073 C CB  . ILE A 391 ? 1.5371 0.6513 0.6079 0.4015  -0.0660 -0.0726 687 ILE A CB  
3074 C CG1 . ILE A 391 ? 1.6764 0.7308 0.7311 0.3530  -0.0810 -0.0681 687 ILE A CG1 
3075 C CG2 . ILE A 391 ? 1.5808 0.6219 0.5846 0.3860  -0.0709 -0.0755 687 ILE A CG2 
3076 C CD1 . ILE A 391 ? 1.7921 0.7217 0.7218 0.3509  -0.0926 -0.0631 687 ILE A CD1 
3077 N N   . THR A 392 ? 1.2439 0.6356 0.5969 0.3815  -0.0495 -0.0688 688 THR A N   
3078 C CA  . THR A 392 ? 1.2205 0.7165 0.6573 0.3890  -0.0443 -0.0620 688 THR A CA  
3079 C C   . THR A 392 ? 1.1622 0.7999 0.6973 0.3860  -0.0302 -0.0585 688 THR A C   
3080 O O   . THR A 392 ? 1.0994 0.7561 0.6637 0.3501  -0.0291 -0.0579 688 THR A O   
3081 C CB  . THR A 392 ? 1.2217 0.7121 0.6995 0.3332  -0.0569 -0.0556 688 THR A CB  
3082 O OG1 . THR A 392 ? 1.1244 0.6639 0.6720 0.2754  -0.0596 -0.0524 688 THR A OG1 
3083 C CG2 . THR A 392 ? 1.3594 0.7086 0.7374 0.3200  -0.0715 -0.0574 688 THR A CG2 
3084 N N   . PRO A 393 ? 1.1566 0.8940 0.7381 0.4213  -0.0199 -0.0555 689 PRO A N   
3085 C CA  . PRO A 393 ? 0.9940 0.8615 0.6507 0.4194  -0.0051 -0.0523 689 PRO A CA  
3086 C C   . PRO A 393 ? 0.8424 0.7666 0.5841 0.3533  -0.0079 -0.0456 689 PRO A C   
3087 O O   . PRO A 393 ? 0.9025 0.9004 0.6868 0.3383  0.0023  -0.0428 689 PRO A O   
3088 C CB  . PRO A 393 ? 1.1602 1.1184 0.8389 0.4694  0.0031  -0.0505 689 PRO A CB  
3089 C CG  . PRO A 393 ? 1.1893 1.0860 0.8467 0.4699  -0.0106 -0.0493 689 PRO A CG  
3090 C CD  . PRO A 393 ? 1.2309 0.9717 0.7988 0.4590  -0.0226 -0.0541 689 PRO A CD  
3091 N N   . VAL A 394 ? 0.7994 0.6881 0.5604 0.3144  -0.0211 -0.0429 690 VAL A N   
3092 C CA  . VAL A 394 ? 0.6881 0.6276 0.5223 0.2601  -0.0235 -0.0373 690 VAL A CA  
3093 C C   . VAL A 394 ? 0.7326 0.6379 0.5581 0.2292  -0.0259 -0.0379 690 VAL A C   
3094 O O   . VAL A 394 ? 0.8419 0.7978 0.7183 0.1973  -0.0235 -0.0333 690 VAL A O   
3095 C CB  . VAL A 394 ? 0.7214 0.6391 0.5771 0.2316  -0.0358 -0.0347 690 VAL A CB  
3096 C CG1 . VAL A 394 ? 0.7693 0.7334 0.6414 0.2595  -0.0338 -0.0331 690 VAL A CG1 
3097 C CG2 . VAL A 394 ? 0.9044 0.7129 0.6980 0.2201  -0.0484 -0.0377 690 VAL A CG2 
3098 N N   . PHE A 395 ? 0.7984 0.6125 0.5531 0.2375  -0.0318 -0.0434 691 PHE A N   
3099 C CA  . PHE A 395 ? 0.7933 0.5779 0.5341 0.2117  -0.0350 -0.0443 691 PHE A CA  
3100 C C   . PHE A 395 ? 0.8785 0.7340 0.6478 0.2182  -0.0204 -0.0419 691 PHE A C   
3101 O O   . PHE A 395 ? 0.7506 0.6148 0.5397 0.1870  -0.0224 -0.0387 691 PHE A O   
3102 C CB  . PHE A 395 ? 0.9049 0.5820 0.5517 0.2268  -0.0418 -0.0519 691 PHE A CB  
3103 C CG  . PHE A 395 ? 0.9661 0.6079 0.5886 0.2016  -0.0471 -0.0539 691 PHE A CG  
3104 C CD1 . PHE A 395 ? 0.9010 0.4898 0.5077 0.1586  -0.0644 -0.0539 691 PHE A CD1 
3105 C CD2 . PHE A 395 ? 1.0096 0.6752 0.6210 0.2214  -0.0351 -0.0555 691 PHE A CD2 
