data_9CVM
# 
_entry.id   9CVM 
# 
_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   9CVM         pdb_00009cvm 10.2210/pdb9cvm/pdb 
WWPDB D_1000286176 ?            ?                   
# 
_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                        9CVM 
_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 'ACETATE ION'                                                    59.044    1  ?          ?     ? ? 
5 non-polymer syn 'ZINC ION'                                                       65.409    1  ?          ?     ? ? 
6 non-polymer syn "(2M)-4-methyl-5'-[(methylamino)methyl][2,3'-bipyridin]-6-amine" 228.293   1  ?          ?     ? ? 
7 water       nat water                                                            18.015    52 ?          ?     ? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        'BNOS,Constitutive NOS,NC-NOS,NOS type I,Neuronal NOS,nNOS,Peptidyl-cysteine S-nitrosylase NOS1' 
# 
_entity_poly.entity_id                      1 
_entity_poly.type                           'polypeptide(L)' 
_entity_poly.nstd_linkage                   no 
_entity_poly.nstd_monomer                   no 
_entity_poly.pdbx_seq_one_letter_code       
;CPRFLKVKNWETDVVLTDTLHLKSTLETGCTEHICMGSIMLPSQHTRKPEDVATKDQLFPLAKEFLDQYYSSIKRFGSKA
HMDRLEEVNKEIESTSTYQLKDTELIYGAKHAWRNASRCVGRIQWSKLQVFDARDCTTAHGMFNYICNHVKYATNKGNLR
SAITIFPQRTDGKHDFRVWNSQLIRYAGYKQPDGSTLGDPANVQFTEICIQQGWKAPRGRFDVLPLLLQANGNDPELFQI
PPELVLEVPIRHPKFDWFKDLGLKWYGLPAVSNMLLEIGGLEFSACPFSGWYMGTEIGVRDYCDNSRYNILEEVAKKMDL
DMRKTSSLWKDQALVEINIAVLYSFQSDKVTIVDHHSATESFIKHMENEYRCRGGCPADWVWIVPPMSGSITPVFHQEML
NYRLTPSFEYQPDPWNTHVWKG
;
_entity_poly.pdbx_seq_one_letter_code_can   
;CPRFLKVKNWETDVVLTDTLHLKSTLETGCTEHICMGSIMLPSQHTRKPEDVATKDQLFPLAKEFLDQYYSSIKRFGSKA
HMDRLEEVNKEIESTSTYQLKDTELIYGAKHAWRNASRCVGRIQWSKLQVFDARDCTTAHGMFNYICNHVKYATNKGNLR
SAITIFPQRTDGKHDFRVWNSQLIRYAGYKQPDGSTLGDPANVQFTEICIQQGWKAPRGRFDVLPLLLQANGNDPELFQI
PPELVLEVPIRHPKFDWFKDLGLKWYGLPAVSNMLLEIGGLEFSACPFSGWYMGTEIGVRDYCDNSRYNILEEVAKKMDL
DMRKTSSLWKDQALVEINIAVLYSFQSDKVTIVDHHSATESFIKHMENEYRCRGGCPADWVWIVPPMSGSITPVFHQEML
NYRLTPSFEYQPDPWNTHVWKG
;
_entity_poly.pdbx_strand_id                 A 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 'PROTOPORPHYRIN IX CONTAINING FE'                                HEM   
3 5,6,7,8-TETRAHYDROBIOPTERIN                                      H4B   
4 'ACETATE ION'                                                    ACT   
5 'ZINC ION'                                                       ZN    
6 "(2M)-4-methyl-5'-[(methylamino)methyl][2,3'-bipyridin]-6-amine" A1A0E 
7 water                                                            HOH   
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   CYS n 
1 2   PRO n 
1 3   ARG n 
1 4   PHE n 
1 5   LEU n 
1 6   LYS n 
1 7   VAL n 
1 8   LYS n 
1 9   ASN n 
1 10  TRP n 
1 11  GLU n 
1 12  THR n 
1 13  ASP n 
1 14  VAL n 
1 15  VAL n 
1 16  LEU n 
1 17  THR n 
1 18  ASP n 
1 19  THR n 
1 20  LEU n 
1 21  HIS n 
1 22  LEU n 
1 23  LYS n 
1 24  SER n 
1 25  THR n 
1 26  LEU n 
1 27  GLU n 
1 28  THR n 
1 29  GLY n 
1 30  CYS n 
1 31  THR n 
1 32  GLU n 
1 33  HIS n 
1 34  ILE n 
1 35  CYS n 
1 36  MET n 
1 37  GLY n 
1 38  SER n 
1 39  ILE n 
1 40  MET n 
1 41  LEU n 
1 42  PRO n 
1 43  SER n 
1 44  GLN n 
1 45  HIS n 
1 46  THR n 
1 47  ARG n 
1 48  LYS n 
1 49  PRO n 
1 50  GLU n 
1 51  ASP n 
1 52  VAL n 
1 53  ALA n 
1 54  THR n 
1 55  LYS n 
1 56  ASP n 
1 57  GLN n 
1 58  LEU n 
1 59  PHE n 
1 60  PRO n 
1 61  LEU n 
1 62  ALA n 
1 63  LYS n 
1 64  GLU n 
1 65  PHE n 
1 66  LEU n 
1 67  ASP n 
1 68  GLN n 
1 69  TYR n 
1 70  TYR n 
1 71  SER n 
1 72  SER n 
1 73  ILE n 
1 74  LYS n 
1 75  ARG n 
1 76  PHE n 
1 77  GLY n 
1 78  SER n 
1 79  LYS n 
1 80  ALA n 
1 81  HIS n 
1 82  MET n 
1 83  ASP n 
1 84  ARG n 
1 85  LEU n 
1 86  GLU n 
1 87  GLU n 
1 88  VAL n 
1 89  ASN n 
1 90  LYS n 
1 91  GLU n 
1 92  ILE n 
1 93  GLU n 
1 94  SER n 
1 95  THR n 
1 96  SER n 
1 97  THR n 
1 98  TYR n 
1 99  GLN n 
1 100 LEU n 
1 101 LYS n 
1 102 ASP n 
1 103 THR n 
1 104 GLU n 
1 105 LEU n 
1 106 ILE n 
1 107 TYR n 
1 108 GLY n 
1 109 ALA n 
1 110 LYS n 
1 111 HIS n 
1 112 ALA n 
1 113 TRP n 
1 114 ARG n 
1 115 ASN n 
1 116 ALA n 
1 117 SER n 
1 118 ARG n 
1 119 CYS n 
1 120 VAL n 
1 121 GLY n 
1 122 ARG n 
1 123 ILE n 
1 124 GLN n 
1 125 TRP n 
1 126 SER n 
1 127 LYS n 
1 128 LEU n 
1 129 GLN n 
1 130 VAL n 
1 131 PHE n 
1 132 ASP n 
1 133 ALA n 
1 134 ARG n 
1 135 ASP n 
1 136 CYS n 
1 137 THR n 
1 138 THR n 
1 139 ALA n 
1 140 HIS n 
1 141 GLY n 
1 142 MET n 
1 143 PHE n 
1 144 ASN n 
1 145 TYR n 
1 146 ILE n 
1 147 CYS n 
1 148 ASN n 
1 149 HIS n 
1 150 VAL n 
1 151 LYS n 
1 152 TYR n 
1 153 ALA n 
1 154 THR n 
1 155 ASN n 
1 156 LYS n 
1 157 GLY n 
1 158 ASN n 
1 159 LEU n 
1 160 ARG n 
1 161 SER n 
1 162 ALA n 
1 163 ILE n 
1 164 THR n 
1 165 ILE n 
1 166 PHE n 
1 167 PRO n 
1 168 GLN n 
1 169 ARG n 
1 170 THR n 
1 171 ASP n 
1 172 GLY n 
1 173 LYS n 
1 174 HIS n 
1 175 ASP n 
1 176 PHE n 
1 177 ARG n 
1 178 VAL n 
1 179 TRP n 
1 180 ASN n 
1 181 SER n 
1 182 GLN n 
1 183 LEU n 
1 184 ILE n 
1 185 ARG n 
1 186 TYR n 
1 187 ALA n 
1 188 GLY n 
1 189 TYR n 
1 190 LYS n 
1 191 GLN n 
1 192 PRO n 
1 193 ASP n 
1 194 GLY n 
1 195 SER n 
1 196 THR n 
1 197 LEU n 
1 198 GLY n 
1 199 ASP n 
1 200 PRO n 
1 201 ALA n 
1 202 ASN n 
1 203 VAL n 
1 204 GLN n 
1 205 PHE n 
1 206 THR n 
1 207 GLU n 
1 208 ILE n 
1 209 CYS n 
1 210 ILE n 
1 211 GLN n 
1 212 GLN n 
1 213 GLY n 
1 214 TRP n 
1 215 LYS n 
1 216 ALA n 
1 217 PRO n 
1 218 ARG n 
1 219 GLY n 
1 220 ARG n 
1 221 PHE n 
1 222 ASP n 
1 223 VAL n 
1 224 LEU n 
1 225 PRO n 
1 226 LEU n 
1 227 LEU n 
1 228 LEU n 
1 229 GLN n 
1 230 ALA n 
1 231 ASN n 
1 232 GLY n 
1 233 ASN n 
1 234 ASP n 
1 235 PRO n 
1 236 GLU n 
1 237 LEU n 
1 238 PHE n 
1 239 GLN n 
1 240 ILE n 
1 241 PRO n 
1 242 PRO n 
1 243 GLU n 
1 244 LEU n 
1 245 VAL n 
1 246 LEU n 
1 247 GLU n 
1 248 VAL n 
1 249 PRO n 
1 250 ILE n 
1 251 ARG n 
1 252 HIS n 
1 253 PRO n 
1 254 LYS n 
1 255 PHE n 
1 256 ASP n 
1 257 TRP n 
1 258 PHE n 
1 259 LYS n 
1 260 ASP n 
1 261 LEU n 
1 262 GLY n 
1 263 LEU n 
1 264 LYS n 
1 265 TRP n 
1 266 TYR n 
1 267 GLY n 
1 268 LEU n 
1 269 PRO n 
1 270 ALA n 
1 271 VAL n 
1 272 SER n 
1 273 ASN n 
1 274 MET n 
1 275 LEU n 
1 276 LEU n 
1 277 GLU n 
1 278 ILE n 
1 279 GLY n 
1 280 GLY n 
1 281 LEU n 
1 282 GLU n 
1 283 PHE n 
1 284 SER n 
1 285 ALA n 
1 286 CYS n 
1 287 PRO n 
1 288 PHE n 
1 289 SER n 
1 290 GLY n 
1 291 TRP n 
1 292 TYR n 
1 293 MET n 
1 294 GLY n 
1 295 THR n 
1 296 GLU n 
1 297 ILE n 
1 298 GLY n 
1 299 VAL n 
1 300 ARG n 
1 301 ASP n 
1 302 TYR n 
1 303 CYS n 
1 304 ASP n 
1 305 ASN n 
1 306 SER n 
1 307 ARG n 
1 308 TYR n 
1 309 ASN n 
1 310 ILE n 
1 311 LEU n 
1 312 GLU n 
1 313 GLU n 
1 314 VAL n 
1 315 ALA n 
1 316 LYS n 
1 317 LYS n 
1 318 MET n 
1 319 ASP n 
1 320 LEU n 
1 321 ASP n 
1 322 MET n 
1 323 ARG n 
1 324 LYS n 
1 325 THR n 
1 326 SER n 
1 327 SER n 
1 328 LEU n 
1 329 TRP n 
1 330 LYS n 
1 331 ASP n 
1 332 GLN n 
1 333 ALA n 
1 334 LEU n 
1 335 VAL n 
1 336 GLU n 
1 337 ILE n 
1 338 ASN n 
1 339 ILE n 
1 340 ALA n 
1 341 VAL n 
1 342 LEU n 
1 343 TYR n 
1 344 SER n 
1 345 PHE n 
1 346 GLN n 
1 347 SER n 
1 348 ASP n 
1 349 LYS n 
1 350 VAL n 
1 351 THR n 
1 352 ILE n 
1 353 VAL n 
1 354 ASP n 
1 355 HIS n 
1 356 HIS n 
1 357 SER n 
1 358 ALA n 
1 359 THR n 
1 360 GLU n 
1 361 SER n 
1 362 PHE n 
1 363 ILE n 
1 364 LYS n 
1 365 HIS n 
1 366 MET n 
1 367 GLU n 
1 368 ASN n 
1 369 GLU n 
1 370 TYR n 
1 371 ARG n 
1 372 CYS n 
1 373 ARG n 
1 374 GLY n 
1 375 GLY n 
1 376 CYS n 
1 377 PRO n 
1 378 ALA n 
1 379 ASP n 
1 380 TRP n 
1 381 VAL n 
1 382 TRP n 
1 383 ILE n 
1 384 VAL n 
1 385 PRO n 
1 386 PRO n 
1 387 MET n 
1 388 SER n 
1 389 GLY n 
1 390 SER n 
1 391 ILE n 
1 392 THR n 
1 393 PRO n 
1 394 VAL n 
1 395 PHE n 
1 396 HIS n 
1 397 GLN n 
1 398 GLU n 
1 399 MET n 
1 400 LEU n 
1 401 ASN n 
1 402 TYR n 
1 403 ARG n 
1 404 LEU n 
1 405 THR n 
1 406 PRO n 
1 407 SER n 
1 408 PHE n 
1 409 GLU n 
1 410 TYR n 
1 411 GLN n 
1 412 PRO n 
1 413 ASP n 
1 414 PRO n 
1 415 TRP n 
1 416 ASN n 
1 417 THR n 
1 418 HIS n 
1 419 VAL n 
1 420 TRP n 
1 421 LYS n 
1 422 GLY n 
# 
_entity_src_gen.entity_id                          1 
_entity_src_gen.pdbx_src_id                        1 
_entity_src_gen.pdbx_alt_source_flag               sample 
_entity_src_gen.pdbx_seq_type                      'Biological sequence' 
_entity_src_gen.pdbx_beg_seq_num                   1 
_entity_src_gen.pdbx_end_seq_num                   422 
_entity_src_gen.gene_src_common_name               'Norway rat' 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 'Nos1, Bnos' 
_entity_src_gen.gene_src_species                   ? 
_entity_src_gen.gene_src_strain                    ? 
_entity_src_gen.gene_src_tissue                    ? 
_entity_src_gen.gene_src_tissue_fraction           ? 
_entity_src_gen.gene_src_details                   ? 
_entity_src_gen.pdbx_gene_src_fragment             ? 
_entity_src_gen.pdbx_gene_src_scientific_name      'Rattus norvegicus' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     10116 
_entity_src_gen.pdbx_gene_src_variant              ? 
_entity_src_gen.pdbx_gene_src_cell_line            ? 
_entity_src_gen.pdbx_gene_src_atcc                 ? 
_entity_src_gen.pdbx_gene_src_organ                brain 
_entity_src_gen.pdbx_gene_src_organelle            ? 
_entity_src_gen.pdbx_gene_src_cell                 ? 
_entity_src_gen.pdbx_gene_src_cellular_location    ? 
_entity_src_gen.host_org_common_name               ? 
_entity_src_gen.pdbx_host_org_scientific_name      'Escherichia coli BL21(DE3)' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     469008 
_entity_src_gen.host_org_genus                     ? 
_entity_src_gen.pdbx_host_org_gene                 ? 
_entity_src_gen.pdbx_host_org_organ                ? 
_entity_src_gen.host_org_species                   ? 
_entity_src_gen.pdbx_host_org_tissue               ? 
_entity_src_gen.pdbx_host_org_tissue_fraction      ? 
_entity_src_gen.pdbx_host_org_strain               ? 
_entity_src_gen.pdbx_host_org_variant              ? 
_entity_src_gen.pdbx_host_org_cell_line            ? 
_entity_src_gen.pdbx_host_org_atcc                 ? 
_entity_src_gen.pdbx_host_org_culture_collection   ? 
_entity_src_gen.pdbx_host_org_cell                 ? 
_entity_src_gen.pdbx_host_org_organelle            ? 
_entity_src_gen.pdbx_host_org_cellular_location    ? 
_entity_src_gen.pdbx_host_org_vector_type          plasmid 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       pET22b 
_entity_src_gen.plasmid_details                    ? 
_entity_src_gen.pdbx_description                   ? 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
A1A0E non-polymer         . "(2M)-4-methyl-5'-[(methylamino)methyl][2,3'-bipyridin]-6-amine" ?    'C13 H16 N4'       228.293 
ACT   non-polymer         . 'ACETATE ION'                                                    ?    'C2 H3 O2 -1'      59.044  
ALA   'L-peptide linking' y ALANINE                                                          ?    'C3 H7 N O2'       89.093  
ARG   'L-peptide linking' y ARGININE                                                         ?    'C6 H15 N4 O2 1'   175.209 
ASN   'L-peptide linking' y ASPARAGINE                                                       ?    'C4 H8 N2 O3'      132.118 
ASP   'L-peptide linking' y 'ASPARTIC ACID'                                                  ?    'C4 H7 N O4'       133.103 
CYS   'L-peptide linking' y CYSTEINE                                                         ?    'C3 H7 N O2 S'     121.158 
GLN   'L-peptide linking' y GLUTAMINE                                                        ?    'C5 H10 N2 O3'     146.144 
GLU   'L-peptide linking' y 'GLUTAMIC ACID'                                                  ?    'C5 H9 N O4'       147.129 
GLY   'peptide linking'   y GLYCINE                                                          ?    'C2 H5 N O2'       75.067  
H4B   non-polymer         . 5,6,7,8-TETRAHYDROBIOPTERIN                                      ?    'C9 H15 N5 O3'     241.247 
HEM   non-polymer         . 'PROTOPORPHYRIN IX CONTAINING FE'                                HEME 'C34 H32 Fe N4 O4' 616.487 
HIS   'L-peptide linking' y HISTIDINE                                                        ?    'C6 H10 N3 O2 1'   156.162 
HOH   non-polymer         . WATER                                                            ?    'H2 O'             18.015  
ILE   'L-peptide linking' y ISOLEUCINE                                                       ?    'C6 H13 N O2'      131.173 
LEU   'L-peptide linking' y LEUCINE                                                          ?    'C6 H13 N O2'      131.173 
LYS   'L-peptide linking' y LYSINE                                                           ?    'C6 H15 N2 O2 1'   147.195 
MET   'L-peptide linking' y METHIONINE                                                       ?    'C5 H11 N O2 S'    149.211 
PHE   'L-peptide linking' y PHENYLALANINE                                                    ?    'C9 H11 N O2'      165.189 
PRO   'L-peptide linking' y PROLINE                                                          ?    'C5 H9 N O2'       115.130 
SER   'L-peptide linking' y SERINE                                                           ?    'C3 H7 N O3'       105.093 
THR   'L-peptide linking' y THREONINE                                                        ?    'C4 H9 N O3'       119.119 
TRP   'L-peptide linking' y TRYPTOPHAN                                                       ?    'C11 H12 N2 O2'    204.225 
TYR   'L-peptide linking' y TYROSINE                                                         ?    'C9 H11 N O3'      181.189 
VAL   'L-peptide linking' y VALINE                                                           ?    'C5 H11 N O2'      117.146 
ZN    non-polymer         . 'ZINC ION'                                                       ?    'Zn 2'             65.409  
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   CYS 1   297 ?   ?   ?   A . n 
A 1 2   PRO 2   298 ?   ?   ?   A . n 
A 1 3   ARG 3   299 299 ARG ARG A . n 
A 1 4   PHE 4   300 300 PHE PHE A . n 
A 1 5   LEU 5   301 301 LEU LEU A . n 
A 1 6   LYS 6   302 302 LYS LYS A . n 
A 1 7   VAL 7   303 303 VAL VAL A . n 
A 1 8   LYS 8   304 304 LYS LYS A . n 
A 1 9   ASN 9   305 305 ASN ASN A . n 
A 1 10  TRP 10  306 306 TRP TRP A . n 
A 1 11  GLU 11  307 307 GLU GLU A . n 
A 1 12  THR 12  308 308 THR THR A . n 
A 1 13  ASP 13  309 309 ASP ASP A . n 
A 1 14  VAL 14  310 310 VAL VAL A . n 
A 1 15  VAL 15  311 311 VAL VAL A . n 
A 1 16  LEU 16  312 312 LEU LEU A . n 
A 1 17  THR 17  313 313 THR THR A . n 
A 1 18  ASP 18  314 314 ASP ASP A . n 
A 1 19  THR 19  315 315 THR THR A . n 
A 1 20  LEU 20  316 316 LEU LEU A . n 
A 1 21  HIS 21  317 317 HIS HIS A . n 
A 1 22  LEU 22  318 318 LEU LEU A . n 
A 1 23  LYS 23  319 319 LYS LYS A . n 
A 1 24  SER 24  320 320 SER SER A . n 
A 1 25  THR 25  321 321 THR THR A . n 
A 1 26  LEU 26  322 322 LEU LEU A . n 
A 1 27  GLU 27  323 323 GLU GLU A . n 
A 1 28  THR 28  324 324 THR THR A . n 
A 1 29  GLY 29  325 325 GLY GLY A . n 
A 1 30  CYS 30  326 326 CYS CYS A . n 
A 1 31  THR 31  327 327 THR THR A . n 
A 1 32  GLU 32  328 328 GLU GLU A . n 
A 1 33  HIS 33  329 329 HIS HIS A . n 
A 1 34  ILE 34  330 330 ILE ILE A . n 
A 1 35  CYS 35  331 331 CYS CYS A . n 
A 1 36  MET 36  332 332 MET MET A . n 
A 1 37  GLY 37  333 333 GLY GLY A . n 
A 1 38  SER 38  334 334 SER SER A . n 
A 1 39  ILE 39  335 335 ILE ILE A . n 
A 1 40  MET 40  336 336 MET MET A . n 
A 1 41  LEU 41  337 337 LEU LEU A . n 
A 1 42  PRO 42  338 338 PRO PRO A . n 
A 1 43  SER 43  339 339 SER SER A . n 
A 1 44  GLN 44  340 ?   ?   ?   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        A1A0E 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   A1A0E 
_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 ACT   1  803 860 ACT   ACT A . 
E 5 ZN    1  804 900 ZN    ZN  A . 
F 6 A1A0E 1  805 800 A1A0E 4V6 A . 
G 7 HOH   1  901 34  HOH   HOH A . 
G 7 HOH   2  902 20  HOH   HOH A . 
G 7 HOH   3  903 5   HOH   HOH A . 
G 7 HOH   4  904 12  HOH   HOH A . 
G 7 HOH   5  905 49  HOH   HOH A . 
G 7 HOH   6  906 4   HOH   HOH A . 
G 7 HOH   7  907 13  HOH   HOH A . 
G 7 HOH   8  908 39  HOH   HOH A . 
G 7 HOH   9  909 18  HOH   HOH A . 
G 7 HOH   10 910 11  HOH   HOH A . 
G 7 HOH   11 911 2   HOH   HOH A . 
G 7 HOH   12 912 28  HOH   HOH A . 
G 7 HOH   13 913 19  HOH   HOH A . 
G 7 HOH   14 914 44  HOH   HOH A . 
G 7 HOH   15 915 21  HOH   HOH A . 
G 7 HOH   16 916 38  HOH   HOH A . 
G 7 HOH   17 917 32  HOH   HOH A . 
G 7 HOH   18 918 45  HOH   HOH A . 
G 7 HOH   19 919 41  HOH   HOH A . 
G 7 HOH   20 920 51  HOH   HOH A . 
G 7 HOH   21 921 36  HOH   HOH A . 
G 7 HOH   22 922 33  HOH   HOH A . 
G 7 HOH   23 923 8   HOH   HOH A . 
G 7 HOH   24 924 6   HOH   HOH A . 
G 7 HOH   25 925 15  HOH   HOH A . 
G 7 HOH   26 926 30  HOH   HOH A . 
G 7 HOH   27 927 9   HOH   HOH A . 
G 7 HOH   28 928 27  HOH   HOH A . 
G 7 HOH   29 929 14  HOH   HOH A . 
G 7 HOH   30 930 50  HOH   HOH A . 
G 7 HOH   31 931 1   HOH   HOH A . 
G 7 HOH   32 932 16  HOH   HOH A . 
G 7 HOH   33 933 35  HOH   HOH A . 
G 7 HOH   34 934 25  HOH   HOH A . 
G 7 HOH   35 935 24  HOH   HOH A . 
G 7 HOH   36 936 40  HOH   HOH A . 
G 7 HOH   37 937 3   HOH   HOH A . 
G 7 HOH   38 938 47  HOH   HOH A . 
G 7 HOH   39 939 52  HOH   HOH A . 
G 7 HOH   40 940 43  HOH   HOH A . 
G 7 HOH   41 941 37  HOH   HOH A . 
G 7 HOH   42 942 17  HOH   HOH A . 
G 7 HOH   43 943 29  HOH   HOH A . 
G 7 HOH   44 944 42  HOH   HOH A . 
G 7 HOH   45 945 48  HOH   HOH A . 
G 7 HOH   46 946 22  HOH   HOH A . 
G 7 HOH   47 947 7   HOH   HOH A . 
G 7 HOH   48 948 23  HOH   HOH A . 
G 7 HOH   49 949 10  HOH   HOH A . 
G 7 HOH   50 950 46  HOH   HOH A . 
G 7 HOH   51 951 26  HOH   HOH A . 
G 7 HOH   52 952 31  HOH   HOH A . 
# 
loop_
_software.citation_id 
_software.classification 
_software.compiler_name 
_software.compiler_version 
_software.contact_author 
_software.contact_author_email 
_software.date 
_software.description 
_software.dependencies 
_software.hardware 
_software.language 
_software.location 
_software.mods 
_software.name 
_software.os 
_software.os_version 
_software.type 
_software.version 
_software.pdbx_ordinal 
? refinement       ? ? ? ? ? ? ? ? ? ? ? PHENIX  ? ? ? '(1.11.1_2575: ???)' 1 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? Aimless ? ? ? .                    2 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? XDS     ? ? ? .                    3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? REFMAC  ? ? ? .                    4 
# 
_cell.angle_alpha                  90.00 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   90.00 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.00 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     9CVM 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     48.462 
_cell.length_a_esd                 ? 
_cell.length_b                     113.007 
_cell.length_b_esd                 ? 
_cell.length_c                     162.788 
_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                         9CVM 
_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                   9CVM 
_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         2023-03-17 
_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                                       9CVM 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              1.80 
_reflns.d_resolution_low                               46.42 
_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                                     41948 
_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                           100.0 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                11.2 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          9.2 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               ? 
_reflns.pdbx_scaling_rejects                           ? 
_reflns.pdbx_d_res_high_opt                            ? 
_reflns.pdbx_d_res_low_opt                             ? 
_reflns.pdbx_d_res_opt_method                          ? 
_reflns.phase_calculation_details                      ? 
_reflns.pdbx_Rrim_I_all                                0.090 
_reflns.pdbx_Rpim_I_all                                0.027 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       468353 
_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                              0.086 
_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                                    1.80 
_reflns_shell.d_res_low                                     1.84 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           ? 
_reflns_shell.number_measured_all                           21887 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             2427 
_reflns_shell.percent_possible_obs                          100.0 
_reflns_shell.Rmerge_F_all                                  ? 
_reflns_shell.Rmerge_F_obs                                  ? 
_reflns_shell.meanI_over_sigI_gt                            ? 
_reflns_shell.meanI_over_uI_all                             ? 
_reflns_shell.meanI_over_uI_gt                              ? 
_reflns_shell.number_measured_gt                            ? 
_reflns_shell.number_unique_gt                              ? 
_reflns_shell.percent_possible_gt                           ? 
_reflns_shell.Rmerge_F_gt                                   ? 
_reflns_shell.Rmerge_I_gt                                   ? 
_reflns_shell.pdbx_redundancy                               9.0 
_reflns_shell.pdbx_chi_squared                              ? 
_reflns_shell.pdbx_netI_over_sigmaI_all                     ? 
_reflns_shell.pdbx_netI_over_sigmaI_obs                     0.4 
_reflns_shell.pdbx_Rrim_I_all                               6.066 
_reflns_shell.pdbx_Rpim_I_all                               2.007 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.714 
_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                                  5.713 
_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                                 9CVM 
_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                            1.800 
_refine.ls_d_res_low                             46.416 
_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                     39804 
_refine.ls_number_reflns_R_free                  3815 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    94.27 
_refine.ls_percent_reflns_R_free                 5.06 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.2183 
_refine.ls_R_factor_R_free                       0.2564 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.2162 
_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                          0.04 
_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                 43.94 
_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                            0.23 
_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             52 
_refine_hist.number_atoms_total               3475 
_refine_hist.d_res_high                       1.800 
_refine_hist.d_res_low                        46.416 
# 
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  ? 3530 ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 1.015  ? 4801 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 18.407 ? 2054 ? f_dihedral_angle_d ? ? 
'X-RAY DIFFRACTION' ? 0.048  ? 498  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.006  ? 606  ? f_plane_restr      ? ? 
# 
loop_
_refine_ls_shell.pdbx_refine_id 
_refine_ls_shell.d_res_high 
_refine_ls_shell.d_res_low 
_refine_ls_shell.number_reflns_all 
_refine_ls_shell.number_reflns_obs 
_refine_ls_shell.number_reflns_R_free 
_refine_ls_shell.number_reflns_R_work 
_refine_ls_shell.percent_reflns_obs 
_refine_ls_shell.percent_reflns_R_free 
_refine_ls_shell.R_factor_all 
_refine_ls_shell.R_factor_obs 
_refine_ls_shell.R_factor_R_free_error 
_refine_ls_shell.R_factor_R_work 
_refine_ls_shell.redundancy_reflns_all 
_refine_ls_shell.redundancy_reflns_obs 
_refine_ls_shell.wR_factor_all 
_refine_ls_shell.wR_factor_obs 
_refine_ls_shell.wR_factor_R_free 
_refine_ls_shell.wR_factor_R_work 
_refine_ls_shell.pdbx_R_complete 
_refine_ls_shell.pdbx_total_number_of_bins_used 
_refine_ls_shell.pdbx_phase_error 
_refine_ls_shell.pdbx_fsc_work 
_refine_ls_shell.pdbx_fsc_free 
_refine_ls_shell.R_factor_R_free 
'X-RAY DIFFRACTION' 1.8000 1.8228 . . 105 2196 79.00  . . . . 0.4660 . . . . . . . . . . . 0.4838 
'X-RAY DIFFRACTION' 1.8228 1.8468 . . 121 2268 80.00  . . . . 0.4429 . . . . . . . . . . . 0.4331 
'X-RAY DIFFRACTION' 1.8468 1.8721 . . 122 2333 83.00  . . . . 0.4324 . . . . . . . . . . . 0.4731 
'X-RAY DIFFRACTION' 1.8721 1.8988 . . 116 2318 84.00  . . . . 0.4235 . . . . . . . . . . . 0.4492 
'X-RAY DIFFRACTION' 1.8988 1.9272 . . 125 2481 86.00  . . . . 0.4011 . . . . . . . . . . . 0.4323 
'X-RAY DIFFRACTION' 1.9272 1.9573 . . 160 2431 88.00  . . . . 0.4092 . . . . . . . . . . . 0.3956 
'X-RAY DIFFRACTION' 1.9573 1.9894 . . 140 2560 90.00  . . . . 0.3810 . . . . . . . . . . . 0.4326 
'X-RAY DIFFRACTION' 1.9894 2.0237 . . 121 2588 91.00  . . . . 0.3484 . . . . . . . . . . . 0.4598 
'X-RAY DIFFRACTION' 2.0237 2.0605 . . 112 2679 95.00  . . . . 0.3369 . . . . . . . . . . . 0.3815 
'X-RAY DIFFRACTION' 2.0605 2.1001 . . 164 2710 95.00  . . . . 0.3243 . . . . . . . . . . . 0.3426 
'X-RAY DIFFRACTION' 2.1001 2.1430 . . 140 2669 97.00  . . . . 0.3134 . . . . . . . . . . . 0.3755 
'X-RAY DIFFRACTION' 2.1430 2.1896 . . 143 2754 97.00  . . . . 0.3112 . . . . . . . . . . . 0.3685 
'X-RAY DIFFRACTION' 2.1896 2.2405 . . 166 2701 97.00  . . . . 0.2901 . . . . . . . . . . . 0.3667 
'X-RAY DIFFRACTION' 2.2405 2.2965 . . 147 2765 98.00  . . . . 0.2764 . . . . . . . . . . . 0.3532 
'X-RAY DIFFRACTION' 2.2965 2.3586 . . 149 2737 97.00  . . . . 0.2850 . . . . . . . . . . . 0.3536 
'X-RAY DIFFRACTION' 2.3586 2.4280 . . 145 2750 98.00  . . . . 0.2885 . . . . . . . . . . . 0.3397 
'X-RAY DIFFRACTION' 2.4280 2.5064 . . 124 2713 97.00  . . . . 0.2725 . . . . . . . . . . . 0.3407 
'X-RAY DIFFRACTION' 2.5064 2.5960 . . 133 2795 97.00  . . . . 0.2641 . . . . . . . . . . . 0.3133 
'X-RAY DIFFRACTION' 2.5960 2.6999 . . 145 2799 99.00  . . . . 0.2790 . . . . . . . . . . . 0.3622 
'X-RAY DIFFRACTION' 2.6999 2.8227 . . 141 2752 99.00  . . . . 0.2748 . . . . . . . . . . . 0.2650 
'X-RAY DIFFRACTION' 2.8227 2.9715 . . 115 2837 99.00  . . . . 0.2679 . . . . . . . . . . . 0.3448 
'X-RAY DIFFRACTION' 2.9715 3.1577 . . 173 2755 99.00  . . . . 0.2703 . . . . . . . . . . . 0.3413 
'X-RAY DIFFRACTION' 3.1577 3.4014 . . 174 2826 100.00 . . . . 0.2322 . . . . . . . . . . . 0.2924 
'X-RAY DIFFRACTION' 3.4014 3.7436 . . 158 2779 100.00 . . . . 0.1977 . . . . . . . . . . . 0.2128 
'X-RAY DIFFRACTION' 3.7436 4.2850 . . 162 2798 100.00 . . . . 0.1678 . . . . . . . . . . . 0.1931 
'X-RAY DIFFRACTION' 4.2850 5.3973 . . 158 2823 100.00 . . . . 0.1470 . . . . . . . . . . . 0.1783 
'X-RAY DIFFRACTION' 5.3973 46.416 . . 156 2801 100.00 . . . . 0.1549 . . . . . . . . . . . 0.2005 
# 
_struct.entry_id                     9CVM 
_struct.title                        
;Structure of rat neuronal nitric oxide synthase R349A mutant bound with 4-methyl-5'-((methylamino)methyl)-[2,3'-bipyridin]-6-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        9CVM 
_struct_keywords.text            'nitric oxide synthase inhibitor binding, OXIDOREDUCTASE' 
_struct_keywords.pdbx_keywords   OXIDOREDUCTASE 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 2 ? 
C N N 3 ? 
D N N 4 ? 
E N N 5 ? 
F N N 6 ? 
G N N 7 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    NOS1_RAT 
_struct_ref.pdbx_db_accession          P29476 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;CPRFLKVKNWETDVVLTDTLHLKSTLETGCTEHICMGSIMLPSQHTRKPEDVRTKDQLFPLAKEFLDQYYSSIKRFGSKA
HMDRLEEVNKEIESTSTYQLKDTELIYGAKHAWRNASRCVGRIQWSKLQVFDARDCTTAHGMFNYICNHVKYATNKGNLR
SAITIFPQRTDGKHDFRVWNSQLIRYAGYKQPDGSTLGDPANVQFTEICIQQGWKAPRGRFDVLPLLLQANGNDPELFQI
PPELVLEVPIRHPKFDWFKDLGLKWYGLPAVSNMLLEIGGLEFSACPFSGWYMGTEIGVRDYCDNSRYNILEEVAKKMDL
DMRKTSSLWKDQALVEINIAVLYSFQSDKVTIVDHHSATESFIKHMENEYRCRGGCPADWVWIVPPMSGSITPVFHQEML
NYRLTPSFEYQPDPWNTHVWKG
;
_struct_ref.pdbx_align_begin           297 
# 
_struct_ref_seq.align_id                      1 
_struct_ref_seq.ref_id                        1 
_struct_ref_seq.pdbx_PDB_id_code              9CVM 
_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             9CVM 
_struct_ref_seq_dif.mon_id                       ALA 
_struct_ref_seq_dif.pdbx_pdb_strand_id           A 
_struct_ref_seq_dif.seq_num                      53 
_struct_ref_seq_dif.pdbx_pdb_ins_code            ? 
_struct_ref_seq_dif.pdbx_seq_db_name             UNP 
_struct_ref_seq_dif.pdbx_seq_db_accession_code   P29476 
_struct_ref_seq_dif.db_mon_id                    ARG 
_struct_ref_seq_dif.pdbx_seq_db_seq_num          349 
_struct_ref_seq_dif.details                      'engineered mutation' 
_struct_ref_seq_dif.pdbx_auth_seq_num            349 
_struct_ref_seq_dif.pdbx_ordinal                 1 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_defined_assembly 
_pdbx_struct_assembly.method_details       ? 
_pdbx_struct_assembly.oligomeric_details   monomeric 
_pdbx_struct_assembly.oligomeric_count     1 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,D,E,F,G 
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   'gel filtration' 
_pdbx_struct_assembly_auth_evidence.details                ? 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1  AA1 THR A 19  ? SER A 24  ? THR A 315 SER A 320 5 ? 6  
HELX_P HELX_P2  AA2 GLN A 57  ? ILE A 73  ? GLN A 353 ILE A 369 1 ? 17 
HELX_P HELX_P3  AA3 SER A 78  ? SER A 96  ? SER A 374 SER A 392 1 ? 19 
HELX_P HELX_P4  AA4 LYS A 101 ? ASN A 115 ? LYS A 397 ASN A 411 1 ? 15 
HELX_P HELX_P5  AA5 GLY A 121 ? TRP A 125 ? GLY A 417 TRP A 421 5 ? 5  
HELX_P HELX_P6  AA6 THR A 138 ? ASN A 155 ? THR A 434 ASN A 451 1 ? 18 
HELX_P HELX_P7  AA7 LYS A 156 ? ASN A 158 ? LYS A 452 ASN A 454 5 ? 3  
HELX_P HELX_P8  AA8 ASN A 202 ? GLN A 212 ? ASN A 498 GLN A 508 1 ? 11 
HELX_P HELX_P9  AA9 PRO A 241 ? VAL A 245 ? PRO A 537 VAL A 541 5 ? 5  
HELX_P HELX_P10 AB1 TRP A 257 ? GLY A 262 ? TRP A 553 GLY A 558 1 ? 6  
HELX_P HELX_P11 AB2 GLY A 294 ? VAL A 299 ? GLY A 590 VAL A 595 1 ? 6  
HELX_P HELX_P12 AB3 VAL A 299 ? ASP A 304 ? VAL A 595 ASP A 600 1 ? 6  
HELX_P HELX_P13 AB4 ILE A 310 ? MET A 318 ? ILE A 606 MET A 614 1 ? 9  
HELX_P HELX_P14 AB5 LYS A 324 ? SER A 327 ? LYS A 620 SER A 623 5 ? 4  
HELX_P HELX_P15 AB6 LEU A 328 ? ASP A 348 ? LEU A 624 ASP A 644 1 ? 21 
HELX_P HELX_P16 AB7 ASP A 354 ? 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 E ZN  . ZN ? ? A CYS 326 A ZN  804 1_555 ? ? ? ? ? ? ? 2.368 ? ? 
metalc2 metalc ? ? A CYS 30  SG ? ? ? 1_555 E ZN  . ZN ? ? A CYS 326 A ZN  804 3_455 ? ? ? ? ? ? ? 2.375 ? ? 
metalc3 metalc ? ? A CYS 35  SG ? ? ? 1_555 E ZN  . ZN ? ? A CYS 331 A ZN  804 1_555 ? ? ? ? ? ? ? 2.261 ? ? 
metalc4 metalc ? ? A CYS 35  SG ? ? ? 1_555 E ZN  . ZN ? ? A CYS 331 A ZN  804 3_455 ? ? ? ? ? ? ? 2.250 ? ? 
metalc5 metalc ? ? A CYS 119 SG ? ? ? 1_555 B HEM . FE ? ? A CYS 415 A HEM 801 1_555 ? ? ? ? ? ? ? 2.351 ? ? 
# 
_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 ? E ZN  . ? A ZN  804 ? 1_555 SG ? A CYS 30 ? A CYS 326 ? 1_555 0.0   ? 
2  SG ? A CYS 30  ? A CYS 326 ? 1_555 ZN ? E ZN  . ? A ZN  804 ? 1_555 SG ? A CYS 35 ? A CYS 331 ? 1_555 113.6 ? 
3  SG ? A CYS 30  ? A CYS 326 ? 1_555 ZN ? E ZN  . ? A ZN  804 ? 1_555 SG ? A CYS 35 ? A CYS 331 ? 1_555 113.6 ? 
4  SG ? A CYS 30  ? A CYS 326 ? 1_555 ZN ? E ZN  . ? A ZN  804 ? 1_555 SG ? A CYS 35 ? A CYS 331 ? 1_555 113.6 ? 
5  SG ? A CYS 30  ? A CYS 326 ? 1_555 ZN ? E ZN  . ? A ZN  804 ? 1_555 SG ? A CYS 35 ? A CYS 331 ? 1_555 113.6 ? 
6  SG ? A CYS 35  ? A CYS 331 ? 1_555 ZN ? E ZN  . ? A ZN  804 ? 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_555 101.7 ? 
8  SG ? A CYS 119 ? A CYS 415 ? 1_555 FE ? B HEM . ? A HEM 801 ? 1_555 NB ? B HEM .  ? A HEM 801 ? 1_555 102.0 ? 
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 85.8  ? 
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_555 103.1 ? 
11 NA ? B HEM .   ? A HEM 801 ? 1_555 FE ? B HEM . ? A HEM 801 ? 1_555 NC ? B HEM .  ? A HEM 801 ? 1_555 154.8 ? 
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 84.9  ? 
13 SG ? A CYS 119 ? A CYS 415 ? 1_555 FE ? B HEM . ? A HEM 801 ? 1_555 ND ? B HEM .  ? A HEM 801 ? 1_555 107.8 ? 
14 NA ? B HEM .   ? A HEM 801 ? 1_555 FE ? B HEM . ? A HEM 801 ? 1_555 ND ? B HEM .  ? A HEM 801 ? 1_555 90.1  ? 
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 86.4  ? 
# 
_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       -1.47 
# 
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 PHE A 283 ? O PHE A 579 N LEU A 276 ? N LEU A 572 
AA6 2 3 N LEU A 275 ? N LEU A 571 O GLU A 409 ? O GLU A 705 
AA7 1 2 N TYR A 292 ? N TYR A 588 O VAL A 353 ? O VAL A 649 
# 
_pdbx_entry_details.entry_id                   9CVM 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.has_protein_modification   N 
# 
_pdbx_validate_close_contact.id               1 
_pdbx_validate_close_contact.PDB_model_num    1 
_pdbx_validate_close_contact.auth_atom_id_1   O 
_pdbx_validate_close_contact.auth_asym_id_1   A 
_pdbx_validate_close_contact.auth_comp_id_1   HIS 
_pdbx_validate_close_contact.auth_seq_id_1    470 
_pdbx_validate_close_contact.PDB_ins_code_1   ? 
_pdbx_validate_close_contact.label_alt_id_1   ? 
_pdbx_validate_close_contact.auth_atom_id_2   O 
_pdbx_validate_close_contact.auth_asym_id_2   A 
_pdbx_validate_close_contact.auth_comp_id_2   HOH 
_pdbx_validate_close_contact.auth_seq_id_2    901 
_pdbx_validate_close_contact.PDB_ins_code_2   ? 
_pdbx_validate_close_contact.label_alt_id_2   ? 
_pdbx_validate_close_contact.dist             2.04 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1  1 THR A 393 ? ? -167.87 -165.94 
2  1 THR A 466 ? ? -112.53 -90.42  
3  1 SER A 491 ? ? -86.37  -154.17 
4  1 PRO A 513 ? ? -80.65  33.25   
5  1 ARG A 514 ? ? -3.86   67.37   
6  1 ARG A 516 ? ? -80.07  -87.69  
7  1 LYS A 550 ? ? -135.10 -43.24  
8  1 CYS A 582 ? ? -150.98 54.85   
9  1 VAL A 595 ? ? -105.16 -61.34  
10 1 ARG A 603 ? ? -114.77 -130.83 
11 1 ASP A 615 ? ? 63.47   80.03   
12 1 ARG A 669 ? ? -150.33 -17.08  
13 1 TRP A 716 ? ? -70.06  -167.02 
# 
_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     804 
_pdbx_struct_special_symmetry.PDB_ins_code    ? 
_pdbx_struct_special_symmetry.label_asym_id   E 
_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         -23.5044 
_pdbx_refine_tls.origin_y         -4.8780 
_pdbx_refine_tls.origin_z         22.1518 
_pdbx_refine_tls.T[1][1]          0.3674 
_pdbx_refine_tls.T[1][1]_esd      ? 
_pdbx_refine_tls.T[1][2]          -0.0546 
_pdbx_refine_tls.T[1][2]_esd      ? 
_pdbx_refine_tls.T[1][3]          -0.0786 
_pdbx_refine_tls.T[1][3]_esd      ? 
_pdbx_refine_tls.T[2][2]          0.3971 
_pdbx_refine_tls.T[2][2]_esd      ? 
_pdbx_refine_tls.T[2][3]          -0.0024 
_pdbx_refine_tls.T[2][3]_esd      ? 
_pdbx_refine_tls.T[3][3]          0.4768 
_pdbx_refine_tls.T[3][3]_esd      ? 
_pdbx_refine_tls.L[1][1]          1.0372 
_pdbx_refine_tls.L[1][1]_esd      ? 
_pdbx_refine_tls.L[1][2]          -0.1148 
_pdbx_refine_tls.L[1][2]_esd      ? 
_pdbx_refine_tls.L[1][3]          0.2859 
_pdbx_refine_tls.L[1][3]_esd      ? 
_pdbx_refine_tls.L[2][2]          1.3560 
_pdbx_refine_tls.L[2][2]_esd      ? 
_pdbx_refine_tls.L[2][3]          -0.1299 
_pdbx_refine_tls.L[2][3]_esd      ? 
_pdbx_refine_tls.L[3][3]          9.2175 
_pdbx_refine_tls.L[3][3]_esd      ? 
_pdbx_refine_tls.S[1][1]          -0.0367 
_pdbx_refine_tls.S[1][1]_esd      ? 
_pdbx_refine_tls.S[1][2]          0.1446 
_pdbx_refine_tls.S[1][2]_esd      ? 
_pdbx_refine_tls.S[1][3]          0.0035 
_pdbx_refine_tls.S[1][3]_esd      ? 
_pdbx_refine_tls.S[2][1]          -0.0201 
_pdbx_refine_tls.S[2][1]_esd      ? 
_pdbx_refine_tls.S[2][2]          -0.0790 
_pdbx_refine_tls.S[2][2]_esd      ? 
_pdbx_refine_tls.S[2][3]          -0.0400 
_pdbx_refine_tls.S[2][3]_esd      ? 
_pdbx_refine_tls.S[3][1]          -0.8481 
_pdbx_refine_tls.S[3][1]_esd      ? 
_pdbx_refine_tls.S[3][2]          0.1968 
_pdbx_refine_tls.S[3][2]_esd      ? 
_pdbx_refine_tls.S[3][3]          0.0594 
_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)' 
# 
_pdbx_distant_solvent_atoms.id                                1 
_pdbx_distant_solvent_atoms.PDB_model_num                     1 
_pdbx_distant_solvent_atoms.auth_atom_id                      O 
_pdbx_distant_solvent_atoms.label_alt_id                      ? 
_pdbx_distant_solvent_atoms.auth_asym_id                      A 
_pdbx_distant_solvent_atoms.auth_comp_id                      HOH 
_pdbx_distant_solvent_atoms.auth_seq_id                       952 
_pdbx_distant_solvent_atoms.PDB_ins_code                      ? 
_pdbx_distant_solvent_atoms.neighbor_macromolecule_distance   5.84 
_pdbx_distant_solvent_atoms.neighbor_ligand_distance          . 
# 
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 
A1A0E C02  C  Y N 1   
A1A0E C03  C  Y N 2   
A1A0E C04  C  Y N 3   
A1A0E C05  C  Y N 4   
A1A0E C06  C  Y N 5   
A1A0E C07  C  N N 6   
A1A0E C12  C  Y N 7   
A1A0E C13  C  Y N 8   
A1A0E C14  C  Y N 9   
A1A0E C15  C  Y N 10  
A1A0E C16  C  Y N 11  
A1A0E C17  C  N N 12  
A1A0E C19  C  N N 13  
A1A0E N01  N  Y N 14  
A1A0E N02  N  N N 15  
A1A0E N11  N  Y N 16  
A1A0E N18  N  N N 17  
A1A0E H1   H  N N 18  
A1A0E H2   H  N N 19  
A1A0E H3   H  N N 20  
A1A0E H4   H  N N 21  
A1A0E H5   H  N N 22  
A1A0E H6   H  N N 23  
A1A0E H7   H  N N 24  
A1A0E H8   H  N N 25  
A1A0E H9   H  N N 26  
A1A0E H10  H  N N 27  
A1A0E H11  H  N N 28  
A1A0E H12  H  N N 29  
A1A0E H13  H  N N 30  
A1A0E H14  H  N N 31  
A1A0E H15  H  N N 32  
A1A0E H16  H  N N 33  
ACT   C    C  N N 34  
ACT   O    O  N N 35  
ACT   OXT  O  N N 36  
ACT   CH3  C  N N 37  
ACT   H1   H  N N 38  
ACT   H2   H  N N 39  
ACT   H3   H  N N 40  
ALA   N    N  N N 41  
ALA   CA   C  N S 42  
ALA   C    C  N N 43  
ALA   O    O  N N 44  
ALA   CB   C  N N 45  
ALA   OXT  O  N N 46  
ALA   H    H  N N 47  
ALA   H2   H  N N 48  
ALA   HA   H  N N 49  
ALA   HB1  H  N N 50  
ALA   HB2  H  N N 51  
ALA   HB3  H  N N 52  
ALA   HXT  H  N N 53  
ARG   N    N  N N 54  
ARG   CA   C  N S 55  
ARG   C    C  N N 56  
ARG   O    O  N N 57  
ARG   CB   C  N N 58  
ARG   CG   C  N N 59  
ARG   CD   C  N N 60  
ARG   NE   N  N N 61  
ARG   CZ   C  N N 62  
ARG   NH1  N  N N 63  
ARG   NH2  N  N N 64  
ARG   OXT  O  N N 65  
ARG   H    H  N N 66  
ARG   H2   H  N N 67  
ARG   HA   H  N N 68  
ARG   HB2  H  N N 69  
ARG   HB3  H  N N 70  
ARG   HG2  H  N N 71  
ARG   HG3  H  N N 72  
ARG   HD2  H  N N 73  
ARG   HD3  H  N N 74  
ARG   HE   H  N N 75  
ARG   HH11 H  N N 76  
ARG   HH12 H  N N 77  
ARG   HH21 H  N N 78  
ARG   HH22 H  N N 79  
ARG   HXT  H  N N 80  
ASN   N    N  N N 81  
ASN   CA   C  N S 82  
ASN   C    C  N N 83  
ASN   O    O  N N 84  
ASN   CB   C  N N 85  
ASN   CG   C  N N 86  
ASN   OD1  O  N N 87  
ASN   ND2  N  N N 88  
ASN   OXT  O  N N 89  
ASN   H    H  N N 90  
ASN   H2   H  N N 91  
ASN   HA   H  N N 92  
ASN   HB2  H  N N 93  
ASN   HB3  H  N N 94  
ASN   HD21 H  N N 95  
ASN   HD22 H  N N 96  
ASN   HXT  H  N N 97  
ASP   N    N  N N 98  
ASP   CA   C  N S 99  
ASP   C    C  N N 100 
ASP   O    O  N N 101 
ASP   CB   C  N N 102 
ASP   CG   C  N N 103 
ASP   OD1  O  N N 104 
ASP   OD2  O  N N 105 
ASP   OXT  O  N N 106 
ASP   H    H  N N 107 
ASP   H2   H  N N 108 
ASP   HA   H  N N 109 
ASP   HB2  H  N N 110 
ASP   HB3  H  N N 111 
ASP   HD2  H  N N 112 
ASP   HXT  H  N N 113 
CYS   N    N  N N 114 
CYS   CA   C  N R 115 
CYS   C    C  N N 116 
CYS   O    O  N N 117 
CYS   CB   C  N N 118 
CYS   SG   S  N N 119 
CYS   OXT  O  N N 120 
CYS   H    H  N N 121 
CYS   H2   H  N N 122 
CYS   HA   H  N N 123 
CYS   HB2  H  N N 124 
CYS   HB3  H  N N 125 
CYS   HG   H  N N 126 
CYS   HXT  H  N N 127 
GLN   N    N  N N 128 
GLN   CA   C  N S 129 
GLN   C    C  N N 130 
GLN   O    O  N N 131 
GLN   CB   C  N N 132 
GLN   CG   C  N N 133 
GLN   CD   C  N N 134 
GLN   OE1  O  N N 135 
GLN   NE2  N  N N 136 
GLN   OXT  O  N N 137 
GLN   H    H  N N 138 
GLN   H2   H  N N 139 
GLN   HA   H  N N 140 
GLN   HB2  H  N N 141 
GLN   HB3  H  N N 142 
GLN   HG2  H  N N 143 
GLN   HG3  H  N N 144 
GLN   HE21 H  N N 145 
GLN   HE22 H  N N 146 
GLN   HXT  H  N N 147 
GLU   N    N  N N 148 
GLU   CA   C  N S 149 
GLU   C    C  N N 150 
GLU   O    O  N N 151 
GLU   CB   C  N N 152 
GLU   CG   C  N N 153 
GLU   CD   C  N N 154 
GLU   OE1  O  N N 155 
GLU   OE2  O  N N 156 
GLU   OXT  O  N N 157 
GLU   H    H  N N 158 
GLU   H2   H  N N 159 
GLU   HA   H  N N 160 
GLU   HB2  H  N N 161 
GLU   HB3  H  N N 162 
GLU   HG2  H  N N 163 
GLU   HG3  H  N N 164 
GLU   HE2  H  N N 165 
GLU   HXT  H  N N 166 
GLY   N    N  N N 167 
GLY   CA   C  N N 168 
GLY   C    C  N N 169 
GLY   O    O  N N 170 
GLY   OXT  O  N N 171 
GLY   H    H  N N 172 
GLY   H2   H  N N 173 
GLY   HA2  H  N N 174 
GLY   HA3  H  N N 175 
GLY   HXT  H  N N 176 
H4B   N1   N  Y N 177 
H4B   C2   C  Y N 178 
H4B   N2   N  N N 179 
H4B   N3   N  Y N 180 
H4B   C4   C  Y N 181 
H4B   O4   O  N N 182 
H4B   C4A  C  Y N 183 
H4B   C8A  C  Y N 184 
H4B   N5   N  N N 185 
H4B   N8   N  N N 186 
H4B   C6   C  N R 187 
H4B   C7   C  N N 188 
H4B   C9   C  N R 189 
H4B   O9   O  N N 190 
H4B   C10  C  N S 191 
H4B   C11  C  N N 192 
H4B   O10  O  N N 193 
H4B   HN21 H  N N 194 
H4B   HN22 H  N N 195 
H4B   HN3  H  N N 196 
H4B   HN5  H  N N 197 
H4B   HN8  H  N N 198 
H4B   H6   H  N N 199 
H4B   H71  H  N N 200 
H4B   H72  H  N N 201 
H4B   H9   H  N N 202 
H4B   HO9  H  N N 203 
H4B   H10  H  N N 204 
H4B   H111 H  N N 205 
H4B   H112 H  N N 206 
H4B   H113 H  N N 207 
H4B   HO0  H  N N 208 
HEM   CHA  C  N N 209 
HEM   CHB  C  N N 210 
HEM   CHC  C  N N 211 
HEM   CHD  C  N N 212 
HEM   C1A  C  Y N 213 
HEM   C2A  C  Y N 214 
HEM   C3A  C  Y N 215 
HEM   C4A  C  Y N 216 
HEM   CMA  C  N N 217 
HEM   CAA  C  N N 218 
HEM   CBA  C  N N 219 
HEM   CGA  C  N N 220 
HEM   O1A  O  N N 221 
HEM   O2A  O  N N 222 
HEM   C1B  C  N N 223 
HEM   C2B  C  N N 224 
HEM   C3B  C  N N 225 
HEM   C4B  C  N N 226 
HEM   CMB  C  N N 227 
HEM   CAB  C  N N 228 
HEM   CBB  C  N N 229 
HEM   C1C  C  Y N 230 
HEM   C2C  C  Y N 231 
HEM   C3C  C  Y N 232 
HEM   C4C  C  Y N 233 
HEM   CMC  C  N N 234 
HEM   CAC  C  N N 235 
HEM   CBC  C  N N 236 
HEM   C1D  C  N N 237 
HEM   C2D  C  N N 238 
HEM   C3D  C  N N 239 
HEM   C4D  C  N N 240 
HEM   CMD  C  N N 241 
HEM   CAD  C  N N 242 
HEM   CBD  C  N N 243 
HEM   CGD  C  N N 244 
HEM   O1D  O  N N 245 
HEM   O2D  O  N N 246 
HEM   NA   N  Y N 247 
HEM   NB   N  N N 248 
HEM   NC   N  Y N 249 
HEM   ND   N  N N 250 
HEM   FE   FE N N 251 
HEM   HHB  H  N N 252 
HEM   HHC  H  N N 253 
HEM   HHD  H  N N 254 
HEM   HMA  H  N N 255 
HEM   HMAA H  N N 256 
HEM   HMAB H  N N 257 
HEM   HAA  H  N N 258 
HEM   HAAA H  N N 259 
HEM   HBA  H  N N 260 
HEM   HBAA H  N N 261 
HEM   HMB  H  N N 262 
HEM   HMBA H  N N 263 
HEM   HMBB H  N N 264 
HEM   HAB  H  N N 265 
HEM   HBB  H  N N 266 
HEM   HBBA H  N N 267 
HEM   HMC  H  N N 268 
HEM   HMCA H  N N 269 
HEM   HMCB H  N N 270 
HEM   HAC  H  N N 271 
HEM   HBC  H  N N 272 
HEM   HBCA H  N N 273 
HEM   HMD  H  N N 274 
HEM   HMDA H  N N 275 
HEM   HMDB H  N N 276 
HEM   HAD  H  N N 277 
HEM   HADA H  N N 278 
HEM   HBD  H  N N 279 
HEM   HBDA H  N N 280 
HEM   H2A  H  N N 281 
HEM   H2D  H  N N 282 
HEM   HHA  H  N N 283 
HIS   N    N  N N 284 
HIS   CA   C  N S 285 
HIS   C    C  N N 286 
HIS   O    O  N N 287 
HIS   CB   C  N N 288 
HIS   CG   C  Y N 289 
HIS   ND1  N  Y N 290 
HIS   CD2  C  Y N 291 
HIS   CE1  C  Y N 292 
HIS   NE2  N  Y N 293 
HIS   OXT  O  N N 294 
HIS   H    H  N N 295 
HIS   H2   H  N N 296 
HIS   HA   H  N N 297 
HIS   HB2  H  N N 298 
HIS   HB3  H  N N 299 
HIS   HD1  H  N N 300 
HIS   HD2  H  N N 301 
HIS   HE1  H  N N 302 
HIS   HE2  H  N N 303 
HIS   HXT  H  N N 304 
HOH   O    O  N N 305 
HOH   H1   H  N N 306 
HOH   H2   H  N N 307 
ILE   N    N  N N 308 
ILE   CA   C  N S 309 
ILE   C    C  N N 310 
ILE   O    O  N N 311 
ILE   CB   C  N S 312 
ILE   CG1  C  N N 313 
ILE   CG2  C  N N 314 
ILE   CD1  C  N N 315 
ILE   OXT  O  N N 316 
ILE   H    H  N N 317 
ILE   H2   H  N N 318 
ILE   HA   H  N N 319 
ILE   HB   H  N N 320 
ILE   HG12 H  N N 321 
ILE   HG13 H  N N 322 
ILE   HG21 H  N N 323 
ILE   HG22 H  N N 324 
ILE   HG23 H  N N 325 
ILE   HD11 H  N N 326 
ILE   HD12 H  N N 327 
ILE   HD13 H  N N 328 
ILE   HXT  H  N N 329 
LEU   N    N  N N 330 
LEU   CA   C  N S 331 
LEU   C    C  N N 332 
LEU   O    O  N N 333 
LEU   CB   C  N N 334 
LEU   CG   C  N N 335 
LEU   CD1  C  N N 336 
LEU   CD2  C  N N 337 
LEU   OXT  O  N N 338 
LEU   H    H  N N 339 
LEU   H2   H  N N 340 
LEU   HA   H  N N 341 
LEU   HB2  H  N N 342 
LEU   HB3  H  N N 343 
LEU   HG   H  N N 344 
LEU   HD11 H  N N 345 
LEU   HD12 H  N N 346 
LEU   HD13 H  N N 347 
LEU   HD21 H  N N 348 
LEU   HD22 H  N N 349 
LEU   HD23 H  N N 350 
LEU   HXT  H  N N 351 
LYS   N    N  N N 352 
LYS   CA   C  N S 353 
LYS   C    C  N N 354 
LYS   O    O  N N 355 
LYS   CB   C  N N 356 
LYS   CG   C  N N 357 
LYS   CD   C  N N 358 
LYS   CE   C  N N 359 
LYS   NZ   N  N N 360 
LYS   OXT  O  N N 361 
LYS   H    H  N N 362 
LYS   H2   H  N N 363 
LYS   HA   H  N N 364 
LYS   HB2  H  N N 365 
LYS   HB3  H  N N 366 
LYS   HG2  H  N N 367 
LYS   HG3  H  N N 368 
LYS   HD2  H  N N 369 
LYS   HD3  H  N N 370 
LYS   HE2  H  N N 371 
LYS   HE3  H  N N 372 
LYS   HZ1  H  N N 373 
LYS   HZ2  H  N N 374 
LYS   HZ3  H  N N 375 
LYS   HXT  H  N N 376 
MET   N    N  N N 377 
MET   CA   C  N S 378 
MET   C    C  N N 379 
MET   O    O  N N 380 
MET   CB   C  N N 381 
MET   CG   C  N N 382 
MET   SD   S  N N 383 
MET   CE   C  N N 384 
MET   OXT  O  N N 385 
MET   H    H  N N 386 
MET   H2   H  N N 387 
MET   HA   H  N N 388 
MET   HB2  H  N N 389 
MET   HB3  H  N N 390 
MET   HG2  H  N N 391 
MET   HG3  H  N N 392 
MET   HE1  H  N N 393 
MET   HE2  H  N N 394 
MET   HE3  H  N N 395 
MET   HXT  H  N N 396 
PHE   N    N  N N 397 
PHE   CA   C  N S 398 
PHE   C    C  N N 399 
PHE   O    O  N N 400 
PHE   CB   C  N N 401 
PHE   CG   C  Y N 402 
PHE   CD1  C  Y N 403 
PHE   CD2  C  Y N 404 
PHE   CE1  C  Y N 405 
PHE   CE2  C  Y N 406 
PHE   CZ   C  Y N 407 
PHE   OXT  O  N N 408 
PHE   H    H  N N 409 
PHE   H2   H  N N 410 
PHE   HA   H  N N 411 
PHE   HB2  H  N N 412 
PHE   HB3  H  N N 413 
PHE   HD1  H  N N 414 
PHE   HD2  H  N N 415 
PHE   HE1  H  N N 416 
PHE   HE2  H  N N 417 
PHE   HZ   H  N N 418 
PHE   HXT  H  N N 419 
PRO   N    N  N N 420 
PRO   CA   C  N S 421 
PRO   C    C  N N 422 
PRO   O    O  N N 423 
PRO   CB   C  N N 424 
PRO   CG   C  N N 425 
PRO   CD   C  N N 426 
PRO   OXT  O  N N 427 
PRO   H    H  N N 428 
PRO   HA   H  N N 429 
PRO   HB2  H  N N 430 
PRO   HB3  H  N N 431 
PRO   HG2  H  N N 432 
PRO   HG3  H  N N 433 
PRO   HD2  H  N N 434 
PRO   HD3  H  N N 435 
PRO   HXT  H  N N 436 
SER   N    N  N N 437 
SER   CA   C  N S 438 
SER   C    C  N N 439 
SER   O    O  N N 440 
SER   CB   C  N N 441 
SER   OG   O  N N 442 
SER   OXT  O  N N 443 
SER   H    H  N N 444 
SER   H2   H  N N 445 
SER   HA   H  N N 446 
SER   HB2  H  N N 447 
SER   HB3  H  N N 448 
SER   HG   H  N N 449 
SER   HXT  H  N N 450 
THR   N    N  N N 451 
THR   CA   C  N S 452 
THR   C    C  N N 453 
THR   O    O  N N 454 
THR   CB   C  N R 455 
THR   OG1  O  N N 456 
THR   CG2  C  N N 457 
THR   OXT  O  N N 458 
THR   H    H  N N 459 
THR   H2   H  N N 460 
THR   HA   H  N N 461 
THR   HB   H  N N 462 
THR   HG1  H  N N 463 
THR   HG21 H  N N 464 
THR   HG22 H  N N 465 
THR   HG23 H  N N 466 
THR   HXT  H  N N 467 
TRP   N    N  N N 468 
TRP   CA   C  N S 469 
TRP   C    C  N N 470 
TRP   O    O  N N 471 
TRP   CB   C  N N 472 
TRP   CG   C  Y N 473 
TRP   CD1  C  Y N 474 
TRP   CD2  C  Y N 475 
TRP   NE1  N  Y N 476 
TRP   CE2  C  Y N 477 
TRP   CE3  C  Y N 478 
TRP   CZ2  C  Y N 479 
TRP   CZ3  C  Y N 480 
TRP   CH2  C  Y N 481 
TRP   OXT  O  N N 482 
TRP   H    H  N N 483 
TRP   H2   H  N N 484 
TRP   HA   H  N N 485 
TRP   HB2  H  N N 486 
TRP   HB3  H  N N 487 
TRP   HD1  H  N N 488 
TRP   HE1  H  N N 489 
TRP   HE3  H  N N 490 
TRP   HZ2  H  N N 491 
TRP   HZ3  H  N N 492 
TRP   HH2  H  N N 493 
TRP   HXT  H  N N 494 
TYR   N    N  N N 495 
TYR   CA   C  N S 496 
TYR   C    C  N N 497 
TYR   O    O  N N 498 
TYR   CB   C  N N 499 
TYR   CG   C  Y N 500 
TYR   CD1  C  Y N 501 
TYR   CD2  C  Y N 502 
TYR   CE1  C  Y N 503 
TYR   CE2  C  Y N 504 
TYR   CZ   C  Y N 505 
TYR   OH   O  N N 506 
TYR   OXT  O  N N 507 
TYR   H    H  N N 508 
TYR   H2   H  N N 509 
TYR   HA   H  N N 510 
TYR   HB2  H  N N 511 
TYR   HB3  H  N N 512 
TYR   HD1  H  N N 513 
TYR   HD2  H  N N 514 
TYR   HE1  H  N N 515 
TYR   HE2  H  N N 516 
TYR   HH   H  N N 517 
TYR   HXT  H  N N 518 
VAL   N    N  N N 519 
VAL   CA   C  N S 520 
VAL   C    C  N N 521 
VAL   O    O  N N 522 
VAL   CB   C  N N 523 
VAL   CG1  C  N N 524 
VAL   CG2  C  N N 525 
VAL   OXT  O  N N 526 
VAL   H    H  N N 527 
VAL   H2   H  N N 528 
VAL   HA   H  N N 529 
VAL   HB   H  N N 530 
VAL   HG11 H  N N 531 
VAL   HG12 H  N N 532 
VAL   HG13 H  N N 533 
VAL   HG21 H  N N 534 
VAL   HG22 H  N N 535 
VAL   HG23 H  N N 536 
VAL   HXT  H  N N 537 
ZN    ZN   ZN N N 538 
# 
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 
A1A0E C07 C04  sing N N 1   
A1A0E C04 C05  doub Y N 2   
A1A0E C04 C03  sing Y N 3   
A1A0E C05 C06  sing Y N 4   
A1A0E C03 C02  doub Y N 5   
A1A0E C06 N01  doub Y N 6   
A1A0E C06 C13  sing N N 7   
A1A0E C02 N01  sing Y N 8   
A1A0E C02 N02  sing N N 9   
A1A0E C13 C12  doub Y N 10  
A1A0E C13 C14  sing Y N 11  
A1A0E C12 N11  sing Y N 12  
A1A0E C14 C16  doub Y N 13  
A1A0E N11 C15  doub Y N 14  
A1A0E C16 C15  sing Y N 15  
A1A0E C16 C17  sing N N 16  
A1A0E C17 N18  sing N N 17  
A1A0E N18 C19  sing N N 18  
A1A0E C03 H1   sing N N 19  
A1A0E C05 H2   sing N N 20  
A1A0E C07 H3   sing N N 21  
A1A0E C07 H4   sing N N 22  
A1A0E C07 H5   sing N N 23  
A1A0E C12 H6   sing N N 24  
A1A0E C14 H7   sing N N 25  
A1A0E C15 H8   sing N N 26  
A1A0E C17 H9   sing N N 27  
A1A0E C17 H10  sing N N 28  
A1A0E C19 H11  sing N N 29  
A1A0E C19 H12  sing N N 30  
A1A0E C19 H13  sing N N 31  
A1A0E N02 H14  sing N N 32  
A1A0E N02 H15  sing N N 33  
A1A0E N18 H16  sing N N 34  
ACT   C   O    doub N N 35  
ACT   C   OXT  sing N N 36  
ACT   C   CH3  sing N N 37  
ACT   CH3 H1   sing N N 38  
ACT   CH3 H2   sing N N 39  
ACT   CH3 H3   sing N N 40  
ALA   N   CA   sing N N 41  
ALA   N   H    sing N N 42  
ALA   N   H2   sing N N 43  
ALA   CA  C    sing N N 44  
ALA   CA  CB   sing N N 45  
ALA   CA  HA   sing N N 46  
ALA   C   O    doub N N 47  
ALA   C   OXT  sing N N 48  
ALA   CB  HB1  sing N N 49  
ALA   CB  HB2  sing N N 50  
ALA   CB  HB3  sing N N 51  
ALA   OXT HXT  sing N N 52  
ARG   N   CA   sing N N 53  
ARG   N   H    sing N N 54  
ARG   N   H2   sing N N 55  
ARG   CA  C    sing N N 56  
ARG   CA  CB   sing N N 57  
ARG   CA  HA   sing N N 58  
ARG   C   O    doub N N 59  
ARG   C   OXT  sing N N 60  
ARG   CB  CG   sing N N 61  
ARG   CB  HB2  sing N N 62  
ARG   CB  HB3  sing N N 63  
ARG   CG  CD   sing N N 64  
ARG   CG  HG2  sing N N 65  
ARG   CG  HG3  sing N N 66  
ARG   CD  NE   sing N N 67  
ARG   CD  HD2  sing N N 68  
ARG   CD  HD3  sing N N 69  
ARG   NE  CZ   sing N N 70  
ARG   NE  HE   sing N N 71  
ARG   CZ  NH1  sing N N 72  
ARG   CZ  NH2  doub N N 73  
ARG   NH1 HH11 sing N N 74  
ARG   NH1 HH12 sing N N 75  
ARG   NH2 HH21 sing N N 76  
ARG   NH2 HH22 sing N N 77  
ARG   OXT HXT  sing N N 78  
ASN   N   CA   sing N N 79  
ASN   N   H    sing N N 80  
ASN   N   H2   sing N N 81  
ASN   CA  C    sing N N 82  
ASN   CA  CB   sing N N 83  
ASN   CA  HA   sing N N 84  
ASN   C   O    doub N N 85  
ASN   C   OXT  sing N N 86  
ASN   CB  CG   sing N N 87  
ASN   CB  HB2  sing N N 88  
ASN   CB  HB3  sing N N 89  
ASN   CG  OD1  doub N N 90  
ASN   CG  ND2  sing N N 91  
ASN   ND2 HD21 sing N N 92  
ASN   ND2 HD22 sing N N 93  
ASN   OXT HXT  sing N N 94  
ASP   N   CA   sing N N 95  
ASP   N   H    sing N N 96  
ASP   N   H2   sing N N 97  
ASP   CA  C    sing N N 98  
ASP   CA  CB   sing N N 99  
ASP   CA  HA   sing N N 100 
ASP   C   O    doub N N 101 
ASP   C   OXT  sing N N 102 
ASP   CB  CG   sing N N 103 
ASP   CB  HB2  sing N N 104 
ASP   CB  HB3  sing N N 105 
ASP   CG  OD1  doub N N 106 
ASP   CG  OD2  sing N N 107 
ASP   OD2 HD2  sing N N 108 
ASP   OXT HXT  sing N N 109 
CYS   N   CA   sing N N 110 
CYS   N   H    sing N N 111 
CYS   N   H2   sing N N 112 
CYS   CA  C    sing N N 113 
CYS   CA  CB   sing N N 114 
CYS   CA  HA   sing N N 115 
CYS   C   O    doub N N 116 
CYS   C   OXT  sing N N 117 
CYS   CB  SG   sing N N 118 
CYS   CB  HB2  sing N N 119 
CYS   CB  HB3  sing N N 120 
CYS   SG  HG   sing N N 121 
CYS   OXT HXT  sing N N 122 
GLN   N   CA   sing N N 123 
GLN   N   H    sing N N 124 
GLN   N   H2   sing N N 125 
GLN   CA  C    sing N N 126 
GLN   CA  CB   sing N N 127 
GLN   CA  HA   sing N N 128 
GLN   C   O    doub N N 129 
GLN   C   OXT  sing N N 130 
GLN   CB  CG   sing N N 131 
GLN   CB  HB2  sing N N 132 
GLN   CB  HB3  sing N N 133 
GLN   CG  CD   sing N N 134 
GLN   CG  HG2  sing N N 135 
GLN   CG  HG3  sing N N 136 
GLN   CD  OE1  doub N N 137 
GLN   CD  NE2  sing N N 138 
GLN   NE2 HE21 sing N N 139 
GLN   NE2 HE22 sing N N 140 
GLN   OXT HXT  sing N N 141 
GLU   N   CA   sing N N 142 
GLU   N   H    sing N N 143 
GLU   N   H2   sing N N 144 
GLU   CA  C    sing N N 145 
GLU   CA  CB   sing N N 146 
GLU   CA  HA   sing N N 147 
GLU   C   O    doub N N 148 
GLU   C   OXT  sing N N 149 
GLU   CB  CG   sing N N 150 
GLU   CB  HB2  sing N N 151 
GLU   CB  HB3  sing N N 152 
GLU   CG  CD   sing N N 153 
GLU   CG  HG2  sing N N 154 
GLU   CG  HG3  sing N N 155 
GLU   CD  OE1  doub N N 156 
GLU   CD  OE2  sing N N 157 
GLU   OE2 HE2  sing N N 158 
GLU   OXT HXT  sing N N 159 
GLY   N   CA   sing N N 160 
GLY   N   H    sing N N 161 
GLY   N   H2   sing N N 162 
GLY   CA  C    sing N N 163 
GLY   CA  HA2  sing N N 164 
GLY   CA  HA3  sing N N 165 
GLY   C   O    doub N N 166 
GLY   C   OXT  sing N N 167 
GLY   OXT HXT  sing N N 168 
H4B   N1  C2   doub Y N 169 
H4B   N1  C8A  sing Y N 170 
H4B   C2  N2   sing N N 171 
H4B   C2  N3   sing Y N 172 
H4B   N2  HN21 sing N N 173 
H4B   N2  HN22 sing N N 174 
H4B   N3  C4   sing Y N 175 
H4B   N3  HN3  sing N N 176 
H4B   C4  O4   doub N N 177 
H4B   C4  C4A  sing Y N 178 
H4B   C4A C8A  doub Y N 179 
H4B   C4A N5   sing N N 180 
H4B   C8A N8   sing N N 181 
H4B   N5  C6   sing N N 182 
H4B   N5  HN5  sing N N 183 
H4B   N8  C7   sing N N 184 
H4B   N8  HN8  sing N N 185 
H4B   C6  C7   sing N N 186 
H4B   C6  C9   sing N N 187 
H4B   C6  H6   sing N N 188 
H4B   C7  H71  sing N N 189 
H4B   C7  H72  sing N N 190 
H4B   C9  O9   sing N N 191 
H4B   C9  C10  sing N N 192 
H4B   C9  H9   sing N N 193 
H4B   O9  HO9  sing N N 194 
H4B   C10 C11  sing N N 195 
H4B   C10 O10  sing N N 196 
H4B   C10 H10  sing N N 197 
H4B   C11 H111 sing N N 198 
H4B   C11 H112 sing N N 199 
H4B   C11 H113 sing N N 200 
H4B   O10 HO0  sing N N 201 
HEM   CHA C1A  sing N N 202 
HEM   CHA C4D  doub N N 203 
HEM   CHA HHA  sing N N 204 
HEM   CHB C4A  sing N N 205 
HEM   CHB C1B  doub N N 206 
HEM   CHB HHB  sing N N 207 
HEM   CHC C4B  sing N N 208 
HEM   CHC C1C  doub N N 209 
HEM   CHC HHC  sing N N 210 
HEM   CHD C4C  doub N N 211 
HEM   CHD C1D  sing N N 212 
HEM   CHD HHD  sing N N 213 
HEM   C1A C2A  doub Y N 214 
HEM   C1A NA   sing Y N 215 
HEM   C2A C3A  sing Y N 216 
HEM   C2A CAA  sing N N 217 
HEM   C3A C4A  doub Y N 218 
HEM   C3A CMA  sing N N 219 
HEM   C4A NA   sing Y N 220 
HEM   CMA HMA  sing N N 221 
HEM   CMA HMAA sing N N 222 
HEM   CMA HMAB sing N N 223 
HEM   CAA CBA  sing N N 224 
HEM   CAA HAA  sing N N 225 
HEM   CAA HAAA sing N N 226 
HEM   CBA CGA  sing N N 227 
HEM   CBA HBA  sing N N 228 
HEM   CBA HBAA sing N N 229 
HEM   CGA O1A  doub N N 230 
HEM   CGA O2A  sing N N 231 
HEM   C1B C2B  sing N N 232 
HEM   C1B NB   sing N N 233 
HEM   C2B C3B  doub N N 234 
HEM   C2B CMB  sing N N 235 
HEM   C3B C4B  sing N N 236 
HEM   C3B CAB  sing N N 237 
HEM   C4B NB   doub N N 238 
HEM   CMB HMB  sing N N 239 
HEM   CMB HMBA sing N N 240 
HEM   CMB HMBB sing N N 241 
HEM   CAB CBB  doub N N 242 
HEM   CAB HAB  sing N N 243 
HEM   CBB HBB  sing N N 244 
HEM   CBB HBBA sing N N 245 
HEM   C1C C2C  sing Y N 246 
HEM   C1C NC   sing Y N 247 
HEM   C2C C3C  doub Y N 248 
HEM   C2C CMC  sing N N 249 
HEM   C3C C4C  sing Y N 250 
HEM   C3C CAC  sing N N 251 
HEM   C4C NC   sing Y N 252 
HEM   CMC HMC  sing N N 253 
HEM   CMC HMCA sing N N 254 
HEM   CMC HMCB sing N N 255 
HEM   CAC CBC  doub N N 256 
HEM   CAC HAC  sing N N 257 
HEM   CBC HBC  sing N N 258 
HEM   CBC HBCA sing N N 259 
HEM   C1D C2D  sing N N 260 
HEM   C1D ND   doub N N 261 
HEM   C2D C3D  doub N N 262 
HEM   C2D CMD  sing N N 263 
HEM   C3D C4D  sing N N 264 
HEM   C3D CAD  sing N N 265 
HEM   C4D ND   sing N N 266 
HEM   CMD HMD  sing N N 267 
HEM   CMD HMDA sing N N 268 
HEM   CMD HMDB sing N N 269 
HEM   CAD CBD  sing N N 270 
HEM   CAD HAD  sing N N 271 
HEM   CAD HADA sing N N 272 
HEM   CBD CGD  sing N N 273 
HEM   CBD HBD  sing N N 274 
HEM   CBD HBDA sing N N 275 
HEM   CGD O1D  doub N N 276 
HEM   CGD O2D  sing N N 277 
HEM   O2A H2A  sing N N 278 
HEM   O2D H2D  sing N N 279 
HEM   FE  NA   sing N N 280 
HEM   FE  NB   sing N N 281 
HEM   FE  NC   sing N N 282 
HEM   FE  ND   sing N N 283 
HIS   N   CA   sing N N 284 
HIS   N   H    sing N N 285 
HIS   N   H2   sing N N 286 
HIS   CA  C    sing N N 287 
HIS   CA  CB   sing N N 288 
HIS   CA  HA   sing N N 289 
HIS   C   O    doub N N 290 
HIS   C   OXT  sing N N 291 
HIS   CB  CG   sing N N 292 
HIS   CB  HB2  sing N N 293 
HIS   CB  HB3  sing N N 294 
HIS   CG  ND1  sing Y N 295 
HIS   CG  CD2  doub Y N 296 
HIS   ND1 CE1  doub Y N 297 
HIS   ND1 HD1  sing N N 298 
HIS   CD2 NE2  sing Y N 299 
HIS   CD2 HD2  sing N N 300 
HIS   CE1 NE2  sing Y N 301 
HIS   CE1 HE1  sing N N 302 
HIS   NE2 HE2  sing N N 303 
HIS   OXT HXT  sing N N 304 
HOH   O   H1   sing N N 305 
HOH   O   H2   sing N N 306 
ILE   N   CA   sing N N 307 
ILE   N   H    sing N N 308 
ILE   N   H2   sing N N 309 
ILE   CA  C    sing N N 310 
ILE   CA  CB   sing N N 311 
ILE   CA  HA   sing N N 312 
ILE   C   O    doub N N 313 
ILE   C   OXT  sing N N 314 
ILE   CB  CG1  sing N N 315 
ILE   CB  CG2  sing N N 316 
ILE   CB  HB   sing N N 317 
ILE   CG1 CD1  sing N N 318 
ILE   CG1 HG12 sing N N 319 
ILE   CG1 HG13 sing N N 320 
ILE   CG2 HG21 sing N N 321 
ILE   CG2 HG22 sing N N 322 
ILE   CG2 HG23 sing N N 323 
ILE   CD1 HD11 sing N N 324 
ILE   CD1 HD12 sing N N 325 
ILE   CD1 HD13 sing N N 326 
ILE   OXT HXT  sing N N 327 
LEU   N   CA   sing N N 328 
LEU   N   H    sing N N 329 
LEU   N   H2   sing N N 330 
LEU   CA  C    sing N N 331 
LEU   CA  CB   sing N N 332 
LEU   CA  HA   sing N N 333 
LEU   C   O    doub N N 334 
LEU   C   OXT  sing N N 335 
LEU   CB  CG   sing N N 336 
LEU   CB  HB2  sing N N 337 
LEU   CB  HB3  sing N N 338 
LEU   CG  CD1  sing N N 339 
LEU   CG  CD2  sing N N 340 
LEU   CG  HG   sing N N 341 
LEU   CD1 HD11 sing N N 342 
LEU   CD1 HD12 sing N N 343 
LEU   CD1 HD13 sing N N 344 
LEU   CD2 HD21 sing N N 345 
LEU   CD2 HD22 sing N N 346 
LEU   CD2 HD23 sing N N 347 
LEU   OXT HXT  sing N N 348 
LYS   N   CA   sing N N 349 
LYS   N   H    sing N N 350 
LYS   N   H2   sing N N 351 
LYS   CA  C    sing N N 352 
LYS   CA  CB   sing N N 353 
LYS   CA  HA   sing N N 354 
LYS   C   O    doub N N 355 
LYS   C   OXT  sing N N 356 
LYS   CB  CG   sing N N 357 
LYS   CB  HB2  sing N N 358 
LYS   CB  HB3  sing N N 359 
LYS   CG  CD   sing N N 360 
LYS   CG  HG2  sing N N 361 
LYS   CG  HG3  sing N N 362 
LYS   CD  CE   sing N N 363 
LYS   CD  HD2  sing N N 364 
LYS   CD  HD3  sing N N 365 
LYS   CE  NZ   sing N N 366 
LYS   CE  HE2  sing N N 367 
LYS   CE  HE3  sing N N 368 
LYS   NZ  HZ1  sing N N 369 
LYS   NZ  HZ2  sing N N 370 
LYS   NZ  HZ3  sing N N 371 
LYS   OXT HXT  sing N N 372 
MET   N   CA   sing N N 373 
MET   N   H    sing N N 374 
MET   N   H2   sing N N 375 
MET   CA  C    sing N N 376 
MET   CA  CB   sing N N 377 
MET   CA  HA   sing N N 378 
MET   C   O    doub N N 379 
MET   C   OXT  sing N N 380 
MET   CB  CG   sing N N 381 
MET   CB  HB2  sing N N 382 
MET   CB  HB3  sing N N 383 
MET   CG  SD   sing N N 384 
MET   CG  HG2  sing N N 385 
MET   CG  HG3  sing N N 386 
MET   SD  CE   sing N N 387 
MET   CE  HE1  sing N N 388 
MET   CE  HE2  sing N N 389 
MET   CE  HE3  sing N N 390 
MET   OXT HXT  sing N N 391 
PHE   N   CA   sing N N 392 
PHE   N   H    sing N N 393 
PHE   N   H2   sing N N 394 
PHE   CA  C    sing N N 395 
PHE   CA  CB   sing N N 396 
PHE   CA  HA   sing N N 397 
PHE   C   O    doub N N 398 
PHE   C   OXT  sing N N 399 
PHE   CB  CG   sing N N 400 
PHE   CB  HB2  sing N N 401 
PHE   CB  HB3  sing N N 402 
PHE   CG  CD1  doub Y N 403 
PHE   CG  CD2  sing Y N 404 
PHE   CD1 CE1  sing Y N 405 
PHE   CD1 HD1  sing N N 406 
PHE   CD2 CE2  doub Y N 407 
PHE   CD2 HD2  sing N N 408 
PHE   CE1 CZ   doub Y N 409 
PHE   CE1 HE1  sing N N 410 
PHE   CE2 CZ   sing Y N 411 
PHE   CE2 HE2  sing N N 412 
PHE   CZ  HZ   sing N N 413 
PHE   OXT HXT  sing N N 414 
PRO   N   CA   sing N N 415 
PRO   N   CD   sing N N 416 
PRO   N   H    sing N N 417 
PRO   CA  C    sing N N 418 
PRO   CA  CB   sing N N 419 
PRO   CA  HA   sing N N 420 
PRO   C   O    doub N N 421 
PRO   C   OXT  sing N N 422 
PRO   CB  CG   sing N N 423 
PRO   CB  HB2  sing N N 424 
PRO   CB  HB3  sing N N 425 
PRO   CG  CD   sing N N 426 
PRO   CG  HG2  sing N N 427 
PRO   CG  HG3  sing N N 428 
PRO   CD  HD2  sing N N 429 
PRO   CD  HD3  sing N N 430 
PRO   OXT HXT  sing N N 431 
SER   N   CA   sing N N 432 
SER   N   H    sing N N 433 
SER   N   H2   sing N N 434 
SER   CA  C    sing N N 435 
SER   CA  CB   sing N N 436 
SER   CA  HA   sing N N 437 
SER   C   O    doub N N 438 
SER   C   OXT  sing N N 439 
SER   CB  OG   sing N N 440 
SER   CB  HB2  sing N N 441 
SER   CB  HB3  sing N N 442 
SER   OG  HG   sing N N 443 
SER   OXT HXT  sing N N 444 
THR   N   CA   sing N N 445 
THR   N   H    sing N N 446 
THR   N   H2   sing N N 447 
THR   CA  C    sing N N 448 
THR   CA  CB   sing N N 449 
THR   CA  HA   sing N N 450 
THR   C   O    doub N N 451 
THR   C   OXT  sing N N 452 
THR   CB  OG1  sing N N 453 
THR   CB  CG2  sing N N 454 
THR   CB  HB   sing N N 455 
THR   OG1 HG1  sing N N 456 
THR   CG2 HG21 sing N N 457 
THR   CG2 HG22 sing N N 458 
THR   CG2 HG23 sing N N 459 
THR   OXT HXT  sing N N 460 
TRP   N   CA   sing N N 461 
TRP   N   H    sing N N 462 
TRP   N   H2   sing N N 463 
TRP   CA  C    sing N N 464 
TRP   CA  CB   sing N N 465 
TRP   CA  HA   sing N N 466 
TRP   C   O    doub N N 467 
TRP   C   OXT  sing N N 468 
TRP   CB  CG   sing N N 469 
TRP   CB  HB2  sing N N 470 
TRP   CB  HB3  sing N N 471 
TRP   CG  CD1  doub Y N 472 
TRP   CG  CD2  sing Y N 473 
TRP   CD1 NE1  sing Y N 474 
TRP   CD1 HD1  sing N N 475 
TRP   CD2 CE2  doub Y N 476 
TRP   CD2 CE3  sing Y N 477 
TRP   NE1 CE2  sing Y N 478 
TRP   NE1 HE1  sing N N 479 
TRP   CE2 CZ2  sing Y N 480 
TRP   CE3 CZ3  doub Y N 481 
TRP   CE3 HE3  sing N N 482 
TRP   CZ2 CH2  doub Y N 483 
TRP   CZ2 HZ2  sing N N 484 
TRP   CZ3 CH2  sing Y N 485 
TRP   CZ3 HZ3  sing N N 486 
TRP   CH2 HH2  sing N N 487 
TRP   OXT HXT  sing N N 488 
TYR   N   CA   sing N N 489 
TYR   N   H    sing N N 490 
TYR   N   H2   sing N N 491 
TYR   CA  C    sing N N 492 
TYR   CA  CB   sing N N 493 
TYR   CA  HA   sing N N 494 
TYR   C   O    doub N N 495 
TYR   C   OXT  sing N N 496 
TYR   CB  CG   sing N N 497 
TYR   CB  HB2  sing N N 498 
TYR   CB  HB3  sing N N 499 
TYR   CG  CD1  doub Y N 500 
TYR   CG  CD2  sing Y N 501 
TYR   CD1 CE1  sing Y N 502 
TYR   CD1 HD1  sing N N 503 
TYR   CD2 CE2  doub Y N 504 
TYR   CD2 HD2  sing N N 505 
TYR   CE1 CZ   doub Y N 506 
TYR   CE1 HE1  sing N N 507 
TYR   CE2 CZ   sing Y N 508 
TYR   CE2 HE2  sing N N 509 
TYR   CZ  OH   sing N N 510 
TYR   OH  HH   sing N N 511 
TYR   OXT HXT  sing N N 512 
VAL   N   CA   sing N N 513 
VAL   N   H    sing N N 514 
VAL   N   H2   sing N N 515 
VAL   CA  C    sing N N 516 
VAL   CA  CB   sing N N 517 
VAL   CA  HA   sing N N 518 
VAL   C   O    doub N N 519 
VAL   C   OXT  sing N N 520 
VAL   CB  CG1  sing N N 521 
VAL   CB  CG2  sing N N 522 
VAL   CB  HB   sing N N 523 
VAL   CG1 HG11 sing N N 524 
VAL   CG1 HG12 sing N N 525 
VAL   CG1 HG13 sing N N 526 
VAL   CG2 HG21 sing N N 527 
VAL   CG2 HG22 sing N N 528 
VAL   CG2 HG23 sing N N 529 
VAL   OXT HXT  sing N N 530 
# 
_pdbx_audit_support.funding_organization   
'National Institutes of Health/National Institute of General Medical Sciences (NIH/NIGMS)' 
_pdbx_audit_support.country                'United States' 
_pdbx_audit_support.grant_number           GM131920 
_pdbx_audit_support.ordinal                1 
# 
_pdbx_initial_refinement_model.id               1 
_pdbx_initial_refinement_model.entity_id_list   ? 