3106 C CE1 . PHE A 395 ? 1.0684 0.6320 0.6527 0.1364  -0.0712 -0.0555 691 PHE A CE1 
3107 C CE2 . PHE A 395 ? 1.0505 0.6810 0.6352 0.1997  -0.0410 -0.0572 691 PHE A CE2 
3108 C CZ  . PHE A 395 ? 1.0852 0.6639 0.6560 0.1580  -0.0600 -0.0574 691 PHE A CZ  
3109 N N   . HIS A 396 ? 0.9156 0.8246 0.6834 0.2592  -0.0059 -0.0428 692 HIS A N   
3110 C CA  . HIS A 396 ? 0.9082 0.8830 0.6866 0.2704  0.0102  -0.0410 692 HIS A CA  
3111 C C   . HIS A 396 ? 0.7641 0.8479 0.6175 0.2467  0.0190  -0.0326 692 HIS A C   
3112 O O   . HIS A 396 ? 0.7371 0.8921 0.6033 0.2513  0.0341  -0.0294 692 HIS A O   
3113 C CB  . HIS A 396 ? 1.0180 0.9935 0.7424 0.3329  0.0218  -0.0474 692 HIS A CB  
3114 C CG  . HIS A 396 ? 1.1147 0.9659 0.7474 0.3559  0.0128  -0.0565 692 HIS A CG  
3115 N ND1 . HIS A 396 ? 1.0542 0.8408 0.6464 0.3367  0.0082  -0.0597 692 HIS A ND1 
3116 C CD2 . HIS A 396 ? 1.1291 0.9004 0.6942 0.3931  0.0063  -0.0629 692 HIS A CD2 
3117 C CE1 . HIS A 396 ? 1.1559 0.8295 0.6592 0.3579  -0.0008 -0.0683 692 HIS A CE1 
3118 N NE2 . HIS A 396 ? 1.2205 0.8767 0.7024 0.3918  -0.0021 -0.0701 692 HIS A NE2 
3119 N N   . GLN A 397 ? 0.7795 0.8749 0.6774 0.2178  0.0098  -0.0288 693 GLN A N   
3120 C CA  . GLN A 397 ? 0.7287 0.9157 0.6875 0.1954  0.0154  -0.0221 693 GLN A CA  
3121 C C   . GLN A 397 ? 0.6943 0.8632 0.6805 0.1437  0.0076  -0.0168 693 GLN A C   
3122 O O   . GLN A 397 ? 0.6598 0.7769 0.6500 0.1278  -0.0062 -0.0179 693 GLN A O   
3123 C CB  . GLN A 397 ? 0.7077 0.9157 0.6852 0.2107  0.0103  -0.0231 693 GLN A CB  
3124 C CG  . GLN A 397 ? 0.5079 0.8078 0.5436 0.1850  0.0137  -0.0171 693 GLN A CG  
3125 C CD  . GLN A 397 ? 0.6835 1.0914 0.7347 0.1996  0.0301  -0.0141 693 GLN A CD  
3126 O OE1 . GLN A 397 ? 0.7553 1.1986 0.7879 0.2504  0.0369  -0.0175 693 GLN A OE1 
3127 N NE2 . GLN A 397 ? 0.7145 1.1761 0.7944 0.1556  0.0365  -0.0073 693 GLN A NE2 
3128 N N   . GLU A 398 ? 0.5592 0.7691 0.5585 0.1192  0.0164  -0.0107 694 GLU A N   
3129 C CA  . GLU A 398 ? 0.6538 0.8476 0.6728 0.0746  0.0094  -0.0049 694 GLU A CA  
3130 C C   . GLU A 398 ? 0.6247 0.8450 0.6810 0.0576  0.0036  -0.0035 694 GLU A C   
3131 O O   . GLU A 398 ? 0.6474 0.9354 0.7252 0.0663  0.0101  -0.0032 694 GLU A O   
3132 C CB  . GLU A 398 ? 0.4644 0.6956 0.4809 0.0498  0.0211  0.0026  694 GLU A CB  
3133 C CG  . GLU A 398 ? 0.7468 0.9499 0.7235 0.0661  0.0270  0.0013  694 GLU A CG  
3134 C CD  . GLU A 398 ? 0.7721 1.0142 0.7418 0.0409  0.0402  0.0097  694 GLU A CD  
3135 O OE1 . GLU A 398 ? 0.8452 1.0616 0.7805 0.0498  0.0448  0.0095  694 GLU A OE1 
3136 O OE2 . GLU A 398 ? 0.8158 1.1117 0.8096 0.0089  0.0456  0.0167  694 GLU A OE2 
3137 N N   . MET A 399 ? 0.6620 0.8324 0.7239 0.0363  -0.0091 -0.0030 695 MET A N   
3138 C CA  . MET A 399 ? 0.6317 0.8145 0.7218 0.0216  -0.0156 -0.0029 695 MET A CA  