_pdbx_initial_refinement_model.type             'experimental model' 
_pdbx_initial_refinement_model.source_name      PDB 
_pdbx_initial_refinement_model.accession_code   7TS9 
_pdbx_initial_refinement_model.details          ? 
# 
_atom_sites.entry_id                    9CVM 
_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]   0.020635 
_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]   0.008849 
_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]   0.006143 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
_atom_sites.solution_primary            ? 
_atom_sites.solution_secondary          ? 
_atom_sites.solution_hydrogens          ? 
_atom_sites.special_details             ? 
# 
loop_
_atom_type.symbol 
C  
FE 
N  
O  
S  
ZN 
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N  N   . ARG   A 1 3   ? -38.018 -24.509 41.668 1.00 146.14 ? 299 ARG   A N   1 
ATOM   2    C  CA  . ARG   A 1 3   ? -37.888 -24.924 40.275 1.00 146.64 ? 299 ARG   A CA  1 
ATOM   3    C  C   . ARG   A 1 3   ? -38.644 -23.981 39.347 1.00 139.10 ? 299 ARG   A C   1 
ATOM   4    O  O   . ARG   A 1 3   ? -38.506 -24.045 38.126 1.00 141.54 ? 299 ARG   A O   1 
ATOM   5    C  CB  . ARG   A 1 3   ? -38.403 -26.350 40.095 1.00 156.93 ? 299 ARG   A CB  1 
ATOM   6    C  CG  . ARG   A 1 3   ? -37.739 -27.123 38.970 1.00 160.45 ? 299 ARG   A CG  1 
ATOM   7    C  CD  . ARG   A 1 3   ? -36.249 -27.288 39.226 1.00 160.22 ? 299 ARG   A CD  1 
ATOM   8    N  NE  . ARG   A 1 3   ? -35.441 -26.398 38.396 1.00 155.75 ? 299 ARG   A NE  1 
ATOM   9    C  CZ  . ARG   A 1 3   ? -34.931 -26.742 37.218 1.00 154.55 ? 299 ARG   A CZ  1 
ATOM   10   N  NH1 . ARG   A 1 3   ? -35.150 -27.956 36.729 1.00 158.12 ? 299 ARG   A NH1 1 
ATOM   11   N  NH2 . ARG   A 1 3   ? -34.205 -25.872 36.525 1.00 149.29 ? 299 ARG   A NH2 1 
ATOM   12   N  N   . PHE   A 1 4   ? -39.459 -23.104 39.949 1.00 129.00 ? 300 PHE   A N   1 
ATOM   13   C  CA  . PHE   A 1 4   ? -40.313 -22.162 39.235 1.00 118.75 ? 300 PHE   A CA  1 
ATOM   14   C  C   . PHE   A 1 4   ? -40.197 -20.827 39.981 1.00 114.31 ? 300 PHE   A C   1 
ATOM   15   O  O   . PHE   A 1 4   ? -41.137 -20.342 40.608 1.00 121.25 ? 300 PHE   A O   1 
ATOM   16   C  CB  . PHE   A 1 4   ? -41.751 -22.679 39.161 1.00 120.19 ? 300 PHE   A CB  1 
ATOM   17   C  CG  . PHE   A 1 4   ? -41.837 -24.174 38.972 1.00 123.60 ? 300 PHE   A CG  1 
ATOM   18   C  CD1 . PHE   A 1 4   ? -42.125 -25.009 40.045 1.00 125.93 ? 300 PHE   A CD1 1 
ATOM   19   C  CD2 . PHE   A 1 4   ? -41.594 -24.746 37.729 1.00 122.43 ? 300 PHE   A CD2 1 
ATOM   20   C  CE1 . PHE   A 1 4   ? -42.194 -26.385 39.879 1.00 127.84 ? 300 PHE   A CE1 1 
ATOM   21   C  CE2 . PHE   A 1 4   ? -41.658 -26.122 37.556 1.00 126.65 ? 300 PHE   A CE2 1 
ATOM   22   C  CZ  . PHE   A 1 4   ? -41.958 -26.942 38.633 1.00 130.41 ? 300 PHE   A CZ  1 
ATOM   23   N  N   . LEU   A 1 5   ? -39.015 -20.219 39.880 1.00 104.00 ? 301 LEU   A N   1 
ATOM   24   C  CA  . LEU   A 1 5   ? -38.482 -19.287 40.867 1.00 93.19  ? 301 LEU   A CA  1 
ATOM   25   C  C   . LEU   A 1 5   ? -39.156 -17.920 40.813 1.00 88.38  ? 301 LEU   A C   1 
ATOM   26   O  O   . LEU   A 1 5   ? -39.678 -17.484 39.785 1.00 83.27  ? 301 LEU   A O   1 
ATOM   27   C  CB  . LEU   A 1 5   ? -36.982 -19.109 40.660 1.00 86.79  ? 301 LEU   A CB  1 
ATOM   28   C  CG  . LEU   A 1 5   ? -36.224 -20.430 40.598 1.00 90.52  ? 301 LEU   A CG  1 
ATOM   29   C  CD1 . LEU   A 1 5   ? -35.037 -20.304 39.667 1.00 90.99  ? 301 LEU   A CD1 1 
ATOM   30   C  CD2 . LEU   A 1 5   ? -35.796 -20.867 41.980 1.00 92.48  ? 301 LEU   A CD2 1 
ATOM   31   N  N   . LYS   A 1 6   ? -39.104 -17.226 41.950 1.00 85.25  ? 302 LYS   A N   1 
ATOM   32   C  CA  . LYS   A 1 6   ? -39.669 -15.894 42.098 1.00 85.58  ? 302 LYS   A CA  1 
ATOM   33   C  C   . LYS   A 1 6   ? -38.555 -14.854 42.137 1.00 77.14  ? 302 LYS   A C   1 
ATOM   34   O  O   . LYS   A 1 6   ? -37.535 -15.046 42.811 1.00 66.63  ? 302 LYS   A O   1 
ATOM   35   C  CB  . LYS   A 1 6   ? -40.513 -15.796 43.376 1.00 96.00  ? 302 LYS   A CB  1 
ATOM   36   C  CG  . LYS   A 1 6   ? -41.484 -16.958 43.599 1.00 107.19 ? 302 LYS   A CG  1 
ATOM   37   C  CD  . LYS   A 1 6   ? -42.705 -16.859 42.691 1.00 112.77 ? 302 LYS   A CD  1 
ATOM   38   C  CE  . LYS   A 1 6   ? -43.626 -18.074 42.829 1.00 116.71 ? 302 LYS   A CE  1 
ATOM   39   N  NZ  . LYS   A 1 6   ? -44.295 -18.162 44.157 1.00 117.08 ? 302 LYS   A NZ  1 
ATOM   40   N  N   . VAL   A 1 7   ? -38.753 -13.756 41.412 1.00 71.61  ? 303 VAL   A N   1 
ATOM   41   C  CA  . VAL   A 1 7   ? -37.900 -12.577 41.496 1.00 70.95  ? 303 VAL   A CA  1 
ATOM   42   C  C   . VAL   A 1 7   ? -38.751 -11.422 42.004 1.00 74.62  ? 303 VAL   A C   1 
ATOM   43   O  O   . VAL   A 1 7   ? -39.883 -11.226 41.546 1.00 76.81  ? 303 VAL   A O   1 
ATOM   44   C  CB  . VAL   A 1 7   ? -37.238 -12.241 40.144 1.00 70.25  ? 303 VAL   A CB  1 
ATOM   45   C  CG1 . VAL   A 1 7   ? -36.537 -13.457 39.604 1.00 66.17  ? 303 VAL   A CG1 1 
ATOM   46   C  CG2 . VAL   A 1 7   ? -38.246 -11.733 39.119 1.00 77.73  ? 303 VAL   A CG2 1 
ATOM   47   N  N   . LYS   A 1 8   ? -38.224 -10.678 42.974 1.00 66.45  ? 304 LYS   A N   1 
ATOM   48   C  CA  . LYS   A 1 8   ? -38.975 -9.609  43.617 1.00 72.02  ? 304 LYS   A CA  1 
ATOM   49   C  C   . LYS   A 1 8   ? -38.367 -8.259  43.260 1.00 71.23  ? 304 LYS   A C   1 
ATOM   50   O  O   . LYS   A 1 8   ? -37.163 -8.144  43.024 1.00 73.18  ? 304 LYS   A O   1 
ATOM   51   C  CB  . LYS   A 1 8   ? -39.003 -9.789  45.142 1.00 78.68  ? 304 LYS   A CB  1 
ATOM   52   C  CG  . LYS   A 1 8   ? -39.813 -8.724  45.893 1.00 82.65  ? 304 LYS   A CG  1 
ATOM   53   C  CD  . LYS   A 1 8   ? -39.950 -9.029  47.373 1.00 88.69  ? 304 LYS   A CD  1 
ATOM   54   C  CE  . LYS   A 1 8   ? -40.610 -7.866  48.116 1.00 93.49  ? 304 LYS   A CE  1 
ATOM   55   N  NZ  . LYS   A 1 8   ? -40.842 -8.156  49.556 1.00 99.51  ? 304 LYS   A NZ  1 
ATOM   56   N  N   . ASN   A 1 9   ? -39.218 -7.243  43.188 1.00 70.23  ? 305 ASN   A N   1 
ATOM   57   C  CA  . ASN   A 1 9   ? -38.771 -5.860  43.137 1.00 74.21  ? 305 ASN   A CA  1 
ATOM   58   C  C   . ASN   A 1 9   ? -38.989 -5.274  44.524 1.00 73.06  ? 305 ASN   A C   1 
ATOM   59   O  O   . ASN   A 1 9   ? -40.083 -5.387  45.078 1.00 85.30  ? 305 ASN   A O   1 
ATOM   60   C  CB  . ASN   A 1 9   ? -39.520 -5.057  42.064 1.00 79.64  ? 305 ASN   A CB  1 
ATOM   61   C  CG  . ASN   A 1 9   ? -39.031 -3.613  41.957 1.00 81.03  ? 305 ASN   A CG  1 
ATOM   62   O  OD1 . ASN   A 1 9   ? -38.956 -2.891  42.958 1.00 84.18  ? 305 ASN   A OD1 1 
ATOM   63   N  ND2 . ASN   A 1 9   ? -38.684 -3.189  40.742 1.00 76.04  ? 305 ASN   A ND2 1 
ATOM   64   N  N   . TRP   A 1 10  ? -37.946 -4.683  45.093 1.00 64.79  ? 306 TRP   A N   1 
ATOM   65   C  CA  . TRP   A 1 10  ? -38.005 -4.209  46.475 1.00 72.75  ? 306 TRP   A CA  1 
ATOM   66   C  C   . TRP   A 1 10  ? -38.312 -2.722  46.574 1.00 80.12  ? 306 TRP   A C   1 
ATOM   67   O  O   . TRP   A 1 10  ? -38.229 -2.151  47.667 1.00 90.53  ? 306 TRP   A O   1 
ATOM   68   C  CB  . TRP   A 1 10  ? -36.701 -4.529  47.198 1.00 75.91  ? 306 TRP   A CB  1 
ATOM   69   C  CG  . TRP   A 1 10  ? -36.465 -5.991  47.364 1.00 71.41  ? 306 TRP   A CG  1 
ATOM   70   C  CD1 . TRP   A 1 10  ? -35.810 -6.818  46.497 1.00 68.10  ? 306 TRP   A CD1 1 
ATOM   71   C  CD2 . TRP   A 1 10  ? -36.879 -6.808  48.464 1.00 75.92  ? 306 TRP   A CD2 1 
ATOM   72   N  NE1 . TRP   A 1 10  ? -35.791 -8.101  46.991 1.00 61.23  ? 306 TRP   A NE1 1 
ATOM   73   C  CE2 . TRP   A 1 10  ? -36.439 -8.120  48.198 1.00 73.79  ? 306 TRP   A CE2 1 
ATOM   74   C  CE3 . TRP   A 1 10  ? -37.579 -6.557  49.647 1.00 73.62  ? 306 TRP   A CE3 1 
ATOM   75   C  CZ2 . TRP   A 1 10  ? -36.678 -9.178  49.070 1.00 76.25  ? 306 TRP   A CZ2 1 
ATOM   76   C  CZ3 . TRP   A 1 10  ? -37.815 -7.611  50.517 1.00 83.70  ? 306 TRP   A CZ3 1 
ATOM   77   C  CH2 . TRP   A 1 10  ? -37.367 -8.905  50.223 1.00 84.62  ? 306 TRP   A CH2 1 
ATOM   78   N  N   . GLU   A 1 11  ? -38.649 -2.083  45.458 1.00 83.64  ? 307 GLU   A N   1 
ATOM   79   C  CA  . GLU   A 1 11  ? -39.176 -0.727  45.447 1.00 86.64  ? 307 GLU   A CA  1 
ATOM   80   C  C   . GLU   A 1 11  ? -40.685 -0.704  45.266 1.00 96.13  ? 307 GLU   A C   1 
ATOM   81   O  O   . GLU   A 1 11  ? -41.358 0.149   45.855 1.00 101.60 ? 307 GLU   A O   1 
ATOM   82   C  CB  . GLU   A 1 11  ? -38.512 0.089   44.328 1.00 84.74  ? 307 GLU   A CB  1 
ATOM   83   C  CG  . GLU   A 1 11  ? -38.603 1.607   44.472 1.00 86.19  ? 307 GLU   A CG  1 
ATOM   84   C  CD  . GLU   A 1 11  ? -38.624 2.332   43.117 1.00 98.08  ? 307 GLU   A CD  1 
ATOM   85   O  OE1 . GLU   A 1 11  ? -39.613 3.050   42.847 1.00 102.56 ? 307 GLU   A OE1 1 
ATOM   86   O  OE2 . GLU   A 1 11  ? -37.667 2.185   42.322 1.00 96.61  ? 307 GLU   A OE2 1 
ATOM   87   N  N   . THR   A 1 12  ? -41.228 -1.643  44.482 1.00 95.47  ? 308 THR   A N   1 
ATOM   88   C  CA  . THR   A 1 12  ? -42.660 -1.747  44.243 1.00 95.44  ? 308 THR   A CA  1 
ATOM   89   C  C   . THR   A 1 12  ? -43.315 -2.950  44.911 1.00 93.81  ? 308 THR   A C   1 
ATOM   90   O  O   . THR   A 1 12  ? -44.549 -3.035  44.909 1.00 94.47  ? 308 THR   A O   1 
ATOM   91   C  CB  . THR   A 1 12  ? -42.938 -1.809  42.735 1.00 91.47  ? 308 THR   A CB  1 
ATOM   92   O  OG1 . THR   A 1 12  ? -42.298 -2.966  42.178 1.00 89.35  ? 308 THR   A OG1 1 
ATOM   93   C  CG2 . THR   A 1 12  ? -42.398 -0.568  42.058 1.00 93.23  ? 308 THR   A CG2 1 
ATOM   94   N  N   . ASP   A 1 13  ? -42.535 -3.876  45.471 1.00 96.41  ? 309 ASP   A N   1 
ATOM   95   C  CA  . ASP   A 1 13  ? -43.032 -5.125  46.050 1.00 103.59 ? 309 ASP   A CA  1 
ATOM   96   C  C   . ASP   A 1 13  ? -43.652 -6.046  44.998 1.00 104.96 ? 309 ASP   A C   1 
ATOM   97   O  O   . ASP   A 1 13  ? -44.356 -6.998  45.340 1.00 110.23 ? 309 ASP   A O   1 
ATOM   98   C  CB  . ASP   A 1 13  ? -44.035 -4.866  47.186 1.00 113.78 ? 309 ASP   A CB  1 
ATOM   99   C  CG  . ASP   A 1 13  ? -43.364 -4.384  48.461 1.00 120.21 ? 309 ASP   A CG  1 
ATOM   100  O  OD1 . ASP   A 1 13  ? -42.528 -5.133  49.005 1.00 120.83 ? 309 ASP   A OD1 1 
ATOM   101  O  OD2 . ASP   A 1 13  ? -43.665 -3.256  48.914 1.00 126.05 ? 309 ASP   A OD2 1 
ATOM   102  N  N   . VAL   A 1 14  ? -43.397 -5.797  43.719 1.00 105.65 ? 310 VAL   A N   1 
ATOM   103  C  CA  . VAL   A 1 14  ? -43.918 -6.659  42.665 1.00 101.42 ? 310 VAL   A CA  1 
ATOM   104  C  C   . VAL   A 1 14  ? -43.094 -7.935  42.605 1.00 101.39 ? 310 VAL   A C   1 
ATOM   105  O  O   . VAL   A 1 14  ? -41.862 -7.907  42.718 1.00 101.76 ? 310 VAL   A O   1 
ATOM   106  C  CB  . VAL   A 1 14  ? -43.917 -5.928  41.312 1.00 93.62  ? 310 VAL   A CB  1 
ATOM   107  C  CG1 . VAL   A 1 14  ? -44.338 -6.876  40.200 1.00 92.07  ? 310 VAL   A CG1 1 
ATOM   108  C  CG2 . VAL   A 1 14  ? -44.851 -4.735  41.355 1.00 94.68  ? 310 VAL   A CG2 1 
ATOM   109  N  N   . VAL   A 1 15  ? -43.776 -9.065  42.451 1.00 98.55  ? 311 VAL   A N   1 
ATOM   110  C  CA  . VAL   A 1 15  ? -43.127 -10.355 42.284 1.00 91.98  ? 311 VAL   A CA  1 
ATOM   111  C  C   . VAL   A 1 15  ? -43.521 -10.916 40.927 1.00 94.57  ? 311 VAL   A C   1 
ATOM   112  O  O   . VAL   A 1 15  ? -44.655 -10.730 40.472 1.00 101.65 ? 311 VAL   A O   1 
ATOM   113  C  CB  . VAL   A 1 15  ? -43.497 -11.336 43.414 1.00 87.46  ? 311 VAL   A CB  1 
ATOM   114  C  CG1 . VAL   A 1 15  ? -42.741 -12.651 43.254 1.00 78.85  ? 311 VAL   A CG1 1 
ATOM   115  C  CG2 . VAL   A 1 15  ? -43.194 -10.712 44.762 1.00 84.67  ? 311 VAL   A CG2 1 
ATOM   116  N  N   . LEU   A 1 16  ? -42.574 -11.578 40.273 1.00 85.91  ? 312 LEU   A N   1 
ATOM   117  C  CA  . LEU   A 1 16  ? -42.831 -12.293 39.036 1.00 87.98  ? 312 LEU   A CA  1 
ATOM   118  C  C   . LEU   A 1 16  ? -42.210 -13.677 39.127 1.00 82.96  ? 312 LEU   A C   1 
ATOM   119  O  O   . LEU   A 1 16  ? -41.180 -13.871 39.779 1.00 77.92  ? 312 LEU   A O   1 
ATOM   120  C  CB  . LEU   A 1 16  ? -42.280 -11.532 37.826 1.00 87.48  ? 312 LEU   A CB  1 
ATOM   121  C  CG  . LEU   A 1 16  ? -43.062 -10.253 37.536 1.00 95.90  ? 312 LEU   A CG  1 
ATOM   122  C  CD1 . LEU   A 1 16  ? -42.468 -9.507  36.354 1.00 100.29 ? 312 LEU   A CD1 1 
ATOM   123  C  CD2 . LEU   A 1 16  ? -44.533 -10.588 37.289 1.00 103.20 ? 312 LEU   A CD2 1 
ATOM   124  N  N   . THR   A 1 17  ? -42.853 -14.641 38.473 1.00 81.78  ? 313 THR   A N   1 
ATOM   125  C  CA  . THR   A 1 17  ? -42.412 -16.028 38.493 1.00 79.74  ? 313 THR   A CA  1 
ATOM   126  C  C   . THR   A 1 17  ? -41.689 -16.362 37.199 1.00 82.25  ? 313 THR   A C   1 
ATOM   127  O  O   . THR   A 1 17  ? -42.224 -16.140 36.105 1.00 80.83  ? 313 THR   A O   1 
ATOM   128  C  CB  . THR   A 1 17  ? -43.589 -16.980 38.679 1.00 85.24  ? 313 THR   A CB  1 
ATOM   129  O  OG1 . THR   A 1 17  ? -44.280 -16.649 39.887 1.00 83.34  ? 313 THR   A OG1 1 
ATOM   130  C  CG2 . THR   A 1 17  ? -43.097 -18.421 38.748 1.00 87.81  ? 313 THR   A CG2 1 
ATOM   131  N  N   . ASP   A 1 18  ? -40.486 -16.909 37.326 1.00 78.43  ? 314 ASP   A N   1 
ATOM   132  C  CA  . ASP   A 1 18  ? -39.667 -17.265 36.176 1.00 79.03  ? 314 ASP   A CA  1 
ATOM   133  C  C   . ASP   A 1 18  ? -39.731 -18.770 35.959 1.00 81.15  ? 314 ASP   A C   1 
ATOM   134  O  O   . ASP   A 1 18  ? -39.339 -19.544 36.841 1.00 79.14  ? 314 ASP   A O   1 
ATOM   135  C  CB  . ASP   A 1 18  ? -38.223 -16.814 36.389 1.00 75.24  ? 314 ASP   A CB  1 
ATOM   136  C  CG  . ASP   A 1 18  ? -37.396 -16.909 35.126 1.00 70.89  ? 314 ASP   A CG  1 
ATOM   137  O  OD1 . ASP   A 1 18  ? -37.195 -18.042 34.649 1.00 69.97  ? 314 ASP   A OD1 1 
ATOM   138  O  OD2 . ASP   A 1 18  ? -36.959 -15.862 34.606 1.00 68.37  ? 314 ASP   A OD2 1 
ATOM   139  N  N   . THR   A 1 19  ? -40.260 -19.183 34.806 1.00 77.27  ? 315 THR   A N   1 
ATOM   140  C  CA  . THR   A 1 19  ? -40.114 -20.552 34.335 1.00 80.05  ? 315 THR   A CA  1 
ATOM   141  C  C   . THR   A 1 19  ? -39.254 -20.648 33.089 1.00 79.14  ? 315 THR   A C   1 
ATOM   142  O  O   . THR   A 1 19  ? -38.847 -21.755 32.721 1.00 77.56  ? 315 THR   A O   1 
ATOM   143  C  CB  . THR   A 1 19  ? -41.481 -21.186 34.039 1.00 87.16  ? 315 THR   A CB  1 
ATOM   144  O  OG1 . THR   A 1 19  ? -42.237 -20.320 33.183 1.00 91.09  ? 315 THR   A OG1 1 
ATOM   145  C  CG2 . THR   A 1 19  ? -42.241 -21.434 35.324 1.00 88.99  ? 315 THR   A CG2 1 
ATOM   146  N  N   . LEU   A 1 20  ? -38.966 -19.516 32.442 1.00 72.47  ? 316 LEU   A N   1 
ATOM   147  C  CA  . LEU   A 1 20  ? -38.137 -19.513 31.246 1.00 74.37  ? 316 LEU   A CA  1 
ATOM   148  C  C   . LEU   A 1 20  ? -36.753 -20.092 31.516 1.00 76.58  ? 316 LEU   A C   1 
ATOM   149  O  O   . LEU   A 1 20  ? -36.142 -20.679 30.617 1.00 80.16  ? 316 LEU   A O   1 
ATOM   150  C  CB  . LEU   A 1 20  ? -38.033 -18.084 30.707 1.00 68.97  ? 316 LEU   A CB  1 
ATOM   151  C  CG  . LEU   A 1 20  ? -37.348 -17.897 29.355 1.00 69.37  ? 316 LEU   A CG  1 
ATOM   152  C  CD1 . LEU   A 1 20  ? -38.061 -18.716 28.304 1.00 72.00  ? 316 LEU   A CD1 1 
ATOM   153  C  CD2 . LEU   A 1 20  ? -37.308 -16.419 28.979 1.00 63.23  ? 316 LEU   A CD2 1 
ATOM   154  N  N   . HIS   A 1 21  ? -36.240 -19.942 32.744 1.00 73.43  ? 317 HIS   A N   1 
ATOM   155  C  CA  . HIS   A 1 21  ? -34.923 -20.481 33.066 1.00 65.64  ? 317 HIS   A CA  1 
ATOM   156  C  C   . HIS   A 1 21  ? -34.857 -21.993 32.880 1.00 67.87  ? 317 HIS   A C   1 
ATOM   157  O  O   . HIS   A 1 21  ? -33.756 -22.545 32.776 1.00 62.99  ? 317 HIS   A O   1 
ATOM   158  C  CB  . HIS   A 1 21  ? -34.544 -20.126 34.511 1.00 66.81  ? 317 HIS   A CB  1 
ATOM   159  C  CG  . HIS   A 1 21  ? -35.321 -20.888 35.535 1.00 67.49  ? 317 HIS   A CG  1 
ATOM   160  N  ND1 . HIS   A 1 21  ? -36.590 -20.523 35.933 1.00 71.43  ? 317 HIS   A ND1 1 
ATOM   161  C  CD2 . HIS   A 1 21  ? -35.020 -22.014 36.223 1.00 73.61  ? 317 HIS   A CD2 1 
ATOM   162  C  CE1 . HIS   A 1 21  ? -37.034 -21.389 36.825 1.00 77.65  ? 317 HIS   A CE1 1 
ATOM   163  N  NE2 . HIS   A 1 21  ? -36.101 -22.303 37.018 1.00 76.52  ? 317 HIS   A NE2 1 
ATOM   164  N  N   . LEU   A 1 22  ? -36.011 -22.672 32.854 1.00 72.26  ? 318 LEU   A N   1 
ATOM   165  C  CA  . LEU   A 1 22  ? -36.036 -24.106 32.582 1.00 85.45  ? 318 LEU   A CA  1 
ATOM   166  C  C   . LEU   A 1 22  ? -35.568 -24.413 31.163 1.00 86.62  ? 318 LEU   A C   1 
ATOM   167  O  O   . LEU   A 1 22  ? -34.885 -25.421 30.934 1.00 81.79  ? 318 LEU   A O   1 
ATOM   168  C  CB  . LEU   A 1 22  ? -37.445 -24.660 32.811 1.00 90.87  ? 318 LEU   A CB  1 
ATOM   169  C  CG  . LEU   A 1 22  ? -38.031 -24.460 34.211 1.00 88.97  ? 318 LEU   A CG  1 
ATOM   170  C  CD1 . LEU   A 1 22  ? -39.438 -25.039 34.319 1.00 92.44  ? 318 LEU   A CD1 1 
ATOM   171  C  CD2 . LEU   A 1 22  ? -37.116 -25.068 35.249 1.00 90.89  ? 318 LEU   A CD2 1 
ATOM   172  N  N   . LYS   A 1 23  ? -35.928 -23.564 30.193 1.00 87.71  ? 319 LYS   A N   1 
ATOM   173  C  CA  . LYS   A 1 23  ? -35.436 -23.758 28.834 1.00 87.84  ? 319 LYS   A CA  1 
ATOM   174  C  C   . LYS   A 1 23  ? -33.952 -23.441 28.718 1.00 87.13  ? 319 LYS   A C   1 
ATOM   175  O  O   . LYS   A 1 23  ? -33.357 -23.741 27.681 1.00 92.78  ? 319 LYS   A O   1 
ATOM   176  C  CB  . LYS   A 1 23  ? -36.221 -22.899 27.825 1.00 84.84  ? 319 LYS   A CB  1 
ATOM   177  C  CG  . LYS   A 1 23  ? -37.757 -22.990 27.894 1.00 89.67  ? 319 LYS   A CG  1 
ATOM   178  C  CD  . LYS   A 1 23  ? -38.299 -24.403 27.696 1.00 100.87 ? 319 LYS   A CD  1 
ATOM   179  C  CE  . LYS   A 1 23  ? -38.396 -24.797 26.228 1.00 108.07 ? 319 LYS   A CE  1 
ATOM   180  N  NZ  . LYS   A 1 23  ? -39.496 -24.100 25.495 1.00 111.22 ? 319 LYS   A NZ  1 
ATOM   181  N  N   . SER   A 1 24  ? -33.345 -22.862 29.756 1.00 87.15  ? 320 SER   A N   1 
ATOM   182  C  CA  . SER   A 1 24  ? -31.931 -22.516 29.698 1.00 86.97  ? 320 SER   A CA  1 
ATOM   183  C  C   . SER   A 1 24  ? -31.079 -23.760 29.504 1.00 89.47  ? 320 SER   A C   1 
ATOM   184  O  O   . SER   A 1 24  ? -31.350 -24.820 30.072 1.00 84.23  ? 320 SER   A O   1 
ATOM   185  C  CB  . SER   A 1 24  ? -31.490 -21.790 30.966 1.00 88.73  ? 320 SER   A CB  1 
ATOM   186  O  OG  . SER   A 1 24  ? -30.078 -21.803 31.071 1.00 91.34  ? 320 SER   A OG  1 
ATOM   187  N  N   . THR   A 1 25  ? -30.036 -23.614 28.697 1.00 98.95  ? 321 THR   A N   1 
ATOM   188  C  CA  . THR   A 1 25  ? -29.193 -24.731 28.303 1.00 109.25 ? 321 THR   A CA  1 
ATOM   189  C  C   . THR   A 1 25  ? -27.765 -24.580 28.799 1.00 101.66 ? 321 THR   A C   1 
ATOM   190  O  O   . THR   A 1 25  ? -27.249 -25.481 29.475 1.00 98.81  ? 321 THR   A O   1 
ATOM   191  C  CB  . THR   A 1 25  ? -29.227 -24.878 26.767 1.00 116.23 ? 321 THR   A CB  1 
ATOM   192  O  OG1 . THR   A 1 25  ? -28.056 -25.564 26.310 1.00 118.78 ? 321 THR   A OG1 1 
ATOM   193  C  CG2 . THR   A 1 25  ? -29.328 -23.507 26.088 1.00 113.87 ? 321 THR   A CG2 1 
ATOM   194  N  N   . LEU   A 1 26  ? -27.124 -23.452 28.506 1.00 93.90  ? 322 LEU   A N   1 
ATOM   195  C  CA  . LEU   A 1 26  ? -25.716 -23.261 28.804 1.00 92.46  ? 322 LEU   A CA  1 
ATOM   196  C  C   . LEU   A 1 26  ? -25.493 -23.029 30.299 1.00 91.79  ? 322 LEU   A C   1 
ATOM   197  O  O   . LEU   A 1 26  ? -26.430 -22.854 31.083 1.00 88.32  ? 322 LEU   A O   1 
ATOM   198  C  CB  . LEU   A 1 26  ? -25.163 -22.093 27.995 1.00 88.76  ? 322 LEU   A CB  1 
ATOM   199  C  CG  . LEU   A 1 26  ? -25.295 -22.240 26.480 1.00 88.35  ? 322 LEU   A CG  1 
ATOM   200  C  CD1 . LEU   A 1 26  ? -25.050 -20.909 25.801 1.00 86.27  ? 322 LEU   A CD1 1 
ATOM   201  C  CD2 . LEU   A 1 26  ? -24.320 -23.297 25.978 1.00 88.82  ? 322 LEU   A CD2 1 
ATOM   202  N  N   . GLU   A 1 27  ? -24.219 -23.024 30.682 1.00 91.44  ? 323 GLU   A N   1 
ATOM   203  C  CA  . GLU   A 1 27  ? -23.805 -22.908 32.069 1.00 91.00  ? 323 GLU   A CA  1 
ATOM   204  C  C   . GLU   A 1 27  ? -23.304 -21.494 32.359 1.00 88.31  ? 323 GLU   A C   1 
ATOM   205  O  O   . GLU   A 1 27  ? -22.783 -20.805 31.477 1.00 89.40  ? 323 GLU   A O   1 
ATOM   206  C  CB  . GLU   A 1 27  ? -22.730 -23.951 32.392 1.00 92.98  ? 323 GLU   A CB  1 
ATOM   207  C  CG  . GLU   A 1 27  ? -23.116 -25.356 31.930 1.00 101.14 ? 323 GLU   A CG  1 
ATOM   208  C  CD  . GLU   A 1 27  ? -22.423 -26.466 32.705 1.00 113.01 ? 323 GLU   A CD  1 
ATOM   209  O  OE1 . GLU   A 1 27  ? -21.838 -26.179 33.772 1.00 114.62 ? 323 GLU   A OE1 1 
ATOM   210  O  OE2 . GLU   A 1 27  ? -22.472 -27.631 32.249 1.00 117.60 ? 323 GLU   A OE2 1 
ATOM   211  N  N   . THR   A 1 28  ? -23.480 -21.068 33.614 1.00 82.40  ? 324 THR   A N   1 
ATOM   212  C  CA  . THR   A 1 28  ? -23.297 -19.676 34.010 1.00 79.10  ? 324 THR   A CA  1 
ATOM   213  C  C   . THR   A 1 28  ? -21.907 -19.353 34.544 1.00 75.39  ? 324 THR   A C   1 
ATOM   214  O  O   . THR   A 1 28  ? -21.495 -18.191 34.479 1.00 76.95  ? 324 THR   A O   1 
ATOM   215  C  CB  . THR   A 1 28  ? -24.319 -19.291 35.091 1.00 74.96  ? 324 THR   A CB  1 
ATOM   216  O  OG1 . THR   A 1 28  ? -24.150 -20.142 36.236 1.00 81.04  ? 324 THR   A OG1 1 
ATOM   217  C  CG2 . THR   A 1 28  ? -25.739 -19.426 34.568 1.00 77.82  ? 324 THR   A CG2 1 
ATOM   218  N  N   . GLY   A 1 29  ? -21.173 -20.337 35.059 1.00 72.14  ? 325 GLY   A N   1 
ATOM   219  C  CA  . GLY   A 1 29  ? -19.963 -20.100 35.813 1.00 70.27  ? 325 GLY   A CA  1 
ATOM   220  C  C   . GLY   A 1 29  ? -20.157 -20.258 37.306 1.00 74.03  ? 325 GLY   A C   1 
ATOM   221  O  O   . GLY   A 1 29  ? -19.206 -20.601 38.022 1.00 81.20  ? 325 GLY   A O   1 
ATOM   222  N  N   . CYS   A 1 30  ? -21.373 -20.029 37.785 1.00 70.94  ? 326 CYS   A N   1 
ATOM   223  C  CA  . CYS   A 1 30  ? -21.684 -20.219 39.190 1.00 66.61  ? 326 CYS   A CA  1 
ATOM   224  C  C   . CYS   A 1 30  ? -21.909 -21.692 39.488 1.00 70.47  ? 326 CYS   A C   1 
ATOM   225  O  O   . CYS   A 1 30  ? -22.350 -22.464 38.635 1.00 72.41  ? 326 CYS   A O   1 
ATOM   226  C  CB  . CYS   A 1 30  ? -22.932 -19.430 39.577 1.00 60.42  ? 326 CYS   A CB  1 
ATOM   227  S  SG  . CYS   A 1 30  ? -22.871 -17.676 39.193 1.00 67.70  ? 326 CYS   A SG  1 
ATOM   228  N  N   . THR   A 1 31  ? -21.603 -22.076 40.714 1.00 70.17  ? 327 THR   A N   1 
ATOM   229  C  CA  . THR   A 1 31  ? -21.950 -23.390 41.218 1.00 77.90  ? 327 THR   A CA  1 
ATOM   230  C  C   . THR   A 1 31  ? -22.850 -23.216 42.433 1.00 81.06  ? 327 THR   A C   1 
ATOM   231  O  O   . THR   A 1 31  ? -23.225 -22.098 42.800 1.00 86.10  ? 327 THR   A O   1 
ATOM   232  C  CB  . THR   A 1 31  ? -20.694 -24.192 41.560 1.00 75.28  ? 327 THR   A CB  1 
ATOM   233  O  OG1 . THR   A 1 31  ? -20.031 -23.582 42.675 1.00 77.55  ? 327 THR   A OG1 1 
ATOM   234  C  CG2 . THR   A 1 31  ? -19.758 -24.214 40.369 1.00 61.73  ? 327 THR   A CG2 1 
ATOM   235  N  N   . GLU   A 1 32  ? -23.204 -24.335 43.061 1.00 85.43  ? 328 GLU   A N   1 
ATOM   236  C  CA  . GLU   A 1 32  ? -23.974 -24.253 44.292 1.00 91.33  ? 328 GLU   A CA  1 
ATOM   237  C  C   . GLU   A 1 32  ? -23.192 -23.565 45.403 1.00 84.17  ? 328 GLU   A C   1 
ATOM   238  O  O   . GLU   A 1 32  ? -23.799 -23.048 46.346 1.00 84.54  ? 328 GLU   A O   1 
ATOM   239  C  CB  . GLU   A 1 32  ? -24.418 -25.653 44.734 1.00 104.56 ? 328 GLU   A CB  1 
ATOM   240  C  CG  . GLU   A 1 32  ? -25.638 -26.199 43.983 1.00 114.89 ? 328 GLU   A CG  1 
ATOM   241  C  CD  . GLU   A 1 32  ? -25.279 -26.985 42.727 1.00 124.08 ? 328 GLU   A CD  1 
ATOM   242  O  OE1 . GLU   A 1 32  ? -25.929 -28.022 42.466 1.00 129.85 ? 328 GLU   A OE1 1 
ATOM   243  O  OE2 . GLU   A 1 32  ? -24.349 -26.571 42.004 1.00 125.21 ? 328 GLU   A OE2 1 
ATOM   244  N  N   . HIS   A 1 33  ? -21.863 -23.516 45.297 1.00 79.58  ? 329 HIS   A N   1 
ATOM   245  C  CA  . HIS   A 1 33  ? -21.020 -23.007 46.363 1.00 86.82  ? 329 HIS   A CA  1 
ATOM   246  C  C   . HIS   A 1 33  ? -20.224 -21.767 45.978 1.00 80.18  ? 329 HIS   A C   1 
ATOM   247  O  O   . HIS   A 1 33  ? -19.455 -21.262 46.806 1.00 69.62  ? 329 HIS   A O   1 
ATOM   248  C  CB  . HIS   A 1 33  ? -20.069 -24.114 46.843 1.00 100.83 ? 329 HIS   A CB  1 
ATOM   249  C  CG  . HIS   A 1 33  ? -20.753 -25.425 47.093 1.00 110.80 ? 329 HIS   A CG  1 
ATOM   250  N  ND1 . HIS   A 1 33  ? -20.830 -26.420 46.141 1.00 114.09 ? 329 HIS   A ND1 1 
ATOM   251  C  CD2 . HIS   A 1 33  ? -21.407 -25.896 48.182 1.00 112.83 ? 329 HIS   A CD2 1 
ATOM   252  C  CE1 . HIS   A 1 33  ? -21.494 -27.450 46.635 1.00 117.50 ? 329 HIS   A CE1 1 
ATOM   253  N  NE2 . HIS   A 1 33  ? -21.855 -27.158 47.872 1.00 116.95 ? 329 HIS   A NE2 1 
ATOM   254  N  N   . ILE   A 1 34  ? -20.392 -21.240 44.766 1.00 75.55  ? 330 ILE   A N   1 
ATOM   255  C  CA  . ILE   A 1 34  ? -19.706 -20.013 44.387 1.00 74.58  ? 330 ILE   A CA  1 
ATOM   256  C  C   . ILE   A 1 34  ? -20.541 -19.287 43.344 1.00 68.98  ? 330 ILE   A C   1 
ATOM   257  O  O   . ILE   A 1 34  ? -21.188 -19.903 42.496 1.00 75.67  ? 330 ILE   A O   1 
ATOM   258  C  CB  . ILE   A 1 34  ? -18.271 -20.287 43.881 1.00 79.66  ? 330 ILE   A CB  1 
ATOM   259  C  CG1 . ILE   A 1 34  ? -17.492 -18.977 43.809 1.00 75.98  ? 330 ILE   A CG1 1 
ATOM   260  C  CG2 . ILE   A 1 34  ? -18.290 -20.957 42.516 1.00 91.24  ? 330 ILE   A CG2 1 
ATOM   261  C  CD1 . ILE   A 1 34  ? -16.007 -19.154 43.866 1.00 73.48  ? 330 ILE   A CD1 1 
ATOM   262  N  N   . CYS   A 1 35  ? -20.549 -17.963 43.432 1.00 66.85  ? 331 CYS   A N   1 
ATOM   263  C  CA  . CYS   A 1 35  ? -21.262 -17.129 42.481 1.00 59.11  ? 331 CYS   A CA  1 
ATOM   264  C  C   . CYS   A 1 35  ? -20.247 -16.280 41.737 1.00 65.63  ? 331 CYS   A C   1 
ATOM   265  O  O   . CYS   A 1 35  ? -19.443 -15.576 42.363 1.00 56.24  ? 331 CYS   A O   1 
ATOM   266  C  CB  . CYS   A 1 35  ? -22.300 -16.244 43.174 1.00 59.94  ? 331 CYS   A CB  1 
ATOM   267  S  SG  . CYS   A 1 35  ? -23.068 -15.069 42.053 1.00 53.93  ? 331 CYS   A SG  1 
ATOM   268  N  N   . MET   A 1 36  ? -20.275 -16.371 40.404 1.00 60.87  ? 332 MET   A N   1 
ATOM   269  C  CA  . MET   A 1 36  ? -19.381 -15.624 39.532 1.00 67.89  ? 332 MET   A CA  1 
ATOM   270  C  C   . MET   A 1 36  ? -20.087 -14.473 38.832 1.00 63.58  ? 332 MET   A C   1 
ATOM   271  O  O   . MET   A 1 36  ? -19.601 -13.981 37.800 1.00 62.52  ? 332 MET   A O   1 
ATOM   272  C  CB  . MET   A 1 36  ? -18.756 -16.561 38.506 1.00 81.22  ? 332 MET   A CB  1 
ATOM   273  C  CG  . MET   A 1 36  ? -17.989 -17.690 39.146 1.00 91.96  ? 332 MET   A CG  1 
ATOM   274  S  SD  . MET   A 1 36  ? -16.610 -18.189 38.115 1.00 104.45 ? 332 MET   A SD  1 
ATOM   275  C  CE  . MET   A 1 36  ? -15.460 -18.667 39.388 1.00 106.37 ? 332 MET   A CE  1 
ATOM   276  N  N   . GLY   A 1 37  ? -21.216 -14.018 39.379 1.00 57.70  ? 333 GLY   A N   1 
ATOM   277  C  CA  . GLY   A 1 37  ? -21.999 -12.970 38.737 1.00 54.77  ? 333 GLY   A CA  1 
ATOM   278  C  C   . GLY   A 1 37  ? -21.262 -11.665 38.499 1.00 57.95  ? 333 GLY   A C   1 
ATOM   279  O  O   . GLY   A 1 37  ? -21.807 -10.801 37.806 1.00 58.47  ? 333 GLY   A O   1 
ATOM   280  N  N   . SER   A 1 38  ? -20.071 -11.463 39.068 1.00 47.09  ? 334 SER   A N   1 
ATOM   281  C  CA  . SER   A 1 38  ? -19.321 -10.262 38.714 1.00 53.65  ? 334 SER   A CA  1 
ATOM   282  C  C   . SER   A 1 38  ? -18.052 -10.554 37.928 1.00 51.12  ? 334 SER   A C   1 
ATOM   283  O  O   . SER   A 1 38  ? -17.270 -9.631  37.685 1.00 55.72  ? 334 SER   A O   1 
ATOM   284  C  CB  . SER   A 1 38  ? -18.977 -9.443  39.960 1.00 52.92  ? 334 SER   A CB  1 
ATOM   285  O  OG  . SER   A 1 38  ? -18.157 -10.168 40.862 1.00 55.14  ? 334 SER   A OG  1 
ATOM   286  N  N   . ILE   A 1 39  ? -17.816 -11.809 37.543 1.00 50.21  ? 335 ILE   A N   1 
ATOM   287  C  CA  . ILE   A 1 39  ? -16.726 -12.107 36.626 1.00 55.00  ? 335 ILE   A CA  1 
ATOM   288  C  C   . ILE   A 1 39  ? -17.132 -11.624 35.241 1.00 53.45  ? 335 ILE   A C   1 
ATOM   289  O  O   . ILE   A 1 39  ? -18.248 -11.900 34.783 1.00 59.73  ? 335 ILE   A O   1 
ATOM   290  C  CB  . ILE   A 1 39  ? -16.410 -13.611 36.627 1.00 57.91  ? 335 ILE   A CB  1 
ATOM   291  C  CG1 . ILE   A 1 39  ? -16.098 -14.114 38.051 1.00 59.08  ? 335 ILE   A CG1 1 
ATOM   292  C  CG2 . ILE   A 1 39  ? -15.288 -13.916 35.628 1.00 54.70  ? 335 ILE   A CG2 1 
ATOM   293  C  CD1 . ILE   A 1 39  ? -14.920 -13.444 38.717 1.00 63.15  ? 335 ILE   A CD1 1 
ATOM   294  N  N   . MET   A 1 40  ? -16.231 -10.895 34.569 1.00 56.88  ? 336 MET   A N   1 
ATOM   295  C  CA  . MET   A 1 40  ? -16.609 -10.185 33.340 1.00 66.97  ? 336 MET   A CA  1 
ATOM   296  C  C   . MET   A 1 40  ? -16.860 -11.143 32.175 1.00 73.02  ? 336 MET   A C   1 
ATOM   297  O  O   . MET   A 1 40  ? -17.874 -11.033 31.470 1.00 73.26  ? 336 MET   A O   1 
ATOM   298  C  CB  . MET   A 1 40  ? -15.528 -9.169  32.964 1.00 73.29  ? 336 MET   A CB  1 
ATOM   299  C  CG  . MET   A 1 40  ? -15.807 -8.431  31.667 1.00 82.24  ? 336 MET   A CG  1 
ATOM   300  S  SD  . MET   A 1 40  ? -16.387 -6.740  31.914 1.00 88.10  ? 336 MET   A SD  1 
ATOM   301  C  CE  . MET   A 1 40  ? -14.858 -5.909  32.309 1.00 85.33  ? 336 MET   A CE  1 
ATOM   302  N  N   . LEU   A 1 41  ? -15.933 -12.065 31.928 1.00 77.64  ? 337 LEU   A N   1 
ATOM   303  C  CA  . LEU   A 1 41  ? -16.032 -13.008 30.812 1.00 91.68  ? 337 LEU   A CA  1 
ATOM   304  C  C   . LEU   A 1 41  ? -15.787 -14.419 31.330 1.00 104.65 ? 337 LEU   A C   1 
ATOM   305  O  O   . LEU   A 1 41  ? -14.727 -15.008 31.083 1.00 113.16 ? 337 LEU   A O   1 
ATOM   306  C  CB  . LEU   A 1 41  ? -15.037 -12.660 29.702 1.00 95.32  ? 337 LEU   A CB  1 
ATOM   307  C  CG  . LEU   A 1 41  ? -14.614 -11.202 29.494 1.00 96.80  ? 337 LEU   A CG  1 
ATOM   308  C  CD1 . LEU   A 1 41  ? -13.200 -11.141 28.928 1.00 98.86  ? 337 LEU   A CD1 1 
ATOM   309  C  CD2 . LEU   A 1 41  ? -15.586 -10.459 28.585 1.00 94.69  ? 337 LEU   A CD2 1 
ATOM   310  N  N   . PRO   A 1 42  ? -16.747 -14.996 32.051 1.00 104.67 ? 338 PRO   A N   1 
ATOM   311  C  CA  . PRO   A 1 42  ? -16.557 -16.363 32.547 1.00 108.13 ? 338 PRO   A CA  1 
ATOM   312  C  C   . PRO   A 1 42  ? -16.685 -17.376 31.419 1.00 110.80 ? 338 PRO   A C   1 
ATOM   313  O  O   . PRO   A 1 42  ? -17.357 -17.133 30.412 1.00 110.45 ? 338 PRO   A O   1 
ATOM   314  C  CB  . PRO   A 1 42  ? -17.672 -16.531 33.591 1.00 106.78 ? 338 PRO   A CB  1 
ATOM   315  C  CG  . PRO   A 1 42  ? -18.478 -15.234 33.566 1.00 104.67 ? 338 PRO   A CG  1 
ATOM   316  C  CD  . PRO   A 1 42  ? -18.106 -14.503 32.318 1.00 101.84 ? 338 PRO   A CD  1 
ATOM   317  N  N   . SER   A 1 43  ? -16.022 -18.519 31.613 1.00 109.91 ? 339 SER   A N   1 
ATOM   318  C  CA  . SER   A 1 43  ? -15.881 -19.605 30.630 1.00 109.66 ? 339 SER   A CA  1 
ATOM   319  C  C   . SER   A 1 43  ? -16.886 -19.623 29.480 1.00 110.71 ? 339 SER   A C   1 
ATOM   320  O  O   . SER   A 1 43  ? -16.569 -20.079 28.383 1.00 115.66 ? 339 SER   A O   1 
ATOM   321  C  CB  . SER   A 1 43  ? -15.947 -20.955 31.347 1.00 107.19 ? 339 SER   A CB  1 
ATOM   322  O  OG  . SER   A 1 43  ? -14.742 -21.224 32.043 1.00 109.33 ? 339 SER   A OG  1 
ATOM   323  N  N   . VAL   A 1 52  ? -13.497 -26.370 16.642 1.00 135.86 ? 348 VAL   A N   1 
ATOM   324  C  CA  . VAL   A 1 52  ? -14.378 -26.761 15.546 1.00 134.08 ? 348 VAL   A CA  1 
ATOM   325  C  C   . VAL   A 1 52  ? -15.543 -27.590 16.101 1.00 136.73 ? 348 VAL   A C   1 
ATOM   326  O  O   . VAL   A 1 52  ? -15.367 -28.364 17.044 1.00 143.01 ? 348 VAL   A O   1 
ATOM   327  C  CB  . VAL   A 1 52  ? -13.590 -27.524 14.443 1.00 131.20 ? 348 VAL   A CB  1 
ATOM   328  C  CG1 . VAL   A 1 52  ? -12.941 -28.786 15.001 1.00 133.70 ? 348 VAL   A CG1 1 
ATOM   329  C  CG2 . VAL   A 1 52  ? -14.483 -27.843 13.253 1.00 126.91 ? 348 VAL   A CG2 1 
ATOM   330  N  N   . ALA   A 1 53  ? -16.736 -27.404 15.532 1.00 129.05 ? 349 ALA   A N   1 
ATOM   331  C  CA  . ALA   A 1 53  ? -17.946 -28.073 15.997 1.00 123.16 ? 349 ALA   A CA  1 
ATOM   332  C  C   . ALA   A 1 53  ? -18.293 -29.239 15.080 1.00 124.41 ? 349 ALA   A C   1 
ATOM   333  O  O   . ALA   A 1 53  ? -18.179 -29.129 13.855 1.00 127.26 ? 349 ALA   A O   1 
ATOM   334  C  CB  . ALA   A 1 53  ? -19.120 -27.093 16.061 1.00 116.26 ? 349 ALA   A CB  1 
ATOM   335  N  N   . THR   A 1 54  ? -18.729 -30.354 15.675 1.00 121.96 ? 350 THR   A N   1 
ATOM   336  C  CA  . THR   A 1 54  ? -18.983 -31.582 14.933 1.00 122.36 ? 350 THR   A CA  1 
ATOM   337  C  C   . THR   A 1 54  ? -20.481 -31.776 14.681 1.00 119.55 ? 350 THR   A C   1 
ATOM   338  O  O   . THR   A 1 54  ? -21.336 -31.053 15.201 1.00 112.81 ? 350 THR   A O   1 
ATOM   339  C  CB  . THR   A 1 54  ? -18.394 -32.795 15.665 1.00 124.11 ? 350 THR   A CB  1 
ATOM   340  O  OG1 . THR   A 1 54  ? -19.434 -33.481 16.371 1.00 126.60 ? 350 THR   A OG1 1 
ATOM   341  C  CG2 . THR   A 1 54  ? -17.306 -32.366 16.646 1.00 122.35 ? 350 THR   A CG2 1 
ATOM   342  N  N   . LYS   A 1 55  ? -20.793 -32.798 13.878 1.00 125.28 ? 351 LYS   A N   1 
ATOM   343  C  CA  . LYS   A 1 55  ? -22.127 -33.017 13.326 1.00 127.94 ? 351 LYS   A CA  1 
ATOM   344  C  C   . LYS   A 1 55  ? -23.077 -33.723 14.280 1.00 129.82 ? 351 LYS   A C   1 
ATOM   345  O  O   . LYS   A 1 55  ? -24.293 -33.522 14.185 1.00 125.44 ? 351 LYS   A O   1 
ATOM   346  C  CB  . LYS   A 1 55  ? -22.018 -33.825 12.035 1.00 135.14 ? 351 LYS   A CB  1 
ATOM   347  C  CG  . LYS   A 1 55  ? -20.837 -34.778 12.020 1.00 141.85 ? 351 LYS   A CG  1 
ATOM   348  C  CD  . LYS   A 1 55  ? -20.692 -35.470 10.680 1.00 149.05 ? 351 LYS   A CD  1 
ATOM   349  C  CE  . LYS   A 1 55  ? -19.504 -36.420 10.684 1.00 155.91 ? 351 LYS   A CE  1 
ATOM   350  N  NZ  . LYS   A 1 55  ? -19.429 -37.235 9.437  1.00 159.50 ? 351 LYS   A NZ  1 
ATOM   351  N  N   . ASP   A 1 56  ? -22.558 -34.561 15.180 1.00 136.06 ? 352 ASP   A N   1 
ATOM   352  C  CA  . ASP   A 1 56  ? -23.402 -35.142 16.219 1.00 140.36 ? 352 ASP   A CA  1 
ATOM   353  C  C   . ASP   A 1 56  ? -24.008 -34.046 17.081 1.00 127.56 ? 352 ASP   A C   1 
ATOM   354  O  O   . ASP   A 1 56  ? -25.226 -33.997 17.290 1.00 129.16 ? 352 ASP   A O   1 
ATOM   355  C  CB  . ASP   A 1 56  ? -22.589 -36.107 17.081 1.00 152.61 ? 352 ASP   A CB  1 
ATOM   356  C  CG  . ASP   A 1 56  ? -21.428 -36.723 16.328 1.00 163.76 ? 352 ASP   A CG  1 
ATOM   357  O  OD1 . ASP   A 1 56  ? -21.607 -37.800 15.721 1.00 170.28 ? 352 ASP   A OD1 1 
ATOM   358  O  OD2 . ASP   A 1 56  ? -20.335 -36.117 16.331 1.00 164.83 ? 352 ASP   A OD2 1 
ATOM   359  N  N   . GLN   A 1 57  ? -23.161 -33.142 17.576 1.00 113.63 ? 353 GLN   A N   1 
ATOM   360  C  CA  . GLN   A 1 57  ? -23.611 -32.049 18.426 1.00 107.74 ? 353 GLN   A CA  1 
ATOM   361  C  C   . GLN   A 1 57  ? -24.534 -31.082 17.699 1.00 100.82 ? 353 GLN   A C   1 
ATOM   362  O  O   . GLN   A 1 57  ? -25.231 -30.298 18.355 1.00 94.12  ? 353 GLN   A O   1 
ATOM   363  C  CB  . GLN   A 1 57  ? -22.401 -31.285 18.962 1.00 106.30 ? 353 GLN   A CB  1 
ATOM   364  C  CG  . GLN   A 1 57  ? -21.067 -31.913 18.588 1.00 113.29 ? 353 GLN   A CG  1 
ATOM   365  C  CD  . GLN   A 1 57  ? -19.919 -30.926 18.659 1.00 113.25 ? 353 GLN   A CD  1 
ATOM   366  O  OE1 . GLN   A 1 57  ? -19.996 -29.826 18.112 1.00 108.35 ? 353 GLN   A OE1 1 
ATOM   367  N  NE2 . GLN   A 1 57  ? -18.847 -31.312 19.343 1.00 117.36 ? 353 GLN   A NE2 1 
ATOM   368  N  N   . LEU   A 1 58  ? -24.565 -31.128 16.363 1.00 100.90 ? 354 LEU   A N   1 
ATOM   369  C  CA  . LEU   A 1 58  ? -25.179 -30.055 15.595 1.00 94.43  ? 354 LEU   A CA  1 
ATOM   370  C  C   . LEU   A 1 58  ? -26.677 -30.245 15.390 1.00 95.97  ? 354 LEU   A C   1 
ATOM   371  O  O   . LEU   A 1 58  ? -27.399 -29.250 15.261 1.00 94.86  ? 354 LEU   A O   1 
ATOM   372  C  CB  . LEU   A 1 58  ? -24.478 -29.924 14.245 1.00 98.20  ? 354 LEU   A CB  1 
ATOM   373  C  CG  . LEU   A 1 58  ? -24.321 -28.509 13.690 1.00 94.91  ? 354 LEU   A CG  1 
ATOM   374  C  CD1 . LEU   A 1 58  ? -23.483 -27.640 14.635 1.00 88.02  ? 354 LEU   A CD1 1 
ATOM   375  C  CD2 . LEU   A 1 58  ? -23.709 -28.561 12.296 1.00 99.61  ? 354 LEU   A CD2 1 
ATOM   376  N  N   . PHE   A 1 59  ? -27.177 -31.489 15.349 1.00 99.33  ? 355 PHE   A N   1 
ATOM   377  C  CA  . PHE   A 1 59  ? -28.612 -31.616 15.102 1.00 107.17 ? 355 PHE   A CA  1 
ATOM   378  C  C   . PHE   A 1 59  ? -29.492 -31.270 16.303 1.00 112.01 ? 355 PHE   A C   1 
ATOM   379  O  O   . PHE   A 1 59  ? -30.541 -30.646 16.105 1.00 115.22 ? 355 PHE   A O   1 
ATOM   380  C  CB  . PHE   A 1 59  ? -29.007 -33.007 14.614 1.00 121.42 ? 355 PHE   A CB  1 
ATOM   381  C  CG  . PHE   A 1 59  ? -30.448 -33.080 14.186 1.00 130.89 ? 355 PHE   A CG  1 
ATOM   382  C  CD1 . PHE   A 1 59  ? -30.864 -32.445 13.026 1.00 133.71 ? 355 PHE   A CD1 1 
ATOM   383  C  CD2 . PHE   A 1 59  ? -31.394 -33.728 14.964 1.00 135.69 ? 355 PHE   A CD2 1 
ATOM   384  C  CE1 . PHE   A 1 59  ? -32.189 -32.478 12.634 1.00 135.18 ? 355 PHE   A CE1 1 
ATOM   385  C  CE2 . PHE   A 1 59  ? -32.724 -33.768 14.572 1.00 139.48 ? 355 PHE   A CE2 1 
ATOM   386  C  CZ  . PHE   A 1 59  ? -33.119 -33.142 13.403 1.00 139.03 ? 355 PHE   A CZ  1 
ATOM   387  N  N   . PRO   A 1 60  ? -29.159 -31.673 17.542 1.00 111.05 ? 356 PRO   A N   1 
ATOM   388  C  CA  . PRO   A 1 60  ? -29.971 -31.197 18.677 1.00 106.14 ? 356 PRO   A CA  1 
ATOM   389  C  C   . PRO   A 1 60  ? -30.110 -29.689 18.700 1.00 93.48  ? 356 PRO   A C   1 
ATOM   390  O  O   . PRO   A 1 60  ? -31.215 -29.172 18.901 1.00 91.87  ? 356 PRO   A O   1 
ATOM   391  C  CB  . PRO   A 1 60  ? -29.211 -31.720 19.908 1.00 110.46 ? 356 PRO   A CB  1 
ATOM   392  C  CG  . PRO   A 1 60  ? -27.853 -32.092 19.403 1.00 112.62 ? 356 PRO   A CG  1 
ATOM   393  C  CD  . PRO   A 1 60  ? -28.085 -32.567 18.006 1.00 112.29 ? 356 PRO   A CD  1 
ATOM   394  N  N   . LEU   A 1 61  ? -29.009 -28.973 18.460 1.00 89.11  ? 357 LEU   A N   1 
ATOM   395  C  CA  . LEU   A 1 61  ? -29.041 -27.515 18.417 1.00 77.90  ? 357 LEU   A CA  1 
ATOM   396  C  C   . LEU   A 1 61  ? -29.924 -27.009 17.283 1.00 85.21  ? 357 LEU   A C   1 
ATOM   397  O  O   . LEU   A 1 61  ? -30.670 -26.035 17.453 1.00 85.20  ? 357 LEU   A O   1 
ATOM   398  C  CB  . LEU   A 1 61  ? -27.621 -26.985 18.258 1.00 78.59  ? 357 LEU   A CB  1 
ATOM   399  C  CG  . LEU   A 1 61  ? -26.616 -27.569 19.248 1.00 90.04  ? 357 LEU   A CG  1 
ATOM   400  C  CD1 . LEU   A 1 61  ? -25.193 -27.180 18.887 1.00 93.89  ? 357 LEU   A CD1 1 
ATOM   401  C  CD2 . LEU   A 1 61  ? -26.957 -27.109 20.648 1.00 92.67  ? 357 LEU   A CD2 1 
ATOM   402  N  N   . ALA   A 1 62  ? -29.834 -27.641 16.109 1.00 79.87  ? 358 ALA   A N   1 
ATOM   403  C  CA  . ALA   A 1 62  ? -30.716 -27.280 15.005 1.00 80.57  ? 358 ALA   A CA  1 
ATOM   404  C  C   . ALA   A 1 62  ? -32.166 -27.580 15.358 1.00 85.38  ? 358 ALA   A C   1 
ATOM   405  O  O   . ALA   A 1 62  ? -33.057 -26.745 15.148 1.00 85.93  ? 358 ALA   A O   1 
ATOM   406  C  CB  . ALA   A 1 62  ? -30.309 -28.029 13.734 1.00 80.05  ? 358 ALA   A CB  1 
ATOM   407  N  N   . LYS   A 1 63  ? -32.415 -28.779 15.901 1.00 81.03  ? 359 LYS   A N   1 
ATOM   408  C  CA  . LYS   A 1 63  ? -33.771 -29.199 16.242 1.00 86.22  ? 359 LYS   A CA  1 
ATOM   409  C  C   . LYS   A 1 63  ? -34.364 -28.307 17.322 1.00 90.74  ? 359 LYS   A C   1 
ATOM   410  O  O   . LYS   A 1 63  ? -35.485 -27.804 17.182 1.00 96.54  ? 359 LYS   A O   1 
ATOM   411  C  CB  . LYS   A 1 63  ? -33.770 -30.659 16.702 1.00 90.14  ? 359 LYS   A CB  1 
ATOM   412  C  CG  . LYS   A 1 63  ? -35.069 -31.067 17.370 1.00 89.06  ? 359 LYS   A CG  1 
ATOM   413  C  CD  . LYS   A 1 63  ? -35.051 -32.498 17.870 1.00 95.25  ? 359 LYS   A CD  1 
ATOM   414  C  CE  . LYS   A 1 63  ? -36.279 -33.244 17.370 1.00 102.33 ? 359 LYS   A CE  1 
ATOM   415  N  NZ  . LYS   A 1 63  ? -37.488 -32.367 17.379 1.00 100.38 ? 359 LYS   A NZ  1 
ATOM   416  N  N   . GLU   A 1 64  ? -33.622 -28.108 18.413 1.00 81.36  ? 360 GLU   A N   1 
ATOM   417  C  CA  . GLU   A 1 64  ? -34.081 -27.226 19.478 1.00 92.12  ? 360 GLU   A CA  1 
ATOM   418  C  C   . GLU   A 1 64  ? -34.433 -25.850 18.930 1.00 88.95  ? 360 GLU   A C   1 
ATOM   419  O  O   . GLU   A 1 64  ? -35.472 -25.281 19.283 1.00 85.97  ? 360 GLU   A O   1 
ATOM   420  C  CB  . GLU   A 1 64  ? -33.008 -27.124 20.564 1.00 95.99  ? 360 GLU   A CB  1 
ATOM   421  C  CG  . GLU   A 1 64  ? -33.313 -26.145 21.685 1.00 102.57 ? 360 GLU   A CG  1 
ATOM   422  C  CD  . GLU   A 1 64  ? -32.057 -25.701 22.416 1.00 109.42 ? 360 GLU   A CD  1 
ATOM   423  O  OE1 . GLU   A 1 64  ? -31.085 -26.489 22.451 1.00 113.98 ? 360 GLU   A OE1 1 
ATOM   424  O  OE2 . GLU   A 1 64  ? -32.035 -24.564 22.941 1.00 106.77 ? 360 GLU   A OE2 1 
ATOM   425  N  N   . PHE   A 1 65  ? -33.600 -25.312 18.035 1.00 85.27  ? 361 PHE   A N   1 
ATOM   426  C  CA  . PHE   A 1 65  ? -33.883 -23.991 17.489 1.00 76.51  ? 361 PHE   A CA  1 
ATOM   427  C  C   . PHE   A 1 65  ? -35.096 -24.025 16.574 1.00 77.51  ? 361 PHE   A C   1 
ATOM   428  O  O   . PHE   A 1 65  ? -35.995 -23.184 16.696 1.00 72.97  ? 361 PHE   A O   1 
ATOM   429  C  CB  . PHE   A 1 65  ? -32.675 -23.445 16.741 1.00 78.78  ? 361 PHE   A CB  1 
ATOM   430  C  CG  . PHE   A 1 65  ? -32.968 -22.191 15.977 1.00 78.19  ? 361 PHE   A CG  1 
ATOM   431  C  CD1 . PHE   A 1 65  ? -33.078 -20.977 16.639 1.00 72.76  ? 361 PHE   A CD1 1 
ATOM   432  C  CD2 . PHE   A 1 65  ? -33.150 -22.221 14.601 1.00 70.06  ? 361 PHE   A CD2 1 
ATOM   433  C  CE1 . PHE   A 1 65  ? -33.353 -19.815 15.939 1.00 76.87  ? 361 PHE   A CE1 1 
ATOM   434  C  CE2 . PHE   A 1 65  ? -33.427 -21.061 13.896 1.00 75.04  ? 361 PHE   A CE2 1 
ATOM   435  C  CZ  . PHE   A 1 65  ? -33.529 -19.856 14.572 1.00 73.16  ? 361 PHE   A CZ  1 
ATOM   436  N  N   . LEU   A 1 66  ? -35.128 -24.985 15.636 1.00 78.47  ? 362 LEU   A N   1 
ATOM   437  C  CA  . LEU   A 1 66  ? -36.240 -25.078 14.698 1.00 82.91  ? 362 LEU   A CA  1 
ATOM   438  C  C   . LEU   A 1 66  ? -37.564 -25.283 15.420 1.00 87.36  ? 362 LEU   A C   1 
ATOM   439  O  O   . LEU   A 1 66  ? -38.604 -24.780 14.977 1.00 89.41  ? 362 LEU   A O   1 
ATOM   440  C  CB  . LEU   A 1 66  ? -35.996 -26.219 13.704 1.00 84.27  ? 362 LEU   A CB  1 
ATOM   441  C  CG  . LEU   A 1 66  ? -34.932 -26.023 12.623 1.00 81.76  ? 362 LEU   A CG  1 
ATOM   442  C  CD1 . LEU   A 1 66  ? -35.021 -27.151 11.616 1.00 86.48  ? 362 LEU   A CD1 1 
ATOM   443  C  CD2 . LEU   A 1 66  ? -35.084 -24.675 11.943 1.00 79.01  ? 362 LEU   A CD2 1 
ATOM   444  N  N   . ASP   A 1 67  ? -37.548 -26.027 16.528 1.00 93.02  ? 363 ASP   A N   1 
ATOM   445  C  CA  . ASP   A 1 67  ? -38.768 -26.235 17.301 1.00 99.41  ? 363 ASP   A CA  1 
ATOM   446  C  C   . ASP   A 1 67  ? -39.305 -24.922 17.862 1.00 90.93  ? 363 ASP   A C   1 
ATOM   447  O  O   . ASP   A 1 67  ? -40.519 -24.687 17.857 1.00 92.35  ? 363 ASP   A O   1 
ATOM   448  C  CB  . ASP   A 1 67  ? -38.506 -27.233 18.430 1.00 104.16 ? 363 ASP   A CB  1 
ATOM   449  C  CG  . ASP   A 1 67  ? -38.669 -28.669 17.986 1.00 114.83 ? 363 ASP   A CG  1 
ATOM   450  O  OD1 . ASP   A 1 67  ? -39.822 -29.131 17.884 1.00 123.38 ? 363 ASP   A OD1 1 
ATOM   451  O  OD2 . ASP   A 1 67  ? -37.647 -29.332 17.723 1.00 117.24 ? 363 ASP   A OD2 1 
ATOM   452  N  N   . GLN   A 1 68  ? -38.423 -24.051 18.351 1.00 87.79  ? 364 GLN   A N   1 
ATOM   453  C  CA  . GLN   A 1 68  ? -38.918 -22.801 18.914 1.00 87.15  ? 364 GLN   A CA  1 
ATOM   454  C  C   . GLN   A 1 68  ? -39.277 -21.810 17.817 1.00 86.10  ? 364 GLN   A C   1 
ATOM   455  O  O   . GLN   A 1 68  ? -40.217 -21.024 17.980 1.00 86.35  ? 364 GLN   A O   1 
ATOM   456  C  CB  . GLN   A 1 68  ? -37.899 -22.210 19.896 1.00 85.35  ? 364 GLN   A CB  1 
ATOM   457  C  CG  . GLN   A 1 68  ? -36.566 -21.810 19.297 1.00 86.60  ? 364 GLN   A CG  1 
ATOM   458  C  CD  . GLN   A 1 68  ? -35.457 -21.707 20.332 1.00 86.42  ? 364 GLN   A CD  1 
ATOM   459  O  OE1 . GLN   A 1 68  ? -34.951 -20.617 20.613 1.00 83.34  ? 364 GLN   A OE1 1 
ATOM   460  N  NE2 . GLN   A 1 68  ? -35.061 -22.847 20.889 1.00 85.75  ? 364 GLN   A NE2 1 
ATOM   461  N  N   . TYR   A 1 69  ? -38.578 -21.854 16.682 1.00 83.84  ? 365 TYR   A N   1 
ATOM   462  C  CA  . TYR   A 1 69  ? -38.964 -20.998 15.565 1.00 82.31  ? 365 TYR   A CA  1 
ATOM   463  C  C   . TYR   A 1 69  ? -40.355 -21.354 15.057 1.00 86.64  ? 365 TYR   A C   1 
ATOM   464  O  O   . TYR   A 1 69  ? -41.207 -20.475 14.882 1.00 85.71  ? 365 TYR   A O   1 
ATOM   465  C  CB  . TYR   A 1 69  ? -37.948 -21.095 14.431 1.00 76.61  ? 365 TYR   A CB  1 
ATOM   466  C  CG  . TYR   A 1 69  ? -38.461 -20.430 13.184 1.00 81.26  ? 365 TYR   A CG  1 
ATOM   467  C  CD1 . TYR   A 1 69  ? -38.735 -19.066 13.167 1.00 81.18  ? 365 TYR   A CD1 1 
ATOM   468  C  CD2 . TYR   A 1 69  ? -38.700 -21.164 12.028 1.00 78.71  ? 365 TYR   A CD2 1 
ATOM   469  C  CE1 . TYR   A 1 69  ? -39.223 -18.454 12.030 1.00 84.57  ? 365 TYR   A CE1 1 
ATOM   470  C  CE2 . TYR   A 1 69  ? -39.185 -20.556 10.892 1.00 85.31  ? 365 TYR   A CE2 1 
ATOM   471  C  CZ  . TYR   A 1 69  ? -39.442 -19.202 10.901 1.00 86.37  ? 365 TYR   A CZ  1 
ATOM   472  O  OH  . TYR   A 1 69  ? -39.925 -18.592 9.769  1.00 92.63  ? 365 TYR   A OH  1 
ATOM   473  N  N   . TYR   A 1 70  ? -40.597 -22.641 14.790 1.00 97.35  ? 366 TYR   A N   1 
ATOM   474  C  CA  . TYR   A 1 70  ? -41.907 -23.052 14.300 1.00 97.09  ? 366 TYR   A CA  1 
ATOM   475  C  C   . TYR   A 1 70  ? -42.974 -22.899 15.369 1.00 102.65 ? 366 TYR   A C   1 
ATOM   476  O  O   . TYR   A 1 70  ? -44.134 -22.616 15.048 1.00 106.19 ? 366 TYR   A O   1 
ATOM   477  C  CB  . TYR   A 1 70  ? -41.849 -24.487 13.780 1.00 100.79 ? 366 TYR   A CB  1 
ATOM   478  C  CG  . TYR   A 1 70  ? -41.299 -24.533 12.376 1.00 95.78  ? 366 TYR   A CG  1 
ATOM   479  C  CD1 . TYR   A 1 70  ? -39.976 -24.884 12.133 1.00 90.36  ? 366 TYR   A CD1 1 
ATOM   480  C  CD2 . TYR   A 1 70  ? -42.089 -24.166 11.294 1.00 96.10  ? 366 TYR   A CD2 1 
ATOM   481  C  CE1 . TYR   A 1 70  ? -39.465 -24.902 10.836 1.00 91.06  ? 366 TYR   A CE1 1 
ATOM   482  C  CE2 . TYR   A 1 70  ? -41.588 -24.177 10.006 1.00 97.11  ? 366 TYR   A CE2 1 
ATOM   483  C  CZ  . TYR   A 1 70  ? -40.277 -24.545 9.782  1.00 90.89  ? 366 TYR   A CZ  1 
ATOM   484  O  OH  . TYR   A 1 70  ? -39.786 -24.545 8.486  1.00 80.63  ? 366 TYR   A OH  1 
ATOM   485  N  N   . SER   A 1 71  ? -42.603 -23.070 16.638 1.00 98.91  ? 367 SER   A N   1 
ATOM   486  C  CA  . SER   A 1 71  ? -43.507 -22.701 17.717 1.00 101.08 ? 367 SER   A CA  1 
ATOM   487  C  C   . SER   A 1 71  ? -43.886 -21.228 17.618 1.00 95.70  ? 367 SER   A C   1 
ATOM   488  O  O   . SER   A 1 71  ? -45.051 -20.864 17.817 1.00 105.50 ? 367 SER   A O   1 
ATOM   489  C  CB  . SER   A 1 71  ? -42.855 -23.008 19.067 1.00 98.38  ? 367 SER   A CB  1 
ATOM   490  O  OG  . SER   A 1 71  ? -43.802 -22.993 20.119 1.00 107.25 ? 367 SER   A OG  1 
ATOM   491  N  N   . SER   A 1 72  ? -42.922 -20.372 17.267 1.00 83.53  ? 368 SER   A N   1 
ATOM   492  C  CA  . SER   A 1 72  ? -43.148 -18.930 17.299 1.00 80.85  ? 368 SER   A CA  1 
ATOM   493  C  C   . SER   A 1 72  ? -44.128 -18.468 16.224 1.00 92.74  ? 368 SER   A C   1 
ATOM   494  O  O   . SER   A 1 72  ? -44.899 -17.531 16.461 1.00 94.63  ? 368 SER   A O   1 
ATOM   495  C  CB  . SER   A 1 72  ? -41.822 -18.187 17.151 1.00 75.46  ? 368 SER   A CB  1 
ATOM   496  O  OG  . SER   A 1 72  ? -41.633 -17.700 15.833 1.00 87.83  ? 368 SER   A OG  1 
ATOM   497  N  N   . ILE   A 1 73  ? -44.116 -19.091 15.043 1.00 99.31  ? 369 ILE   A N   1 
ATOM   498  C  CA  . ILE   A 1 73  ? -45.027 -18.690 13.975 1.00 106.53 ? 369 ILE   A CA  1 
ATOM   499  C  C   . ILE   A 1 73  ? -46.347 -19.436 14.127 1.00 116.58 ? 369 ILE   A C   1 
ATOM   500  O  O   . ILE   A 1 73  ? -47.133 -19.528 13.177 1.00 122.48 ? 369 ILE   A O   1 
ATOM   501  C  CB  . ILE   A 1 73  ? -44.407 -18.925 12.583 1.00 109.97 ? 369 ILE   A CB  1 
ATOM   502  C  CG1 . ILE   A 1 73  ? -43.896 -20.361 12.454 1.00 109.52 ? 369 ILE   A CG1 1 
ATOM   503  C  CG2 . ILE   A 1 73  ? -43.285 -17.924 12.318 1.00 104.18 ? 369 ILE   A CG2 1 
ATOM   504  C  CD1 . ILE   A 1 73  ? -43.057 -20.595 11.223 1.00 104.96 ? 369 ILE   A CD1 1 
ATOM   505  N  N   . LYS   A 1 74  ? -46.602 -19.956 15.332 1.00 117.86 ? 370 LYS   A N   1 
ATOM   506  C  CA  . LYS   A 1 74  ? -47.843 -20.659 15.678 1.00 126.29 ? 370 LYS   A CA  1 
ATOM   507  C  C   . LYS   A 1 74  ? -48.062 -21.897 14.806 1.00 130.76 ? 370 LYS   A C   1 
ATOM   508  O  O   . LYS   A 1 74  ? -49.197 -22.224 14.449 1.00 137.29 ? 370 LYS   A O   1 
ATOM   509  C  CB  . LYS   A 1 74  ? -49.064 -19.731 15.601 1.00 130.26 ? 370 LYS   A CB  1 
ATOM   510  C  CG  . LYS   A 1 74  ? -48.785 -18.264 15.918 1.00 126.10 ? 370 LYS   A CG  1 
ATOM   511  C  CD  . LYS   A 1 74  ? -49.392 -17.805 17.231 1.00 125.16 ? 370 LYS   A CD  1 
ATOM   512  C  CE  . LYS   A 1 74  ? -49.143 -16.313 17.416 1.00 123.03 ? 370 LYS   A CE  1 
ATOM   513  N  NZ  . LYS   A 1 74  ? -49.471 -15.823 18.781 1.00 122.85 ? 370 LYS   A NZ  1 
ATOM   514  N  N   . ARG   A 1 75  ? -46.980 -22.594 14.455 1.00 122.53 ? 371 ARG   A N   1 
ATOM   515  C  CA  . ARG   A 1 75  ? -47.049 -23.832 13.679 1.00 118.22 ? 371 ARG   A CA  1 
ATOM   516  C  C   . ARG   A 1 75  ? -46.062 -24.862 14.228 1.00 123.86 ? 371 ARG   A C   1 
ATOM   517  O  O   . ARG   A 1 75  ? -45.281 -25.464 13.489 1.00 125.65 ? 371 ARG   A O   1 
ATOM   518  C  CB  . ARG   A 1 75  ? -46.782 -23.564 12.200 1.00 106.91 ? 371 ARG   A CB  1 
ATOM   519  C  CG  . ARG   A 1 75  ? -47.703 -22.523 11.598 1.00 107.22 ? 371 ARG   A CG  1 
ATOM   520  C  CD  . ARG   A 1 75  ? -46.926 -21.493 10.806 1.00 107.30 ? 371 ARG   A CD  1 
ATOM   521  N  NE  . ARG   A 1 75  ? -47.258 -21.579 9.393  1.00 115.33 ? 371 ARG   A NE  1 
ATOM   522  C  CZ  . ARG   A 1 75  ? -46.694 -22.441 8.557  1.00 121.32 ? 371 ARG   A CZ  1 
ATOM   523  N  NH1 . ARG   A 1 75  ? -47.054 -22.465 7.282  1.00 125.93 ? 371 ARG   A NH1 1 
ATOM   524  N  NH2 . ARG   A 1 75  ? -45.767 -23.281 8.998  1.00 121.23 ? 371 ARG   A NH2 1 
ATOM   525  N  N   . PHE   A 1 76  ? -46.096 -25.073 15.546 1.00 126.03 ? 372 PHE   A N   1 
ATOM   526  C  CA  . PHE   A 1 76  ? -45.287 -26.111 16.176 1.00 127.39 ? 372 PHE   A CA  1 
ATOM   527  C  C   . PHE   A 1 76  ? -45.676 -27.479 15.629 1.00 134.66 ? 372 PHE   A C   1 
ATOM   528  O  O   . PHE   A 1 76  ? -46.859 -27.831 15.587 1.00 140.47 ? 372 PHE   A O   1 
ATOM   529  C  CB  . PHE   A 1 76  ? -45.480 -26.072 17.699 1.00 127.32 ? 372 PHE   A CB  1 
ATOM   530  C  CG  . PHE   A 1 76  ? -44.513 -26.941 18.486 1.00 126.09 ? 372 PHE   A CG  1 
ATOM   531  C  CD1 . PHE   A 1 76  ? -44.517 -28.322 18.361 1.00 127.93 ? 372 PHE   A CD1 1 
ATOM   532  C  CD2 . PHE   A 1 76  ? -43.635 -26.368 19.392 1.00 127.32 ? 372 PHE   A CD2 1 
ATOM   533  C  CE1 . PHE   A 1 76  ? -43.642 -29.109 19.088 1.00 127.38 ? 372 PHE   A CE1 1 
ATOM   534  C  CE2 . PHE   A 1 76  ? -42.760 -27.154 20.132 1.00 128.23 ? 372 PHE   A CE2 1 
ATOM   535  C  CZ  . PHE   A 1 76  ? -42.765 -28.526 19.974 1.00 128.67 ? 372 PHE   A CZ  1 
ATOM   536  N  N   . GLY   A 1 77  ? -44.672 -28.250 15.213 1.00 136.50 ? 373 GLY   A N   1 
ATOM   537  C  CA  . GLY   A 1 77  ? -44.862 -29.648 14.871 1.00 145.55 ? 373 GLY   A CA  1 
ATOM   538  C  C   . GLY   A 1 77  ? -45.737 -29.899 13.661 1.00 150.63 ? 373 GLY   A C   1 
ATOM   539  O  O   . GLY   A 1 77  ? -46.139 -31.039 13.400 1.00 157.28 ? 373 GLY   A O   1 
ATOM   540  N  N   . SER   A 1 78  ? -46.032 -28.847 12.909 1.00 145.22 ? 374 SER   A N   1 
ATOM   541  C  CA  . SER   A 1 78  ? -46.875 -28.961 11.728 1.00 143.78 ? 374 SER   A CA  1 
ATOM   542  C  C   . SER   A 1 78  ? -46.108 -29.692 10.626 1.00 135.43 ? 374 SER   A C   1 
ATOM   543  O  O   . SER   A 1 78  ? -45.007 -30.215 10.828 1.00 130.84 ? 374 SER   A O   1 
ATOM   544  C  CB  . SER   A 1 78  ? -47.345 -27.578 11.285 1.00 145.28 ? 374 SER   A CB  1 
ATOM   545  O  OG  . SER   A 1 78  ? -46.243 -26.730 11.019 1.00 141.57 ? 374 SER   A OG  1 
ATOM   546  N  N   . LYS   A 1 79  ? -46.704 -29.736 9.432  1.00 129.41 ? 375 LYS   A N   1 
ATOM   547  C  CA  . LYS   A 1 79  ? -46.064 -30.399 8.300  1.00 124.68 ? 375 LYS   A CA  1 
ATOM   548  C  C   . LYS   A 1 79  ? -44.803 -29.659 7.870  1.00 113.69 ? 375 LYS   A C   1 
ATOM   549  O  O   . LYS   A 1 79  ? -43.754 -30.276 7.651  1.00 106.27 ? 375 LYS   A O   1 
ATOM   550  C  CB  . LYS   A 1 79  ? -47.044 -30.511 7.132  1.00 126.36 ? 375 LYS   A CB  1 
ATOM   551  C  CG  . LYS   A 1 79  ? -46.497 -31.276 5.932  1.00 125.49 ? 375 LYS   A CG  1 
ATOM   552  C  CD  . LYS   A 1 79  ? -46.807 -32.767 6.034  1.00 130.93 ? 375 LYS   A CD  1 
ATOM   553  C  CE  . LYS   A 1 79  ? -46.112 -33.573 4.941  1.00 126.57 ? 375 LYS   A CE  1 
ATOM   554  N  NZ  . LYS   A 1 79  ? -44.645 -33.688 5.167  1.00 120.25 ? 375 LYS   A NZ  1 
ATOM   555  N  N   . ALA   A 1 80  ? -44.886 -28.331 7.747  1.00 114.25 ? 376 ALA   A N   1 
ATOM   556  C  CA  . ALA   A 1 80  ? -43.717 -27.553 7.346  1.00 112.11 ? 376 ALA   A CA  1 
ATOM   557  C  C   . ALA   A 1 80  ? -42.575 -27.718 8.341  1.00 110.84 ? 376 ALA   A C   1 
ATOM   558  O  O   . ALA   A 1 80  ? -41.404 -27.769 7.946  1.00 109.25 ? 376 ALA   A O   1 
ATOM   559  C  CB  . ALA   A 1 80  ? -44.090 -26.078 7.189  1.00 107.04 ? 376 ALA   A CB  1 
ATOM   560  N  N   . HIS   A 1 81  ? -42.895 -27.813 9.635  1.00 114.95 ? 377 HIS   A N   1 
ATOM   561  C  CA  . HIS   A 1 81  ? -41.862 -28.018 10.648 1.00 111.22 ? 377 HIS   A CA  1 
ATOM   562  C  C   . HIS   A 1 81  ? -41.178 -29.367 10.471 1.00 115.72 ? 377 HIS   A C   1 
ATOM   563  O  O   . HIS   A 1 81  ? -39.957 -29.439 10.284 1.00 112.96 ? 377 HIS   A O   1 
ATOM   564  C  CB  . HIS   A 1 81  ? -42.462 -27.905 12.052 1.00 114.37 ? 377 HIS   A CB  1 
ATOM   565  C  CG  . HIS   A 1 81  ? -41.493 -28.219 13.155 1.00 115.25 ? 377 HIS   A CG  1 
ATOM   566  N  ND1 . HIS   A 1 81  ? -41.893 -28.415 14.459 1.00 117.75 ? 377 HIS   A ND1 1 
ATOM   567  C  CD2 . HIS   A 1 81  ? -40.146 -28.364 13.152 1.00 112.86 ? 377 HIS   A CD2 1 
ATOM   568  C  CE1 . HIS   A 1 81  ? -40.838 -28.670 15.212 1.00 113.61 ? 377 HIS   A CE1 1 
ATOM   569  N  NE2 . HIS   A 1 81  ? -39.765 -28.645 14.444 1.00 113.37 ? 377 HIS   A NE2 1 
ATOM   570  N  N   . MET   A 1 82  ? -41.951 -30.454 10.539 1.00 124.84 ? 378 MET   A N   1 
ATOM   571  C  CA  . MET   A 1 82  ? -41.364 -31.788 10.474 1.00 130.08 ? 378 MET   A CA  1 
ATOM   572  C  C   . MET   A 1 82  ? -40.573 -32.004 9.187  1.00 124.98 ? 378 MET   A C   1 
ATOM   573  O  O   . MET   A 1 82  ? -39.608 -32.777 9.179  1.00 126.83 ? 378 MET   A O   1 
ATOM   574  C  CB  . MET   A 1 82  ? -42.457 -32.846 10.622 1.00 143.41 ? 378 MET   A CB  1 
ATOM   575  C  CG  . MET   A 1 82  ? -43.157 -32.816 11.974 1.00 152.06 ? 378 MET   A CG  1 
ATOM   576  S  SD  . MET   A 1 82  ? -42.015 -33.069 13.350 1.00 156.71 ? 378 MET   A SD  1 
ATOM   577  C  CE  . MET   A 1 82  ? -43.124 -32.963 14.756 1.00 159.69 ? 378 MET   A CE  1 
ATOM   578  N  N   . ASP   A 1 83  ? -40.947 -31.328 8.097  1.00 114.36 ? 379 ASP   A N   1 
ATOM   579  C  CA  . ASP   A 1 83  ? -40.173 -31.462 6.866  1.00 111.26 ? 379 ASP   A CA  1 
ATOM   580  C  C   . ASP   A 1 83  ? -38.873 -30.676 6.929  1.00 104.28 ? 379 ASP   A C   1 
ATOM   581  O  O   . ASP   A 1 83  ? -37.826 -31.177 6.502  1.00 100.59 ? 379 ASP   A O   1 
ATOM   582  C  CB  . ASP   A 1 83  ? -40.996 -31.019 5.657  1.00 110.84 ? 379 ASP   A CB  1 
ATOM   583  C  CG  . ASP   A 1 83  ? -41.861 -32.129 5.112  1.00 119.91 ? 379 ASP   A CG  1 
ATOM   584  O  OD1 . ASP   A 1 83  ? -43.058 -31.882 4.860  1.00 125.45 ? 379 ASP   A OD1 1 
ATOM   585  O  OD2 . ASP   A 1 83  ? -41.347 -33.258 4.957  1.00 125.52 ? 379 ASP   A OD2 1 
ATOM   586  N  N   . ARG   A 1 84  ? -38.922 -29.443 7.444  1.00 100.38 ? 380 ARG   A N   1 
ATOM   587  C  CA  . ARG   A 1 84  ? -37.701 -28.666 7.624  1.00 100.25 ? 380 ARG   A CA  1 
ATOM   588  C  C   . ARG   A 1 84  ? -36.768 -29.335 8.625  1.00 105.58 ? 380 ARG   A C   1 
ATOM   589  O  O   . ARG   A 1 84  ? -35.542 -29.281 8.473  1.00 111.62 ? 380 ARG   A O   1 
ATOM   590  C  CB  . ARG   A 1 84  ? -38.046 -27.247 8.080  1.00 98.75  ? 380 ARG   A CB  1 
ATOM   591  C  CG  . ARG   A 1 84  ? -36.841 -26.402 8.470  1.00 93.30  ? 380 ARG   A CG  1 
ATOM   592  C  CD  . ARG   A 1 84  ? -36.635 -25.327 7.436  1.00 93.44  ? 380 ARG   A CD  1 
ATOM   593  N  NE  . ARG   A 1 84  ? -35.363 -24.633 7.590  1.00 88.79  ? 380 ARG   A NE  1 
ATOM   594  C  CZ  . ARG   A 1 84  ? -34.255 -24.983 6.948  1.00 78.38  ? 380 ARG   A CZ  1 
ATOM   595  N  NH1 . ARG   A 1 84  ? -34.282 -26.014 6.119  1.00 85.85  ? 380 ARG   A NH1 1 
ATOM   596  N  NH2 . ARG   A 1 84  ? -33.126 -24.305 7.120  1.00 68.14  ? 380 ARG   A NH2 1 
ATOM   597  N  N   . LEU   A 1 85  ? -37.332 -29.952 9.665  1.00 101.81 ? 381 LEU   A N   1 
ATOM   598  C  CA  . LEU   A 1 85  ? -36.543 -30.777 10.571 1.00 104.38 ? 381 LEU   A CA  1 
ATOM   599  C  C   . LEU   A 1 85  ? -35.804 -31.860 9.793  1.00 103.31 ? 381 LEU   A C   1 
ATOM   600  O  O   . LEU   A 1 85  ? -34.571 -31.948 9.830  1.00 101.14 ? 381 LEU   A O   1 
ATOM   601  C  CB  . LEU   A 1 85  ? -37.463 -31.393 11.632 1.00 109.37 ? 381 LEU   A CB  1 
ATOM   602  C  CG  . LEU   A 1 85  ? -36.910 -31.696 13.023 1.00 113.16 ? 381 LEU   A CG  1 
ATOM   603  C  CD1 . LEU   A 1 85  ? -36.606 -30.406 13.755 1.00 102.14 ? 381 LEU   A CD1 1 
ATOM   604  C  CD2 . LEU   A 1 85  ? -37.900 -32.540 13.813 1.00 123.99 ? 381 LEU   A CD2 1 
ATOM   605  N  N   . GLU   A 1 86  ? -36.559 -32.683 9.062  1.00 109.91 ? 382 GLU   A N   1 
ATOM   606  C  CA  . GLU   A 1 86  ? -35.963 -33.694 8.193  1.00 116.22 ? 382 GLU   A CA  1 
ATOM   607  C  C   . GLU   A 1 86  ? -34.968 -33.077 7.219  1.00 104.96 ? 382 GLU   A C   1 
ATOM   608  O  O   . GLU   A 1 86  ? -33.863 -33.598 7.034  1.00 101.76 ? 382 GLU   A O   1 
ATOM   609  C  CB  . GLU   A 1 86  ? -37.063 -34.427 7.426  1.00 130.83 ? 382 GLU   A CB  1 
ATOM   610  C  CG  . GLU   A 1 86  ? -36.564 -35.489 6.467  1.00 143.31 ? 382 GLU   A CG  1 
ATOM   611  C  CD  . GLU   A 1 86  ? -36.402 -36.849 7.120  1.00 156.82 ? 382 GLU   A CD  1 
ATOM   612  O  OE1 . GLU   A 1 86  ? -36.093 -37.819 6.394  1.00 164.20 ? 382 GLU   A OE1 1 
ATOM   613  O  OE2 . GLU   A 1 86  ? -36.588 -36.952 8.354  1.00 159.62 ? 382 GLU   A OE2 1 
ATOM   614  N  N   . GLU   A 1 87  ? -35.337 -31.948 6.611  1.00 99.82  ? 383 GLU   A N   1 
ATOM   615  C  CA  . GLU   A 1 87  ? -34.485 -31.306 5.615  1.00 95.21  ? 383 GLU   A CA  1 
ATOM   616  C  C   . GLU   A 1 87  ? -33.140 -30.879 6.197  1.00 91.16  ? 383 GLU   A C   1 
ATOM   617  O  O   . GLU   A 1 87  ? -32.100 -31.015 5.541  1.00 87.73  ? 383 GLU   A O   1 
ATOM   618  C  CB  . GLU   A 1 87  ? -35.217 -30.105 5.026  1.00 94.83  ? 383 GLU   A CB  1 
ATOM   619  C  CG  . GLU   A 1 87  ? -34.383 -29.263 4.102  1.00 97.94  ? 383 GLU   A CG  1 
ATOM   620  C  CD  . GLU   A 1 87  ? -35.165 -28.099 3.534  1.00 95.89  ? 383 GLU   A CD  1 
ATOM   621  O  OE1 . GLU   A 1 87  ? -35.727 -27.313 4.338  1.00 90.87  ? 383 GLU   A OE1 1 
ATOM   622  O  OE2 . GLU   A 1 87  ? -35.226 -27.981 2.287  1.00 89.00  ? 383 GLU   A OE2 1 
ATOM   623  N  N   . VAL   A 1 88  ? -33.137 -30.336 7.419  1.00 86.40  ? 384 VAL   A N   1 
ATOM   624  C  CA  . VAL   A 1 88  ? -31.884 -29.869 8.005  1.00 85.20  ? 384 VAL   A CA  1 
ATOM   625  C  C   . VAL   A 1 88  ? -31.037 -31.048 8.474  1.00 92.31  ? 384 VAL   A C   1 
ATOM   626  O  O   . VAL   A 1 88  ? -29.807 -31.035 8.344  1.00 96.72  ? 384 VAL   A O   1 
ATOM   627  C  CB  . VAL   A 1 88  ? -32.165 -28.877 9.148  1.00 89.18  ? 384 VAL   A CB  1 
ATOM   628  C  CG1 . VAL   A 1 88  ? -30.877 -28.513 9.861  1.00 89.50  ? 384 VAL   A CG1 1 
ATOM   629  C  CG2 . VAL   A 1 88  ? -32.828 -27.633 8.594  1.00 86.54  ? 384 VAL   A CG2 1 
ATOM   630  N  N   . ASN   A 1 89  ? -31.678 -32.079 9.031  1.00 93.42  ? 385 ASN   A N   1 
ATOM   631  C  CA  . ASN   A 1 89  ? -30.973 -33.317 9.355  1.00 104.80 ? 385 ASN   A CA  1 
ATOM   632  C  C   . ASN   A 1 89  ? -30.248 -33.871 8.128  1.00 106.54 ? 385 ASN   A C   1 
ATOM   633  O  O   . ASN   A 1 89  ? -29.059 -34.204 8.187  1.00 107.11 ? 385 ASN   A O   1 
ATOM   634  C  CB  . ASN   A 1 89  ? -31.969 -34.337 9.912  1.00 116.29 ? 385 ASN   A CB  1 
ATOM   635  C  CG  . ASN   A 1 89  ? -31.295 -35.517 10.593 1.00 123.21 ? 385 ASN   A CG  1 
ATOM   636  O  OD1 . ASN   A 1 89  ? -31.376 -36.652 10.114 1.00 130.89 ? 385 ASN   A OD1 1 
ATOM   637  N  ND2 . ASN   A 1 89  ? -30.639 -35.260 11.720 1.00 113.80 ? 385 ASN   A ND2 1 
ATOM   638  N  N   . LYS   A 1 90  ? -30.951 -33.957 6.997  1.00 107.99 ? 386 LYS   A N   1 
ATOM   639  C  CA  . LYS   A 1 90  ? -30.324 -34.458 5.776  1.00 112.40 ? 386 LYS   A CA  1 
ATOM   640  C  C   . LYS   A 1 90  ? -29.146 -33.589 5.349  1.00 107.38 ? 386 LYS   A C   1 
ATOM   641  O  O   . LYS   A 1 90  ? -28.130 -34.109 4.876  1.00 104.51 ? 386 LYS   A O   1 
ATOM   642  C  CB  . LYS   A 1 90  ? -31.356 -34.545 4.654  1.00 120.28 ? 386 LYS   A CB  1 
ATOM   643  C  CG  . LYS   A 1 90  ? -32.474 -35.559 4.878  1.00 127.44 ? 386 LYS   A CG  1 
ATOM   644  C  CD  . LYS   A 1 90  ? -33.673 -35.225 3.997  1.00 129.26 ? 386 LYS   A CD  1 
ATOM   645  C  CE  . LYS   A 1 90  ? -34.531 -36.449 3.707  1.00 135.01 ? 386 LYS   A CE  1 
ATOM   646  N  NZ  . LYS   A 1 90  ? -35.770 -36.085 2.959  1.00 135.79 ? 386 LYS   A NZ  1 
ATOM   647  N  N   . GLU   A 1 91  ? -29.251 -32.270 5.523  1.00 104.42 ? 387 GLU   A N   1 
ATOM   648  C  CA  . GLU   A 1 91  ? -28.143 -31.390 5.171  1.00 102.91 ? 387 GLU   A CA  1 
ATOM   649  C  C   . GLU   A 1 91  ? -26.995 -31.483 6.172  1.00 105.73 ? 387 GLU   A C   1 
ATOM   650  O  O   . GLU   A 1 91  ? -25.839 -31.243 5.804  1.00 104.43 ? 387 GLU   A O   1 
ATOM   651  C  CB  . GLU   A 1 91  ? -28.639 -29.951 5.057  1.00 100.43 ? 387 GLU   A CB  1 
ATOM   652  C  CG  . GLU   A 1 91  ? -27.556 -28.946 4.718  1.00 97.19  ? 387 GLU   A CG  1 
ATOM   653  C  CD  . GLU   A 1 91  ? -28.107 -27.560 4.504  1.00 98.26  ? 387 GLU   A CD  1 
ATOM   654  O  OE1 . GLU   A 1 91  ? -27.346 -26.686 4.039  1.00 95.75  ? 387 GLU   A OE1 1 
ATOM   655  O  OE2 . GLU   A 1 91  ? -29.300 -27.345 4.802  1.00 101.50 ? 387 GLU   A OE2 1 
ATOM   656  N  N   . ILE   A 1 92  ? -27.286 -31.823 7.430  1.00 105.05 ? 388 ILE   A N   1 
ATOM   657  C  CA  . ILE   A 1 92  ? -26.211 -32.067 8.386  1.00 98.30  ? 388 ILE   A CA  1 
ATOM   658  C  C   . ILE   A 1 92  ? -25.555 -33.420 8.123  1.00 104.03 ? 388 ILE   A C   1 
ATOM   659  O  O   . ILE   A 1 92  ? -24.377 -33.618 8.440  1.00 103.54 ? 388 ILE   A O   1 
ATOM   660  C  CB  . ILE   A 1 92  ? -26.732 -31.966 9.830  1.00 93.02  ? 388 ILE   A CB  1 
ATOM   661  C  CG1 . ILE   A 1 92  ? -27.325 -30.580 10.096 1.00 89.42  ? 388 ILE   A CG1 1 
ATOM   662  C  CG2 . ILE   A 1 92  ? -25.607 -32.218 10.819 1.00 95.19  ? 388 ILE   A CG2 1 
ATOM   663  C  CD1 . ILE   A 1 92  ? -28.013 -30.473 11.444 1.00 87.09  ? 388 ILE   A CD1 1 
ATOM   664  N  N   . GLU   A 1 93  ? -26.288 -34.375 7.555  1.00 113.62 ? 389 GLU   A N   1 
ATOM   665  C  CA  . GLU   A 1 93  ? -25.637 -35.564 7.019  1.00 119.55 ? 389 GLU   A CA  1 
ATOM   666  C  C   . GLU   A 1 93  ? -24.744 -35.195 5.841  1.00 117.93 ? 389 GLU   A C   1 
ATOM   667  O  O   . GLU   A 1 93  ? -23.530 -35.435 5.861  1.00 114.12 ? 389 GLU   A O   1 
ATOM   668  C  CB  . GLU   A 1 93  ? -26.685 -36.595 6.599  1.00 127.24 ? 389 GLU   A CB  1 
ATOM   669  C  CG  . GLU   A 1 93  ? -27.469 -37.198 7.747  1.00 134.69 ? 389 GLU   A CG  1 
ATOM   670  C  CD  . GLU   A 1 93  ? -26.634 -38.145 8.586  1.00 144.53 ? 389 GLU   A CD  1 
ATOM   671  O  OE1 . GLU   A 1 93  ? -25.597 -38.628 8.083  1.00 147.24 ? 389 GLU   A OE1 1 
ATOM   672  O  OE2 . GLU   A 1 93  ? -27.016 -38.403 9.749  1.00 148.20 ? 389 GLU   A OE2 1 
ATOM   673  N  N   . SER   A 1 94  ? -25.333 -34.563 4.820  1.00 125.19 ? 390 SER   A N   1 
ATOM   674  C  CA  . SER   A 1 94  ? -24.642 -34.322 3.557  1.00 125.06 ? 390 SER   A CA  1 
ATOM   675  C  C   . SER   A 1 94  ? -23.420 -33.426 3.739  1.00 125.23 ? 390 SER   A C   1 
ATOM   676  O  O   . SER   A 1 94  ? -22.327 -33.746 3.257  1.00 120.06 ? 390 SER   A O   1 
ATOM   677  C  CB  . SER   A 1 94  ? -25.615 -33.701 2.558  1.00 125.81 ? 390 SER   A CB  1 
ATOM   678  O  OG  . SER   A 1 94  ? -25.000 -32.648 1.838  1.00 127.36 ? 390 SER   A OG  1 
ATOM   679  N  N   . THR   A 1 95  ? -23.590 -32.292 4.429  1.00 125.49 ? 391 THR   A N   1 
ATOM   680  C  CA  . THR   A 1 95  ? -22.557 -31.266 4.545  1.00 126.50 ? 391 THR   A CA  1 
ATOM   681  C  C   . THR   A 1 95  ? -21.885 -31.215 5.910  1.00 122.62 ? 391 THR   A C   1 
ATOM   682  O  O   . THR   A 1 95  ? -20.878 -30.514 6.053  1.00 117.79 ? 391 THR   A O   1 
ATOM   683  C  CB  . THR   A 1 95  ? -23.141 -29.875 4.262  1.00 126.74 ? 391 THR   A CB  1 
ATOM   684  O  OG1 . THR   A 1 95  ? -24.484 -30.000 3.784  1.00 134.93 ? 391 THR   A OG1 1 
ATOM   685  C  CG2 . THR   A 1 95  ? -22.293 -29.130 3.237  1.00 122.01 ? 391 THR   A CG2 1 
ATOM   686  N  N   . SER   A 1 96  ? -22.421 -31.916 6.910  1.00 123.03 ? 392 SER   A N   1 
ATOM   687  C  CA  . SER   A 1 96  ? -21.977 -31.788 8.299  1.00 122.64 ? 392 SER   A CA  1 
ATOM   688  C  C   . SER   A 1 96  ? -22.156 -30.359 8.809  1.00 114.35 ? 392 SER   A C   1 
ATOM   689  O  O   . SER   A 1 96  ? -21.411 -29.897 9.678  1.00 116.40 ? 392 SER   A O   1 
ATOM   690  C  CB  . SER   A 1 96  ? -20.529 -32.258 8.483  1.00 129.00 ? 392 SER   A CB  1 
ATOM   691  O  OG  . SER   A 1 96  ? -19.620 -31.407 7.807  1.00 126.30 ? 392 SER   A OG  1 
ATOM   692  N  N   . THR   A 1 97  ? -23.142 -29.661 8.258  1.00 102.05 ? 393 THR   A N   1 
ATOM   693  C  CA  . THR   A 1 97  ? -23.573 -28.332 8.686  1.00 88.87  ? 393 THR   A CA  1 
ATOM   694  C  C   . THR   A 1 97  ? -24.903 -28.059 7.989  1.00 85.43  ? 393 THR   A C   1 
ATOM   695  O  O   . THR   A 1 97  ? -25.530 -28.978 7.451  1.00 86.54  ? 393 THR   A O   1 
ATOM   696  C  CB  . THR   A 1 97  ? -22.523 -27.263 8.381  1.00 82.28  ? 393 THR   A CB  1 
ATOM   697  O  OG1 . THR   A 1 97  ? -22.984 -25.996 8.870  1.00 83.20  ? 393 THR   A OG1 1 
ATOM   698  C  CG2 . THR   A 1 97  ? -22.267 -27.168 6.883  1.00 86.50  ? 393 THR   A CG2 1 
ATOM   699  N  N   . TYR   A 1 98  ? -25.348 -26.807 7.996  1.00 82.10  ? 394 TYR   A N   1 
ATOM   700  C  CA  . TYR   A 1 98  ? -26.596 -26.485 7.314  1.00 80.93  ? 394 TYR   A CA  1 
ATOM   701  C  C   . TYR   A 1 98  ? -26.713 -24.971 7.180  1.00 77.77  ? 394 TYR   A C   1 
ATOM   702  O  O   . TYR   A 1 98  ? -25.897 -24.212 7.709  1.00 73.32  ? 394 TYR   A O   1 
ATOM   703  C  CB  . TYR   A 1 98  ? -27.809 -27.086 8.039  1.00 79.64  ? 394 TYR   A CB  1 
ATOM   704  C  CG  . TYR   A 1 98  ? -28.149 -26.443 9.362  1.00 82.78  ? 394 TYR   A CG  1 
ATOM   705  C  CD1 . TYR   A 1 98  ? -29.162 -25.500 9.445  1.00 82.37  ? 394 TYR   A CD1 1 
ATOM   706  C  CD2 . TYR   A 1 98  ? -27.470 -26.786 10.532 1.00 81.22  ? 394 TYR   A CD2 1 
ATOM   707  C  CE1 . TYR   A 1 98  ? -29.489 -24.909 10.637 1.00 77.58  ? 394 TYR   A CE1 1 
ATOM   708  C  CE2 . TYR   A 1 98  ? -27.794 -26.192 11.748 1.00 78.04  ? 394 TYR   A CE2 1 
ATOM   709  C  CZ  . TYR   A 1 98  ? -28.808 -25.257 11.788 1.00 74.12  ? 394 TYR   A CZ  1 
ATOM   710  O  OH  . TYR   A 1 98  ? -29.159 -24.644 12.956 1.00 71.79  ? 394 TYR   A OH  1 
ATOM   711  N  N   . GLN   A 1 99  ? -27.729 -24.543 6.441  1.00 83.96  ? 395 GLN   A N   1 
ATOM   712  C  CA  . GLN   A 1 99  ? -27.953 -23.136 6.148  1.00 78.06  ? 395 GLN   A CA  1 
ATOM   713  C  C   . GLN   A 1 99  ? -29.319 -22.723 6.675  1.00 72.41  ? 395 GLN   A C   1 
ATOM   714  O  O   . GLN   A 1 99  ? -30.303 -23.457 6.524  1.00 72.25  ? 395 GLN   A O   1 
ATOM   715  C  CB  . GLN   A 1 99  ? -27.864 -22.860 4.634  1.00 75.61  ? 395 GLN   A CB  1 
ATOM   716  C  CG  . GLN   A 1 99  ? -26.494 -23.127 4.020  1.00 71.18  ? 395 GLN   A CG  1 
ATOM   717  C  CD  . GLN   A 1 99  ? -25.410 -22.200 4.549  1.00 77.86  ? 395 GLN   A CD  1 
ATOM   718  O  OE1 . GLN   A 1 99  ? -25.668 -21.039 4.882  1.00 80.15  ? 395 GLN   A OE1 1 
ATOM   719  N  NE2 . GLN   A 1 99  ? -24.188 -22.716 4.633  1.00 78.81  ? 395 GLN   A NE2 1 
ATOM   720  N  N   . LEU   A 1 100 ? -29.375 -21.554 7.305  1.00 65.49  ? 396 LEU   A N   1 
ATOM   721  C  CA  . LEU   A 1 100 ? -30.637 -21.022 7.796  1.00 59.60  ? 396 LEU   A CA  1 
ATOM   722  C  C   . LEU   A 1 100 ? -31.449 -20.395 6.671  1.00 64.79  ? 396 LEU   A C   1 
ATOM   723  O  O   . LEU   A 1 100 ? -30.894 -19.760 5.772  1.00 64.09  ? 396 LEU   A O   1 
ATOM   724  C  CB  . LEU   A 1 100 ? -30.383 -19.964 8.860  1.00 53.61  ? 396 LEU   A CB  1 
ATOM   725  C  CG  . LEU   A 1 100 ? -29.769 -20.533 10.138 1.00 55.76  ? 396 LEU   A CG  1 
ATOM   726  C  CD1 . LEU   A 1 100 ? -29.271 -19.413 11.016 1.00 57.66  ? 396 LEU   A CD1 1 
ATOM   727  C  CD2 . LEU   A 1 100 ? -30.813 -21.357 10.860 1.00 66.49  ? 396 LEU   A CD2 1 
ATOM   728  N  N   . LYS   A 1 101 ? -32.770 -20.551 6.750  1.00 65.79  ? 397 LYS   A N   1 
ATOM   729  C  CA  . LYS   A 1 101 ? -33.664 -19.746 5.928  1.00 72.69  ? 397 LYS   A CA  1 
ATOM   730  C  C   . LYS   A 1 101 ? -33.559 -18.281 6.335  1.00 72.42  ? 397 LYS   A C   1 
ATOM   731  O  O   . LYS   A 1 101 ? -33.224 -17.959 7.477  1.00 70.13  ? 397 LYS   A O   1 
ATOM   732  C  CB  . LYS   A 1 101 ? -35.110 -20.219 6.078  1.00 72.73  ? 397 LYS   A CB  1 
ATOM   733  C  CG  . LYS   A 1 101 ? -35.374 -21.614 5.569  1.00 78.60  ? 397 LYS   A CG  1 
ATOM   734  C  CD  . LYS   A 1 101 ? -35.233 -21.643 4.073  1.00 84.11  ? 397 LYS   A CD  1 
ATOM   735  C  CE  . LYS   A 1 101 ? -35.260 -23.053 3.548  1.00 92.10  ? 397 LYS   A CE  1 
ATOM   736  N  NZ  . LYS   A 1 101 ? -34.916 -23.065 2.099  1.00 93.07  ? 397 LYS   A NZ  1 
ATOM   737  N  N   . ASP   A 1 102 ? -33.847 -17.384 5.386  1.00 60.89  ? 398 ASP   A N   1 
ATOM   738  C  CA  . ASP   A 1 102 ? -33.870 -15.957 5.709  1.00 67.16  ? 398 ASP   A CA  1 
ATOM   739  C  C   . ASP   A 1 102 ? -34.769 -15.670 6.907  1.00 66.67  ? 398 ASP   A C   1 
ATOM   740  O  O   . ASP   A 1 102 ? -34.421 -14.864 7.780  1.00 64.31  ? 398 ASP   A O   1 
ATOM   741  C  CB  . ASP   A 1 102 ? -34.342 -15.139 4.508  1.00 82.06  ? 398 ASP   A CB  1 
ATOM   742  C  CG  . ASP   A 1 102 ? -33.248 -14.897 3.494  1.00 90.14  ? 398 ASP   A CG  1 
ATOM   743  O  OD1 . ASP   A 1 102 ? -32.158 -15.495 3.622  1.00 90.97  ? 398 ASP   A OD1 1 
ATOM   744  O  OD2 . ASP   A 1 102 ? -33.483 -14.095 2.566  1.00 92.96  ? 398 ASP   A OD2 1 
ATOM   745  N  N   . THR   A 1 103 ? -35.934 -16.318 6.963  1.00 66.14  ? 399 THR   A N   1 
ATOM   746  C  CA  . THR   A 1 103 ? -36.828 -16.127 8.102  1.00 73.01  ? 399 THR   A CA  1 
ATOM   747  C  C   . THR   A 1 103 ? -36.190 -16.609 9.400  1.00 74.83  ? 399 THR   A C   1 
ATOM   748  O  O   . THR   A 1 103 ? -36.350 -15.984 10.457 1.00 72.97  ? 399 THR   A O   1 
ATOM   749  C  CB  . THR   A 1 103 ? -38.133 -16.873 7.858  1.00 74.95  ? 399 THR   A CB  1 
ATOM   750  O  OG1 . THR   A 1 103 ? -37.834 -18.235 7.532  1.00 81.22  ? 399 THR   A OG1 1 
ATOM   751  C  CG2 . THR   A 1 103 ? -38.912 -16.239 6.732  1.00 66.87  ? 399 THR   A CG2 1 
ATOM   752  N  N   . GLU   A 1 104 ? -35.475 -17.733 9.337  1.00 76.87  ? 400 GLU   A N   1 
ATOM   753  C  CA  . GLU   A 1 104 ? -34.835 -18.299 10.516 1.00 72.16  ? 400 GLU   A CA  1 
ATOM   754  C  C   . GLU   A 1 104 ? -33.692 -17.420 10.997 1.00 69.15  ? 400 GLU   A C   1 
ATOM   755  O  O   . GLU   A 1 104 ? -33.489 -17.251 12.212 1.00 67.87  ? 400 GLU   A O   1 
ATOM   756  C  CB  . GLU   A 1 104 ? -34.336 -19.702 10.186 1.00 67.90  ? 400 GLU   A CB  1 
ATOM   757  C  CG  . GLU   A 1 104 ? -35.456 -20.650 9.886  1.00 66.59  ? 400 GLU   A CG  1 
ATOM   758  C  CD  . GLU   A 1 104 ? -34.992 -21.944 9.246  1.00 78.45  ? 400 GLU   A CD  1 
ATOM   759  O  OE1 . GLU   A 1 104 ? -35.850 -22.820 9.029  1.00 84.92  ? 400 GLU   A OE1 1 
ATOM   760  O  OE2 . GLU   A 1 104 ? -33.782 -22.087 8.954  1.00 81.42  ? 400 GLU   A OE2 1 
ATOM   761  N  N   . LEU   A 1 105 ? -32.934 -16.859 10.053 1.00 59.76  ? 401 LEU   A N   1 
ATOM   762  C  CA  . LEU   A 1 105 ? -31.851 -15.950 10.403 1.00 64.54  ? 401 LEU   A CA  1 
ATOM   763  C  C   . LEU   A 1 105 ? -32.379 -14.724 11.136 1.00 64.10  ? 401 LEU   A C   1 
ATOM   764  O  O   . LEU   A 1 105 ? -31.803 -14.307 12.144 1.00 55.30  ? 401 LEU   A O   1 
ATOM   765  C  CB  . LEU   A 1 105 ? -31.078 -15.547 9.148  1.00 62.18  ? 401 LEU   A CB  1 
ATOM   766  C  CG  . LEU   A 1 105 ? -29.750 -14.814 9.351  1.00 56.46  ? 401 LEU   A CG  1 
ATOM   767  C  CD1 . LEU   A 1 105 ? -28.638 -15.763 9.756  1.00 54.99  ? 401 LEU   A CD1 1 
ATOM   768  C  CD2 . LEU   A 1 105 ? -29.377 -14.083 8.068  1.00 59.05  ? 401 LEU   A CD2 1 
ATOM   769  N  N   . ILE   A 1 106 ? -33.492 -14.154 10.669 1.00 60.56  ? 402 ILE   A N   1 
ATOM   770  C  CA  . ILE   A 1 106 ? -34.041 -12.958 11.311 1.00 62.03  ? 402 ILE   A CA  1 
ATOM   771  C  C   . ILE   A 1 106 ? -34.593 -13.297 12.696 1.00 61.56  ? 402 ILE   A C   1 
ATOM   772  O  O   . ILE   A 1 106 ? -34.366 -12.570 13.676 1.00 61.39  ? 402 ILE   A O   1 
ATOM   773  C  CB  . ILE   A 1 106 ? -35.103 -12.320 10.389 1.00 64.60  ? 402 ILE   A CB  1 
ATOM   774  C  CG1 . ILE   A 1 106 ? -34.430 -11.813 9.115  1.00 61.66  ? 402 ILE   A CG1 1 
ATOM   775  C  CG2 . ILE   A 1 106 ? -35.830 -11.177 11.085 1.00 67.36  ? 402 ILE   A CG2 1 
ATOM   776  C  CD1 . ILE   A 1 106 ? -35.388 -11.513 7.950  1.00 61.12  ? 402 ILE   A CD1 1 
ATOM   777  N  N   . TYR   A 1 107 ? -35.316 -14.415 12.800 1.00 61.99  ? 403 TYR   A N   1 
ATOM   778  C  CA  . TYR   A 1 107 ? -35.782 -14.891 14.095 1.00 65.17  ? 403 TYR   A CA  1 
ATOM   779  C  C   . TYR   A 1 107 ? -34.608 -15.114 15.041 1.00 65.80  ? 403 TYR   A C   1 
ATOM   780  O  O   . TYR   A 1 107 ? -34.579 -14.574 16.157 1.00 57.28  ? 403 TYR   A O   1 
ATOM   781  C  CB  . TYR   A 1 107 ? -36.588 -16.182 13.914 1.00 71.36  ? 403 TYR   A CB  1 
ATOM   782  C  CG  . TYR   A 1 107 ? -36.974 -16.833 15.224 1.00 75.03  ? 403 TYR   A CG  1 
ATOM   783  C  CD1 . TYR   A 1 107 ? -38.217 -16.606 15.794 1.00 80.54  ? 403 TYR   A CD1 1 
ATOM   784  C  CD2 . TYR   A 1 107 ? -36.093 -17.675 15.892 1.00 75.54  ? 403 TYR   A CD2 1 
ATOM   785  C  CE1 . TYR   A 1 107 ? -38.571 -17.204 17.005 1.00 79.43  ? 403 TYR   A CE1 1 
ATOM   786  C  CE2 . TYR   A 1 107 ? -36.428 -18.263 17.100 1.00 73.46  ? 403 TYR   A CE2 1 
ATOM   787  C  CZ  . TYR   A 1 107 ? -37.670 -18.027 17.652 1.00 75.22  ? 403 TYR   A CZ  1 
ATOM   788  O  OH  . TYR   A 1 107 ? -38.008 -18.622 18.850 1.00 70.50  ? 403 TYR   A OH  1 
ATOM   789  N  N   . GLY   A 1 108 ? -33.624 -15.910 14.606 1.00 58.27  ? 404 GLY   A N   1 
ATOM   790  C  CA  . GLY   A 1 108 ? -32.469 -16.186 15.452 1.00 55.79  ? 404 GLY   A CA  1 
ATOM   791  C  C   . GLY   A 1 108 ? -31.767 -14.929 15.924 1.00 62.16  ? 404 GLY   A C   1 
ATOM   792  O  O   . GLY   A 1 108 ? -31.453 -14.789 17.106 1.00 52.50  ? 404 GLY   A O   1 
ATOM   793  N  N   . ALA   A 1 109 ? -31.499 -14.000 15.004 1.00 63.03  ? 405 ALA   A N   1 
ATOM   794  C  CA  . ALA   A 1 109 ? -30.822 -12.768 15.397 1.00 58.34  ? 405 ALA   A CA  1 
ATOM   795  C  C   . ALA   A 1 109 ? -31.648 -11.986 16.406 1.00 57.69  ? 405 ALA   A C   1 
ATOM   796  O  O   . ALA   A 1 109 ? -31.125 -11.530 17.432 1.00 56.41  ? 405 ALA   A O   1 
ATOM   797  C  CB  . ALA   A 1 109 ? -30.532 -11.907 14.163 1.00 52.60  ? 405 ALA   A CB  1 
ATOM   798  N  N   . LYS   A 1 110 ? -32.947 -11.822 16.136 1.00 49.27  ? 406 LYS   A N   1 
ATOM   799  C  CA  . LYS   A 1 110 ? -33.778 -11.035 17.041 1.00 57.02  ? 406 LYS   A CA  1 
ATOM   800  C  C   . LYS   A 1 110 ? -33.806 -11.643 18.433 1.00 60.10  ? 406 LYS   A C   1 
ATOM   801  O  O   . LYS   A 1 110 ? -33.887 -10.913 19.430 1.00 63.40  ? 406 LYS   A O   1 
ATOM   802  C  CB  . LYS   A 1 110 ? -35.197 -10.913 16.497 1.00 61.73  ? 406 LYS   A CB  1 
ATOM   803  C  CG  . LYS   A 1 110 ? -35.345 -9.844  15.436 1.00 56.18  ? 406 LYS   A CG  1 
ATOM   804  C  CD  . LYS   A 1 110 ? -36.740 -9.865  14.835 1.00 59.52  ? 406 LYS   A CD  1 
ATOM   805  C  CE  . LYS   A 1 110 ? -36.873 -8.803  13.762 1.00 61.96  ? 406 LYS   A CE  1 
ATOM   806  N  NZ  . LYS   A 1 110 ? -38.298 -8.553  13.421 1.00 70.40  ? 406 LYS   A NZ  1 
ATOM   807  N  N   . HIS   A 1 111 ? -33.735 -12.969 18.520 1.00 56.43  ? 407 HIS   A N   1 
ATOM   808  C  CA  . HIS   A 1 111 ? -33.795 -13.635 19.813 1.00 57.64  ? 407 HIS   A CA  1 
ATOM   809  C  C   . HIS   A 1 111 ? -32.444 -13.726 20.502 1.00 61.03  ? 407 HIS   A C   1 
ATOM   810  O  O   . HIS   A 1 111 ? -32.390 -13.762 21.743 1.00 54.60  ? 407 HIS   A O   1 
ATOM   811  C  CB  . HIS   A 1 111 ? -34.430 -15.011 19.648 1.00 59.10  ? 407 HIS   A CB  1 
ATOM   812  C  CG  . HIS   A 1 111 ? -35.917 -14.946 19.542 1.00 64.57  ? 407 HIS   A CG  1 
ATOM   813  N  ND1 . HIS   A 1 111 ? -36.560 -14.535 18.395 1.00 66.17  ? 407 HIS   A ND1 1 
ATOM   814  C  CD2 . HIS   A 1 111 ? -36.886 -15.174 20.460 1.00 63.53  ? 407 HIS   A CD2 1 
ATOM   815  C  CE1 . HIS   A 1 111 ? -37.865 -14.542 18.600 1.00 68.73  ? 407 HIS   A CE1 1 
ATOM   816  N  NE2 . HIS   A 1 111 ? -38.090 -14.929 19.843 1.00 72.31  ? 407 HIS   A NE2 1 
ATOM   817  N  N   . ALA   A 1 112 ? -31.353 -13.736 19.734 1.00 55.47  ? 408 ALA   A N   1 
ATOM   818  C  CA  . ALA   A 1 112 ? -30.038 -13.506 20.323 1.00 48.99  ? 408 ALA   A CA  1 
ATOM   819  C  C   . ALA   A 1 112 ? -29.999 -12.184 21.078 1.00 55.02  ? 408 ALA   A C   1 
ATOM   820  O  O   . ALA   A 1 112 ? -29.392 -12.087 22.155 1.00 53.62  ? 408 ALA   A O   1 
ATOM   821  C  CB  . ALA   A 1 112 ? -28.969 -13.523 19.232 1.00 48.32  ? 408 ALA   A CB  1 
ATOM   822  N  N   . TRP   A 1 113 ? -30.657 -11.155 20.542 1.00 47.43  ? 409 TRP   A N   1 
ATOM   823  C  CA  . TRP   A 1 113 ? -30.738 -9.886  21.264 1.00 50.09  ? 409 TRP   A CA  1 
ATOM   824  C  C   . TRP   A 1 113 ? -31.680 -9.999  22.461 1.00 50.48  ? 409 TRP   A C   1 
ATOM   825  O  O   . TRP   A 1 113 ? -31.331 -9.613  23.584 1.00 57.46  ? 409 TRP   A O   1 
ATOM   826  C  CB  . TRP   A 1 113 ? -31.198 -8.792  20.302 1.00 45.89  ? 409 TRP   A CB  1 
ATOM   827  C  CG  . TRP   A 1 113 ? -31.323 -7.435  20.901 1.00 46.26  ? 409 TRP   A CG  1 
ATOM   828  C  CD1 . TRP   A 1 113 ? -30.894 -7.019  22.139 1.00 48.16  ? 409 TRP   A CD1 1 
ATOM   829  C  CD2 . TRP   A 1 113 ? -31.915 -6.298  20.280 1.00 51.44  ? 409 TRP   A CD2 1 
ATOM   830  N  NE1 . TRP   A 1 113 ? -31.195 -5.689  22.318 1.00 49.19  ? 409 TRP   A NE1 1 
ATOM   831  C  CE2 . TRP   A 1 113 ? -31.830 -5.226  21.195 1.00 54.90  ? 409 TRP   A CE2 1 
ATOM   832  C  CE3 . TRP   A 1 113 ? -32.525 -6.084  19.038 1.00 51.96  ? 409 TRP   A CE3 1 
ATOM   833  C  CZ2 . TRP   A 1 113 ? -32.314 -3.959  20.900 1.00 55.20  ? 409 TRP   A CZ2 1 
ATOM   834  C  CZ3 . TRP   A 1 113 ? -33.010 -4.832  18.749 1.00 60.74  ? 409 TRP   A CZ3 1 
ATOM   835  C  CH2 . TRP   A 1 113 ? -32.907 -3.782  19.680 1.00 61.24  ? 409 TRP   A CH2 1 
ATOM   836  N  N   . ARG   A 1 114 ? -32.883 -10.526 22.229 1.00 51.28  ? 410 ARG   A N   1 
ATOM   837  C  CA  . ARG   A 1 114 ? -33.862 -10.739 23.284 1.00 54.64  ? 410 ARG   A CA  1 
ATOM   838  C  C   . ARG   A 1 114 ? -33.278 -11.496 24.461 1.00 61.31  ? 410 ARG   A C   1 
ATOM   839  O  O   . ARG   A 1 114 ? -33.660 -11.245 25.614 1.00 56.39  ? 410 ARG   A O   1 
ATOM   840  C  CB  . ARG   A 1 114 ? -35.054 -11.501 22.715 1.00 56.86  ? 410 ARG   A CB  1 
ATOM   841  C  CG  . ARG   A 1 114 ? -36.245 -11.612 23.627 1.00 59.20  ? 410 ARG   A CG  1 
ATOM   842  C  CD  . ARG   A 1 114 ? -37.310 -12.517 23.001 1.00 58.05  ? 410 ARG   A CD  1 
ATOM   843  N  NE  . ARG   A 1 114 ? -38.588 -12.410 23.704 1.00 65.28  ? 410 ARG   A NE  1 
ATOM   844  C  CZ  . ARG   A 1 114 ? -39.699 -13.035 23.331 1.00 75.13  ? 410 ARG   A CZ  1 
ATOM   845  N  NH1 . ARG   A 1 114 ? -40.816 -12.871 24.024 1.00 75.19  ? 410 ARG   A NH1 1 
ATOM   846  N  NH2 . ARG   A 1 114 ? -39.697 -13.812 22.254 1.00 78.98  ? 410 ARG   A NH2 1 
ATOM   847  N  N   . ASN   A 1 115 ? -32.340 -12.402 24.193 1.00 58.70  ? 411 ASN   A N   1 
ATOM   848  C  CA  . ASN   A 1 115 ? -31.738 -13.240 25.221 1.00 56.52  ? 411 ASN   A CA  1 
ATOM   849  C  C   . ASN   A 1 115 ? -30.491 -12.641 25.843 1.00 53.57  ? 411 ASN   A C   1 
ATOM   850  O  O   . ASN   A 1 115 ? -29.926 -13.243 26.771 1.00 51.72  ? 411 ASN   A O   1 
ATOM   851  C  CB  . ASN   A 1 115 ? -31.397 -14.604 24.635 1.00 49.59  ? 411 ASN   A CB  1 
ATOM   852  C  CG  . ASN   A 1 115 ? -32.622 -15.388 24.275 1.00 58.54  ? 411 ASN   A CG  1 
ATOM   853  O  OD1 . ASN   A 1 115 ? -33.712 -15.100 24.760 1.00 60.61  ? 411 ASN   A OD1 1 
ATOM   854  N  ND2 . ASN   A 1 115 ? -32.458 -16.393 23.412 1.00 57.42  ? 411 ASN   A ND2 1 
ATOM   855  N  N   . ALA   A 1 116 ? -30.047 -11.487 25.350 1.00 49.77  ? 412 ALA   A N   1 
ATOM   856  C  CA  . ALA   A 1 116 ? -28.831 -10.848 25.843 1.00 48.54  ? 412 ALA   A CA  1 
ATOM   857  C  C   . ALA   A 1 116 ? -29.056 -10.314 27.254 1.00 48.15  ? 412 ALA   A C   1 
ATOM   858  O  O   . ALA   A 1 116 ? -29.577 -9.213  27.433 1.00 50.41  ? 412 ALA   A O   1 
ATOM   859  C  CB  . ALA   A 1 116 ? -28.404 -9.727  24.888 1.00 48.48  ? 412 ALA   A CB  1 
ATOM   860  N  N   . SER   A 1 117 ? -28.657 -11.070 28.270 1.00 47.78  ? 413 SER   A N   1 
ATOM   861  C  CA  . SER   A 1 117 ? -29.053 -10.696 29.619 1.00 48.73  ? 413 SER   A CA  1 
ATOM   862  C  C   . SER   A 1 117 ? -28.350 -9.425  30.089 1.00 52.58  ? 413 SER   A C   1 
ATOM   863  O  O   . SER   A 1 117 ? -28.831 -8.747  31.011 1.00 48.44  ? 413 SER   A O   1 
ATOM   864  C  CB  . SER   A 1 117 ? -28.789 -11.862 30.572 1.00 53.89  ? 413 SER   A CB  1 
ATOM   865  O  OG  . SER   A 1 117 ? -27.438 -12.273 30.527 1.00 54.70  ? 413 SER   A OG  1 
ATOM   866  N  N   . ARG   A 1 118 ? -27.225 -9.076  29.475 1.00 45.49  ? 414 ARG   A N   1 
ATOM   867  C  CA  . ARG   A 1 118 ? -26.514 -7.858  29.840 1.00 47.42  ? 414 ARG   A CA  1 
ATOM   868  C  C   . ARG   A 1 118 ? -27.038 -6.600  29.149 1.00 50.66  ? 414 ARG   A C   1 
ATOM   869  O  O   . ARG   A 1 118 ? -26.491 -5.513  29.389 1.00 46.30  ? 414 ARG   A O   1 
ATOM   870  C  CB  . ARG   A 1 118 ? -25.031 -8.035  29.536 1.00 50.98  ? 414 ARG   A CB  1 
ATOM   871  C  CG  . ARG   A 1 118 ? -24.389 -9.065  30.469 1.00 47.77  ? 414 ARG   A CG  1 
ATOM   872  C  CD  . ARG   A 1 118 ? -22.896 -9.157  30.225 1.00 55.57  ? 414 ARG   A CD  1 
ATOM   873  N  NE  . ARG   A 1 118 ? -22.248 -9.913  31.292 1.00 56.38  ? 414 ARG   A NE  1 
ATOM   874  C  CZ  . ARG   A 1 118 ? -20.949 -10.181 31.339 1.00 60.29  ? 414 ARG   A CZ  1 
ATOM   875  N  NH1 . ARG   A 1 118 ? -20.149 -9.753  30.376 1.00 62.93  ? 414 ARG   A NH1 1 
ATOM   876  N  NH2 . ARG   A 1 118 ? -20.450 -10.873 32.352 1.00 59.33  ? 414 ARG   A NH2 1 
ATOM   877  N  N   . CYS   A 1 119 ? -28.085 -6.695  28.326 1.00 46.24  ? 415 CYS   A N   1 
ATOM   878  C  CA  . CYS   A 1 119 ? -28.545 -5.561  27.528 1.00 53.38  ? 415 CYS   A CA  1 
ATOM   879  C  C   . CYS   A 1 119 ? -29.776 -4.933  28.164 1.00 52.35  ? 415 CYS   A C   1 
ATOM   880  O  O   . CYS   A 1 119 ? -30.824 -5.578  28.267 1.00 55.36  ? 415 CYS   A O   1 
ATOM   881  C  CB  . CYS   A 1 119 ? -28.874 -5.973  26.090 1.00 47.12  ? 415 CYS   A CB  1 
ATOM   882  S  SG  . CYS   A 1 119 ? -29.629 -4.635  25.154 1.00 48.88  ? 415 CYS   A SG  1 
ATOM   883  N  N   . VAL   A 1 120 ? -29.669 -3.653  28.518 1.00 53.47  ? 416 VAL   A N   1 
ATOM   884  C  CA  . VAL   A 1 120 ? -30.798 -2.945  29.115 1.00 48.95  ? 416 VAL   A CA  1 
ATOM   885  C  C   . VAL   A 1 120 ? -31.760 -2.413  28.060 1.00 53.40  ? 416 VAL   A C   1 
ATOM   886  O  O   . VAL   A 1 120 ? -32.840 -1.914  28.400 1.00 60.63  ? 416 VAL   A O   1 
ATOM   887  C  CB  . VAL   A 1 120 ? -30.214 -1.841  30.022 1.00 48.72  ? 416 VAL   A CB  1 
ATOM   888  C  CG1 . VAL   A 1 120 ? -29.591 -0.710  29.177 1.00 46.45  ? 416 VAL   A CG1 1 
ATOM   889  C  CG2 . VAL   A 1 120 ? -31.269 -1.315  30.996 1.00 55.09  ? 416 VAL   A CG2 1 
ATOM   890  N  N   . GLY   A 1 121 ? -31.429 -2.557  26.782 1.00 51.06  ? 417 GLY   A N   1 
ATOM   891  C  CA  . GLY   A 1 121 ? -32.224 -2.006  25.702 1.00 43.77  ? 417 GLY   A CA  1 
ATOM   892  C  C   . GLY   A 1 121 ? -33.193 -2.960  25.038 1.00 53.88  ? 417 GLY   A C   1 
ATOM   893  O  O   . GLY   A 1 121 ? -33.848 -2.568  24.065 1.00 57.76  ? 417 GLY   A O   1 
ATOM   894  N  N   . ARG   A 1 122 ? -33.353 -4.180  25.559 1.00 56.15  ? 418 ARG   A N   1 
ATOM   895  C  CA  . ARG   A 1 122 ? -34.064 -5.227  24.830 1.00 52.39  ? 418 ARG   A CA  1 
ATOM   896  C  C   . ARG   A 1 122 ? -35.555 -4.984  24.667 1.00 56.19  ? 418 ARG   A C   1 
ATOM   897  O  O   . ARG   A 1 122 ? -36.202 -5.780  23.983 1.00 58.56  ? 418 ARG   A O   1 
ATOM   898  C  CB  . ARG   A 1 122 ? -33.860 -6.566  25.519 1.00 50.26  ? 418 ARG   A CB  1 
ATOM   899  C  CG  . ARG   A 1 122 ? -32.447 -7.045  25.437 1.00 52.52  ? 418 ARG   A CG  1 
ATOM   900  C  CD  . ARG   A 1 122 ? -32.319 -8.314  26.214 1.00 55.37  ? 418 ARG   A CD  1 
ATOM   901  N  NE  . ARG   A 1 122 ? -32.159 -8.089  27.647 1.00 57.88  ? 418 ARG   A NE  1 
ATOM   902  C  CZ  . ARG   A 1 122 ? -32.305 -9.048  28.554 1.00 54.62  ? 418 ARG   A CZ  1 
ATOM   903  N  NH1 . ARG   A 1 122 ? -32.632 -10.270 28.169 1.00 47.46  ? 418 ARG   A NH1 1 
ATOM   904  N  NH2 . ARG   A 1 122 ? -32.120 -8.790  29.846 1.00 57.97  ? 418 ARG   A NH2 1 
ATOM   905  N  N   . ILE   A 1 123 ? -36.139 -3.941  25.261 1.00 59.74  ? 419 ILE   A N   1 
ATOM   906  C  CA  . ILE   A 1 123 ? -37.534 -3.644  24.956 1.00 65.48  ? 419 ILE   A CA  1 
ATOM   907  C  C   . ILE   A 1 123 ? -37.736 -3.492  23.444 1.00 70.57  ? 419 ILE   A C   1 
ATOM   908  O  O   . ILE   A 1 123 ? -38.853 -3.659  22.943 1.00 70.10  ? 419 ILE   A O   1 
ATOM   909  C  CB  . ILE   A 1 123 ? -38.003 -2.386  25.718 1.00 66.90  ? 419 ILE   A CB  1 
ATOM   910  C  CG1 . ILE   A 1 123 ? -39.525 -2.421  25.899 1.00 73.72  ? 419 ILE   A CG1 1 
ATOM   911  C  CG2 . ILE   A 1 123 ? -37.530 -1.108  25.008 1.00 65.54  ? 419 ILE   A CG2 1 
ATOM   912  C  CD1 . ILE   A 1 123 ? -40.182 -1.060  25.899 1.00 86.68  ? 419 ILE   A CD1 1 
ATOM   913  N  N   . GLN   A 1 124 ? -36.665 -3.220  22.701 1.00 70.70  ? 420 GLN   A N   1 
ATOM   914  C  CA  . GLN   A 1 124 ? -36.715 -2.986  21.270 1.00 78.46  ? 420 GLN   A CA  1 
ATOM   915  C  C   . GLN   A 1 124 ? -36.398 -4.227  20.449 1.00 70.37  ? 420 GLN   A C   1 
ATOM   916  O  O   . GLN   A 1 124 ? -36.233 -4.113  19.234 1.00 63.32  ? 420 GLN   A O   1 
ATOM   917  C  CB  . GLN   A 1 124 ? -35.736 -1.868  20.898 1.00 86.18  ? 420 GLN   A CB  1 
ATOM   918  C  CG  . GLN   A 1 124 ? -36.249 -0.462  21.138 1.00 96.90  ? 420 GLN   A CG  1 
ATOM   919  C  CD  . GLN   A 1 124 ? -37.066 0.062   19.974 1.00 103.13 ? 420 GLN   A CD  1 
ATOM   920  O  OE1 . GLN   A 1 124 ? -37.457 -0.693  19.086 1.00 104.25 ? 420 GLN   A OE1 1 
ATOM   921  N  NE2 . GLN   A 1 124 ? -37.324 1.363   19.973 1.00 110.48 ? 420 GLN   A NE2 1 
ATOM   922  N  N   . TRP   A 1 125 ? -36.331 -5.407  21.074 1.00 65.87  ? 421 TRP   A N   1 
ATOM   923  C  CA  . TRP   A 1 125 ? -35.661 -6.545  20.443 1.00 57.46  ? 421 TRP   A CA  1 
ATOM   924  C  C   . TRP   A 1 125 ? -36.351 -6.989  19.157 1.00 62.53  ? 421 TRP   A C   1 
ATOM   925  O  O   . TRP   A 1 125 ? -35.681 -7.423  18.215 1.00 64.09  ? 421 TRP   A O   1 
ATOM   926  C  CB  . TRP   A 1 125 ? -35.573 -7.711  21.430 1.00 55.16  ? 421 TRP   A CB  1 
ATOM   927  C  CG  . TRP   A 1 125 ? -36.889 -8.358  21.692 1.00 61.89  ? 421 TRP   A CG  1 
ATOM   928  C  CD1 . TRP   A 1 125 ? -37.760 -8.071  22.706 1.00 66.05  ? 421 TRP   A CD1 1 
ATOM   929  C  CD2 . TRP   A 1 125 ? -37.497 -9.403  20.925 1.00 65.64  ? 421 TRP   A CD2 1 
ATOM   930  N  NE1 . TRP   A 1 125 ? -38.871 -8.872  22.615 1.00 66.04  ? 421 TRP   A NE1 1 
ATOM   931  C  CE2 . TRP   A 1 125 ? -38.735 -9.698  21.530 1.00 69.62  ? 421 TRP   A CE2 1 
ATOM   932  C  CE3 . TRP   A 1 125 ? -37.114 -10.118 19.787 1.00 59.88  ? 421 TRP   A CE3 1 
ATOM   933  C  CZ2 . TRP   A 1 125 ? -39.590 -10.678 21.035 1.00 67.96  ? 421 TRP   A CZ2 1 
ATOM   934  C  CZ3 . TRP   A 1 125 ? -37.963 -11.093 19.300 1.00 65.07  ? 421 TRP   A CZ3 1 
ATOM   935  C  CH2 . TRP   A 1 125 ? -39.187 -11.364 19.924 1.00 70.85  ? 421 TRP   A CH2 1 
ATOM   936  N  N   . SER   A 1 126 ? -37.679 -6.895  19.097 1.00 67.40  ? 422 SER   A N   1 
ATOM   937  C  CA  . SER   A 1 126 ? -38.410 -7.325  17.918 1.00 75.64  ? 422 SER   A CA  1 
ATOM   938  C  C   . SER   A 1 126 ? -38.295 -6.330  16.769 1.00 77.42  ? 422 SER   A C   1 
ATOM   939  O  O   . SER   A 1 126 ? -38.610 -6.681  15.630 1.00 77.93  ? 422 SER   A O   1 
ATOM   940  C  CB  . SER   A 1 126 ? -39.879 -7.555  18.277 1.00 77.07  ? 422 SER   A CB  1 
ATOM   941  O  OG  . SER   A 1 126 ? -40.564 -6.330  18.468 1.00 75.96  ? 422 SER   A OG  1 
ATOM   942  N  N   . LYS   A 1 127 ? -37.855 -5.101  17.045 1.00 77.25  ? 423 LYS   A N   1 
ATOM   943  C  CA  . LYS   A 1 127 ? -37.581 -4.115  16.004 1.00 69.36  ? 423 LYS   A CA  1 
ATOM   944  C  C   . LYS   A 1 127 ? -36.078 -4.126  15.747 1.00 73.17  ? 423 LYS   A C   1 
ATOM   945  O  O   . LYS   A 1 127 ? -35.314 -3.316  16.271 1.00 74.44  ? 423 LYS   A O   1 
ATOM   946  C  CB  . LYS   A 1 127 ? -38.082 -2.731  16.399 1.00 68.83  ? 423 LYS   A CB  1 
ATOM   947  C  CG  . LYS   A 1 127 ? -39.594 -2.608  16.431 1.00 80.23  ? 423 LYS   A CG  1 
ATOM   948  C  CD  . LYS   A 1 127 ? -40.030 -1.184  16.115 1.00 96.24  ? 423 LYS   A CD  1 
ATOM   949  C  CE  . LYS   A 1 127 ? -39.571 -0.760  14.727 1.00 101.95 ? 423 LYS   A CE  1 
ATOM   950  N  NZ  . LYS   A 1 127 ? -39.630 0.717   14.550 1.00 107.65 ? 423 LYS   A NZ  1 
ATOM   951  N  N   . LEU   A 1 128 ? -35.656 -5.080  14.929 1.00 72.88  ? 424 LEU   A N   1 
ATOM   952  C  CA  . LEU   A 1 128 ? -34.262 -5.222  14.542 1.00 66.07  ? 424 LEU   A CA  1 
ATOM   953  C  C   . LEU   A 1 128 ? -34.223 -5.461  13.044 1.00 62.67  ? 424 LEU   A C   1 
ATOM   954  O  O   . LEU   A 1 128 ? -34.935 -6.334  12.542 1.00 66.47  ? 424 LEU   A O   1 
ATOM   955  C  CB  . LEU   A 1 128 ? -33.594 -6.386  15.280 1.00 53.42  ? 424 LEU   A CB  1 
ATOM   956  C  CG  . LEU   A 1 128 ? -32.124 -6.671  14.955 1.00 52.23  ? 424 LEU   A CG  1 
ATOM   957  C  CD1 . LEU   A 1 128 ? -31.257 -5.527  15.411 1.00 52.16  ? 424 LEU   A CD1 1 
ATOM   958  C  CD2 . LEU   A 1 128 ? -31.631 -7.981  15.582 1.00 48.98  ? 424 LEU   A CD2 1 
ATOM   959  N  N   . GLN   A 1 129 ? -33.412 -4.682  12.339 1.00 63.80  ? 425 GLN   A N   1 
ATOM   960  C  CA  . GLN   A 1 129 ? -33.249 -4.834  10.898 1.00 64.32  ? 425 GLN   A CA  1 
ATOM   961  C  C   . GLN   A 1 129 ? -32.084 -5.773  10.646 1.00 60.98  ? 425 GLN   A C   1 
ATOM   962  O  O   . GLN   A 1 129 ? -30.952 -5.484  11.044 1.00 62.63  ? 425 GLN   A O   1 
ATOM   963  C  CB  . GLN   A 1 129 ? -33.000 -3.484  10.228 1.00 67.25  ? 425 GLN   A CB  1 
ATOM   964  C  CG  . GLN   A 1 129 ? -32.813 -3.555  8.711  1.00 69.65  ? 425 GLN   A CG  1 
ATOM   965  C  CD  . GLN   A 1 129 ? -33.989 -4.193  7.997  1.00 79.80  ? 425 GLN   A CD  1 
ATOM   966  O  OE1 . GLN   A 1 129 ? -35.134 -4.107  8.452  1.00 85.21  ? 425 GLN   A OE1 1 
ATOM   967  N  NE2 . GLN   A 1 129 ? -33.710 -4.840  6.868  1.00 78.13  ? 425 GLN   A NE2 1 
ATOM   968  N  N   . VAL   A 1 130 ? -32.355 -6.902  10.016 1.00 59.78  ? 426 VAL   A N   1 
ATOM   969  C  CA  . VAL   A 1 130 ? -31.341 -7.929  9.848  1.00 57.26  ? 426 VAL   A CA  1 
ATOM   970  C  C   . VAL   A 1 130 ? -30.834 -7.839  8.420  1.00 54.52  ? 426 VAL   A C   1 
ATOM   971  O  O   . VAL   A 1 130 ? -31.620 -7.931  7.472  1.00 55.09  ? 426 VAL   A O   1 
ATOM   972  C  CB  . VAL   A 1 130 ? -31.896 -9.325  10.168 1.00 57.19  ? 426 VAL   A CB  1 
ATOM   973  C  CG1 . VAL   A 1 130 ? -30.815 -10.367 9.966  1.00 60.79  ? 426 VAL   A CG1 1 
ATOM   974  C  CG2 . VAL   A 1 130 ? -32.432 -9.357  11.606 1.00 51.24  ? 426 VAL   A CG2 1 
ATOM   975  N  N   . PHE   A 1 131 ? -29.533 -7.638  8.267  1.00 54.16  ? 427 PHE   A N   1 
ATOM   976  C  CA  . PHE   A 1 131 ? -28.908 -7.540  6.959  1.00 55.87  ? 427 PHE   A CA  1 
ATOM   977  C  C   . PHE   A 1 131 ? -28.162 -8.834  6.684  1.00 51.66  ? 427 PHE   A C   1 
ATOM   978  O  O   . PHE   A 1 131 ? -27.218 -9.179  7.397  1.00 52.34  ? 427 PHE   A O   1 
ATOM   979  C  CB  . PHE   A 1 131 ? -27.972 -6.339  6.882  1.00 54.15  ? 427 PHE   A CB  1 
ATOM   980  C  CG  . PHE   A 1 131 ? -28.687 -5.015  6.838  1.00 54.06  ? 427 PHE   A CG  1 
ATOM   981  C  CD1 . PHE   A 1 131 ? -29.502 -4.681  5.772  1.00 53.35  ? 427 PHE   A CD1 1 
ATOM   982  C  CD2 . PHE   A 1 131 ? -28.563 -4.118  7.884  1.00 55.66  ? 427 PHE   A CD2 1 
ATOM   983  C  CE1 . PHE   A 1 131 ? -30.158 -3.457  5.737  1.00 57.30  ? 427 PHE   A CE1 1 
ATOM   984  C  CE2 . PHE   A 1 131 ? -29.214 -2.904  7.861  1.00 58.47  ? 427 PHE   A CE2 1 
ATOM   985  C  CZ  . PHE   A 1 131 ? -30.000 -2.567  6.804  1.00 58.73  ? 427 PHE   A CZ  1 
ATOM   986  N  N   . ASP   A 1 132 ? -28.594 -9.558  5.660  1.00 60.82  ? 428 ASP   A N   1 
ATOM   987  C  CA  . ASP   A 1 132 ? -28.028 -10.869 5.375  1.00 53.10  ? 428 ASP   A CA  1 
ATOM   988  C  C   . ASP   A 1 132 ? -26.824 -10.672 4.471  1.00 52.32  ? 428 ASP   A C   1 
ATOM   989  O  O   . ASP   A 1 132 ? -26.968 -10.306 3.306  1.00 55.35  ? 428 ASP   A O   1 
ATOM   990  C  CB  . ASP   A 1 132 ? -29.080 -11.777 4.760  1.00 47.58  ? 428 ASP   A CB  1 
ATOM   991  C  CG  . ASP   A 1 132 ? -28.557 -13.183 4.500  1.00 56.78  ? 428 ASP   A CG  1 
ATOM   992  O  OD1 . ASP   A 1 132 ? -29.358 -14.036 4.064  1.00 60.54  ? 428 ASP   A OD1 1 
ATOM   993  O  OD2 . ASP   A 1 132 ? -27.355 -13.439 4.739  1.00 60.24  ? 428 ASP   A OD2 1 
ATOM   994  N  N   . ALA   A 1 133 ? -25.633 -10.877 5.021  1.00 50.83  ? 429 ALA   A N   1 
ATOM   995  C  CA  . ALA   A 1 133 ? -24.396 -10.734 4.267  1.00 53.66  ? 429 ALA   A CA  1 
ATOM   996  C  C   . ALA   A 1 133 ? -23.710 -12.075 4.079  1.00 53.02  ? 429 ALA   A C   1 
ATOM   997  O  O   . ALA   A 1 133 ? -22.490 -12.129 3.902  1.00 59.65  ? 429 ALA   A O   1 
ATOM   998  C  CB  . ALA   A 1 133 ? -23.462 -9.746  4.971  1.00 54.13  ? 429 ALA   A CB  1 
ATOM   999  N  N   . ARG   A 1 134 ? -24.474 -13.161 4.150  1.00 55.93  ? 430 ARG   A N   1 
ATOM   1000 C  CA  . ARG   A 1 134 ? -23.915 -14.494 4.014  1.00 57.64  ? 430 ARG   A CA  1 
ATOM   1001 C  C   . ARG   A 1 134 ? -23.458 -14.813 2.594  1.00 60.16  ? 430 ARG   A C   1 
ATOM   1002 O  O   . ARG   A 1 134 ? -22.824 -15.855 2.397  1.00 64.96  ? 430 ARG   A O   1 
ATOM   1003 C  CB  . ARG   A 1 134 ? -24.939 -15.525 4.485  1.00 54.74  ? 430 ARG   A CB  1 
ATOM   1004 C  CG  . ARG   A 1 134 ? -25.053 -15.591 6.023  1.00 52.58  ? 430 ARG   A CG  1 
ATOM   1005 C  CD  . ARG   A 1 134 ? -26.167 -16.530 6.461  1.00 57.33  ? 430 ARG   A CD  1 
ATOM   1006 N  NE  . ARG   A 1 134 ? -27.431 -16.197 5.804  1.00 61.03  ? 430 ARG   A NE  1 
ATOM   1007 C  CZ  . ARG   A 1 134 ? -28.484 -17.006 5.734  1.00 61.07  ? 430 ARG   A CZ  1 
ATOM   1008 N  NH1 . ARG   A 1 134 ? -28.446 -18.217 6.288  1.00 65.95  ? 430 ARG   A NH1 1 
ATOM   1009 N  NH2 . ARG   A 1 134 ? -29.584 -16.597 5.111  1.00 57.90  ? 430 ARG   A NH2 1 
ATOM   1010 N  N   . ASP   A 1 135 ? -23.763 -13.962 1.609  1.00 56.23  ? 431 ASP   A N   1 
ATOM   1011 C  CA  . ASP   A 1 135 ? -23.200 -14.091 0.268  1.00 64.20  ? 431 ASP   A CA  1 
ATOM   1012 C  C   . ASP   A 1 135 ? -21.907 -13.305 0.103  1.00 62.85  ? 431 ASP   A C   1 
ATOM   1013 O  O   . ASP   A 1 135 ? -21.345 -13.285 -0.999 1.00 62.02  ? 431 ASP   A O   1 
ATOM   1014 C  CB  . ASP   A 1 135 ? -24.218 -13.646 -0.808 1.00 66.41  ? 431 ASP   A CB  1 
ATOM   1015 C  CG  . ASP   A 1 135 ? -24.784 -12.249 -0.551 1.00 71.18  ? 431 ASP   A CG  1 
ATOM   1016 O  OD1 . ASP   A 1 135 ? -25.055 -11.918 0.632  1.00 72.00  ? 431 ASP   A OD1 1 
ATOM   1017 O  OD2 . ASP   A 1 135 ? -24.983 -11.497 -1.527 1.00 67.76  ? 431 ASP   A OD2 1 
ATOM   1018 N  N   . CYS   A 1 136 ? -21.434 -12.657 1.164  1.00 57.10  ? 432 CYS   A N   1 
ATOM   1019 C  CA  . CYS   A 1 136 ? -20.165 -11.945 1.126  1.00 56.32  ? 432 CYS   A CA  1 
ATOM   1020 C  C   . CYS   A 1 136 ? -19.013 -12.931 0.957  1.00 64.85  ? 432 CYS   A C   1 
ATOM   1021 O  O   . CYS   A 1 136 ? -19.086 -14.084 1.392  1.00 66.10  ? 432 CYS   A O   1 
ATOM   1022 C  CB  . CYS   A 1 136 ? -19.977 -11.123 2.410  1.00 59.01  ? 432 CYS   A CB  1 
ATOM   1023 S  SG  . CYS   A 1 136 ? -18.654 -9.918  2.312  1.00 61.69  ? 432 CYS   A SG  1 
ATOM   1024 N  N   . THR   A 1 137 ? -17.961 -12.487 0.259  1.00 67.37  ? 433 THR   A N   1 
ATOM   1025 C  CA  . THR   A 1 137 ? -16.787 -13.331 0.052  1.00 59.61  ? 433 THR   A CA  1 
ATOM   1026 C  C   . THR   A 1 137 ? -15.453 -12.626 0.252  1.00 57.36  ? 433 THR   A C   1 
ATOM   1027 O  O   . THR   A 1 137 ? -14.456 -13.311 0.497  1.00 68.85  ? 433 THR   A O   1 
ATOM   1028 C  CB  . THR   A 1 137 ? -16.799 -13.946 -1.359 1.00 66.12  ? 433 THR   A CB  1 
ATOM   1029 O  OG1 . THR   A 1 137 ? -16.842 -12.907 -2.351 1.00 64.29  ? 433 THR   A OG1 1 
ATOM   1030 C  CG2 . THR   A 1 137 ? -17.987 -14.883 -1.542 1.00 71.70  ? 433 THR   A CG2 1 
ATOM   1031 N  N   . THR   A 1 138 ? -15.372 -11.304 0.139  1.00 64.38  ? 434 THR   A N   1 
ATOM   1032 C  CA  . THR   A 1 138 ? -14.125 -10.570 0.309  1.00 66.20  ? 434 THR   A CA  1 
ATOM   1033 C  C   . THR   A 1 138 ? -14.287 -9.515  1.387  1.00 63.41  ? 434 THR   A C   1 
ATOM   1034 O  O   . THR   A 1 138 ? -15.405 -9.161  1.773  1.00 63.31  ? 434 THR   A O   1 
ATOM   1035 C  CB  . THR   A 1 138 ? -13.691 -9.873  -0.996 1.00 67.22  ? 434 THR   A CB  1 
ATOM   1036 O  OG1 . THR   A 1 138 ? -14.655 -8.868  -1.318 1.00 68.20  ? 434 THR   A OG1 1 
ATOM   1037 C  CG2 . THR   A 1 138 ? -13.581 -10.861 -2.116 1.00 70.77  ? 434 THR   A CG2 1 
ATOM   1038 N  N   . ALA   A 1 139 ? -13.145 -9.016  1.872  1.00 74.40  ? 435 ALA   A N   1 
ATOM   1039 C  CA  . ALA   A 1 139 ? -13.164 -7.931  2.846  1.00 66.55  ? 435 ALA   A CA  1 
ATOM   1040 C  C   . ALA   A 1 139 ? -13.750 -6.661  2.248  1.00 71.07  ? 435 ALA   A C   1 
ATOM   1041 O  O   . ALA   A 1 139 ? -14.356 -5.858  2.965  1.00 73.39  ? 435 ALA   A O   1 
ATOM   1042 C  CB  . ALA   A 1 139 ? -11.753 -7.667  3.374  1.00 77.33  ? 435 ALA   A CB  1 
ATOM   1043 N  N   . HIS   A 1 140 ? -13.576 -6.463  0.940  1.00 67.09  ? 436 HIS   A N   1 
ATOM   1044 C  CA  . HIS   A 1 140 ? -14.206 -5.334  0.259  1.00 67.80  ? 436 HIS   A CA  1 
ATOM   1045 C  C   . HIS   A 1 140 ? -15.723 -5.439  0.318  1.00 65.07  ? 436 HIS   A C   1 
ATOM   1046 O  O   . HIS   A 1 140 ? -16.414 -4.444  0.566  1.00 72.79  ? 436 HIS   A O   1 
ATOM   1047 C  CB  . HIS   A 1 140 ? -13.728 -5.259  -1.192 1.00 77.45  ? 436 HIS   A CB  1 
ATOM   1048 C  CG  . HIS   A 1 140 ? -12.419 -4.557  -1.361 1.00 77.12  ? 436 HIS   A CG  1 
ATOM   1049 N  ND1 . HIS   A 1 140 ? -11.241 -5.041  -0.833 1.00 80.60  ? 436 HIS   A ND1 1 
ATOM   1050 C  CD2 . HIS   A 1 140 ? -12.102 -3.404  -1.996 1.00 80.03  ? 436 HIS   A CD2 1 
ATOM   1051 C  CE1 . HIS   A 1 140 ? -10.253 -4.220  -1.143 1.00 86.66  ? 436 HIS   A CE1 1 
ATOM   1052 N  NE2 . HIS   A 1 140 ? -10.748 -3.221  -1.851 1.00 83.43  ? 436 HIS   A NE2 1 
ATOM   1053 N  N   . GLY   A 1 141 ? -16.260 -6.635  0.077  1.00 64.80  ? 437 GLY   A N   1 
ATOM   1054 C  CA  . GLY   A 1 141 ? -17.683 -6.841  0.270  1.00 62.60  ? 437 GLY   A CA  1 
ATOM   1055 C  C   . GLY   A 1 141 ? -18.113 -6.543  1.689  1.00 62.91  ? 437 GLY   A C   1 
ATOM   1056 O  O   . GLY   A 1 141 ? -19.157 -5.926  1.911  1.00 64.24  ? 437 GLY   A O   1 
ATOM   1057 N  N   . MET   A 1 142 ? -17.310 -6.977  2.672  1.00 60.41  ? 438 MET   A N   1 
ATOM   1058 C  CA  . MET   A 1 142 ? -17.612 -6.672  4.070  1.00 54.41  ? 438 MET   A CA  1 
ATOM   1059 C  C   . MET   A 1 142 ? -17.663 -5.169  4.301  1.00 57.07  ? 438 MET   A C   1 
ATOM   1060 O  O   . MET   A 1 142 ? -18.639 -4.642  4.844  1.00 63.37  ? 438 MET   A O   1 
ATOM   1061 C  CB  . MET   A 1 142 ? -16.572 -7.308  4.996  1.00 56.54  ? 438 MET   A CB  1 
ATOM   1062 C  CG  . MET   A 1 142 ? -16.544 -8.818  4.993  1.00 54.27  ? 438 MET   A CG  1 
ATOM   1063 S  SD  . MET   A 1 142 ? -15.249 -9.496  6.066  1.00 60.82  ? 438 MET   A SD  1 
ATOM   1064 C  CE  . MET   A 1 142 ? -15.774 -8.979  7.703  1.00 61.21  ? 438 MET   A CE  1 
ATOM   1065 N  N   . PHE   A 1 143 ? -16.617 -4.460  3.879  1.00 61.72  ? 439 PHE   A N   1 
ATOM   1066 C  CA  . PHE   A 1 143 ? -16.613 -3.003  3.971  1.00 62.12  ? 439 PHE   A CA  1 
ATOM   1067 C  C   . PHE   A 1 143 ? -17.896 -2.409  3.402  1.00 62.79  ? 439 PHE   A C   1 
ATOM   1068 O  O   . PHE   A 1 143 ? -18.528 -1.548  4.024  1.00 60.40  ? 439 PHE   A O   1 
ATOM   1069 C  CB  . PHE   A 1 143 ? -15.393 -2.444  3.246  1.00 72.32  ? 439 PHE   A CB  1 
ATOM   1070 C  CG  . PHE   A 1 143 ? -15.378 -0.954  3.175  1.00 74.55  ? 439 PHE   A CG  1 
ATOM   1071 C  CD1 . PHE   A 1 143 ? -15.416 -0.305  1.954  1.00 71.03  ? 439 PHE   A CD1 1 
ATOM   1072 C  CD2 . PHE   A 1 143 ? -15.359 -0.201  4.329  1.00 67.17  ? 439 PHE   A CD2 1 
ATOM   1073 C  CE1 . PHE   A 1 143 ? -15.412 1.076   1.900  1.00 74.70  ? 439 PHE   A CE1 1 
ATOM   1074 C  CE2 . PHE   A 1 143 ? -15.351 1.167   4.272  1.00 72.93  ? 439 PHE   A CE2 1 
ATOM   1075 C  CZ  . PHE   A 1 143 ? -15.380 1.807   3.076  1.00 73.02  ? 439 PHE   A CZ  1 
ATOM   1076 N  N   . ASN   A 1 144 ? -18.311 -2.885  2.227  1.00 57.69  ? 440 ASN   A N   1 
ATOM   1077 C  CA  . ASN   A 1 144 ? -19.507 -2.358  1.583  1.00 53.72  ? 440 ASN   A CA  1 
ATOM   1078 C  C   . ASN   A 1 144 ? -20.760 -2.674  2.391  1.00 57.99  ? 440 ASN   A C   1 
ATOM   1079 O  O   . ASN   A 1 144 ? -21.635 -1.816  2.567  1.00 63.73  ? 440 ASN   A O   1 
ATOM   1080 C  CB  . ASN   A 1 144 ? -19.630 -2.928  0.172  1.00 66.47  ? 440 ASN   A CB  1 
ATOM   1081 C  CG  . ASN   A 1 144 ? -20.735 -2.273  -0.603 1.00 61.57  ? 440 ASN   A CG  1 
ATOM   1082 O  OD1 . ASN   A 1 144 ? -20.701 -1.071  -0.822 1.00 67.57  ? 440 ASN   A OD1 1 
ATOM   1083 N  ND2 . ASN   A 1 144 ? -21.745 -3.046  -0.974 1.00 57.47  ? 440 ASN   A ND2 1 
ATOM   1084 N  N   . TYR   A 1 145 ? -20.883 -3.915  2.863  1.00 55.10  ? 441 TYR   A N   1 
ATOM   1085 C  CA  . TYR   A 1 145 ? -22.007 -4.267  3.730  1.00 63.01  ? 441 TYR   A CA  1 
ATOM   1086 C  C   . TYR   A 1 145 ? -22.010 -3.444  5.009  1.00 58.75  ? 441 TYR   A C   1 
ATOM   1087 O  O   . TYR   A 1 145 ? -23.071 -3.009  5.477  1.00 59.46  ? 441 TYR   A O   1 
ATOM   1088 C  CB  . TYR   A 1 145 ? -21.952 -5.750  4.078  1.00 58.34  ? 441 TYR   A CB  1 
ATOM   1089 C  CG  . TYR   A 1 145 ? -22.749 -6.654  3.160  1.00 54.41  ? 441 TYR   A CG  1 
ATOM   1090 C  CD1 . TYR   A 1 145 ? -22.127 -7.573  2.363  1.00 47.72  ? 441 TYR   A CD1 1 
ATOM   1091 C  CD2 . TYR   A 1 145 ? -24.132 -6.609  3.150  1.00 58.08  ? 441 TYR   A CD2 1 
ATOM   1092 C  CE1 . TYR   A 1 145 ? -22.859 -8.426  1.535  1.00 55.06  ? 441 TYR   A CE1 1 
ATOM   1093 C  CE2 . TYR   A 1 145 ? -24.869 -7.432  2.373  1.00 56.51  ? 441 TYR   A CE2 1 
ATOM   1094 C  CZ  . TYR   A 1 145 ? -24.234 -8.342  1.552  1.00 58.95  ? 441 TYR   A CZ  1 
ATOM   1095 O  OH  . TYR   A 1 145 ? -25.003 -9.155  0.773  1.00 61.94  ? 441 TYR   A OH  1 
ATOM   1096 N  N   . ILE   A 1 146 ? -20.833 -3.237  5.598  1.00 57.64  ? 442 ILE   A N   1 
ATOM   1097 C  CA  . ILE   A 1 146 ? -20.750 -2.502  6.855  1.00 54.85  ? 442 ILE   A CA  1 
ATOM   1098 C  C   . ILE   A 1 146 ? -21.125 -1.038  6.645  1.00 59.67  ? 442 ILE   A C   1 
ATOM   1099 O  O   . ILE   A 1 146 ? -21.875 -0.457  7.440  1.00 63.02  ? 442 ILE   A O   1 
ATOM   1100 C  CB  . ILE   A 1 146 ? -19.347 -2.663  7.465  1.00 57.45  ? 442 ILE   A CB  1 
ATOM   1101 C  CG1 . ILE   A 1 146 ? -19.197 -4.075  8.048  1.00 57.82  ? 442 ILE   A CG1 1 
ATOM   1102 C  CG2 . ILE   A 1 146 ? -19.111 -1.608  8.546  1.00 51.93  ? 442 ILE   A CG2 1 
ATOM   1103 C  CD1 . ILE   A 1 146 ? -17.833 -4.364  8.618  1.00 64.51  ? 442 ILE   A CD1 1 
ATOM   1104 N  N   . CYS   A 1 147 ? -20.644 -0.431  5.552  1.00 59.14  ? 443 CYS   A N   1 
ATOM   1105 C  CA  . CYS   A 1 147 ? -21.023 0.944   5.222  1.00 50.97  ? 443 CYS   A CA  1 
ATOM   1106 C  C   . CYS   A 1 147 ? -22.528 1.069   5.074  1.00 56.55  ? 443 CYS   A C   1 
ATOM   1107 O  O   . CYS   A 1 147 ? -23.132 2.033   5.558  1.00 63.93  ? 443 CYS   A O   1 
ATOM   1108 C  CB  . CYS   A 1 147 ? -20.358 1.408   3.930  1.00 52.33  ? 443 CYS   A CB  1 
ATOM   1109 S  SG  . CYS   A 1 147 ? -18.655 1.915   4.069  1.00 74.10  ? 443 CYS   A SG  1 
ATOM   1110 N  N   . ASN   A 1 148 ? -23.151 0.119   4.381  1.00 51.81  ? 444 ASN   A N   1 
ATOM   1111 C  CA  . ASN   A 1 148 ? -24.601 0.173   4.239  1.00 59.95  ? 444 ASN   A CA  1 
ATOM   1112 C  C   . ASN   A 1 148 ? -25.279 0.047   5.598  1.00 52.69  ? 444 ASN   A C   1 
ATOM   1113 O  O   . ASN   A 1 148 ? -26.258 0.747   5.876  1.00 54.61  ? 444 ASN   A O   1 
ATOM   1114 C  CB  . ASN   A 1 148 ? -25.086 -0.907  3.275  1.00 64.64  ? 444 ASN   A CB  1 
ATOM   1115 C  CG  . ASN   A 1 148 ? -24.727 -0.597  1.843  1.00 68.46  ? 444 ASN   A CG  1 
ATOM   1116 O  OD1 . ASN   A 1 148 ? -24.268 0.500   1.539  1.00 63.88  ? 444 ASN   A OD1 1 
ATOM   1117 N  ND2 . ASN   A 1 148 ? -24.962 -1.552  0.950  1.00 66.87  ? 444 ASN   A ND2 1 
ATOM   1118 N  N   . HIS   A 1 149 ? -24.763 -0.841  6.456  1.00 52.52  ? 445 HIS   A N   1 
ATOM   1119 C  CA  . HIS   A 1 149 ? -25.249 -0.951  7.829  1.00 57.97  ? 445 HIS   A CA  1 
ATOM   1120 C  C   . HIS   A 1 149 ? -25.134 0.381   8.560  1.00 59.84  ? 445 HIS   A C   1 
ATOM   1121 O  O   . HIS   A 1 149 ? -26.113 0.864   9.141  1.00 57.98  ? 445 HIS   A O   1 
ATOM   1122 C  CB  . HIS   A 1 149 ? -24.469 -2.042  8.563  1.00 55.33  ? 445 HIS   A CB  1 
ATOM   1123 C  CG  . HIS   A 1 149 ? -24.833 -2.202  10.012 1.00 54.84  ? 445 HIS   A CG  1 
ATOM   1124 N  ND1 . HIS   A 1 149 ? -25.087 -3.432  10.580 1.00 50.89  ? 445 HIS   A ND1 1 
ATOM   1125 C  CD2 . HIS   A 1 149 ? -24.953 -1.295  11.013 1.00 52.75  ? 445 HIS   A CD2 1 
ATOM   1126 C  CE1 . HIS   A 1 149 ? -25.364 -3.275  11.866 1.00 49.95  ? 445 HIS   A CE1 1 
ATOM   1127 N  NE2 . HIS   A 1 149 ? -25.291 -1.988  12.154 1.00 54.21  ? 445 HIS   A NE2 1 
ATOM   1128 N  N   . VAL   A 1 150 ? -23.933 0.977   8.564  1.00 57.16  ? 446 VAL   A N   1 
ATOM   1129 C  CA  . VAL   A 1 150 ? -23.731 2.254   9.250  1.00 63.14  ? 446 VAL   A CA  1 
ATOM   1130 C  C   . VAL   A 1 150 ? -24.722 3.292   8.742  1.00 68.31  ? 446 VAL   A C   1 
ATOM   1131 O  O   . VAL   A 1 150 ? -25.440 3.921   9.523  1.00 72.29  ? 446 VAL   A O   1 
ATOM   1132 C  CB  . VAL   A 1 150 ? -22.279 2.737   9.081  1.00 57.00  ? 446 VAL   A CB  1 
ATOM   1133 C  CG1 . VAL   A 1 150 ? -22.121 4.149   9.603  1.00 59.92  ? 446 VAL   A CG1 1 
ATOM   1134 C  CG2 . VAL   A 1 150 ? -21.332 1.836   9.831  1.00 57.50  ? 446 VAL   A CG2 1 
ATOM   1135 N  N   . LYS   A 1 151 ? -24.810 3.459   7.423  1.00 64.10  ? 447 LYS   A N   1 
ATOM   1136 C  CA  . LYS   A 1 151 ? -25.689 4.498   6.897  1.00 69.19  ? 447 LYS   A CA  1 
ATOM   1137 C  C   . LYS   A 1 151 ? -27.142 4.235   7.279  1.00 67.97  ? 447 LYS   A C   1 
ATOM   1138 O  O   . LYS   A 1 151 ? -27.859 5.146   7.714  1.00 69.04  ? 447 LYS   A O   1 
ATOM   1139 C  CB  . LYS   A 1 151 ? -25.535 4.591   5.380  1.00 64.73  ? 447 LYS   A CB  1 
ATOM   1140 C  CG  . LYS   A 1 151 ? -26.226 5.771   4.785  1.00 69.47  ? 447 LYS   A CG  1 
ATOM   1141 C  CD  . LYS   A 1 151 ? -25.762 5.914   3.379  1.00 66.12  ? 447 LYS   A CD  1 
ATOM   1142 C  CE  . LYS   A 1 151 ? -25.868 7.342   2.877  1.00 77.89  ? 447 LYS   A CE  1 
ATOM   1143 N  NZ  . LYS   A 1 151 ? -25.475 7.364   1.467  1.00 71.03  ? 447 LYS   A NZ  1 
ATOM   1144 N  N   . TYR   A 1 152 ? -27.584 2.983   7.144  1.00 61.32  ? 448 TYR   A N   1 
ATOM   1145 C  CA  . TYR   A 1 152 ? -28.942 2.629   7.543  1.00 67.56  ? 448 TYR   A CA  1 
ATOM   1146 C  C   . TYR   A 1 152 ? -29.179 2.893   9.029  1.00 64.75  ? 448 TYR   A C   1 
ATOM   1147 O  O   . TYR   A 1 152 ? -30.116 3.611   9.397  1.00 73.39  ? 448 TYR   A O   1 
ATOM   1148 C  CB  . TYR   A 1 152 ? -29.232 1.162   7.220  1.00 66.08  ? 448 TYR   A CB  1 
ATOM   1149 C  CG  . TYR   A 1 152 ? -30.613 0.749   7.676  1.00 65.60  ? 448 TYR   A CG  1 
ATOM   1150 C  CD1 . TYR   A 1 152 ? -31.716 0.937   6.858  1.00 74.10  ? 448 TYR   A CD1 1 
ATOM   1151 C  CD2 . TYR   A 1 152 ? -30.819 0.196   8.936  1.00 60.94  ? 448 TYR   A CD2 1 
ATOM   1152 C  CE1 . TYR   A 1 152 ? -32.984 0.576   7.275  1.00 75.68  ? 448 TYR   A CE1 1 
ATOM   1153 C  CE2 . TYR   A 1 152 ? -32.079 -0.165  9.358  1.00 60.57  ? 448 TYR   A CE2 1 
ATOM   1154 C  CZ  . TYR   A 1 152 ? -33.155 0.021   8.527  1.00 70.88  ? 448 TYR   A CZ  1 
ATOM   1155 O  OH  . TYR   A 1 152 ? -34.409 -0.347  8.957  1.00 79.46  ? 448 TYR   A OH  1 
ATOM   1156 N  N   . ALA   A 1 153 ? -28.350 2.302   9.903  1.00 55.03  ? 449 ALA   A N   1 
ATOM   1157 C  CA  . ALA   A 1 153 ? -28.614 2.379   11.332 1.00 58.59  ? 449 ALA   A CA  1 
ATOM   1158 C  C   . ALA   A 1 153 ? -28.539 3.810   11.837 1.00 61.67  ? 449 ALA   A C   1 