3139 C C   . MET A 399 ? 0.6471 0.7959 0.7355 -0.0110 -0.0222 0.0012  695 MET A C   
3140 O O   . MET A 399 ? 0.7906 0.8866 0.8603 -0.0113 -0.0293 0.0013  695 MET A O   
3141 C CB  . MET A 399 ? 0.6238 0.7718 0.7151 0.0408  -0.0260 -0.0086 695 MET A CB  
3142 C CG  . MET A 399 ? 0.6702 0.8284 0.7486 0.0772  -0.0224 -0.0129 695 MET A CG  
3143 S SD  . MET A 399 ? 0.5971 0.6833 0.6551 0.0875  -0.0361 -0.0178 695 MET A SD  
3144 C CE  . MET A 399 ? 0.4360 0.5151 0.4565 0.1335  -0.0311 -0.0221 695 MET A CE  
3145 N N   . LEU A 400 ? 0.5771 0.7538 0.6792 -0.0368 -0.0210 0.0043  696 LEU A N   
3146 C CA  . LEU A 400 ? 0.5987 0.7296 0.6868 -0.0641 -0.0282 0.0073  696 LEU A CA  
3147 C C   . LEU A 400 ? 0.6680 0.7738 0.7692 -0.0573 -0.0393 0.0024  696 LEU A C   
3148 O O   . LEU A 400 ? 0.5433 0.6851 0.6666 -0.0573 -0.0392 -0.0002 696 LEU A O   
3149 C CB  . LEU A 400 ? 0.6305 0.7926 0.7129 -0.1019 -0.0218 0.0131  696 LEU A CB  
3150 C CG  . LEU A 400 ? 0.6910 0.8730 0.7525 -0.1211 -0.0106 0.0203  696 LEU A CG  
3151 C CD1 . LEU A 400 ? 0.7364 0.9561 0.7933 -0.1668 -0.0060 0.0260  696 LEU A CD1 
3152 C CD2 . LEU A 400 ? 0.6714 0.7750 0.6937 -0.1231 -0.0155 0.0238  696 LEU A CD2 
3153 N N   . ASN A 401 ? 0.6656 0.7169 0.7529 -0.0504 -0.0487 0.0013  697 ASN A N   
3154 C CA  . ASN A 401 ? 0.6673 0.7007 0.7647 -0.0442 -0.0579 -0.0029 697 ASN A CA  
3155 C C   . ASN A 401 ? 0.6669 0.6639 0.7409 -0.0631 -0.0618 -0.0013 697 ASN A C   
3156 O O   . ASN A 401 ? 0.5412 0.4995 0.5811 -0.0735 -0.0622 0.0034  697 ASN A O   
3157 C CB  . ASN A 401 ? 0.7103 0.7192 0.8070 -0.0239 -0.0662 -0.0054 697 ASN A CB  
3158 C CG  . ASN A 401 ? 0.6542 0.6687 0.7697 -0.0154 -0.0723 -0.0100 697 ASN A CG  
3159 O OD1 . ASN A 401 ? 0.6390 0.6764 0.7702 -0.0192 -0.0697 -0.0119 697 ASN A OD1 
3160 N ND2 . ASN A 401 ? 0.4556 0.4561 0.5694 -0.0047 -0.0805 -0.0112 697 ASN A ND2 
3161 N N   . TYR A 402 ? 0.6650 0.6671 0.7491 -0.0670 -0.0650 -0.0051 698 TYR A N   
3162 C CA  . TYR A 402 ? 0.5326 0.4876 0.5851 -0.0808 -0.0703 -0.0057 698 TYR A CA  
3163 C C   . TYR A 402 ? 0.7013 0.6703 0.7726 -0.0753 -0.0740 -0.0119 698 TYR A C   
3164 O O   . TYR A 402 ? 0.6372 0.6561 0.7442 -0.0686 -0.0716 -0.0140 698 TYR A O   
3165 C CB  . TYR A 402 ? 0.6821 0.6280 0.7046 -0.1188 -0.0657 -0.0005 698 TYR A CB  
3166 C CG  . TYR A 402 ? 0.7070 0.7297 0.7605 -0.1382 -0.0573 0.0010  698 TYR A CG  
3167 C CD1 . TYR A 402 ? 0.7840 0.8393 0.8522 -0.1527 -0.0591 -0.0023 698 TYR A CD1 
3168 C CD2 . TYR A 402 ? 0.6559 0.7242 0.7221 -0.1386 -0.0479 0.0056  698 TYR A CD2 
3169 C CE1 . TYR A 402 ? 0.7247 0.8626 0.8223 -0.1661 -0.0526 -0.0006 698 TYR A CE1 
3170 C CE2 . TYR A 402 ? 0.6800 0.8305 0.7740 -0.1491 -0.0398 0.0069  698 TYR A CE2 