ATOM   1159 O  O   . ALA   A 1 153 ? -29.178 4.147   12.841 1.00 69.76  ? 449 ALA   A O   1 
ATOM   1160 C  CB  . ALA   A 1 153 ? -27.632 1.491   12.105 1.00 60.89  ? 449 ALA   A CB  1 
ATOM   1161 N  N   . THR   A 1 154 ? -27.765 4.662   11.167 1.00 58.32  ? 450 THR   A N   1 
ATOM   1162 C  CA  . THR   A 1 154 ? -27.697 6.058   11.578 1.00 64.80  ? 450 THR   A CA  1 
ATOM   1163 C  C   . THR   A 1 154 ? -28.957 6.821   11.183 1.00 73.82  ? 450 THR   A C   1 
ATOM   1164 O  O   . THR   A 1 154 ? -29.526 7.552   11.999 1.00 71.69  ? 450 THR   A O   1 
ATOM   1165 C  CB  . THR   A 1 154 ? -26.443 6.690   10.983 1.00 64.76  ? 450 THR   A CB  1 
ATOM   1166 O  OG1 . THR   A 1 154 ? -25.311 6.000   11.532 1.00 62.94  ? 450 THR   A OG1 1 
ATOM   1167 C  CG2 . THR   A 1 154 ? -26.370 8.159   11.363 1.00 66.25  ? 450 THR   A CG2 1 
ATOM   1168 N  N   . ASN   A 1 155 ? -29.418 6.660   9.939  1.00 70.55  ? 451 ASN   A N   1 
ATOM   1169 C  CA  . ASN   A 1 155 ? -30.690 7.248   9.519  1.00 69.71  ? 451 ASN   A CA  1 
ATOM   1170 C  C   . ASN   A 1 155 ? -30.763 8.727   9.901  1.00 76.23  ? 451 ASN   A C   1 
ATOM   1171 O  O   . ASN   A 1 155 ? -31.759 9.207   10.448 1.00 87.60  ? 451 ASN   A O   1 
ATOM   1172 C  CB  . ASN   A 1 155 ? -31.873 6.463   10.102 1.00 70.80  ? 451 ASN   A CB  1 
ATOM   1173 C  CG  . ASN   A 1 155 ? -33.226 6.909   9.546  1.00 77.03  ? 451 ASN   A CG  1 
ATOM   1174 O  OD1 . ASN   A 1 155 ? -33.312 7.471   8.448  1.00 84.01  ? 451 ASN   A OD1 1 
ATOM   1175 N  ND2 . ASN   A 1 155 ? -34.286 6.653   10.299 1.00 79.57  ? 451 ASN   A ND2 1 
ATOM   1176 N  N   . LYS   A 1 156 ? -29.671 9.446   9.649  1.00 80.34  ? 452 LYS   A N   1 
ATOM   1177 C  CA  . LYS   A 1 156 ? -29.612 10.890  9.854  1.00 86.90  ? 452 LYS   A CA  1 
ATOM   1178 C  C   . LYS   A 1 156 ? -29.810 11.261  11.319 1.00 85.63  ? 452 LYS   A C   1 
ATOM   1179 O  O   . LYS   A 1 156 ? -30.293 12.352  11.616 1.00 99.01  ? 452 LYS   A O   1 
ATOM   1180 C  CB  . LYS   A 1 156 ? -30.649 11.636  9.001  1.00 90.00  ? 452 LYS   A CB  1 
ATOM   1181 C  CG  . LYS   A 1 156 ? -30.749 11.277  7.520  1.00 107.30 ? 452 LYS   A CG  1 
ATOM   1182 C  CD  . LYS   A 1 156 ? -31.699 12.239  6.775  1.00 119.77 ? 452 LYS   A CD  1 
ATOM   1183 C  CE  . LYS   A 1 156 ? -32.781 12.840  7.684  1.00 133.50 ? 452 LYS   A CE  1 
ATOM   1184 N  NZ  . LYS   A 1 156 ? -33.742 11.851  8.265  1.00 135.89 ? 452 LYS   A NZ  1 
ATOM   1185 N  N   . GLY   A 1 157 ? -29.463 10.358  12.241 1.00 76.49  ? 453 GLY   A N   1 
ATOM   1186 C  CA  . GLY   A 1 157 ? -29.616 10.586  13.662 1.00 78.23  ? 453 GLY   A CA  1 
ATOM   1187 C  C   . GLY   A 1 157 ? -30.860 9.967   14.262 1.00 78.96  ? 453 GLY   A C   1 
ATOM   1188 O  O   . GLY   A 1 157 ? -30.938 9.820   15.491 1.00 73.78  ? 453 GLY   A O   1 
ATOM   1189 N  N   . ASN   A 1 158 ? -31.849 9.621   13.434 1.00 81.04  ? 454 ASN   A N   1 
ATOM   1190 C  CA  . ASN   A 1 158 ? -32.989 8.847   13.924 1.00 80.25  ? 454 ASN   A CA  1 
ATOM   1191 C  C   . ASN   A 1 158 ? -32.611 7.366   13.915 1.00 74.17  ? 454 ASN   A C   1 
ATOM   1192 O  O   . ASN   A 1 158 ? -33.113 6.562   13.128 1.00 83.87  ? 454 ASN   A O   1 
ATOM   1193 C  CB  . ASN   A 1 158 ? -34.234 9.132   13.098 1.00 90.94  ? 454 ASN   A CB  1 
ATOM   1194 C  CG  . ASN   A 1 158 ? -35.444 8.373   13.600 1.00 98.27  ? 454 ASN   A CG  1 
ATOM   1195 O  OD1 . ASN   A 1 158 ? -35.477 7.934   14.754 1.00 107.03 ? 454 ASN   A OD1 1 
ATOM   1196 N  ND2 . ASN   A 1 158 ? -36.439 8.202   12.740 1.00 97.15  ? 454 ASN   A ND2 1 
ATOM   1197 N  N   . LEU   A 1 159 ? -31.691 7.028   14.827 1.00 73.31  ? 455 LEU   A N   1 
ATOM   1198 C  CA  . LEU   A 1 159 ? -31.002 5.743   14.810 1.00 67.54  ? 455 LEU   A CA  1 
ATOM   1199 C  C   . LEU   A 1 159 ? -31.979 4.575   14.796 1.00 71.43  ? 455 LEU   A C   1 
ATOM   1200 O  O   . LEU   A 1 159 ? -33.033 4.601   15.441 1.00 74.63  ? 455 LEU   A O   1 
ATOM   1201 C  CB  . LEU   A 1 159 ? -30.067 5.619   16.026 1.00 66.69  ? 455 LEU   A CB  1 
ATOM   1202 C  CG  . LEU   A 1 159 ? -28.624 6.140   15.919 1.00 72.18  ? 455 LEU   A CG  1 
ATOM   1203 C  CD1 . LEU   A 1 159 ? -28.546 7.353   15.016 1.00 77.37  ? 455 LEU   A CD1 1 
ATOM   1204 C  CD2 . LEU   A 1 159 ? -28.047 6.483   17.279 1.00 72.51  ? 455 LEU   A CD2 1 
ATOM   1205 N  N   . ARG   A 1 160 ? -31.584 3.531   14.080 1.00 59.86  ? 456 ARG   A N   1 
ATOM   1206 C  CA  . ARG   A 1 160 ? -32.383 2.334   13.851 1.00 60.85  ? 456 ARG   A CA  1 
ATOM   1207 C  C   . ARG   A 1 160 ? -31.499 1.147   14.160 1.00 58.26  ? 456 ARG   A C   1 
ATOM   1208 O  O   . ARG   A 1 160 ? -30.362 1.079   13.684 1.00 61.80  ? 456 ARG   A O   1 
ATOM   1209 C  CB  . ARG   A 1 160 ? -32.882 2.237   12.391 1.00 56.11  ? 456 ARG   A CB  1 
ATOM   1210 C  CG  . ARG   A 1 160 ? -33.800 3.361   11.970 1.00 63.51  ? 456 ARG   A CG  1 
ATOM   1211 C  CD  . ARG   A 1 160 ? -34.300 3.180   10.536 1.00 68.47  ? 456 ARG   A CD  1 
ATOM   1212 N  NE  . ARG   A 1 160 ? -33.259 3.419   9.542  1.00 69.93  ? 456 ARG   A NE  1 
ATOM   1213 C  CZ  . ARG   A 1 160 ? -33.509 3.737   8.271  1.00 76.80  ? 456 ARG   A CZ  1 
ATOM   1214 N  NH1 . ARG   A 1 160 ? -34.763 3.857   7.861  1.00 79.83  ? 456 ARG   A NH1 1 
ATOM   1215 N  NH2 . ARG   A 1 160 ? -32.510 3.950   7.421  1.00 68.54  ? 456 ARG   A NH2 1 
ATOM   1216 N  N   . SER   A 1 161 ? -32.003 0.217   14.947 1.00 54.20  ? 457 SER   A N   1 
ATOM   1217 C  CA  . SER   A 1 161 ? -31.151 -0.896  15.310 1.00 57.77  ? 457 SER   A CA  1 
ATOM   1218 C  C   . SER   A 1 161 ? -31.078 -1.862  14.138 1.00 53.26  ? 457 SER   A C   1 
ATOM   1219 O  O   . SER   A 1 161 ? -32.018 -1.984  13.346 1.00 57.78  ? 457 SER   A O   1 
ATOM   1220 C  CB  . SER   A 1 161 ? -31.646 -1.594  16.583 1.00 67.66  ? 457 SER   A CB  1 
ATOM   1221 O  OG  . SER   A 1 161 ? -32.980 -2.052  16.459 1.00 79.63  ? 457 SER   A OG  1 
ATOM   1222 N  N   . ALA   A 1 162 ? -29.934 -2.526  14.016 1.00 52.19  ? 458 ALA   A N   1 
ATOM   1223 C  CA  . ALA   A 1 162 ? -29.665 -3.337  12.839 1.00 51.50  ? 458 ALA   A CA  1 
ATOM   1224 C  C   . ALA   A 1 162 ? -28.516 -4.284  13.137 1.00 51.58  ? 458 ALA   A C   1 
ATOM   1225 O  O   . ALA   A 1 162 ? -27.707 -4.045  14.033 1.00 54.90  ? 458 ALA   A O   1 
ATOM   1226 C  CB  . ALA   A 1 162 ? -29.335 -2.468  11.617 1.00 56.81  ? 458 ALA   A CB  1 
ATOM   1227 N  N   . ILE   A 1 163 ? -28.438 -5.358  12.353 1.00 48.62  ? 459 ILE   A N   1 
ATOM   1228 C  CA  . ILE   A 1 163 ? -27.356 -6.321  12.494 1.00 52.16  ? 459 ILE   A CA  1 
ATOM   1229 C  C   . ILE   A 1 163 ? -27.022 -6.846  11.109 1.00 53.18  ? 459 ILE   A C   1 
ATOM   1230 O  O   . ILE   A 1 163 ? -27.912 -7.027  10.270 1.00 63.50  ? 459 ILE   A O   1 
ATOM   1231 C  CB  . ILE   A 1 163 ? -27.725 -7.467  13.464 1.00 52.45  ? 459 ILE   A CB  1 
ATOM   1232 C  CG1 . ILE   A 1 163 ? -26.557 -8.432  13.584 1.00 47.24  ? 459 ILE   A CG1 1 
ATOM   1233 C  CG2 . ILE   A 1 163 ? -28.970 -8.202  13.000 1.00 55.08  ? 459 ILE   A CG2 1 
ATOM   1234 C  CD1 . ILE   A 1 163 ? -26.801 -9.567  14.578 1.00 45.76  ? 459 ILE   A CD1 1 
ATOM   1235 N  N   . THR   A 1 164 ? -25.734 -7.024  10.840 1.00 52.00  ? 460 THR   A N   1 
ATOM   1236 C  CA  . THR   A 1 164 ? -25.283 -7.548  9.556  1.00 47.62  ? 460 THR   A CA  1 
ATOM   1237 C  C   . THR   A 1 164 ? -24.583 -8.868  9.817  1.00 53.32  ? 460 THR   A C   1 
ATOM   1238 O  O   . THR   A 1 164 ? -23.691 -8.933  10.661 1.00 55.49  ? 460 THR   A O   1 
ATOM   1239 C  CB  . THR   A 1 164 ? -24.361 -6.571  8.836  1.00 47.30  ? 460 THR   A CB  1 
ATOM   1240 O  OG1 . THR   A 1 164 ? -25.062 -5.337  8.660  1.00 53.32  ? 460 THR   A OG1 1 
ATOM   1241 C  CG2 . THR   A 1 164 ? -24.009 -7.124  7.416  1.00 47.14  ? 460 THR   A CG2 1 
ATOM   1242 N  N   . ILE   A 1 165 ? -24.991 -9.914  9.107  1.00 47.01  ? 461 ILE   A N   1 
ATOM   1243 C  CA  . ILE   A 1 165 ? -24.585 -11.272 9.440  1.00 45.68  ? 461 ILE   A CA  1 
ATOM   1244 C  C   . ILE   A 1 165 ? -23.763 -11.812 8.286  1.00 53.81  ? 461 ILE   A C   1 
ATOM   1245 O  O   . ILE   A 1 165 ? -24.300 -12.093 7.208  1.00 54.63  ? 461 ILE   A O   1 
ATOM   1246 C  CB  . ILE   A 1 165 ? -25.794 -12.151 9.760  1.00 55.77  ? 461 ILE   A CB  1 
ATOM   1247 C  CG1 . ILE   A 1 165 ? -26.458 -11.581 11.022 1.00 53.46  ? 461 ILE   A CG1 1 
ATOM   1248 C  CG2 . ILE   A 1 165 ? -25.350 -13.549 10.041 1.00 56.27  ? 461 ILE   A CG2 1 
ATOM   1249 C  CD1 . ILE   A 1 165 ? -27.741 -12.244 11.438 1.00 50.46  ? 461 ILE   A CD1 1 
ATOM   1250 N  N   . PHE   A 1 166 ? -22.459 -11.899 8.501  1.00 54.53  ? 462 PHE   A N   1 
ATOM   1251 C  CA  . PHE   A 1 166 ? -21.510 -12.397 7.525  1.00 51.95  ? 462 PHE   A CA  1 
ATOM   1252 C  C   . PHE   A 1 166 ? -21.520 -13.915 7.551  1.00 56.79  ? 462 PHE   A C   1 
ATOM   1253 O  O   . PHE   A 1 166 ? -22.115 -14.511 8.459  1.00 56.94  ? 462 PHE   A O   1 
ATOM   1254 C  CB  . PHE   A 1 166 ? -20.139 -11.798 7.829  1.00 53.43  ? 462 PHE   A CB  1 
ATOM   1255 C  CG  . PHE   A 1 166 ? -20.062 -10.342 7.490  1.00 61.74  ? 462 PHE   A CG  1 
ATOM   1256 C  CD1 . PHE   A 1 166 ? -20.092 -9.936  6.149  1.00 59.69  ? 462 PHE   A CD1 1 
ATOM   1257 C  CD2 . PHE   A 1 166 ? -20.037 -9.380  8.483  1.00 55.50  ? 462 PHE   A CD2 1 
ATOM   1258 C  CE1 . PHE   A 1 166 ? -20.046 -8.590  5.815  1.00 65.25  ? 462 PHE   A CE1 1 
ATOM   1259 C  CE2 . PHE   A 1 166 ? -19.990 -8.019  8.148  1.00 54.64  ? 462 PHE   A CE2 1 
ATOM   1260 C  CZ  . PHE   A 1 166 ? -19.997 -7.632  6.817  1.00 64.01  ? 462 PHE   A CZ  1 
ATOM   1261 N  N   . PRO   A 1 167 ? -20.899 -14.570 6.557  1.00 54.85  ? 463 PRO   A N   1 
ATOM   1262 C  CA  . PRO   A 1 167 ? -21.009 -16.030 6.464  1.00 59.64  ? 463 PRO   A CA  1 
ATOM   1263 C  C   . PRO   A 1 167 ? -20.614 -16.727 7.762  1.00 61.83  ? 463 PRO   A C   1 
ATOM   1264 O  O   . PRO   A 1 167 ? -19.753 -16.265 8.516  1.00 60.32  ? 463 PRO   A O   1 
ATOM   1265 C  CB  . PRO   A 1 167 ? -20.062 -16.384 5.315  1.00 59.70  ? 463 PRO   A CB  1 
ATOM   1266 C  CG  . PRO   A 1 167 ? -20.110 -15.182 4.417  1.00 56.85  ? 463 PRO   A CG  1 
ATOM   1267 C  CD  . PRO   A 1 167 ? -20.249 -13.998 5.355  1.00 55.02  ? 463 PRO   A CD  1 
ATOM   1268 N  N   . GLN   A 1 168 ? -21.257 -17.859 8.007  1.00 61.89  ? 464 GLN   A N   1 
ATOM   1269 C  CA  . GLN   A 1 168 ? -21.044 -18.586 9.247  1.00 57.24  ? 464 GLN   A CA  1 
ATOM   1270 C  C   . GLN   A 1 168 ? -19.715 -19.327 9.215  1.00 61.33  ? 464 GLN   A C   1 
ATOM   1271 O  O   . GLN   A 1 168 ? -19.214 -19.707 8.157  1.00 56.07  ? 464 GLN   A O   1 
ATOM   1272 C  CB  . GLN   A 1 168 ? -22.175 -19.581 9.476  1.00 48.42  ? 464 GLN   A CB  1 
ATOM   1273 C  CG  . GLN   A 1 168 ? -22.270 -20.644 8.376  1.00 57.30  ? 464 GLN   A CG  1 
ATOM   1274 C  CD  . GLN   A 1 168 ? -23.668 -21.192 8.267  1.00 64.92  ? 464 GLN   A CD  1 
ATOM   1275 O  OE1 . GLN   A 1 168 ? -24.641 -20.440 8.297  1.00 70.13  ? 464 GLN   A OE1 1 
ATOM   1276 N  NE2 . GLN   A 1 168 ? -23.784 -22.510 8.166  1.00 73.25  ? 464 GLN   A NE2 1 
ATOM   1277 N  N   . ARG   A 1 169 ? -19.135 -19.528 10.397 1.00 63.54  ? 465 ARG   A N   1 
ATOM   1278 C  CA  . ARG   A 1 169 ? -17.940 -20.352 10.479 1.00 62.86  ? 465 ARG   A CA  1 
ATOM   1279 C  C   . ARG   A 1 169 ? -18.211 -21.725 9.871  1.00 70.36  ? 465 ARG   A C   1 
ATOM   1280 O  O   . ARG   A 1 169 ? -19.287 -22.300 10.054 1.00 73.51  ? 465 ARG   A O   1 
ATOM   1281 C  CB  . ARG   A 1 169 ? -17.498 -20.506 11.935 1.00 70.44  ? 465 ARG   A CB  1 
ATOM   1282 C  CG  . ARG   A 1 169 ? -16.391 -21.516 12.098 1.00 74.24  ? 465 ARG   A CG  1 
ATOM   1283 C  CD  . ARG   A 1 169 ? -15.860 -21.507 13.493 1.00 81.41  ? 465 ARG   A CD  1 
ATOM   1284 N  NE  . ARG   A 1 169 ? -15.332 -20.196 13.836 1.00 81.93  ? 465 ARG   A NE  1 
ATOM   1285 C  CZ  . ARG   A 1 169 ? -15.482 -19.637 15.027 1.00 75.90  ? 465 ARG   A CZ  1 
ATOM   1286 N  NH1 . ARG   A 1 169 ? -16.157 -20.278 15.966 1.00 86.67  ? 465 ARG   A NH1 1 
ATOM   1287 N  NH2 . ARG   A 1 169 ? -14.977 -18.435 15.271 1.00 67.49  ? 465 ARG   A NH2 1 
ATOM   1288 N  N   . THR   A 1 170 ? -17.241 -22.235 9.105  1.00 75.44  ? 466 THR   A N   1 
ATOM   1289 C  CA  . THR   A 1 170 ? -17.314 -23.596 8.594  1.00 76.34  ? 466 THR   A CA  1 
ATOM   1290 C  C   . THR   A 1 170 ? -16.225 -24.398 9.268  1.00 82.55  ? 466 THR   A C   1 
ATOM   1291 O  O   . THR   A 1 170 ? -16.453 -24.967 10.360 1.00 87.81  ? 466 THR   A O   1 
ATOM   1292 C  CB  . THR   A 1 170 ? -17.226 -23.616 7.059  1.00 79.63  ? 466 THR   A CB  1 
ATOM   1293 O  OG1 . THR   A 1 170 ? -16.166 -22.756 6.627  1.00 81.17  ? 466 THR   A OG1 1 
ATOM   1294 C  CG2 . THR   A 1 170 ? -18.538 -23.159 6.446  1.00 74.96  ? 466 THR   A CG2 1 
ATOM   1295 N  N   . ASP   A 1 171 ? -15.017 -24.475 8.706  1.00 84.85  ? 467 ASP   A N   1 
ATOM   1296 C  CA  . ASP   A 1 171 ? -13.976 -25.314 9.290  1.00 94.09  ? 467 ASP   A CA  1 
ATOM   1297 C  C   . ASP   A 1 171 ? -13.427 -24.711 10.578 1.00 96.53  ? 467 ASP   A C   1 
ATOM   1298 O  O   . ASP   A 1 171 ? -13.127 -25.439 11.530 1.00 110.64 ? 467 ASP   A O   1 
ATOM   1299 C  CB  . ASP   A 1 171 ? -12.845 -25.515 8.286  1.00 105.32 ? 467 ASP   A CB  1 
ATOM   1300 C  CG  . ASP   A 1 171 ? -12.078 -24.237 8.023  1.00 109.70 ? 467 ASP   A CG  1 
ATOM   1301 O  OD1 . ASP   A 1 171 ? -12.705 -23.155 8.071  1.00 107.64 ? 467 ASP   A OD1 1 
ATOM   1302 O  OD2 . ASP   A 1 171 ? -10.853 -24.308 7.791  1.00 114.16 ? 467 ASP   A OD2 1 
ATOM   1303 N  N   . GLY   A 1 172 ? -13.286 -23.388 10.627 1.00 92.87  ? 468 GLY   A N   1 
ATOM   1304 C  CA  . GLY   A 1 172 ? -12.617 -22.722 11.728 1.00 90.39  ? 468 GLY   A CA  1 
ATOM   1305 C  C   . GLY   A 1 172 ? -11.468 -21.851 11.258 1.00 94.34  ? 468 GLY   A C   1 
ATOM   1306 O  O   . GLY   A 1 172 ? -11.266 -20.752 11.779 1.00 92.09  ? 468 GLY   A O   1 
ATOM   1307 N  N   . LYS   A 1 173 ? -10.709 -22.329 10.270 1.00 100.41 ? 469 LYS   A N   1 
ATOM   1308 C  CA  . LYS   A 1 173 ? -9.637  -21.550 9.661  1.00 104.01 ? 469 LYS   A CA  1 
ATOM   1309 C  C   . LYS   A 1 173 ? -10.130 -20.672 8.519  1.00 103.31 ? 469 LYS   A C   1 
ATOM   1310 O  O   . LYS   A 1 173 ? -9.326  -19.969 7.898  1.00 101.42 ? 469 LYS   A O   1 
ATOM   1311 C  CB  . LYS   A 1 173 ? -8.519  -22.478 9.165  1.00 109.98 ? 469 LYS   A CB  1 
ATOM   1312 C  CG  . LYS   A 1 173 ? -7.734  -23.132 10.298 1.00 118.30 ? 469 LYS   A CG  1 
ATOM   1313 C  CD  . LYS   A 1 173 ? -6.617  -24.024 9.785  1.00 128.78 ? 469 LYS   A CD  1 
ATOM   1314 C  CE  . LYS   A 1 173 ? -5.851  -24.653 10.943 1.00 138.38 ? 469 LYS   A CE  1 
ATOM   1315 N  NZ  . LYS   A 1 173 ? -4.773  -25.570 10.475 1.00 147.25 ? 469 LYS   A NZ  1 
ATOM   1316 N  N   . HIS   A 1 174 ? -11.424 -20.712 8.224  1.00 104.29 ? 470 HIS   A N   1 
ATOM   1317 C  CA  . HIS   A 1 174 ? -12.072 -19.774 7.316  1.00 105.00 ? 470 HIS   A CA  1 
ATOM   1318 C  C   . HIS   A 1 174 ? -13.103 -19.032 8.150  1.00 108.80 ? 470 HIS   A C   1 
ATOM   1319 O  O   . HIS   A 1 174 ? -14.230 -19.502 8.329  1.00 115.17 ? 470 HIS   A O   1 
ATOM   1320 C  CB  . HIS   A 1 174 ? -12.707 -20.487 6.131  1.00 102.00 ? 470 HIS   A CB  1 
ATOM   1321 C  CG  . HIS   A 1 174 ? -11.731 -21.272 5.322  1.00 106.91 ? 470 HIS   A CG  1 
ATOM   1322 N  ND1 . HIS   A 1 174 ? -11.713 -22.649 5.310  1.00 109.10 ? 470 HIS   A ND1 1 
ATOM   1323 C  CD2 . HIS   A 1 174 ? -10.719 -20.873 4.517  1.00 109.00 ? 470 HIS   A CD2 1 
ATOM   1324 C  CE1 . HIS   A 1 174 ? -10.741 -23.066 4.519  1.00 115.01 ? 470 HIS   A CE1 1 
ATOM   1325 N  NE2 . HIS   A 1 174 ? -10.121 -22.008 4.027  1.00 114.99 ? 470 HIS   A NE2 1 
ATOM   1326 N  N   . ASP   A 1 175 ? -12.705 -17.888 8.687  1.00 100.00 ? 471 ASP   A N   1 
ATOM   1327 C  CA  . ASP   A 1 175 ? -13.564 -17.112 9.562  1.00 80.95  ? 471 ASP   A CA  1 
ATOM   1328 C  C   . ASP   A 1 175 ? -13.695 -15.707 9.008  1.00 79.38  ? 471 ASP   A C   1 
ATOM   1329 O  O   . ASP   A 1 175 ? -12.699 -15.099 8.608  1.00 85.95  ? 471 ASP   A O   1 
ATOM   1330 C  CB  . ASP   A 1 175 ? -13.006 -17.060 10.983 1.00 85.10  ? 471 ASP   A CB  1 
ATOM   1331 C  CG  . ASP   A 1 175 ? -13.555 -18.157 11.857 1.00 82.67  ? 471 ASP   A CG  1 
ATOM   1332 O  OD1 . ASP   A 1 175 ? -14.374 -18.959 11.373 1.00 86.93  ? 471 ASP   A OD1 1 
ATOM   1333 O  OD2 . ASP   A 1 175 ? -13.166 -18.214 13.038 1.00 86.31  ? 471 ASP   A OD2 1 
ATOM   1334 N  N   . PHE   A 1 176 ? -14.919 -15.202 8.978  1.00 71.41  ? 472 PHE   A N   1 
ATOM   1335 C  CA  . PHE   A 1 176 ? -15.152 -13.782 8.778  1.00 67.38  ? 472 PHE   A CA  1 
ATOM   1336 C  C   . PHE   A 1 176 ? -15.084 -13.110 10.137 1.00 59.26  ? 472 PHE   A C   1 
ATOM   1337 O  O   . PHE   A 1 176 ? -15.777 -13.527 11.067 1.00 58.32  ? 472 PHE   A O   1 
ATOM   1338 C  CB  . PHE   A 1 176 ? -16.499 -13.529 8.111  1.00 62.02  ? 472 PHE   A CB  1 
ATOM   1339 C  CG  . PHE   A 1 176 ? -16.534 -13.927 6.679  1.00 61.08  ? 472 PHE   A CG  1 
ATOM   1340 C  CD1 . PHE   A 1 176 ? -16.548 -15.262 6.319  1.00 60.56  ? 472 PHE   A CD1 1 
ATOM   1341 C  CD2 . PHE   A 1 176 ? -16.534 -12.962 5.685  1.00 69.00  ? 472 PHE   A CD2 1 
ATOM   1342 C  CE1 . PHE   A 1 176 ? -16.576 -15.625 4.956  1.00 67.88  ? 472 PHE   A CE1 1 
ATOM   1343 C  CE2 . PHE   A 1 176 ? -16.565 -13.316 4.370  1.00 66.79  ? 472 PHE   A CE2 1 
ATOM   1344 C  CZ  . PHE   A 1 176 ? -16.580 -14.652 4.000  1.00 67.55  ? 472 PHE   A CZ  1 
ATOM   1345 N  N   . ARG   A 1 177 ? -14.231 -12.096 10.254 1.00 60.14  ? 473 ARG   A N   1 
ATOM   1346 C  CA  . ARG   A 1 177 ? -14.080 -11.363 11.504 1.00 59.18  ? 473 ARG   A CA  1 
ATOM   1347 C  C   . ARG   A 1 177 ? -13.970 -9.879  11.203 1.00 63.38  ? 473 ARG   A C   1 
ATOM   1348 O  O   . ARG   A 1 177 ? -13.261 -9.484  10.273 1.00 66.40  ? 473 ARG   A O   1 
ATOM   1349 C  CB  . ARG   A 1 177 ? -12.839 -11.821 12.280 1.00 67.08  ? 473 ARG   A CB  1 
ATOM   1350 C  CG  . ARG   A 1 177 ? -12.955 -13.191 12.913 1.00 60.71  ? 473 ARG   A CG  1 
ATOM   1351 C  CD  . ARG   A 1 177 ? -14.133 -13.247 13.869 1.00 68.21  ? 473 ARG   A CD  1 
ATOM   1352 N  NE  . ARG   A 1 177 ? -13.996 -12.298 14.975 1.00 70.45  ? 473 ARG   A NE  1 
ATOM   1353 C  CZ  . ARG   A 1 177 ? -13.258 -12.512 16.057 1.00 73.41  ? 473 ARG   A CZ  1 
ATOM   1354 N  NH1 . ARG   A 1 177 ? -12.578 -13.645 16.183 1.00 69.42  ? 473 ARG   A NH1 1 
ATOM   1355 N  NH2 . ARG   A 1 177 ? -13.195 -11.593 17.018 1.00 70.79  ? 473 ARG   A NH2 1 
ATOM   1356 N  N   . VAL   A 1 178 ? -14.678 -9.068  11.978 1.00 57.80  ? 474 VAL   A N   1 
ATOM   1357 C  CA  . VAL   A 1 178 ? -14.346 -7.657  12.107 1.00 55.89  ? 474 VAL   A CA  1 
ATOM   1358 C  C   . VAL   A 1 178 ? -13.356 -7.570  13.258 1.00 68.99  ? 474 VAL   A C   1 
ATOM   1359 O  O   . VAL   A 1 178 ? -13.673 -7.964  14.385 1.00 69.45  ? 474 VAL   A O   1 
ATOM   1360 C  CB  . VAL   A 1 178 ? -15.596 -6.802  12.364 1.00 55.01  ? 474 VAL   A CB  1 
ATOM   1361 C  CG1 . VAL   A 1 178 ? -15.267 -5.320  12.235 1.00 60.44  ? 474 VAL   A CG1 1 
ATOM   1362 C  CG2 . VAL   A 1 178 ? -16.725 -7.189  11.422 1.00 59.89  ? 474 VAL   A CG2 1 
ATOM   1363 N  N   . TRP   A 1 179 ? -12.134 -7.119  12.968 1.00 75.58  ? 475 TRP   A N   1 
ATOM   1364 C  CA  . TRP   A 1 179 ? -11.130 -7.068  14.028 1.00 75.26  ? 475 TRP   A CA  1 
ATOM   1365 C  C   . TRP   A 1 179 ? -11.407 -5.933  15.005 1.00 68.55  ? 475 TRP   A C   1 
ATOM   1366 O  O   . TRP   A 1 179 ? -11.011 -6.010  16.179 1.00 72.54  ? 475 TRP   A O   1 
ATOM   1367 C  CB  . TRP   A 1 179 ? -9.728  -6.948  13.424 1.00 79.52  ? 475 TRP   A CB  1 
ATOM   1368 C  CG  . TRP   A 1 179 ? -9.222  -8.251  12.882 1.00 74.98  ? 475 TRP   A CG  1 
ATOM   1369 C  CD1 . TRP   A 1 179 ? -9.958  -9.237  12.292 1.00 78.01  ? 475 TRP   A CD1 1 
ATOM   1370 C  CD2 . TRP   A 1 179 ? -7.872  -8.721  12.906 1.00 77.60  ? 475 TRP   A CD2 1 
ATOM   1371 N  NE1 . TRP   A 1 179 ? -9.145  -10.284 11.926 1.00 79.26  ? 475 TRP   A NE1 1 
ATOM   1372 C  CE2 . TRP   A 1 179 ? -7.860  -9.993  12.299 1.00 80.04  ? 475 TRP   A CE2 1 
ATOM   1373 C  CE3 . TRP   A 1 179 ? -6.670  -8.188  13.377 1.00 77.32  ? 475 TRP   A CE3 1 
ATOM   1374 C  CZ2 . TRP   A 1 179 ? -6.695  -10.740 12.156 1.00 81.81  ? 475 TRP   A CZ2 1 
ATOM   1375 C  CZ3 . TRP   A 1 179 ? -5.517  -8.926  13.224 1.00 78.14  ? 475 TRP   A CZ3 1 
ATOM   1376 C  CH2 . TRP   A 1 179 ? -5.538  -10.189 12.627 1.00 79.64  ? 475 TRP   A CH2 1 
ATOM   1377 N  N   . ASN   A 1 180 ? -12.086 -4.883  14.548 1.00 55.32  ? 476 ASN   A N   1 
ATOM   1378 C  CA  . ASN   A 1 180 ? -12.555 -3.839  15.446 1.00 64.40  ? 476 ASN   A CA  1 
ATOM   1379 C  C   . ASN   A 1 180 ? -13.533 -4.413  16.465 1.00 69.25  ? 476 ASN   A C   1 
ATOM   1380 O  O   . ASN   A 1 180 ? -14.350 -5.284  16.148 1.00 66.24  ? 476 ASN   A O   1 
ATOM   1381 C  CB  . ASN   A 1 180 ? -13.256 -2.736  14.663 1.00 72.16  ? 476 ASN   A CB  1 
ATOM   1382 C  CG  . ASN   A 1 180 ? -12.439 -2.235  13.503 1.00 73.88  ? 476 ASN   A CG  1 
ATOM   1383 O  OD1 . ASN   A 1 180 ? -11.987 -3.012  12.658 1.00 81.22  ? 476 ASN   A OD1 1 
ATOM   1384 N  ND2 . ASN   A 1 180 ? -12.225 -0.925  13.462 1.00 75.58  ? 476 ASN   A ND2 1 
ATOM   1385 N  N   . SER   A 1 181 ? -13.467 -3.894  17.695 1.00 66.13  ? 477 SER   A N   1 
ATOM   1386 C  CA  . SER   A 1 181 ? -14.450 -4.262  18.713 1.00 61.65  ? 477 SER   A CA  1 
ATOM   1387 C  C   . SER   A 1 181 ? -15.762 -3.516  18.548 1.00 61.88  ? 477 SER   A C   1 
ATOM   1388 O  O   . SER   A 1 181 ? -16.813 -4.026  18.956 1.00 56.59  ? 477 SER   A O   1 
ATOM   1389 C  CB  . SER   A 1 181 ? -13.892 -4.009  20.114 1.00 58.65  ? 477 SER   A CB  1 
ATOM   1390 O  OG  . SER   A 1 181 ? -13.240 -2.757  20.165 1.00 66.47  ? 477 SER   A OG  1 
ATOM   1391 N  N   . GLN   A 1 182 ? -15.716 -2.317  17.970 1.00 63.30  ? 478 GLN   A N   1 
ATOM   1392 C  CA  . GLN   A 1 182 ? -16.896 -1.598  17.517 1.00 58.58  ? 478 GLN   A CA  1 
ATOM   1393 C  C   . GLN   A 1 182 ? -16.580 -1.020  16.152 1.00 57.84  ? 478 GLN   A C   1 
ATOM   1394 O  O   . GLN   A 1 182 ? -15.445 -0.624  15.893 1.00 69.27  ? 478 GLN   A O   1 
ATOM   1395 C  CB  . GLN   A 1 182 ? -17.308 -0.430  18.422 1.00 61.08  ? 478 GLN   A CB  1 
ATOM   1396 C  CG  . GLN   A 1 182 ? -17.731 -0.784  19.826 1.00 67.70  ? 478 GLN   A CG  1 
ATOM   1397 C  CD  . GLN   A 1 182 ? -17.861 0.457   20.701 1.00 69.12  ? 478 GLN   A CD  1 
ATOM   1398 O  OE1 . GLN   A 1 182 ? -18.303 1.517   20.240 1.00 66.62  ? 478 GLN   A OE1 1 
ATOM   1399 N  NE2 . GLN   A 1 182 ? -17.455 0.336   21.958 1.00 65.08  ? 478 GLN   A NE2 1 
ATOM   1400 N  N   . LEU   A 1 183 ? -17.599 -0.959  15.290 1.00 60.39  ? 479 LEU   A N   1 
ATOM   1401 C  CA  . LEU   A 1 183 ? -17.412 -0.426  13.939 1.00 55.22  ? 479 LEU   A CA  1 
ATOM   1402 C  C   . LEU   A 1 183 ? -16.799 0.968   13.969 1.00 63.55  ? 479 LEU   A C   1 
ATOM   1403 O  O   . LEU   A 1 183 ? -15.948 1.305   13.135 1.00 72.81  ? 479 LEU   A O   1 
ATOM   1404 C  CB  . LEU   A 1 183 ? -18.745 -0.392  13.191 1.00 54.13  ? 479 LEU   A CB  1 
ATOM   1405 C  CG  . LEU   A 1 183 ? -19.487 -1.703  12.915 1.00 60.43  ? 479 LEU   A CG  1 
ATOM   1406 C  CD1 . LEU   A 1 183 ? -20.744 -1.415  12.097 1.00 62.68  ? 479 LEU   A CD1 1 
ATOM   1407 C  CD2 . LEU   A 1 183 ? -18.586 -2.719  12.206 1.00 67.15  ? 479 LEU   A CD2 1 
ATOM   1408 N  N   . ILE   A 1 184 ? -17.213 1.788   14.929 1.00 64.48  ? 480 ILE   A N   1 
ATOM   1409 C  CA  . ILE   A 1 184 ? -16.769 3.167   15.059 1.00 58.81  ? 480 ILE   A CA  1 
ATOM   1410 C  C   . ILE   A 1 184 ? -16.184 3.331   16.459 1.00 70.31  ? 480 ILE   A C   1 
ATOM   1411 O  O   . ILE   A 1 184 ? -16.916 3.313   17.455 1.00 70.18  ? 480 ILE   A O   1 
ATOM   1412 C  CB  . ILE   A 1 184 ? -17.916 4.151   14.793 1.00 61.34  ? 480 ILE   A CB  1 
ATOM   1413 C  CG1 . ILE   A 1 184 ? -18.390 4.003   13.343 1.00 68.32  ? 480 ILE   A CG1 1 
ATOM   1414 C  CG2 . ILE   A 1 184 ? -17.472 5.586   15.023 1.00 70.48  ? 480 ILE   A CG2 1 
ATOM   1415 C  CD1 . ILE   A 1 184 ? -19.585 4.847   12.998 1.00 65.44  ? 480 ILE   A CD1 1 
ATOM   1416 N  N   . ARG   A 1 185 ? -14.858 3.453   16.534 1.00 73.84  ? 481 ARG   A N   1 
ATOM   1417 C  CA  . ARG   A 1 185 ? -14.147 3.720   17.773 1.00 76.21  ? 481 ARG   A CA  1 
ATOM   1418 C  C   . ARG   A 1 185 ? -13.092 4.782   17.524 1.00 80.42  ? 481 ARG   A C   1 
ATOM   1419 O  O   . ARG   A 1 185 ? -12.554 4.891   16.422 1.00 86.12  ? 481 ARG   A O   1 
ATOM   1420 C  CB  . ARG   A 1 185 ? -13.458 2.474   18.339 1.00 75.50  ? 481 ARG   A CB  1 
ATOM   1421 C  CG  . ARG   A 1 185 ? -14.388 1.369   18.728 1.00 77.59  ? 481 ARG   A CG  1 
ATOM   1422 C  CD  . ARG   A 1 185 ? -13.831 0.559   19.890 1.00 75.39  ? 481 ARG   A CD  1 
ATOM   1423 N  NE  . ARG   A 1 185 ? -14.081 1.186   21.185 1.00 79.08  ? 481 ARG   A NE  1 
ATOM   1424 C  CZ  . ARG   A 1 185 ? -13.771 0.617   22.343 1.00 80.37  ? 481 ARG   A CZ  1 
ATOM   1425 N  NH1 . ARG   A 1 185 ? -13.206 -0.585  22.352 1.00 71.04  ? 481 ARG   A NH1 1 
ATOM   1426 N  NH2 . ARG   A 1 185 ? -14.030 1.238   23.489 1.00 87.96  ? 481 ARG   A NH2 1 
ATOM   1427 N  N   . TYR   A 1 186 ? -12.782 5.550   18.566 1.00 71.74  ? 482 TYR   A N   1 
ATOM   1428 C  CA  . TYR   A 1 186 ? -11.740 6.557   18.470 1.00 77.38  ? 482 TYR   A CA  1 
ATOM   1429 C  C   . TYR   A 1 186 ? -10.374 5.931   18.725 1.00 82.56  ? 482 TYR   A C   1 
ATOM   1430 O  O   . TYR   A 1 186 ? -10.234 4.983   19.505 1.00 81.59  ? 482 TYR   A O   1 
ATOM   1431 C  CB  . TYR   A 1 186 ? -12.004 7.705   19.453 1.00 83.90  ? 482 TYR   A CB  1 
ATOM   1432 C  CG  . TYR   A 1 186 ? -13.246 8.504   19.095 1.00 88.75  ? 482 TYR   A CG  1 
ATOM   1433 C  CD1 . TYR   A 1 186 ? -14.240 8.746   20.035 1.00 93.39  ? 482 TYR   A CD1 1 
ATOM   1434 C  CD2 . TYR   A 1 186 ? -13.437 8.993   17.802 1.00 88.37  ? 482 TYR   A CD2 1 
ATOM   1435 C  CE1 . TYR   A 1 186 ? -15.381 9.469   19.703 1.00 94.41  ? 482 TYR   A CE1 1 
ATOM   1436 C  CE2 . TYR   A 1 186 ? -14.575 9.715   17.466 1.00 85.86  ? 482 TYR   A CE2 1 
ATOM   1437 C  CZ  . TYR   A 1 186 ? -15.542 9.951   18.427 1.00 93.31  ? 482 TYR   A CZ  1 
ATOM   1438 O  OH  . TYR   A 1 186 ? -16.678 10.666  18.110 1.00 93.03  ? 482 TYR   A OH  1 
ATOM   1439 N  N   . ALA   A 1 187 ? -9.366  6.476   18.054 1.00 88.78  ? 483 ALA   A N   1 
ATOM   1440 C  CA  . ALA   A 1 187 ? -8.031  5.907   18.118 1.00 89.83  ? 483 ALA   A CA  1 
ATOM   1441 C  C   . ALA   A 1 187 ? -7.392  6.176   19.470 1.00 95.30  ? 483 ALA   A C   1 
ATOM   1442 O  O   . ALA   A 1 187 ? -7.706  7.157   20.146 1.00 90.76  ? 483 ALA   A O   1 
ATOM   1443 C  CB  . ALA   A 1 187 ? -7.148  6.484   17.015 1.00 99.06  ? 483 ALA   A CB  1 
ATOM   1444 N  N   . GLY   A 1 188 ? -6.475  5.294   19.852 1.00 94.36  ? 484 GLY   A N   1 
ATOM   1445 C  CA  . GLY   A 1 188 ? -5.700  5.485   21.056 1.00 104.59 ? 484 GLY   A CA  1 
ATOM   1446 C  C   . GLY   A 1 188 ? -4.214  5.396   20.798 1.00 110.72 ? 484 GLY   A C   1 
ATOM   1447 O  O   . GLY   A 1 188 ? -3.698  4.335   20.438 1.00 110.05 ? 484 GLY   A O   1 
ATOM   1448 N  N   . TYR   A 1 189 ? -3.512  6.508   20.975 1.00 115.80 ? 485 TYR   A N   1 
ATOM   1449 C  CA  . TYR   A 1 189 ? -2.067  6.548   20.815 1.00 118.94 ? 485 TYR   A CA  1 
ATOM   1450 C  C   . TYR   A 1 189 ? -1.433  6.801   22.171 1.00 123.68 ? 485 TYR   A C   1 
ATOM   1451 O  O   . TYR   A 1 189 ? -1.700  7.829   22.806 1.00 116.65 ? 485 TYR   A O   1 
ATOM   1452 C  CB  . TYR   A 1 189 ? -1.638  7.633   19.828 1.00 120.53 ? 485 TYR   A CB  1 
ATOM   1453 C  CG  . TYR   A 1 189 ? -2.557  7.821   18.648 1.00 113.88 ? 485 TYR   A CG  1 
ATOM   1454 C  CD1 . TYR   A 1 189 ? -3.603  8.730   18.707 1.00 113.29 ? 485 TYR   A CD1 1 
ATOM   1455 C  CD2 . TYR   A 1 189 ? -2.372  7.107   17.472 1.00 111.30 ? 485 TYR   A CD2 1 
ATOM   1456 C  CE1 . TYR   A 1 189 ? -4.447  8.918   17.637 1.00 110.11 ? 485 TYR   A CE1 1 
ATOM   1457 C  CE2 . TYR   A 1 189 ? -3.215  7.291   16.390 1.00 111.52 ? 485 TYR   A CE2 1 
ATOM   1458 C  CZ  . TYR   A 1 189 ? -4.247  8.202   16.475 1.00 107.52 ? 485 TYR   A CZ  1 
ATOM   1459 O  OH  . TYR   A 1 189 ? -5.092  8.397   15.409 1.00 96.01  ? 485 TYR   A OH  1 
ATOM   1460 N  N   . LYS   A 1 190 ? -0.601  5.865   22.613 1.00 129.90 ? 486 LYS   A N   1 
ATOM   1461 C  CA  . LYS   A 1 190 ? 0.336   6.157   23.679 1.00 137.32 ? 486 LYS   A CA  1 
ATOM   1462 C  C   . LYS   A 1 190 ? 1.255   7.299   23.244 1.00 145.57 ? 486 LYS   A C   1 
ATOM   1463 O  O   . LYS   A 1 190 ? 1.359   7.634   22.061 1.00 150.53 ? 486 LYS   A O   1 
ATOM   1464 C  CB  . LYS   A 1 190 ? 1.140   4.907   24.023 1.00 140.00 ? 486 LYS   A CB  1 
ATOM   1465 C  CG  . LYS   A 1 190 ? 1.580   4.146   22.782 1.00 141.66 ? 486 LYS   A CG  1 
ATOM   1466 C  CD  . LYS   A 1 190 ? 2.534   3.013   23.108 1.00 143.79 ? 486 LYS   A CD  1 
ATOM   1467 C  CE  . LYS   A 1 190 ? 1.818   1.833   23.739 1.00 135.48 ? 486 LYS   A CE  1 
ATOM   1468 N  NZ  . LYS   A 1 190 ? 2.673   0.614   23.698 1.00 135.38 ? 486 LYS   A NZ  1 
ATOM   1469 N  N   . GLN   A 1 191 ? 1.930   7.902   24.210 1.00 146.53 ? 487 GLN   A N   1 
ATOM   1470 C  CA  . GLN   A 1 191 ? 2.719   9.097   23.961 1.00 151.90 ? 487 GLN   A CA  1 
ATOM   1471 C  C   . GLN   A 1 191 ? 4.200   8.850   24.218 1.00 158.93 ? 487 GLN   A C   1 
ATOM   1472 O  O   . GLN   A 1 191 ? 4.572   7.868   24.872 1.00 160.20 ? 487 GLN   A O   1 
ATOM   1473 C  CB  . GLN   A 1 191 ? 2.225   10.259  24.836 1.00 153.84 ? 487 GLN   A CB  1 
ATOM   1474 C  CG  . GLN   A 1 191 ? 0.893   10.855  24.396 1.00 149.93 ? 487 GLN   A CG  1 
ATOM   1475 C  CD  . GLN   A 1 191 ? 0.991   11.675  23.114 1.00 154.52 ? 487 GLN   A CD  1 
ATOM   1476 O  OE1 . GLN   A 1 191 ? 1.558   11.235  22.110 1.00 156.66 ? 487 GLN   A OE1 1 
ATOM   1477 N  NE2 . GLN   A 1 191 ? 0.430   12.877  23.145 1.00 156.36 ? 487 GLN   A NE2 1 
ATOM   1478 N  N   . PRO   A 1 192 ? 5.080   9.715   23.699 1.00 165.17 ? 488 PRO   A N   1 
ATOM   1479 C  CA  . PRO   A 1 192 ? 6.505   9.596   24.050 1.00 171.60 ? 488 PRO   A CA  1 
ATOM   1480 C  C   . PRO   A 1 192 ? 6.778   9.807   25.529 1.00 172.78 ? 488 PRO   A C   1 
ATOM   1481 O  O   . PRO   A 1 192 ? 7.758   9.262   26.053 1.00 177.12 ? 488 PRO   A O   1 
ATOM   1482 C  CB  . PRO   A 1 192 ? 7.173   10.677  23.187 1.00 179.64 ? 488 PRO   A CB  1 
ATOM   1483 C  CG  . PRO   A 1 192 ? 6.068   11.606  22.791 1.00 177.23 ? 488 PRO   A CG  1 
ATOM   1484 C  CD  . PRO   A 1 192 ? 4.856   10.741  22.666 1.00 168.70 ? 488 PRO   A CD  1 
ATOM   1485 N  N   . ASP   A 1 193 ? 5.941   10.578  26.223 1.00 168.15 ? 489 ASP   A N   1 
ATOM   1486 C  CA  . ASP   A 1 193 ? 6.061   10.745  27.664 1.00 165.64 ? 489 ASP   A CA  1 
ATOM   1487 C  C   . ASP   A 1 193 ? 5.301   9.676   28.440 1.00 156.26 ? 489 ASP   A C   1 
ATOM   1488 O  O   . ASP   A 1 193 ? 5.012   9.873   29.626 1.00 151.45 ? 489 ASP   A O   1 
ATOM   1489 C  CB  . ASP   A 1 193 ? 5.580   12.135  28.083 1.00 168.21 ? 489 ASP   A CB  1 
ATOM   1490 C  CG  . ASP   A 1 193 ? 4.139   12.392  27.704 1.00 163.19 ? 489 ASP   A CG  1 
ATOM   1491 O  OD1 . ASP   A 1 193 ? 3.834   12.400  26.492 1.00 163.08 ? 489 ASP   A OD1 1 
ATOM   1492 O  OD2 . ASP   A 1 193 ? 3.311   12.578  28.621 1.00 159.70 ? 489 ASP   A OD2 1 
ATOM   1493 N  N   . GLY   A 1 194 ? 4.964   8.559   27.796 1.00 151.76 ? 490 GLY   A N   1 
ATOM   1494 C  CA  . GLY   A 1 194 ? 4.343   7.436   28.464 1.00 146.65 ? 490 GLY   A CA  1 
ATOM   1495 C  C   . GLY   A 1 194 ? 2.856   7.554   28.721 1.00 142.99 ? 490 GLY   A C   1 
ATOM   1496 O  O   . GLY   A 1 194 ? 2.247   6.573   29.170 1.00 138.90 ? 490 GLY   A O   1 
ATOM   1497 N  N   . SER   A 1 195 ? 2.244   8.711   28.465 1.00 144.67 ? 491 SER   A N   1 
ATOM   1498 C  CA  . SER   A 1 195 ? 0.805   8.855   28.665 1.00 140.07 ? 491 SER   A CA  1 
ATOM   1499 C  C   . SER   A 1 195 ? 0.043   8.403   27.421 1.00 138.47 ? 491 SER   A C   1 
ATOM   1500 O  O   . SER   A 1 195 ? 0.545   7.578   26.651 1.00 138.89 ? 491 SER   A O   1 
ATOM   1501 C  CB  . SER   A 1 195 ? 0.449   10.298  29.031 1.00 140.05 ? 491 SER   A CB  1 
ATOM   1502 O  OG  . SER   A 1 195 ? 0.914   11.211  28.054 1.00 145.82 ? 491 SER   A OG  1 
ATOM   1503 N  N   . THR   A 1 196 ? -1.165  8.930   27.211 1.00 136.09 ? 492 THR   A N   1 
ATOM   1504 C  CA  . THR   A 1 196 ? -2.032  8.445   26.142 1.00 129.65 ? 492 THR   A CA  1 
ATOM   1505 C  C   . THR   A 1 196 ? -2.903  9.574   25.605 1.00 129.84 ? 492 THR   A C   1 
ATOM   1506 O  O   . THR   A 1 196 ? -3.471  10.344  26.384 1.00 133.06 ? 492 THR   A O   1 
ATOM   1507 C  CB  . THR   A 1 196 ? -2.928  7.299   26.638 1.00 121.86 ? 492 THR   A CB  1 
ATOM   1508 O  OG1 . THR   A 1 196 ? -2.119  6.206   27.099 1.00 120.24 ? 492 THR   A OG1 1 
ATOM   1509 C  CG2 . THR   A 1 196 ? -3.855  6.814   25.518 1.00 111.58 ? 492 THR   A CG2 1 
ATOM   1510 N  N   . LEU   A 1 197 ? -3.006  9.657   24.278 1.00 123.78 ? 493 LEU   A N   1 
ATOM   1511 C  CA  . LEU   A 1 197 ? -3.968  10.513  23.596 1.00 120.76 ? 493 LEU   A CA  1 
ATOM   1512 C  C   . LEU   A 1 197 ? -5.033  9.653   22.926 1.00 112.70 ? 493 LEU   A C   1 
ATOM   1513 O  O   . LEU   A 1 197 ? -4.753  8.549   22.451 1.00 100.64 ? 493 LEU   A O   1 
ATOM   1514 C  CB  . LEU   A 1 197 ? -3.286  11.403  22.542 1.00 121.69 ? 493 LEU   A CB  1 
ATOM   1515 C  CG  . LEU   A 1 197 ? -4.169  12.441  21.837 1.00 119.76 ? 493 LEU   A CG  1 
ATOM   1516 C  CD1 . LEU   A 1 197 ? -4.967  13.238  22.857 1.00 119.42 ? 493 LEU   A CD1 1 
ATOM   1517 C  CD2 . LEU   A 1 197 ? -3.348  13.382  20.960 1.00 124.49 ? 493 LEU   A CD2 1 
ATOM   1518 N  N   . GLY   A 1 198 ? -6.251  10.162  22.900 1.00 119.05 ? 494 GLY   A N   1 
ATOM   1519 C  CA  . GLY   A 1 198 ? -7.355  9.481   22.232 1.00 117.47 ? 494 GLY   A CA  1 
ATOM   1520 C  C   . GLY   A 1 198 ? -8.101  8.560   23.186 1.00 110.93 ? 494 GLY   A C   1 
ATOM   1521 O  O   . GLY   A 1 198 ? -8.618  9.015   24.204 1.00 119.54 ? 494 GLY   A O   1 
ATOM   1522 N  N   . ASP   A 1 199 ? -8.135  7.275   22.861 1.00 93.09  ? 495 ASP   A N   1 
ATOM   1523 C  CA  . ASP   A 1 199 ? -8.857  6.294   23.668 1.00 80.09  ? 495 ASP   A CA  1 
ATOM   1524 C  C   . ASP   A 1 199 ? -7.897  5.204   24.129 1.00 86.67  ? 495 ASP   A C   1 
ATOM   1525 O  O   . ASP   A 1 199 ? -7.487  4.361   23.311 1.00 81.67  ? 495 ASP   A O   1 
ATOM   1526 C  CB  . ASP   A 1 199 ? -10.022 5.690   22.880 1.00 81.79  ? 495 ASP   A CB  1 
ATOM   1527 C  CG  . ASP   A 1 199 ? -11.058 5.046   23.787 1.00 88.02  ? 495 ASP   A CG  1 
ATOM   1528 O  OD1 . ASP   A 1 199 ? -10.680 4.676   24.924 1.00 82.62  ? 495 ASP   A OD1 1 
ATOM   1529 O  OD2 . ASP   A 1 199 ? -12.237 4.917   23.389 1.00 83.84  ? 495 ASP   A OD2 1 
ATOM   1530 N  N   . PRO   A 1 200 ? -7.509  5.168   25.408 1.00 88.26  ? 496 PRO   A N   1 
ATOM   1531 C  CA  . PRO   A 1 200 ? -6.553  4.139   25.856 1.00 87.29  ? 496 PRO   A CA  1 
ATOM   1532 C  C   . PRO   A 1 200 ? -7.031  2.708   25.635 1.00 84.65  ? 496 PRO   A C   1 
ATOM   1533 O  O   . PRO   A 1 200 ? -6.190  1.807   25.545 1.00 91.00  ? 496 PRO   A O   1 
ATOM   1534 C  CB  . PRO   A 1 200 ? -6.372  4.451   27.350 1.00 92.80  ? 496 PRO   A CB  1 
ATOM   1535 C  CG  . PRO   A 1 200 ? -6.757  5.900   27.491 1.00 93.50  ? 496 PRO   A CG  1 
ATOM   1536 C  CD  . PRO   A 1 200 ? -7.873  6.098   26.489 1.00 90.22  ? 496 PRO   A CD  1 
ATOM   1537 N  N   . ALA   A 1 201 ? -8.342  2.473   25.527 1.00 83.03  ? 497 ALA   A N   1 
ATOM   1538 C  CA  . ALA   A 1 201 ? -8.847  1.126   25.261 1.00 84.49  ? 497 ALA   A CA  1 
ATOM   1539 C  C   . ALA   A 1 201 ? -8.288  0.558   23.964 1.00 89.12  ? 497 ALA   A C   1 
ATOM   1540 O  O   . ALA   A 1 201 ? -7.982  -0.636  23.875 1.00 89.92  ? 497 ALA   A O   1 
ATOM   1541 C  CB  . ALA   A 1 201 ? -10.375 1.140   25.190 1.00 78.69  ? 497 ALA   A CB  1 
ATOM   1542 N  N   . ASN   A 1 202 ? -8.153  1.397   22.948 1.00 94.53  ? 498 ASN   A N   1 
ATOM   1543 C  CA  . ASN   A 1 202 ? -7.877  0.943   21.597 1.00 94.41  ? 498 ASN   A CA  1 
ATOM   1544 C  C   . ASN   A 1 202 ? -6.403  1.036   21.236 1.00 98.69  ? 498 ASN   A C   1 
ATOM   1545 O  O   . ASN   A 1 202 ? -6.057  0.873   20.063 1.00 96.87  ? 498 ASN   A O   1 
ATOM   1546 C  CB  . ASN   A 1 202 ? -8.722  1.752   20.616 1.00 92.78  ? 498 ASN   A CB  1 
ATOM   1547 C  CG  . ASN   A 1 202 ? -10.182 1.805   21.024 1.00 85.17  ? 498 ASN   A CG  1 
ATOM   1548 O  OD1 . ASN   A 1 202 ? -10.789 0.775   21.324 1.00 82.59  ? 498 ASN   A OD1 1 
ATOM   1549 N  ND2 . ASN   A 1 202 ? -10.752 3.007   21.049 1.00 84.75  ? 498 ASN   A ND2 1 
ATOM   1550 N  N   . VAL   A 1 203 ? -5.529  1.268   22.220 1.00 96.48  ? 499 VAL   A N   1 
ATOM   1551 C  CA  . VAL   A 1 203 ? -4.127  1.565   21.925 1.00 97.29  ? 499 VAL   A CA  1 
ATOM   1552 C  C   . VAL   A 1 203 ? -3.462  0.400   21.203 1.00 90.60  ? 499 VAL   A C   1 
ATOM   1553 O  O   . VAL   A 1 203 ? -2.657  0.602   20.286 1.00 93.60  ? 499 VAL   A O   1 
ATOM   1554 C  CB  . VAL   A 1 203 ? -3.373  1.935   23.214 1.00 99.77  ? 499 VAL   A CB  1 
ATOM   1555 C  CG1 . VAL   A 1 203 ? -1.878  1.899   22.975 1.00 103.79 ? 499 VAL   A CG1 1 
ATOM   1556 C  CG2 . VAL   A 1 203 ? -3.788  3.315   23.682 1.00 106.84 ? 499 VAL   A CG2 1 
ATOM   1557 N  N   . GLN   A 1 204 ? -3.777  -0.835  21.603 1.00 86.65  ? 500 GLN   A N   1 
ATOM   1558 C  CA  . GLN   A 1 204 ? -3.243  -1.983  20.876 1.00 91.40  ? 500 GLN   A CA  1 
ATOM   1559 C  C   . GLN   A 1 204 ? -3.837  -2.061  19.478 1.00 89.92  ? 500 GLN   A C   1 
ATOM   1560 O  O   . GLN   A 1 204 ? -3.106  -2.182  18.489 1.00 94.40  ? 500 GLN   A O   1 
ATOM   1561 C  CB  . GLN   A 1 204 ? -3.508  -3.284  21.630 1.00 92.38  ? 500 GLN   A CB  1 
ATOM   1562 C  CG  . GLN   A 1 204 ? -3.005  -4.509  20.876 1.00 96.32  ? 500 GLN   A CG  1 
ATOM   1563 C  CD  . GLN   A 1 204 ? -3.079  -5.791  21.682 1.00 106.39 ? 500 GLN   A CD  1 
ATOM   1564 O  OE1 . GLN   A 1 204 ? -3.701  -5.840  22.745 1.00 108.54 ? 500 GLN   A OE1 1 
ATOM   1565 N  NE2 . GLN   A 1 204 ? -2.436  -6.839  21.182 1.00 112.00 ? 500 GLN   A NE2 1 
ATOM   1566 N  N   . PHE   A 1 205 ? -5.168  -2.001  19.381 1.00 87.61  ? 501 PHE   A N   1 
ATOM   1567 C  CA  . PHE   A 1 205 ? -5.821  -2.047  18.078 1.00 87.39  ? 501 PHE   A CA  1 
ATOM   1568 C  C   . PHE   A 1 205 ? -5.387  -0.877  17.201 1.00 86.50  ? 501 PHE   A C   1 
ATOM   1569 O  O   . PHE   A 1 205 ? -5.167  -1.045  15.994 1.00 86.20  ? 501 PHE   A O   1 
ATOM   1570 C  CB  . PHE   A 1 205 ? -7.338  -2.062  18.255 1.00 85.97  ? 501 PHE   A CB  1 
ATOM   1571 C  CG  . PHE   A 1 205 ? -8.088  -2.028  16.963 1.00 92.94  ? 501 PHE   A CG  1 
ATOM   1572 C  CD1 . PHE   A 1 205 ? -8.175  -3.162  16.165 1.00 93.08  ? 501 PHE   A CD1 1 
ATOM   1573 C  CD2 . PHE   A 1 205 ? -8.693  -0.859  16.529 1.00 95.06  ? 501 PHE   A CD2 1 
ATOM   1574 C  CE1 . PHE   A 1 205 ? -8.857  -3.128  14.966 1.00 88.89  ? 501 PHE   A CE1 1 
ATOM   1575 C  CE2 . PHE   A 1 205 ? -9.378  -0.824  15.339 1.00 87.66  ? 501 PHE   A CE2 1 
ATOM   1576 C  CZ  . PHE   A 1 205 ? -9.454  -1.960  14.554 1.00 90.20  ? 501 PHE   A CZ  1 
ATOM   1577 N  N   . THR   A 1 206 ? -5.263  0.318   17.788 1.00 82.02  ? 502 THR   A N   1 
ATOM   1578 C  CA  . THR   A 1 206 ? -4.725  1.451   17.040 1.00 92.51  ? 502 THR   A CA  1 
ATOM   1579 C  C   . THR   A 1 206 ? -3.342  1.131   16.487 1.00 100.57 ? 502 THR   A C   1 
ATOM   1580 O  O   . THR   A 1 206 ? -2.993  1.564   15.384 1.00 97.51  ? 502 THR   A O   1 
ATOM   1581 C  CB  . THR   A 1 206 ? -4.682  2.703   17.928 1.00 93.87  ? 502 THR   A CB  1 
ATOM   1582 O  OG1 . THR   A 1 206 ? -6.020  3.096   18.261 1.00 89.84  ? 502 THR   A OG1 1 
ATOM   1583 C  CG2 . THR   A 1 206 ? -3.981  3.874   17.218 1.00 84.25  ? 502 THR   A CG2 1 
ATOM   1584 N  N   . GLU   A 1 207 ? -2.543  0.362   17.232 1.00 108.51 ? 503 GLU   A N   1 
ATOM   1585 C  CA  . GLU   A 1 207 ? -1.213  -0.005  16.756 1.00 116.75 ? 503 GLU   A CA  1 
ATOM   1586 C  C   . GLU   A 1 207 ? -1.257  -1.120  15.718 1.00 112.22 ? 503 GLU   A C   1 
ATOM   1587 O  O   . GLU   A 1 207 ? -0.435  -1.130  14.792 1.00 114.39 ? 503 GLU   A O   1 
ATOM   1588 C  CB  . GLU   A 1 207 ? -0.325  -0.403  17.934 1.00 124.09 ? 503 GLU   A CB  1 
ATOM   1589 C  CG  . GLU   A 1 207 ? 0.393   0.777   18.566 1.00 138.44 ? 503 GLU   A CG  1 
ATOM   1590 C  CD  . GLU   A 1 207 ? 0.516   0.651   20.072 1.00 148.50 ? 503 GLU   A CD  1 
ATOM   1591 O  OE1 . GLU   A 1 207 ? 0.512   -0.492  20.576 1.00 149.40 ? 503 GLU   A OE1 1 
ATOM   1592 O  OE2 . GLU   A 1 207 ? 0.607   1.697   20.751 1.00 152.55 ? 503 GLU   A OE2 1 
ATOM   1593 N  N   . ILE   A 1 208 ? -2.204  -2.052  15.844 1.00 105.30 ? 504 ILE   A N   1 
ATOM   1594 C  CA  . ILE   A 1 208 ? -2.346  -3.103  14.837 1.00 99.25  ? 504 ILE   A CA  1 
ATOM   1595 C  C   . ILE   A 1 208 ? -2.687  -2.497  13.482 1.00 97.74  ? 504 ILE   A C   1 
ATOM   1596 O  O   . ILE   A 1 208 ? -2.163  -2.922  12.447 1.00 91.88  ? 504 ILE   A O   1 
ATOM   1597 C  CB  . ILE   A 1 208 ? -3.400  -4.135  15.277 1.00 92.95  ? 504 ILE   A CB  1 
ATOM   1598 C  CG1 . ILE   A 1 208 ? -2.926  -4.884  16.521 1.00 90.99  ? 504 ILE   A CG1 1 
ATOM   1599 C  CG2 . ILE   A 1 208 ? -3.675  -5.120  14.155 1.00 94.40  ? 504 ILE   A CG2 1 
ATOM   1600 C  CD1 . ILE   A 1 208 ? -4.044  -5.590  17.281 1.00 91.76  ? 504 ILE   A CD1 1 
ATOM   1601 N  N   . CYS   A 1 209 ? -3.570  -1.493  13.465 1.00 96.33  ? 505 CYS   A N   1 
ATOM   1602 C  CA  . CYS   A 1 209 ? -3.855  -0.783  12.223 1.00 96.39  ? 505 CYS   A CA  1 
ATOM   1603 C  C   . CYS   A 1 209 ? -2.597  -0.134  11.664 1.00 102.58 ? 505 CYS   A C   1 
ATOM   1604 O  O   . CYS   A 1 209 ? -2.360  -0.167  10.447 1.00 108.04 ? 505 CYS   A O   1 
ATOM   1605 C  CB  . CYS   A 1 209 ? -4.942  0.269   12.450 1.00 95.00  ? 505 CYS   A CB  1 
ATOM   1606 S  SG  . CYS   A 1 209 ? -6.523  -0.393  13.017 1.00 91.43  ? 505 CYS   A SG  1 
ATOM   1607 N  N   . ILE   A 1 210 ? -1.776  0.464   12.532 1.00 101.77 ? 506 ILE   A N   1 
ATOM   1608 C  CA  . ILE   A 1 210 ? -0.509  1.030   12.075 1.00 108.59 ? 506 ILE   A CA  1 
ATOM   1609 C  C   . ILE   A 1 210 ? 0.397   -0.073  11.541 1.00 113.45 ? 506 ILE   A C   1 
ATOM   1610 O  O   . ILE   A 1 210 ? 1.095   0.106   10.534 1.00 113.72 ? 506 ILE   A O   1 
ATOM   1611 C  CB  . ILE   A 1 210 ? 0.172   1.824   13.205 1.00 107.36 ? 506 ILE   A CB  1 
ATOM   1612 C  CG1 . ILE   A 1 210 ? -0.714  2.971   13.692 1.00 102.92 ? 506 ILE   A CG1 1 
ATOM   1613 C  CG2 . ILE   A 1 210 ? 1.498   2.388   12.727 1.00 115.73 ? 506 ILE   A CG2 1 
ATOM   1614 C  CD1 . ILE   A 1 210 ? -0.235  3.568   15.034 1.00 100.22 ? 506 ILE   A CD1 1 
ATOM   1615 N  N   . GLN   A 1 211 ? 0.392   -1.235  12.205 1.00 114.48 ? 507 GLN   A N   1 
ATOM   1616 C  CA  . GLN   A 1 211 ? 1.155   -2.384  11.724 1.00 116.05 ? 507 GLN   A CA  1 
ATOM   1617 C  C   . GLN   A 1 211 ? 0.734   -2.782  10.312 1.00 113.70 ? 507 GLN   A C   1 
ATOM   1618 O  O   . GLN   A 1 211 ? 1.585   -3.043  9.452  1.00 108.71 ? 507 GLN   A O   1 
ATOM   1619 C  CB  . GLN   A 1 211 ? 0.986   -3.560  12.689 1.00 114.46 ? 507 GLN   A CB  1 
ATOM   1620 C  CG  . GLN   A 1 211 ? 2.011   -3.614  13.817 1.00 119.10 ? 507 GLN   A CG  1 
ATOM   1621 C  CD  . GLN   A 1 211 ? 3.257   -4.396  13.433 1.00 126.24 ? 507 GLN   A CD  1 
ATOM   1622 O  OE1 . GLN   A 1 211 ? 3.204   -5.287  12.584 1.00 129.43 ? 507 GLN   A OE1 1 
ATOM   1623 N  NE2 . GLN   A 1 211 ? 4.388   -4.060  14.054 1.00 127.40 ? 507 GLN   A NE2 1 
ATOM   1624 N  N   . GLN   A 1 212 ? -0.572  -2.832  10.051 1.00 115.20 ? 508 GLN   A N   1 
ATOM   1625 C  CA  . GLN   A 1 212 ? -1.081  -3.168  8.726  1.00 116.67 ? 508 GLN   A CA  1 
ATOM   1626 C  C   . GLN   A 1 212 ? -1.061  -1.987  7.768  1.00 115.97 ? 508 GLN   A C   1 
ATOM   1627 O  O   . GLN   A 1 212 ? -1.560  -2.114  6.644  1.00 113.64 ? 508 GLN   A O   1 
ATOM   1628 C  CB  . GLN   A 1 212 ? -2.501  -3.732  8.828  1.00 115.18 ? 508 GLN   A CB  1 
ATOM   1629 C  CG  . GLN   A 1 212 ? -2.568  -5.074  9.525  1.00 117.61 ? 508 GLN   A CG  1 
ATOM   1630 C  CD  . GLN   A 1 212 ? -1.640  -6.091  8.897  1.00 126.77 ? 508 GLN   A CD  1 
ATOM   1631 O  OE1 . GLN   A 1 212 ? -0.717  -6.589  9.543  1.00 132.37 ? 508 GLN   A OE1 1 
ATOM   1632 N  NE2 . GLN   A 1 212 ? -1.880  -6.409  7.629  1.00 125.07 ? 508 GLN   A NE2 1 
ATOM   1633 N  N   . GLY   A 1 213 ? -0.511  -0.849  8.180  1.00 120.09 ? 509 GLY   A N   1 
ATOM   1634 C  CA  . GLY   A 1 213 ? -0.280  0.260   7.281  1.00 121.37 ? 509 GLY   A CA  1 
ATOM   1635 C  C   . GLY   A 1 213 ? -1.128  1.495   7.490  1.00 117.98 ? 509 GLY   A C   1 
ATOM   1636 O  O   . GLY   A 1 213 ? -1.049  2.416   6.668  1.00 116.43 ? 509 GLY   A O   1 
ATOM   1637 N  N   . TRP   A 1 214 ? -1.930  1.558   8.551  1.00 117.42 ? 510 TRP   A N   1 
ATOM   1638 C  CA  . TRP   A 1 214 ? -2.739  2.748   8.776  1.00 118.56 ? 510 TRP   A CA  1 
ATOM   1639 C  C   . TRP   A 1 214 ? -1.843  3.953   9.014  1.00 122.69 ? 510 TRP   A C   1 
ATOM   1640 O  O   . TRP   A 1 214 ? -0.824  3.872   9.709  1.00 117.12 ? 510 TRP   A O   1 
ATOM   1641 C  CB  . TRP   A 1 214 ? -3.685  2.568   9.968  1.00 114.66 ? 510 TRP   A CB  1 
ATOM   1642 C  CG  . TRP   A 1 214 ? -4.722  3.659   10.065 1.00 110.88 ? 510 TRP   A CG  1 
ATOM   1643 C  CD1 . TRP   A 1 214 ? -5.535  4.096   9.060  1.00 106.98 ? 510 TRP   A CD1 1 
ATOM   1644 C  CD2 . TRP   A 1 214 ? -5.056  4.441   11.221 1.00 109.32 ? 510 TRP   A CD2 1 
ATOM   1645 N  NE1 . TRP   A 1 214 ? -6.355  5.099   9.517  1.00 105.50 ? 510 TRP   A NE1 1 
ATOM   1646 C  CE2 . TRP   A 1 214 ? -6.080  5.331   10.838 1.00 105.64 ? 510 TRP   A CE2 1 
ATOM   1647 C  CE3 . TRP   A 1 214 ? -4.592  4.474   12.543 1.00 108.02 ? 510 TRP   A CE3 1 
ATOM   1648 C  CZ2 . TRP   A 1 214 ? -6.647  6.246   11.723 1.00 104.75 ? 510 TRP   A CZ2 1 
ATOM   1649 C  CZ3 . TRP   A 1 214 ? -5.158  5.385   13.423 1.00 105.96 ? 510 TRP   A CZ3 1 
ATOM   1650 C  CH2 . TRP   A 1 214 ? -6.175  6.256   13.009 1.00 108.02 ? 510 TRP   A CH2 1 
ATOM   1651 N  N   . LYS   A 1 215 ? -2.223  5.074   8.416  1.00 123.74 ? 511 LYS   A N   1 
ATOM   1652 C  CA  . LYS   A 1 215 ? -1.562  6.348   8.653  1.00 128.71 ? 511 LYS   A CA  1 
ATOM   1653 C  C   . LYS   A 1 215 ? -2.397  7.128   9.660  1.00 121.42 ? 511 LYS   A C   1 
ATOM   1654 O  O   . LYS   A 1 215 ? -3.518  7.552   9.360  1.00 119.81 ? 511 LYS   A O   1 
ATOM   1655 C  CB  . LYS   A 1 215 ? -1.366  7.106   7.345  1.00 130.86 ? 511 LYS   A CB  1 
ATOM   1656 C  CG  . LYS   A 1 215 ? -0.285  6.490   6.456  1.00 137.81 ? 511 LYS   A CG  1 
ATOM   1657 C  CD  . LYS   A 1 215 ? 1.112   7.064   6.747  1.00 147.29 ? 511 LYS   A CD  1 
ATOM   1658 C  CE  . LYS   A 1 215 ? 1.770   6.470   7.999  1.00 146.01 ? 511 LYS   A CE  1 
ATOM   1659 N  NZ  . LYS   A 1 215 ? 2.843   7.341   8.566  1.00 150.57 ? 511 LYS   A NZ  1 
ATOM   1660 N  N   . ALA   A 1 216 ? -1.858  7.300   10.843 1.00 117.71 ? 512 ALA   A N   1 
ATOM   1661 C  CA  . ALA   A 1 216 ? -2.636  7.790   11.972 1.00 110.91 ? 512 ALA   A CA  1 
ATOM   1662 C  C   . ALA   A 1 216 ? -2.577  9.310   12.044 1.00 116.96 ? 512 ALA   A C   1 
ATOM   1663 O  O   . ALA   A 1 216 ? -1.479  9.881   12.048 1.00 122.60 ? 512 ALA   A O   1 
ATOM   1664 C  CB  . ALA   A 1 216 ? -2.118  7.192   13.268 1.00 107.88 ? 512 ALA   A CB  1 
ATOM   1665 N  N   . PRO   A 1 217 ? -3.728  9.995   12.101 1.00 114.93 ? 513 PRO   A N   1 
ATOM   1666 C  CA  . PRO   A 1 217 ? -3.722  11.455  12.272 1.00 118.84 ? 513 PRO   A CA  1 
ATOM   1667 C  C   . PRO   A 1 217 ? -3.520  11.889  13.717 1.00 125.84 ? 513 PRO   A C   1 
ATOM   1668 O  O   . PRO   A 1 217 ? -4.059  12.922  14.125 1.00 130.11 ? 513 PRO   A O   1 
ATOM   1669 C  CB  . PRO   A 1 217 ? -5.110  11.868  11.768 1.00 114.86 ? 513 PRO   A CB  1 
ATOM   1670 C  CG  . PRO   A 1 217 ? -5.966  10.671  12.024 1.00 108.74 ? 513 PRO   A CG  1 
ATOM   1671 C  CD  . PRO   A 1 217 ? -5.081  9.467   11.847 1.00 110.96 ? 513 PRO   A CD  1 
ATOM   1672 N  N   . ARG   A 1 218 ? -2.738  11.108  14.473 1.00 128.38 ? 514 ARG   A N   1 
ATOM   1673 C  CA  . ARG   A 1 218 ? -2.502  11.213  15.916 1.00 127.15 ? 514 ARG   A CA  1 
ATOM   1674 C  C   . ARG   A 1 218 ? -3.154  12.391  16.628 1.00 126.10 ? 514 ARG   A C   1 
ATOM   1675 O  O   . ARG   A 1 218 ? -2.461  13.287  17.123 1.00 130.54 ? 514 ARG   A O   1 
ATOM   1676 C  CB  . ARG   A 1 218 ? -0.998  11.239  16.192 1.00 134.67 ? 514 ARG   A CB  1 
ATOM   1677 C  CG  . ARG   A 1 218 ? -0.353  9.898   15.946 1.00 135.67 ? 514 ARG   A CG  1 
ATOM   1678 C  CD  . ARG   A 1 218 ? 1.016   9.761   16.588 1.00 141.71 ? 514 ARG   A CD  1 
ATOM   1679 N  NE  . ARG   A 1 218 ? 1.263   8.374   16.979 1.00 137.90 ? 514 ARG   A NE  1 
ATOM   1680 C  CZ  . ARG   A 1 218 ? 1.439   7.370   16.123 1.00 135.14 ? 514 ARG   A CZ  1 
ATOM   1681 N  NH1 . ARG   A 1 218 ? 1.651   6.141   16.574 1.00 129.63 ? 514 ARG   A NH1 1 
ATOM   1682 N  NH2 . ARG   A 1 218 ? 1.397   7.587   14.814 1.00 140.00 ? 514 ARG   A NH2 1 
ATOM   1683 N  N   . GLY   A 1 219 ? -4.484  12.382  16.700 1.00 120.67 ? 515 GLY   A N   1 
ATOM   1684 C  CA  . GLY   A 1 219 ? -5.210  13.327  17.527 1.00 119.93 ? 515 GLY   A CA  1 
ATOM   1685 C  C   . GLY   A 1 219 ? -6.084  12.618  18.543 1.00 114.76 ? 515 GLY   A C   1 
ATOM   1686 O  O   . GLY   A 1 219 ? -5.819  11.467  18.900 1.00 104.07 ? 515 GLY   A O   1 
ATOM   1687 N  N   . ARG   A 1 220 ? -7.139  13.285  19.004 1.00 120.90 ? 516 ARG   A N   1 
ATOM   1688 C  CA  . ARG   A 1 220 ? -8.081  12.680  19.937 1.00 122.69 ? 516 ARG   A CA  1 
ATOM   1689 C  C   . ARG   A 1 220 ? -9.071  11.778  19.215 1.00 122.05 ? 516 ARG   A C   1 
ATOM   1690 O  O   . ARG   A 1 220 ? -8.850  10.571  19.062 1.00 121.95 ? 516 ARG   A O   1 
ATOM   1691 C  CB  . ARG   A 1 220 ? -8.852  13.766  20.688 1.00 124.32 ? 516 ARG   A CB  1 
ATOM   1692 C  CG  . ARG   A 1 220 ? -9.230  13.422  22.113 1.00 123.40 ? 516 ARG   A CG  1 
ATOM   1693 C  CD  . ARG   A 1 220 ? -8.375  14.239  23.054 1.00 130.64 ? 516 ARG   A CD  1 
ATOM   1694 N  NE  . ARG   A 1 220 ? -9.056  14.570  24.299 1.00 132.31 ? 516 ARG   A NE  1 
ATOM   1695 C  CZ  . ARG   A 1 220 ? -8.778  14.009  25.468 1.00 130.75 ? 516 ARG   A CZ  1 
ATOM   1696 N  NH1 . ARG   A 1 220 ? -7.827  13.088  25.548 1.00 127.12 ? 516 ARG   A NH1 1 
ATOM   1697 N  NH2 . ARG   A 1 220 ? -9.443  14.374  26.556 1.00 134.04 ? 516 ARG   A NH2 1 
ATOM   1698 N  N   . PHE   A 1 221 ? -10.165 12.384  18.756 1.00 112.61 ? 517 PHE   A N   1 
ATOM   1699 C  CA  . PHE   A 1 221 ? -11.323 11.658  18.248 1.00 102.44 ? 517 PHE   A CA  1 
ATOM   1700 C  C   . PHE   A 1 221 ? -11.129 11.315  16.767 1.00 109.44 ? 517 PHE   A C   1 
ATOM   1701 O  O   . PHE   A 1 221 ? -11.866 11.742  15.876 1.00 115.64 ? 517 PHE   A O   1 
ATOM   1702 C  CB  . PHE   A 1 221 ? -12.583 12.476  18.495 1.00 99.48  ? 517 PHE   A CB  1 
ATOM   1703 C  CG  . PHE   A 1 221 ? -12.776 12.885  19.941 1.00 98.51  ? 517 PHE   A CG  1 
ATOM   1704 C  CD1 . PHE   A 1 221 ? -12.459 14.166  20.366 1.00 104.67 ? 517 PHE   A CD1 1 
ATOM   1705 C  CD2 . PHE   A 1 221 ? -13.268 11.986  20.868 1.00 87.56  ? 517 PHE   A CD2 1 
ATOM   1706 C  CE1 . PHE   A 1 221 ? -12.638 14.541  21.689 1.00 111.16 ? 517 PHE   A CE1 1 
ATOM   1707 C  CE2 . PHE   A 1 221 ? -13.454 12.361  22.193 1.00 97.24  ? 517 PHE   A CE2 1 
ATOM   1708 C  CZ  . PHE   A 1 221 ? -13.129 13.638  22.604 1.00 99.21  ? 517 PHE   A CZ  1 
ATOM   1709 N  N   . ASP   A 1 222 ? -10.091 10.516  16.530 1.00 107.45 ? 518 ASP   A N   1 
ATOM   1710 C  CA  . ASP   A 1 222 ? -9.753  10.000  15.210 1.00 96.45  ? 518 ASP   A CA  1 
ATOM   1711 C  C   . ASP   A 1 222 ? -10.450 8.658   15.023 1.00 90.66  ? 518 ASP   A C   1 
ATOM   1712 O  O   . ASP   A 1 222 ? -10.027 7.649   15.596 1.00 90.59  ? 518 ASP   A O   1 
ATOM   1713 C  CB  . ASP   A 1 222 ? -8.242  9.848   15.070 1.00 95.15  ? 518 ASP   A CB  1 
ATOM   1714 C  CG  . ASP   A 1 222 ? -7.510  11.161  15.218 1.00 108.49 ? 518 ASP   A CG  1 
ATOM   1715 O  OD1 . ASP   A 1 222 ? -8.178  12.215  15.232 1.00 114.78 ? 518 ASP   A OD1 1 
ATOM   1716 O  OD2 . ASP   A 1 222 ? -6.265  11.137  15.327 1.00 116.75 ? 518 ASP   A OD2 1 
ATOM   1717 N  N   . VAL   A 1 223 ? -11.525 8.651   14.230 1.00 89.78  ? 519 VAL   A N   1 
ATOM   1718 C  CA  . VAL   A 1 223 ? -12.230 7.412   13.920 1.00 85.80  ? 519 VAL   A CA  1 
ATOM   1719 C  C   . VAL   A 1 223 ? -11.240 6.391   13.376 1.00 85.88  ? 519 VAL   A C   1 
ATOM   1720 O  O   . VAL   A 1 223 ? -10.402 6.706   12.525 1.00 85.10  ? 519 VAL   A O   1 
ATOM   1721 C  CB  . VAL   A 1 223 ? -13.363 7.688   12.919 1.00 85.31  ? 519 VAL   A CB  1 
ATOM   1722 C  CG1 . VAL   A 1 223 ? -14.214 6.458   12.705 1.00 76.93  ? 519 VAL   A CG1 1 
ATOM   1723 C  CG2 . VAL   A 1 223 ? -14.221 8.863   13.389 1.00 91.58  ? 519 VAL   A CG2 1 
ATOM   1724 N  N   . LEU   A 1 224 ? -11.319 5.163   13.878 1.00 85.05  ? 520 LEU   A N   1 
ATOM   1725 C  CA  . LEU   A 1 224 ? -10.404 4.126   13.428 1.00 85.74  ? 520 LEU   A CA  1 
ATOM   1726 C  C   . LEU   A 1 224 ? -10.859 3.530   12.101 1.00 82.00  ? 520 LEU   A C   1 
ATOM   1727 O  O   . LEU   A 1 224 ? -12.029 3.633   11.725 1.00 76.47  ? 520 LEU   A O   1 
ATOM   1728 C  CB  . LEU   A 1 224 ? -10.301 3.024   14.474 1.00 76.17  ? 520 LEU   A CB  1 
ATOM   1729 C  CG  . LEU   A 1 224 ? -9.398  3.327   15.667 1.00 82.15  ? 520 LEU   A CG  1 
ATOM   1730 C  CD1 . LEU   A 1 224 ? -10.070 2.780   16.906 1.00 68.52  ? 520 LEU   A CD1 1 
ATOM   1731 C  CD2 . LEU   A 1 224 ? -8.012  2.721   15.478 1.00 84.75  ? 520 LEU   A CD2 1 
ATOM   1732 N  N   . PRO   A 1 225 ? -9.950  2.898   11.367 1.00 84.17  ? 521 PRO   A N   1 
ATOM   1733 C  CA  . PRO   A 1 225 ? -10.345 2.213   10.134 1.00 86.11  ? 521 PRO   A CA  1 
ATOM   1734 C  C   . PRO   A 1 225 ? -10.787 0.791   10.426 1.00 81.25  ? 521 PRO   A C   1 
ATOM   1735 O  O   . PRO   A 1 225 ? -10.310 0.137   11.355 1.00 79.87  ? 521 PRO   A O   1 
ATOM   1736 C  CB  . PRO   A 1 225 ? -9.052  2.230   9.308  1.00 87.45  ? 521 PRO   A CB  1 
ATOM   1737 C  CG  . PRO   A 1 225 ? -7.982  2.115   10.359 1.00 89.59  ? 521 PRO   A CG  1 
ATOM   1738 C  CD  . PRO   A 1 225 ? -8.486  2.892   11.549 1.00 89.25  ? 521 PRO   A CD  1 
ATOM   1739 N  N   . LEU   A 1 226 ? -11.736 0.320   9.624  1.00 74.95  ? 522 LEU   A N   1 
ATOM   1740 C  CA  . LEU   A 1 226 ? -12.145 -1.072  9.721  1.00 72.74  ? 522 LEU   A CA  1 
ATOM   1741 C  C   . LEU   A 1 226 ? -10.981 -1.982  9.355  1.00 74.90  ? 522 LEU   A C   1 
ATOM   1742 O  O   . LEU   A 1 226 ? -10.251 -1.727  8.397  1.00 82.56  ? 522 LEU   A O   1 
ATOM   1743 C  CB  . LEU   A 1 226 ? -13.332 -1.347  8.799  1.00 73.48  ? 522 LEU   A CB  1 
ATOM   1744 C  CG  . LEU   A 1 226 ? -14.664 -0.669  9.124  1.00 71.58  ? 522 LEU   A CG  1 
ATOM   1745 C  CD1 . LEU   A 1 226 ? -15.585 -0.730  7.898  1.00 69.98  ? 522 LEU   A CD1 1 
ATOM   1746 C  CD2 . LEU   A 1 226 ? -15.321 -1.310  10.352 1.00 62.94  ? 522 LEU   A CD2 1 
ATOM   1747 N  N   . LEU   A 1 227 ? -10.786 -3.035  10.148 1.00 74.29  ? 523 LEU   A N   1 
ATOM   1748 C  CA  . LEU   A 1 227 ? -9.871  -4.122  9.806  1.00 78.21  ? 523 LEU   A CA  1 
ATOM   1749 C  C   . LEU   A 1 227 ? -10.723 -5.362  9.598  1.00 74.62  ? 523 LEU   A C   1 
ATOM   1750 O  O   . LEU   A 1 227 ? -11.184 -5.964  10.565 1.00 65.01  ? 523 LEU   A O   1 
ATOM   1751 C  CB  . LEU   A 1 227 ? -8.834  -4.362  10.894 1.00 72.90  ? 523 LEU   A CB  1 
ATOM   1752 C  CG  . LEU   A 1 227 ? -7.337  -4.215  10.633 1.00 79.54  ? 523 LEU   A CG  1 
ATOM   1753 C  CD1 . LEU   A 1 227 ? -6.568  -4.864  11.794 1.00 77.54  ? 523 LEU   A CD1 1 
ATOM   1754 C  CD2 . LEU   A 1 227 ? -6.896  -4.780  9.299  1.00 80.13  ? 523 LEU   A CD2 1 
ATOM   1755 N  N   . LEU   A 1 228 ? -10.932 -5.746  8.346  1.00 68.59  ? 524 LEU   A N   1 
ATOM   1756 C  CA  . LEU   A 1 228 ? -11.907 -6.774  8.018  1.00 71.45  ? 524 LEU   A CA  1 
ATOM   1757 C  C   . LEU   A 1 228 ? -11.200 -8.001  7.466  1.00 73.89  ? 524 LEU   A C   1 
ATOM   1758 O  O   . LEU   A 1 228 ? -10.462 -7.912  6.480  1.00 81.29  ? 524 LEU   A O   1 
ATOM   1759 C  CB  . LEU   A 1 228 ? -12.938 -6.244  7.022  1.00 66.53  ? 524 LEU   A CB  1 
ATOM   1760 C  CG  . LEU   A 1 228 ? -13.550 -4.905  7.445  1.00 58.23  ? 524 LEU   A CG  1 
ATOM   1761 C  CD1 . LEU   A 1 228 ? -14.436 -4.374  6.333  1.00 58.97  ? 524 LEU   A CD1 1 
ATOM   1762 C  CD2 . LEU   A 1 228 ? -14.318 -4.980  8.777  1.00 52.20  ? 524 LEU   A CD2 1 
ATOM   1763 N  N   . GLN   A 1 229 ? -11.424 -9.134  8.118  1.00 77.69  ? 525 GLN   A N   1 
ATOM   1764 C  CA  . GLN   A 1 229 ? -10.925 -10.431 7.689  1.00 73.29  ? 525 GLN   A CA  1 
ATOM   1765 C  C   . GLN   A 1 229 ? -12.068 -11.205 7.044  1.00 67.37  ? 525 GLN   A C   1 
ATOM   1766 O  O   . GLN   A 1 229 ? -13.139 -11.353 7.642  1.00 70.91  ? 525 GLN   A O   1 
ATOM   1767 C  CB  . GLN   A 1 229 ? -10.346 -11.186 8.890  1.00 58.82  ? 525 GLN   A CB  1 
ATOM   1768 C  CG  . GLN   A 1 229 ? -10.402 -12.707 8.824  1.00 65.28  ? 525 GLN   A CG  1 
ATOM   1769 C  CD  . GLN   A 1 229 ? -9.883  -13.362 10.089 1.00 78.12  ? 525 GLN   A CD  1 
ATOM   1770 O  OE1 . GLN   A 1 229 ? -9.501  -12.679 11.042 1.00 81.83  ? 525 GLN   A OE1 1 
ATOM   1771 N  NE2 . GLN   A 1 229 ? -9.880  -14.690 10.111 1.00 81.07  ? 525 GLN   A NE2 1 
ATOM   1772 N  N   . ALA   A 1 230 ? -11.856 -11.669 5.819  1.00 61.78  ? 526 ALA   A N   1 
ATOM   1773 C  CA  . ALA   A 1 230 ? -12.874 -12.418 5.098  1.00 63.47  ? 526 ALA   A CA  1 
ATOM   1774 C  C   . ALA   A 1 230 ? -12.352 -13.808 4.768  1.00 67.67  ? 526 ALA   A C   1 
ATOM   1775 O  O   . ALA   A 1 230 ? -11.218 -13.959 4.302  1.00 73.90  ? 526 ALA   A O   1 
ATOM   1776 C  CB  . ALA   A 1 230 ? -13.292 -11.699 3.814  1.00 69.86  ? 526 ALA   A CB  1 
ATOM   1777 N  N   . ASN   A 1 231 ? -13.196 -14.812 5.016  1.00 70.28  ? 527 ASN   A N   1 
ATOM   1778 C  CA  . ASN   A 1 231 ? -12.900 -16.215 4.717  1.00 75.89  ? 527 ASN   A CA  1 
ATOM   1779 C  C   . ASN   A 1 231 ? -11.545 -16.626 5.282  1.00 79.53  ? 527 ASN   A C   1 
ATOM   1780 O  O   . ASN   A 1 231 ? -10.761 -17.326 4.636  1.00 83.19  ? 527 ASN   A O   1 
ATOM   1781 C  CB  . ASN   A 1 231 ? -12.975 -16.490 3.213  1.00 80.03  ? 527 ASN   A CB  1 
ATOM   1782 C  CG  . ASN   A 1 231 ? -13.188 -17.962 2.898  1.00 81.32  ? 527 ASN   A CG  1 
ATOM   1783 O  OD1 . ASN   A 1 231 ? -13.849 -18.679 3.652  1.00 79.65  ? 527 ASN   A OD1 1 
ATOM   1784 N  ND2 . ASN   A 1 231 ? -12.621 -18.422 1.785  1.00 83.64  ? 527 ASN   A ND2 1 
ATOM   1785 N  N   . GLY   A 1 232 ? -11.264 -16.177 6.504  1.00 85.08  ? 528 GLY   A N   1 
ATOM   1786 C  CA  . GLY   A 1 232 ? -10.021 -16.497 7.171  1.00 89.50  ? 528 GLY   A CA  1 
ATOM   1787 C  C   . GLY   A 1 232 ? -8.787  -15.802 6.639  1.00 95.12  ? 528 GLY   A C   1 
ATOM   1788 O  O   . GLY   A 1 232 ? -7.697  -16.030 7.175  1.00 100.91 ? 528 GLY   A O   1 
ATOM   1789 N  N   . ASN   A 1 233 ? -8.910  -14.966 5.608  1.00 95.35  ? 529 ASN   A N   1 
ATOM   1790 C  CA  . ASN   A 1 233 ? -7.749  -14.293 5.043  1.00 94.90  ? 529 ASN   A CA  1 
ATOM   1791 C  C   . ASN   A 1 233 ? -7.241  -13.193 5.970  1.00 95.29  ? 529 ASN   A C   1 
ATOM   1792 O  O   . ASN   A 1 233 ? -7.956  -12.697 6.842  1.00 97.21  ? 529 ASN   A O   1 
ATOM   1793 C  CB  . ASN   A 1 233 ? -8.083  -13.692 3.681  1.00 91.83  ? 529 ASN   A CB  1 
ATOM   1794 C  CG  . ASN   A 1 233 ? -7.998  -14.704 2.561  1.00 88.53  ? 529 ASN   A CG  1 
ATOM   1795 O  OD1 . ASN   A 1 233 ? -6.977  -14.807 1.882  1.00 95.49  ? 529 ASN   A OD1 1 
ATOM   1796 N  ND2 . ASN   A 1 233 ? -9.068  -15.467 2.370  1.00 79.11  ? 529 ASN   A ND2 1 
ATOM   1797 N  N   . ASP   A 1 234 ? -5.989  -12.802 5.757  1.00 100.02 ? 530 ASP   A N   1 
ATOM   1798 C  CA  . ASP   A 1 234 ? -5.415  -11.716 6.536  1.00 103.14 ? 530 ASP   A CA  1 
ATOM   1799 C  C   . ASP   A 1 234 ? -6.244  -10.447 6.339  1.00 96.95  ? 530 ASP   A C   1 
ATOM   1800 O  O   . ASP   A 1 234 ? -6.624  -10.124 5.206  1.00 102.07 ? 530 ASP   A O   1 
ATOM   1801 C  CB  . ASP   A 1 234 ? -3.956  -11.477 6.134  1.00 112.80 ? 530 ASP   A CB  1 
ATOM   1802 C  CG  . ASP   A 1 234 ? -3.086  -12.719 6.300  1.00 119.71 ? 530 ASP   A CG  1 
ATOM   1803 O  OD1 . ASP   A 1 234 ? -2.199  -12.942 5.454  1.00 125.64 ? 530 ASP   A OD1 1 
ATOM   1804 O  OD2 . ASP   A 1 234 ? -3.292  -13.482 7.269  1.00 121.97 ? 530 ASP   A OD2 1 
ATOM   1805 N  N   . PRO   A 1 235 ? -6.552  -9.717  7.405  1.00 85.76  ? 531 PRO   A N   1 
ATOM   1806 C  CA  . PRO   A 1 235 ? -7.494  -8.600  7.295  1.00 80.24  ? 531 PRO   A CA  1 
ATOM   1807 C  C   . PRO   A 1 235 ? -6.873  -7.393  6.609  1.00 77.26  ? 531 PRO   A C   1 
ATOM   1808 O  O   . PRO   A 1 235 ? -5.652  -7.224  6.568  1.00 85.40  ? 531 PRO   A O   1 
ATOM   1809 C  CB  . PRO   A 1 235 ? -7.823  -8.280  8.755  1.00 79.54  ? 531 PRO   A CB  1 
ATOM   1810 C  CG  . PRO   A 1 235 ? -6.569  -8.629  9.469  1.00 83.82  ? 531 PRO   A CG  1 
ATOM   1811 C  CD  . PRO   A 1 235 ? -6.022  -9.850  8.775  1.00 84.82  ? 531 PRO   A CD  1 
ATOM   1812 N  N   . GLU   A 1 236 ? -7.752  -6.534  6.090  1.00 82.35  ? 532 GLU   A N   1 
ATOM   1813 C  CA  . GLU   A 1 236 ? -7.365  -5.383  5.284  1.00 88.32  ? 532 GLU   A CA  1 
ATOM   1814 C  C   . GLU   A 1 236 ? -8.045  -4.134  5.825  1.00 85.77  ? 532 GLU   A C   1 
ATOM   1815 O  O   . GLU   A 1 236 ? -9.138  -4.199  6.389  1.00 80.71  ? 532 GLU   A O   1 
ATOM   1816 C  CB  . GLU   A 1 236 ? -7.748  -5.562  3.813  1.00 95.40  ? 532 GLU   A CB  1 
ATOM   1817 C  CG  . GLU   A 1 236 ? -7.671  -6.987  3.298  1.00 97.73  ? 532 GLU   A CG  1 
ATOM   1818 C  CD  . GLU   A 1 236 ? -8.414  -7.156  1.986  1.00 97.12  ? 532 GLU   A CD  1 
ATOM   1819 O  OE1 . GLU   A 1 236 ? -8.468  -6.184  1.205  1.00 98.18  ? 532 GLU   A OE1 1 
ATOM   1820 O  OE2 . GLU   A 1 236 ? -8.959  -8.252  1.745  1.00 94.64  ? 532 GLU   A OE2 1 
ATOM   1821 N  N   . LEU   A 1 237 ? -7.399  -2.990  5.636  1.00 89.67  ? 533 LEU   A N   1 
ATOM   1822 C  CA  . LEU   A 1 237 ? -7.877  -1.738  6.206  1.00 85.63  ? 533 LEU   A CA  1 
ATOM   1823 C  C   . LEU   A 1 237 ? -8.819  -1.025  5.247  1.00 88.57  ? 533 LEU   A C   1 
ATOM   1824 O  O   . LEU   A 1 237 ? -8.586  -0.999  4.038  1.00 90.60  ? 533 LEU   A O   1 
ATOM   1825 C  CB  . LEU   A 1 237 ? -6.702  -0.825  6.543  1.00 85.06  ? 533 LEU   A CB  1 
ATOM   1826 C  CG  . LEU   A 1 237 ? -5.841  -1.263  7.729  1.00 84.59  ? 533 LEU   A CG  1 
ATOM   1827 C  CD1 . LEU   A 1 237 ? -4.515  -0.518  7.708  1.00 88.92  ? 533 LEU   A CD1 1 
ATOM   1828 C  CD2 . LEU   A 1 237 ? -6.582  -1.049  9.049  1.00 75.09  ? 533 LEU   A CD2 1 
ATOM   1829 N  N   . PHE   A 1 238 ? -9.887  -0.449  5.795  1.00 90.27  ? 534 PHE   A N   1 
ATOM   1830 C  CA  . PHE   A 1 238 ? -10.802 0.374   5.018  1.00 92.16  ? 534 PHE   A CA  1 
ATOM   1831 C  C   . PHE   A 1 238 ? -11.295 1.518   5.888  1.00 92.60  ? 534 PHE   A C   1 
ATOM   1832 O  O   . PHE   A 1 238 ? -11.578 1.330   7.073  1.00 90.87  ? 534 PHE   A O   1 
ATOM   1833 C  CB  . PHE   A 1 238 ? -12.013 -0.418  4.491  1.00 81.94  ? 534 PHE   A CB  1 
ATOM   1834 C  CG  . PHE   A 1 238 ? -11.667 -1.727  3.846  1.00 79.04  ? 534 PHE   A CG  1 
ATOM   1835 C  CD1 . PHE   A 1 238 ? -11.432 -2.859  4.621  1.00 76.97  ? 534 PHE   A CD1 1 
ATOM   1836 C  CD2 . PHE   A 1 238 ? -11.609 -1.837  2.463  1.00 80.13  ? 534 PHE   A CD2 1 
ATOM   1837 C  CE1 . PHE   A 1 238 ? -11.125 -4.070  4.026  1.00 76.65  ? 534 PHE   A CE1 1 
ATOM   1838 C  CE2 . PHE   A 1 238 ? -11.307 -3.042  1.861  1.00 78.89  ? 534 PHE   A CE2 1 
ATOM   1839 C  CZ  . PHE   A 1 238 ? -11.062 -4.157  2.628  1.00 78.47  ? 534 PHE   A CZ  1 
ATOM   1840 N  N   . GLN   A 1 239 ? -11.409 2.699   5.284  1.00 98.63  ? 535 GLN   A N   1 
ATOM   1841 C  CA  . GLN   A 1 239 ? -11.836 3.910   5.976  1.00 95.24  ? 535 GLN   A CA  1 
ATOM   1842 C  C   . GLN   A 1 239 ? -13.311 4.172   5.702  1.00 88.97  ? 535 GLN   A C   1 
ATOM   1843 O  O   . GLN   A 1 239 ? -13.704 4.386   4.551  1.00 90.06  ? 535 GLN   A O   1 
ATOM   1844 C  CB  . GLN   A 1 239 ? -11.009 5.111   5.528  1.00 100.44 ? 535 GLN   A CB  1 
ATOM   1845 C  CG  . GLN   A 1 239 ? -11.508 6.411   6.125  1.00 109.00 ? 535 GLN   A CG  1 
ATOM   1846 C  CD  . GLN   A 1 239 ? -11.340 7.589   5.196  1.00 118.22 ? 535 GLN   A CD  1 
ATOM   1847 O  OE1 . GLN   A 1 239 ? -12.186 8.482   5.151  1.00 122.18 ? 535 GLN   A OE1 1 
ATOM   1848 N  NE2 . GLN   A 1 239 ? -10.244 7.602   4.449  1.00 122.33 ? 535 GLN   A NE2 1 
ATOM   1849 N  N   . ILE   A 1 240 ? -14.116 4.182   6.758  1.00 79.14  ? 536 ILE   A N   1 
ATOM   1850 C  CA  . ILE   A 1 240 ? -15.531 4.523   6.646  1.00 79.41  ? 536 ILE   A CA  1 
ATOM   1851 C  C   . ILE   A 1 240 ? -15.629 5.961   6.163  1.00 86.10  ? 536 ILE   A C   1 
ATOM   1852 O  O   . ILE   A 1 240 ? -15.077 6.864   6.810  1.00 86.41  ? 536 ILE   A O   1 
ATOM   1853 C  CB  . ILE   A 1 240 ? -16.271 4.352   7.982  1.00 78.12  ? 536 ILE   A CB  1 
ATOM   1854 C  CG1 . ILE   A 1 240 ? -16.033 2.955   8.553  1.00 80.69  ? 536 ILE   A CG1 1 
ATOM   1855 C  CG2 . ILE   A 1 240 ? -17.762 4.637   7.799  1.00 71.48  ? 536 ILE   A CG2 1 
ATOM   1856 C  CD1 . ILE   A 1 240 ? -15.104 2.928   9.763  1.00 85.73  ? 536 ILE   A CD1 1 
ATOM   1857 N  N   . PRO   A 1 241 ? -16.310 6.215   5.046  1.00 82.37  ? 537 PRO   A N   1 
ATOM   1858 C  CA  . PRO   A 1 241 ? -16.446 7.584   4.549  1.00 87.14  ? 537 PRO   A CA  1 
ATOM   1859 C  C   . PRO   A 1 241 ? -16.953 8.495   5.650  1.00 92.09  ? 537 PRO   A C   1 
ATOM   1860 O  O   . PRO   A 1 241 ? -17.974 8.208   6.296  1.00 89.71  ? 537 PRO   A O   1 
ATOM   1861 C  CB  . PRO   A 1 241 ? -17.459 7.451   3.398  1.00 88.50  ? 537 PRO   A CB  1 
ATOM   1862 C  CG  . PRO   A 1 241 ? -17.387 5.995   3.005  1.00 83.71  ? 537 PRO   A CG  1 
ATOM   1863 C  CD  . PRO   A 1 241 ? -17.137 5.265   4.287  1.00 86.00  ? 537 PRO   A CD  1 
ATOM   1864 N  N   . PRO   A 1 242 ? -16.218 9.562   5.951  1.00 95.71  ? 538 PRO   A N   1 
ATOM   1865 C  CA  . PRO   A 1 242 ? -16.529 10.343  7.155  1.00 91.78  ? 538 PRO   A CA  1 
ATOM   1866 C  C   . PRO   A 1 242 ? -17.931 10.919  7.156  1.00 95.21  ? 538 PRO   A C   1 
ATOM   1867 O  O   . PRO   A 1 242 ? -18.487 11.145  8.238  1.00 103.02 ? 538 PRO   A O   1 
ATOM   1868 C  CB  . PRO   A 1 242 ? -15.454 11.436  7.145  1.00 92.87  ? 538 PRO   A CB  1 
ATOM   1869 C  CG  . PRO   A 1 242 ? -14.318 10.816  6.369  1.00 96.24  ? 538 PRO   A CG  1 
ATOM   1870 C  CD  . PRO   A 1 242 ? -14.996 10.035  5.284  1.00 96.13  ? 538 PRO   A CD  1 
ATOM   1871 N  N   . GLU   A 1 243 ? -18.537 11.131  5.982  1.00 89.16  ? 539 GLU   A N   1 
ATOM   1872 C  CA  . GLU   A 1 243 ? -19.939 11.523  5.929  1.00 84.14  ? 539 GLU   A CA  1 
ATOM   1873 C  C   . GLU   A 1 243 ? -20.860 10.450  6.499  1.00 81.91  ? 539 GLU   A C   1 
ATOM   1874 O  O   . GLU   A 1 243 ? -22.026 10.744  6.794  1.00 81.00  ? 539 GLU   A O   1 
ATOM   1875 C  CB  . GLU   A 1 243 ? -20.343 11.862  4.485  1.00 96.60  ? 539 GLU   A CB  1 
ATOM   1876 C  CG  . GLU   A 1 243 ? -20.318 10.695  3.495  1.00 93.20  ? 539 GLU   A CG  1 
ATOM   1877 C  CD  . GLU   A 1 243 ? -19.039 10.634  2.665  1.00 96.90  ? 539 GLU   A CD  1 
ATOM   1878 O  OE1 . GLU   A 1 243 ? -17.955 10.840  3.247  1.00 97.49  ? 539 GLU   A OE1 1 
ATOM   1879 O  OE2 . GLU   A 1 243 ? -19.117 10.380  1.430  1.00 89.54  ? 539 GLU   A OE2 1 
ATOM   1880 N  N   . LEU   A 1 244 ? -20.371 9.219   6.668  1.00 75.41  ? 540 LEU   A N   1 
ATOM   1881 C  CA  . LEU   A 1 244 ? -21.172 8.156   7.252  1.00 75.96  ? 540 LEU   A CA  1 
ATOM   1882 C  C   . LEU   A 1 244 ? -21.020 8.053   8.759  1.00 72.72  ? 540 LEU   A C   1 
ATOM   1883 O  O   . LEU   A 1 244 ? -21.801 7.326   9.379  1.00 70.83  ? 540 LEU   A O   1 
ATOM   1884 C  CB  . LEU   A 1 244 ? -20.813 6.799   6.642  1.00 78.64  ? 540 LEU   A CB  1 
ATOM   1885 C  CG  . LEU   A 1 244 ? -21.188 6.588   5.182  1.00 82.84  ? 540 LEU   A CG  1 
ATOM   1886 C  CD1 . LEU   A 1 244 ? -21.050 5.116   4.835  1.00 72.48  ? 540 LEU   A CD1 1 
ATOM   1887 C  CD2 . LEU   A 1 244 ? -22.598 7.096   4.917  1.00 88.04  ? 540 LEU   A CD2 1 
ATOM   1888 N  N   . VAL   A 1 245 ? -20.052 8.754   9.353  1.00 75.45  ? 541 VAL   A N   1 
ATOM   1889 C  CA  . VAL   A 1 245 ? -19.789 8.678   10.790 1.00 81.86  ? 541 VAL   A CA  1 
ATOM   1890 C  C   . VAL   A 1 245 ? -20.373 9.942   11.408 1.00 79.82  ? 541 VAL   A C   1 
ATOM   1891 O  O   . VAL   A 1 245 ? -19.736 10.995  11.446 1.00 82.08  ? 541 VAL   A O   1 
ATOM   1892 C  CB  . VAL   A 1 245 ? -18.297 8.528   11.097 1.00 86.45  ? 541 VAL   A CB  1 
ATOM   1893 C  CG1 . VAL   A 1 245 ? -18.064 8.395   12.613 1.00 87.96  ? 541 VAL   A CG1 1 
ATOM   1894 C  CG2 . VAL   A 1 245 ? -17.740 7.338   10.364 1.00 82.99  ? 541 VAL   A CG2 1 
ATOM   1895 N  N   . LEU   A 1 246 ? -21.600 9.828   11.903 1.00 80.27  ? 542 LEU   A N   1 
ATOM   1896 C  CA  . LEU   A 1 246 ? -22.249 10.949  12.566 1.00 80.16  ? 542 LEU   A CA  1 
ATOM   1897 C  C   . LEU   A 1 246 ? -21.646 11.170  13.947 1.00 82.82  ? 542 LEU   A C   1 
ATOM   1898 O  O   . LEU   A 1 246 ? -21.393 10.226  14.698 1.00 77.72  ? 542 LEU   A O   1 
ATOM   1899 C  CB  . LEU   A 1 246 ? -23.751 10.704  12.676 1.00 83.72  ? 542 LEU   A CB  1 
ATOM   1900 C  CG  . LEU   A 1 246 ? -24.625 11.648  13.505 1.00 85.78  ? 542 LEU   A CG  1 
ATOM   1901 C  CD1 . LEU   A 1 246 ? -24.642 13.062  12.945 1.00 92.45  ? 542 LEU   A CD1 1 
ATOM   1902 C  CD2 . LEU   A 1 246 ? -26.033 11.076  13.595 1.00 84.91  ? 542 LEU   A CD2 1 
ATOM   1903 N  N   . GLU   A 1 247 ? -21.406 12.430  14.273 1.00 86.06  ? 543 GLU   A N   1 
ATOM   1904 C  CA  . GLU   A 1 247 ? -20.788 12.785  15.536 1.00 85.94  ? 543 GLU   A CA  1 
ATOM   1905 C  C   . GLU   A 1 247 ? -21.565 13.920  16.179 1.00 85.51  ? 543 GLU   A C   1 
ATOM   1906 O  O   . GLU   A 1 247 ? -22.081 14.807  15.484 1.00 90.55  ? 543 GLU   A O   1 
ATOM   1907 C  CB  . GLU   A 1 247 ? -19.318 13.172  15.336 1.00 89.61  ? 543 GLU   A CB  1 
ATOM   1908 C  CG  . GLU   A 1 247 ? -18.406 11.956  15.203 1.00 89.13  ? 543 GLU   A CG  1 
ATOM   1909 C  CD  . GLU   A 1 247 ? -17.007 12.333  14.771 1.00 100.16 ? 543 GLU   A CD  1 
ATOM   1910 O  OE1 . GLU   A 1 247 ? -16.873 13.059  13.762 1.00 106.14 ? 543 GLU   A OE1 1 
ATOM   1911 O  OE2 . GLU   A 1 247 ? -16.041 11.913  15.438 1.00 97.82  ? 543 GLU   A OE2 1 
ATOM   1912 N  N   . VAL   A 1 248 ? -21.645 13.870  17.504 1.00 83.92  ? 544 VAL   A N   1 
ATOM   1913 C  CA  . VAL   A 1 248 ? -22.362 14.834  18.332 1.00 85.47  ? 544 VAL   A CA  1 
ATOM   1914 C  C   . VAL   A 1 248 ? -21.330 15.654  19.099 1.00 92.20  ? 544 VAL   A C   1 
ATOM   1915 O  O   . VAL   A 1 248 ? -20.567 15.085  19.888 1.00 86.57  ? 544 VAL   A O   1 
ATOM   1916 C  CB  . VAL   A 1 248 ? -23.330 14.137  19.302 1.00 85.02  ? 544 VAL   A CB  1 
ATOM   1917 C  CG1 . VAL   A 1 248 ? -24.061 15.181  20.175 1.00 96.84  ? 544 VAL   A CG1 1 
ATOM   1918 C  CG2 . VAL   A 1 248 ? -24.302 13.230  18.551 1.00 78.27  ? 544 VAL   A CG2 1 
ATOM   1919 N  N   . PRO   A 1 249 ? -21.249 16.969  18.889 1.00 100.70 ? 545 PRO   A N   1 
ATOM   1920 C  CA  . PRO   A 1 249 ? -20.421 17.800  19.775 1.00 107.08 ? 545 PRO   A CA  1 
ATOM   1921 C  C   . PRO   A 1 249 ? -21.098 17.960  21.127 1.00 101.81 ? 545 PRO   A C   1 
ATOM   1922 O  O   . PRO   A 1 249 ? -22.290 18.261  21.208 1.00 99.67  ? 545 PRO   A O   1 
ATOM   1923 C  CB  . PRO   A 1 249 ? -20.316 19.135  19.023 1.00 112.78 ? 545 PRO   A CB  1 
ATOM   1924 C  CG  . PRO   A 1 249 ? -21.485 19.148  18.090 1.00 106.23 ? 545 PRO   A CG  1 
ATOM   1925 C  CD  . PRO   A 1 249 ? -21.750 17.721  17.722 1.00 101.87 ? 545 PRO   A CD  1 
ATOM   1926 N  N   . ILE   A 1 250 ? -20.334 17.743  22.194 1.00 105.37 ? 546 ILE   A N   1 
ATOM   1927 C  CA  . ILE   A 1 250 ? -20.879 17.730  23.546 1.00 100.01 ? 546 ILE   A CA  1 
ATOM   1928 C  C   . ILE   A 1 250 ? -20.797 19.144  24.108 1.00 108.80 ? 546 ILE   A C   1 
ATOM   1929 O  O   . ILE   A 1 250 ? -19.704 19.666  24.347 1.00 113.43 ? 546 ILE   A O   1 
ATOM   1930 C  CB  . ILE   A 1 250 ? -20.140 16.732  24.446 1.00 98.10  ? 546 ILE   A CB  1 
ATOM   1931 C  CG1 . ILE   A 1 250 ? -20.061 15.356  23.775 1.00 92.61  ? 546 ILE   A CG1 1 
ATOM   1932 C  CG2 . ILE   A 1 250 ? -20.830 16.617  25.808 1.00 92.94  ? 546 ILE   A CG2 1 
ATOM   1933 C  CD1 . ILE   A 1 250 ? -21.407 14.769  23.394 1.00 91.43  ? 546 ILE   A CD1 1 
ATOM   1934 N  N   . ARG   A 1 251 ? -21.954 19.763  24.328 1.00 111.70 ? 547 ARG   A N   1 
ATOM   1935 C  CA  . ARG   A 1 251 ? -22.029 21.056  24.988 1.00 116.09 ? 547 ARG   A CA  1 
ATOM   1936 C  C   . ARG   A 1 251 ? -22.978 20.963  26.174 1.00 114.60 ? 547 ARG   A C   1 
ATOM   1937 O  O   . ARG   A 1 251 ? -23.876 20.117  26.210 1.00 106.52 ? 547 ARG   A O   1 
ATOM   1938 C  CB  . ARG   A 1 251 ? -22.487 22.173  24.021 1.00 121.07 ? 547 ARG   A CB  1 
ATOM   1939 C  CG  . ARG   A 1 251 ? -23.911 22.042  23.487 1.00 120.37 ? 547 ARG   A CG  1 
ATOM   1940 C  CD  . ARG   A 1 251 ? -23.967 21.217  22.205 1.00 118.06 ? 547 ARG   A CD  1 
ATOM   1941 N  NE  . ARG   A 1 251 ? -25.282 21.276  21.576 1.00 113.96 ? 547 ARG   A NE  1 
ATOM   1942 C  CZ  . ARG   A 1 251 ? -25.643 20.541  20.536 1.00 114.88 ? 547 ARG   A CZ  1 
ATOM   1943 N  NH1 . ARG   A 1 251 ? -26.856 20.675  20.022 1.00 120.43 ? 547 ARG   A NH1 1 
ATOM   1944 N  NH2 . ARG   A 1 251 ? -24.787 19.681  19.997 1.00 105.41 ? 547 ARG   A NH2 1 
ATOM   1945 N  N   . HIS   A 1 252 ? -22.757 21.831  27.160 1.00 118.92 ? 548 HIS   A N   1 
ATOM   1946 C  CA  . HIS   A 1 252 ? -23.696 21.814  28.264 1.00 118.50 ? 548 HIS   A CA  1 
ATOM   1947 C  C   . HIS   A 1 252 ? -24.762 22.885  28.065 1.00 124.21 ? 548 HIS   A C   1 
ATOM   1948 O  O   . HIS   A 1 252 ? -24.518 23.898  27.402 1.00 123.15 ? 548 HIS   A O   1 
ATOM   1949 C  CB  . HIS   A 1 252 ? -22.982 22.057  29.595 1.00 113.89 ? 548 HIS   A CB  1 
ATOM   1950 C  CG  . HIS   A 1 252 ? -23.723 21.535  30.787 1.00 122.13 ? 548 HIS   A CG  1 
ATOM   1951 N  ND1 . HIS   A 1 252 ? -24.576 22.316  31.541 1.00 121.73 ? 548 HIS   A ND1 1 
ATOM   1952 C  CD2 . HIS   A 1 252 ? -23.733 20.308  31.360 1.00 113.43 ? 548 HIS   A CD2 1 
ATOM   1953 C  CE1 . HIS   A 1 252 ? -25.083 21.590  32.520 1.00 115.79 ? 548 HIS   A CE1 1 
ATOM   1954 N  NE2 . HIS   A 1 252 ? -24.586 20.369  32.434 1.00 111.42 ? 548 HIS   A NE2 1 
ATOM   1955 N  N   . PRO   A 1 253 ? -25.964 22.679  28.606 1.00 119.50 ? 549 PRO   A N   1 
ATOM   1956 C  CA  . PRO   A 1 253 ? -26.996 23.717  28.545 1.00 128.63 ? 549 PRO   A CA  1 
ATOM   1957 C  C   . PRO   A 1 253 ? -26.854 24.807  29.592 1.00 138.43 ? 549 PRO   A C   1 
ATOM   1958 O  O   . PRO   A 1 253 ? -27.773 25.616  29.732 1.00 144.26 ? 549 PRO   A O   1 
ATOM   1959 C  CB  . PRO   A 1 253 ? -28.293 22.921  28.755 1.00 118.98 ? 549 PRO   A CB  1 
ATOM   1960 C  CG  . PRO   A 1 253 ? -27.901 21.730  29.505 1.00 112.64 ? 549 PRO   A CG  1 
ATOM   1961 C  CD  . PRO   A 1 253 ? -26.506 21.391  29.072 1.00 110.78 ? 549 PRO   A CD  1 
ATOM   1962 N  N   . LYS   A 1 254 ? -25.735 24.848  30.314 1.00 140.21 ? 550 LYS   A N   1 
ATOM   1963 C  CA  . LYS   A 1 254 ? -25.489 25.890  31.300 1.00 145.94 ? 550 LYS   A CA  1 
ATOM   1964 C  C   . LYS   A 1 254 ? -24.071 26.434  31.184 1.00 146.82 ? 550 LYS   A C   1 
ATOM   1965 O  O   . LYS   A 1 254 ? -23.858 27.651  31.232 1.00 157.45 ? 550 LYS   A O   1 
ATOM   1966 C  CB  . LYS   A 1 254 ? -25.721 25.355  32.714 1.00 147.74 ? 550 LYS   A CB  1 
ATOM   1967 C  CG  . LYS   A 1 254 ? -27.152 24.934  33.019 1.00 150.70 ? 550 LYS   A CG  1 
ATOM   1968 C  CD  . LYS   A 1 254 ? -28.009 26.129  33.404 1.00 162.91 ? 550 LYS   A CD  1 
ATOM   1969 C  CE  . LYS   A 1 254 ? -29.362 25.698  33.954 1.00 162.13 ? 550 LYS   A CE  1 
ATOM   1970 N  NZ  . LYS   A 1 254 ? -30.293 25.250  32.878 1.00 157.57 ? 550 LYS   A NZ  1 
ATOM   1971 N  N   . PHE   A 1 255 ? -23.099 25.541  31.013 1.00 134.26 ? 551 PHE   A N   1 
ATOM   1972 C  CA  . PHE   A 1 255 ? -21.685 25.874  31.175 1.00 138.31 ? 551 PHE   A CA  1 
ATOM   1973 C  C   . PHE   A 1 255 ? -21.060 26.111  29.803 1.00 141.33 ? 551 PHE   A C   1 
ATOM   1974 O  O   . PHE   A 1 255 ? -20.574 25.188  29.151 1.00 132.26 ? 551 PHE   A O   1 
ATOM   1975 C  CB  . PHE   A 1 255 ? -20.975 24.764  31.941 1.00 138.64 ? 551 PHE   A CB  1 
ATOM   1976 C  CG  . PHE   A 1 255 ? -21.556 24.497  33.314 1.00 141.33 ? 551 PHE   A CG  1 
ATOM   1977 C  CD1 . PHE   A 1 255 ? -22.562 23.560  33.487 1.00 140.27 ? 551 PHE   A CD1 1 
ATOM   1978 C  CD2 . PHE   A 1 255 ? -21.088 25.173  34.430 1.00 143.89 ? 551 PHE   A CD2 1 
ATOM   1979 C  CE1 . PHE   A 1 255 ? -23.097 23.303  34.744 1.00 134.75 ? 551 PHE   A CE1 1 
ATOM   1980 C  CE2 . PHE   A 1 255 ? -21.620 24.918  35.695 1.00 140.33 ? 551 PHE   A CE2 1 
ATOM   1981 C  CZ  . PHE   A 1 255 ? -22.625 23.985  35.846 1.00 133.44 ? 551 PHE   A CZ  1 
ATOM   1982 N  N   . ASP   A 1 256 ? -21.044 27.373  29.374 1.00 150.98 ? 552 ASP   A N   1 
ATOM   1983 C  CA  . ASP   A 1 256 ? -20.478 27.711  28.074 1.00 159.80 ? 552 ASP   A CA  1 
ATOM   1984 C  C   . ASP   A 1 256 ? -18.969 27.504  27.997 1.00 157.22 ? 552 ASP   A C   1 
ATOM   1985 O  O   . ASP   A 1 256 ? -18.396 27.716  26.926 1.00 163.96 ? 552 ASP   A O   1 
ATOM   1986 C  CB  . ASP   A 1 256 ? -20.826 29.154  27.710 1.00 175.47 ? 552 ASP   A CB  1 
ATOM   1987 C  CG  . ASP   A 1 256 ? -22.203 29.274  27.100 1.00 180.45 ? 552 ASP   A CG  1 
ATOM   1988 O  OD1 . ASP   A 1 256 ? -23.162 29.555  27.851 1.00 181.36 ? 552 ASP   A OD1 1 
ATOM   1989 O  OD2 . ASP   A 1 256 ? -22.325 29.073  25.869 1.00 180.83 ? 552 ASP   A OD2 1 
ATOM   1990 N  N   . TRP   A 1 257 ? -18.306 27.115  29.086 1.00 145.88 ? 553 TRP   A N   1 
ATOM   1991 C  CA  . TRP   A 1 257 ? -16.936 26.641  28.958 1.00 146.06 ? 553 TRP   A CA  1 
ATOM   1992 C  C   . TRP   A 1 257 ? -16.877 25.184  28.540 1.00 140.42 ? 553 TRP   A C   1 
ATOM   1993 O  O   . TRP   A 1 257 ? -15.784 24.668  28.283 1.00 136.74 ? 553 TRP   A O   1 
ATOM   1994 C  CB  . TRP   A 1 257 ? -16.181 26.827  30.268 1.00 146.99 ? 553 TRP   A CB  1 
ATOM   1995 C  CG  . TRP   A 1 257 ? -16.936 26.301  31.438 1.00 143.02 ? 553 TRP   A CG  1 
ATOM   1996 C  CD1 . TRP   A 1 257 ? -17.757 27.009  32.265 1.00 149.28 ? 553 TRP   A CD1 1 
ATOM   1997 C  CD2 . TRP   A 1 257 ? -16.958 24.949  31.910 1.00 137.74 ? 553 TRP   A CD2 1 
ATOM   1998 N  NE1 . TRP   A 1 257 ? -18.281 26.183  33.233 1.00 143.64 ? 553 TRP   A NE1 1 
ATOM   1999 C  CE2 . TRP   A 1 257 ? -17.804 24.913  33.037 1.00 138.33 ? 553 TRP   A CE2 1 
ATOM   2000 C  CE3 . TRP   A 1 257 ? -16.340 23.766  31.495 1.00 133.39 ? 553 TRP   A CE3 1 
ATOM   2001 C  CZ2 . TRP   A 1 257 ? -18.054 23.742  33.744 1.00 131.59 ? 553 TRP   A CZ2 1 
ATOM   2002 C  CZ3 . TRP   A 1 257 ? -16.584 22.606  32.204 1.00 127.86 ? 553 TRP   A CZ3 1 
ATOM   2003 C  CH2 . TRP   A 1 257 ? -17.435 22.602  33.313 1.00 125.41 ? 553 TRP   A CH2 1 
ATOM   2004 N  N   . PHE   A 1 258 ? -18.029 24.516  28.473 1.00 140.42 ? 554 PHE   A N   1 
ATOM   2005 C  CA  . PHE   A 1 258 ? -18.053 23.118  28.068 1.00 140.21 ? 554 PHE   A CA  1 
ATOM   2006 C  C   . PHE   A 1 258 ? -17.534 22.944  26.652 1.00 135.31 ? 554 PHE   A C   1 
ATOM   2007 O  O   . PHE   A 1 258 ? -16.833 21.969  26.363 1.00 128.78 ? 554 PHE   A O   1 
ATOM   2008 C  CB  . PHE   A 1 258 ? -19.467 22.560  28.180 1.00 137.45 ? 554 PHE   A CB  1 
ATOM   2009 C  CG  . PHE   A 1 258 ? -19.523 21.236  28.832 1.00 126.42 ? 554 PHE   A CG  1 
ATOM   2010 C  CD1 . PHE   A 1 258 ? -19.610 21.143  30.208 1.00 129.74 ? 554 PHE   A CD1 1 
ATOM   2011 C  CD2 . PHE   A 1 258 ? -19.458 20.074  28.081 1.00 117.16 ? 554 PHE   A CD2 1 
ATOM   2012 C  CE1 . PHE   A 1 258 ? -19.648 19.920  30.831 1.00 121.07 ? 554 PHE   A CE1 1 
ATOM   2013 C  CE2 . PHE   A 1 258 ? -19.497 18.836  28.701 1.00 116.60 ? 554 PHE   A CE2 1 
ATOM   2014 C  CZ  . PHE   A 1 258 ? -19.592 18.763  30.080 1.00 115.96 ? 554 PHE   A CZ  1 
ATOM   2015 N  N   . LYS   A 1 259 ? -17.867 23.878  25.754 1.00 127.20 ? 555 LYS   A N   1 
ATOM   2016 C  CA  . LYS   A 1 259 ? -17.407 23.763  24.372 1.00 139.59 ? 555 LYS   A CA  1 
ATOM   2017 C  C   . LYS   A 1 259 ? -15.888 23.741  24.304 1.00 143.45 ? 555 LYS   A C   1 
ATOM   2018 O  O   . LYS   A 1 259 ? -15.304 23.012  23.492 1.00 128.80 ? 555 LYS   A O   1 
ATOM   2019 C  CB  . LYS   A 1 259 ? -17.957 24.911  23.517 1.00 138.37 ? 555 LYS   A CB  1 
ATOM   2020 C  CG  . LYS   A 1 259 ? -18.595 26.060  24.288 1.00 146.79 ? 555 LYS   A CG  1 
ATOM   2021 C  CD  . LYS   A 1 259 ? -18.729 27.316  23.428 1.00 161.01 ? 555 LYS   A CD  1 
ATOM   2022 C  CE  . LYS   A 1 259 ? -19.952 28.132  23.821 1.00 169.10 ? 555 LYS   A CE  1 
ATOM   2023 N  NZ  . LYS   A 1 259 ? -21.203 27.357  23.582 1.00 165.76 ? 555 LYS   A NZ  1 
ATOM   2024 N  N   . ASP   A 1 260 ? -15.231 24.521  25.169 1.00 150.89 ? 556 ASP   A N   1 
ATOM   2025 C  CA  . ASP   A 1 260 ? -13.775 24.586  25.162 1.00 157.88 ? 556 ASP   A CA  1 
ATOM   2026 C  C   . ASP   A 1 260 ? -13.159 23.255  25.560 1.00 147.43 ? 556 ASP   A C   1 
ATOM   2027 O  O   . ASP   A 1 260 ? -12.010 22.972  25.203 1.00 147.79 ? 556 ASP   A O   1 
ATOM   2028 C  CB  . ASP   A 1 260 ? -13.300 25.707  26.088 1.00 170.22 ? 556 ASP   A CB  1 
ATOM   2029 C  CG  . ASP   A 1 260 ? -13.753 27.080  25.620 1.00 183.13 ? 556 ASP   A CG  1 
ATOM   2030 O  OD1 . ASP   A 1 260 ? -13.448 27.449  24.466 1.00 188.22 ? 556 ASP   A OD1 1 
ATOM   2031 O  OD2 . ASP   A 1 260 ? -14.422 27.788  26.403 1.00 188.98 ? 556 ASP   A OD2 1 
ATOM   2032 N  N   . LEU   A 1 261 ? -13.906 22.426  26.297 1.00 139.24 ? 557 LEU   A N   1 
ATOM   2033 C  CA  . LEU   A 1 261 ? -13.462 21.059  26.550 1.00 132.02 ? 557 LEU   A CA  1 
ATOM   2034 C  C   . LEU   A 1 261 ? -13.204 20.329  25.239 1.00 135.09 ? 557 LEU   A C   1 
ATOM   2035 O  O   . LEU   A 1 261 ? -12.248 19.551  25.126 1.00 129.63 ? 557 LEU   A O   1 
ATOM   2036 C  CB  . LEU   A 1 261 ? -14.498 20.312  27.395 1.00 122.78 ? 557 LEU   A CB  1 
ATOM   2037 C  CG  . LEU   A 1 261 ? -14.655 20.722  28.866 1.00 123.93 ? 557 LEU   A CG  1 
ATOM   2038 C  CD1 . LEU   A 1 261 ? -15.829 20.005  29.541 1.00 115.06 ? 557 LEU   A CD1 1 
ATOM   2039 C  CD2 . LEU   A 1 261 ? -13.372 20.436  29.625 1.00 129.58 ? 557 LEU   A CD2 1 
ATOM   2040 N  N   . GLY   A 1 262 ? -14.028 20.589  24.229 1.00 139.19 ? 558 GLY   A N   1 
ATOM   2041 C  CA  . GLY   A 1 262 ? -13.796 20.045  22.908 1.00 144.70 ? 558 GLY   A CA  1 
ATOM   2042 C  C   . GLY   A 1 262 ? -14.052 18.558  22.829 1.00 138.09 ? 558 GLY   A C   1 
ATOM   2043 O  O   . GLY   A 1 262 ? -13.273 17.819  22.219 1.00 135.68 ? 558 GLY   A O   1 
ATOM   2044 N  N   . LEU   A 1 263 ? -15.137 18.109  23.448 1.00 131.01 ? 559 LEU   A N   1 
ATOM   2045 C  CA  . LEU   A 1 263 ? -15.508 16.705  23.423 1.00 114.32 ? 559 LEU   A CA  1 
ATOM   2046 C  C   . LEU   A 1 263 ? -16.583 16.450  22.375 1.00 106.18 ? 559 LEU   A C   1 
ATOM   2047 O  O   . LEU   A 1 263 ? -17.379 17.329  22.030 1.00 100.30 ? 559 LEU   A O   1 
ATOM   2048 C  CB  . LEU   A 1 263 ? -16.002 16.246  24.790 1.00 106.95 ? 559 LEU   A CB  1 
ATOM   2049 C  CG  . LEU   A 1 263 ? -14.998 16.446  25.923 1.00 107.41 ? 559 LEU   A CG  1 
ATOM   2050 C  CD1 . LEU   A 1 263 ? -15.661 16.109  27.228 1.00 105.11 ? 559 LEU   A CD1 1 
ATOM   2051 C  CD2 . LEU   A 1 263 ? -13.746 15.596  25.707 1.00 101.80 ? 559 LEU   A CD2 1 
ATOM   2052 N  N   . LYS   A 1 264 ? -16.578 15.226  21.862 1.00 100.85 ? 560 LYS   A N   1 
ATOM   2053 C  CA  . LYS   A 1 264 ? -17.596 14.751  20.947 1.00 102.59 ? 560 LYS   A CA  1 
ATOM   2054 C  C   . LYS   A 1 264 ? -17.602 13.239  21.024 1.00 97.88  ? 560 LYS   A C   1 
ATOM   2055 O  O   . LYS   A 1 264 ? -16.600 12.611  21.375 1.00 89.86  ? 560 LYS   A O   1 
ATOM   2056 C  CB  . LYS   A 1 264 ? -17.346 15.202  19.507 1.00 100.38 ? 560 LYS   A CB  1 
ATOM   2057 C  CG  . LYS   A 1 264 ? -16.017 14.733  18.939 1.00 106.78 ? 560 LYS   A CG  1 
ATOM   2058 C  CD  . LYS   A 1 264 ? -15.926 15.019  17.441 1.00 114.67 ? 560 LYS   A CD  1 
ATOM   2059 C  CE  . LYS   A 1 264 ? -14.487 14.959  16.951 1.00 114.10 ? 560 LYS   A CE  1 
ATOM   2060 N  NZ  . LYS   A 1 264 ? -14.350 15.230  15.505 1.00 104.41 ? 560 LYS   A NZ  1 
ATOM   2061 N  N   . TRP   A 1 265 ? -18.742 12.658  20.692 1.00 94.57  ? 561 TRP   A N   1 
ATOM   2062 C  CA  . TRP   A 1 265 ? -18.829 11.216  20.618 1.00 83.86  ? 561 TRP   A CA  1 
ATOM   2063 C  C   . TRP   A 1 265 ? -19.609 10.850  19.368 1.00 78.87  ? 561 TRP   A C   1 
ATOM   2064 O  O   . TRP   A 1 265 ? -20.378 11.660  18.842 1.00 83.39  ? 561 TRP   A O   1 
ATOM   2065 C  CB  . TRP   A 1 265 ? -19.488 10.615  21.854 1.00 70.73  ? 561 TRP   A CB  1 
ATOM   2066 C  CG  . TRP   A 1 265 ? -19.056 9.198   22.060 1.00 71.33  ? 561 TRP   A CG  1 
ATOM   2067 C  CD1 . TRP   A 1 265 ? -19.792 8.078   21.841 1.00 72.33  ? 561 TRP   A CD1 1 
ATOM   2068 C  CD2 . TRP   A 1 265 ? -17.771 8.754   22.515 1.00 81.41  ? 561 TRP   A CD2 1 
ATOM   2069 N  NE1 . TRP   A 1 265 ? -19.052 6.956   22.133 1.00 75.48  ? 561 TRP   A NE1 1 
ATOM   2070 C  CE2 . TRP   A 1 265 ? -17.806 7.347   22.552 1.00 80.12  ? 561 TRP   A CE2 1 
ATOM   2071 C  CE3 . TRP   A 1 265 ? -16.596 9.412   22.908 1.00 80.01  ? 561 TRP   A CE3 1 
ATOM   2072 C  CZ2 . TRP   A 1 265 ? -16.712 6.580   22.959 1.00 79.34  ? 561 TRP   A CZ2 1 
ATOM   2073 C  CZ3 . TRP   A 1 265 ? -15.508 8.646   23.297 1.00 76.48  ? 561 TRP   A CZ3 1 
ATOM   2074 C  CH2 . TRP   A 1 265 ? -15.579 7.243   23.330 1.00 70.00  ? 561 TRP   A CH2 1 
ATOM   2075 N  N   . TYR   A 1 266 ? -19.379 9.640   18.878 1.00 77.91  ? 562 TYR   A N   1 
ATOM   2076 C  CA  . TYR   A 1 266 ? -20.098 9.181   17.699 1.00 79.65  ? 562 TYR   A CA  1 
ATOM   2077 C  C   . TYR   A 1 266 ? -21.484 8.692   18.093 1.00 81.44  ? 562 TYR   A C   1 
ATOM   2078 O  O   . TYR   A 1 266 ? -21.704 8.206   19.208 1.00 74.46  ? 562 TYR   A O   1 
ATOM   2079 C  CB  . TYR   A 1 266 ? -19.332 8.064   16.989 1.00 75.98  ? 562 TYR   A CB  1 
ATOM   2080 C  CG  . TYR   A 1 266 ? -18.810 6.987   17.919 1.00 74.86  ? 562 TYR   A CG  1 
ATOM   2081 C  CD1 . TYR   A 1 266 ? -19.601 5.898   18.261 1.00 66.55  ? 562 TYR   A CD1 1 
ATOM   2082 C  CD2 . TYR   A 1 266 ? -17.523 7.054   18.446 1.00 65.62  ? 562 TYR   A CD2 1 
ATOM   2083 C  CE1 . TYR   A 1 266 ? -19.132 4.915   19.078 1.00 69.63  ? 562 TYR   A CE1 1 
ATOM   2084 C  CE2 . TYR   A 1 266 ? -17.050 6.068   19.277 1.00 71.98  ? 562 TYR   A CE2 1 
ATOM   2085 C  CZ  . TYR   A 1 266 ? -17.860 5.006   19.600 1.00 75.10  ? 562 TYR   A CZ  1 
ATOM   2086 O  OH  . TYR   A 1 266 ? -17.396 4.015   20.433 1.00 73.97  ? 562 TYR   A OH  1 
ATOM   2087 N  N   . GLY   A 1 267 ? -22.428 8.821   17.161 1.00 74.50  ? 563 GLY   A N   1 
ATOM   2088 C  CA  . GLY   A 1 267 ? -23.794 8.459   17.477 1.00 71.94  ? 563 GLY   A CA  1 
ATOM   2089 C  C   . GLY   A 1 267 ? -24.055 6.971   17.498 1.00 74.01  ? 563 GLY   A C   1 
ATOM   2090 O  O   . GLY   A 1 267 ? -24.952 6.524   18.220 1.00 67.16  ? 563 GLY   A O   1 
ATOM   2091 N  N   . LEU   A 1 268 ? -23.278 6.187   16.745 1.00 68.94  ? 564 LEU   A N   1 
ATOM   2092 C  CA  . LEU   A 1 268 ? -23.642 4.800   16.488 1.00 65.51  ? 564 LEU   A CA  1 
ATOM   2093 C  C   . LEU   A 1 268 ? -22.849 3.833   17.362 1.00 63.08  ? 564 LEU   A C   1 
ATOM   2094 O  O   . LEU   A 1 268 ? -21.658 3.597   17.091 1.00 56.95  ? 564 LEU   A O   1 
ATOM   2095 C  CB  . LEU   A 1 268 ? -23.427 4.475   15.004 1.00 63.50  ? 564 LEU   A CB  1 
ATOM   2096 C  CG  . LEU   A 1 268 ? -24.182 3.228   14.548 1.00 63.82  ? 564 LEU   A CG  1 
ATOM   2097 C  CD1 . LEU   A 1 268 ? -25.639 3.563   14.262 1.00 75.29  ? 564 LEU   A CD1 1 
ATOM   2098 C  CD2 . LEU   A 1 268 ? -23.521 2.615   13.347 1.00 65.76  ? 564 LEU   A CD2 1 
ATOM   2099 N  N   . PRO   A 1 269 ? -23.447 3.240   18.405 1.00 60.15  ? 565 PRO   A N   1 
ATOM   2100 C  CA  . PRO   A 1 269 ? -22.775 2.147   19.127 1.00 52.37  ? 565 PRO   A CA  1 
ATOM   2101 C  C   . PRO   A 1 269 ? -23.004 0.833   18.390 1.00 54.48  ? 565 PRO   A C   1 
ATOM   2102 O  O   . PRO   A 1 269 ? -24.143 0.378   18.241 1.00 56.90  ? 565 PRO   A O   1 
ATOM   2103 C  CB  . PRO   A 1 269 ? -23.463 2.154   20.498 1.00 56.54  ? 565 PRO   A CB  1 
ATOM   2104 C  CG  . PRO   A 1 269 ? -24.857 2.614   20.187 1.00 63.67  ? 565 PRO   A CG  1 
ATOM   2105 C  CD  . PRO   A 1 269 ? -24.777 3.532   18.973 1.00 64.43  ? 565 PRO   A CD  1 
ATOM   2106 N  N   . ALA   A 1 270 ? -21.921 0.214   17.926 1.00 51.69  ? 566 ALA   A N   1 
ATOM   2107 C  CA  . ALA   A 1 270 ? -22.041 -0.911  16.997 1.00 54.38  ? 566 ALA   A CA  1 
ATOM   2108 C  C   . ALA   A 1 270 ? -20.980 -1.929  17.384 1.00 53.52  ? 566 ALA   A C   1 
ATOM   2109 O  O   . ALA   A 1 270 ? -19.808 -1.768  17.041 1.00 65.15  ? 566 ALA   A O   1 
ATOM   2110 C  CB  . ALA   A 1 270 ? -21.892 -0.465  15.538 1.00 52.51  ? 566 ALA   A CB  1 
ATOM   2111 N  N   . VAL   A 1 271 ? -21.394 -2.974  18.090 1.00 50.62  ? 567 VAL   A N   1 
ATOM   2112 C  CA  . VAL   A 1 271 ? -20.461 -3.986  18.552 1.00 51.83  ? 567 VAL   A CA  1 
ATOM   2113 C  C   . VAL   A 1 271 ? -20.154 -4.935  17.414 1.00 49.43  ? 567 VAL   A C   1 
ATOM   2114 O  O   . VAL   A 1 271 ? -21.068 -5.495  16.801 1.00 55.19  ? 567 VAL   A O   1 
ATOM   2115 C  CB  . VAL   A 1 271 ? -21.035 -4.749  19.751 1.00 45.47  ? 567 VAL   A CB  1 
ATOM   2116 C  CG1 . VAL   A 1 271 ? -20.179 -5.975  20.024 1.00 48.77  ? 567 VAL   A CG1 1 
ATOM   2117 C  CG2 . VAL   A 1 271 ? -21.111 -3.832  20.952 1.00 47.22  ? 567 VAL   A CG2 1 
ATOM   2118 N  N   . SER   A 1 272 ? -18.867 -5.159  17.163 1.00 52.89  ? 568 SER   A N   1 
ATOM   2119 C  CA  . SER   A 1 272 ? -18.458 -5.933  16.003 1.00 53.16  ? 568 SER   A CA  1 
ATOM   2120 C  C   . SER   A 1 272 ? -17.568 -7.124  16.323 1.00 52.94  ? 568 SER   A C   1 
ATOM   2121 O  O   . SER   A 1 272 ? -17.123 -7.806  15.392 1.00 68.59  ? 568 SER   A O   1 
ATOM   2122 C  CB  . SER   A 1 272 ? -17.749 -5.022  14.991 1.00 63.28  ? 568 SER   A CB  1 
ATOM   2123 O  OG  . SER   A 1 272 ? -16.722 -4.254  15.590 1.00 64.68  ? 568 SER   A OG  1 
ATOM   2124 N  N   . ASN   A 1 273 ? -17.293 -7.400  17.600 1.00 54.85  ? 569 ASN   A N   1 
ATOM   2125 C  CA  . ASN   A 1 273 ? -16.342 -8.442  17.965 1.00 57.69  ? 569 ASN   A CA  1 
ATOM   2126 C  C   . ASN   A 1 273 ? -17.006 -9.672  18.569 1.00 61.78  ? 569 ASN   A C   1 
ATOM   2127 O  O   . ASN   A 1 273 ? -16.302 -10.581 19.011 1.00 62.02  ? 569 ASN   A O   1 
ATOM   2128 C  CB  . ASN   A 1 273 ? -15.296 -7.890  18.936 1.00 60.58  ? 569 ASN   A CB  1 
ATOM   2129 C  CG  . ASN   A 1 273 ? -15.905 -7.377  20.221 1.00 65.60  ? 569 ASN   A CG  1 
ATOM   2130 O  OD1 . ASN   A 1 273 ? -17.129 -7.270  20.352 1.00 58.33  ? 569 ASN   A OD1 1 
ATOM   2131 N  ND2 . ASN   A 1 273 ? -15.043 -7.050  21.189 1.00 62.67  ? 569 ASN   A ND2 1 
ATOM   2132 N  N   . MET   A 1 274 ? -18.330 -9.736  18.590 1.00 53.41  ? 570 MET   A N   1 
ATOM   2133 C  CA  . MET   A 1 274 ? -19.007 -10.849 19.230 1.00 49.82  ? 570 MET   A CA  1 
ATOM   2134 C  C   . MET   A 1 274 ? -19.437 -11.890 18.209 1.00 53.13  ? 570 MET   A C   1 
ATOM   2135 O  O   . MET   A 1 274 ? -19.326 -11.705 17.000 1.00 57.47  ? 570 MET   A O   1 
ATOM   2136 C  CB  . MET   A 1 274 ? -20.197 -10.347 20.048 1.00 53.63  ? 570 MET   A CB  1 
ATOM   2137 C  CG  . MET   A 1 274 ? -19.730 -9.577  21.302 1.00 54.28  ? 570 MET   A CG  1 
ATOM   2138 S  SD  . MET   A 1 274 ? -21.084 -9.136  22.365 1.00 57.20  ? 570 MET   A SD  1 
ATOM   2139 C  CE  . MET   A 1 274 ? -21.401 -10.699 23.184 1.00 48.66  ? 570 MET   A CE  1 
ATOM   2140 N  N   . LEU   A 1 275 ? -19.938 -12.999 18.729 1.00 51.78  ? 571 LEU   A N   1 
ATOM   2141 C  CA  . LEU   A 1 275 ? -20.288 -14.176 17.958 1.00 51.64  ? 571 LEU   A CA  1 
ATOM   2142 C  C   . LEU   A 1 275 ? -21.770 -14.440 18.150 1.00 55.46  ? 571 LEU   A C   1 
ATOM   2143 O  O   . LEU   A 1 275 ? -22.248 -14.519 19.286 1.00 54.42  ? 571 LEU   A O   1 
ATOM   2144 C  CB  . LEU   A 1 275 ? -19.457 -15.384 18.397 1.00 57.08  ? 571 LEU   A CB  1 
ATOM   2145 C  CG  . LEU   A 1 275 ? -19.342 -16.566 17.437 1.00 62.98  ? 571 LEU   A CG  1 
ATOM   2146 C  CD1 . LEU   A 1 275 ? -18.021 -17.273 17.659 1.00 70.91  ? 571 LEU   A CD1 1 
ATOM   2147 C  CD2 . LEU   A 1 275 ? -20.501 -17.522 17.620 1.00 62.74  ? 571 LEU   A CD2 1 
ATOM   2148 N  N   . LEU   A 1 276 ? -22.488 -14.555 17.036 1.00 49.16  ? 572 LEU   A N   1 
ATOM   2149 C  CA  . LEU   A 1 276 ? -23.908 -14.877 17.016 1.00 56.01  ? 572 LEU   A CA  1 
ATOM   2150 C  C   . LEU   A 1 276 ? -24.064 -16.386 16.849 1.00 58.21  ? 572 LEU   A C   1 
ATOM   2151 O  O   . LEU   A 1 276 ? -23.539 -16.965 15.891 1.00 63.64  ? 572 LEU   A O   1 
ATOM   2152 C  CB  . LEU   A 1 276 ? -24.603 -14.127 15.871 1.00 52.95  ? 572 LEU   A CB  1 
ATOM   2153 C  CG  . LEU   A 1 276 ? -26.048 -14.471 15.527 1.00 56.29  ? 572 LEU   A CG  1 
ATOM   2154 C  CD1 . LEU   A 1 276 ? -26.903 -14.439 16.763 1.00 50.19  ? 572 LEU   A CD1 1 
ATOM   2155 C  CD2 . LEU   A 1 276 ? -26.578 -13.480 14.528 1.00 58.44  ? 572 LEU   A CD2 1 
ATOM   2156 N  N   . GLU   A 1 277 ? -24.771 -17.021 17.781 1.00 58.93  ? 573 GLU   A N   1 
ATOM   2157 C  CA  . GLU   A 1 277 ? -25.079 -18.442 17.706 1.00 66.45  ? 573 GLU   A CA  1 
ATOM   2158 C  C   . GLU   A 1 277 ? -26.562 -18.635 17.442 1.00 65.18  ? 573 GLU   A C   1 
ATOM   2159 O  O   . GLU   A 1 277 ? -27.403 -18.119 18.184 1.00 55.89  ? 573 GLU   A O   1 
ATOM   2160 C  CB  . GLU   A 1 277 ? -24.690 -19.173 18.987 1.00 73.67  ? 573 GLU   A CB  1 
ATOM   2161 C  CG  . GLU   A 1 277 ? -23.326 -19.811 18.951 1.00 82.26  ? 573 GLU   A CG  1 
ATOM   2162 C  CD  . GLU   A 1 277 ? -23.244 -21.027 19.851 1.00 91.04  ? 573 GLU   A CD  1 
ATOM   2163 O  OE1 . GLU   A 1 277 ? -24.243 -21.780 19.919 1.00 90.11  ? 573 GLU   A OE1 1 
ATOM   2164 O  OE2 . GLU   A 1 277 ? -22.188 -21.222 20.490 1.00 95.66  ? 573 GLU   A OE2 1 
ATOM   2165 N  N   . ILE   A 1 278 ? -26.872 -19.387 16.392 1.00 64.72  ? 574 ILE   A N   1 
ATOM   2166 C  CA  . ILE   A 1 278 ? -28.241 -19.677 15.981 1.00 63.30  ? 574 ILE   A CA  1 
ATOM   2167 C  C   . ILE   A 1 278 ? -28.285 -21.137 15.571 1.00 66.33  ? 574 ILE   A C   1 
ATOM   2168 O  O   . ILE   A 1 278 ? -27.547 -21.546 14.668 1.00 69.20  ? 574 ILE   A O   1 
ATOM   2169 C  CB  . ILE   A 1 278 ? -28.709 -18.797 14.811 1.00 62.68  ? 574 ILE   A CB  1 
ATOM   2170 C  CG1 . ILE   A 1 278 ? -28.748 -17.330 15.225 1.00 65.95  ? 574 ILE   A CG1 1 
ATOM   2171 C  CG2 . ILE   A 1 278 ? -30.077 -19.241 14.347 1.00 64.94  ? 574 ILE   A CG2 1 
ATOM   2172 C  CD1 . ILE   A 1 278 ? -28.955 -16.388 14.079 1.00 62.97  ? 574 ILE   A CD1 1 
ATOM   2173 N  N   . GLY   A 1 279 ? -29.125 -21.924 16.236 1.00 71.49  ? 575 GLY   A N   1 
ATOM   2174 C  CA  . GLY   A 1 279 ? -29.255 -23.328 15.870 1.00 74.40  ? 575 GLY   A CA  1 
ATOM   2175 C  C   . GLY   A 1 279 ? -27.935 -24.062 15.789 1.00 72.65  ? 575 GLY   A C   1 
ATOM   2176 O  O   . GLY   A 1 279 ? -27.766 -24.945 14.939 1.00 74.86  ? 575 GLY   A O   1 
ATOM   2177 N  N   . GLY   A 1 280 ? -26.985 -23.709 16.651 1.00 71.92  ? 576 GLY   A N   1 
ATOM   2178 C  CA  . GLY   A 1 280 ? -25.685 -24.340 16.640 1.00 77.32  ? 576 GLY   A CA  1 
ATOM   2179 C  C   . GLY   A 1 280 ? -24.730 -23.814 15.595 1.00 71.01  ? 576 GLY   A C   1 
ATOM   2180 O  O   . GLY   A 1 280 ? -23.573 -24.254 15.562 1.00 71.05  ? 576 GLY   A O   1 
ATOM   2181 N  N   . LEU   A 1 281 ? -25.178 -22.903 14.736 1.00 65.84  ? 577 LEU   A N   1 
ATOM   2182 C  CA  . LEU   A 1 281 ? -24.324 -22.261 13.749 1.00 66.27  ? 577 LEU   A CA  1 
ATOM   2183 C  C   . LEU   A 1 281 ? -23.689 -21.022 14.359 1.00 64.38  ? 577 LEU   A C   1 
ATOM   2184 O  O   . LEU   A 1 281 ? -24.339 -20.285 15.100 1.00 64.65  ? 577 LEU   A O   1 
ATOM   2185 C  CB  . LEU   A 1 281 ? -25.124 -21.861 12.508 1.00 71.36  ? 577 LEU   A CB  1 
ATOM   2186 C  CG  . LEU   A 1 281 ? -25.786 -22.962 11.689 1.00 66.36  ? 577 LEU   A CG  1 
ATOM   2187 C  CD1 . LEU   A 1 281 ? -26.496 -22.364 10.470 1.00 67.46  ? 577 LEU   A CD1 1 
ATOM   2188 C  CD2 . LEU   A 1 281 ? -24.751 -23.997 11.297 1.00 64.28  ? 577 LEU   A CD2 1 
ATOM   2189 N  N   . GLU   A 1 282 ? -22.425 -20.782 14.018 1.00 64.46  ? 578 GLU   A N   1 
ATOM   2190 C  CA  . GLU   A 1 282 ? -21.632 -19.730 14.637 1.00 65.46  ? 578 GLU   A CA  1 
ATOM   2191 C  C   . GLU   A 1 282 ? -21.302 -18.670 13.597 1.00 62.35  ? 578 GLU   A C   1 
ATOM   2192 O  O   . GLU   A 1 282 ? -20.622 -18.958 12.607 1.00 59.56  ? 578 GLU   A O   1 
ATOM   2193 C  CB  . GLU   A 1 282 ? -20.358 -20.305 15.257 1.00 65.28  ? 578 GLU   A CB  1 
ATOM   2194 C  CG  . GLU   A 1 282 ? -20.629 -21.262 16.408 1.00 77.60  ? 578 GLU   A CG  1 
ATOM   2195 C  CD  . GLU   A 1 282 ? -19.358 -21.816 17.003 1.00 89.02  ? 578 GLU   A CD  1 
ATOM   2196 O  OE1 . GLU   A 1 282 ? -18.359 -21.902 16.258 1.00 89.93  ? 578 GLU   A OE1 1 
ATOM   2197 O  OE2 . GLU   A 1 282 ? -19.355 -22.155 18.209 1.00 98.28  ? 578 GLU   A OE2 1 
ATOM   2198 N  N   . PHE   A 1 283 ? -21.770 -17.448 13.833 1.00 52.79  ? 579 PHE   A N   1 
ATOM   2199 C  CA  . PHE   A 1 283 ? -21.509 -16.321 12.947 1.00 53.11  ? 579 PHE   A CA  1 
ATOM   2200 C  C   . PHE   A 1 283 ? -20.466 -15.427 13.614 1.00 52.34  ? 579 PHE   A C   1 
ATOM   2201 O  O   . PHE   A 1 283 ? -20.796 -14.587 14.449 1.00 60.90  ? 579 PHE   A O   1 
ATOM   2202 C  CB  . PHE   A 1 283 ? -22.803 -15.576 12.626 1.00 54.43  ? 579 PHE   A CB  1 
ATOM   2203 C  CG  . PHE   A 1 283 ? -23.820 -16.419 11.893 1.00 51.65  ? 579 PHE   A CG  1 
ATOM   2204 C  CD1 . PHE   A 1 283 ? -24.791 -17.129 12.587 1.00 51.70  ? 579 PHE   A CD1 1 
ATOM   2205 C  CD2 . PHE   A 1 283 ? -23.766 -16.550 10.506 1.00 54.63  ? 579 PHE   A CD2 1 
ATOM   2206 C  CE1 . PHE   A 1 283 ? -25.716 -17.920 11.921 1.00 55.94  ? 579 PHE   A CE1 1 
ATOM   2207 C  CE2 . PHE   A 1 283 ? -24.697 -17.323 9.832  1.00 60.28  ? 579 PHE   A CE2 1 
ATOM   2208 C  CZ  . PHE   A 1 283 ? -25.667 -18.015 10.540 1.00 59.12  ? 579 PHE   A CZ  1 
ATOM   2209 N  N   . SER   A 1 284 ? -19.197 -15.607 13.222 1.00 54.28  ? 580 SER   A N   1 
ATOM   2210 C  CA  . SER   A 1 284 ? -18.073 -14.935 13.872 1.00 55.05  ? 580 SER   A CA  1 
ATOM   2211 C  C   . SER   A 1 284 ? -18.008 -13.444 13.565 1.00 57.41  ? 580 SER   A C   1 
ATOM   2212 O  O   . SER   A 1 284 ? -17.292 -12.710 14.250 1.00 53.85  ? 580 SER   A O   1 
ATOM   2213 C  CB  . SER   A 1 284 ? -16.769 -15.604 13.444 1.00 56.01  ? 580 SER   A CB  1 
ATOM   2214 O  OG  . SER   A 1 284 ? -16.739 -15.815 12.041 1.00 61.16  ? 580 SER   A OG  1 
ATOM   2215 N  N   . ALA   A 1 285 ? -18.705 -12.978 12.536 1.00 61.05  ? 581 ALA   A N   1 
ATOM   2216 C  CA  . ALA   A 1 285 ? -18.759 -11.555 12.235 1.00 53.79  ? 581 ALA   A CA  1 
ATOM   2217 C  C   . ALA   A 1 285 ? -20.221 -11.189 12.075 1.00 57.48  ? 581 ALA   A C   1 
ATOM   2218 O  O   . ALA   A 1 285 ? -20.873 -11.617 11.112 1.00 54.52  ? 581 ALA   A O   1 
ATOM   2219 C  CB  . ALA   A 1 285 ? -17.958 -11.209 10.982 1.00 53.96  ? 581 ALA   A CB  1 
ATOM   2220 N  N   . CYS   A 1 286 ? -20.723 -10.392 13.006 1.00 53.50  ? 582 CYS   A N   1 
ATOM   2221 C  CA  . CYS   A 1 286 ? -22.139 -10.066 13.065 1.00 50.05  ? 582 CYS   A CA  1 
ATOM   2222 C  C   . CYS   A 1 286 ? -22.325 -8.689  13.682 1.00 50.60  ? 582 CYS   A C   1 
ATOM   2223 O  O   . CYS   A 1 286 ? -23.101 -8.553  14.636 1.00 54.60  ? 582 CYS   A O   1 
ATOM   2224 C  CB  . CYS   A 1 286 ? -22.895 -11.110 13.887 1.00 51.56  ? 582 CYS   A CB  1 
ATOM   2225 S  SG  . CYS   A 1 286 ? -22.169 -11.374 15.505 1.00 53.28  ? 582 CYS   A SG  1 
ATOM   2226 N  N   . PRO   A 1 287 ? -21.680 -7.651  13.142 1.00 51.59  ? 583 PRO   A N   1 
ATOM   2227 C  CA  . PRO   A 1 287 ? -21.765 -6.324  13.765 1.00 49.20  ? 583 PRO   A CA  1 
ATOM   2228 C  C   . PRO   A 1 287 ? -23.213 -5.913  13.994 1.00 52.92  ? 583 PRO   A C   1 
ATOM   2229 O  O   . PRO   A 1 287 ? -24.054 -6.044  13.112 1.00 49.46  ? 583 PRO   A O   1 
ATOM   2230 C  CB  . PRO   A 1 287 ? -21.078 -5.416  12.743 1.00 49.52  ? 583 PRO   A CB  1 
ATOM   2231 C  CG  . PRO   A 1 287 ? -21.264 -6.115  11.415 1.00 54.88  ? 583 PRO   A CG  1 
ATOM   2232 C  CD  . PRO   A 1 287 ? -21.172 -7.583  11.753 1.00 55.36  ? 583 PRO   A CD  1 
ATOM   2233 N  N   . PHE   A 1 288 ? -23.506 -5.388  15.181 1.00 46.60  ? 584 PHE   A N   1 
ATOM   2234 C  CA  . PHE   A 1 288 ? -24.872 -5.002  15.520 1.00 43.38  ? 584 PHE   A CA  1 
ATOM   2235 C  C   . PHE   A 1 288 ? -24.879 -3.662  16.243 1.00 52.12  ? 584 PHE   A C   1 
ATOM   2236 O  O   . PHE   A 1 288 ? -23.975 -3.352  17.017 1.00 45.33  ? 584 PHE   A O   1 
ATOM   2237 C  CB  . PHE   A 1 288 ? -25.576 -6.084  16.368 1.00 48.25  ? 584 PHE   A CB  1 
ATOM   2238 C  CG  . PHE   A 1 288 ? -24.874 -6.415  17.666 1.00 51.34  ? 584 PHE   A CG  1 
ATOM   2239 C  CD1 . PHE   A 1 288 ? -25.042 -5.608  18.789 1.00 52.44  ? 584 PHE   A CD1 1 
ATOM   2240 C  CD2 . PHE   A 1 288 ? -24.096 -7.561  17.779 1.00 54.55  ? 584 PHE   A CD2 1 
ATOM   2241 C  CE1 . PHE   A 1 288 ? -24.420 -5.916  19.969 1.00 44.19  ? 584 PHE   A CE1 1 
ATOM   2242 C  CE2 . PHE   A 1 288 ? -23.475 -7.875  18.985 1.00 45.24  ? 584 PHE   A CE2 1 
ATOM   2243 C  CZ  . PHE   A 1 288 ? -23.647 -7.049  20.064 1.00 46.86  ? 584 PHE   A CZ  1 
ATOM   2244 N  N   . SER   A 1 289 ? -25.903 -2.855  15.975 1.00 51.87  ? 585 SER   A N   1 
ATOM   2245 C  CA  . SER   A 1 289 ? -25.916 -1.493  16.483 1.00 53.06  ? 585 SER   A CA  1 
ATOM   2246 C  C   . SER   A 1 289 ? -27.297 -1.133  17.006 1.00 52.64  ? 585 SER   A C   1 
ATOM   2247 O  O   . SER   A 1 289 ? -28.313 -1.646  16.537 1.00 52.92  ? 585 SER   A O   1 
ATOM   2248 C  CB  . SER   A 1 289 ? -25.477 -0.477  15.415 1.00 54.14  ? 585 SER   A CB  1 
ATOM   2249 O  OG  . SER   A 1 289 ? -26.281 -0.550  14.242 1.00 53.88  ? 585 SER   A OG  1 
ATOM   2250 N  N   . GLY   A 1 290 ? -27.315 -0.247  18.003 1.00 54.88  ? 586 GLY   A N   1 
ATOM   2251 C  CA  . GLY   A 1 290 ? -28.543 0.375   18.443 1.00 52.10  ? 586 GLY   A CA  1 
ATOM   2252 C  C   . GLY   A 1 290 ? -28.333 1.864   18.611 1.00 61.43  ? 586 GLY   A C   1 
ATOM   2253 O  O   . GLY   A 1 290 ? -27.825 2.537   17.709 1.00 66.23  ? 586 GLY   A O   1 
ATOM   2254 N  N   . TRP   A 1 291 ? -28.732 2.397   19.759 1.00 57.73  ? 587 TRP   A N   1 
ATOM   2255 C  CA  . TRP   A 1 291 ? -28.427 3.773   20.117 1.00 58.35  ? 587 TRP   A CA  1 
ATOM   2256 C  C   . TRP   A 1 291 ? -27.877 3.787   21.529 1.00 62.38  ? 587 TRP   A C   1 
ATOM   2257 O  O   . TRP   A 1 291 ? -28.059 2.837   22.295 1.00 55.34  ? 587 TRP   A O   1 
ATOM   2258 C  CB  . TRP   A 1 291 ? -29.643 4.697   20.000 1.00 66.18  ? 587 TRP   A CB  1 
ATOM   2259 C  CG  . TRP   A 1 291 ? -30.884 4.186   20.630 1.00 68.14  ? 587 TRP   A CG  1 
ATOM   2260 C  CD1 . TRP   A 1 291 ? -31.247 4.284   21.963 1.00 70.00  ? 587 TRP   A CD1 1 
ATOM   2261 C  CD2 . TRP   A 1 291 ? -31.957 3.520   19.970 1.00 69.69  ? 587 TRP   A CD2 1 
ATOM   2262 N  NE1 . TRP   A 1 291 ? -32.481 3.705   22.150 1.00 68.30  ? 587 TRP   A NE1 1 
ATOM   2263 C  CE2 . TRP   A 1 291 ? -32.935 3.226   20.945 1.00 75.85  ? 587 TRP   A CE2 1 
ATOM   2264 C  CE3 . TRP   A 1 291 ? -32.185 3.133   18.646 1.00 73.86  ? 587 TRP   A CE3 1 
ATOM   2265 C  CZ2 . TRP   A 1 291 ? -34.120 2.564   20.634 1.00 80.52  ? 587 TRP   A CZ2 1 
ATOM   2266 C  CZ3 . TRP   A 1 291 ? -33.362 2.483   18.340 1.00 78.85  ? 587 TRP   A CZ3 1 
ATOM   2267 C  CH2 . TRP   A 1 291 ? -34.313 2.201   19.329 1.00 80.51  ? 587 TRP   A CH2 1 
ATOM   2268 N  N   . TYR   A 1 292 ? -27.194 4.875   21.863 1.00 62.22  ? 588 TYR   A N   1 
ATOM   2269 C  CA  . TYR   A 1 292 ? -26.508 4.959   23.148 1.00 59.19  ? 588 TYR   A CA  1 
ATOM   2270 C  C   . TYR   A 1 292 ? -27.464 5.285   24.276 1.00 64.11  ? 588 TYR   A C   1 
ATOM   2271 O  O   . TYR   A 1 292 ? -28.400 6.075   24.110 1.00 63.26  ? 588 TYR   A O   1 
ATOM   2272 C  CB  . TYR   A 1 292 ? -25.430 6.036   23.108 1.00 66.02  ? 588 TYR   A CB  1 
ATOM   2273 C  CG  . TYR   A 1 292 ? -24.043 5.552   22.767 1.00 67.04  ? 588 TYR   A CG  1 
ATOM   2274 C  CD1 . TYR   A 1 292 ? -23.410 5.981   21.612 1.00 64.96  ? 588 TYR   A CD1 1 
ATOM   2275 C  CD2 . TYR   A 1 292 ? -23.360 4.692   23.615 1.00 66.38  ? 588 TYR   A CD2 1 
ATOM   2276 C  CE1 . TYR   A 1 292 ? -22.137 5.572   21.303 1.00 67.11  ? 588 TYR   A CE1 1 
ATOM   2277 C  CE2 . TYR   A 1 292 ? -22.083 4.272   23.316 1.00 69.59  ? 588 TYR   A CE2 1 
ATOM   2278 C  CZ  . TYR   A 1 292 ? -21.476 4.713   22.162 1.00 64.74  ? 588 TYR   A CZ  1 
ATOM   2279 O  OH  . TYR   A 1 292 ? -20.207 4.280   21.856 1.00 64.87  ? 588 TYR   A OH  1 
ATOM   2280 N  N   . MET   A 1 293 ? -27.200 4.676   25.436 1.00 60.33  ? 589 MET   A N   1 
ATOM   2281 C  CA  . MET   A 1 293 ? -27.626 5.214   26.712 1.00 60.85  ? 589 MET   A CA  1 
ATOM   2282 C  C   . MET   A 1 293 ? -26.551 6.184   27.187 1.00 69.18  ? 589 MET   A C   1 
ATOM   2283 O  O   . MET   A 1 293 ? -25.356 5.870   27.127 1.00 68.50  ? 589 MET   A O   1 
ATOM   2284 C  CB  . MET   A 1 293 ? -27.839 4.084   27.726 1.00 51.38  ? 589 MET   A CB  1 
ATOM   2285 C  CG  . MET   A 1 293 ? -28.442 4.547   29.082 1.00 54.02  ? 589 MET   A CG  1 
ATOM   2286 S  SD  . MET   A 1 293 ? -28.938 3.170   30.126 1.00 61.40  ? 589 MET   A SD  1 
ATOM   2287 C  CE  . MET   A 1 293 ? -27.374 2.399   30.546 1.00 61.18  ? 589 MET   A CE  1 
ATOM   2288 N  N   . GLY   A 1 294 ? -26.980 7.380   27.605 1.00 68.33  ? 590 GLY   A N   1 
ATOM   2289 C  CA  . GLY   A 1 294 ? -26.040 8.451   27.933 1.00 66.96  ? 590 GLY   A CA  1 
ATOM   2290 C  C   . GLY   A 1 294 ? -24.843 7.994   28.743 1.00 71.23  ? 590 GLY   A C   1 
ATOM   2291 O  O   . GLY   A 1 294 ? -23.709 8.390   28.465 1.00 78.00  ? 590 GLY   A O   1 
ATOM   2292 N  N   . THR   A 1 295 ? -25.076 7.142   29.743 1.00 65.71  ? 591 THR   A N   1 
ATOM   2293 C  CA  . THR   A 1 295 ? -24.030 6.816   30.714 1.00 65.90  ? 591 THR   A CA  1 
ATOM   2294 C  C   . THR   A 1 295 ? -22.862 6.079   30.080 1.00 66.55  ? 591 THR   A C   1 
ATOM   2295 O  O   . THR   A 1 295 ? -21.731 6.168   30.576 1.00 63.50  ? 591 THR   A O   1 
ATOM   2296 C  CB  . THR   A 1 295 ? -24.592 5.968   31.851 1.00 58.41  ? 591 THR   A CB  1 
ATOM   2297 O  OG1 . THR   A 1 295 ? -25.394 4.918   31.318 1.00 59.19  ? 591 THR   A OG1 1 
ATOM   2298 C  CG2 . THR   A 1 295 ? -25.410 6.827   32.822 1.00 61.49  ? 591 THR   A CG2 1 
ATOM   2299 N  N   . GLU   A 1 296 ? -23.113 5.328   29.011 1.00 59.19  ? 592 GLU   A N   1 
ATOM   2300 C  CA  . GLU   A 1 296 ? -22.028 4.631   28.327 1.00 59.17  ? 592 GLU   A CA  1 
ATOM   2301 C  C   . GLU   A 1 296 ? -20.947 5.606   27.894 1.00 64.21  ? 592 GLU   A C   1 
ATOM   2302 O  O   . GLU   A 1 296 ? -19.753 5.366   28.109 1.00 68.94  ? 592 GLU   A O   1 
ATOM   2303 C  CB  . GLU   A 1 296 ? -22.574 3.896   27.111 1.00 55.06  ? 592 GLU   A CB  1 
ATOM   2304 C  CG  . GLU   A 1 296 ? -23.602 2.848   27.409 1.00 60.19  ? 592 GLU   A CG  1 
ATOM   2305 C  CD  . GLU   A 1 296 ? -24.059 2.189   26.121 1.00 59.90  ? 592 GLU   A CD  1 
ATOM   2306 O  OE1 . GLU   A 1 296 ? -23.320 1.312   25.614 1.00 62.05  ? 592 GLU   A OE1 1 
ATOM   2307 O  OE2 . GLU   A 1 296 ? -25.121 2.588   25.588 1.00 67.05  ? 592 GLU   A OE2 1 
ATOM   2308 N  N   . ILE   A 1 297 ? -21.363 6.721   27.286 1.00 62.19  ? 593 ILE   A N   1 
ATOM   2309 C  CA  . ILE   A 1 297 ? -20.444 7.803   26.941 1.00 63.60  ? 593 ILE   A CA  1 
ATOM   2310 C  C   . ILE   A 1 297 ? -20.014 8.578   28.181 1.00 72.62  ? 593 ILE   A C   1 
ATOM   2311 O  O   . ILE   A 1 297 ? -18.819 8.731   28.454 1.00 76.68  ? 593 ILE   A O   1 
ATOM   2312 C  CB  . ILE   A 1 297 ? -21.103 8.757   25.939 1.00 67.74  ? 593 ILE   A CB  1 
ATOM   2313 C  CG1 . ILE   A 1 297 ? -21.721 7.971   24.789 1.00 69.14  ? 593 ILE   A CG1 1 
ATOM   2314 C  CG2 . ILE   A 1 297 ? -20.092 9.737   25.414 1.00 70.45  ? 593 ILE   A CG2 1 
ATOM   2315 C  CD1 . ILE   A 1 297 ? -22.682 8.806   24.008 1.00 67.41  ? 593 ILE   A CD1 1 
ATOM   2316 N  N   . GLY   A 1 298 ? -20.986 9.156   28.895 1.00 71.99  ? 594 GLY   A N   1 
ATOM   2317 C  CA  . GLY   A 1 298 ? -20.691 10.180  29.886 1.00 77.41  ? 594 GLY   A CA  1 
ATOM   2318 C  C   . GLY   A 1 298 ? -20.060 9.656   31.153 1.00 74.01  ? 594 GLY   A C   1 
ATOM   2319 O  O   . GLY   A 1 298 ? -19.377 10.411  31.853 1.00 76.12  ? 594 GLY   A O   1 
ATOM   2320 N  N   . VAL   A 1 299 ? -20.265 8.382   31.464 1.00 73.85  ? 595 VAL   A N   1 
ATOM   2321 C  CA  . VAL   A 1 299 ? -19.722 7.768   32.676 1.00 78.25  ? 595 VAL   A CA  1 
ATOM   2322 C  C   . VAL   A 1 299 ? -18.539 6.863   32.352 1.00 71.91  ? 595 VAL   A C   1 
ATOM   2323 O  O   . VAL   A 1 299 ? -17.426 7.080   32.832 1.00 82.15  ? 595 VAL   A O   1 
ATOM   2324 C  CB  . VAL   A 1 299 ? -20.816 6.997   33.446 1.00 71.75  ? 595 VAL   A CB  1 
ATOM   2325 C  CG1 . VAL   A 1 299 ? -20.221 6.394   34.671 1.00 72.44  ? 595 VAL   A CG1 1 