3171 C CZ  . TYR A 402 ? 0.7305 0.9192 0.8418 -0.1623 -0.0428 0.0040  698 TYR A CZ  
3172 O OH  . TYR A 402 ? 0.6333 0.9158 0.7737 -0.1687 -0.0361 0.0055  698 TYR A OH  
3173 N N   . ARG A 403 ? 0.6175 0.5359 0.6574 -0.0748 -0.0803 -0.0148 699 ARG A N   
3174 C CA  . ARG A 403 ? 0.7754 0.6989 0.8265 -0.0640 -0.0841 -0.0213 699 ARG A CA  
3175 C C   . ARG A 403 ? 0.8296 0.7463 0.8623 -0.0948 -0.0848 -0.0232 699 ARG A C   
3176 O O   . ARG A 403 ? 0.9797 0.8351 0.9597 -0.1135 -0.0880 -0.0228 699 ARG A O   
3177 C CB  . ARG A 403 ? 0.8941 0.7719 0.9199 -0.0359 -0.0904 -0.0247 699 ARG A CB  
3178 C CG  . ARG A 403 ? 0.9339 0.8272 0.9764 -0.0088 -0.0920 -0.0228 699 ARG A CG  
3179 C CD  . ARG A 403 ? 1.0418 0.9948 1.1335 0.0002  -0.0903 -0.0242 699 ARG A CD  
3180 N NE  . ARG A 403 ? 1.2007 1.1665 1.3016 0.0168  -0.0928 -0.0292 699 ARG A NE  
3181 C CZ  . ARG A 403 ? 1.2484 1.2558 1.3790 0.0262  -0.0931 -0.0295 699 ARG A CZ  
3182 N NH1 . ARG A 403 ? 1.1636 1.1928 1.3116 0.0212  -0.0924 -0.0260 699 ARG A NH1 
3183 N NH2 . ARG A 403 ? 1.2017 1.2258 1.3385 0.0387  -0.0940 -0.0333 699 ARG A NH2 
3184 N N   . LEU A 404 ? 0.8225 0.7975 0.8916 -0.1012 -0.0828 -0.0249 700 LEU A N   
3185 C CA  . LEU A 404 ? 0.7604 0.7393 0.8166 -0.1286 -0.0858 -0.0279 700 LEU A CA  
3186 C C   . LEU A 404 ? 0.8507 0.8216 0.9117 -0.1091 -0.0904 -0.0351 700 LEU A C   
3187 O O   . LEU A 404 ? 0.8531 0.8319 0.9357 -0.0774 -0.0898 -0.0367 700 LEU A O   
3188 C CB  . LEU A 404 ? 0.6541 0.7143 0.7454 -0.1479 -0.0814 -0.0246 700 LEU A CB  
3189 C CG  . LEU A 404 ? 0.6892 0.7830 0.7834 -0.1674 -0.0744 -0.0173 700 LEU A CG  
3190 C CD1 . LEU A 404 ? 0.5551 0.7461 0.6887 -0.1743 -0.0705 -0.0155 700 LEU A CD1 
3191 C CD2 . LEU A 404 ? 0.7505 0.7885 0.7895 -0.2083 -0.0758 -0.0139 700 LEU A CD2 
3192 N N   . THR A 405 ? 0.8226 0.7799 0.8599 -0.1324 -0.0950 -0.0392 701 THR A N   
3193 C CA  . THR A 405 ? 0.7767 0.7239 0.8106 -0.1182 -0.0991 -0.0466 701 THR A CA  
3194 C C   . THR A 405 ? 0.7164 0.7074 0.7597 -0.1473 -0.1024 -0.0481 701 THR A C   
3195 O O   . THR A 405 ? 0.6514 0.6556 0.6817 -0.1857 -0.1036 -0.0449 701 THR A O   
3196 C CB  . THR A 405 ? 0.8580 0.7146 0.8289 -0.1103 -0.1038 -0.0524 701 THR A CB  
3197 O OG1 . THR A 405 ? 0.9625 0.8163 0.9337 -0.0872 -0.1056 -0.0597 701 THR A OG1 
3198 C CG2 . THR A 405 ? 0.8643 0.6631 0.7734 -0.1535 -0.1091 -0.0531 701 THR A CG2 
3199 N N   . PRO A 406 ? 0.6988 0.7209 0.7652 -0.1318 -0.1042 -0.0520 702 PRO A N   
3200 C CA  . PRO A 406 ? 0.6876 0.7126 0.7731 -0.0947 -0.1023 -0.0547 702 PRO A CA  
3201 C C   . PRO A 406 ? 0.6920 0.7414 0.8118 -0.0693 -0.0963 -0.0491 702 PRO A C   
3202 O O   . PRO A 406 ? 0.6672 0.7504 0.8079 -0.0753 -0.0933 -0.0435 702 PRO A O   
3203 C CB  . PRO A 406 ? 0.5917 0.6674 0.6992 -0.0985 -0.1054 -0.0561 702 PRO A CB  
3204 C CG  . PRO A 406 ? 0.6260 0.7025 0.7086 -0.1378 -0.1119 -0.0583 702 PRO A CG  
3205 C CD  . PRO A 406 ? 0.6939 0.7581 0.7632 -0.1613 -0.1096 -0.0534 702 PRO A CD  
3206 N N   . SER A 407 ? 0.6800 0.7166 0.8030 -0.0426 -0.0946 -0.0508 703 SER A N   
3207 C CA  . SER A 407 ? 0.6442 0.6952 0.7892 -0.0263 -0.0907 -0.0458 703 SER A CA  
3208 C C   . SER A 407 ? 0.5874 0.6509 0.7442 -0.0055 -0.0892 -0.0467 703 SER A C   
3209 O O   . SER A 407 ? 0.6994 0.7506 0.8413 0.0036  -0.0899 -0.0518 703 SER A O   
3210 C CB  . SER A 407 ? 0.5632 0.5761 0.6859 -0.0242 -0.0909 -0.0446 703 SER A CB  
3211 O OG  . SER A 407 ? 0.6236 0.6031 0.7212 -0.0046 -0.0927 -0.0493 703 SER A OG  
3212 N N   . PHE A 408 ? 0.6179 0.7048 0.7963 0.0001  -0.0870 -0.0416 704 PHE A N   
3213 C CA  . PHE A 408 ? 0.6512 0.7535 0.8378 0.0113  -0.0857 -0.0405 704 PHE A CA  
3214 C C   . PHE A 408 ? 0.6351 0.7317 0.8179 0.0213  -0.0863 -0.0399 704 PHE A C   
3215 O O   . PHE A 408 ? 0.6823 0.7673 0.8636 0.0178  -0.0872 -0.0371 704 PHE A O   
3216 C CB  . PHE A 408 ? 0.4830 0.6024 0.6816 0.0068  -0.0847 -0.0351 704 PHE A CB  
3217 C CG  . PHE A 408 ? 0.5280 0.6556 0.7262 0.0043  -0.0849 -0.0348 704 PHE A CG  
3218 C CD1 . PHE A 408 ? 0.4671 0.5997 0.6670 0.0031  -0.0860 -0.0331 704 PHE A CD1 
3219 C CD2 . PHE A 408 ? 0.4892 0.6256 0.6841 0.0057  -0.0840 -0.0358 704 PHE A CD2 
3220 C CE1 . PHE A 408 ? 0.5370 0.6816 0.7345 0.0058  -0.0878 -0.0323 704 PHE A CE1 
3221 C CE2 . PHE A 408 ? 0.4259 0.5669 0.6162 0.0049  -0.0852 -0.0348 704 PHE A CE2 
3222 C CZ  . PHE A 408 ? 0.4807 0.6249 0.6717 0.0062  -0.0879 -0.0331 704 PHE A CZ  
3223 N N   . GLU A 409 ? 0.5270 0.6379 0.7075 0.0360  -0.0859 -0.0422 705 GLU A N   
3224 C CA  . GLU A 409 ? 0.5472 0.6636 0.7229 0.0523  -0.0877 -0.0420 705 GLU A CA  
3225 C C   . GLU A 409 ? 0.5879 0.7588 0.7826 0.0551  -0.0865 -0.0394 705 GLU A C   
3226 O O   . GLU A 409 ? 0.6008 0.7960 0.8041 0.0472  -0.0831 -0.0390 705 GLU A O   
3227 C CB  . GLU A 409 ? 0.4969 0.5794 0.6403 0.0749  -0.0892 -0.0481 705 GLU A CB  
3228 C CG  . GLU A 409 ? 0.7273 0.7503 0.8409 0.0631  -0.0911 -0.0505 705 GLU A CG  
3229 C CD  . GLU A 409 ? 0.8068 0.8064 0.9140 0.0531  -0.0932 -0.0456 705 GLU A CD  
3230 O OE1 . GLU A 409 ? 0.8467 0.8660 0.9651 0.0630  -0.0944 -0.0419 705 GLU A OE1 
3231 O OE2 . GLU A 409 ? 0.8232 0.7897 0.9133 0.0328  -0.0936 -0.0453 705 GLU A OE2 
3232 N N   . TYR A 410 ? 0.4863 0.6790 0.6850 0.0634  -0.0896 -0.0370 706 TYR A N   
3233 C CA  . TYR A 410 ? 0.4460 0.7038 0.6618 0.0634  -0.0894 -0.0343 706 TYR A CA  
3234 C C   . TYR A 410 ? 0.5078 0.7955 0.7172 0.0959  -0.0870 -0.0393 706 TYR A C   
3235 O O   . TYR A 410 ? 0.6877 0.9330 0.8706 0.1228  -0.0880 -0.0447 706 TYR A O   
3236 C CB  . TYR A 410 ? 0.3713 0.6508 0.5936 0.0586  -0.0955 -0.0299 706 TYR A CB  