ATOM   2326 C  CG2 . VAL   A 1 299 ? -21.952 7.909   33.820 1.00 70.92  ? 595 VAL   A CG2 1 
ATOM   2327 N  N   . ARG   A 1 300 ? -18.770 5.824   31.555 1.00 63.43  ? 596 ARG   A N   1 
ATOM   2328 C  CA  . ARG   A 1 300 ? -17.718 4.869   31.238 1.00 61.57  ? 596 ARG   A CA  1 
ATOM   2329 C  C   . ARG   A 1 300 ? -16.708 5.446   30.244 1.00 74.14  ? 596 ARG   A C   1 
ATOM   2330 O  O   . ARG   A 1 300 ? -15.505 5.499   30.525 1.00 73.71  ? 596 ARG   A O   1 
ATOM   2331 C  CB  . ARG   A 1 300 ? -18.361 3.587   30.710 1.00 59.40  ? 596 ARG   A CB  1 
ATOM   2332 C  CG  . ARG   A 1 300 ? -19.454 3.068   31.659 1.00 61.13  ? 596 ARG   A CG  1 
ATOM   2333 C  CD  . ARG   A 1 300 ? -18.879 2.854   33.060 1.00 67.28  ? 596 ARG   A CD  1 
ATOM   2334 N  NE  . ARG   A 1 300 ? -17.644 2.077   33.015 1.00 59.58  ? 596 ARG   A NE  1 
ATOM   2335 C  CZ  . ARG   A 1 300 ? -17.598 0.788   32.689 1.00 59.07  ? 596 ARG   A CZ  1 
ATOM   2336 N  NH1 . ARG   A 1 300 ? -18.717 0.127   32.400 1.00 54.60  ? 596 ARG   A NH1 1 
ATOM   2337 N  NH2 . ARG   A 1 300 ? -16.433 0.158   32.654 1.00 66.24  ? 596 ARG   A NH2 1 
ATOM   2338 N  N   . ASP   A 1 301 ? -17.171 5.874   29.066 1.00 74.64  ? 597 ASP   A N   1 
ATOM   2339 C  CA  . ASP   A 1 301 ? -16.228 6.330   28.045 1.00 73.89  ? 597 ASP   A CA  1 
ATOM   2340 C  C   . ASP   A 1 301 ? -15.431 7.539   28.522 1.00 78.09  ? 597 ASP   A C   1 
ATOM   2341 O  O   . ASP   A 1 301 ? -14.225 7.635   28.268 1.00 86.18  ? 597 ASP   A O   1 
ATOM   2342 C  CB  . ASP   A 1 301 ? -16.958 6.640   26.725 1.00 67.42  ? 597 ASP   A CB  1 
ATOM   2343 C  CG  . ASP   A 1 301 ? -17.478 5.399   26.037 1.00 69.12  ? 597 ASP   A CG  1 
ATOM   2344 O  OD1 . ASP   A 1 301 ? -16.809 4.342   26.109 1.00 77.28  ? 597 ASP   A OD1 1 
ATOM   2345 O  OD2 . ASP   A 1 301 ? -18.560 5.477   25.411 1.00 73.68  ? 597 ASP   A OD2 1 
ATOM   2346 N  N   . TYR   A 1 302 ? -16.077 8.459   29.239 1.00 76.94  ? 598 TYR   A N   1 
ATOM   2347 C  CA  . TYR   A 1 302 ? -15.459 9.738   29.569 1.00 79.65  ? 598 TYR   A CA  1 
ATOM   2348 C  C   . TYR   A 1 302 ? -14.779 9.744   30.930 1.00 84.20  ? 598 TYR   A C   1 
ATOM   2349 O  O   . TYR   A 1 302 ? -13.799 10.479  31.123 1.00 82.79  ? 598 TYR   A O   1 
ATOM   2350 C  CB  . TYR   A 1 302 ? -16.507 10.859  29.536 1.00 87.99  ? 598 TYR   A CB  1 
ATOM   2351 C  CG  . TYR   A 1 302 ? -16.846 11.418  28.157 1.00 93.07  ? 598 TYR   A CG  1 
ATOM   2352 C  CD1 . TYR   A 1 302 ? -18.036 12.114  27.935 1.00 93.77  ? 598 TYR   A CD1 1 
ATOM   2353 C  CD2 . TYR   A 1 302 ? -15.971 11.269  27.085 1.00 89.23  ? 598 TYR   A CD2 1 
ATOM   2354 C  CE1 . TYR   A 1 302 ? -18.350 12.637  26.667 1.00 88.73  ? 598 TYR   A CE1 1 
ATOM   2355 C  CE2 . TYR   A 1 302 ? -16.277 11.785  25.835 1.00 93.36  ? 598 TYR   A CE2 1 
ATOM   2356 C  CZ  . TYR   A 1 302 ? -17.462 12.464  25.632 1.00 89.56  ? 598 TYR   A CZ  1 
ATOM   2357 O  OH  . TYR   A 1 302 ? -17.748 12.983  24.376 1.00 83.03  ? 598 TYR   A OH  1 
ATOM   2358 N  N   . CYS   A 1 303 ? -15.258 8.934   31.873 1.00 74.94  ? 599 CYS   A N   1 
ATOM   2359 C  CA  . CYS   A 1 303 ? -14.818 9.042   33.257 1.00 80.45  ? 599 CYS   A CA  1 
ATOM   2360 C  C   . CYS   A 1 303 ? -14.181 7.779   33.819 1.00 80.68  ? 599 CYS   A C   1 
ATOM   2361 O  O   . CYS   A 1 303 ? -13.654 7.829   34.939 1.00 83.13  ? 599 CYS   A O   1 
ATOM   2362 C  CB  . CYS   A 1 303 ? -15.995 9.451   34.149 1.00 80.13  ? 599 CYS   A CB  1 
ATOM   2363 S  SG  . CYS   A 1 303 ? -16.738 11.023  33.681 1.00 86.38  ? 599 CYS   A SG  1 
ATOM   2364 N  N   . ASP   A 1 304 ? -14.222 6.654   33.102 1.00 81.26  ? 600 ASP   A N   1 
ATOM   2365 C  CA  . ASP   A 1 304 ? -13.383 5.520   33.473 1.00 86.54  ? 600 ASP   A CA  1 
ATOM   2366 C  C   . ASP   A 1 304 ? -11.943 5.994   33.609 1.00 93.71  ? 600 ASP   A C   1 
ATOM   2367 O  O   . ASP   A 1 304 ? -11.472 6.825   32.828 1.00 101.81 ? 600 ASP   A O   1 
ATOM   2368 C  CB  . ASP   A 1 304 ? -13.465 4.403   32.424 1.00 86.71  ? 600 ASP   A CB  1 
ATOM   2369 C  CG  . ASP   A 1 304 ? -14.434 3.284   32.809 1.00 78.03  ? 600 ASP   A CG  1 
ATOM   2370 O  OD1 . ASP   A 1 304 ? -15.218 3.481   33.758 1.00 75.52  ? 600 ASP   A OD1 1 
ATOM   2371 O  OD2 . ASP   A 1 304 ? -14.415 2.209   32.154 1.00 70.12  ? 600 ASP   A OD2 1 
ATOM   2372 N  N   . ASN   A 1 305 ? -11.256 5.487   34.631 1.00 95.70  ? 601 ASN   A N   1 
ATOM   2373 C  CA  . ASN   A 1 305 ? -9.877  5.900   34.866 1.00 94.10  ? 601 ASN   A CA  1 
ATOM   2374 C  C   . ASN   A 1 305 ? -8.978  5.523   33.697 1.00 87.79  ? 601 ASN   A C   1 
ATOM   2375 O  O   . ASN   A 1 305 ? -8.072  6.281   33.332 1.00 90.77  ? 601 ASN   A O   1 
ATOM   2376 C  CB  . ASN   A 1 305 ? -9.355  5.277   36.158 1.00 94.25  ? 601 ASN   A CB  1 
ATOM   2377 C  CG  . ASN   A 1 305 ? -9.411  6.234   37.330 1.00 102.66 ? 601 ASN   A CG  1 
ATOM   2378 O  OD1 . ASN   A 1 305 ? -9.381  7.451   37.153 1.00 110.02 ? 601 ASN   A OD1 1 
ATOM   2379 N  ND2 . ASN   A 1 305 ? -9.480  5.687   38.541 1.00 100.15 ? 601 ASN   A ND2 1 
ATOM   2380 N  N   . SER   A 1 306 ? -9.205  4.350   33.106 1.00 89.33  ? 602 SER   A N   1 
ATOM   2381 C  CA  . SER   A 1 306 ? -8.421  3.882   31.973 1.00 94.09  ? 602 SER   A CA  1 
ATOM   2382 C  C   . SER   A 1 306 ? -9.079  4.195   30.633 1.00 91.05  ? 602 SER   A C   1 
ATOM   2383 O  O   . SER   A 1 306 ? -8.724  3.578   29.623 1.00 91.26  ? 602 SER   A O   1 
ATOM   2384 C  CB  . SER   A 1 306 ? -8.156  2.380   32.094 1.00 97.42  ? 602 SER   A CB  1 
ATOM   2385 O  OG  . SER   A 1 306 ? -9.369  1.658   32.193 1.00 96.14  ? 602 SER   A OG  1 
ATOM   2386 N  N   . ARG   A 1 307 ? -10.032 5.128   30.603 1.00 87.20  ? 603 ARG   A N   1 
ATOM   2387 C  CA  . ARG   A 1 307 ? -10.548 5.647   29.340 1.00 85.47  ? 603 ARG   A CA  1 
ATOM   2388 C  C   . ARG   A 1 307 ? -10.187 7.122   29.217 1.00 90.32  ? 603 ARG   A C   1 
ATOM   2389 O  O   . ARG   A 1 307 ? -9.029  7.490   29.437 1.00 99.30  ? 603 ARG   A O   1 
ATOM   2390 C  CB  . ARG   A 1 307 ? -12.060 5.425   29.229 1.00 72.97  ? 603 ARG   A CB  1 
ATOM   2391 C  CG  . ARG   A 1 307 ? -12.464 3.955   29.239 1.00 66.36  ? 603 ARG   A CG  1 
ATOM   2392 C  CD  . ARG   A 1 307 ? -11.988 3.185   28.012 1.00 68.74  ? 603 ARG   A CD  1 
ATOM   2393 N  NE  . ARG   A 1 307 ? -12.558 3.721   26.787 1.00 68.17  ? 603 ARG   A NE  1 
ATOM   2394 C  CZ  . ARG   A 1 307 ? -13.832 3.574   26.439 1.00 75.70  ? 603 ARG   A CZ  1 
ATOM   2395 N  NH1 . ARG   A 1 307 ? -14.658 2.907   27.233 1.00 68.81  ? 603 ARG   A NH1 1 
ATOM   2396 N  NH2 . ARG   A 1 307 ? -14.273 4.090   25.301 1.00 85.75  ? 603 ARG   A NH2 1 
ATOM   2397 N  N   . TYR   A 1 308 ? -11.158 7.979   28.884 1.00 86.70  ? 604 TYR   A N   1 
ATOM   2398 C  CA  . TYR   A 1 308 ? -10.828 9.376   28.601 1.00 89.12  ? 604 TYR   A CA  1 
ATOM   2399 C  C   . TYR   A 1 308 ? -10.488 10.144  29.871 1.00 99.43  ? 604 TYR   A C   1 
ATOM   2400 O  O   . TYR   A 1 308 ? -9.726  11.120  29.817 1.00 106.83 ? 604 TYR   A O   1 
ATOM   2401 C  CB  . TYR   A 1 308 ? -11.970 10.050  27.844 1.00 87.08  ? 604 TYR   A CB  1 
ATOM   2402 C  CG  . TYR   A 1 308 ? -11.829 9.895   26.336 1.00 92.37  ? 604 TYR   A CG  1 
ATOM   2403 C  CD1 . TYR   A 1 308 ? -11.972 8.656   25.732 1.00 87.91  ? 604 TYR   A CD1 1 
ATOM   2404 C  CD2 . TYR   A 1 308 ? -11.525 10.981  25.533 1.00 101.16 ? 604 TYR   A CD2 1 
ATOM   2405 C  CE1 . TYR   A 1 308 ? -11.828 8.498   24.366 1.00 84.95  ? 604 TYR   A CE1 1 
ATOM   2406 C  CE2 . TYR   A 1 308 ? -11.374 10.840  24.148 1.00 97.84  ? 604 TYR   A CE2 1 
ATOM   2407 C  CZ  . TYR   A 1 308 ? -11.533 9.593   23.574 1.00 93.85  ? 604 TYR   A CZ  1 
ATOM   2408 O  OH  . TYR   A 1 308 ? -11.391 9.427   22.212 1.00 92.45  ? 604 TYR   A OH  1 
ATOM   2409 N  N   . ASN   A 1 309 ? -11.049 9.729   31.007 1.00 92.36  ? 605 ASN   A N   1 
ATOM   2410 C  CA  . ASN   A 1 309 ? -10.590 10.162  32.324 1.00 97.74  ? 605 ASN   A CA  1 
ATOM   2411 C  C   . ASN   A 1 309 ? -10.645 11.687  32.455 1.00 106.60 ? 605 ASN   A C   1 
ATOM   2412 O  O   . ASN   A 1 309 ? -9.643  12.361  32.711 1.00 112.99 ? 605 ASN   A O   1 
ATOM   2413 C  CB  . ASN   A 1 309 ? -9.181  9.628   32.584 1.00 101.40 ? 605 ASN   A CB  1 
ATOM   2414 C  CG  . ASN   A 1 309 ? -8.755  9.818   33.997 1.00 98.93  ? 605 ASN   A CG  1 
ATOM   2415 O  OD1 . ASN   A 1 309 ? -9.594  9.835   34.896 1.00 93.72  ? 605 ASN   A OD1 1 
ATOM   2416 N  ND2 . ASN   A 1 309 ? -7.455  9.984   34.214 1.00 106.68 ? 605 ASN   A ND2 1 
ATOM   2417 N  N   . ILE   A 1 310 ? -11.853 12.226  32.261 1.00 102.23 ? 606 ILE   A N   1 
ATOM   2418 C  CA  . ILE   A 1 310 ? -12.038 13.668  32.174 1.00 104.54 ? 606 ILE   A CA  1 
ATOM   2419 C  C   . ILE   A 1 310 ? -12.605 14.276  33.452 1.00 105.09 ? 606 ILE   A C   1 
ATOM   2420 O  O   . ILE   A 1 310 ? -12.806 15.496  33.497 1.00 109.71 ? 606 ILE   A O   1 
ATOM   2421 C  CB  . ILE   A 1 310 ? -12.932 14.038  30.974 1.00 106.93 ? 606 ILE   A CB  1 
ATOM   2422 C  CG1 . ILE   A 1 310 ? -14.379 13.626  31.245 1.00 103.03 ? 606 ILE   A CG1 1 
ATOM   2423 C  CG2 . ILE   A 1 310 ? -12.412 13.387  29.684 1.00 94.25  ? 606 ILE   A CG2 1 
ATOM   2424 C  CD1 . ILE   A 1 310 ? -15.346 14.175  30.227 1.00 90.17  ? 606 ILE   A CD1 1 
ATOM   2425 N  N   . LEU   A 1 311 ? -12.878 13.472  34.490 1.00 100.05 ? 607 LEU   A N   1 
ATOM   2426 C  CA  . LEU   A 1 311 ? -13.351 14.055  35.749 1.00 101.75 ? 607 LEU   A CA  1 
ATOM   2427 C  C   . LEU   A 1 311 ? -12.414 15.153  36.229 1.00 103.64 ? 607 LEU   A C   1 
ATOM   2428 O  O   . LEU   A 1 311 ? -12.873 16.161  36.775 1.00 100.69 ? 607 LEU   A O   1 
ATOM   2429 C  CB  . LEU   A 1 311 ? -13.512 12.978  36.830 1.00 85.61  ? 607 LEU   A CB  1 
ATOM   2430 C  CG  . LEU   A 1 311 ? -14.755 12.078  36.754 1.00 85.65  ? 607 LEU   A CG  1 
ATOM   2431 C  CD1 . LEU   A 1 311 ? -14.743 11.000  37.849 1.00 87.44  ? 607 LEU   A CD1 1 
ATOM   2432 C  CD2 . LEU   A 1 311 ? -16.050 12.896  36.775 1.00 81.06  ? 607 LEU   A CD2 1 
ATOM   2433 N  N   . GLU   A 1 312 ? -11.109 14.987  35.995 1.00 124.01 ? 608 GLU   A N   1 
ATOM   2434 C  CA  . GLU   A 1 312 ? -10.082 15.993  36.251 1.00 141.65 ? 608 GLU   A CA  1 
ATOM   2435 C  C   . GLU   A 1 312 ? -10.492 17.404  35.844 1.00 140.21 ? 608 GLU   A C   1 
ATOM   2436 O  O   . GLU   A 1 312 ? -10.653 18.282  36.699 1.00 135.90 ? 608 GLU   A O   1 
ATOM   2437 C  CB  . GLU   A 1 312 ? -8.796  15.625  35.503 1.00 154.27 ? 608 GLU   A CB  1 
ATOM   2438 C  CG  . GLU   A 1 312 ? -8.096  14.377  36.009 1.00 158.14 ? 608 GLU   A CG  1 
ATOM   2439 C  CD  . GLU   A 1 312 ? -7.184  14.660  37.188 1.00 165.46 ? 608 GLU   A CD  1 
ATOM   2440 O  OE1 . GLU   A 1 312 ? -7.407  15.665  37.896 1.00 168.74 ? 608 GLU   A OE1 1 
ATOM   2441 O  OE2 . GLU   A 1 312 ? -6.235  13.877  37.402 1.00 166.81 ? 608 GLU   A OE2 1 
ATOM   2442 N  N   . GLU   A 1 313 ? -10.650 17.629  34.538 1.00 139.30 ? 609 GLU   A N   1 
ATOM   2443 C  CA  . GLU   A 1 313 ? -10.858 18.981  34.034 1.00 147.51 ? 609 GLU   A CA  1 
ATOM   2444 C  C   . GLU   A 1 313 ? -12.267 19.493  34.290 1.00 142.98 ? 609 GLU   A C   1 
ATOM   2445 O  O   . GLU   A 1 313 ? -12.449 20.691  34.531 1.00 155.45 ? 609 GLU   A O   1 
ATOM   2446 C  CB  . GLU   A 1 313 ? -10.543 19.041  32.539 1.00 153.65 ? 609 GLU   A CB  1 
ATOM   2447 C  CG  . GLU   A 1 313 ? -9.064  19.228  32.220 1.00 163.31 ? 609 GLU   A CG  1 
ATOM   2448 C  CD  . GLU   A 1 313 ? -8.581  20.657  32.439 1.00 173.95 ? 609 GLU   A CD  1 
ATOM   2449 O  OE1 . GLU   A 1 313 ? -8.684  21.171  33.572 1.00 174.91 ? 609 GLU   A OE1 1 
ATOM   2450 O  OE2 . GLU   A 1 313 ? -8.101  21.272  31.463 1.00 179.70 ? 609 GLU   A OE2 1 
ATOM   2451 N  N   . VAL   A 1 314 ? -13.272 18.619  34.242 1.00 124.31 ? 610 VAL   A N   1 
ATOM   2452 C  CA  . VAL   A 1 314 ? -14.637 19.070  34.487 1.00 116.13 ? 610 VAL   A CA  1 
ATOM   2453 C  C   . VAL   A 1 314 ? -14.810 19.543  35.928 1.00 118.51 ? 610 VAL   A C   1 
ATOM   2454 O  O   . VAL   A 1 314 ? -15.573 20.479  36.199 1.00 120.61 ? 610 VAL   A O   1 
ATOM   2455 C  CB  . VAL   A 1 314 ? -15.621 17.950  34.127 1.00 106.24 ? 610 VAL   A CB  1 
ATOM   2456 C  CG1 . VAL   A 1 314 ? -17.038 18.334  34.519 1.00 106.78 ? 610 VAL   A CG1 1 
ATOM   2457 C  CG2 . VAL   A 1 314 ? -15.525 17.657  32.623 1.00 100.31 ? 610 VAL   A CG2 1 
ATOM   2458 N  N   . ALA   A 1 315 ? -14.117 18.920  36.875 1.00 117.30 ? 611 ALA   A N   1 
ATOM   2459 C  CA  . ALA   A 1 315 ? -14.144 19.448  38.233 1.00 122.75 ? 611 ALA   A CA  1 
ATOM   2460 C  C   . ALA   A 1 315 ? -13.528 20.837  38.270 1.00 133.18 ? 611 ALA   A C   1 
ATOM   2461 O  O   . ALA   A 1 315 ? -14.072 21.757  38.890 1.00 142.52 ? 611 ALA   A O   1 
ATOM   2462 C  CB  . ALA   A 1 315 ? -13.411 18.507  39.181 1.00 121.73 ? 611 ALA   A CB  1 
ATOM   2463 N  N   . LYS   A 1 316 ? -12.402 21.007  37.584 1.00 134.17 ? 612 LYS   A N   1 
ATOM   2464 C  CA  . LYS   A 1 316 ? -11.662 22.259  37.590 1.00 145.18 ? 612 LYS   A CA  1 
ATOM   2465 C  C   . LYS   A 1 316 ? -12.535 23.433  37.167 1.00 147.38 ? 612 LYS   A C   1 
ATOM   2466 O  O   . LYS   A 1 316 ? -12.780 24.348  37.961 1.00 150.14 ? 612 LYS   A O   1 
ATOM   2467 C  CB  . LYS   A 1 316 ? -10.443 22.143  36.677 1.00 141.41 ? 612 LYS   A CB  1 
ATOM   2468 C  CG  . LYS   A 1 316 ? -9.377  21.209  37.220 1.00 143.01 ? 612 LYS   A CG  1 
ATOM   2469 C  CD  . LYS   A 1 316 ? -8.030  21.508  36.598 1.00 150.22 ? 612 LYS   A CD  1 
ATOM   2470 C  CE  . LYS   A 1 316 ? -7.727  23.004  36.647 1.00 162.95 ? 612 LYS   A CE  1 
ATOM   2471 N  NZ  . LYS   A 1 316 ? -6.624  23.409  35.720 1.00 169.31 ? 612 LYS   A NZ  1 
ATOM   2472 N  N   . LYS   A 1 317 ? -13.030 23.396  35.929 1.00 139.66 ? 613 LYS   A N   1 
ATOM   2473 C  CA  . LYS   A 1 317 ? -13.770 24.519  35.364 1.00 144.60 ? 613 LYS   A CA  1 
ATOM   2474 C  C   . LYS   A 1 317 ? -15.111 24.756  36.044 1.00 145.90 ? 613 LYS   A C   1 
ATOM   2475 O  O   . LYS   A 1 317 ? -15.731 25.798  35.802 1.00 149.83 ? 613 LYS   A O   1 
ATOM   2476 C  CB  . LYS   A 1 317 ? -13.972 24.295  33.866 1.00 143.38 ? 613 LYS   A CB  1 
ATOM   2477 C  CG  . LYS   A 1 317 ? -12.670 24.203  33.112 1.00 143.50 ? 613 LYS   A CG  1 
ATOM   2478 C  CD  . LYS   A 1 317 ? -12.877 23.998  31.642 1.00 144.90 ? 613 LYS   A CD  1 
ATOM   2479 C  CE  . LYS   A 1 317 ? -11.537 23.974  30.945 1.00 148.65 ? 613 LYS   A CE  1 
ATOM   2480 N  NZ  . LYS   A 1 317 ? -10.551 23.181  31.734 1.00 142.77 ? 613 LYS   A NZ  1 
ATOM   2481 N  N   . MET   A 1 318 ? -15.566 23.828  36.883 1.00 144.20 ? 614 MET   A N   1 
ATOM   2482 C  CA  . MET   A 1 318 ? -16.763 24.025  37.688 1.00 148.15 ? 614 MET   A CA  1 
ATOM   2483 C  C   . MET   A 1 318 ? -16.491 24.734  39.004 1.00 150.80 ? 614 MET   A C   1 
ATOM   2484 O  O   . MET   A 1 318 ? -17.450 25.117  39.681 1.00 153.74 ? 614 MET   A O   1 
ATOM   2485 C  CB  . MET   A 1 318 ? -17.428 22.683  37.989 1.00 138.82 ? 614 MET   A CB  1 
ATOM   2486 C  CG  . MET   A 1 318 ? -18.226 22.125  36.840 1.00 139.63 ? 614 MET   A CG  1 
ATOM   2487 S  SD  . MET   A 1 318 ? -19.015 20.574  37.276 1.00 130.54 ? 614 MET   A SD  1 
ATOM   2488 C  CE  . MET   A 1 318 ? -20.009 21.094  38.680 1.00 127.04 ? 614 MET   A CE  1 
ATOM   2489 N  N   . ASP   A 1 319 ? -15.218 24.913  39.371 1.00 158.40 ? 615 ASP   A N   1 
ATOM   2490 C  CA  . ASP   A 1 319 ? -14.808 25.414  40.681 1.00 169.49 ? 615 ASP   A CA  1 
ATOM   2491 C  C   . ASP   A 1 319 ? -15.234 24.439  41.773 1.00 161.65 ? 615 ASP   A C   1 
ATOM   2492 O  O   . ASP   A 1 319 ? -16.251 24.648  42.441 1.00 164.03 ? 615 ASP   A O   1 
ATOM   2493 C  CB  . ASP   A 1 319 ? -15.378 26.814  40.943 1.00 181.50 ? 615 ASP   A CB  1 
ATOM   2494 C  CG  . ASP   A 1 319 ? -14.634 27.555  42.042 1.00 191.53 ? 615 ASP   A CG  1 
ATOM   2495 O  OD1 . ASP   A 1 319 ? -13.386 27.589  41.990 1.00 195.40 ? 615 ASP   A OD1 1 
ATOM   2496 O  OD2 . ASP   A 1 319 ? -15.290 28.127  42.939 1.00 194.79 ? 615 ASP   A OD2 1 
ATOM   2497 N  N   . LEU   A 1 320 ? -14.460 23.367  41.955 1.00 153.71 ? 616 LEU   A N   1 
ATOM   2498 C  CA  . LEU   A 1 320 ? -14.765 22.323  42.924 1.00 143.06 ? 616 LEU   A CA  1 
ATOM   2499 C  C   . LEU   A 1 320 ? -13.559 22.063  43.815 1.00 143.87 ? 616 LEU   A C   1 
ATOM   2500 O  O   . LEU   A 1 320 ? -12.410 22.164  43.376 1.00 142.53 ? 616 LEU   A O   1 
ATOM   2501 C  CB  . LEU   A 1 320 ? -15.175 21.013  42.236 1.00 129.04 ? 616 LEU   A CB  1 
ATOM   2502 C  CG  . LEU   A 1 320 ? -16.470 21.035  41.429 1.00 123.63 ? 616 LEU   A CG  1 
ATOM   2503 C  CD1 . LEU   A 1 320 ? -16.772 19.644  40.890 1.00 117.19 ? 616 LEU   A CD1 1 
ATOM   2504 C  CD2 . LEU   A 1 320 ? -17.605 21.541  42.303 1.00 123.89 ? 616 LEU   A CD2 1 
ATOM   2505 N  N   . ASP   A 1 321 ? -13.838 21.714  45.071 1.00 143.51 ? 617 ASP   A N   1 
ATOM   2506 C  CA  . ASP   A 1 321 ? -12.804 21.339  46.033 1.00 146.27 ? 617 ASP   A CA  1 
ATOM   2507 C  C   . ASP   A 1 321 ? -12.271 19.960  45.668 1.00 131.33 ? 617 ASP   A C   1 
ATOM   2508 O  O   . ASP   A 1 321 ? -12.906 18.942  45.946 1.00 123.18 ? 617 ASP   A O   1 
ATOM   2509 C  CB  . ASP   A 1 321 ? -13.371 21.367  47.450 1.00 156.74 ? 617 ASP   A CB  1 
ATOM   2510 C  CG  . ASP   A 1 321 ? -12.444 20.730  48.473 1.00 165.62 ? 617 ASP   A CG  1 
ATOM   2511 O  OD1 . ASP   A 1 321 ? -12.888 19.808  49.191 1.00 165.42 ? 617 ASP   A OD1 1 
ATOM   2512 O  OD2 . ASP   A 1 321 ? -11.269 21.142  48.555 1.00 174.13 ? 617 ASP   A OD2 1 
ATOM   2513 N  N   . MET   A 1 322 ? -11.100 19.920  45.032 1.00 131.74 ? 618 MET   A N   1 
ATOM   2514 C  CA  . MET   A 1 322 ? -10.507 18.663  44.594 1.00 137.10 ? 618 MET   A CA  1 
ATOM   2515 C  C   . MET   A 1 322 ? -9.492  18.096  45.580 1.00 147.72 ? 618 MET   A C   1 
ATOM   2516 O  O   . MET   A 1 322 ? -9.019  16.972  45.379 1.00 148.08 ? 618 MET   A O   1 
ATOM   2517 C  CB  . MET   A 1 322 ? -9.845  18.836  43.217 1.00 142.09 ? 618 MET   A CB  1 
ATOM   2518 C  CG  . MET   A 1 322 ? -10.780 18.581  42.042 1.00 137.89 ? 618 MET   A CG  1 
ATOM   2519 S  SD  . MET   A 1 322 ? -10.038 18.868  40.417 1.00 145.16 ? 618 MET   A SD  1 
ATOM   2520 C  CE  . MET   A 1 322 ? -8.740  17.632  40.376 1.00 144.41 ? 618 MET   A CE  1 
ATOM   2521 N  N   . ARG   A 1 323 ? -9.152  18.833  46.639 1.00 152.83 ? 619 ARG   A N   1 
ATOM   2522 C  CA  . ARG   A 1 323 ? -8.163  18.334  47.588 1.00 157.43 ? 619 ARG   A CA  1 
ATOM   2523 C  C   . ARG   A 1 323 ? -8.713  17.169  48.403 1.00 153.62 ? 619 ARG   A C   1 
ATOM   2524 O  O   . ARG   A 1 323 ? -7.993  16.204  48.681 1.00 154.33 ? 619 ARG   A O   1 
ATOM   2525 C  CB  . ARG   A 1 323 ? -7.707  19.466  48.508 1.00 165.57 ? 619 ARG   A CB  1 
ATOM   2526 C  CG  . ARG   A 1 323 ? -7.040  20.619  47.779 1.00 172.36 ? 619 ARG   A CG  1 
ATOM   2527 C  CD  . ARG   A 1 323 ? -7.245  21.932  48.515 1.00 181.16 ? 619 ARG   A CD  1 
ATOM   2528 N  NE  . ARG   A 1 323 ? -8.639  22.109  48.910 1.00 181.33 ? 619 ARG   A NE  1 
ATOM   2529 C  CZ  . ARG   A 1 323 ? -9.186  23.276  49.233 1.00 187.92 ? 619 ARG   A CZ  1 
ATOM   2530 N  NH1 . ARG   A 1 323 ? -8.461  24.385  49.201 1.00 197.03 ? 619 ARG   A NH1 1 
ATOM   2531 N  NH2 . ARG   A 1 323 ? -10.465 23.335  49.581 1.00 185.14 ? 619 ARG   A NH2 1 
ATOM   2532 N  N   . LYS   A 1 324 ? -9.984  17.235  48.785 1.00 148.72 ? 620 LYS   A N   1 
ATOM   2533 C  CA  . LYS   A 1 324 ? -10.585 16.256  49.681 1.00 141.66 ? 620 LYS   A CA  1 
ATOM   2534 C  C   . LYS   A 1 324 ? -11.393 15.248  48.877 1.00 136.05 ? 620 LYS   A C   1 
ATOM   2535 O  O   . LYS   A 1 324 ? -12.218 15.631  48.042 1.00 138.63 ? 620 LYS   A O   1 
ATOM   2536 C  CB  . LYS   A 1 324 ? -11.473 16.940  50.723 1.00 142.11 ? 620 LYS   A CB  1 
ATOM   2537 C  CG  . LYS   A 1 324 ? -10.734 17.423  51.966 1.00 148.58 ? 620 LYS   A CG  1 
ATOM   2538 C  CD  . LYS   A 1 324 ? -9.690  18.487  51.648 1.00 154.67 ? 620 LYS   A CD  1 
ATOM   2539 C  CE  . LYS   A 1 324 ? -8.857  18.834  52.873 1.00 152.65 ? 620 LYS   A CE  1 
ATOM   2540 N  NZ  . LYS   A 1 324 ? -7.745  19.760  52.527 1.00 157.37 ? 620 LYS   A NZ  1 
ATOM   2541 N  N   . THR   A 1 325 ? -11.148 13.960  49.130 1.00 123.76 ? 621 THR   A N   1 
ATOM   2542 C  CA  . THR   A 1 325 ? -11.895 12.909  48.446 1.00 105.97 ? 621 THR   A CA  1 
ATOM   2543 C  C   . THR   A 1 325 ? -13.397 13.049  48.679 1.00 99.96  ? 621 THR   A C   1 
ATOM   2544 O  O   . THR   A 1 325 ? -14.201 12.868  47.752 1.00 93.16  ? 621 THR   A O   1 
ATOM   2545 C  CB  . THR   A 1 325 ? -11.401 11.534  48.908 1.00 108.79 ? 621 THR   A CB  1 
ATOM   2546 O  OG1 . THR   A 1 325 ? -12.367 10.534  48.564 1.00 108.55 ? 621 THR   A OG1 1 
ATOM   2547 C  CG2 . THR   A 1 325 ? -11.154 11.506  50.426 1.00 122.44 ? 621 THR   A CG2 1 
ATOM   2548 N  N   . SER   A 1 326 ? -13.783 13.415  49.900 1.00 109.65 ? 622 SER   A N   1 
ATOM   2549 C  CA  . SER   A 1 326 ? -15.159 13.440  50.378 1.00 104.55 ? 622 SER   A CA  1 
ATOM   2550 C  C   . SER   A 1 326 ? -15.916 14.703  49.995 1.00 102.94 ? 622 SER   A C   1 
ATOM   2551 O  O   . SER   A 1 326 ? -17.071 14.860  50.403 1.00 103.01 ? 622 SER   A O   1 
ATOM   2552 C  CB  . SER   A 1 326 ? -15.161 13.288  51.897 1.00 99.53  ? 622 SER   A CB  1 
ATOM   2553 O  OG  . SER   A 1 326 ? -14.083 14.017  52.449 1.00 102.79 ? 622 SER   A OG  1 
ATOM   2554 N  N   . SER   A 1 327 ? -15.295 15.623  49.259 1.00 104.26 ? 623 SER   A N   1 
ATOM   2555 C  CA  . SER   A 1 327 ? -16.066 16.701  48.661 1.00 111.03 ? 623 SER   A CA  1 
ATOM   2556 C  C   . SER   A 1 327 ? -16.996 16.207  47.557 1.00 108.59 ? 623 SER   A C   1 
ATOM   2557 O  O   . SER   A 1 327 ? -17.798 16.999  47.054 1.00 116.62 ? 623 SER   A O   1 
ATOM   2558 C  CB  . SER   A 1 327 ? -15.125 17.779  48.110 1.00 119.45 ? 623 SER   A CB  1 
ATOM   2559 O  OG  . SER   A 1 327 ? -14.259 17.255  47.117 1.00 116.58 ? 623 SER   A OG  1 
ATOM   2560 N  N   . LEU   A 1 328 ? -16.906 14.926  47.174 1.00 97.84  ? 624 LEU   A N   1 
ATOM   2561 C  CA  . LEU   A 1 328 ? -17.693 14.342  46.072 1.00 96.46  ? 624 LEU   A CA  1 
ATOM   2562 C  C   . LEU   A 1 328 ? -17.592 15.172  44.798 1.00 101.96 ? 624 LEU   A C   1 
ATOM   2563 O  O   . LEU   A 1 328 ? -18.503 15.173  43.959 1.00 102.88 ? 624 LEU   A O   1 
ATOM   2564 C  CB  . LEU   A 1 328 ? -19.158 14.146  46.462 1.00 95.99  ? 624 LEU   A CB  1 
ATOM   2565 C  CG  . LEU   A 1 328 ? -19.358 13.302  47.727 1.00 92.85  ? 624 LEU   A CG  1 
ATOM   2566 C  CD1 . LEU   A 1 328 ? -20.799 12.861  47.844 1.00 83.12  ? 624 LEU   A CD1 1 
ATOM   2567 C  CD2 . LEU   A 1 328 ? -18.444 12.103  47.668 1.00 95.45  ? 624 LEU   A CD2 1 
ATOM   2568 N  N   . TRP   A 1 329 ? -16.471 15.874  44.631 1.00 101.27 ? 625 TRP   A N   1 
ATOM   2569 C  CA  . TRP   A 1 329 ? -16.253 16.593  43.383 1.00 104.22 ? 625 TRP   A CA  1 
ATOM   2570 C  C   . TRP   A 1 329 ? -16.317 15.659  42.183 1.00 99.50  ? 625 TRP   A C   1 
ATOM   2571 O  O   . TRP   A 1 329 ? -16.748 16.075  41.100 1.00 101.73 ? 625 TRP   A O   1 
ATOM   2572 C  CB  . TRP   A 1 329 ? -14.909 17.308  43.421 1.00 109.87 ? 625 TRP   A CB  1 
ATOM   2573 C  CG  . TRP   A 1 329 ? -13.746 16.382  43.537 1.00 107.18 ? 625 TRP   A CG  1 
ATOM   2574 C  CD1 . TRP   A 1 329 ? -13.173 15.928  44.678 1.00 109.66 ? 625 TRP   A CD1 1 
ATOM   2575 C  CD2 . TRP   A 1 329 ? -13.011 15.791  42.457 1.00 111.61 ? 625 TRP   A CD2 1 
ATOM   2576 N  NE1 . TRP   A 1 329 ? -12.120 15.095  44.386 1.00 105.86 ? 625 TRP   A NE1 1 
ATOM   2577 C  CE2 . TRP   A 1 329 ? -12.003 14.992  43.027 1.00 109.47 ? 625 TRP   A CE2 1 
ATOM   2578 C  CE3 . TRP   A 1 329 ? -13.110 15.858  41.064 1.00 99.98  ? 625 TRP   A CE3 1 
ATOM   2579 C  CZ2 . TRP   A 1 329 ? -11.098 14.270  42.254 1.00 105.25 ? 625 TRP   A CZ2 1 
ATOM   2580 C  CZ3 . TRP   A 1 329 ? -12.211 15.153  40.304 1.00 98.41  ? 625 TRP   A CZ3 1 
ATOM   2581 C  CH2 . TRP   A 1 329 ? -11.217 14.367  40.896 1.00 103.18 ? 625 TRP   A CH2 1 
ATOM   2582 N  N   . LYS   A 1 330 ? -15.895 14.400  42.349 1.00 96.54  ? 626 LYS   A N   1 
ATOM   2583 C  CA  . LYS   A 1 330 ? -15.989 13.448  41.241 1.00 101.06 ? 626 LYS   A CA  1 
ATOM   2584 C  C   . LYS   A 1 330 ? -17.440 13.199  40.857 1.00 95.09  ? 626 LYS   A C   1 
ATOM   2585 O  O   . LYS   A 1 330 ? -17.793 13.202  39.670 1.00 96.40  ? 626 LYS   A O   1 
ATOM   2586 C  CB  . LYS   A 1 330 ? -15.304 12.129  41.609 1.00 101.96 ? 626 LYS   A CB  1 
ATOM   2587 C  CG  . LYS   A 1 330 ? -13.788 12.152  41.540 1.00 103.51 ? 626 LYS   A CG  1 
ATOM   2588 C  CD  . LYS   A 1 330 ? -13.217 10.762  41.270 1.00 95.25  ? 626 LYS   A CD  1 
ATOM   2589 C  CE  . LYS   A 1 330 ? -11.697 10.755  41.407 1.00 96.96  ? 626 LYS   A CE  1 
ATOM   2590 N  NZ  . LYS   A 1 330 ? -11.144 9.372   41.499 1.00 95.00  ? 626 LYS   A NZ  1 
ATOM   2591 N  N   . ASP   A 1 331 ? -18.293 12.967  41.858 1.00 92.69  ? 627 ASP   A N   1 
ATOM   2592 C  CA  . ASP   A 1 331 ? -19.708 12.708  41.617 1.00 89.58  ? 627 ASP   A CA  1 
ATOM   2593 C  C   . ASP   A 1 331 ? -20.372 13.893  40.944 1.00 87.53  ? 627 ASP   A C   1 
ATOM   2594 O  O   . ASP   A 1 331 ? -21.122 13.735  39.972 1.00 87.14  ? 627 ASP   A O   1 
ATOM   2595 C  CB  . ASP   A 1 331 ? -20.416 12.405  42.936 1.00 93.53  ? 627 ASP   A CB  1 
ATOM   2596 C  CG  . ASP   A 1 331 ? -19.752 11.290  43.712 1.00 93.78  ? 627 ASP   A CG  1 
ATOM   2597 O  OD1 . ASP   A 1 331 ? -18.599 11.470  44.157 1.00 90.24  ? 627 ASP   A OD1 1 
ATOM   2598 O  OD2 . ASP   A 1 331 ? -20.390 10.234  43.877 1.00 92.22  ? 627 ASP   A OD2 1 
ATOM   2599 N  N   . GLN   A 1 332 ? -20.109 15.094  41.461 1.00 89.98  ? 628 GLN   A N   1 
ATOM   2600 C  CA  . GLN   A 1 332 ? -20.752 16.294  40.940 1.00 103.73 ? 628 GLN   A CA  1 
ATOM   2601 C  C   . GLN   A 1 332 ? -20.348 16.572  39.496 1.00 99.07  ? 628 GLN   A C   1 
ATOM   2602 O  O   . GLN   A 1 332 ? -21.194 16.939  38.668 1.00 95.05  ? 628 GLN   A O   1 
ATOM   2603 C  CB  . GLN   A 1 332 ? -20.414 17.481  41.836 1.00 119.16 ? 628 GLN   A CB  1 
ATOM   2604 C  CG  . GLN   A 1 332 ? -21.591 18.379  42.114 1.00 123.90 ? 628 GLN   A CG  1 
ATOM   2605 C  CD  . GLN   A 1 332 ? -21.316 19.348  43.237 1.00 126.79 ? 628 GLN   A CD  1 
ATOM   2606 O  OE1 . GLN   A 1 332 ? -20.213 19.389  43.786 1.00 129.03 ? 628 GLN   A OE1 1 
ATOM   2607 N  NE2 . GLN   A 1 332 ? -22.319 20.134  43.592 1.00 129.91 ? 628 GLN   A NE2 1 
ATOM   2608 N  N   . ALA   A 1 333 ? -19.060 16.433  39.176 1.00 95.62  ? 629 ALA   A N   1 
ATOM   2609 C  CA  . ALA   A 1 333 ? -18.643 16.618  37.794 1.00 102.26 ? 629 ALA   A CA  1 
ATOM   2610 C  C   . ALA   A 1 333 ? -19.181 15.501  36.910 1.00 99.13  ? 629 ALA   A C   1 
ATOM   2611 O  O   . ALA   A 1 333 ? -19.411 15.708  35.710 1.00 95.21  ? 629 ALA   A O   1 
ATOM   2612 C  CB  . ALA   A 1 333 ? -17.117 16.700  37.712 1.00 102.02 ? 629 ALA   A CB  1 
ATOM   2613 N  N   . LEU   A 1 334 ? -19.427 14.323  37.490 1.00 89.58  ? 630 LEU   A N   1 
ATOM   2614 C  CA  . LEU   A 1 334 ? -19.936 13.216  36.688 1.00 84.32  ? 630 LEU   A CA  1 
ATOM   2615 C  C   . LEU   A 1 334 ? -21.358 13.490  36.209 1.00 87.44  ? 630 LEU   A C   1 
ATOM   2616 O  O   . LEU   A 1 334 ? -21.713 13.139  35.075 1.00 91.62  ? 630 LEU   A O   1 
ATOM   2617 C  CB  . LEU   A 1 334 ? -19.874 11.910  37.481 1.00 84.78  ? 630 LEU   A CB  1 
ATOM   2618 C  CG  . LEU   A 1 334 ? -20.389 10.659  36.755 1.00 78.51  ? 630 LEU   A CG  1 
ATOM   2619 C  CD1 . LEU   A 1 334 ? -19.368 10.092  35.791 1.00 72.41  ? 630 LEU   A CD1 1 
ATOM   2620 C  CD2 . LEU   A 1 334 ? -20.777 9.615   37.777 1.00 74.73  ? 630 LEU   A CD2 1 
ATOM   2621 N  N   . VAL   A 1 335 ? -22.181 14.120  37.053 1.00 85.82  ? 631 VAL   A N   1 
ATOM   2622 C  CA  . VAL   A 1 335 ? -23.567 14.415  36.687 1.00 88.63  ? 631 VAL   A CA  1 
ATOM   2623 C  C   . VAL   A 1 335 ? -23.626 15.456  35.569 1.00 92.12  ? 631 VAL   A C   1 
ATOM   2624 O  O   . VAL   A 1 335 ? -24.318 15.258  34.554 1.00 89.25  ? 631 VAL   A O   1 
ATOM   2625 C  CB  . VAL   A 1 335 ? -24.372 14.865  37.921 1.00 99.83  ? 631 VAL   A CB  1 
ATOM   2626 C  CG1 . VAL   A 1 335 ? -25.725 15.400  37.483 1.00 109.47 ? 631 VAL   A CG1 1 
ATOM   2627 C  CG2 . VAL   A 1 335 ? -24.557 13.702  38.885 1.00 97.08  ? 631 VAL   A CG2 1 
ATOM   2628 N  N   . GLU   A 1 336 ? -22.907 16.578  35.726 1.00 94.96  ? 632 GLU   A N   1 
ATOM   2629 C  CA  . GLU   A 1 336 ? -22.892 17.591  34.659 1.00 104.76 ? 632 GLU   A CA  1 
ATOM   2630 C  C   . GLU   A 1 336 ? -22.486 16.996  33.318 1.00 96.93  ? 632 GLU   A C   1 
ATOM   2631 O  O   . GLU   A 1 336 ? -23.029 17.371  32.266 1.00 98.19  ? 632 GLU   A O   1 
ATOM   2632 C  CB  . GLU   A 1 336 ? -21.935 18.731  34.999 1.00 115.57 ? 632 GLU   A CB  1 
ATOM   2633 C  CG  . GLU   A 1 336 ? -22.020 19.204  36.412 1.00 121.22 ? 632 GLU   A CG  1 
ATOM   2634 C  CD  . GLU   A 1 336 ? -23.269 19.996  36.681 1.00 130.37 ? 632 GLU   A CD  1 
ATOM   2635 O  OE1 . GLU   A 1 336 ? -23.901 20.466  35.702 1.00 131.57 ? 632 GLU   A OE1 1 
ATOM   2636 O  OE2 . GLU   A 1 336 ? -23.616 20.143  37.875 1.00 132.07 ? 632 GLU   A OE2 1 
ATOM   2637 N  N   . ILE   A 1 337 ? -21.506 16.088  33.331 1.00 92.63  ? 633 ILE   A N   1 
ATOM   2638 C  CA  . ILE   A 1 337 ? -21.015 15.498  32.088 1.00 94.18  ? 633 ILE   A CA  1 
ATOM   2639 C  C   . ILE   A 1 337 ? -22.116 14.723  31.384 1.00 98.74  ? 633 ILE   A C   1 
ATOM   2640 O  O   . ILE   A 1 337 ? -22.194 14.724  30.149 1.00 105.21 ? 633 ILE   A O   1 
ATOM   2641 C  CB  . ILE   A 1 337 ? -19.781 14.615  32.372 1.00 83.66  ? 633 ILE   A CB  1 
ATOM   2642 C  CG1 . ILE   A 1 337 ? -18.571 15.490  32.682 1.00 90.56  ? 633 ILE   A CG1 1 
ATOM   2643 C  CG2 . ILE   A 1 337 ? -19.445 13.708  31.186 1.00 80.50  ? 633 ILE   A CG2 1 
ATOM   2644 C  CD1 . ILE   A 1 337 ? -17.398 14.690  33.225 1.00 95.30  ? 633 ILE   A CD1 1 
ATOM   2645 N  N   . ASN   A 1 338 ? -22.996 14.077  32.144 1.00 97.62  ? 634 ASN   A N   1 
ATOM   2646 C  CA  . ASN   A 1 338 ? -24.065 13.277  31.560 1.00 87.23  ? 634 ASN   A CA  1 
ATOM   2647 C  C   . ASN   A 1 338 ? -25.298 14.098  31.185 1.00 88.51  ? 634 ASN   A C   1 
ATOM   2648 O  O   . ASN   A 1 338 ? -26.006 13.723  30.242 1.00 88.57  ? 634 ASN   A O   1 
ATOM   2649 C  CB  . ASN   A 1 338 ? -24.443 12.140  32.516 1.00 82.67  ? 634 ASN   A CB  1 
ATOM   2650 C  CG  . ASN   A 1 338 ? -23.409 11.031  32.525 1.00 79.33  ? 634 ASN   A CG  1 
ATOM   2651 O  OD1 . ASN   A 1 338 ? -23.494 10.079  31.755 1.00 83.16  ? 634 ASN   A OD1 1 
ATOM   2652 N  ND2 . ASN   A 1 338 ? -22.409 11.167  33.374 1.00 73.17  ? 634 ASN   A ND2 1 
ATOM   2653 N  N   . ILE   A 1 339 ? -25.577 15.207  31.888 1.00 85.06  ? 635 ILE   A N   1 
ATOM   2654 C  CA  . ILE   A 1 339 ? -26.581 16.149  31.395 1.00 87.64  ? 635 ILE   A CA  1 
ATOM   2655 C  C   . ILE   A 1 339 ? -26.131 16.710  30.056 1.00 91.79  ? 635 ILE   A C   1 
ATOM   2656 O  O   . ILE   A 1 339 ? -26.957 17.005  29.182 1.00 93.41  ? 635 ILE   A O   1 
ATOM   2657 C  CB  . ILE   A 1 339 ? -26.842 17.299  32.394 1.00 97.01  ? 635 ILE   A CB  1 
ATOM   2658 C  CG1 . ILE   A 1 339 ? -27.373 16.784  33.728 1.00 92.08  ? 635 ILE   A CG1 1 
ATOM   2659 C  CG2 . ILE   A 1 339 ? -27.855 18.308  31.823 1.00 96.47  ? 635 ILE   A CG2 1 
ATOM   2660 C  CD1 . ILE   A 1 339 ? -27.626 17.883  34.718 1.00 105.26 ? 635 ILE   A CD1 1 
ATOM   2661 N  N   . ALA   A 1 340 ? -24.814 16.835  29.870 1.00 91.24  ? 636 ALA   A N   1 
ATOM   2662 C  CA  . ALA   A 1 340 ? -24.250 17.422  28.661 1.00 101.71 ? 636 ALA   A CA  1 
ATOM   2663 C  C   . ALA   A 1 340 ? -24.290 16.443  27.490 1.00 97.92  ? 636 ALA   A C   1 
ATOM   2664 O  O   . ALA   A 1 340 ? -24.642 16.814  26.361 1.00 90.04  ? 636 ALA   A O   1 
ATOM   2665 C  CB  . ALA   A 1 340 ? -22.818 17.872  28.946 1.00 107.36 ? 636 ALA   A CB  1 
ATOM   2666 N  N   . VAL   A 1 341 ? -23.903 15.189  27.730 1.00 93.17  ? 637 VAL   A N   1 
ATOM   2667 C  CA  . VAL   A 1 341 ? -24.004 14.191  26.675 1.00 83.57  ? 637 VAL   A CA  1 
ATOM   2668 C  C   . VAL   A 1 341 ? -25.442 14.110  26.185 1.00 90.90  ? 637 VAL   A C   1 
ATOM   2669 O  O   . VAL   A 1 341 ? -25.718 14.224  24.984 1.00 92.43  ? 637 VAL   A O   1 
ATOM   2670 C  CB  . VAL   A 1 341 ? -23.497 12.824  27.168 1.00 85.00  ? 637 VAL   A CB  1 
ATOM   2671 C  CG1 . VAL   A 1 341 ? -23.712 11.779  26.095 1.00 80.61  ? 637 VAL   A CG1 1 
ATOM   2672 C  CG2 . VAL   A 1 341 ? -22.031 12.900  27.526 1.00 91.10  ? 637 VAL   A CG2 1 
ATOM   2673 N  N   . LEU   A 1 342 ? -26.381 13.974  27.124 1.00 85.68  ? 638 LEU   A N   1 
ATOM   2674 C  CA  . LEU   A 1 342 ? -27.797 13.890  26.778 1.00 83.54  ? 638 LEU   A CA  1 
ATOM   2675 C  C   . LEU   A 1 342 ? -28.247 15.108  25.984 1.00 87.82  ? 638 LEU   A C   1 
ATOM   2676 O  O   . LEU   A 1 342 ? -28.788 14.982  24.879 1.00 89.96  ? 638 LEU   A O   1 
ATOM   2677 C  CB  . LEU   A 1 342 ? -28.627 13.760  28.053 1.00 92.22  ? 638 LEU   A CB  1 
ATOM   2678 C  CG  . LEU   A 1 342 ? -28.486 12.445  28.800 1.00 82.66  ? 638 LEU   A CG  1 
ATOM   2679 C  CD1 . LEU   A 1 342 ? -29.553 12.385  29.862 1.00 81.13  ? 638 LEU   A CD1 1 
ATOM   2680 C  CD2 . LEU   A 1 342 ? -28.612 11.315  27.792 1.00 78.06  ? 638 LEU   A CD2 1 
ATOM   2681 N  N   . TYR   A 1 343 ? -28.053 16.303  26.557 1.00 92.68  ? 639 TYR   A N   1 
ATOM   2682 C  CA  . TYR   A 1 343 ? -28.529 17.531  25.922 1.00 102.86 ? 639 TYR   A CA  1 
ATOM   2683 C  C   . TYR   A 1 343 ? -27.940 17.700  24.531 1.00 103.22 ? 639 TYR   A C   1 
ATOM   2684 O  O   . TYR   A 1 343 ? -28.631 18.132  23.598 1.00 102.57 ? 639 TYR   A O   1 
ATOM   2685 C  CB  . TYR   A 1 343 ? -28.186 18.742  26.797 1.00 108.59 ? 639 TYR   A CB  1 
ATOM   2686 C  CG  . TYR   A 1 343 ? -28.438 20.085  26.127 1.00 115.90 ? 639 TYR   A CG  1 
ATOM   2687 C  CD1 . TYR   A 1 343 ? -29.707 20.647  26.120 1.00 116.49 ? 639 TYR   A CD1 1 
ATOM   2688 C  CD2 . TYR   A 1 343 ? -27.408 20.789  25.514 1.00 112.29 ? 639 TYR   A CD2 1 
ATOM   2689 C  CE1 . TYR   A 1 343 ? -29.949 21.860  25.520 1.00 119.59 ? 639 TYR   A CE1 1 
ATOM   2690 C  CE2 . TYR   A 1 343 ? -27.641 22.016  24.907 1.00 116.30 ? 639 TYR   A CE2 1 
ATOM   2691 C  CZ  . TYR   A 1 343 ? -28.915 22.545  24.913 1.00 119.66 ? 639 TYR   A CZ  1 
ATOM   2692 O  OH  . TYR   A 1 343 ? -29.162 23.763  24.320 1.00 125.17 ? 639 TYR   A OH  1 
ATOM   2693 N  N   . SER   A 1 344 ? -26.658 17.372  24.373 1.00 97.88  ? 640 SER   A N   1 
ATOM   2694 C  CA  . SER   A 1 344 ? -26.011 17.527  23.072 1.00 97.54  ? 640 SER   A CA  1 
ATOM   2695 C  C   . SER   A 1 344 ? -26.665 16.635  22.026 1.00 94.31  ? 640 SER   A C   1 
ATOM   2696 O  O   . SER   A 1 344 ? -26.966 17.083  20.912 1.00 90.58  ? 640 SER   A O   1 
ATOM   2697 C  CB  . SER   A 1 344 ? -24.522 17.212  23.197 1.00 89.81  ? 640 SER   A CB  1 
ATOM   2698 O  OG  . SER   A 1 344 ? -23.906 18.125  24.093 1.00 105.33 ? 640 SER   A OG  1 
ATOM   2699 N  N   . PHE   A 1 345 ? -26.892 15.363  22.372 1.00 98.49  ? 641 PHE   A N   1 
ATOM   2700 C  CA  . PHE   A 1 345 ? -27.539 14.434  21.448 1.00 91.63  ? 641 PHE   A CA  1 
ATOM   2701 C  C   . PHE   A 1 345 ? -28.971 14.872  21.138 1.00 95.51  ? 641 PHE   A C   1 
ATOM   2702 O  O   . PHE   A 1 345 ? -29.385 14.892  19.975 1.00 93.75  ? 641 PHE   A O   1 
ATOM   2703 C  CB  . PHE   A 1 345 ? -27.534 13.016  22.029 1.00 86.79  ? 641 PHE   A CB  1 
ATOM   2704 C  CG  . PHE   A 1 345 ? -26.277 12.199  21.739 1.00 76.29  ? 641 PHE   A CG  1 
ATOM   2705 C  CD1 . PHE   A 1 345 ? -25.033 12.586  22.223 1.00 80.41  ? 641 PHE   A CD1 1 
ATOM   2706 C  CD2 . PHE   A 1 345 ? -26.367 10.996  21.031 1.00 71.11  ? 641 PHE   A CD2 1 
ATOM   2707 C  CE1 . PHE   A 1 345 ? -23.896 11.808  21.990 1.00 76.21  ? 641 PHE   A CE1 1 
ATOM   2708 C  CE2 . PHE   A 1 345 ? -25.237 10.194  20.804 1.00 64.16  ? 641 PHE   A CE2 1 
ATOM   2709 C  CZ  . PHE   A 1 345 ? -24.000 10.613  21.270 1.00 73.93  ? 641 PHE   A CZ  1 
ATOM   2710 N  N   . GLN   A 1 346 ? -29.749 15.223  22.171 1.00 95.74  ? 642 GLN   A N   1 
ATOM   2711 C  CA  . GLN   A 1 346 ? -31.149 15.582  21.950 1.00 87.99  ? 642 GLN   A CA  1 
ATOM   2712 C  C   . GLN   A 1 346 ? -31.271 16.814  21.066 1.00 91.54  ? 642 GLN   A C   1 
ATOM   2713 O  O   . GLN   A 1 346 ? -32.082 16.843  20.137 1.00 94.14  ? 642 GLN   A O   1 
ATOM   2714 C  CB  . GLN   A 1 346 ? -31.861 15.840  23.269 1.00 94.31  ? 642 GLN   A CB  1 
ATOM   2715 C  CG  . GLN   A 1 346 ? -32.045 14.628  24.126 1.00 100.51 ? 642 GLN   A CG  1 
ATOM   2716 C  CD  . GLN   A 1 346 ? -32.251 15.035  25.553 1.00 110.11 ? 642 GLN   A CD  1 
ATOM   2717 O  OE1 . GLN   A 1 346 ? -31.292 15.301  26.267 1.00 119.88 ? 642 GLN   A OE1 1 
ATOM   2718 N  NE2 . GLN   A 1 346 ? -33.506 15.136  25.968 1.00 113.40 ? 642 GLN   A NE2 1 
ATOM   2719 N  N   . SER   A 1 347 ? -30.490 17.858  21.362 1.00 96.11  ? 643 SER   A N   1 
ATOM   2720 C  CA  . SER   A 1 347 ? -30.568 19.081  20.567 1.00 105.74 ? 643 SER   A CA  1 
ATOM   2721 C  C   . SER   A 1 347 ? -30.132 18.857  19.117 1.00 111.08 ? 643 SER   A C   1 
ATOM   2722 O  O   . SER   A 1 347 ? -30.409 19.707  18.261 1.00 104.38 ? 643 SER   A O   1 
ATOM   2723 C  CB  . SER   A 1 347 ? -29.730 20.194  21.226 1.00 105.69 ? 643 SER   A CB  1 
ATOM   2724 O  OG  . SER   A 1 347 ? -30.062 20.419  22.612 1.00 106.96 ? 643 SER   A OG  1 
ATOM   2725 N  N   . ASP   A 1 348 ? -29.490 17.728  18.813 1.00 107.18 ? 644 ASP   A N   1 
ATOM   2726 C  CA  . ASP   A 1 348 ? -29.075 17.397  17.454 1.00 109.85 ? 644 ASP   A CA  1 
ATOM   2727 C  C   . ASP   A 1 348 ? -29.969 16.357  16.790 1.00 105.00 ? 644 ASP   A C   1 
ATOM   2728 O  O   . ASP   A 1 348 ? -29.653 15.912  15.681 1.00 89.96  ? 644 ASP   A O   1 
ATOM   2729 C  CB  . ASP   A 1 348 ? -27.631 16.891  17.442 1.00 104.46 ? 644 ASP   A CB  1 
ATOM   2730 C  CG  . ASP   A 1 348 ? -26.613 17.995  17.666 1.00 110.50 ? 644 ASP   A CG  1 
ATOM   2731 O  OD1 . ASP   A 1 348 ? -27.003 19.180  17.798 1.00 115.00 ? 644 ASP   A OD1 1 
ATOM   2732 O  OD2 . ASP   A 1 348 ? -25.408 17.664  17.706 1.00 104.27 ? 644 ASP   A OD2 1 
ATOM   2733 N  N   . LYS   A 1 349 ? -31.059 15.944  17.441 1.00 113.76 ? 645 LYS   A N   1 
ATOM   2734 C  CA  . LYS   A 1 349 ? -31.954 14.903  16.933 1.00 119.19 ? 645 LYS   A CA  1 
ATOM   2735 C  C   . LYS   A 1 349 ? -31.239 13.565  16.758 1.00 111.70 ? 645 LYS   A C   1 
ATOM   2736 O  O   . LYS   A 1 349 ? -31.680 12.723  15.969 1.00 103.81 ? 645 LYS   A O   1 
ATOM   2737 C  CB  . LYS   A 1 349 ? -32.611 15.319  15.608 1.00 130.48 ? 645 LYS   A CB  1 
ATOM   2738 C  CG  . LYS   A 1 349 ? -34.136 15.301  15.600 1.00 137.32 ? 645 LYS   A CG  1 
ATOM   2739 C  CD  . LYS   A 1 349 ? -34.707 16.452  16.411 1.00 143.58 ? 645 LYS   A CD  1 
ATOM   2740 C  CE  . LYS   A 1 349 ? -36.209 16.602  16.205 1.00 148.49 ? 645 LYS   A CE  1 
ATOM   2741 N  NZ  . LYS   A 1 349 ? -36.983 15.427  16.694 1.00 146.17 ? 645 LYS   A NZ  1 
ATOM   2742 N  N   . VAL   A 1 350 ? -30.132 13.354  17.469 1.00 106.23 ? 646 VAL   A N   1 
ATOM   2743 C  CA  . VAL   A 1 350 ? -29.455 12.061  17.488 1.00 89.85  ? 646 VAL   A CA  1 
ATOM   2744 C  C   . VAL   A 1 350 ? -30.027 11.248  18.643 1.00 87.55  ? 646 VAL   A C   1 
ATOM   2745 O  O   . VAL   A 1 350 ? -29.967 11.675  19.804 1.00 87.86  ? 646 VAL   A O   1 
ATOM   2746 C  CB  . VAL   A 1 350 ? -27.934 12.212  17.638 1.00 82.60  ? 646 VAL   A CB  1 
ATOM   2747 C  CG1 . VAL   A 1 350 ? -27.240 10.819  17.582 1.00 71.15  ? 646 VAL   A CG1 1 
ATOM   2748 C  CG2 . VAL   A 1 350 ? -27.380 13.152  16.620 1.00 79.67  ? 646 VAL   A CG2 1 
ATOM   2749 N  N   . THR   A 1 351 ? -30.574 10.082  18.313 1.00 85.75  ? 647 THR   A N   1 
ATOM   2750 C  CA  . THR   A 1 351 ? -31.229 9.226   19.286 1.00 79.64  ? 647 THR   A CA  1 
ATOM   2751 C  C   . THR   A 1 351 ? -30.279 8.915   20.422 1.00 81.54  ? 647 THR   A C   1 
ATOM   2752 O  O   . THR   A 1 351 ? -29.120 8.556   20.188 1.00 78.15  ? 647 THR   A O   1 
ATOM   2753 C  CB  . THR   A 1 351 ? -31.683 7.929   18.608 1.00 80.14  ? 647 THR   A CB  1 
ATOM   2754 O  OG1 . THR   A 1 351 ? -32.524 8.243   17.496 1.00 81.30  ? 647 THR   A OG1 1 
ATOM   2755 C  CG2 . THR   A 1 351 ? -32.439 7.041   19.596 1.00 67.86  ? 647 THR   A CG2 1 
ATOM   2756 N  N   . ILE   A 1 352 ? -30.774 9.104   21.648 1.00 76.20  ? 648 ILE   A N   1 
ATOM   2757 C  CA  . ILE   A 1 352 ? -30.075 8.738   22.868 1.00 71.28  ? 648 ILE   A CA  1 
ATOM   2758 C  C   . ILE   A 1 352 ? -31.142 8.537   23.934 1.00 74.21  ? 648 ILE   A C   1 
ATOM   2759 O  O   . ILE   A 1 352 ? -32.222 9.127   23.869 1.00 80.29  ? 648 ILE   A O   1 
ATOM   2760 C  CB  . ILE   A 1 352 ? -29.043 9.817   23.283 1.00 74.99  ? 648 ILE   A CB  1 
ATOM   2761 C  CG1 . ILE   A 1 352 ? -28.048 9.235   24.295 1.00 72.33  ? 648 ILE   A CG1 1 
ATOM   2762 C  CG2 . ILE   A 1 352 ? -29.750 11.025  23.896 1.00 75.62  ? 648 ILE   A CG2 1 
ATOM   2763 C  CD1 . ILE   A 1 352 ? -26.827 10.093  24.490 1.00 83.21  ? 648 ILE   A CD1 1 
ATOM   2764 N  N   . VAL   A 1 353 ? -30.853 7.687   24.907 1.00 71.66  ? 649 VAL   A N   1 
ATOM   2765 C  CA  . VAL   A 1 353 ? -31.793 7.422   25.985 1.00 72.08  ? 649 VAL   A CA  1 
ATOM   2766 C  C   . VAL   A 1 353 ? -31.076 7.661   27.308 1.00 71.73  ? 649 VAL   A C   1 
ATOM   2767 O  O   . VAL   A 1 353 ? -29.891 7.340   27.447 1.00 72.88  ? 649 VAL   A O   1 
ATOM   2768 C  CB  . VAL   A 1 353 ? -32.373 5.993   25.880 1.00 70.41  ? 649 VAL   A CB  1 
ATOM   2769 C  CG1 . VAL   A 1 353 ? -31.267 4.950   25.872 1.00 64.25  ? 649 VAL   A CG1 1 
ATOM   2770 C  CG2 . VAL   A 1 353 ? -33.406 5.727   26.973 1.00 76.84  ? 649 VAL   A CG2 1 
ATOM   2771 N  N   . ASP   A 1 354 ? -31.769 8.280   28.257 1.00 78.93  ? 650 ASP   A N   1 
ATOM   2772 C  CA  . ASP   A 1 354 ? -31.154 8.495   29.552 1.00 72.23  ? 650 ASP   A CA  1 
ATOM   2773 C  C   . ASP   A 1 354 ? -31.331 7.236   30.398 1.00 71.52  ? 650 ASP   A C   1 
ATOM   2774 O  O   . ASP   A 1 354 ? -32.147 6.359   30.089 1.00 69.44  ? 650 ASP   A O   1 
ATOM   2775 C  CB  . ASP   A 1 354 ? -31.726 9.736   30.247 1.00 81.52  ? 650 ASP   A CB  1 
ATOM   2776 C  CG  . ASP   A 1 354 ? -33.163 9.564   30.706 1.00 86.78  ? 650 ASP   A CG  1 
ATOM   2777 O  OD1 . ASP   A 1 354 ? -34.058 10.259  30.192 1.00 93.04  ? 650 ASP   A OD1 1 
ATOM   2778 O  OD2 . ASP   A 1 354 ? -33.402 8.743   31.605 1.00 86.48  ? 650 ASP   A OD2 1 
ATOM   2779 N  N   . HIS   A 1 355 ? -30.513 7.114   31.442 1.00 69.06  ? 651 HIS   A N   1 
ATOM   2780 C  CA  . HIS   A 1 355 ? -30.533 5.870   32.207 1.00 65.49  ? 651 HIS   A CA  1 
ATOM   2781 C  C   . HIS   A 1 355 ? -31.832 5.682   32.982 1.00 72.72  ? 651 HIS   A C   1 
ATOM   2782 O  O   . HIS   A 1 355 ? -32.156 4.549   33.355 1.00 78.92  ? 651 HIS   A O   1 
ATOM   2783 C  CB  . HIS   A 1 355 ? -29.324 5.786   33.156 1.00 70.51  ? 651 HIS   A CB  1 
ATOM   2784 C  CG  . HIS   A 1 355 ? -29.025 7.053   33.905 1.00 70.70  ? 651 HIS   A CG  1 
ATOM   2785 N  ND1 . HIS   A 1 355 ? -28.486 8.168   33.298 1.00 67.80  ? 651 HIS   A ND1 1 
ATOM   2786 C  CD2 . HIS   A 1 355 ? -29.121 7.355   35.223 1.00 77.13  ? 651 HIS   A CD2 1 
ATOM   2787 C  CE1 . HIS   A 1 355 ? -28.294 9.114   34.203 1.00 80.84  ? 651 HIS   A CE1 1 
ATOM   2788 N  NE2 . HIS   A 1 355 ? -28.679 8.650   35.380 1.00 77.38  ? 651 HIS   A NE2 1 
ATOM   2789 N  N   . HIS   A 1 356 ? -32.577 6.760   33.237 1.00 73.23  ? 652 HIS   A N   1 
ATOM   2790 C  CA  . HIS   A 1 356 ? -33.870 6.631   33.899 1.00 71.17  ? 652 HIS   A CA  1 
ATOM   2791 C  C   . HIS   A 1 356 ? -34.917 6.077   32.943 1.00 74.17  ? 652 HIS   A C   1 
ATOM   2792 O  O   . HIS   A 1 356 ? -35.618 5.107   33.262 1.00 71.34  ? 652 HIS   A O   1 
ATOM   2793 C  CB  . HIS   A 1 356 ? -34.293 7.982   34.460 1.00 76.55  ? 652 HIS   A CB  1 
ATOM   2794 C  CG  . HIS   A 1 356 ? -33.265 8.592   35.351 1.00 83.15  ? 652 HIS   A CG  1 
ATOM   2795 N  ND1 . HIS   A 1 356 ? -33.120 8.227   36.675 1.00 79.96  ? 652 HIS   A ND1 1 
ATOM   2796 C  CD2 . HIS   A 1 356 ? -32.306 9.513   35.105 1.00 83.08  ? 652 HIS   A CD2 1 
ATOM   2797 C  CE1 . HIS   A 1 356 ? -32.126 8.913   37.209 1.00 84.06  ? 652 HIS   A CE1 1 
ATOM   2798 N  NE2 . HIS   A 1 356 ? -31.616 9.701   36.278 1.00 86.74  ? 652 HIS   A NE2 1 
ATOM   2799 N  N   . SER   A 1 357 ? -35.024 6.668   31.751 1.00 80.05  ? 653 SER   A N   1 
ATOM   2800 C  CA  . SER   A 1 357 ? -35.967 6.144   30.776 1.00 83.16  ? 653 SER   A CA  1 
ATOM   2801 C  C   . SER   A 1 357 ? -35.583 4.736   30.349 1.00 69.78  ? 653 SER   A C   1 
ATOM   2802 O  O   . SER   A 1 357 ? -36.447 3.861   30.240 1.00 72.89  ? 653 SER   A O   1 
ATOM   2803 C  CB  . SER   A 1 357 ? -36.047 7.067   29.563 1.00 86.96  ? 653 SER   A CB  1 
ATOM   2804 O  OG  . SER   A 1 357 ? -37.299 6.904   28.933 1.00 94.49  ? 653 SER   A OG  1 
ATOM   2805 N  N   . ALA   A 1 358 ? -34.286 4.485   30.138 1.00 67.23  ? 654 ALA   A N   1 
ATOM   2806 C  CA  . ALA   A 1 358 ? -33.862 3.168   29.666 1.00 66.56  ? 654 ALA   A CA  1 
ATOM   2807 C  C   . ALA   A 1 358 ? -34.129 2.097   30.714 1.00 65.66  ? 654 ALA   A C   1 
ATOM   2808 O  O   . ALA   A 1 358 ? -34.569 0.987   30.386 1.00 59.58  ? 654 ALA   A O   1 
ATOM   2809 C  CB  . ALA   A 1 358 ? -32.379 3.183   29.298 1.00 60.49  ? 654 ALA   A CB  1 
ATOM   2810 N  N   . THR   A 1 359 ? -33.854 2.400   31.984 1.00 63.40  ? 655 THR   A N   1 
ATOM   2811 C  CA  . THR   A 1 359 ? -34.106 1.388   32.996 1.00 59.40  ? 655 THR   A CA  1 
ATOM   2812 C  C   . THR   A 1 359 ? -35.585 1.280   33.318 1.00 61.22  ? 655 THR   A C   1 
ATOM   2813 O  O   . THR   A 1 359 ? -36.055 0.188   33.657 1.00 64.82  ? 655 THR   A O   1 
ATOM   2814 C  CB  . THR   A 1 359 ? -33.285 1.663   34.240 1.00 56.42  ? 655 THR   A CB  1 
ATOM   2815 O  OG1 . THR   A 1 359 ? -33.594 2.969   34.752 1.00 64.89  ? 655 THR   A OG1 1 
ATOM   2816 C  CG2 . THR   A 1 359 ? -31.820 1.587   33.898 1.00 56.70  ? 655 THR   A CG2 1 
ATOM   2817 N  N   . GLU   A 1 360 ? -36.348 2.367   33.165 1.00 64.91  ? 656 GLU   A N   1 
ATOM   2818 C  CA  . GLU   A 1 360 ? -37.790 2.222   33.334 1.00 75.31  ? 656 GLU   A CA  1 
ATOM   2819 C  C   . GLU   A 1 360 ? -38.358 1.279   32.287 1.00 74.80  ? 656 GLU   A C   1 
ATOM   2820 O  O   . GLU   A 1 360 ? -39.177 0.409   32.604 1.00 73.78  ? 656 GLU   A O   1 
ATOM   2821 C  CB  . GLU   A 1 360 ? -38.510 3.563   33.259 1.00 79.50  ? 656 GLU   A CB  1 
ATOM   2822 C  CG  . GLU   A 1 360 ? -40.008 3.404   33.517 1.00 92.90  ? 656 GLU   A CG  1 
ATOM   2823 C  CD  . GLU   A 1 360 ? -40.816 4.632   33.164 1.00 108.37 ? 656 GLU   A CD  1 
ATOM   2824 O  OE1 . GLU   A 1 360 ? -42.065 4.555   33.205 1.00 115.62 ? 656 GLU   A OE1 1 
ATOM   2825 O  OE2 . GLU   A 1 360 ? -40.205 5.670   32.836 1.00 112.64 ? 656 GLU   A OE2 1 
ATOM   2826 N  N   . SER   A 1 361 ? -37.920 1.433   31.036 1.00 75.19  ? 657 SER   A N   1 
ATOM   2827 C  CA  A SER   A 1 361 ? -38.435 0.589   29.967 0.47 73.14  ? 657 SER   A CA  1 
ATOM   2828 C  CA  B SER   A 1 361 ? -38.426 0.588   29.958 0.53 73.22  ? 657 SER   A CA  1 
ATOM   2829 C  C   . SER   A 1 361 ? -38.029 -0.864  30.170 1.00 70.72  ? 657 SER   A C   1 
ATOM   2830 O  O   . SER   A 1 361 ? -38.803 -1.782  29.869 1.00 71.82  ? 657 SER   A O   1 
ATOM   2831 C  CB  A SER   A 1 361 ? -37.946 1.112   28.618 0.47 70.19  ? 657 SER   A CB  1 
ATOM   2832 C  CB  B SER   A 1 361 ? -37.910 1.089   28.606 0.53 70.07  ? 657 SER   A CB  1 
ATOM   2833 O  OG  A SER   A 1 361 ? -38.245 2.491   28.486 0.47 67.80  ? 657 SER   A OG  1 
ATOM   2834 O  OG  B SER   A 1 361 ? -36.585 0.643   28.350 0.53 66.87  ? 657 SER   A OG  1 
ATOM   2835 N  N   . PHE   A 1 362 ? -36.825 -1.095  30.695 1.00 66.61  ? 658 PHE   A N   1 
ATOM   2836 C  CA  . PHE   A 1 362 ? -36.391 -2.468  30.888 1.00 64.11  ? 658 PHE   A CA  1 
ATOM   2837 C  C   . PHE   A 1 362 ? -37.226 -3.173  31.952 1.00 64.88  ? 658 PHE   A C   1 
ATOM   2838 O  O   . PHE   A 1 362 ? -37.501 -4.370  31.827 1.00 64.65  ? 658 PHE   A O   1 
ATOM   2839 C  CB  . PHE   A 1 362 ? -34.912 -2.530  31.239 1.00 64.48  ? 658 PHE   A CB  1 
ATOM   2840 C  CG  . PHE   A 1 362 ? -34.431 -3.924  31.438 1.00 64.16  ? 658 PHE   A CG  1 
ATOM   2841 C  CD1 . PHE   A 1 362 ? -34.132 -4.721  30.339 1.00 58.94  ? 658 PHE   A CD1 1 
ATOM   2842 C  CD2 . PHE   A 1 362 ? -34.348 -4.470  32.713 1.00 65.48  ? 658 PHE   A CD2 1 
ATOM   2843 C  CE1 . PHE   A 1 362 ? -33.715 -6.020  30.511 1.00 58.47  ? 658 PHE   A CE1 1 
ATOM   2844 C  CE2 . PHE   A 1 362 ? -33.931 -5.771  32.892 1.00 61.29  ? 658 PHE   A CE2 1 
ATOM   2845 C  CZ  . PHE   A 1 362 ? -33.612 -6.551  31.790 1.00 61.11  ? 658 PHE   A CZ  1 
ATOM   2846 N  N   . ILE   A 1 363 ? -37.639 -2.459  33.005 1.00 70.12  ? 659 ILE   A N   1 
ATOM   2847 C  CA  . ILE   A 1 363 ? -38.600 -3.039  33.940 1.00 73.76  ? 659 ILE   A CA  1 
ATOM   2848 C  C   . ILE   A 1 363 ? -39.893 -3.385  33.209 1.00 74.00  ? 659 ILE   A C   1 
ATOM   2849 O  O   . ILE   A 1 363 ? -40.432 -4.490  33.349 1.00 74.45  ? 659 ILE   A O   1 
ATOM   2850 C  CB  . ILE   A 1 363 ? -38.861 -2.090  35.127 1.00 72.28  ? 659 ILE   A CB  1 
ATOM   2851 C  CG1 . ILE   A 1 363 ? -37.591 -1.879  35.957 1.00 62.20  ? 659 ILE   A CG1 1 
ATOM   2852 C  CG2 . ILE   A 1 363 ? -39.991 -2.624  35.992 1.00 83.05  ? 659 ILE   A CG2 1 
ATOM   2853 C  CD1 . ILE   A 1 363 ? -37.190 -3.084  36.792 1.00 63.31  ? 659 ILE   A CD1 1 
ATOM   2854 N  N   . LYS   A 1 364 ? -40.403 -2.447  32.408 1.00 75.74  ? 660 LYS   A N   1 
ATOM   2855 C  CA  . LYS   A 1 364 ? -41.593 -2.732  31.609 1.00 83.24  ? 660 LYS   A CA  1 
ATOM   2856 C  C   . LYS   A 1 364 ? -41.360 -3.919  30.683 1.00 76.57  ? 660 LYS   A C   1 
ATOM   2857 O  O   . LYS   A 1 364 ? -42.210 -4.810  30.575 1.00 81.30  ? 660 LYS   A O   1 
ATOM   2858 C  CB  . LYS   A 1 364 ? -42.014 -1.497  30.806 1.00 79.99  ? 660 LYS   A CB  1 
ATOM   2859 C  CG  . LYS   A 1 364 ? -43.501 -1.473  30.466 1.00 86.60  ? 660 LYS   A CG  1 
ATOM   2860 C  CD  . LYS   A 1 364 ? -43.799 -0.484  29.346 1.00 103.03 ? 660 LYS   A CD  1 
ATOM   2861 C  CE  . LYS   A 1 364 ? -45.019 -0.907  28.532 1.00 107.82 ? 660 LYS   A CE  1 
ATOM   2862 N  NZ  . LYS   A 1 364 ? -44.774 -0.803  27.065 1.00 112.00 ? 660 LYS   A NZ  1 
ATOM   2863 N  N   . HIS   A 1 365 ? -40.204 -3.946  30.004 1.00 71.20  ? 661 HIS   A N   1 
ATOM   2864 C  CA  . HIS   A 1 365 ? -39.860 -5.090  29.161 1.00 71.21  ? 661 HIS   A CA  1 
ATOM   2865 C  C   . HIS   A 1 365 ? -39.797 -6.373  29.971 1.00 70.89  ? 661 HIS   A C   1 
ATOM   2866 O  O   . HIS   A 1 365 ? -40.270 -7.426  29.527 1.00 76.24  ? 661 HIS   A O   1 
ATOM   2867 C  CB  . HIS   A 1 365 ? -38.519 -4.866  28.461 1.00 75.44  ? 661 HIS   A CB  1 
ATOM   2868 C  CG  . HIS   A 1 365 ? -38.011 -6.079  27.736 1.00 77.24  ? 661 HIS   A CG  1 
ATOM   2869 N  ND1 . HIS   A 1 365 ? -36.872 -6.756  28.119 1.00 71.49  ? 661 HIS   A ND1 1 
ATOM   2870 C  CD2 . HIS   A 1 365 ? -38.498 -6.744  26.661 1.00 77.18  ? 661 HIS   A CD2 1 
ATOM   2871 C  CE1 . HIS   A 1 365 ? -36.677 -7.782  27.311 1.00 73.14  ? 661 HIS   A CE1 1 
ATOM   2872 N  NE2 . HIS   A 1 365 ? -37.646 -7.794  26.413 1.00 77.87  ? 661 HIS   A NE2 1 
ATOM   2873 N  N   . MET   A 1 366 ? -39.205 -6.307  31.161 1.00 63.70  ? 662 MET   A N   1 
ATOM   2874 C  CA  . MET   A 1 366 ? -39.164 -7.484  32.013 1.00 60.90  ? 662 MET   A CA  1 
ATOM   2875 C  C   . MET   A 1 366 ? -40.567 -7.990  32.312 1.00 63.65  ? 662 MET   A C   1 
ATOM   2876 O  O   . MET   A 1 366 ? -40.815 -9.200  32.266 1.00 64.19  ? 662 MET   A O   1 
ATOM   2877 C  CB  . MET   A 1 366 ? -38.423 -7.160  33.308 1.00 55.99  ? 662 MET   A CB  1 
ATOM   2878 C  CG  . MET   A 1 366 ? -37.317 -8.130  33.609 1.00 58.58  ? 662 MET   A CG  1 
ATOM   2879 S  SD  . MET   A 1 366 ? -36.525 -7.547  35.101 1.00 67.36  ? 662 MET   A SD  1 
ATOM   2880 C  CE  . MET   A 1 366 ? -35.952 -9.100  35.796 1.00 68.68  ? 662 MET   A CE  1 
ATOM   2881 N  N   . GLU   A 1 367 ? -41.499 -7.075  32.607 1.00 69.19  ? 663 GLU   A N   1 
ATOM   2882 C  CA  . GLU   A 1 367 ? -42.882 -7.467  32.866 1.00 80.81  ? 663 GLU   A CA  1 
ATOM   2883 C  C   . GLU   A 1 367 ? -43.460 -8.239  31.688 1.00 86.24  ? 663 GLU   A C   1 
ATOM   2884 O  O   . GLU   A 1 367 ? -44.082 -9.292  31.865 1.00 90.70  ? 663 GLU   A O   1 
ATOM   2885 C  CB  . GLU   A 1 367 ? -43.743 -6.234  33.152 1.00 91.49  ? 663 GLU   A CB  1 
ATOM   2886 C  CG  . GLU   A 1 367 ? -43.377 -5.435  34.395 1.00 102.29 ? 663 GLU   A CG  1 
ATOM   2887 C  CD  . GLU   A 1 367 ? -44.246 -4.196  34.552 1.00 110.42 ? 663 GLU   A CD  1 
ATOM   2888 O  OE1 . GLU   A 1 367 ? -45.290 -4.102  33.865 1.00 117.43 ? 663 GLU   A OE1 1 
ATOM   2889 O  OE2 . GLU   A 1 367 ? -43.878 -3.311  35.349 1.00 108.67 ? 663 GLU   A OE2 1 
ATOM   2890 N  N   . ASN   A 1 368 ? -43.264 -7.720  30.474 1.00 86.94  ? 664 ASN   A N   1 
ATOM   2891 C  CA  . ASN   A 1 368 ? -43.790 -8.376  29.283 1.00 85.69  ? 664 ASN   A CA  1 
ATOM   2892 C  C   . ASN   A 1 368 ? -43.176 -9.758  29.098 1.00 83.66  ? 664 ASN   A C   1 
ATOM   2893 O  O   . ASN   A 1 368 ? -43.873 -10.711 28.726 1.00 86.98  ? 664 ASN   A O   1 
ATOM   2894 C  CB  . ASN   A 1 368 ? -43.527 -7.503  28.056 1.00 81.74  ? 664 ASN   A CB  1 
ATOM   2895 C  CG  . ASN   A 1 368 ? -44.136 -6.113  28.182 1.00 87.34  ? 664 ASN   A CG  1 
ATOM   2896 O  OD1 . ASN   A 1 368 ? -45.123 -5.919  28.889 1.00 100.22 ? 664 ASN   A OD1 1 
ATOM   2897 N  ND2 . ASN   A 1 368 ? -43.553 -5.141  27.479 1.00 78.66  ? 664 ASN   A ND2 1 
ATOM   2898 N  N   . GLU   A 1 369 ? -41.871 -9.885  29.347 1.00 75.46  ? 665 GLU   A N   1 
ATOM   2899 C  CA  . GLU   A 1 369 ? -41.205 -11.171 29.181 1.00 67.19  ? 665 GLU   A CA  1 
ATOM   2900 C  C   . GLU   A 1 369 ? -41.740 -12.198 30.173 1.00 80.77  ? 665 GLU   A C   1 
ATOM   2901 O  O   . GLU   A 1 369 ? -42.028 -13.339 29.805 1.00 85.17  ? 665 GLU   A O   1 
ATOM   2902 C  CB  . GLU   A 1 369 ? -39.696 -10.998 29.338 1.00 68.42  ? 665 GLU   A CB  1 
ATOM   2903 C  CG  . GLU   A 1 369 ? -39.018 -10.249 28.223 1.00 74.19  ? 665 GLU   A CG  1 
ATOM   2904 C  CD  . GLU   A 1 369 ? -38.603 -11.171 27.093 1.00 77.38  ? 665 GLU   A CD  1 
ATOM   2905 O  OE1 . GLU   A 1 369 ? -37.547 -11.843 27.210 1.00 81.02  ? 665 GLU   A OE1 1 
ATOM   2906 O  OE2 . GLU   A 1 369 ? -39.357 -11.242 26.114 1.00 62.60  ? 665 GLU   A OE2 1 
ATOM   2907 N  N   . TYR   A 1 370 ? -41.890 -11.811 31.444 1.00 85.68  ? 666 TYR   A N   1 
ATOM   2908 C  CA  . TYR   A 1 370 ? -42.416 -12.753 32.426 1.00 87.04  ? 666 TYR   A CA  1 
ATOM   2909 C  C   . TYR   A 1 370 ? -43.853 -13.151 32.113 1.00 94.70  ? 666 TYR   A C   1 