3237 C CG  . TYR A 410 ? 0.4729 0.7221 0.6943 0.0293  -0.0974 -0.0257 706 TYR A CG  
3238 C CD1 . TYR A 410 ? 0.6057 0.8039 0.8148 0.0314  -0.0988 -0.0259 706 TYR A CD1 
3239 C CD2 . TYR A 410 ? 0.5522 0.8187 0.7771 0.0001  -0.0973 -0.0214 706 TYR A CD2 
3240 C CE1 . TYR A 410 ? 0.7028 0.8752 0.9069 0.0118  -0.0994 -0.0230 706 TYR A CE1 
3241 C CE2 . TYR A 410 ? 0.7567 0.9823 0.9679 -0.0200 -0.0993 -0.0186 706 TYR A CE2 
3242 C CZ  . TYR A 410 ? 0.7275 0.9098 0.9304 -0.0106 -0.1000 -0.0199 706 TYR A CZ  
3243 O OH  . TYR A 410 ? 0.6294 0.7745 0.8156 -0.0234 -0.1007 -0.0180 706 TYR A OH  
3244 N N   . GLN A 411 ? 0.3936 0.7534 0.6209 0.0933  -0.0838 -0.0373 707 GLN A N   
3245 C CA  . GLN A 411 ? 0.3878 0.7946 0.6110 0.1291  -0.0801 -0.0419 707 GLN A CA  
3246 C C   . GLN A 411 ? 0.4140 0.9239 0.6647 0.1206  -0.0797 -0.0364 707 GLN A C   
3247 O O   . GLN A 411 ? 0.4654 0.9975 0.7318 0.0778  -0.0808 -0.0295 707 GLN A O   
3248 C CB  . GLN A 411 ? 0.5905 0.9813 0.8026 0.1327  -0.0728 -0.0469 707 GLN A CB  
3249 C CG  . GLN A 411 ? 0.6262 1.0590 0.8581 0.0973  -0.0676 -0.0415 707 GLN A CG  
3250 C CD  . GLN A 411 ? 0.7424 1.1454 0.9600 0.0975  -0.0620 -0.0458 707 GLN A CD  
3251 O OE1 . GLN A 411 ? 0.8232 1.1973 1.0172 0.1288  -0.0605 -0.0542 707 GLN A OE1 
3252 N NE2 . GLN A 411 ? 0.6655 1.0676 0.8892 0.0628  -0.0600 -0.0402 707 GLN A NE2 
3253 N N   . PRO A 412 ? 0.5131 1.0875 0.7647 0.1604  -0.0787 -0.0391 708 PRO A N   
3254 C CA  . PRO A 412 ? 0.5707 1.2262 0.8341 0.1424  -0.0740 -0.0319 708 PRO A CA  
3255 C C   . PRO A 412 ? 0.6330 1.3355 0.9085 0.1063  -0.0650 -0.0277 708 PRO A C   
3256 O O   . PRO A 412 ? 0.6068 1.2934 0.8797 0.1101  -0.0597 -0.0316 708 PRO A O   
3257 C CB  . PRO A 412 ? 0.5867 1.2689 0.8278 0.1958  -0.0700 -0.0364 708 PRO A CB  
3258 C CG  . PRO A 412 ? 0.7227 1.3346 0.9349 0.2367  -0.0693 -0.0462 708 PRO A CG  
3259 C CD  . PRO A 412 ? 0.6482 1.1853 0.8656 0.2171  -0.0784 -0.0472 708 PRO A CD  
3260 N N   . ASP A 413 ? 0.6674 1.4262 0.9515 0.0692  -0.0640 -0.0196 709 ASP A N   
3261 C CA  . ASP A 413 ? 0.7141 1.5185 1.0003 0.0314  -0.0556 -0.0140 709 ASP A CA  
3262 C C   . ASP A 413 ? 0.7443 1.6012 1.0247 0.0668  -0.0441 -0.0183 709 ASP A C   
3263 O O   . ASP A 413 ? 0.7329 1.6280 1.0059 0.1085  -0.0424 -0.0220 709 ASP A O   
3264 C CB  . ASP A 413 ? 0.7457 1.6008 1.0316 -0.0130 -0.0573 -0.0048 709 ASP A CB  
3265 C CG  . ASP A 413 ? 0.7660 1.5610 1.0472 -0.0558 -0.0678 -0.0004 709 ASP A CG  
3266 O OD1 . ASP A 413 ? 0.7233 1.4469 1.0023 -0.0607 -0.0718 -0.0028 709 ASP A OD1 
3267 O OD2 . ASP A 413 ? 0.7520 1.5725 1.0274 -0.0843 -0.0723 0.0050  709 ASP A OD2 
3268 N N   . PRO A 414 ? 0.8307 1.6894 1.1095 0.0539  -0.0365 -0.0184 710 PRO A N   
3269 C CA  . PRO A 414 ? 0.8666 1.7650 1.1353 0.0937  -0.0259 -0.0244 710 PRO A CA  