ATOM   2910 O  O   . TYR   A 1 370 ? -44.258 -14.285 32.394 1.00 95.27  ? 666 TYR   A O   1 
ATOM   2911 C  CB  . TYR   A 1 370 ? -42.308 -12.162 33.829 1.00 85.07  ? 666 TYR   A CB  1 
ATOM   2912 C  CG  . TYR   A 1 370 ? -40.940 -12.366 34.429 1.00 77.50  ? 666 TYR   A CG  1 
ATOM   2913 C  CD1 . TYR   A 1 370 ? -39.914 -11.471 34.181 1.00 72.64  ? 666 TYR   A CD1 1 
ATOM   2914 C  CD2 . TYR   A 1 370 ? -40.665 -13.476 35.214 1.00 83.63  ? 666 TYR   A CD2 1 
ATOM   2915 C  CE1 . TYR   A 1 370 ? -38.657 -11.659 34.716 1.00 73.41  ? 666 TYR   A CE1 1 
ATOM   2916 C  CE2 . TYR   A 1 370 ? -39.407 -13.673 35.754 1.00 84.92  ? 666 TYR   A CE2 1 
ATOM   2917 C  CZ  . TYR   A 1 370 ? -38.408 -12.763 35.494 1.00 80.70  ? 666 TYR   A CZ  1 
ATOM   2918 O  OH  . TYR   A 1 370 ? -37.153 -12.954 36.022 1.00 83.51  ? 666 TYR   A OH  1 
ATOM   2919 N  N   . ARG   A 1 371 ? -44.627 -12.252 31.505 1.00 99.90  ? 667 ARG   A N   1 
ATOM   2920 C  CA  . ARG   A 1 371 ? -46.018 -12.566 31.187 1.00 107.96 ? 667 ARG   A CA  1 
ATOM   2921 C  C   . ARG   A 1 371 ? -46.104 -13.481 29.968 1.00 109.92 ? 667 ARG   A C   1 
ATOM   2922 O  O   . ARG   A 1 371 ? -46.516 -14.640 30.076 1.00 112.67 ? 667 ARG   A O   1 
ATOM   2923 C  CB  . ARG   A 1 371 ? -46.810 -11.272 30.974 1.00 116.30 ? 667 ARG   A CB  1 
ATOM   2924 C  CG  . ARG   A 1 371 ? -48.318 -11.465 30.886 1.00 130.25 ? 667 ARG   A CG  1 
ATOM   2925 C  CD  . ARG   A 1 371 ? -49.018 -10.133 30.656 1.00 138.21 ? 667 ARG   A CD  1 
ATOM   2926 N  NE  . ARG   A 1 371 ? -48.269 -9.291  29.727 1.00 140.87 ? 667 ARG   A NE  1 
ATOM   2927 C  CZ  . ARG   A 1 371 ? -48.269 -9.450  28.407 1.00 148.02 ? 667 ARG   A CZ  1 
ATOM   2928 N  NH1 . ARG   A 1 371 ? -48.977 -10.425 27.850 1.00 154.33 ? 667 ARG   A NH1 1 
ATOM   2929 N  NH2 . ARG   A 1 371 ? -47.554 -8.637  27.642 1.00 146.51 ? 667 ARG   A NH2 1 
ATOM   2930 N  N   . CYS   A 1 372 ? -45.699 -12.978 28.798 1.00 107.49 ? 668 CYS   A N   1 
ATOM   2931 C  CA  . CYS   A 1 372 ? -45.867 -13.696 27.542 1.00 106.53 ? 668 CYS   A CA  1 
ATOM   2932 C  C   . CYS   A 1 372 ? -44.661 -14.557 27.171 1.00 97.42  ? 668 CYS   A C   1 
ATOM   2933 O  O   . CYS   A 1 372 ? -44.545 -14.966 26.009 1.00 101.37 ? 668 CYS   A O   1 
ATOM   2934 C  CB  . CYS   A 1 372 ? -46.172 -12.709 26.410 1.00 114.17 ? 668 CYS   A CB  1 
ATOM   2935 S  SG  . CYS   A 1 372 ? -44.788 -11.636 25.940 1.00 113.64 ? 668 CYS   A SG  1 
ATOM   2936 N  N   . ARG   A 1 373 ? -43.764 -14.845 28.119 1.00 86.15  ? 669 ARG   A N   1 
ATOM   2937 C  CA  . ARG   A 1 373 ? -42.605 -15.685 27.828 1.00 82.77  ? 669 ARG   A CA  1 
ATOM   2938 C  C   . ARG   A 1 373 ? -42.146 -16.465 29.054 1.00 88.35  ? 669 ARG   A C   1 
ATOM   2939 O  O   . ARG   A 1 373 ? -41.397 -17.440 28.934 1.00 84.93  ? 669 ARG   A O   1 
ATOM   2940 C  CB  . ARG   A 1 373 ? -41.442 -14.847 27.287 1.00 79.86  ? 669 ARG   A CB  1 
ATOM   2941 C  CG  . ARG   A 1 373 ? -40.361 -15.683 26.613 1.00 77.38  ? 669 ARG   A CG  1 
ATOM   2942 C  CD  . ARG   A 1 373 ? -39.123 -14.877 26.249 1.00 73.79  ? 669 ARG   A CD  1 
ATOM   2943 N  NE  . ARG   A 1 373 ? -38.253 -15.651 25.363 1.00 76.54  ? 669 ARG   A NE  1 
ATOM   2944 C  CZ  . ARG   A 1 373 ? -36.950 -15.436 25.221 1.00 70.09  ? 669 ARG   A CZ  1 
ATOM   2945 N  NH1 . ARG   A 1 373 ? -36.360 -14.470 25.913 1.00 61.04  ? 669 ARG   A NH1 1 
ATOM   2946 N  NH2 . ARG   A 1 373 ? -36.235 -16.194 24.399 1.00 66.72  ? 669 ARG   A NH2 1 
ATOM   2947 N  N   . GLY   A 1 374 ? -42.584 -16.043 30.238 1.00 97.37  ? 670 GLY   A N   1 
ATOM   2948 C  CA  . GLY   A 1 374 ? -42.254 -16.759 31.455 1.00 100.15 ? 670 GLY   A CA  1 
ATOM   2949 C  C   . GLY   A 1 374 ? -40.931 -16.404 32.083 1.00 98.60  ? 670 GLY   A C   1 
ATOM   2950 O  O   . GLY   A 1 374 ? -40.404 -17.190 32.879 1.00 100.38 ? 670 GLY   A O   1 
ATOM   2951 N  N   . GLY   A 1 375 ? -40.366 -15.256 31.749 1.00 93.00  ? 671 GLY   A N   1 
ATOM   2952 C  CA  . GLY   A 1 375 ? -39.092 -14.855 32.319 1.00 83.37  ? 671 GLY   A CA  1 
ATOM   2953 C  C   . GLY   A 1 375 ? -38.310 -13.988 31.357 1.00 76.13  ? 671 GLY   A C   1 
ATOM   2954 O  O   . GLY   A 1 375 ? -38.691 -13.791 30.205 1.00 74.88  ? 671 GLY   A O   1 
ATOM   2955 N  N   . CYS   A 1 376 ? -37.198 -13.473 31.859 1.00 65.70  ? 672 CYS   A N   1 
ATOM   2956 C  CA  . CYS   A 1 376 ? -36.294 -12.596 31.125 1.00 62.95  ? 672 CYS   A CA  1 
ATOM   2957 C  C   . CYS   A 1 376 ? -34.911 -12.732 31.744 1.00 63.73  ? 672 CYS   A C   1 
ATOM   2958 O  O   . CYS   A 1 376 ? -34.680 -12.211 32.837 1.00 66.87  ? 672 CYS   A O   1 
ATOM   2959 C  CB  . CYS   A 1 376 ? -36.761 -11.136 31.187 1.00 58.42  ? 672 CYS   A CB  1 
ATOM   2960 S  SG  . CYS   A 1 376 ? -35.700 -9.944  30.333 1.00 64.72  ? 672 CYS   A SG  1 
ATOM   2961 N  N   . PRO   A 1 377 ? -33.978 -13.434 31.109 1.00 59.41  ? 673 PRO   A N   1 
ATOM   2962 C  CA  . PRO   A 1 377 ? -32.616 -13.490 31.660 1.00 53.13  ? 673 PRO   A CA  1 
ATOM   2963 C  C   . PRO   A 1 377 ? -32.039 -12.089 31.770 1.00 54.30  ? 673 PRO   A C   1 
ATOM   2964 O  O   . PRO   A 1 377 ? -32.137 -11.287 30.835 1.00 47.75  ? 673 PRO   A O   1 
ATOM   2965 C  CB  . PRO   A 1 377 ? -31.856 -14.342 30.641 1.00 57.29  ? 673 PRO   A CB  1 
ATOM   2966 C  CG  . PRO   A 1 377 ? -32.628 -14.115 29.316 1.00 49.06  ? 673 PRO   A CG  1 
ATOM   2967 C  CD  . PRO   A 1 377 ? -34.074 -13.994 29.741 1.00 53.62  ? 673 PRO   A CD  1 
ATOM   2968 N  N   . ALA   A 1 378 ? -31.455 -11.783 32.932 1.00 55.56  ? 674 ALA   A N   1 
ATOM   2969 C  CA  . ALA   A 1 378 ? -30.969 -10.431 33.181 1.00 50.14  ? 674 ALA   A CA  1 
ATOM   2970 C  C   . ALA   A 1 378 ? -29.761 -10.449 34.116 1.00 48.85  ? 674 ALA   A C   1 
ATOM   2971 O  O   . ALA   A 1 378 ? -29.749 -11.161 35.123 1.00 57.74  ? 674 ALA   A O   1 
ATOM   2972 C  CB  . ALA   A 1 378 ? -32.090 -9.546  33.745 1.00 46.29  ? 674 ALA   A CB  1 
ATOM   2973 N  N   . ASP   A 1 379 ? -28.743 -9.659  33.760 1.00 49.53  ? 675 ASP   A N   1 
ATOM   2974 C  CA  . ASP   A 1 379 ? -27.492 -9.553  34.500 1.00 46.00  ? 675 ASP   A CA  1 
ATOM   2975 C  C   . ASP   A 1 379 ? -27.526 -8.228  35.254 1.00 54.71  ? 675 ASP   A C   1 
ATOM   2976 O  O   . ASP   A 1 379 ? -27.217 -7.165  34.697 1.00 47.51  ? 675 ASP   A O   1 
ATOM   2977 C  CB  . ASP   A 1 379 ? -26.287 -9.630  33.578 1.00 45.62  ? 675 ASP   A CB  1 
ATOM   2978 C  CG  . ASP   A 1 379 ? -24.981 -9.769  34.326 1.00 54.56  ? 675 ASP   A CG  1 
ATOM   2979 O  OD1 . ASP   A 1 379 ? -24.044 -10.361 33.762 1.00 55.38  ? 675 ASP   A OD1 1 
ATOM   2980 O  OD2 . ASP   A 1 379 ? -24.883 -9.298  35.484 1.00 54.34  ? 675 ASP   A OD2 1 
ATOM   2981 N  N   . TRP   A 1 380 ? -27.907 -8.313  36.527 1.00 45.81  ? 676 TRP   A N   1 
ATOM   2982 C  CA  . TRP   A 1 380 ? -27.995 -7.132  37.373 1.00 42.00  ? 676 TRP   A CA  1 
ATOM   2983 C  C   . TRP   A 1 380 ? -26.718 -6.319  37.321 1.00 43.76  ? 676 TRP   A C   1 
ATOM   2984 O  O   . TRP   A 1 380 ? -26.761 -5.087  37.189 1.00 48.62  ? 676 TRP   A O   1 
ATOM   2985 C  CB  . TRP   A 1 380 ? -28.293 -7.558  38.800 1.00 42.34  ? 676 TRP   A CB  1 
ATOM   2986 C  CG  . TRP   A 1 380 ? -28.766 -6.487  39.672 1.00 46.51  ? 676 TRP   A CG  1 
ATOM   2987 C  CD1 . TRP   A 1 380 ? -30.060 -6.229  40.017 1.00 54.09  ? 676 TRP   A CD1 1 
ATOM   2988 C  CD2 . TRP   A 1 380 ? -27.957 -5.546  40.391 1.00 49.44  ? 676 TRP   A CD2 1 
ATOM   2989 N  NE1 . TRP   A 1 380 ? -30.106 -5.177  40.897 1.00 55.62  ? 676 TRP   A NE1 1 
ATOM   2990 C  CE2 . TRP   A 1 380 ? -28.831 -4.737  41.138 1.00 51.01  ? 676 TRP   A CE2 1 
ATOM   2991 C  CE3 . TRP   A 1 380 ? -26.584 -5.294  40.453 1.00 44.72  ? 676 TRP   A CE3 1 
ATOM   2992 C  CZ2 . TRP   A 1 380 ? -28.378 -3.683  41.961 1.00 50.39  ? 676 TRP   A CZ2 1 
ATOM   2993 C  CZ3 . TRP   A 1 380 ? -26.130 -4.246  41.278 1.00 48.57  ? 676 TRP   A CZ3 1 
ATOM   2994 C  CH2 . TRP   A 1 380 ? -27.026 -3.460  42.014 1.00 46.33  ? 676 TRP   A CH2 1 
ATOM   2995 N  N   . VAL   A 1 381 ? -25.569 -6.993  37.422 1.00 47.58  ? 677 VAL   A N   1 
ATOM   2996 C  CA  . VAL   A 1 381 ? -24.273 -6.321  37.422 1.00 41.81  ? 677 VAL   A CA  1 
ATOM   2997 C  C   . VAL   A 1 381 ? -24.132 -5.409  36.222 1.00 52.15  ? 677 VAL   A C   1 
ATOM   2998 O  O   . VAL   A 1 381 ? -23.479 -4.365  36.311 1.00 45.54  ? 677 VAL   A O   1 
ATOM   2999 C  CB  . VAL   A 1 381 ? -23.129 -7.361  37.473 1.00 51.89  ? 677 VAL   A CB  1 
ATOM   3000 C  CG1 . VAL   A 1 381 ? -21.790 -6.709  37.157 1.00 45.79  ? 677 VAL   A CG1 1 
ATOM   3001 C  CG2 . VAL   A 1 381 ? -23.075 -8.034  38.829 1.00 51.43  ? 677 VAL   A CG2 1 
ATOM   3002 N  N   . TRP   A 1 382 ? -24.733 -5.781  35.079 1.00 54.76  ? 678 TRP   A N   1 
ATOM   3003 C  CA  . TRP   A 1 382 ? -24.639 -4.997  33.850 1.00 49.49  ? 678 TRP   A CA  1 
ATOM   3004 C  C   . TRP   A 1 382 ? -25.864 -4.134  33.574 1.00 45.69  ? 678 TRP   A C   1 
ATOM   3005 O  O   . TRP   A 1 382 ? -25.725 -3.071  32.953 1.00 49.89  ? 678 TRP   A O   1 
ATOM   3006 C  CB  . TRP   A 1 382 ? -24.406 -5.922  32.641 1.00 49.08  ? 678 TRP   A CB  1 
ATOM   3007 C  CG  . TRP   A 1 382 ? -22.967 -6.296  32.441 1.00 48.10  ? 678 TRP   A CG  1 
ATOM   3008 C  CD1 . TRP   A 1 382 ? -22.167 -7.008  33.301 1.00 58.98  ? 678 TRP   A CD1 1 
ATOM   3009 C  CD2 . TRP   A 1 382 ? -22.145 -5.965  31.312 1.00 50.49  ? 678 TRP   A CD2 1 
ATOM   3010 N  NE1 . TRP   A 1 382 ? -20.905 -7.148  32.761 1.00 57.12  ? 678 TRP   A NE1 1 
ATOM   3011 C  CE2 . TRP   A 1 382 ? -20.867 -6.517  31.543 1.00 56.90  ? 678 TRP   A CE2 1 
ATOM   3012 C  CE3 . TRP   A 1 382 ? -22.378 -5.282  30.119 1.00 43.14  ? 678 TRP   A CE3 1 
ATOM   3013 C  CZ2 . TRP   A 1 382 ? -19.820 -6.387  30.628 1.00 62.26  ? 678 TRP   A CZ2 1 
ATOM   3014 C  CZ3 . TRP   A 1 382 ? -21.328 -5.156  29.205 1.00 50.01  ? 678 TRP   A CZ3 1 
ATOM   3015 C  CH2 . TRP   A 1 382 ? -20.072 -5.710  29.468 1.00 56.34  ? 678 TRP   A CH2 1 
ATOM   3016 N  N   . ILE   A 1 383 ? -27.053 -4.544  34.031 1.00 47.43  ? 679 ILE   A N   1 
ATOM   3017 C  CA  . ILE   A 1 383 ? -28.258 -3.751  33.785 1.00 52.47  ? 679 ILE   A CA  1 
ATOM   3018 C  C   . ILE   A 1 383 ? -28.220 -2.452  34.592 1.00 55.51  ? 679 ILE   A C   1 
ATOM   3019 O  O   . ILE   A 1 383 ? -28.593 -1.383  34.089 1.00 51.75  ? 679 ILE   A O   1 
ATOM   3020 C  CB  . ILE   A 1 383 ? -29.521 -4.580  34.108 1.00 52.14  ? 679 ILE   A CB  1 
ATOM   3021 C  CG1 . ILE   A 1 383 ? -29.627 -5.794  33.175 1.00 45.41  ? 679 ILE   A CG1 1 
ATOM   3022 C  CG2 . ILE   A 1 383 ? -30.809 -3.728  34.040 1.00 45.20  ? 679 ILE   A CG2 1 
ATOM   3023 C  CD1 . ILE   A 1 383 ? -29.833 -5.450  31.668 1.00 56.82  ? 679 ILE   A CD1 1 
ATOM   3024 N  N   . VAL   A 1 384 ? -27.765 -2.512  35.841 1.00 52.78  ? 680 VAL   A N   1 
ATOM   3025 C  CA  . VAL   A 1 384 ? -27.767 -1.308  36.690 1.00 53.66  ? 680 VAL   A CA  1 
ATOM   3026 C  C   . VAL   A 1 384 ? -26.804 -0.281  36.105 1.00 54.88  ? 680 VAL   A C   1 
ATOM   3027 O  O   . VAL   A 1 384 ? -25.631 -0.611  35.855 1.00 54.59  ? 680 VAL   A O   1 
ATOM   3028 C  CB  . VAL   A 1 384 ? -27.383 -1.663  38.127 1.00 52.66  ? 680 VAL   A CB  1 
ATOM   3029 C  CG1 . VAL   A 1 384 ? -27.208 -0.387  39.030 1.00 50.34  ? 680 VAL   A CG1 1 
ATOM   3030 C  CG2 . VAL   A 1 384 ? -28.421 -2.597  38.720 1.00 59.16  ? 680 VAL   A CG2 1 
ATOM   3031 N  N   . PRO   A 1 385 ? -27.244 0.959   35.886 1.00 59.20  ? 681 PRO   A N   1 
ATOM   3032 C  CA  . PRO   A 1 385 ? -26.366 1.957   35.279 1.00 56.82  ? 681 PRO   A CA  1 
ATOM   3033 C  C   . PRO   A 1 385 ? -25.187 2.260   36.172 1.00 62.04  ? 681 PRO   A C   1 
ATOM   3034 O  O   . PRO   A 1 385 ? -25.272 2.148   37.415 1.00 59.98  ? 681 PRO   A O   1 
ATOM   3035 C  CB  . PRO   A 1 385 ? -27.282 3.182   35.138 1.00 67.57  ? 681 PRO   A CB  1 
ATOM   3036 C  CG  . PRO   A 1 385 ? -28.630 2.597   35.015 1.00 71.95  ? 681 PRO   A CG  1 
ATOM   3037 C  CD  . PRO   A 1 385 ? -28.634 1.438   35.965 1.00 68.26  ? 681 PRO   A CD  1 
ATOM   3038 N  N   . PRO   A 1 386 ? -24.076 2.728   35.593 1.00 56.48  ? 682 PRO   A N   1 
ATOM   3039 C  CA  . PRO   A 1 386 ? -22.851 2.959   36.361 1.00 59.79  ? 682 PRO   A CA  1 
ATOM   3040 C  C   . PRO   A 1 386 ? -22.829 4.253   37.155 1.00 62.99  ? 682 PRO   A C   1 
ATOM   3041 O  O   . PRO   A 1 386 ? -21.763 4.629   37.654 1.00 62.53  ? 682 PRO   A O   1 
ATOM   3042 C  CB  . PRO   A 1 386 ? -21.787 3.013   35.265 1.00 58.25  ? 682 PRO   A CB  1 
ATOM   3043 C  CG  . PRO   A 1 386 ? -22.522 3.718   34.160 1.00 54.08  ? 682 PRO   A CG  1 
ATOM   3044 C  CD  . PRO   A 1 386 ? -23.874 3.028   34.160 1.00 56.15  ? 682 PRO   A CD  1 
ATOM   3045 N  N   . MET   A 1 387 ? -23.945 4.968   37.229 1.00 64.20  ? 683 MET   A N   1 
ATOM   3046 C  CA  . MET   A 1 387 ? -24.086 6.085   38.149 1.00 66.79  ? 683 MET   A CA  1 
ATOM   3047 C  C   . MET   A 1 387 ? -25.524 6.086   38.629 1.00 64.75  ? 683 MET   A C   1 
ATOM   3048 O  O   . MET   A 1 387 ? -26.412 5.549   37.958 1.00 61.45  ? 683 MET   A O   1 
ATOM   3049 C  CB  . MET   A 1 387 ? -23.760 7.436   37.495 1.00 78.04  ? 683 MET   A CB  1 
ATOM   3050 C  CG  . MET   A 1 387 ? -24.875 7.935   36.589 1.00 78.09  ? 683 MET   A CG  1 
ATOM   3051 S  SD  . MET   A 1 387 ? -24.455 9.426   35.659 1.00 89.82  ? 683 MET   A SD  1 
ATOM   3052 C  CE  . MET   A 1 387 ? -24.447 10.660  36.934 1.00 89.06  ? 683 MET   A CE  1 
ATOM   3053 N  N   . SER   A 1 388 ? -25.743 6.647   39.818 1.00 72.71  ? 684 SER   A N   1 
ATOM   3054 C  CA  . SER   A 1 388 ? -27.089 6.826   40.356 1.00 72.85  ? 684 SER   A CA  1 
ATOM   3055 C  C   . SER   A 1 388 ? -27.873 5.520   40.382 1.00 67.35  ? 684 SER   A C   1 
ATOM   3056 O  O   . SER   A 1 388 ? -29.081 5.516   40.157 1.00 72.03  ? 684 SER   A O   1 
ATOM   3057 C  CB  . SER   A 1 388 ? -27.852 7.882   39.553 1.00 75.81  ? 684 SER   A CB  1 
ATOM   3058 O  OG  . SER   A 1 388 ? -27.035 9.011   39.325 1.00 83.46  ? 684 SER   A OG  1 
ATOM   3059 N  N   . GLY   A 1 389 ? -27.177 4.409   40.626 1.00 61.14  ? 685 GLY   A N   1 
ATOM   3060 C  CA  . GLY   A 1 389 ? -27.801 3.095   40.514 1.00 55.11  ? 685 GLY   A CA  1 
ATOM   3061 C  C   . GLY   A 1 389 ? -29.131 2.994   41.235 1.00 59.99  ? 685 GLY   A C   1 
ATOM   3062 O  O   . GLY   A 1 389 ? -30.143 2.628   40.635 1.00 60.99  ? 685 GLY   A O   1 
ATOM   3063 N  N   . SER   A 1 390 ? -29.160 3.344   42.524 1.00 61.01  ? 686 SER   A N   1 
ATOM   3064 C  CA  . SER   A 1 390 ? -30.344 3.031   43.313 1.00 63.24  ? 686 SER   A CA  1 
ATOM   3065 C  C   . SER   A 1 390 ? -31.502 3.994   43.081 1.00 70.59  ? 686 SER   A C   1 
ATOM   3066 O  O   . SER   A 1 390 ? -32.603 3.738   43.581 1.00 74.68  ? 686 SER   A O   1 
ATOM   3067 C  CB  . SER   A 1 390 ? -29.996 2.982   44.806 1.00 62.81  ? 686 SER   A CB  1 
ATOM   3068 O  OG  . SER   A 1 390 ? -29.500 4.231   45.216 1.00 62.24  ? 686 SER   A OG  1 
ATOM   3069 N  N   . ILE   A 1 391 ? -31.308 5.093   42.344 1.00 72.27  ? 687 ILE   A N   1 
ATOM   3070 C  CA  . ILE   A 1 391 ? -32.449 5.925   41.973 1.00 69.88  ? 687 ILE   A CA  1 
ATOM   3071 C  C   . ILE   A 1 391 ? -33.009 5.526   40.614 1.00 73.92  ? 687 ILE   A C   1 
ATOM   3072 O  O   . ILE   A 1 391 ? -33.900 6.210   40.096 1.00 78.84  ? 687 ILE   A O   1 
ATOM   3073 C  CB  . ILE   A 1 391 ? -32.119 7.434   42.002 1.00 78.64  ? 687 ILE   A CB  1 
ATOM   3074 C  CG1 . ILE   A 1 391 ? -31.044 7.789   40.982 1.00 80.30  ? 687 ILE   A CG1 1 
ATOM   3075 C  CG2 . ILE   A 1 391 ? -31.722 7.890   43.428 1.00 82.29  ? 687 ILE   A CG2 1 
ATOM   3076 C  CD1 . ILE   A 1 391 ? -30.964 9.285   40.675 1.00 84.48  ? 687 ILE   A CD1 1 
ATOM   3077 N  N   . THR   A 1 392 ? -32.510 4.428   40.020 1.00 73.17  ? 688 THR   A N   1 
ATOM   3078 C  CA  . THR   A 1 392 ? -33.159 3.780   38.887 1.00 71.90  ? 688 THR   A CA  1 
ATOM   3079 C  C   . THR   A 1 392 ? -33.877 2.518   39.356 1.00 68.61  ? 688 THR   A C   1 
ATOM   3080 O  O   . THR   A 1 392 ? -33.479 1.898   40.349 1.00 65.67  ? 688 THR   A O   1 
ATOM   3081 C  CB  . THR   A 1 392 ? -32.158 3.429   37.772 1.00 74.81  ? 688 THR   A CB  1 
ATOM   3082 O  OG1 . THR   A 1 392 ? -31.315 2.339   38.163 1.00 70.52  ? 688 THR   A OG1 1 
ATOM   3083 C  CG2 . THR   A 1 392 ? -31.301 4.637   37.394 1.00 73.88  ? 688 THR   A CG2 1 
ATOM   3084 N  N   . PRO   A 1 393 ? -34.964 2.127   38.685 1.00 74.70  ? 689 PRO   A N   1 
ATOM   3085 C  CA  . PRO   A 1 393 ? -35.776 1.011   39.197 1.00 73.42  ? 689 PRO   A CA  1 
ATOM   3086 C  C   . PRO   A 1 393 ? -35.118 -0.351  39.060 1.00 64.60  ? 689 PRO   A C   1 
ATOM   3087 O  O   . PRO   A 1 393 ? -35.511 -1.281  39.780 1.00 68.56  ? 689 PRO   A O   1 
ATOM   3088 C  CB  . PRO   A 1 393 ? -37.052 1.094   38.347 1.00 82.56  ? 689 PRO   A CB  1 
ATOM   3089 C  CG  . PRO   A 1 393 ? -36.571 1.677   37.054 1.00 81.13  ? 689 PRO   A CG  1 
ATOM   3090 C  CD  . PRO   A 1 393 ? -35.557 2.716   37.470 1.00 83.23  ? 689 PRO   A CD  1 
ATOM   3091 N  N   . VAL   A 1 394 ? -34.142 -0.510  38.160 1.00 61.50  ? 690 VAL   A N   1 
ATOM   3092 C  CA  . VAL   A 1 394 ? -33.502 -1.814  38.012 1.00 53.18  ? 690 VAL   A CA  1 
ATOM   3093 C  C   . VAL   A 1 394 ? -32.626 -2.161  39.215 1.00 52.95  ? 690 VAL   A C   1 
ATOM   3094 O  O   . VAL   A 1 394 ? -32.454 -3.349  39.522 1.00 54.94  ? 690 VAL   A O   1 
ATOM   3095 C  CB  . VAL   A 1 394 ? -32.692 -1.903  36.698 1.00 50.04  ? 690 VAL   A CB  1 
ATOM   3096 C  CG1 . VAL   A 1 394 ? -33.619 -1.865  35.464 1.00 57.60  ? 690 VAL   A CG1 1 
ATOM   3097 C  CG2 . VAL   A 1 394 ? -31.645 -0.817  36.634 1.00 49.84  ? 690 VAL   A CG2 1 
ATOM   3098 N  N   . PHE   A 1 395 ? -32.122 -1.162  39.958 1.00 60.86  ? 691 PHE   A N   1 
ATOM   3099 C  CA  . PHE   A 1 395 ? -31.351 -1.454  41.171 1.00 50.62  ? 691 PHE   A CA  1 
ATOM   3100 C  C   . PHE   A 1 395 ? -32.152 -2.279  42.167 1.00 56.85  ? 691 PHE   A C   1 
ATOM   3101 O  O   . PHE   A 1 395 ? -31.587 -3.124  42.880 1.00 56.69  ? 691 PHE   A O   1 
ATOM   3102 C  CB  . PHE   A 1 395 ? -30.892 -0.146  41.833 1.00 56.31  ? 691 PHE   A CB  1 
ATOM   3103 C  CG  . PHE   A 1 395 ? -30.033 -0.339  43.067 1.00 56.81  ? 691 PHE   A CG  1 
ATOM   3104 C  CD1 . PHE   A 1 395 ? -28.644 -0.300  42.978 1.00 56.91  ? 691 PHE   A CD1 1 
ATOM   3105 C  CD2 . PHE   A 1 395 ? -30.609 -0.518  44.326 1.00 56.70  ? 691 PHE   A CD2 1 
ATOM   3106 C  CE1 . PHE   A 1 395 ? -27.858 -0.469  44.147 1.00 59.62  ? 691 PHE   A CE1 1 
ATOM   3107 C  CE2 . PHE   A 1 395 ? -29.825 -0.693  45.464 1.00 60.71  ? 691 PHE   A CE2 1 
ATOM   3108 C  CZ  . PHE   A 1 395 ? -28.453 -0.662  45.362 1.00 57.99  ? 691 PHE   A CZ  1 
ATOM   3109 N  N   . HIS   A 1 396 ? -33.459 -2.042  42.238 1.00 59.83  ? 692 HIS   A N   1 
ATOM   3110 C  CA  . HIS   A 1 396 ? -34.329 -2.662  43.225 1.00 59.86  ? 692 HIS   A CA  1 
ATOM   3111 C  C   . HIS   A 1 396 ? -35.013 -3.912  42.710 1.00 62.43  ? 692 HIS   A C   1 
ATOM   3112 O  O   . HIS   A 1 396 ? -35.803 -4.519  43.439 1.00 62.05  ? 692 HIS   A O   1 
ATOM   3113 C  CB  . HIS   A 1 396 ? -35.359 -1.640  43.679 1.00 73.17  ? 692 HIS   A CB  1 
ATOM   3114 C  CG  . HIS   A 1 396 ? -34.734 -0.359  44.119 1.00 76.20  ? 692 HIS   A CG  1 
ATOM   3115 N  ND1 . HIS   A 1 396 ? -33.988 -0.265  45.272 1.00 72.88  ? 692 HIS   A ND1 1 
ATOM   3116 C  CD2 . HIS   A 1 396 ? -34.685 0.860   43.534 1.00 77.58  ? 692 HIS   A CD2 1 
ATOM   3117 C  CE1 . HIS   A 1 396 ? -33.530 0.968   45.394 1.00 78.72  ? 692 HIS   A CE1 1 
ATOM   3118 N  NE2 . HIS   A 1 396 ? -33.940 1.670   44.353 1.00 76.09  ? 692 HIS   A NE2 1 
ATOM   3119 N  N   . GLN   A 1 397 ? -34.701 -4.315  41.492 1.00 57.38  ? 693 GLN   A N   1 
ATOM   3120 C  CA  . GLN   A 1 397 ? -35.341 -5.433  40.813 1.00 61.10  ? 693 GLN   A CA  1 
ATOM   3121 C  C   . GLN   A 1 397 ? -34.405 -6.631  40.873 1.00 52.94  ? 693 GLN   A C   1 
ATOM   3122 O  O   . GLN   A 1 397 ? -33.322 -6.606  40.284 1.00 54.51  ? 693 GLN   A O   1 
ATOM   3123 C  CB  . GLN   A 1 397 ? -35.661 -5.053  39.367 1.00 60.72  ? 693 GLN   A CB  1 
ATOM   3124 C  CG  . GLN   A 1 397 ? -36.362 -6.129  38.564 1.00 58.63  ? 693 GLN   A CG  1 
ATOM   3125 C  CD  . GLN   A 1 397 ? -37.738 -6.444  39.089 1.00 65.44  ? 693 GLN   A CD  1 
ATOM   3126 O  OE1 . GLN   A 1 397 ? -38.645 -5.601  39.066 1.00 63.84  ? 693 GLN   A OE1 1 
ATOM   3127 N  NE2 . GLN   A 1 397 ? -37.907 -7.670  39.574 1.00 68.02  ? 693 GLN   A NE2 1 
ATOM   3128 N  N   . GLU   A 1 398 ? -34.807 -7.662  41.616 1.00 59.43  ? 694 GLU   A N   1 
ATOM   3129 C  CA  . GLU   A 1 398 ? -34.126 -8.945  41.513 1.00 58.92  ? 694 GLU   A CA  1 
ATOM   3130 C  C   . GLU   A 1 398 ? -34.208 -9.441  40.077 1.00 61.34  ? 694 GLU   A C   1 
ATOM   3131 O  O   . GLU   A 1 398 ? -35.211 -9.233  39.390 1.00 64.15  ? 694 GLU   A O   1 
ATOM   3132 C  CB  . GLU   A 1 398 ? -34.752 -9.968  42.452 1.00 53.57  ? 694 GLU   A CB  1 
ATOM   3133 C  CG  . GLU   A 1 398 ? -34.433 -9.714  43.948 1.00 54.70  ? 694 GLU   A CG  1 
ATOM   3134 C  CD  . GLU   A 1 398 ? -35.280 -10.539 44.867 1.00 65.83  ? 694 GLU   A CD  1 
ATOM   3135 O  OE1 . GLU   A 1 398 ? -35.229 -10.288 46.097 1.00 67.89  ? 694 GLU   A OE1 1 
ATOM   3136 O  OE2 . GLU   A 1 398 ? -35.984 -11.440 44.371 1.00 71.36  ? 694 GLU   A OE2 1 
ATOM   3137 N  N   . MET   A 1 399 ? -33.134 -10.092 39.621 1.00 57.97  ? 695 MET   A N   1 
ATOM   3138 C  CA  . MET   A 1 399 ? -33.046 -10.603 38.256 1.00 59.52  ? 695 MET   A CA  1 
ATOM   3139 C  C   . MET   A 1 399 ? -32.337 -11.946 38.241 1.00 61.41  ? 695 MET   A C   1 
ATOM   3140 O  O   . MET   A 1 399 ? -31.246 -12.073 38.803 1.00 62.43  ? 695 MET   A O   1 
ATOM   3141 C  CB  . MET   A 1 399 ? -32.260 -9.666  37.325 1.00 53.57  ? 695 MET   A CB  1 
ATOM   3142 C  CG  . MET   A 1 399 ? -32.814 -8.275  37.180 1.00 52.43  ? 695 MET   A CG  1 
ATOM   3143 S  SD  . MET   A 1 399 ? -31.610 -7.170  36.413 1.00 52.98  ? 695 MET   A SD  1 
ATOM   3144 C  CE  . MET   A 1 399 ? -32.373 -5.601  36.766 1.00 48.78  ? 695 MET   A CE  1 
ATOM   3145 N  N   . LEU   A 1 400 ? -32.921 -12.923 37.544 1.00 54.79  ? 696 LEU   A N   1 
ATOM   3146 C  CA  . LEU   A 1 400 ? -32.257 -14.200 37.309 1.00 54.71  ? 696 LEU   A CA  1 
ATOM   3147 C  C   . LEU   A 1 400 ? -31.455 -14.132 36.018 1.00 60.11  ? 696 LEU   A C   1 
ATOM   3148 O  O   . LEU   A 1 400 ? -31.982 -13.735 34.970 1.00 56.25  ? 696 LEU   A O   1 
ATOM   3149 C  CB  . LEU   A 1 400 ? -33.262 -15.344 37.221 1.00 57.29  ? 696 LEU   A CB  1 
ATOM   3150 C  CG  . LEU   A 1 400 ? -34.165 -15.580 38.417 1.00 56.41  ? 696 LEU   A CG  1 
ATOM   3151 C  CD1 . LEU   A 1 400 ? -35.183 -16.653 38.081 1.00 59.86  ? 696 LEU   A CD1 1 
ATOM   3152 C  CD2 . LEU   A 1 400 ? -33.373 -15.926 39.698 1.00 63.63  ? 696 LEU   A CD2 1 
ATOM   3153 N  N   . ASN   A 1 401 ? -30.182 -14.505 36.100 1.00 59.51  ? 697 ASN   A N   1 
ATOM   3154 C  CA  . ASN   A 1 401 ? -29.314 -14.591 34.939 1.00 53.60  ? 697 ASN   A CA  1 
ATOM   3155 C  C   . ASN   A 1 401 ? -29.177 -16.046 34.523 1.00 60.69  ? 697 ASN   A C   1 
ATOM   3156 O  O   . ASN   A 1 401 ? -28.806 -16.900 35.335 1.00 57.61  ? 697 ASN   A O   1 
ATOM   3157 C  CB  . ASN   A 1 401 ? -27.931 -13.990 35.201 1.00 50.28  ? 697 ASN   A CB  1 
ATOM   3158 C  CG  . ASN   A 1 401 ? -27.197 -13.693 33.913 1.00 53.99  ? 697 ASN   A CG  1 
ATOM   3159 O  OD1 . ASN   A 1 401 ? -27.813 -13.669 32.854 1.00 48.14  ? 697 ASN   A OD1 1 
ATOM   3160 N  ND2 . ASN   A 1 401 ? -25.898 -13.458 33.986 1.00 49.49  ? 697 ASN   A ND2 1 
ATOM   3161 N  N   . TYR   A 1 402 ? -29.477 -16.316 33.258 1.00 60.37  ? 698 TYR   A N   1 
ATOM   3162 C  CA  . TYR   A 1 402 ? -29.281 -17.636 32.696 1.00 53.42  ? 698 TYR   A CA  1 
ATOM   3163 C  C   . TYR   A 1 402 ? -29.067 -17.484 31.191 1.00 59.44  ? 698 TYR   A C   1 
ATOM   3164 O  O   . TYR   A 1 402 ? -29.299 -16.418 30.609 1.00 52.35  ? 698 TYR   A O   1 
ATOM   3165 C  CB  . TYR   A 1 402 ? -30.454 -18.560 33.046 1.00 62.96  ? 698 TYR   A CB  1 
ATOM   3166 C  CG  . TYR   A 1 402 ? -31.833 -17.952 32.883 1.00 65.26  ? 698 TYR   A CG  1 
ATOM   3167 C  CD1 . TYR   A 1 402 ? -32.499 -18.035 31.669 1.00 63.37  ? 698 TYR   A CD1 1 
ATOM   3168 C  CD2 . TYR   A 1 402 ? -32.478 -17.309 33.948 1.00 57.72  ? 698 TYR   A CD2 1 
ATOM   3169 C  CE1 . TYR   A 1 402 ? -33.755 -17.496 31.496 1.00 64.14  ? 698 TYR   A CE1 1 
ATOM   3170 C  CE2 . TYR   A 1 402 ? -33.757 -16.762 33.786 1.00 60.14  ? 698 TYR   A CE2 1 
ATOM   3171 C  CZ  . TYR   A 1 402 ? -34.384 -16.863 32.545 1.00 66.39  ? 698 TYR   A CZ  1 
ATOM   3172 O  OH  . TYR   A 1 402 ? -35.644 -16.342 32.330 1.00 64.09  ? 698 TYR   A OH  1 
ATOM   3173 N  N   . ARG   A 1 403 ? -28.591 -18.551 30.567 1.00 57.78  ? 699 ARG   A N   1 
ATOM   3174 C  CA  . ARG   A 1 403 ? -28.104 -18.494 29.192 1.00 63.57  ? 699 ARG   A CA  1 
ATOM   3175 C  C   . ARG   A 1 403 ? -29.119 -19.186 28.296 1.00 63.85  ? 699 ARG   A C   1 
ATOM   3176 O  O   . ARG   A 1 403 ? -29.224 -20.414 28.296 1.00 68.35  ? 699 ARG   A O   1 
ATOM   3177 C  CB  . ARG   A 1 403 ? -26.729 -19.146 29.076 1.00 74.05  ? 699 ARG   A CB  1 
ATOM   3178 C  CG  . ARG   A 1 403 ? -25.680 -18.574 30.004 1.00 80.21  ? 699 ARG   A CG  1 
ATOM   3179 C  CD  . ARG   A 1 403 ? -25.136 -17.279 29.450 1.00 91.03  ? 699 ARG   A CD  1 
ATOM   3180 N  NE  . ARG   A 1 403 ? -23.891 -17.495 28.724 1.00 104.24 ? 699 ARG   A NE  1 
ATOM   3181 C  CZ  . ARG   A 1 403 ? -23.412 -16.669 27.801 1.00 111.32 ? 699 ARG   A CZ  1 
ATOM   3182 N  NH1 . ARG   A 1 403 ? -24.081 -15.570 27.473 1.00 113.60 ? 699 ARG   A NH1 1 
ATOM   3183 N  NH2 . ARG   A 1 403 ? -22.265 -16.947 27.200 1.00 113.37 ? 699 ARG   A NH2 1 
ATOM   3184 N  N   . LEU   A 1 404 ? -29.875 -18.396 27.549 1.00 65.79  ? 700 LEU   A N   1 
ATOM   3185 C  CA  . LEU   A 1 404 ? -30.724 -18.929 26.499 1.00 63.10  ? 700 LEU   A CA  1 
ATOM   3186 C  C   . LEU   A 1 404 ? -30.017 -18.828 25.157 1.00 61.70  ? 700 LEU   A C   1 
ATOM   3187 O  O   . LEU   A 1 404 ? -29.143 -17.982 24.943 1.00 56.24  ? 700 LEU   A O   1 
ATOM   3188 C  CB  . LEU   A 1 404 ? -32.056 -18.182 26.421 1.00 61.50  ? 700 LEU   A CB  1 
ATOM   3189 C  CG  . LEU   A 1 404 ? -32.976 -18.193 27.642 1.00 63.39  ? 700 LEU   A CG  1 
ATOM   3190 C  CD1 . LEU   A 1 404 ? -34.273 -17.465 27.317 1.00 56.15  ? 700 LEU   A CD1 1 
ATOM   3191 C  CD2 . LEU   A 1 404 ? -33.254 -19.613 28.087 1.00 72.92  ? 700 LEU   A CD2 1 
ATOM   3192 N  N   . THR   A 1 405 ? -30.424 -19.696 24.238 1.00 57.71  ? 701 THR   A N   1 
ATOM   3193 C  CA  . THR   A 1 405 ? -29.955 -19.579 22.873 1.00 64.36  ? 701 THR   A CA  1 
ATOM   3194 C  C   . THR   A 1 405 ? -31.153 -19.396 21.937 1.00 61.69  ? 701 THR   A C   1 
ATOM   3195 O  O   . THR   A 1 405 ? -32.259 -19.846 22.261 1.00 58.62  ? 701 THR   A O   1 
ATOM   3196 C  CB  . THR   A 1 405 ? -29.136 -20.823 22.486 1.00 69.96  ? 701 THR   A CB  1 
ATOM   3197 O  OG1 . THR   A 1 405 ? -28.335 -20.540 21.337 1.00 68.08  ? 701 THR   A OG1 1 
ATOM   3198 C  CG2 . THR   A 1 405 ? -30.031 -22.011 22.223 1.00 70.87  ? 701 THR   A CG2 1 
ATOM   3199 N  N   . PRO   A 1 406 ? -30.992 -18.707 20.786 1.00 63.05  ? 702 PRO   A N   1 
ATOM   3200 C  CA  . PRO   A 1 406 ? -29.852 -18.009 20.174 1.00 57.88  ? 702 PRO   A CA  1 
ATOM   3201 C  C   . PRO   A 1 406 ? -29.239 -16.950 21.067 1.00 56.28  ? 702 PRO   A C   1 
ATOM   3202 O  O   . PRO   A 1 406 ? -29.955 -16.361 21.883 1.00 53.20  ? 702 PRO   A O   1 
ATOM   3203 C  CB  . PRO   A 1 406 ? -30.466 -17.348 18.936 1.00 57.82  ? 702 PRO   A CB  1 
ATOM   3204 C  CG  . PRO   A 1 406 ? -31.601 -18.200 18.572 1.00 58.67  ? 702 PRO   A CG  1 
ATOM   3205 C  CD  . PRO   A 1 406 ? -32.137 -18.789 19.855 1.00 62.41  ? 702 PRO   A CD  1 
ATOM   3206 N  N   . SER   A 1 407 ? -27.946 -16.684 20.895 1.00 52.77  ? 703 SER   A N   1 
ATOM   3207 C  CA  . SER   A 1 407 ? -27.266 -15.788 21.808 1.00 55.68  ? 703 SER   A CA  1 
ATOM   3208 C  C   . SER   A 1 407 ? -26.079 -15.123 21.135 1.00 48.80  ? 703 SER   A C   1 
ATOM   3209 O  O   . SER   A 1 407 ? -25.548 -15.601 20.123 1.00 53.37  ? 703 SER   A O   1 
ATOM   3210 C  CB  . SER   A 1 407 ? -26.788 -16.542 23.056 1.00 59.86  ? 703 SER   A CB  1 
ATOM   3211 O  OG  . SER   A 1 407 ? -25.795 -17.477 22.672 1.00 70.39  ? 703 SER   A OG  1 
ATOM   3212 N  N   . PHE   A 1 408 ? -25.663 -14.004 21.723 1.00 47.52  ? 704 PHE   A N   1 
ATOM   3213 C  CA  . PHE   A 1 408 ? -24.399 -13.373 21.381 1.00 53.75  ? 704 PHE   A CA  1 
ATOM   3214 C  C   . PHE   A 1 408 ? -23.357 -13.813 22.396 1.00 55.34  ? 704 PHE   A C   1 
ATOM   3215 O  O   . PHE   A 1 408 ? -23.566 -13.682 23.609 1.00 53.83  ? 704 PHE   A O   1 
ATOM   3216 C  CB  . PHE   A 1 408 ? -24.507 -11.847 21.369 1.00 47.57  ? 704 PHE   A CB  1 
ATOM   3217 C  CG  . PHE   A 1 408 ? -25.384 -11.296 20.278 1.00 51.70  ? 704 PHE   A CG  1 
ATOM   3218 C  CD1 . PHE   A 1 408 ? -26.684 -10.902 20.552 1.00 53.83  ? 704 PHE   A CD1 1 
ATOM   3219 C  CD2 . PHE   A 1 408 ? -24.898 -11.164 18.975 1.00 52.73  ? 704 PHE   A CD2 1 
ATOM   3220 C  CE1 . PHE   A 1 408 ? -27.493 -10.378 19.561 1.00 50.95  ? 704 PHE   A CE1 1 
ATOM   3221 C  CE2 . PHE   A 1 408 ? -25.707 -10.637 17.955 1.00 42.70  ? 704 PHE   A CE2 1 
ATOM   3222 C  CZ  . PHE   A 1 408 ? -27.008 -10.252 18.238 1.00 44.87  ? 704 PHE   A CZ  1 
ATOM   3223 N  N   . GLU   A 1 409 ? -22.239 -14.337 21.905 1.00 45.94  ? 705 GLU   A N   1 
ATOM   3224 C  CA  . GLU   A 1 409 ? -21.184 -14.809 22.778 1.00 51.67  ? 705 GLU   A CA  1 
ATOM   3225 C  C   . GLU   A 1 409 ? -19.921 -13.997 22.557 1.00 58.73  ? 705 GLU   A C   1 
ATOM   3226 O  O   . GLU   A 1 409 ? -19.698 -13.434 21.478 1.00 67.48  ? 705 GLU   A O   1 
ATOM   3227 C  CB  . GLU   A 1 409 ? -20.892 -16.303 22.564 1.00 54.56  ? 705 GLU   A CB  1 
ATOM   3228 C  CG  . GLU   A 1 409 ? -22.107 -17.219 22.723 1.00 68.87  ? 705 GLU   A CG  1 
ATOM   3229 C  CD  . GLU   A 1 409 ? -22.724 -17.184 24.119 1.00 79.95  ? 705 GLU   A CD  1 
ATOM   3230 O  OE1 . GLU   A 1 409 ? -22.168 -16.523 25.022 1.00 82.68  ? 705 GLU   A OE1 1 
ATOM   3231 O  OE2 . GLU   A 1 409 ? -23.776 -17.827 24.313 1.00 84.64  ? 705 GLU   A OE2 1 
ATOM   3232 N  N   . TYR   A 1 410 ? -19.105 -13.924 23.600 1.00 51.32  ? 706 TYR   A N   1 
ATOM   3233 C  CA  . TYR   A 1 410 ? -17.797 -13.336 23.414 1.00 48.92  ? 706 TYR   A CA  1 
ATOM   3234 C  C   . TYR   A 1 410 ? -16.914 -14.310 22.657 1.00 47.02  ? 706 TYR   A C   1 
ATOM   3235 O  O   . TYR   A 1 410 ? -17.178 -15.517 22.582 1.00 59.21  ? 706 TYR   A O   1 
ATOM   3236 C  CB  . TYR   A 1 410 ? -17.163 -12.971 24.760 1.00 53.66  ? 706 TYR   A CB  1 
ATOM   3237 C  CG  . TYR   A 1 410 ? -17.922 -11.886 25.483 1.00 59.65  ? 706 TYR   A CG  1 
ATOM   3238 C  CD1 . TYR   A 1 410 ? -18.738 -12.190 26.572 1.00 67.97  ? 706 TYR   A CD1 1 
ATOM   3239 C  CD2 . TYR   A 1 410 ? -17.840 -10.558 25.072 1.00 62.96  ? 706 TYR   A CD2 1 
ATOM   3240 C  CE1 . TYR   A 1 410 ? -19.443 -11.201 27.236 1.00 71.06  ? 706 TYR   A CE1 1 
ATOM   3241 C  CE2 . TYR   A 1 410 ? -18.548 -9.563  25.725 1.00 69.51  ? 706 TYR   A CE2 1 
ATOM   3242 C  CZ  . TYR   A 1 410 ? -19.343 -9.893  26.814 1.00 76.58  ? 706 TYR   A CZ  1 
ATOM   3243 O  OH  . TYR   A 1 410 ? -20.054 -8.915  27.474 1.00 74.95  ? 706 TYR   A OH  1 
ATOM   3244 N  N   . GLN   A 1 411 ? -15.846 -13.781 22.090 1.00 50.63  ? 707 GLN   A N   1 
ATOM   3245 C  CA  . GLN   A 1 411 ? -14.961 -14.617 21.301 1.00 61.79  ? 707 GLN   A CA  1 
ATOM   3246 C  C   . GLN   A 1 411 ? -13.580 -14.002 21.371 1.00 66.27  ? 707 GLN   A C   1 
ATOM   3247 O  O   . GLN   A 1 411 ? -13.447 -12.797 21.621 1.00 68.37  ? 707 GLN   A O   1 
ATOM   3248 C  CB  . GLN   A 1 411 ? -15.452 -14.734 19.852 1.00 68.10  ? 707 GLN   A CB  1 
ATOM   3249 C  CG  . GLN   A 1 411 ? -15.230 -13.506 19.024 1.00 72.16  ? 707 GLN   A CG  1 
ATOM   3250 C  CD  . GLN   A 1 411 ? -15.890 -13.617 17.672 1.00 73.14  ? 707 GLN   A CD  1 
ATOM   3251 O  OE1 . GLN   A 1 411 ? -16.034 -14.713 17.132 1.00 76.32  ? 707 GLN   A OE1 1 
ATOM   3252 N  NE2 . GLN   A 1 411 ? -16.312 -12.487 17.125 1.00 75.14  ? 707 GLN   A NE2 1 
ATOM   3253 N  N   . PRO   A 1 412 ? -12.532 -14.807 21.210 1.00 73.43  ? 708 PRO   A N   1 
ATOM   3254 C  CA  . PRO   A 1 412 ? -11.172 -14.273 21.326 1.00 80.69  ? 708 PRO   A CA  1 
ATOM   3255 C  C   . PRO   A 1 412 ? -10.950 -13.128 20.355 1.00 82.99  ? 708 PRO   A C   1 
ATOM   3256 O  O   . PRO   A 1 412 ? -11.593 -13.037 19.308 1.00 81.64  ? 708 PRO   A O   1 
ATOM   3257 C  CB  . PRO   A 1 412 ? -10.285 -15.476 20.980 1.00 87.41  ? 708 PRO   A CB  1 
ATOM   3258 C  CG  . PRO   A 1 412 ? -11.125 -16.664 21.297 1.00 87.59  ? 708 PRO   A CG  1 
ATOM   3259 C  CD  . PRO   A 1 412 ? -12.544 -16.265 21.002 1.00 80.07  ? 708 PRO   A CD  1 
ATOM   3260 N  N   . ASP   A 1 413 ? -10.052 -12.232 20.728 1.00 85.64  ? 709 ASP   A N   1 
ATOM   3261 C  CA  . ASP   A 1 413 ? -9.617  -11.232 19.776 1.00 89.27  ? 709 ASP   A CA  1 
ATOM   3262 C  C   . ASP   A 1 413 ? -8.916  -11.925 18.612 1.00 90.80  ? 709 ASP   A C   1 
ATOM   3263 O  O   . ASP   A 1 413 ? -8.162  -12.883 18.822 1.00 90.35  ? 709 ASP   A O   1 
ATOM   3264 C  CB  . ASP   A 1 413 ? -8.694  -10.215 20.441 1.00 99.05  ? 709 ASP   A CB  1 
ATOM   3265 C  CG  . ASP   A 1 413 ? -9.461  -9.155  21.202 1.00 102.87 ? 709 ASP   A CG  1 
ATOM   3266 O  OD1 . ASP   A 1 413 ? -10.631 -8.897  20.843 1.00 100.55 ? 709 ASP   A OD1 1 
ATOM   3267 O  OD2 . ASP   A 1 413 ? -8.895  -8.578  22.152 1.00 104.50 ? 709 ASP   A OD2 1 
ATOM   3268 N  N   . PRO   A 1 414 ? -9.164  -11.491 17.377 1.00 90.60  ? 710 PRO   A N   1 
ATOM   3269 C  CA  . PRO   A 1 414 ? -8.666  -12.252 16.217 1.00 95.37  ? 710 PRO   A CA  1 
ATOM   3270 C  C   . PRO   A 1 414 ? -7.153  -12.339 16.143 1.00 101.71 ? 710 PRO   A C   1 
ATOM   3271 O  O   . PRO   A 1 414 ? -6.624  -13.369 15.706 1.00 108.86 ? 710 PRO   A O   1 
ATOM   3272 C  CB  . PRO   A 1 414 ? -9.245  -11.483 15.019 1.00 91.38  ? 710 PRO   A CB  1 
ATOM   3273 C  CG  . PRO   A 1 414 ? -10.370 -10.664 15.578 1.00 85.85  ? 710 PRO   A CG  1 
ATOM   3274 C  CD  . PRO   A 1 414 ? -9.985  -10.335 16.987 1.00 91.09  ? 710 PRO   A CD  1 
ATOM   3275 N  N   . TRP   A 1 415 ? -6.437  -11.293 16.556 1.00 99.55  ? 711 TRP   A N   1 
ATOM   3276 C  CA  . TRP   A 1 415 ? -4.982  -11.299 16.453 1.00 103.20 ? 711 TRP   A CA  1 
ATOM   3277 C  C   . TRP   A 1 415 ? -4.318  -12.240 17.451 1.00 101.11 ? 711 TRP   A C   1 
ATOM   3278 O  O   . TRP   A 1 415 ? -3.114  -12.487 17.332 1.00 103.54 ? 711 TRP   A O   1 
ATOM   3279 C  CB  . TRP   A 1 415 ? -4.439  -9.878  16.629 1.00 102.51 ? 711 TRP   A CB  1 
ATOM   3280 C  CG  . TRP   A 1 415 ? -4.873  -9.202  17.894 1.00 93.41  ? 711 TRP   A CG  1 
ATOM   3281 C  CD1 . TRP   A 1 415 ? -4.222  -9.220  19.099 1.00 93.94  ? 711 TRP   A CD1 1 
ATOM   3282 C  CD2 . TRP   A 1 415 ? -6.049  -8.399  18.088 1.00 87.38  ? 711 TRP   A CD2 1 
ATOM   3283 N  NE1 . TRP   A 1 415 ? -4.918  -8.484  20.023 1.00 84.46  ? 711 TRP   A NE1 1 
ATOM   3284 C  CE2 . TRP   A 1 415 ? -6.041  -7.968  19.431 1.00 85.53  ? 711 TRP   A CE2 1 
ATOM   3285 C  CE3 . TRP   A 1 415 ? -7.102  -8.000  17.257 1.00 87.84  ? 711 TRP   A CE3 1 
ATOM   3286 C  CZ2 . TRP   A 1 415 ? -7.047  -7.161  19.963 1.00 85.63  ? 711 TRP   A CZ2 1 
ATOM   3287 C  CZ3 . TRP   A 1 415 ? -8.102  -7.200  17.787 1.00 80.59  ? 711 TRP   A CZ3 1 
ATOM   3288 C  CH2 . TRP   A 1 415 ? -8.067  -6.793  19.130 1.00 85.99  ? 711 TRP   A CH2 1 
ATOM   3289 N  N   . ASN   A 1 416 ? -5.063  -12.768 18.424 1.00 96.63  ? 712 ASN   A N   1 
ATOM   3290 C  CA  . ASN   A 1 416 ? -4.513  -13.780 19.317 1.00 104.26 ? 712 ASN   A CA  1 
ATOM   3291 C  C   . ASN   A 1 416 ? -4.631  -15.179 18.735 1.00 103.12 ? 712 ASN   A C   1 
ATOM   3292 O  O   . ASN   A 1 416 ? -3.942  -16.094 19.199 1.00 106.32 ? 712 ASN   A O   1 
ATOM   3293 C  CB  . ASN   A 1 416 ? -5.222  -13.741 20.675 1.00 103.19 ? 712 ASN   A CB  1 
ATOM   3294 C  CG  . ASN   A 1 416 ? -5.101  -12.395 21.363 1.00 109.09 ? 712 ASN   A CG  1 
ATOM   3295 O  OD1 . ASN   A 1 416 ? -4.144  -11.655 21.138 1.00 117.83 ? 712 ASN   A OD1 1 
ATOM   3296 N  ND2 . ASN   A 1 416 ? -6.072  -12.072 22.213 1.00 104.71 ? 712 ASN   A ND2 1 
ATOM   3297 N  N   . THR   A 1 417 ? -5.480  -15.354 17.723 1.00 96.13  ? 713 THR   A N   1 
ATOM   3298 C  CA  . THR   A 1 417 ? -5.859  -16.663 17.221 1.00 96.66  ? 713 THR   A CA  1 
ATOM   3299 C  C   . THR   A 1 417 ? -5.528  -16.883 15.752 1.00 102.97 ? 713 THR   A C   1 
ATOM   3300 O  O   . THR   A 1 417 ? -5.401  -18.040 15.331 1.00 103.56 ? 713 THR   A O   1 
ATOM   3301 C  CB  . THR   A 1 417 ? -7.368  -16.875 17.423 1.00 94.23  ? 713 THR   A CB  1 
ATOM   3302 O  OG1 . THR   A 1 417 ? -8.081  -15.747 16.896 1.00 92.04  ? 713 THR   A OG1 1 
ATOM   3303 C  CG2 . THR   A 1 417 ? -7.692  -17.008 18.905 1.00 90.10  ? 713 THR   A CG2 1 
ATOM   3304 N  N   . HIS   A 1 418 ? -5.362  -15.816 14.976 1.00 104.30 ? 714 HIS   A N   1 
ATOM   3305 C  CA  . HIS   A 1 418 ? -5.247  -15.912 13.528 1.00 105.39 ? 714 HIS   A CA  1 
ATOM   3306 C  C   . HIS   A 1 418 ? -3.892  -16.480 13.121 1.00 112.87 ? 714 HIS   A C   1 
ATOM   3307 O  O   . HIS   A 1 418 ? -2.847  -16.041 13.610 1.00 116.91 ? 714 HIS   A O   1 
ATOM   3308 C  CB  . HIS   A 1 418 ? -5.451  -14.531 12.904 1.00 101.16 ? 714 HIS   A CB  1 
ATOM   3309 C  CG  . HIS   A 1 418 ? -5.438  -14.531 11.408 1.00 99.65  ? 714 HIS   A CG  1 
ATOM   3310 N  ND1 . HIS   A 1 418 ? -6.042  -15.516 10.657 1.00 100.29 ? 714 HIS   A ND1 1 
ATOM   3311 C  CD2 . HIS   A 1 418 ? -4.905  -13.656 10.521 1.00 102.22 ? 714 HIS   A CD2 1 
ATOM   3312 C  CE1 . HIS   A 1 418 ? -5.874  -15.253 9.372  1.00 100.79 ? 714 HIS   A CE1 1 
ATOM   3313 N  NE2 . HIS   A 1 418 ? -5.188  -14.129 9.262  1.00 101.31 ? 714 HIS   A NE2 1 
ATOM   3314 N  N   . VAL   A 1 419 ? -3.916  -17.457 12.217 1.00 113.65 ? 715 VAL   A N   1 
ATOM   3315 C  CA  . VAL   A 1 419 ? -2.704  -17.996 11.610 1.00 118.79 ? 715 VAL   A CA  1 
ATOM   3316 C  C   . VAL   A 1 419 ? -2.386  -17.111 10.409 1.00 122.38 ? 715 VAL   A C   1 
ATOM   3317 O  O   . VAL   A 1 419 ? -2.983  -17.252 9.339  1.00 116.99 ? 715 VAL   A O   1 
ATOM   3318 C  CB  . VAL   A 1 419 ? -2.868  -19.467 11.221 1.00 113.90 ? 715 VAL   A CB  1 
ATOM   3319 C  CG1 . VAL   A 1 419 ? -1.640  -19.959 10.470 1.00 119.44 ? 715 VAL   A CG1 1 
ATOM   3320 C  CG2 . VAL   A 1 419 ? -3.110  -20.315 12.467 1.00 102.40 ? 715 VAL   A CG2 1 
ATOM   3321 N  N   . TRP   A 1 420 ? -1.450  -16.186 10.599 1.00 132.04 ? 716 TRP   A N   1 
ATOM   3322 C  CA  . TRP   A 1 420 ? -1.142  -15.163 9.608  1.00 139.98 ? 716 TRP   A CA  1 
ATOM   3323 C  C   . TRP   A 1 420 ? -0.455  -15.786 8.395  1.00 161.28 ? 716 TRP   A C   1 
ATOM   3324 O  O   . TRP   A 1 420 ? -0.419  -17.007 8.215  1.00 162.75 ? 716 TRP   A O   1 
ATOM   3325 C  CB  . TRP   A 1 420 ? -0.259  -14.084 10.235 1.00 135.46 ? 716 TRP   A CB  1 
ATOM   3326 C  CG  . TRP   A 1 420 ? -0.997  -13.025 10.980 1.00 126.95 ? 716 TRP   A CG  1 
ATOM   3327 C  CD1 . TRP   A 1 420 ? -1.424  -13.072 12.278 1.00 121.99 ? 716 TRP   A CD1 1 
ATOM   3328 C  CD2 . TRP   A 1 420 ? -1.375  -11.739 10.479 1.00 123.47 ? 716 TRP   A CD2 1 
ATOM   3329 N  NE1 . TRP   A 1 420 ? -2.050  -11.894 12.612 1.00 116.81 ? 716 TRP   A NE1 1 
ATOM   3330 C  CE2 . TRP   A 1 420 ? -2.031  -11.059 11.524 1.00 120.26 ? 716 TRP   A CE2 1 
ATOM   3331 C  CE3 . TRP   A 1 420 ? -1.223  -11.096 9.247  1.00 125.32 ? 716 TRP   A CE3 1 
ATOM   3332 C  CZ2 . TRP   A 1 420 ? -2.534  -9.769  11.373 1.00 117.64 ? 716 TRP   A CZ2 1 
ATOM   3333 C  CZ3 . TRP   A 1 420 ? -1.723  -9.818  9.101  1.00 122.95 ? 716 TRP   A CZ3 1 
ATOM   3334 C  CH2 . TRP   A 1 420 ? -2.372  -9.168  10.158 1.00 116.96 ? 716 TRP   A CH2 1 
ATOM   3335 N  N   . LYS   A 1 421 ? 0.111   -14.921 7.553  1.00 87.65  ? 717 LYS   A N   1 
ATOM   3336 C  CA  . LYS   A 1 421 ? 0.907   -15.333 6.404  1.00 96.62  ? 717 LYS   A CA  1 
ATOM   3337 C  C   . LYS   A 1 421 ? 1.537   -14.107 5.744  1.00 101.58 ? 717 LYS   A C   1 
ATOM   3338 O  O   . LYS   A 1 421 ? 2.097   -13.224 6.400  1.00 104.09 ? 717 LYS   A O   1 
ATOM   3339 C  CB  . LYS   A 1 421 ? 0.056   -16.103 5.385  1.00 98.11  ? 717 LYS   A CB  1 
ATOM   3340 C  CG  . LYS   A 1 421 ? 0.730   -17.350 4.818  1.00 102.41 ? 717 LYS   A CG  1 
ATOM   3341 C  CD  . LYS   A 1 421 ? 1.068   -18.366 5.911  1.00 105.57 ? 717 LYS   A CD  1 
ATOM   3342 C  CE  . LYS   A 1 421 ? 1.540   -19.696 5.316  1.00 105.96 ? 717 LYS   A CE  1 
ATOM   3343 N  NZ  . LYS   A 1 421 ? 2.726   -20.253 6.036  1.00 102.73 ? 717 LYS   A NZ  1 
HETATM 3344 C  CHA . HEM   B 2 .   ? -25.074 -4.416  26.027 1.00 52.76  ? 801 HEM   A CHA 1 
HETATM 3345 C  CHB . HEM   B 2 .   ? -28.167 -0.690  25.617 1.00 53.68  ? 801 HEM   A CHB 1 
HETATM 3346 C  CHC . HEM   B 2 .   ? -29.311 -2.317  21.176 1.00 51.96  ? 801 HEM   A CHC 1 
HETATM 3347 C  CHD . HEM   B 2 .   ? -27.079 -6.476  22.133 1.00 56.46  ? 801 HEM   A CHD 1 
HETATM 3348 C  C1A . HEM   B 2 .   ? -25.686 -3.190  26.205 1.00 58.02  ? 801 HEM   A C1A 1 
HETATM 3349 C  C2A . HEM   B 2 .   ? -25.265 -2.141  27.116 1.00 60.73  ? 801 HEM   A C2A 1 
HETATM 3350 C  C3A . HEM   B 2 .   ? -26.110 -1.116  27.002 1.00 59.55  ? 801 HEM   A C3A 1 
HETATM 3351 C  C4A . HEM   B 2 .   ? -27.111 -1.467  26.025 1.00 54.43  ? 801 HEM   A C4A 1 
HETATM 3352 C  CMA . HEM   B 2 .   ? -26.049 0.208   27.790 1.00 56.00  ? 801 HEM   A CMA 1 
HETATM 3353 C  CAA . HEM   B 2 .   ? -24.031 -2.199  28.040 1.00 59.01  ? 801 HEM   A CAA 1 
HETATM 3354 C  CBA . HEM   B 2 .   ? -22.796 -2.025  27.152 1.00 55.95  ? 801 HEM   A CBA 1 
HETATM 3355 C  CGA . HEM   B 2 .   ? -21.610 -1.866  28.066 1.00 61.73  ? 801 HEM   A CGA 1 
HETATM 3356 O  O1A . HEM   B 2 .   ? -21.834 -1.495  29.246 1.00 57.64  ? 801 HEM   A O1A 1 
HETATM 3357 O  O2A . HEM   B 2 .   ? -20.461 -2.116  27.612 1.00 59.71  ? 801 HEM   A O2A 1 
HETATM 3358 C  C1B . HEM   B 2 .   ? -28.756 -0.804  24.379 1.00 49.03  ? 801 HEM   A C1B 1 
HETATM 3359 C  C2B . HEM   B 2 .   ? -29.719 0.119   23.809 1.00 48.28  ? 801 HEM   A C2B 1 
HETATM 3360 C  C3B . HEM   B 2 .   ? -30.053 -0.337  22.595 1.00 53.83  ? 801 HEM   A C3B 1 
HETATM 3361 C  C4B . HEM   B 2 .   ? -29.290 -1.558  22.335 1.00 50.22  ? 801 HEM   A C4B 1 
HETATM 3362 C  CMB . HEM   B 2 .   ? -30.290 1.378   24.506 1.00 54.03  ? 801 HEM   A CMB 1 
HETATM 3363 C  CAB . HEM   B 2 .   ? -31.067 0.365   21.667 1.00 58.35  ? 801 HEM   A CAB 1 
HETATM 3364 C  CBB . HEM   B 2 .   ? -31.634 -0.271  20.636 1.00 67.03  ? 801 HEM   A CBB 1 
HETATM 3365 C  C1C . HEM   B 2 .   ? -28.793 -3.573  21.017 1.00 52.25  ? 801 HEM   A C1C 1 
HETATM 3366 C  C2C . HEM   B 2 .   ? -28.869 -4.398  19.818 1.00 52.81  ? 801 HEM   A C2C 1 
HETATM 3367 C  C3C . HEM   B 2 .   ? -28.236 -5.562  20.088 1.00 50.48  ? 801 HEM   A C3C 1 
HETATM 3368 C  C4C . HEM   B 2 .   ? -27.763 -5.491  21.453 1.00 48.70  ? 801 HEM   A C4C 1 
HETATM 3369 C  CMC . HEM   B 2 .   ? -29.546 -3.938  18.508 1.00 50.19  ? 801 HEM   A CMC 1 
HETATM 3370 C  CAC . HEM   B 2 .   ? -28.012 -6.812  19.212 1.00 49.07  ? 801 HEM   A CAC 1 
HETATM 3371 C  CBC . HEM   B 2 .   ? -28.696 -7.043  18.083 1.00 56.50  ? 801 HEM   A CBC 1 
HETATM 3372 C  C1D . HEM   B 2 .   ? -26.311 -6.275  23.242 1.00 56.29  ? 801 HEM   A C1D 1 
HETATM 3373 C  C2D . HEM   B 2 .   ? -25.372 -7.227  23.802 1.00 48.10  ? 801 HEM   A C2D 1 
HETATM 3374 C  C3D . HEM   B 2 .   ? -24.818 -6.655  24.873 1.00 49.27  ? 801 HEM   A C3D 1 
HETATM 3375 C  C4D . HEM   B 2 .   ? -25.386 -5.335  25.038 1.00 52.90  ? 801 HEM   A C4D 1 
HETATM 3376 C  CMD . HEM   B 2 .   ? -25.105 -8.634  23.214 1.00 51.80  ? 801 HEM   A CMD 1 
HETATM 3377 C  CAD . HEM   B 2 .   ? -23.768 -7.276  25.826 1.00 55.79  ? 801 HEM   A CAD 1 
HETATM 3378 C  CBD . HEM   B 2 .   ? -22.463 -7.505  25.084 1.00 65.10  ? 801 HEM   A CBD 1 
HETATM 3379 C  CGD . HEM   B 2 .   ? -21.446 -6.544  25.619 1.00 74.00  ? 801 HEM   A CGD 1 
HETATM 3380 O  O1D . HEM   B 2 .   ? -20.627 -6.971  26.479 1.00 66.71  ? 801 HEM   A O1D 1 
HETATM 3381 O  O2D . HEM   B 2 .   ? -21.476 -5.364  25.184 1.00 74.01  ? 801 HEM   A O2D 1 
HETATM 3382 N  NA  . HEM   B 2 .   ? -26.819 -2.727  25.553 1.00 51.46  ? 801 HEM   A NA  1 
HETATM 3383 N  NB  . HEM   B 2 .   ? -28.504 -1.812  23.449 1.00 46.91  ? 801 HEM   A NB  1 
HETATM 3384 N  NC  . HEM   B 2 .   ? -28.123 -4.273  21.974 1.00 49.39  ? 801 HEM   A NC  1 
HETATM 3385 N  ND  . HEM   B 2 .   ? -26.301 -5.129  24.026 1.00 54.00  ? 801 HEM   A ND  1 
HETATM 3386 FE FE  . HEM   B 2 .   ? -27.773 -3.723  24.035 1.00 55.24  ? 801 HEM   A FE  1 
HETATM 3387 N  N1  . H4B   C 3 .   ? -21.747 -3.164  33.535 1.00 59.70  ? 802 H4B   A N1  1 
HETATM 3388 C  C2  . H4B   C 3 .   ? -21.741 -2.679  32.277 1.00 53.23  ? 802 H4B   A C2  1 
HETATM 3389 N  N2  . H4B   C 3 .   ? -22.894 -2.267  31.724 1.00 44.17  ? 802 H4B   A N2  1 
HETATM 3390 N  N3  . H4B   C 3 .   ? -20.602 -2.599  31.573 1.00 55.01  ? 802 H4B   A N3  1 
HETATM 3391 C  C4  . H4B   C 3 .   ? -19.428 -3.015  32.080 1.00 56.70  ? 802 H4B   A C4  1 
HETATM 3392 O  O4  . H4B   C 3 .   ? -18.366 -2.951  31.395 1.00 51.16  ? 802 H4B   A O4  1 
HETATM 3393 C  C4A . H4B   C 3 .   ? -19.421 -3.527  33.367 1.00 59.69  ? 802 H4B   A C4A 1 
HETATM 3394 C  C8A . H4B   C 3 .   ? -20.600 -3.587  34.097 1.00 61.88  ? 802 H4B   A C8A 1 
HETATM 3395 N  N5  . H4B   C 3 .   ? -18.278 -3.955  33.916 1.00 59.62  ? 802 H4B   A N5  1 
HETATM 3396 N  N8  . H4B   C 3 .   ? -20.628 -4.074  35.367 1.00 60.27  ? 802 H4B   A N8  1 
HETATM 3397 C  C6  . H4B   C 3 .   ? -18.420 -4.938  34.993 1.00 59.85  ? 802 H4B   A C6  1 
HETATM 3398 C  C7  . H4B   C 3 .   ? -19.398 -4.432  36.045 1.00 59.61  ? 802 H4B   A C7  1 
HETATM 3399 C  C9  . H4B   C 3 .   ? -17.084 -5.236  35.657 1.00 51.41  ? 802 H4B   A C9  1 
HETATM 3400 O  O9  . H4B   C 3 .   ? -16.545 -3.972  36.012 1.00 51.43  ? 802 H4B   A O9  1 
HETATM 3401 C  C10 . H4B   C 3 .   ? -17.261 -6.083  36.919 1.00 56.02  ? 802 H4B   A C10 1 
HETATM 3402 C  C11 . H4B   C 3 .   ? -15.965 -6.275  37.708 1.00 53.21  ? 802 H4B   A C11 1 
HETATM 3403 O  O10 . H4B   C 3 .   ? -17.794 -7.361  36.563 1.00 61.47  ? 802 H4B   A O10 1 
HETATM 3404 C  C   . ACT   D 4 .   ? -34.584 1.799   25.158 1.00 121.50 ? 803 ACT   A C   1 
HETATM 3405 O  O   . ACT   D 4 .   ? -34.163 2.964   24.982 1.00 121.68 ? 803 ACT   A O   1 
HETATM 3406 O  OXT . ACT   D 4 .   ? -34.920 1.372   26.284 1.00 121.11 ? 803 ACT   A OXT 1 
HETATM 3407 C  CH3 . ACT   D 4 .   ? -34.586 0.852   23.996 1.00 121.91 ? 803 ACT   A CH3 1 
HETATM 3408 ZN ZN  . ZN    E 5 .   ? -24.233 -16.446 40.690 0.50 51.80  ? 804 ZN    A ZN  1 
HETATM 3409 C  C02 . A1A0E F 6 .   ? -25.556 0.245   23.111 1.00 54.90  ? 805 A1A0E A C02 1 
HETATM 3410 C  C03 . A1A0E F 6 .   ? -26.049 -0.580  22.103 1.00 57.65  ? 805 A1A0E A C03 1 
HETATM 3411 C  C04 . A1A0E F 6 .   ? -25.201 -1.512  21.520 1.00 58.58  ? 805 A1A0E A C04 1 
HETATM 3412 C  C05 . A1A0E F 6 .   ? -23.883 -1.606  21.956 1.00 57.30  ? 805 A1A0E A C05 1 
HETATM 3413 C  C06 . A1A0E F 6 .   ? -23.438 -0.772  22.982 1.00 55.19  ? 805 A1A0E A C06 1 
HETATM 3414 C  C07 . A1A0E F 6 .   ? -25.704 -2.422  20.431 1.00 51.85  ? 805 A1A0E A C07 1 
HETATM 3415 C  C12 . A1A0E F 6 .   ? -21.388 0.436   23.496 1.00 76.63  ? 805 A1A0E A C12 1 
HETATM 3416 C  C13 . A1A0E F 6 .   ? -22.023 -0.798  23.430 1.00 66.10  ? 805 A1A0E A C13 1 
HETATM 3417 C  C14 . A1A0E F 6 .   ? -21.312 -1.956  23.735 1.00 62.37  ? 805 A1A0E A C14 1 
HETATM 3418 C  C15 . A1A0E F 6 .   ? -19.404 -0.540  24.172 1.00 79.92  ? 805 A1A0E A C15 1 
HETATM 3419 C  C16 . A1A0E F 6 .   ? -19.975 -1.804  24.102 1.00 69.83  ? 805 A1A0E A C16 1 
HETATM 3420 C  C17 . A1A0E F 6 .   ? -19.090 -2.974  24.452 1.00 68.55  ? 805 A1A0E A C17 1 
HETATM 3421 C  C19 . A1A0E F 6 .   ? -18.539 -4.545  26.143 1.00 62.48  ? 805 A1A0E A C19 1 
HETATM 3422 N  N01 . A1A0E F 6 .   ? -24.271 0.144   23.496 1.00 49.74  ? 805 A1A0E A N01 1 
HETATM 3423 N  N02 . A1A0E F 6 .   ? -26.352 1.165   23.698 1.00 54.70  ? 805 A1A0E A N02 1 
HETATM 3424 N  N11 . A1A0E F 6 .   ? -20.113 0.548   23.871 1.00 84.79  ? 805 A1A0E A N11 1 
HETATM 3425 N  N18 . A1A0E F 6 .   ? -19.652 -3.809  25.510 1.00 65.65  ? 805 A1A0E A N18 1 
HETATM 3426 O  O   . HOH   G 7 .   ? -14.801 -21.203 9.296  1.00 62.39  ? 901 HOH   A O   1 
HETATM 3427 O  O   . HOH   G 7 .   ? -38.507 -22.688 7.985  1.00 64.94  ? 902 HOH   A O   1 
HETATM 3428 O  O   . HOH   G 7 .   ? -18.477 -1.834  28.893 1.00 51.98  ? 903 HOH   A O   1 
HETATM 3429 O  O   . HOH   G 7 .   ? -29.446 -12.990 40.137 1.00 63.46  ? 904 HOH   A O   1 
HETATM 3430 O  O   . HOH   G 7 .   ? -49.329 -11.965 25.898 1.00 93.00  ? 905 HOH   A O   1 
HETATM 3431 O  O   . HOH   G 7 .   ? -14.986 3.469   21.727 1.00 93.44  ? 906 HOH   A O   1 
HETATM 3432 O  O   . HOH   G 7 .   ? -24.631 -10.917 37.395 1.00 61.02  ? 907 HOH   A O   1 
HETATM 3433 O  O   . HOH   G 7 .   ? -28.364 1.045   15.271 1.00 50.73  ? 908 HOH   A O   1 
HETATM 3434 O  O   . HOH   G 7 .   ? -15.973 -29.781 19.085 1.00 88.00  ? 909 HOH   A O   1 
HETATM 3435 O  O   . HOH   G 7 .   ? -19.403 -8.406  34.408 1.00 63.45  ? 910 HOH   A O   1 
HETATM 3436 O  O   . HOH   G 7 .   ? -27.653 -13.277 23.618 1.00 56.94  ? 911 HOH   A O   1 
HETATM 3437 O  O   . HOH   G 7 .   ? -25.291 -4.226  5.899  1.00 59.02  ? 912 HOH   A O   1 
HETATM 3438 O  O   . HOH   G 7 .   ? -26.438 -34.855 13.719 1.00 78.23  ? 913 HOH   A O   1 
HETATM 3439 O  O   . HOH   G 7 .   ? -26.503 7.042   20.212 1.00 71.69  ? 914 HOH   A O   1 
HETATM 3440 O  O   . HOH   G 7 .   ? -29.527 -15.514 27.947 1.00 56.58  ? 915 HOH   A O   1 
HETATM 3441 O  O   . HOH   G 7 .   ? -35.503 -35.916 0.379  1.00 85.40  ? 916 HOH   A O   1 
HETATM 3442 O  O   . HOH   G 7 .   ? -20.036 -14.582 10.524 1.00 64.50  ? 917 HOH   A O   1 
HETATM 3443 O  O   . HOH   G 7 .   ? -34.990 6.513   37.409 1.00 79.25  ? 918 HOH   A O   1 
HETATM 3444 O  O   . HOH   G 7 .   ? -18.981 -9.925  15.074 1.00 66.13  ? 919 HOH   A O   1 
HETATM 3445 O  O   . HOH   G 7 .   ? -34.697 -12.043 35.633 1.00 63.13  ? 920 HOH   A O   1 
HETATM 3446 O  O   . HOH   G 7 .   ? -16.222 -1.994  22.378 1.00 67.25  ? 921 HOH   A O   1 
HETATM 3447 O  O   . HOH   G 7 .   ? -17.196 -16.577 9.297  1.00 67.46  ? 922 HOH   A O   1 
HETATM 3448 O  O   . HOH   G 7 .   ? -24.029 2.607   31.024 1.00 54.25  ? 923 HOH   A O   1 
HETATM 3449 O  O   . HOH   G 7 .   ? -26.969 -2.855  29.628 1.00 54.75  ? 924 HOH   A O   1 
HETATM 3450 O  O   . HOH   G 7 .   ? -21.544 -10.149 35.186 1.00 65.14  ? 925 HOH   A O   1 
HETATM 3451 O  O   . HOH   G 7 .   ? -37.163 3.246   9.024  1.00 81.65  ? 926 HOH   A O   1 
HETATM 3452 O  O   . HOH   G 7 .   ? -21.808 1.176   29.880 1.00 50.26  ? 927 HOH   A O   1 
HETATM 3453 O  O   . HOH   G 7 .   ? -25.787 -3.976  1.980  1.00 91.71  ? 928 HOH   A O   1 
HETATM 3454 O  O   . HOH   G 7 .   ? -28.392 -10.780 37.697 1.00 61.12  ? 929 HOH   A O   1 
HETATM 3455 O  O   . HOH   G 7 .   ? -24.104 -2.122  37.828 1.00 52.56  ? 930 HOH   A O   1 
HETATM 3456 O  O   . HOH   G 7 .   ? -23.235 -0.803  34.448 1.00 51.18  ? 931 HOH   A O   1 
HETATM 3457 O  O   . HOH   G 7 .   ? -22.111 -13.589 27.597 1.00 81.40  ? 932 HOH   A O   1 
HETATM 3458 O  O   . HOH   G 7 .   ? -12.719 -1.062  17.401 1.00 63.19  ? 933 HOH   A O   1 
HETATM 3459 O  O   . HOH   G 7 .   ? -28.739 -15.002 1.347  1.00 85.11  ? 934 HOH   A O   1 
HETATM 3460 O  O   . HOH   G 7 .   ? -30.948 -8.771  4.056  1.00 61.90  ? 935 HOH   A O   1 
HETATM 3461 O  O   . HOH   G 7 .   ? -20.636 -8.419  16.868 1.00 55.45  ? 936 HOH   A O   1 
HETATM 3462 O  O   . HOH   G 7 .   ? -18.387 2.988   23.801 1.00 53.24  ? 937 HOH   A O   1 
HETATM 3463 O  O   . HOH   G 7 .   ? -43.376 -14.698 23.209 1.00 74.54  ? 938 HOH   A O   1 
HETATM 3464 O  O   . HOH   G 7 .   ? -17.192 -18.234 21.199 1.00 80.56  ? 939 HOH   A O   1 
HETATM 3465 O  O   . HOH   G 7 .   ? -29.374 22.648  18.788 1.00 86.39  ? 940 HOH   A O   1 
HETATM 3466 O  O   . HOH   G 7 .   ? -11.352 12.042  12.674 1.00 71.51  ? 941 HOH   A O   1 
HETATM 3467 O  O   . HOH   G 7 .   ? -25.200 -10.492 27.287 1.00 51.66  ? 942 HOH   A O   1 
HETATM 3468 O  O   . HOH   G 7 .   ? -28.401 1.707   3.503  1.00 74.00  ? 943 HOH   A O   1 
HETATM 3469 O  O   . HOH   G 7 .   ? -28.029 23.769  20.697 1.00 98.37  ? 944 HOH   A O   1 
HETATM 3470 O  O   . HOH   G 7 .   ? -44.134 -12.247 23.265 1.00 91.63  ? 945 HOH   A O   1 
HETATM 3471 O  O   . HOH   G 7 .   ? -35.954 -7.657  9.447  1.00 62.32  ? 946 HOH   A O   1 
HETATM 3472 O  O   . HOH   G 7 .   ? -25.208 0.415   32.154 1.00 56.94  ? 947 HOH   A O   1 
HETATM 3473 O  O   . HOH   G 7 .   ? -38.708 -12.213 12.724 1.00 79.42  ? 948 HOH   A O   1 
HETATM 3474 O  O   . HOH   G 7 .   ? -18.098 1.476   28.200 1.00 90.06  ? 949 HOH   A O   1 
HETATM 3475 O  O   . HOH   G 7 .   ? -43.290 -12.431 21.103 1.00 81.26  ? 950 HOH   A O   1 
HETATM 3476 O  O   . HOH   G 7 .   ? -27.224 -16.577 1.679  1.00 68.56  ? 951 HOH   A O   1 
HETATM 3477 O  O   . HOH   G 7 .   ? -31.592 -0.152  3.364  1.00 79.41  ? 952 HOH   A O   1 
# 
loop_
_atom_site_anisotrop.id 
_atom_site_anisotrop.type_symbol 
_atom_site_anisotrop.pdbx_label_atom_id 
_atom_site_anisotrop.pdbx_label_alt_id 
_atom_site_anisotrop.pdbx_label_comp_id 
_atom_site_anisotrop.pdbx_label_asym_id 
_atom_site_anisotrop.pdbx_label_seq_id 
_atom_site_anisotrop.pdbx_PDB_ins_code 
_atom_site_anisotrop.U[1][1] 
_atom_site_anisotrop.U[2][2] 
_atom_site_anisotrop.U[3][3] 
_atom_site_anisotrop.U[1][2] 
_atom_site_anisotrop.U[1][3] 
_atom_site_anisotrop.U[2][3] 
_atom_site_anisotrop.pdbx_auth_seq_id 
_atom_site_anisotrop.pdbx_auth_comp_id 
_atom_site_anisotrop.pdbx_auth_asym_id 
_atom_site_anisotrop.pdbx_auth_atom_id 
1    N N   . ARG A 3   ? 1.9564 1.9359 1.6601 -0.5700 0.0369  0.0574  299 ARG A N   
2    C CA  . ARG A 3   ? 1.9780 1.9219 1.6718 -0.5711 0.0272  0.0494  299 ARG A CA  
3    C C   . ARG A 3   ? 1.8132 1.8868 1.5852 -0.5625 0.0271  0.0401  299 ARG A C   
4    O O   . ARG A 3   ? 1.8453 1.9073 1.6252 -0.5562 0.0194  0.0329  299 ARG A O   
5    C CB  . ARG A 3   ? 2.1606 2.0342 1.7678 -0.6160 0.0247  0.0498  299 ARG A CB  
6    C CG  . ARG A 3   ? 2.2564 2.0248 1.8153 -0.6098 0.0145  0.0452  299 ARG A CG  
7    C CD  . ARG A 3   ? 2.3040 1.9524 1.8311 -0.5680 0.0093  0.0495  299 ARG A CD  
8    N NE  . ARG A 3   ? 2.2210 1.8869 1.8097 -0.5255 0.0037  0.0440  299 ARG A NE  
9    C CZ  . ARG A 3   ? 2.2299 1.8410 1.8012 -0.5111 -0.0045 0.0372  299 ARG A CZ  