3270 C C   . PRO A 414 ? 0.8887 1.8874 1.1538 0.0974  -0.0188 -0.0204 710 PRO A C   
3271 O O   . PRO A 414 ? 1.0156 2.0465 1.2661 0.1460  -0.0128 -0.0269 710 PRO A O   
3272 C CB  . PRO A 414 ? 0.8735 1.7545 1.1425 0.0675  -0.0203 -0.0234 710 PRO A CB  
3273 C CG  . PRO A 414 ? 0.9026 1.7609 1.1773 0.0047  -0.0261 -0.0133 710 PRO A CG  
3274 C CD  . PRO A 414 ? 0.8754 1.6937 1.1555 0.0058  -0.0379 -0.0134 710 PRO A CD  
3275 N N   . TRP A 415 ? 0.8341 1.8821 1.1058 0.0489  -0.0202 -0.0103 711 TRP A N   
3276 C CA  . TRP A 415 ? 0.8237 1.9786 1.0912 0.0495  -0.0142 -0.0061 711 TRP A CA  
3277 C C   . TRP A 415 ? 0.8008 1.9912 1.0662 0.0928  -0.0188 -0.0096 711 TRP A C   
3278 O O   . TRP A 415 ? 0.8075 2.0957 1.0686 0.1004  -0.0148 -0.0068 711 TRP A O   
3279 C CB  . TRP A 415 ? 0.8083 2.0038 1.0746 -0.0226 -0.0145 0.0063  711 TRP A CB  
3280 C CG  . TRP A 415 ? 0.7563 1.9061 1.0247 -0.0595 -0.0256 0.0111  711 TRP A CG  
3281 C CD1 . TRP A 415 ? 0.7466 1.9392 1.0168 -0.0651 -0.0316 0.0141  711 TRP A CD1 
3282 C CD2 . TRP A 415 ? 0.6855 1.7390 0.9503 -0.0948 -0.0324 0.0132  711 TRP A CD2 
3283 N NE1 . TRP A 415 ? 0.6570 1.7817 0.9242 -0.1022 -0.0417 0.0176  711 TRP A NE1 
3284 C CE2 . TRP A 415 ? 0.6492 1.6872 0.9114 -0.1197 -0.0425 0.0170  711 TRP A CE2 
3285 C CE3 . TRP A 415 ? 0.6900 1.6712 0.9507 -0.1061 -0.0316 0.0121  711 TRP A CE3 
3286 C CZ2 . TRP A 415 ? 0.6523 1.6012 0.9042 -0.1534 -0.0516 0.0192  711 TRP A CZ2 
3287 C CZ3 . TRP A 415 ? 0.6270 1.5243 0.8790 -0.1392 -0.0409 0.0147  711 TRP A CZ3 
3288 C CH2 . TRP A 415 ? 0.6635 1.5428 0.9094 -0.1613 -0.0507 0.0180  711 TRP A CH2 
3289 N N   . ASN A 416 ? 0.6864 1.8034 0.9518 0.1211  -0.0275 -0.0152 712 ASN A N   
3290 C CA  . ASN A 416 ? 0.7176 1.8559 0.9724 0.1711  -0.0317 -0.0194 712 ASN A CA  
3291 C C   . ASN A 416 ? 0.7901 1.9012 1.0170 0.2411  -0.0281 -0.0301 712 ASN A C   
3292 O O   . ASN A 416 ? 0.8082 1.9570 1.0149 0.2886  -0.0288 -0.0333 712 ASN A O   
3293 C CB  . ASN A 416 ? 0.7658 1.8366 1.0265 0.1652  -0.0439 -0.0190 712 ASN A CB  
3294 C CG  . ASN A 416 ? 0.8461 1.9185 1.1245 0.0968  -0.0490 -0.0098 712 ASN A CG  
3295 O OD1 . ASN A 416 ? 0.9144 2.0610 1.1960 0.0572  -0.0451 -0.0024 712 ASN A OD1 
3296 N ND2 . ASN A 416 ? 0.8118 1.7991 1.0948 0.0817  -0.0584 -0.0101 712 ASN A ND2 
3297 N N   . THR A 417 ? 0.7934 1.8375 1.0127 0.2490  -0.0249 -0.0357 713 THR A N   
3298 C CA  . THR A 417 ? 0.8898 1.8831 1.0721 0.3118  -0.0231 -0.0467 713 THR A CA  
3299 C C   . THR A 417 ? 0.8903 1.9337 1.0590 0.3287  -0.0121 -0.0495 713 THR A C   
3300 O O   . THR A 417 ? 0.9631 2.0055 1.0929 0.3874  -0.0103 -0.0569 713 THR A O   
3301 C CB  . THR A 417 ? 0.9197 1.7945 1.0954 0.3122  -0.0287 -0.0524 713 THR A CB  
3302 O OG1 . THR A 417 ? 0.8445 1.7063 1.0570 0.2513  -0.0323 -0.0450 713 THR A OG1 
3303 C CG2 . THR A 417 ? 0.9706 1.7682 1.1145 0.3538  -0.0385 -0.0578 713 THR A CG2 
3304 N N   . HIS A 418 ? 0.8518 1.9350 1.0458 0.2789  -0.0054 -0.0434 714 HIS A N   
3305 C CA  . HIS A 418 ? 0.8597 1.9699 1.0415 0.2895  0.0049  -0.0463 714 HIS A CA  
3306 C C   . HIS A 418 ? 0.9067 2.1073 1.0660 0.3324  0.0100  -0.0475 714 HIS A C   
3307 O O   . HIS A 418 ? 0.8695 2.1656 1.0413 0.3169  0.0100  -0.0399 714 HIS A O   
3308 C CB  . HIS A 418 ? 0.7930 1.9380 1.0032 0.2211  0.0103  -0.0367 714 HIS A CB  
3309 C CG  . HIS A 418 ? 0.7929 1.9585 0.9924 0.2255  0.0209  -0.0391 714 HIS A CG  
3310 N ND1 . HIS A 418 ? 0.8397 1.9403 1.0133 0.2718  0.0234  -0.0509 714 HIS A ND1 
3311 C CD2 . HIS A 418 ? 0.7928 2.0323 0.9996 0.1870  0.0292  -0.0310 714 HIS A CD2 
3312 C CE1 . HIS A 418 ? 0.8115 1.9489 0.9802 0.2642  0.0335  -0.0504 714 HIS A CE1 
3313 N NE2 . HIS A 418 ? 0.7769 1.9998 0.9665 0.2127  0.0373  -0.0379 714 HIS A NE2 
3314 N N   . VAL A 419 ? 0.9945 2.1642 1.1163 0.3869  0.0134  -0.0572 715 VAL A N   
3315 C CA  . VAL A 419 ? 1.0735 2.3280 1.1694 0.4307  0.0184  -0.0584 715 VAL A CA  
3316 C C   . VAL A 419 ? 1.0544 2.3902 1.1715 0.3910  0.0286  -0.0519 715 VAL A C   
3317 O O   . VAL A 419 ? 0.9687 2.2564 1.0839 0.3799  0.0340  -0.0552 715 VAL A O   
3318 C CB  . VAL A 419 ? 1.1185 2.2933 1.1549 0.5049  0.0166  -0.0710 715 VAL A CB  
3319 C CG1 . VAL A 419 ? 1.1711 2.4257 1.1816 0.5441  0.0233  -0.0722 715 VAL A CG1 
3320 C CG2 . VAL A 419 ? 1.0846 2.2074 1.0883 0.5492  0.0063  -0.0751 715 VAL A CG2 
3321 N N   . TRP A 420 ? 1.1409 2.6010 1.2751 0.3680  0.0309  -0.0423 716 TRP A N   
3322 C CA  . TRP A 420 ? 1.2148 2.7492 1.3736 0.3062  0.0381  -0.0323 716 TRP A CA  
3323 C C   . TRP A 420 ? 1.4913 3.1515 1.6384 0.3287  0.0437  -0.0295 716 TRP A C   
3324 O O   . TRP A 420 ? 1.5315 3.2575 1.6637 0.3731  0.0403  -0.0306 716 TRP A O   
3325 C CB  . TRP A 420 ? 1.1242 2.6846 1.3137 0.2353  0.0335  -0.0209 716 TRP A CB  
3326 C CG  . TRP A 420 ? 1.0953 2.6440 1.3006 0.1632  0.0376  -0.0124 716 TRP A CG  
3327 C CD1 . TRP A 420 ? 1.1461 2.6941 1.3454 0.1531  0.0461  -0.0125 716 TRP A CD1 
3328 C CD2 . TRP A 420 ? 1.0346 2.5628 1.2564 0.0912  0.0327  -0.0024 716 TRP A CD2 
3329 N NE1 . TRP A 420 ? 1.1364 2.6649 1.3460 0.0789  0.0469  -0.0025 716 TRP A NE1 
3330 C CE2 . TRP A 420 ? 1.0473 2.5594 1.2677 0.0402  0.0383  0.0037  716 TRP A CE2 
3331 C CE3 . TRP A 420 ? 0.9760 2.4931 1.2080 0.0658  0.0239  0.0021  716 TRP A CE3 
3332 C CZ2 . TRP A 420 ? 0.9803 2.4585 1.2025 -0.0338 0.0344  0.0143  716 TRP A CZ2 
3333 C CZ3 . TRP A 420 ? 0.9826 2.4684 1.2192 -0.0075 0.0202  0.0120  716 TRP A CZ3 
3334 C CH2 . TRP A 420 ? 0.9716 2.4346 1.2000 -0.0560 0.0251  0.0180  716 TRP A CH2 
# 