10   N NH1 . ARG A 3   ? 2.3275 1.8606 1.8196 -0.5348 -0.0076 0.0354  299 ARG A NH1 
11   N NH2 . ARG A 3   ? 2.1369 1.7700 1.7654 -0.4743 -0.0097 0.0319  299 ARG A NH2 
12   N N   . PHE A 4   ? 1.6264 1.8234 1.4517 -0.5581 0.0358  0.0401  300 PHE A N   
13   C CA  . PHE A 4   ? 1.4298 1.7590 1.3232 -0.5423 0.0363  0.0319  300 PHE A CA  
14   C C   . PHE A 4   ? 1.3259 1.7362 1.2810 -0.5015 0.0436  0.0325  300 PHE A C   
15   O O   . PHE A 4   ? 1.3720 1.8849 1.3502 -0.4993 0.0523  0.0327  300 PHE A O   
16   C CB  . PHE A 4   ? 1.4291 1.8336 1.3040 -0.5826 0.0391  0.0305  300 PHE A CB  
17   C CG  . PHE A 4   ? 1.5335 1.8394 1.3234 -0.6330 0.0348  0.0330  300 PHE A CG  
18   C CD1 . PHE A 4   ? 1.5961 1.8629 1.3256 -0.6706 0.0397  0.0401  300 PHE A CD1 
19   C CD2 . PHE A 4   ? 1.5471 1.7933 1.3113 -0.6413 0.0257  0.0280  300 PHE A CD2 
20   C CE1 . PHE A 4   ? 1.6827 1.8506 1.3238 -0.7156 0.0351  0.0417  300 PHE A CE1 
21   C CE2 . PHE A 4   ? 1.6624 1.8108 1.3388 -0.6850 0.0219  0.0298  300 PHE A CE2 
22   C CZ  . PHE A 4   ? 1.7451 1.8524 1.3577 -0.7221 0.0263  0.0365  300 PHE A CZ  
23   N N   . LEU A 5   ? 1.2079 1.5619 1.1817 -0.4553 0.0376  0.0309  301 LEU A N   
24   C CA  . LEU A 5   ? 1.0639 1.4192 1.0575 -0.4033 0.0400  0.0319  301 LEU A CA  
25   C C   . LEU A 5   ? 0.9440 1.4178 0.9963 -0.3625 0.0439  0.0250  301 LEU A C   
26   O O   . LEU A 5   ? 0.8457 1.3862 0.9321 -0.3545 0.0406  0.0181  301 LEU A O   
27   C CB  . LEU A 5   ? 1.0202 1.2707 1.0066 -0.3595 0.0287  0.0306  301 LEU A CB  
28   C CG  . LEU A 5   ? 1.1292 1.2575 1.0525 -0.3857 0.0235  0.0365  301 LEU A CG  
29   C CD1 . LEU A 5   ? 1.1548 1.2180 1.0844 -0.3481 0.0113  0.0316  301 LEU A CD1 
30   C CD2 . LEU A 5   ? 1.1888 1.2570 1.0682 -0.3884 0.0275  0.0461  301 LEU A CD2 
31   N N   . LYS A 6   ? 0.8966 1.3889 0.9537 -0.3321 0.0502  0.0267  302 LYS A N   
32   C CA  . LYS A 6   ? 0.8563 1.4423 0.9530 -0.2846 0.0544  0.0202  302 LYS A CA  
33   C C   . LYS A 6   ? 0.7689 1.2897 0.8723 -0.2253 0.0453  0.0156  302 LYS A C   
34   O O   . LYS A 6   ? 0.6735 1.1063 0.7517 -0.2197 0.0416  0.0197  302 LYS A O   
35   C CB  . LYS A 6   ? 0.9661 1.6251 1.0564 -0.2925 0.0692  0.0244  302 LYS A CB  
36   C CG  . LYS A 6   ? 1.0966 1.8083 1.1678 -0.3638 0.0793  0.0318  302 LYS A CG  
37   C CD  . LYS A 6   ? 1.1140 1.9522 1.2184 -0.3793 0.0813  0.0268  302 LYS A CD  
38   C CE  . LYS A 6   ? 1.1762 2.0199 1.2385 -0.4390 0.0810  0.0306  302 LYS A CE  
39   N NZ  . LYS A 6   ? 1.1695 2.0642 1.2149 -0.4511 0.0925  0.0357  302 LYS A NZ  
40   N N   . VAL A 7   ? 0.6746 1.2390 0.8074 -0.1830 0.0413  0.0075  303 VAL A N   
41   C CA  . VAL A 7   ? 0.6829 1.1970 0.8157 -0.1294 0.0340  0.0027  303 VAL A CA  
42   C C   . VAL A 7   ? 0.7023 1.2920 0.8411 -0.0867 0.0415  -0.0024 303 VAL A C   
43   O O   . VAL A 7   ? 0.6898 1.3793 0.8492 -0.0816 0.0469  -0.0056 303 VAL A O   
44   C CB  . VAL A 7   ? 0.6826 1.1573 0.8293 -0.1136 0.0216  -0.0020 303 VAL A CB  
45   C CG1 . VAL A 7   ? 0.6556 1.0661 0.7926 -0.1524 0.0158  0.0023  303 VAL A CG1 
46   C CG2 . VAL A 7   ? 0.7400 1.3007 0.9129 -0.0992 0.0219  -0.0079 303 VAL A CG2 
47   N N   . LYS A 8   ? 0.6212 1.1658 0.7378 -0.0551 0.0417  -0.0034 304 LYS A N   
48   C CA  . LYS A 8   ? 0.6759 1.2764 0.7842 -0.0102 0.0495  -0.0087 304 LYS A CA  
49   C C   . LYS A 8   ? 0.6914 1.2326 0.7825 0.0422  0.0396  -0.0161 304 LYS A C   
50   O O   . LYS A 8   ? 0.7506 1.1991 0.8310 0.0388  0.0282  -0.0155 304 LYS A O   
51   C CB  . LYS A 8   ? 0.7702 1.3654 0.8540 -0.0162 0.0590  -0.0046 304 LYS A CB  
52   C CG  . LYS A 8   ? 0.8060 1.4597 0.8746 0.0335  0.0687  -0.0106 304 LYS A CG  
53   C CD  . LYS A 8   ? 0.8881 1.5479 0.9337 0.0224  0.0799  -0.0060 304 LYS A CD  
54   C CE  . LYS A 8   ? 0.9427 1.6451 0.9645 0.0806  0.0886  -0.0136 304 LYS A CE  
55   N NZ  . LYS A 8   ? 1.0207 1.7401 1.0201 0.0708  0.1011  -0.0094 304 LYS A NZ  
56   N N   . ASN A 9   ? 0.6626 1.2592 0.7465 0.0905  0.0438  -0.0227 305 ASN A N   
57   C CA  . ASN A 9   ? 0.7480 1.2771 0.7944 0.1435  0.0364  -0.0298 305 ASN A CA  
58   C C   . ASN A 9   ? 0.7481 1.2713 0.7564 0.1727  0.0446  -0.0324 305 ASN A C   
59   O O   . ASN A 9   ? 0.8693 1.4877 0.8840 0.1844  0.0580  -0.0328 305 ASN A O   
60   C CB  . ASN A 9   ? 0.8003 1.3762 0.8493 0.1865  0.0341  -0.0358 305 ASN A CB  
61   C CG  . ASN A 9   ? 0.8663 1.3517 0.8609 0.2395  0.0256  -0.0425 305 ASN A CG  
62   O OD1 . ASN A 9   ? 0.9352 1.3795 0.8836 0.2696  0.0284  -0.0462 305 ASN A OD1 
63   N ND2 . ASN A 9   ? 0.8166 1.2634 0.8092 0.2486  0.0149  -0.0440 305 ASN A ND2 
64   N N   . TRP A 10  ? 0.6923 1.1091 0.6601 0.1814  0.0366  -0.0342 306 TRP A N   
65   C CA  . TRP A 10  ? 0.8139 1.2104 0.7399 0.2031  0.0430  -0.0368 306 TRP A CA  
66   C C   . TRP A 10  ? 0.9381 1.2996 0.8066 0.2686  0.0418  -0.0468 306 TRP A C   
67   O O   . TRP A 10  ? 1.0993 1.4210 0.9196 0.2916  0.0449  -0.0509 306 TRP A O   
68   C CB  . TRP A 10  ? 0.8900 1.1945 0.7998 0.1698  0.0348  -0.0326 306 TRP A CB  
69   C CG  . TRP A 10  ? 0.8116 1.1413 0.7604 0.1147  0.0375  -0.0226 306 TRP A CG  
70   C CD1 . TRP A 10  ? 0.7657 1.0756 0.7461 0.0777  0.0294  -0.0171 306 TRP A CD1 
71   C CD2 . TRP A 10  ? 0.8545 1.2250 0.8051 0.0919  0.0493  -0.0166 306 TRP A CD2 
72   N NE1 . TRP A 10  ? 0.6680 0.9950 0.6635 0.0355  0.0347  -0.0084 306 TRP A NE1 
73   C CE2 . TRP A 10  ? 0.8209 1.1843 0.7985 0.0408  0.0469  -0.0074 306 TRP A CE2 
74   C CE3 . TRP A 10  ? 0.8205 1.2298 0.7470 0.1106  0.0620  -0.0181 306 TRP A CE3 
75   C CZ2 . TRP A 10  ? 0.8452 1.2306 0.8213 0.0056  0.0561  0.0011  306 TRP A CZ2 
76   C CZ3 . TRP A 10  ? 0.9354 1.3772 0.8678 0.0734  0.0721  -0.0094 306 TRP A CZ3 
77   C CH2 . TRP A 10  ? 0.9447 1.3708 0.8996 0.0201  0.0687  0.0004  306 TRP A CH2 
78   N N   . GLU A 11  ? 0.9818 1.3492 0.8469 0.3003  0.0369  -0.0511 307 GLU A N   
79   C CA  . GLU A 11  ? 1.0486 1.3910 0.8523 0.3705  0.0371  -0.0603 307 GLU A CA  
80   C C   . GLU A 11  ? 1.1171 1.5944 0.9409 0.4125  0.0501  -0.0628 307 GLU A C   
81   O O   . GLU A 11  ? 1.1991 1.6881 0.9730 0.4737  0.0572  -0.0699 307 GLU A O   
82   C CB  . GLU A 11  ? 1.0666 1.3145 0.8388 0.3834  0.0219  -0.0629 307 GLU A CB  
83   C CG  . GLU A 11  ? 1.1463 1.3042 0.8244 0.4485  0.0176  -0.0721 307 GLU A CG  
84   C CD  . GLU A 11  ? 1.3181 1.4359 0.9724 0.4762  0.0077  -0.0740 307 GLU A CD  
85   O OE1 . GLU A 11  ? 1.3758 1.5259 0.9953 0.5424  0.0118  -0.0794 307 GLU A OE1 
86   O OE2 . GLU A 11  ? 1.3150 1.3728 0.9828 0.4347  -0.0038 -0.0697 307 GLU A OE2 
87   N N   . THR A 12  ? 1.0506 1.6332 0.9436 0.3806  0.0533  -0.0574 308 THR A N   
88   C CA  . THR A 12  ? 0.9905 1.7235 0.9123 0.4102  0.0648  -0.0587 308 THR A CA  
89   C C   . THR A 12  ? 0.9123 1.7663 0.8860 0.3623  0.0794  -0.0521 308 THR A C   
90   O O   . THR A 12  ? 0.8659 1.8613 0.8621 0.3834  0.0908  -0.0530 308 THR A O   
91   C CB  . THR A 12  ? 0.9158 1.6893 0.8705 0.4110  0.0566  -0.0581 308 THR A CB  
92   O OG1 . THR A 12  ? 0.8754 1.6375 0.8819 0.3354  0.0510  -0.0507 308 THR A OG1 
93   C CG2 . THR A 12  ? 0.9970 1.6532 0.8920 0.4605  0.0434  -0.0638 308 THR A CG2 
94   N N   . ASP A 13  ? 0.9565 1.7612 0.9455 0.2986  0.0790  -0.0451 309 ASP A N   
95   C CA  . ASP A 13  ? 1.0038 1.8997 1.0323 0.2421  0.0913  -0.0371 309 ASP A CA  
96   C C   . ASP A 13  ? 0.9699 1.9640 1.0541 0.1989  0.0915  -0.0325 309 ASP A C   
97   O O   . ASP A 13  ? 0.9944 2.0870 1.1068 0.1538  0.1029  -0.0265 309 ASP A O   
98   C CB  . ASP A 13  ? 1.1061 2.0978 1.1193 0.2738  0.1090  -0.0391 309 ASP A CB  
99   C CG  . ASP A 13  ? 1.2378 2.1317 1.1981 0.2919  0.1105  -0.0413 309 ASP A CG  
100  O OD1 . ASP A 13  ? 1.2680 2.0933 1.2296 0.2393  0.1077  -0.0345 309 ASP A OD1 
101  O OD2 . ASP A 13  ? 1.3319 2.2136 1.2439 0.3605  0.1138  -0.0500 309 ASP A OD2 
102  N N   . VAL A 14  ? 0.9840 1.9504 1.0800 0.2073  0.0789  -0.0351 310 VAL A N   
103  C CA  . VAL A 14  ? 0.8868 1.9360 1.0305 0.1646  0.0772  -0.0316 310 VAL A CA  
104  C C   . VAL A 14  ? 0.9040 1.8862 1.0622 0.0877  0.0729  -0.0237 310 VAL A C   
105  O O   . VAL A 14  ? 0.9581 1.8122 1.0962 0.0806  0.0638  -0.0226 310 VAL A O   
106  C CB  . VAL A 14  ? 0.7908 1.8291 0.9370 0.2035  0.0650  -0.0372 310 VAL A CB  
107  C CG1 . VAL A 14  ? 0.7314 1.8430 0.9239 0.1536  0.0614  -0.0340 310 VAL A CG1 
108  C CG2 . VAL A 14  ? 0.7928 1.8919 0.9127 0.2818  0.0675  -0.0438 310 VAL A CG2 
109  N N   . VAL A 15  ? 0.8293 1.8985 1.0166 0.0299  0.0793  -0.0182 311 VAL A N   
110  C CA  . VAL A 15  ? 0.7665 1.7711 0.9573 -0.0417 0.0752  -0.0109 311 VAL A CA  
111  C C   . VAL A 15  ? 0.7739 1.8262 0.9931 -0.0734 0.0686  -0.0114 311 VAL A C   
112  O O   . VAL A 15  ? 0.8225 1.9831 1.0565 -0.0636 0.0700  -0.0142 311 VAL A O   
113  C CB  . VAL A 15  ? 0.7015 1.7390 0.8827 -0.0940 0.0884  -0.0026 311 VAL A CB  
114  C CG1 . VAL A 15  ? 0.6272 1.5730 0.7956 -0.1612 0.0829  0.0050  311 VAL A CG1 
115  C CG2 . VAL A 15  ? 0.6881 1.6883 0.8405 -0.0583 0.0952  -0.0028 311 VAL A CG2 
116  N N   . LEU A 16  ? 0.6995 1.6508 0.9138 -0.1068 0.0579  -0.0092 312 LEU A N   
117  C CA  . LEU A 16  ? 0.7113 1.6878 0.9437 -0.1459 0.0513  -0.0096 312 LEU A CA  
118  C C   . LEU A 16  ? 0.6830 1.5753 0.8936 -0.2125 0.0495  -0.0027 312 LEU A C   
119  O O   . LEU A 16  ? 0.6635 1.4483 0.8487 -0.2120 0.0477  0.0010  312 LEU A O   
120  C CB  . LEU A 16  ? 0.7172 1.6480 0.9584 -0.1050 0.0380  -0.0159 312 LEU A CB  
121  C CG  . LEU A 16  ? 0.7912 1.8078 1.0448 -0.0401 0.0386  -0.0224 312 LEU A CG  
122  C CD1 . LEU A 16  ? 0.8669 1.8239 1.1196 -0.0029 0.0254  -0.0273 312 LEU A CD1 
123  C CD2 . LEU A 16  ? 0.8439 1.9753 1.1021 -0.0566 0.0420  -0.0223 312 LEU A CD2 
124  N N   . THR A 17  ? 0.6564 1.5852 0.8656 -0.2659 0.0484  -0.0013 313 THR A N   
125  C CA  . THR A 17  ? 0.6723 1.5128 0.8449 -0.3287 0.0464  0.0048  313 THR A CA  
126  C C   . THR A 17  ? 0.7283 1.4968 0.9001 -0.3360 0.0338  0.0012  313 THR A C   
127  O O   . THR A 17  ? 0.6919 1.5020 0.8774 -0.3253 0.0275  -0.0044 313 THR A O   
128  C CB  . THR A 17  ? 0.7387 1.6204 0.8795 -0.3773 0.0498  0.0077  313 THR A CB  
129  O OG1 . THR A 17  ? 0.6901 1.6447 0.8317 -0.3692 0.0609  0.0106  313 THR A OG1 
130  C CG2 . THR A 17  ? 0.8257 1.5974 0.9134 -0.4369 0.0474  0.0137  313 THR A CG2 
131  N N   . ASP A 18  ? 0.7311 1.3746 0.8742 -0.3444 0.0290  0.0045  314 ASP A N   
132  C CA  . ASP A 18  ? 0.7691 1.3304 0.9032 -0.3445 0.0173  0.0012  314 ASP A CA  
133  C C   . ASP A 18  ? 0.8318 1.3339 0.9177 -0.4105 0.0165  0.0051  314 ASP A C   
134  O O   . ASP A 18  ? 0.8457 1.2737 0.8875 -0.4347 0.0203  0.0123  314 ASP A O   
135  C CB  . ASP A 18  ? 0.7577 1.2163 0.8850 -0.2989 0.0112  0.0015  314 ASP A CB  
136  C CG  . ASP A 18  ? 0.7231 1.1200 0.8505 -0.2870 0.0002  -0.0029 314 ASP A CG  
137  O OD1 . ASP A 18  ? 0.7420 1.0805 0.8360 -0.3240 -0.0029 -0.0018 314 ASP A OD1 
138  O OD2 . ASP A 18  ? 0.6801 1.0830 0.8346 -0.2417 -0.0051 -0.0075 314 ASP A OD2 
139  N N   . THR A 19  ? 0.7818 1.2945 0.8596 -0.4250 0.0108  0.0003  315 THR A N   
140  C CA  . THR A 19  ? 0.8682 1.2882 0.8852 -0.4676 0.0067  0.0016  315 THR A CA  
141  C C   . THR A 19  ? 0.8792 1.2328 0.8949 -0.4542 -0.0038 -0.0041 315 THR A C   
142  O O   . THR A 19  ? 0.9111 1.1660 0.8698 -0.4797 -0.0076 -0.0035 315 THR A O   
143  C CB  . THR A 19  ? 0.9466 1.4256 0.9395 -0.5067 0.0088  0.0010  315 THR A CB  
144  O OG1 . THR A 19  ? 0.9448 1.5302 0.9861 -0.4825 0.0064  -0.0053 315 THR A OG1 
145  C CG2 . THR A 19  ? 0.9615 1.4835 0.9362 -0.5315 0.0186  0.0074  315 THR A CG2 
146  N N   . LEU A 20  ? 0.7601 1.1624 0.8312 -0.4126 -0.0086 -0.0099 316 LEU A N   
147  C CA  . LEU A 20  ? 0.8018 1.1496 0.8744 -0.3985 -0.0186 -0.0157 316 LEU A CA  
148  C C   . LEU A 20  ? 0.8876 1.1033 0.9186 -0.3835 -0.0212 -0.0125 316 LEU A C   
149  O O   . LEU A 20  ? 0.9665 1.1101 0.9689 -0.3851 -0.0277 -0.0160 316 LEU A O   
150  C CB  . LEU A 20  ? 0.6938 1.1039 0.8230 -0.3415 -0.0220 -0.0205 316 LEU A CB  
151  C CG  . LEU A 20  ? 0.7102 1.0809 0.8447 -0.3187 -0.0313 -0.0263 316 LEU A CG  
152  C CD1 . LEU A 20  ? 0.7440 1.1313 0.8603 -0.3630 -0.0357 -0.0311 316 LEU A CD1 
153  C CD2 . LEU A 20  ? 0.5988 1.0248 0.7789 -0.2644 -0.0337 -0.0292 316 LEU A CD2 
154  N N   . HIS A 21  ? 0.8600 1.0456 0.8844 -0.3654 -0.0164 -0.0061 317 HIS A N   
155  C CA  . HIS A 21  ? 0.8123 0.8842 0.7975 -0.3460 -0.0195 -0.0024 317 HIS A CA  
156  C C   . HIS A 21  ? 0.8978 0.8736 0.8074 -0.3884 -0.0210 -0.0005 317 HIS A C   
157  O O   . HIS A 21  ? 0.8819 0.7596 0.7519 -0.3666 -0.0254 0.0006  317 HIS A O   
158  C CB  . HIS A 21  ? 0.8289 0.8938 0.8158 -0.3262 -0.0145 0.0047  317 HIS A CB  
159  C CG  . HIS A 21  ? 0.8503 0.9142 0.7999 -0.3719 -0.0065 0.0115  317 HIS A CG  
160  N ND1 . HIS A 21  ? 0.8572 1.0239 0.8331 -0.3971 0.0014  0.0119  317 HIS A ND1 
161  C CD2 . HIS A 21  ? 0.9805 0.9533 0.8632 -0.3974 -0.0049 0.0187  317 HIS A CD2 
162  C CE1 . HIS A 21  ? 0.9590 1.1023 0.8889 -0.4413 0.0082  0.0193  317 HIS A CE1 
163  N NE2 . HIS A 21  ? 1.0063 1.0254 0.8758 -0.4430 0.0043  0.0237  317 HIS A NE2 
164  N N   . LEU A 22  ? 0.9536 0.9551 0.8367 -0.4484 -0.0175 0.0000  318 LEU A N   
165  C CA  . LEU A 22  ? 1.1820 1.0835 0.9811 -0.4814 -0.0192 0.0012  318 LEU A CA  
166  C C   . LEU A 22  ? 1.2185 1.0709 1.0016 -0.4716 -0.0277 -0.0070 318 LEU A C   
167  O O   . LEU A 22  ? 1.2209 0.9549 0.9318 -0.4707 -0.0312 -0.0068 318 LEU A O   
168  C CB  . LEU A 22  ? 1.2402 1.1956 1.0169 -0.5268 -0.0134 0.0034  318 LEU A CB  
169  C CG  . LEU A 22  ? 1.1960 1.2035 0.9808 -0.5407 -0.0041 0.0110  318 LEU A CG  
170  C CD1 . LEU A 22  ? 1.2293 1.2950 0.9878 -0.5882 0.0005  0.0121  318 LEU A CD1 
171  C CD2 . LEU A 22  ? 1.2764 1.1720 1.0052 -0.5364 -0.0027 0.0191  318 LEU A CD2 
172  N N   . LYS A 23  ? 1.1827 1.1227 1.0273 -0.4604 -0.0311 -0.0144 319 LYS A N   
173  C CA  . LYS A 23  ? 1.2022 1.1000 1.0352 -0.4493 -0.0391 -0.0225 319 LYS A CA  
174  C C   . LYS A 23  ? 1.2122 1.0475 1.0508 -0.3920 -0.0425 -0.0230 319 LYS A C   
175  O O   . LYS A 23  ? 1.3076 1.0923 1.1254 -0.3757 -0.0479 -0.0289 319 LYS A O   
176  C CB  . LYS A 23  ? 1.1057 1.1164 1.0013 -0.4454 -0.0417 -0.0292 319 LYS A CB  
177  C CG  . LYS A 23  ? 1.1332 1.2367 1.0369 -0.4777 -0.0368 -0.0274 319 LYS A CG  
178  C CD  . LYS A 23  ? 1.3226 1.3635 1.1466 -0.5244 -0.0362 -0.0260 319 LYS A CD  
179  C CE  . LYS A 23  ? 1.4274 1.4479 1.2308 -0.5329 -0.0433 -0.0334 319 LYS A CE  
180  N NZ  . LYS A 23  ? 1.4082 1.5538 1.2637 -0.5366 -0.0444 -0.0370 319 LYS A NZ  
181  N N   . SER A 24  ? 1.2010 1.0445 1.0656 -0.3566 -0.0390 -0.0166 320 SER A N   
182  C CA  . SER A 24  ? 1.2090 1.0121 1.0835 -0.2992 -0.0419 -0.0159 320 SER A CA  
183  C C   . SER A 24  ? 1.3081 0.9884 1.1028 -0.2926 -0.0450 -0.0157 320 SER A C   
184  O O   . SER A 24  ? 1.2903 0.8956 1.0143 -0.3242 -0.0434 -0.0117 320 SER A O   
185  C CB  . SER A 24  ? 1.2119 1.0416 1.1178 -0.2715 -0.0385 -0.0089 320 SER A CB  
186  O OG  . SER A 24  ? 1.2652 1.0436 1.1617 -0.2262 -0.0419 -0.0068 320 SER A OG  
187  N N   . THR A 25  ? 1.4336 1.0918 1.2343 -0.2495 -0.0491 -0.0197 321 THR A N   
188  C CA  . THR A 25  ? 1.6263 1.1742 1.3506 -0.2317 -0.0521 -0.0213 321 THR A CA  
189  C C   . THR A 25  ? 1.5361 1.0630 1.2634 -0.1732 -0.0531 -0.0166 321 THR A C   
190  O O   . THR A 25  ? 1.5510 0.9922 1.2110 -0.1605 -0.0536 -0.0116 321 THR A O   
191  C CB  . THR A 25  ? 1.7191 1.2603 1.4368 -0.2322 -0.0558 -0.0312 321 THR A CB  
192  O OG1 . THR A 25  ? 1.7969 1.2549 1.4614 -0.1897 -0.0582 -0.0334 321 THR A OG1 
193  C CG2 . THR A 25  ? 1.6212 1.2744 1.4308 -0.2169 -0.0563 -0.0347 321 THR A CG2 
194  N N   . LEU A 26  ? 1.3878 0.9925 1.1874 -0.1386 -0.0539 -0.0175 322 LEU A N   
195  C CA  . LEU A 26  ? 1.3677 0.9704 1.1749 -0.0863 -0.0558 -0.0138 322 LEU A CA  
196  C C   . LEU A 26  ? 1.3535 0.9656 1.1685 -0.0801 -0.0549 -0.0048 322 LEU A C   
197  O O   . LEU A 26  ? 1.3011 0.9303 1.1244 -0.1139 -0.0518 -0.0017 322 LEU A O   
198  C CB  . LEU A 26  ? 1.2702 0.9547 1.1475 -0.0625 -0.0569 -0.0171 322 LEU A CB  
199  C CG  . LEU A 26  ? 1.2679 0.9486 1.1403 -0.0645 -0.0577 -0.0257 322 LEU A CG  
200  C CD1 . LEU A 26  ? 1.1888 0.9561 1.1328 -0.0533 -0.0580 -0.0274 322 LEU A CD1 
201  C CD2 . LEU A 26  ? 1.3195 0.9262 1.1290 -0.0297 -0.0589 -0.0281 322 LEU A CD2 
202  N N   . GLU A 27  ? 1.3513 0.9594 1.1636 -0.0351 -0.0578 -0.0009 323 GLU A N   
203  C CA  . GLU A 27  ? 1.3451 0.9561 1.1566 -0.0227 -0.0587 0.0076  323 GLU A CA  
204  C C   . GLU A 27  ? 1.2533 0.9598 1.1423 -0.0099 -0.0603 0.0090  323 GLU A C   
205  O O   . GLU A 27  ? 1.2367 0.9937 1.1664 0.0047  -0.0617 0.0050  323 GLU A O   
206  C CB  . GLU A 27  ? 1.4162 0.9555 1.1611 0.0197  -0.0623 0.0117  323 GLU A CB  
207  C CG  . GLU A 27  ? 1.5887 1.0138 1.2402 0.0109  -0.0616 0.0091  323 GLU A CG  
208  C CD  . GLU A 27  ? 1.7997 1.1301 1.3641 0.0450  -0.0645 0.0158  323 GLU A CD  
209  O OE1 . GLU A 27  ? 1.8057 1.1639 1.3854 0.0674  -0.0669 0.0234  323 GLU A OE1 
210  O OE2 . GLU A 27  ? 1.9240 1.1464 1.3977 0.0499  -0.0652 0.0133  323 GLU A OE2 
211  N N   . THR A 28  ? 1.1678 0.8931 1.0699 -0.0182 -0.0599 0.0147  324 THR A N   
212  C CA  . THR A 28  ? 1.0795 0.8823 1.0438 -0.0174 -0.0612 0.0154  324 THR A CA  
213  C C   . THR A 28  ? 1.0197 0.8498 0.9949 0.0163  -0.0674 0.0198  324 THR A C   
214  O O   . THR A 28  ? 1.0034 0.8951 1.0252 0.0175  -0.0699 0.0189  324 THR A O   
215  C CB  . THR A 28  ? 1.0210 0.8345 0.9924 -0.0455 -0.0572 0.0180  324 THR A CB  
216  O OG1 . THR A 28  ? 1.1310 0.8933 1.0548 -0.0421 -0.0574 0.0252  324 THR A OG1 
217  C CG2 . THR A 28  ? 1.0567 0.8718 1.0283 -0.0812 -0.0513 0.0136  324 THR A CG2 
218  N N   . GLY A 29  ? 1.0088 0.7948 0.9376 0.0429  -0.0705 0.0248  325 GLY A N   
219  C CA  . GLY A 29  ? 0.9712 0.7911 0.9074 0.0731  -0.0771 0.0302  325 GLY A CA  
220  C C   . GLY A 29  ? 1.0342 0.8310 0.9476 0.0678  -0.0784 0.0371  325 GLY A C   
221  O O   . GLY A 29  ? 1.1319 0.9288 1.0246 0.0983  -0.0846 0.0429  325 GLY A O   
222  N N   . CYS A 30  ? 0.9991 0.7816 0.9146 0.0317  -0.0726 0.0367  326 CYS A N   
223  C CA  . CYS A 30  ? 0.9610 0.7190 0.8510 0.0232  -0.0721 0.0433  326 CYS A CA  
224  C C   . CYS A 30  ? 1.0663 0.7319 0.8795 0.0261  -0.0702 0.0485  326 CYS A C   
225  O O   . CYS A 30  ? 1.1186 0.7339 0.8989 0.0171  -0.0667 0.0454  326 CYS A O   
226  C CB  . CYS A 30  ? 0.8645 0.6485 0.7826 -0.0144 -0.0652 0.0408  326 CYS A CB  
227  S SG  . CYS A 30  ? 0.9055 0.7729 0.8940 -0.0191 -0.0670 0.0343  326 CYS A SG  
228  N N   . THR A 31  ? 1.0840 0.7207 0.8614 0.0373  -0.0730 0.0565  327 THR A N   
229  C CA  . THR A 31  ? 1.2429 0.7806 0.9365 0.0335  -0.0707 0.0631  327 THR A CA  
230  C C   . THR A 31  ? 1.2868 0.8200 0.9730 -0.0011 -0.0650 0.0683  327 THR A C   
231  O O   . THR A 31  ? 1.3071 0.9122 1.0520 -0.0176 -0.0627 0.0656  327 THR A O   
232  C CB  . THR A 31  ? 1.2416 0.7365 0.8821 0.0866  -0.0795 0.0694  327 THR A CB  
233  O OG1 . THR A 31  ? 1.2448 0.7916 0.9100 0.1040  -0.0858 0.0746  327 THR A OG1 
234  C CG2 . THR A 31  ? 1.0552 0.5774 0.7127 0.1246  -0.0841 0.0636  327 THR A CG2 
235  N N   . GLU A 32  ? 1.3990 0.8419 1.0051 -0.0116 -0.0624 0.0761  328 GLU A N   
236  C CA  . GLU A 32  ? 1.4797 0.9184 1.0720 -0.0428 -0.0564 0.0825  328 GLU A CA  
237  C C   . GLU A 32  ? 1.3653 0.8498 0.9831 -0.0150 -0.0630 0.0866  328 GLU A C   
238  O O   . GLU A 32  ? 1.3556 0.8685 0.9880 -0.0382 -0.0579 0.0889  328 GLU A O   
239  C CB  . GLU A 32  ? 1.7205 1.0426 1.2097 -0.0619 -0.0528 0.0913  328 GLU A CB  
240  C CG  . GLU A 32  ? 1.8720 1.1586 1.3347 -0.1156 -0.0437 0.0881  328 GLU A CG  
241  C CD  . GLU A 32  ? 2.0244 1.2449 1.4450 -0.1011 -0.0479 0.0831  328 GLU A CD  
242  O OE1 . GLU A 32  ? 2.1547 1.2830 1.4958 -0.1363 -0.0441 0.0851  328 GLU A OE1 
243  O OE2 . GLU A 32  ? 2.0120 1.2714 1.4741 -0.0567 -0.0547 0.0771  328 GLU A OE2 
244  N N   . HIS A 33  ? 1.3000 0.7999 0.9237 0.0336  -0.0742 0.0872  329 HIS A N   
245  C CA  . HIS A 33  ? 1.3737 0.9139 1.0112 0.0594  -0.0827 0.0917  329 HIS A CA  
246  C C   . HIS A 33  ? 1.2298 0.8710 0.9457 0.0746  -0.0900 0.0847  329 HIS A C   
247  O O   . HIS A 33  ? 1.0773 0.7607 0.8070 0.0920  -0.0986 0.0875  329 HIS A O   
248  C CB  . HIS A 33  ? 1.5983 1.0717 1.1610 0.1046  -0.0915 0.1011  329 HIS A CB  
249  C CG  . HIS A 33  ? 1.7966 1.1493 1.2640 0.0900  -0.0853 0.1085  329 HIS A CG  
250  N ND1 . HIS A 33  ? 1.8837 1.1563 1.2947 0.0965  -0.0836 0.1072  329 HIS A ND1 
251  C CD2 . HIS A 33  ? 1.8607 1.1539 1.2723 0.0650  -0.0802 0.1174  329 HIS A CD2 
252  C CE1 . HIS A 33  ? 1.9938 1.1569 1.3137 0.0735  -0.0785 0.1151  329 HIS A CE1 
253  N NE2 . HIS A 33  ? 1.9822 1.1587 1.3026 0.0533  -0.0759 0.1219  329 HIS A NE2 
254  N N   . ILE A 34  ? 1.1424 0.8225 0.9058 0.0647  -0.0872 0.0759  330 ILE A N   
255  C CA  . ILE A 34  ? 1.0783 0.8468 0.9084 0.0708  -0.0933 0.0699  330 ILE A CA  
256  C C   . ILE A 34  ? 0.9832 0.7791 0.8584 0.0419  -0.0857 0.0609  330 ILE A C   
257  O O   . ILE A 34  ? 1.0852 0.8442 0.9456 0.0315  -0.0791 0.0584  330 ILE A O   
258  C CB  . ILE A 34  ? 1.1321 0.9307 0.9639 0.1141  -0.1037 0.0711  330 ILE A CB  
259  C CG1 . ILE A 34  ? 1.0335 0.9271 0.9263 0.1115  -0.1111 0.0671  330 ILE A CG1 
260  C CG2 . ILE A 34  ? 1.2917 1.0624 1.1126 0.1256  -0.0998 0.0670  330 ILE A CG2 
261  C CD1 . ILE A 34  ? 0.9842 0.9297 0.8779 0.1510  -0.1230 0.0709  330 ILE A CD1 
262  N N   . CYS A 35  ? 0.9202 0.7761 0.8438 0.0286  -0.0872 0.0561  331 CYS A N   
263  C CA  . CYS A 35  ? 0.7997 0.6835 0.7629 0.0074  -0.0815 0.0480  331 CYS A CA  
264  C C   . CYS A 35  ? 0.8513 0.7899 0.8523 0.0176  -0.0892 0.0442  331 CYS A C   
265  O O   . CYS A 35  ? 0.7168 0.6915 0.7285 0.0214  -0.0974 0.0455  331 CYS A O   
266  C CB  . CYS A 35  ? 0.8020 0.6981 0.7771 -0.0168 -0.0754 0.0452  331 CYS A CB  
267  S SG  . CYS A 35  ? 0.6994 0.6324 0.7173 -0.0324 -0.0706 0.0356  331 CYS A SG  
268  N N   . MET A 36  ? 0.7834 0.7287 0.8006 0.0189  -0.0867 0.0399  332 MET A N   
269  C CA  . MET A 36  ? 0.8440 0.8411 0.8944 0.0244  -0.0921 0.0368  332 MET A CA  
270  C C   . MET A 36  ? 0.7738 0.7886 0.8535 0.0011  -0.0882 0.0302  332 MET A C   
271  O O   . MET A 36  ? 0.7429 0.7879 0.8446 0.0009  -0.0900 0.0273  332 MET A O   
272  C CB  . MET A 36  ? 1.0170 1.0099 1.0590 0.0486  -0.0923 0.0370  332 MET A CB  
273  C CG  . MET A 36  ? 1.1734 1.1439 1.1768 0.0811  -0.0970 0.0436  332 MET A CG  
274  S SD  . MET A 36  ? 1.3172 1.3279 1.3232 0.1211  -0.1017 0.0437  332 MET A SD  
275  C CE  . MET A 36  ? 1.3430 1.3750 1.3236 0.1566  -0.1122 0.0523  332 MET A CE  
276  N N   . GLY A 37  ? 0.7058 0.7039 0.7824 -0.0159 -0.0827 0.0280  333 GLY A N   
277  C CA  . GLY A 37  ? 0.6585 0.6681 0.7542 -0.0301 -0.0789 0.0219  333 GLY A CA  
278  C C   . GLY A 37  ? 0.6856 0.7218 0.7944 -0.0355 -0.0858 0.0198  333 GLY A C   
279  O O   . GLY A 37  ? 0.6893 0.7265 0.8059 -0.0432 -0.0835 0.0151  333 GLY A O   
280  N N   . SER A 38  ? 0.5420 0.5991 0.6482 -0.0338 -0.0946 0.0233  334 SER A N   
281  C CA  . SER A 38  ? 0.6146 0.6966 0.7274 -0.0479 -0.1015 0.0217  334 SER A CA  
282  C C   . SER A 38  ? 0.5618 0.6894 0.6914 -0.0430 -0.1066 0.0246  334 SER A C   
283  O O   . SER A 38  ? 0.6090 0.7661 0.7421 -0.0606 -0.1128 0.0248  334 SER A O   
284  C CB  . SER A 38  ? 0.6127 0.6920 0.7061 -0.0602 -0.1087 0.0223  334 SER A CB  
285  O OG  . SER A 38  ? 0.6352 0.7351 0.7246 -0.0503 -0.1149 0.0277  334 SER A OG  
286  N N   . ILE A 39  ? 0.5468 0.6801 0.6809 -0.0201 -0.1039 0.0270  335 ILE A N   
287  C CA  . ILE A 39  ? 0.5866 0.7672 0.7359 -0.0088 -0.1066 0.0287  335 ILE A CA  
288  C C   . ILE A 39  ? 0.5631 0.7415 0.7261 -0.0197 -0.1012 0.0243  335 ILE A C   
289  O O   . ILE A 39  ? 0.6573 0.7952 0.8170 -0.0187 -0.0940 0.0206  335 ILE A O   
290  C CB  . ILE A 39  ? 0.6301 0.8032 0.7670 0.0259  -0.1051 0.0318  335 ILE A CB  
291  C CG1 . ILE A 39  ? 0.6543 0.8203 0.7701 0.0393  -0.1107 0.0370  335 ILE A CG1 
292  C CG2 . ILE A 39  ? 0.5665 0.7946 0.7171 0.0448  -0.1067 0.0327  335 ILE A CG2 
293  C CD1 . ILE A 39  ? 0.6808 0.9119 0.8068 0.0336  -0.1216 0.0405  335 ILE A CD1 
294  N N   . MET A 40  ? 0.5863 0.8123 0.7628 -0.0325 -0.1048 0.0251  336 MET A N   
295  C CA  . MET A 40  ? 0.7141 0.9332 0.8974 -0.0478 -0.1006 0.0217  336 MET A CA  
296  C C   . MET A 40  ? 0.7895 1.0042 0.9810 -0.0265 -0.0937 0.0194  336 MET A C   
297  O O   . MET A 40  ? 0.8046 0.9843 0.9948 -0.0304 -0.0883 0.0152  336 MET A O   
298  C CB  . MET A 40  ? 0.7759 1.0447 0.9640 -0.0731 -0.1062 0.0244  336 MET A CB  
299  C CG  . MET A 40  ? 0.8927 1.1513 1.0808 -0.0892 -0.1022 0.0223  336 MET A CG  
300  S SD  . MET A 40  ? 0.9963 1.2002 1.1509 -0.1245 -0.1058 0.0207  336 MET A SD  
301  C CE  . MET A 40  ? 0.9464 1.2044 1.0913 -0.1623 -0.1155 0.0262  336 MET A CE  
302  N N   . LEU A 41  ? 0.8342 1.0856 1.0302 -0.0021 -0.0941 0.0218  337 LEU A N   
303  C CA  . LEU A 41  ? 1.0156 1.2580 1.2100 0.0208  -0.0880 0.0189  337 LEU A CA  
304  C C   . LEU A 41  ? 1.1934 1.4168 1.3661 0.0565  -0.0881 0.0203  337 LEU A C   
305  O O   . LEU A 41  ? 1.2879 1.5530 1.4587 0.0852  -0.0894 0.0225  337 LEU A O   
306  C CB  . LEU A 41  ? 1.0352 1.3399 1.2464 0.0206  -0.0872 0.0197  337 LEU A CB  
307  C CG  . LEU A 41  ? 1.0370 1.3799 1.2610 -0.0167 -0.0904 0.0220  337 LEU A CG  
308  C CD1 . LEU A 41  ? 1.0285 1.4598 1.2678 -0.0142 -0.0912 0.0260  337 LEU A CD1 
309  C CD2 . LEU A 41  ? 1.0258 1.3258 1.2464 -0.0370 -0.0862 0.0182  337 LEU A CD2 
310  N N   . PRO A 42  ? 1.2221 1.3823 1.3727 0.0569  -0.0865 0.0196  338 PRO A N   
311  C CA  . PRO A 42  ? 1.2897 1.4136 1.4053 0.0889  -0.0868 0.0218  338 PRO A CA  
312  C C   . PRO A 42  ? 1.3433 1.4314 1.4350 0.1103  -0.0817 0.0175  338 PRO A C   
313  O O   . PRO A 42  ? 1.3399 1.4157 1.4410 0.0935  -0.0771 0.0122  338 PRO A O   
314  C CB  . PRO A 42  ? 1.2983 1.3638 1.3949 0.0718  -0.0855 0.0225  338 PRO A CB  
315  C CG  . PRO A 42  ? 1.2581 1.3359 1.3830 0.0363  -0.0841 0.0197  338 PRO A CG  
316  C CD  . PRO A 42  ? 1.2005 1.3179 1.3510 0.0299  -0.0834 0.0167  338 PRO A CD  
317  N N   . SER A 43  ? 1.3513 1.4192 1.4056 0.1502  -0.0832 0.0197  339 SER A N   
318  C CA  . SER A 43  ? 1.3745 1.4016 1.3906 0.1813  -0.0794 0.0156  339 SER A CA  
319  C C   . SER A 43  ? 1.4016 1.3890 1.4161 0.1573  -0.0735 0.0081  339 SER A C   
320  O O   . SER A 43  ? 1.4707 1.4535 1.4705 0.1778  -0.0705 0.0036  339 SER A O   
321  C CB  . SER A 43  ? 1.3936 1.3373 1.3419 0.2105  -0.0808 0.0181  339 SER A CB  
322  O OG  . SER A 43  ? 1.4102 1.3946 1.3490 0.2526  -0.0867 0.0242  339 SER A OG  
323  N N   . VAL A 52  ? 1.9385 1.6787 1.5451 0.4927  -0.0271 -0.0725 348 VAL A N   
324  C CA  . VAL A 52  ? 1.9603 1.6134 1.5208 0.4676  -0.0265 -0.0838 348 VAL A CA  
325  C C   . VAL A 52  ? 2.0668 1.5735 1.5549 0.4329  -0.0338 -0.0872 348 VAL A C   
326  O O   . VAL A 52  ? 2.1898 1.6253 1.6186 0.4591  -0.0372 -0.0841 348 VAL A O   
327  C CB  . VAL A 52  ? 1.9531 1.5847 1.4473 0.5329  -0.0198 -0.0935 348 VAL A CB  
328  C CG1 . VAL A 52  ? 2.0420 1.5964 1.4417 0.5920  -0.0218 -0.0920 348 VAL A CG1 
329  C CG2 . VAL A 52  ? 1.9417 1.4898 1.3906 0.5028  -0.0198 -0.1057 348 VAL A CG2 
330  N N   . ALA A 53  ? 1.9811 1.4486 1.4734 0.3719  -0.0365 -0.0928 349 ALA A N   
331  C CA  . ALA A 53  ? 1.9661 1.3146 1.3990 0.3245  -0.0432 -0.0956 349 ALA A CA  
332  C C   . ALA A 53  ? 2.0642 1.2795 1.3834 0.3319  -0.0445 -0.1088 349 ALA A C   
333  O O   . ALA A 53  ? 2.0943 1.3280 1.4132 0.3403  -0.0413 -0.1171 349 ALA A O   
334  C CB  . ALA A 53  ? 1.8343 1.2369 1.3459 0.2490  -0.0465 -0.0927 349 ALA A CB  
335  N N   . THR A 54  ? 2.1143 1.1892 1.3303 0.3257  -0.0493 -0.1108 350 THR A N   
336  C CA  . THR A 54  ? 2.2002 1.1491 1.2999 0.3268  -0.0515 -0.1181 350 THR A CA  
337  C C   . THR A 54  ? 2.1952 1.0779 1.2692 0.2418  -0.0579 -0.1235 350 THR A C   
338  O O   . THR A 54  ? 2.0759 0.9986 1.2116 0.1859  -0.0609 -0.1223 350 THR A O   
339  C CB  . THR A 54  ? 2.2780 1.1504 1.2872 0.3644  -0.0532 -0.1072 350 THR A CB  
340  O OG1 . THR A 54  ? 2.3619 1.1366 1.3116 0.3051  -0.0592 -0.1024 350 THR A OG1 
341  C CG2 . THR A 54  ? 2.2105 1.1670 1.2711 0.4190  -0.0503 -0.0978 350 THR A CG2 
342  N N   . LYS A 55  ? 2.3270 1.1216 1.3115 0.2301  -0.0604 -0.1264 351 LYS A N   
343  C CA  . LYS A 55  ? 2.3828 1.1343 1.3439 0.1524  -0.0662 -0.1317 351 LYS A CA  
344  C C   . LYS A 55  ? 2.4456 1.1291 1.3580 0.0930  -0.0710 -0.1219 351 LYS A C   
345  O O   . LYS A 55  ? 2.3782 1.0759 1.3121 0.0189  -0.0751 -0.1237 351 LYS A O   
346  C CB  . LYS A 55  ? 2.5215 1.2089 1.4042 0.1663  -0.0668 -0.1378 351 LYS A CB  
347  C CG  . LYS A 55  ? 2.6538 1.2817 1.4541 0.2427  -0.0638 -0.1318 351 LYS A CG  
348  C CD  . LYS A 55  ? 2.7888 1.3587 1.5155 0.2600  -0.0643 -0.1381 351 LYS A CD  
349  C CE  . LYS A 55  ? 2.9233 1.4375 1.5632 0.3396  -0.0624 -0.1313 351 LYS A CE  
350  N NZ  . LYS A 55  ? 3.0240 1.4617 1.5746 0.3547  -0.0639 -0.1359 351 LYS A NZ  
351  N N   . ASP A 56  ? 2.5690 1.1864 1.4144 0.1239  -0.0705 -0.1112 352 ASP A N   
352  C CA  . ASP A 56  ? 2.6560 1.2180 1.4590 0.0695  -0.0736 -0.1012 352 ASP A CA  
353  C C   . ASP A 56  ? 2.4282 1.0822 1.3362 0.0272  -0.0733 -0.0992 352 ASP A C   
354  O O   . ASP A 56  ? 2.4405 1.1053 1.3615 -0.0471 -0.0759 -0.0973 352 ASP A O   
355  C CB  . ASP A 56  ? 2.8668 1.3492 1.5824 0.1198  -0.0733 -0.0910 352 ASP A CB  
356  C CG  . ASP A 56  ? 3.0436 1.4850 1.6936 0.1981  -0.0720 -0.0934 352 ASP A CG  
357  O OD1 . ASP A 56  ? 3.1975 1.5348 1.7376 0.1933  -0.0750 -0.0932 352 ASP A OD1 
358  O OD2 . ASP A 56  ? 3.0119 1.5311 1.7198 0.2640  -0.0679 -0.0948 352 ASP A OD2 
359  N N   . GLN A 57  ? 2.2017 0.9301 1.1857 0.0752  -0.0700 -0.0988 353 GLN A N   
360  C CA  . GLN A 57  ? 2.0677 0.8787 1.1471 0.0429  -0.0701 -0.0961 353 GLN A CA  
361  C C   . GLN A 57  ? 1.9301 0.8162 1.0845 -0.0110 -0.0727 -0.1055 353 GLN A C   
362  O O   . GLN A 57  ? 1.7903 0.7611 1.0247 -0.0535 -0.0730 -0.0989 353 GLN A O   
363  C CB  . GLN A 57  ? 2.0085 0.8829 1.1475 0.1115  -0.0667 -0.0936 353 GLN A CB  
364  C CG  . GLN A 57  ? 2.1217 0.9725 1.2102 0.1940  -0.0634 -0.0930 353 GLN A CG  
365  C CD  . GLN A 57  ? 2.0539 1.0195 1.2298 0.2555  -0.0590 -0.0916 353 GLN A CD  
366  O OE1 . GLN A 57  ? 1.9155 1.0054 1.1959 0.2378  -0.0566 -0.0916 353 GLN A OE1 
367  N NE2 . GLN A 57  ? 2.1138 1.0800 1.2653 0.3178  -0.0576 -0.0838 353 GLN A NE2 
368  N N   . LEU A 58  ? 1.9360 0.8200 1.0777 -0.0083 -0.0737 -0.1163 354 LEU A N   
369  C CA  . LEU A 58  ? 1.7827 0.7837 1.0213 -0.0414 -0.0748 -0.1200 354 LEU A CA  
370  C C   . LEU A 58  ? 1.8121 0.8001 1.0341 -0.1258 -0.0816 -0.1243 354 LEU A C   
371  O O   . LEU A 58  ? 1.7267 0.8333 1.0442 -0.1594 -0.0827 -0.1218 354 LEU A O   
372  C CB  . LEU A 58  ? 1.8252 0.8424 1.0637 0.0024  -0.0725 -0.1291 354 LEU A CB  
373  C CG  . LEU A 58  ? 1.6907 0.8611 1.0545 0.0104  -0.0693 -0.1260 354 LEU A CG  
374  C CD1 . LEU A 58  ? 1.5448 0.8074 0.9921 0.0471  -0.0638 -0.1134 354 LEU A CD1 
375  C CD2 . LEU A 58  ? 1.7570 0.9263 1.1016 0.0471  -0.0668 -0.1356 354 LEU A CD2 
376  N N   . PHE A 59  ? 1.9142 0.8144 1.0453 -0.1541 -0.0826 -0.1204 355 PHE A N   
377  C CA  . PHE A 59  ? 2.0003 0.9335 1.1382 -0.2315 -0.0867 -0.1190 355 PHE A CA  
378  C C   . PHE A 59  ? 2.0248 1.0195 1.2115 -0.2797 -0.0858 -0.1087 355 PHE A C   
379  O O   . PHE A 59  ? 2.0125 1.1028 1.2627 -0.3283 -0.0884 -0.1094 355 PHE A O   
380  C CB  . PHE A 59  ? 2.2519 1.0830 1.2785 -0.2552 -0.0881 -0.1166 355 PHE A CB  
381  C CG  . PHE A 59  ? 2.3525 1.2311 1.3896 -0.3313 -0.0921 -0.1161 355 PHE A CG  
382  C CD1 . PHE A 59  ? 2.3479 1.2974 1.4350 -0.3459 -0.0965 -0.1262 355 PHE A CD1 
383  C CD2 . PHE A 59  ? 2.4309 1.2941 1.4306 -0.3868 -0.0913 -0.1052 355 PHE A CD2 
384  C CE1 . PHE A 59  ? 2.3424 1.3500 1.4439 -0.4110 -0.1004 -0.1250 355 PHE A CE1 
385  C CE2 . PHE A 59  ? 2.4551 1.3770 1.4675 -0.4539 -0.0941 -0.1041 355 PHE A CE2 
386  C CZ  . PHE A 59  ? 2.4069 1.4036 1.4721 -0.4644 -0.0988 -0.1138 355 PHE A CZ  
387  N N   . PRO A 60  ? 2.0371 0.9872 1.1950 -0.2673 -0.0821 -0.0985 356 PRO A N   
388  C CA  . PRO A 60  ? 1.9322 0.9544 1.1461 -0.3097 -0.0803 -0.0894 356 PRO A CA  
389  C C   . PRO A 60  ? 1.6901 0.8388 1.0230 -0.3102 -0.0815 -0.0931 356 PRO A C   
390  O O   . PRO A 60  ? 1.6188 0.8623 1.0095 -0.3574 -0.0819 -0.0900 356 PRO A O   
391  C CB  . PRO A 60  ? 2.0270 0.9763 1.1938 -0.2764 -0.0766 -0.0800 356 PRO A CB  
392  C CG  . PRO A 60  ? 2.0965 0.9691 1.2136 -0.2039 -0.0765 -0.0850 356 PRO A CG  
393  C CD  . PRO A 60  ? 2.1174 0.9582 1.1911 -0.2135 -0.0794 -0.0938 356 PRO A CD  
394  N N   . LEU A 61  ? 1.6165 0.7808 0.9885 -0.2526 -0.0811 -0.0977 357 LEU A N   
395  C CA  . LEU A 61  ? 1.3825 0.6962 0.8811 -0.2370 -0.0788 -0.0934 357 LEU A CA  
396  C C   . LEU A 61  ? 1.4379 0.8241 0.9757 -0.2699 -0.0835 -0.1009 357 LEU A C   
397  O O   . LEU A 61  ? 1.3731 0.8718 0.9925 -0.2899 -0.0839 -0.0972 357 LEU A O   
398  C CB  . LEU A 61  ? 1.3712 0.7083 0.9065 -0.1629 -0.0743 -0.0911 357 LEU A CB  
399  C CG  . LEU A 61  ? 1.5551 0.8217 1.0443 -0.1210 -0.0709 -0.0846 357 LEU A CG  
400  C CD1 . LEU A 61  ? 1.5848 0.8811 1.1014 -0.0498 -0.0672 -0.0840 357 LEU A CD1 
401  C CD2 . LEU A 61  ? 1.5581 0.8708 1.0923 -0.1387 -0.0690 -0.0737 357 LEU A CD2 
402  N N   . ALA A 62  ? 1.4117 0.7346 0.8886 -0.2710 -0.0875 -0.1116 358 ALA A N   
403  C CA  . ALA A 62  ? 1.3910 0.7758 0.8944 -0.3055 -0.0935 -0.1192 358 ALA A CA  
404  C C   . ALA A 62  ? 1.4427 0.8607 0.9407 -0.3766 -0.0970 -0.1167 358 ALA A C   
405  O O   . ALA A 62  ? 1.3867 0.9214 0.9570 -0.4003 -0.0998 -0.1160 358 ALA A O   
406  C CB  . ALA A 62  ? 1.4391 0.7368 0.8655 -0.2933 -0.0969 -0.1314 358 ALA A CB  
407  N N   . LYS A 63  ? 1.4403 0.7770 0.8614 -0.3976 -0.0933 -0.1098 359 LYS A N   
408  C CA  . LYS A 63  ? 1.4936 0.8736 0.9087 -0.4559 -0.0921 -0.1019 359 LYS A CA  
409  C C   . LYS A 63  ? 1.4867 0.9766 0.9843 -0.4686 -0.0886 -0.0938 359 LYS A C   
410  O O   . LYS A 63  ? 1.5060 1.1057 1.0564 -0.4990 -0.0894 -0.0919 359 LYS A O   
411  C CB  . LYS A 63  ? 1.6212 0.8786 0.9253 -0.4739 -0.0889 -0.0952 359 LYS A CB  
412  C CG  . LYS A 63  ? 1.5971 0.8964 0.8903 -0.5343 -0.0860 -0.0854 359 LYS A CG  
413  C CD  . LYS A 63  ? 1.7579 0.9295 0.9317 -0.5552 -0.0835 -0.0781 359 LYS A CD  
414  C CE  . LYS A 63  ? 1.8634 1.0402 0.9847 -0.6200 -0.0850 -0.0756 359 LYS A CE  
415  N NZ  . LYS A 63  ? 1.7550 1.0904 0.9687 -0.6556 -0.0844 -0.0745 359 LYS A NZ  
416  N N   . GLU A 64  ? 1.3742 0.8366 0.8806 -0.4417 -0.0845 -0.0887 360 GLU A N   
417  C CA  . GLU A 64  ? 1.4523 1.0133 1.0344 -0.4484 -0.0808 -0.0812 360 GLU A CA  
418  C C   . GLU A 64  ? 1.3366 1.0268 1.0162 -0.4390 -0.0845 -0.0854 360 GLU A C   
419  O O   . GLU A 64  ? 1.2448 1.0430 0.9786 -0.4586 -0.0824 -0.0805 360 GLU A O   
420  C CB  . GLU A 64  ? 1.5219 1.0270 1.0985 -0.4133 -0.0774 -0.0766 360 GLU A CB  
421  C CG  . GLU A 64  ? 1.5485 1.1475 1.2014 -0.4144 -0.0736 -0.0691 360 GLU A CG  
422  C CD  . GLU A 64  ? 1.6361 1.2111 1.3103 -0.3571 -0.0701 -0.0638 360 GLU A CD  
423  O OE1 . GLU A 64  ? 1.7519 1.2189 1.3600 -0.3288 -0.0700 -0.0640 360 GLU A OE1 
424  O OE2 . GLU A 64  ? 1.5441 1.2131 1.2997 -0.3338 -0.0668 -0.0584 360 GLU A OE2 
425  N N   . PHE A 65  ? 1.2870 0.9684 0.9843 -0.4049 -0.0895 -0.0940 361 PHE A N   
426  C CA  . PHE A 65  ? 1.1054 0.9090 0.8926 -0.3822 -0.0909 -0.0939 361 PHE A CA  
427  C C   . PHE A 65  ? 1.0948 0.9630 0.8871 -0.4224 -0.0974 -0.0994 361 PHE A C   
428  O O   . PHE A 65  ? 0.9773 0.9618 0.8333 -0.4256 -0.0972 -0.0954 361 PHE A O   
429  C CB  . PHE A 65  ? 1.1323 0.9209 0.9401 -0.3213 -0.0894 -0.0954 361 PHE A CB  
430  C CG  . PHE A 65  ? 1.0665 0.9581 0.9462 -0.3022 -0.0920 -0.0959 361 PHE A CG  
431  C CD1 . PHE A 65  ? 0.9465 0.9215 0.8966 -0.2795 -0.0888 -0.0880 361 PHE A CD1 
432  C CD2 . PHE A 65  ? 0.9651 0.8629 0.8338 -0.3058 -0.0980 -0.1041 361 PHE A CD2 
433  C CE1 . PHE A 65  ? 0.9542 1.0095 0.9570 -0.2589 -0.0917 -0.0880 361 PHE A CE1 
434  C CE2 . PHE A 65  ? 0.9792 0.9654 0.9067 -0.2861 -0.1009 -0.1036 361 PHE A CE2 
435  C CZ  . PHE A 65  ? 0.9087 0.9704 0.9007 -0.2618 -0.0978 -0.0953 361 PHE A CZ  
436  N N   . LEU A 66  ? 1.1527 0.9501 0.8789 -0.4387 -0.1005 -0.1057 362 LEU A N   
437  C CA  . LEU A 66  ? 1.1871 1.0460 0.9170 -0.4674 -0.1046 -0.1079 362 LEU A CA  
438  C C   . LEU A 66  ? 1.2167 1.1459 0.9566 -0.5059 -0.0997 -0.0985 362 LEU A C   
439  O O   . LEU A 66  ? 1.1941 1.2284 0.9748 -0.5179 -0.1019 -0.0977 362 LEU A O   
440  C CB  . LEU A 66  ? 1.2680 1.0221 0.9119 -0.4812 -0.1079 -0.1152 362 LEU A CB  
441  C CG  . LEU A 66  ? 1.2587 0.9600 0.8879 -0.4452 -0.1133 -0.1270 362 LEU A CG  
442  C CD1 . LEU A 66  ? 1.3753 0.9906 0.9201 -0.4634 -0.1160 -0.1333 362 LEU A CD1 
443  C CD2 . LEU A 66  ? 1.1592 0.9729 0.8698 -0.4262 -0.1192 -0.1307 362 LEU A CD2 
444  N N   . ASP A 67  ? 1.3213 1.1939 1.0193 -0.5241 -0.0930 -0.0913 363 ASP A N   
445  C CA  . ASP A 67  ? 1.3789 1.3176 1.0804 -0.5624 -0.0874 -0.0825 363 ASP A CA  
446  C C   . ASP A 67  ? 1.1959 1.2693 0.9897 -0.5417 -0.0849 -0.0785 363 ASP A C   
447  O O   . ASP A 67  ? 1.1723 1.3460 0.9905 -0.5624 -0.0832 -0.0753 363 ASP A O   
448  C CB  . ASP A 67  ? 1.4930 1.3371 1.1276 -0.5815 -0.0811 -0.0753 363 ASP A CB  
449  C CG  . ASP A 67  ? 1.6981 1.4368 1.2282 -0.6200 -0.0821 -0.0754 363 ASP A CG  
450  O OD1 . ASP A 67  ? 1.8003 1.5811 1.3066 -0.6683 -0.0810 -0.0717 363 ASP A OD1 
451  O OD2 . ASP A 67  ? 1.7912 1.4049 1.2583 -0.6007 -0.0840 -0.0789 363 ASP A OD2 
452  N N   . GLN A 68  ? 1.1392 1.2163 0.9800 -0.4993 -0.0844 -0.0785 364 GLN A N   
453  C CA  . GLN A 68  ? 1.0658 1.2609 0.9847 -0.4757 -0.0817 -0.0743 364 GLN A CA  
454  C C   . GLN A 68  ? 1.0066 1.2885 0.9764 -0.4513 -0.0883 -0.0791 364 GLN A C   
455  O O   . GLN A 68  ? 0.9585 1.3489 0.9735 -0.4415 -0.0864 -0.0757 364 GLN A O   
456  C CB  . GLN A 68  ? 1.0425 1.2116 0.9887 -0.4424 -0.0787 -0.0713 364 GLN A CB  
457  C CG  . GLN A 68  ? 1.0745 1.1882 1.0275 -0.4085 -0.0845 -0.0777 364 GLN A CG  
458  C CD  . GLN A 68  ? 1.0931 1.1462 1.0443 -0.3814 -0.0794 -0.0726 364 GLN A CD  
459  O OE1 . GLN A 68  ? 1.0242 1.1151 1.0272 -0.3343 -0.0765 -0.0683 364 GLN A OE1 
460  N NE2 . GLN A 68  ? 1.1405 1.0922 1.0254 -0.4025 -0.0771 -0.0712 364 GLN A NE2 
461  N N   . TYR A 69  ? 0.9982 1.2326 0.9547 -0.4395 -0.0958 -0.0870 365 TYR A N   
462  C CA  . TYR A 69  ? 0.9402 1.2514 0.9357 -0.4190 -0.1028 -0.0911 365 TYR A CA  
463  C C   . TYR A 69  ? 0.9758 1.3545 0.9614 -0.4509 -0.1033 -0.0903 365 TYR A C   
464  O O   . TYR A 69  ? 0.9136 1.3992 0.9439 -0.4336 -0.1040 -0.0880 365 TYR A O   
465  C CB  . TYR A 69  ? 0.8981 1.1407 0.8722 -0.4053 -0.1105 -0.1004 365 TYR A CB  
466  C CG  . TYR A 69  ? 0.9246 1.2382 0.9249 -0.3921 -0.1183 -0.1044 365 TYR A CG  
467  C CD1 . TYR A 69  ? 0.8720 1.2790 0.9334 -0.3533 -0.1199 -0.1008 365 TYR A CD1 
468  C CD2 . TYR A 69  ? 0.9166 1.1995 0.8743 -0.4162 -0.1240 -0.1113 365 TYR A CD2 
469  C CE1 . TYR A 69  ? 0.8890 1.3563 0.9678 -0.3374 -0.1273 -0.1034 365 TYR A CE1 
470  C CE2 . TYR A 69  ? 0.9707 1.3197 0.9509 -0.4037 -0.1316 -0.1145 365 TYR A CE2 
471  C CZ  . TYR A 69  ? 0.9333 1.3744 0.9740 -0.3635 -0.1333 -0.1103 365 TYR A CZ  
472  O OH  . TYR A 69  ? 0.9871 1.4886 1.0438 -0.3472 -0.1410 -0.1126 365 TYR A OH  
473  N N   . TYR A 70  ? 1.1544 1.4693 1.0751 -0.4964 -0.1031 -0.0919 366 TYR A N   
474  C CA  . TYR A 70  ? 1.1349 1.5138 1.0402 -0.5340 -0.1035 -0.0907 366 TYR A CA  
475  C C   . TYR A 70  ? 1.1695 1.6361 1.0945 -0.5498 -0.0951 -0.0822 366 TYR A C   
476  O O   . TYR A 70  ? 1.1735 1.7439 1.1172 -0.5603 -0.0950 -0.0808 366 TYR A O   
477  C CB  . TYR A 70  ? 1.2433 1.5216 1.0645 -0.5807 -0.1052 -0.0938 366 TYR A CB  
478  C CG  . TYR A 70  ? 1.2002 1.4340 1.0051 -0.5686 -0.1145 -0.1036 366 TYR A CG  
479  C CD1 . TYR A 70  ? 1.1829 1.2986 0.9517 -0.5491 -0.1169 -0.1099 366 TYR A CD1 
480  C CD2 . TYR A 70  ? 1.1705 1.4849 0.9959 -0.5727 -0.1209 -0.1068 366 TYR A CD2 
481  C CE1 . TYR A 70  ? 1.2105 1.2880 0.9613 -0.5361 -0.1250 -0.1198 366 TYR A CE1 
482  C CE2 . TYR A 70  ? 1.2016 1.4771 1.0112 -0.5611 -0.1297 -0.1160 366 TYR A CE2 
483  C CZ  . TYR A 70  ? 1.1748 1.3319 0.9468 -0.5434 -0.1316 -0.1227 366 TYR A CZ  
484  O OH  . TYR A 70  ? 1.0634 1.1842 0.8160 -0.5306 -0.1399 -0.1327 366 TYR A OH  
485  N N   . SER A 71  ? 1.1364 1.5662 1.0556 -0.5503 -0.0879 -0.0769 367 SER A N   
486  C CA  . SER A 71  ? 1.1247 1.6451 1.0708 -0.5549 -0.0798 -0.0696 367 SER A CA  
487  C C   . SER A 71  ? 0.9942 1.6286 1.0132 -0.5046 -0.0807 -0.0696 367 SER A C   
488  O O   . SER A 71  ? 1.0760 1.8184 1.1141 -0.5080 -0.0769 -0.0666 367 SER A O   
489  C CB  . SER A 71  ? 1.1177 1.5718 1.0485 -0.5559 -0.0729 -0.0644 367 SER A CB  
490  O OG  . SER A 71  ? 1.2040 1.7306 1.1404 -0.5746 -0.0647 -0.0576 367 SER A OG  
491  N N   . SER A 72  ? 0.8368 1.4472 0.8900 -0.4566 -0.0858 -0.0730 368 SER A N   
492  C CA  . SER A 72  ? 0.7540 1.4526 0.8655 -0.4035 -0.0864 -0.0719 368 SER A CA  
493  C C   . SER A 72  ? 0.8698 1.6584 0.9954 -0.3947 -0.0913 -0.0743 368 SER A C   
494  O O   . SER A 72  ? 0.8511 1.7356 1.0087 -0.3633 -0.0887 -0.0717 368 SER A O   
495  C CB  . SER A 72  ? 0.6967 1.3392 0.8310 -0.3600 -0.0911 -0.0743 368 SER A CB  
496  O OG  . SER A 72  ? 0.8474 1.4986 0.9912 -0.3381 -0.1003 -0.0795 368 SER A OG  
497  N N   . ILE A 73  ? 0.9721 1.7307 1.0705 -0.4191 -0.0984 -0.0795 369 ILE A N   
498  C CA  . ILE A 73  ? 1.0314 1.8749 1.1412 -0.4122 -0.1037 -0.0818 369 ILE A CA  
499  C C   . ILE A 73  ? 1.1440 2.0554 1.2301 -0.4612 -0.0986 -0.0791 369 ILE A C   
500  O O   . ILE A 73  ? 1.2013 2.1710 1.2813 -0.4750 -0.1028 -0.0814 369 ILE A O   
501  C CB  . ILE A 73  ? 1.0999 1.8860 1.1923 -0.4136 -0.1143 -0.0889 369 ILE A CB  
502  C CG1 . ILE A 73  ? 1.1498 1.8276 1.1837 -0.4653 -0.1148 -0.0924 369 ILE A CG1 
503  C CG2 . ILE A 73  ? 1.0290 1.7796 1.1498 -0.3597 -0.1197 -0.0909 369 ILE A CG2 
504  C CD1 . ILE A 73  ? 1.1243 1.7281 1.1356 -0.4612 -0.1245 -0.1007 369 ILE A CD1 
505  N N   . LYS A 74  ? 1.1663 2.0746 1.2372 -0.4889 -0.0895 -0.0740 370 LYS A N   
506  C CA  . LYS A 74  ? 1.2593 2.2358 1.3034 -0.5393 -0.0834 -0.0702 370 LYS A CA  
507  C C   . LYS A 74  ? 1.3505 2.2798 1.3380 -0.5993 -0.0876 -0.0728 370 LYS A C   
508  O O   . LYS A 74  ? 1.4112 2.4218 1.3834 -0.6345 -0.0867 -0.0716 370 LYS A O   
509  C CB  . LYS A 74  ? 1.2477 2.3737 1.3281 -0.5128 -0.0811 -0.0687 370 LYS A CB  
510  C CG  . LYS A 74  ? 1.1647 2.3299 1.2968 -0.4377 -0.0808 -0.0684 370 LYS A CG  
511  C CD  . LYS A 74  ? 1.1235 2.3609 1.2710 -0.4228 -0.0709 -0.0633 370 LYS A CD  
512  C CE  . LYS A 74  ? 1.0728 2.3408 1.2609 -0.3455 -0.0714 -0.0635 370 LYS A CE  
513  N NZ  . LYS A 74  ? 1.0513 2.3650 1.2512 -0.3244 -0.0622 -0.0594 370 LYS A NZ  
514  N N   . ARG A 75  ? 1.3021 2.1000 1.2535 -0.6111 -0.0922 -0.0764 371 ARG A N   
515  C CA  . ARG A 75  ? 1.2932 2.0210 1.1779 -0.6659 -0.0961 -0.0792 371 ARG A CA  
516  C C   . ARG A 75  ? 1.4340 2.0130 1.2590 -0.6885 -0.0941 -0.0786 371 ARG A C   
517  O O   . ARG A 75  ? 1.5061 1.9790 1.2889 -0.6940 -0.0999 -0.0841 371 ARG A O   
518  C CB  . ARG A 75  ? 1.1498 1.8701 1.0423 -0.6478 -0.1068 -0.0870 371 ARG A CB  
519  C CG  . ARG A 75  ? 1.0893 1.9492 1.0353 -0.6192 -0.1096 -0.0874 371 ARG A CG  
520  C CD  . ARG A 75  ? 1.0792 1.9308 1.0669 -0.5589 -0.1180 -0.0928 371 ARG A CD  
521  N NE  . ARG A 75  ? 1.1773 2.0502 1.1544 -0.5673 -0.1273 -0.0983 371 ARG A NE  
522  C CZ  . ARG A 75  ? 1.3016 2.0777 1.2303 -0.5950 -0.1338 -0.1045 371 ARG A CZ  
523  N NH1 . ARG A 75  ? 1.3539 2.1567 1.2744 -0.6019 -0.1424 -0.1096 371 ARG A NH1 
524  N NH2 . ARG A 75  ? 1.3573 2.0075 1.2415 -0.6132 -0.1316 -0.1059 371 ARG A NH2 
525  N N   . PHE A 76  ? 1.4675 2.0369 1.2841 -0.6991 -0.0856 -0.0719 372 PHE A N   
526  C CA  . PHE A 76  ? 1.5527 1.9839 1.3038 -0.7219 -0.0829 -0.0699 372 PHE A CA  
527  C C   . PHE A 76  ? 1.6982 2.0596 1.3586 -0.7847 -0.0846 -0.0696 372 PHE A C   
528  O O   . PHE A 76  ? 1.7540 2.1890 1.3944 -0.8314 -0.0823 -0.0659 372 PHE A O   
529  C CB  . PHE A 76  ? 1.5428 1.9946 1.3002 -0.7267 -0.0736 -0.0620 372 PHE A CB  
530  C CG  . PHE A 76  ? 1.5942 1.9048 1.2919 -0.7361 -0.0708 -0.0593 372 PHE A CG  
531  C CD1 . PHE A 76  ? 1.6853 1.8898 1.2856 -0.7867 -0.0711 -0.0575 372 PHE A CD1 
532  C CD2 . PHE A 76  ? 1.6066 1.8911 1.3401 -0.6939 -0.0677 -0.0577 372 PHE A CD2 
533  C CE1 . PHE A 76  ? 1.7434 1.8149 1.2815 -0.7891 -0.0687 -0.0545 372 PHE A CE1 
534  C CE2 . PHE A 76  ? 1.6789 1.8375 1.3557 -0.6993 -0.0651 -0.0547 372 PHE A CE2 
535  C CZ  . PHE A 76  ? 1.7532 1.8043 1.3313 -0.7444 -0.0657 -0.0532 372 PHE A CZ  
536  N N   . GLY A 77  ? 1.7894 2.0075 1.3893 -0.7852 -0.0886 -0.0736 373 GLY A N   
537  C CA  . GLY A 77  ? 1.9718 2.0910 1.4675 -0.8416 -0.0896 -0.0723 373 GLY A CA  
538  C C   . GLY A 77  ? 2.0255 2.1943 1.5033 -0.8779 -0.0950 -0.0754 373 GLY A C   
539  O O   . GLY A 77  ? 2.1609 2.2656 1.5494 -0.9344 -0.0954 -0.0730 373 GLY A O   
540  N N   . SER A 78  ? 1.8940 2.1731 1.4506 -0.8460 -0.0996 -0.0805 374 SER A N   
541  C CA  . SER A 78  ? 1.8582 2.1982 1.4067 -0.8753 -0.1053 -0.0838 374 SER A CA  
542  C C   . SER A 78  ? 1.8168 2.0276 1.3012 -0.8796 -0.1131 -0.0915 374 SER A C   
543  O O   . SER A 78  ? 1.8201 1.8940 1.2571 -0.8635 -0.1131 -0.0935 374 SER A O   
544  C CB  . SER A 78  ? 1.7946 2.2836 1.4419 -0.8315 -0.1083 -0.0866 374 SER A CB  
545  O OG  . SER A 78  ? 1.7417 2.1990 1.4385 -0.7666 -0.1129 -0.0929 374 SER A OG  
546  N N   . LYS A 79  ? 1.7273 1.9829 1.2067 -0.8997 -0.1199 -0.0960 375 LYS A N   
547  C CA  . LYS A 79  ? 1.7267 1.8670 1.1438 -0.9038 -0.1278 -0.1041 375 LYS A CA  
548  C C   . LYS A 79  ? 1.5878 1.6840 1.0480 -0.8342 -0.1329 -0.1133 375 LYS A C   
549  O O   . LYS A 79  ? 1.5601 1.5170 0.9608 -0.8207 -0.1345 -0.1184 375 LYS A O   
550  C CB  . LYS A 79  ? 1.7264 1.9391 1.1356 -0.9404 -0.1342 -0.1068 375 LYS A CB  
551  C CG  . LYS A 79  ? 1.7798 1.8727 1.1155 -0.9508 -0.1424 -0.1153 375 LYS A CG  
552  C CD  . LYS A 79  ? 1.9257 1.9090 1.1399 -1.0203 -0.1399 -0.1099 375 LYS A CD  
553  C CE  . LYS A 79  ? 1.9464 1.7869 1.0758 -1.0227 -0.1472 -0.1183 375 LYS A CE  
554  N NZ  . LYS A 79  ? 1.9196 1.6244 1.0250 -0.9672 -0.1463 -0.1233 375 LYS A NZ  
555  N N   . ALA A 80  ? 1.5236 1.7365 1.0811 -0.7882 -0.1353 -0.1154 376 ALA A N   
556  C CA  . ALA A 80  ? 1.4944 1.6742 1.0912 -0.7258 -0.1403 -0.1234 376 ALA A CA  
557  C C   . ALA A 80  ? 1.5163 1.5969 1.0981 -0.6996 -0.1344 -0.1221 376 ALA A C   
558  O O   . ALA A 80  ? 1.5342 1.5216 1.0952 -0.6665 -0.1374 -0.1297 376 ALA A O   
559  C CB  . ALA A 80  ? 1.3498 1.6715 1.0455 -0.6830 -0.1432 -0.1231 376 ALA A CB  
560  N N   . HIS A 81  ? 1.5593 1.6601 1.1482 -0.7133 -0.1257 -0.1126 377 HIS A N   
561  C CA  . HIS A 81  ? 1.5488 1.5570 1.1202 -0.6907 -0.1200 -0.1104 377 HIS A CA  
562  C C   . HIS A 81  ? 1.6962 1.5410 1.1598 -0.7094 -0.1198 -0.1126 377 HIS A C   
563  O O   . HIS A 81  ? 1.7002 1.4497 1.1423 -0.6706 -0.1212 -0.1188 377 HIS A O   
564  C CB  . HIS A 81  ? 1.5617 1.6274 1.1562 -0.7062 -0.1110 -0.0996 377 HIS A CB  
565  C CG  . HIS A 81  ? 1.6132 1.5830 1.1827 -0.6887 -0.1053 -0.0961 377 HIS A CG  
566  N ND1 . HIS A 81  ? 1.6408 1.6270 1.2063 -0.7080 -0.0971 -0.0866 377 HIS A ND1 
567  C CD2 . HIS A 81  ? 1.6278 1.4877 1.1729 -0.6519 -0.1064 -0.1010 377 HIS A CD2 
568  C CE1 . HIS A 81  ? 1.6292 1.5176 1.1698 -0.6843 -0.0940 -0.0854 377 HIS A CE1 
569  N NE2 . HIS A 81  ? 1.6559 1.4679 1.1837 -0.6492 -0.0993 -0.0939 377 HIS A NE2 
570  N N   . MET A 82  ? 1.8487 1.6577 1.2371 -0.7674 -0.1177 -0.1071 378 MET A N   
571  C CA  . MET A 82  ? 2.0085 1.6530 1.2809 -0.7846 -0.1171 -0.1070 378 MET A CA  
572  C C   . MET A 82  ? 1.9837 1.5456 1.2193 -0.7584 -0.1242 -0.1185 378 MET A C   
573  O O   . MET A 82  ? 2.0807 1.5007 1.2376 -0.7390 -0.1233 -0.1206 378 MET A O   
574  C CB  . MET A 82  ? 2.2084 1.8381 1.4023 -0.8579 -0.1148 -0.0988 378 MET A CB  
575  C CG  . MET A 82  ? 2.2918 1.9837 1.5020 -0.8859 -0.1067 -0.0876 378 MET A CG  
576  S SD  . MET A 82  ? 2.3961 1.9788 1.5794 -0.8499 -0.1002 -0.0826 378 MET A SD  
577  C CE  . MET A 82  ? 2.3923 2.0754 1.5996 -0.8921 -0.0917 -0.0706 378 MET A CE  
578  N N   . ASP A 83  ? 1.8032 1.4511 1.0908 -0.7530 -0.1313 -0.1259 379 ASP A N   
579  C CA  . ASP A 83  ? 1.7991 1.3740 1.0541 -0.7253 -0.1379 -0.1378 379 ASP A CA  
580  C C   . ASP A 83  ? 1.7027 1.2573 1.0023 -0.6568 -0.1377 -0.1450 379 ASP A C   
581  O O   . ASP A 83  ? 1.7154 1.1525 0.9541 -0.6262 -0.1378 -0.1520 379 ASP A O   
582  C CB  . ASP A 83  ? 1.7500 1.4210 1.0402 -0.7427 -0.1462 -0.1434 379 ASP A CB  
583  C CG  . ASP A 83  ? 1.9061 1.5378 1.1120 -0.8062 -0.1484 -0.1410 379 ASP A CG  
584  O OD1 . ASP A 83  ? 1.9268 1.6735 1.1664 -0.8446 -0.1507 -0.1375 379 ASP A OD1 
585  O OD2 . ASP A 83  ? 2.0613 1.5458 1.1621 -0.8169 -0.1474 -0.1418 379 ASP A OD2 
586  N N   . ARG A 84  ? 1.5818 1.2499 0.9823 -0.6309 -0.1369 -0.1430 380 ARG A N   
587  C CA  . ARG A 84  ? 1.5721 1.2243 1.0125 -0.5719 -0.1361 -0.1483 380 ARG A CA  
588  C C   . ARG A 84  ? 1.6959 1.2328 1.0828 -0.5544 -0.1286 -0.1446 380 ARG A C   
589  O O   . ARG A 84  ? 1.8032 1.2668 1.1710 -0.5079 -0.1275 -0.1514 380 ARG A O   
590  C CB  . ARG A 84  ? 1.4692 1.2632 1.0198 -0.5529 -0.1367 -0.1443 380 ARG A CB  
591  C CG  . ARG A 84  ? 1.3901 1.1735 0.9816 -0.4999 -0.1351 -0.1473 380 ARG A CG  
592  C CD  . ARG A 84  ? 1.3518 1.2035 0.9948 -0.4704 -0.1427 -0.1548 380 ARG A CD  
593  N NE  . ARG A 84  ? 1.2950 1.1205 0.9581 -0.4241 -0.1416 -0.1591 380 ARG A NE  
594  C CZ  . ARG A 84  ? 1.2113 0.9429 0.8238 -0.3938 -0.1402 -0.1676 380 ARG A CZ  
595  N NH1 . ARG A 84  ? 1.3602 1.0083 0.8933 -0.4102 -0.1429 -0.1760 380 ARG A NH1 
596  N NH2 . ARG A 84  ? 1.0674 0.8015 0.7201 -0.3315 -0.1300 -0.1606 380 ARG A NH2 
597  N N   . LEU A 85  ? 1.6617 1.1849 1.0217 -0.5889 -0.1229 -0.1336 381 LEU A N   
598  C CA  . LEU A 85  ? 1.7574 1.1594 1.0490 -0.5760 -0.1166 -0.1288 381 LEU A CA  
599  C C   . LEU A 85  ? 1.8280 1.0844 1.0128 -0.5621 -0.1179 -0.1348 381 LEU A C   
600  O O   . LEU A 85  ? 1.8365 1.0119 0.9944 -0.5095 -0.1157 -0.1393 381 LEU A O   
601  C CB  . LEU A 85  ? 1.8273 1.2367 1.0915 -0.6259 -0.1114 -0.1160 381 LEU A CB  
602  C CG  . LEU A 85  ? 1.9028 1.2524 1.1442 -0.6118 -0.1044 -0.1076 381 LEU A CG  
603  C CD1 . LEU A 85  ? 1.6956 1.1420 1.0431 -0.5777 -0.1021 -0.1068 381 LEU A CD1 
604  C CD2 . LEU A 85  ? 2.0617 1.4006 1.2489 -0.6703 -0.1002 -0.0962 381 LEU A CD2 
605  N N   . GLU A 86  ? 1.9435 1.1685 1.0640 -0.6070 -0.1214 -0.1347 382 GLU A N   
606  C CA  . GLU A 86  ? 2.1036 1.1934 1.1189 -0.5948 -0.1233 -0.1404 382 GLU A CA  
607  C C   . GLU A 86  ? 1.9529 1.0394 0.9957 -0.5364 -0.1261 -0.1540 382 GLU A C   
608  O O   . GLU A 86  ? 1.9708 0.9468 0.9488 -0.4893 -0.1233 -0.1579 382 GLU A O   
609  C CB  . GLU A 86  ? 2.3095 1.3932 1.2683 -0.6575 -0.1280 -0.1390 382 GLU A CB  
610  C CG  . GLU A 86  ? 2.5527 1.4958 1.3965 -0.6497 -0.1306 -0.1442 382 GLU A CG  
611  C CD  . GLU A 86  ? 2.8153 1.6117 1.5316 -0.6659 -0.1268 -0.1340 382 GLU A CD  
612  O OE1 . GLU A 86  ? 2.9861 1.6587 1.5940 -0.6634 -0.1290 -0.1361 382 GLU A OE1 
613  O OE2 . GLU A 86  ? 2.8479 1.6499 1.5671 -0.6802 -0.1218 -0.1235 382 GLU A OE2 
614  N N   . GLU A 87  ? 1.8154 1.0258 0.9513 -0.5354 -0.1311 -0.1605 383 GLU A N   
615  C CA  . GLU A 87  ? 1.7474 0.9632 0.9069 -0.4860 -0.1340 -0.1736 383 GLU A CA  
616  C C   . GLU A 87  ? 1.7025 0.8837 0.8776 -0.4225 -0.1278 -0.1759 383 GLU A C   
617  O O   . GLU A 87  ? 1.6940 0.8088 0.8304 -0.3734 -0.1259 -0.1847 383 GLU A O   
618  C CB  . GLU A 87  ? 1.6612 1.0240 0.9180 -0.4987 -0.1411 -0.1772 383 GLU A CB  
619  C CG  . GLU A 87  ? 1.6833 1.0667 0.9714 -0.4504 -0.1442 -0.1893 383 GLU A CG  
620  C CD  . GLU A 87  ? 1.5805 1.1063 0.9564 -0.4624 -0.1523 -0.1906 383 GLU A CD  
621  O OE1 . GLU A 87  ? 1.4575 1.0851 0.9102 -0.4720 -0.1522 -0.1820 383 GLU A OE1 
622  O OE2 . GLU A 87  ? 1.4938 1.0293 0.8585 -0.4588 -0.1587 -0.1993 383 GLU A OE2 
623  N N   . VAL A 88  ? 1.6067 0.8376 0.8386 -0.4206 -0.1241 -0.1678 384 VAL A N   
624  C CA  . VAL A 88  ? 1.5937 0.7999 0.8436 -0.3625 -0.1186 -0.1695 384 VAL A CA  
625  C C   . VAL A 88  ? 1.7620 0.8302 0.9151 -0.3323 -0.1121 -0.1659 384 VAL A C   
626  O O   . VAL A 88  ? 1.8422 0.8593 0.9735 -0.2702 -0.1075 -0.1710 384 VAL A O   
627  C CB  . VAL A 88  ? 1.5810 0.8854 0.9219 -0.3707 -0.1175 -0.1617 384 VAL A CB  
628  C CG1 . VAL A 88  ? 1.5941 0.8629 0.9435 -0.3149 -0.1118 -0.1622 384 VAL A CG1 
629  C CG2 . VAL A 88  ? 1.4719 0.9118 0.9045 -0.3849 -0.1243 -0.1647 384 VAL A CG2 
630  N N   . ASN A 89  ? 1.8163 0.8265 0.9066 -0.3725 -0.1112 -0.1559 385 ASN A N   
631  C CA  . ASN A 89  ? 2.0435 0.9136 1.0247 -0.3461 -0.1069 -0.1509 385 ASN A CA  
632  C C   . ASN A 89  ? 2.1164 0.9050 1.0267 -0.3065 -0.1074 -0.1603 385 ASN A C   
633  O O   . ASN A 89  ? 2.1619 0.8798 1.0281 -0.2417 -0.1024 -0.1613 385 ASN A O   
634  C CB  . ASN A 89  ? 2.2277 1.0495 1.1414 -0.4079 -0.1076 -0.1393 385 ASN A CB  
635  C CG  . ASN A 89  ? 2.3984 1.0813 1.2016 -0.3825 -0.1036 -0.1307 385 ASN A CG  
636  O OD1 . ASN A 89  ? 2.5686 1.1432 1.2614 -0.3942 -0.1054 -0.1287 385 ASN A OD1 
637  N ND2 . ASN A 89  ? 2.2708 0.9546 1.0984 -0.3474 -0.0989 -0.1251 385 ASN A ND2 
638  N N   . LYS A 90  ? 2.1323 0.9379 1.0329 -0.3415 -0.1132 -0.1668 386 LYS A N   
639  C CA  . LYS A 90  ? 2.2349 0.9670 1.0687 -0.3058 -0.1137 -0.1760 386 LYS A CA  
640  C C   . LYS A 90  ? 2.1416 0.9122 1.0260 -0.2340 -0.1093 -0.1863 386 LYS A C   
641  O O   . LYS A 90  ? 2.1513 0.8463 0.9735 -0.1756 -0.1046 -0.1897 386 LYS A O   
642  C CB  . LYS A 90  ? 2.3270 1.0882 1.1548 -0.3598 -0.1215 -0.1816 386 LYS A CB  
643  C CG  . LYS A 90  ? 2.4574 1.1697 1.2151 -0.4307 -0.1250 -0.1717 386 LYS A CG  
644  C CD  . LYS A 90  ? 2.4387 1.2380 1.2346 -0.4894 -0.1328 -0.1761 386 LYS A CD  
645  C CE  . LYS A 90  ? 2.5728 1.2917 1.2652 -0.5501 -0.1362 -0.1698 386 LYS A CE  
646  N NZ  . LYS A 90  ? 2.5338 1.3547 1.2709 -0.6093 -0.1437 -0.1727 386 LYS A NZ  
647  N N   . GLU A 91  ? 2.0286 0.9180 1.0210 -0.2354 -0.1103 -0.1901 387 GLU A N   
648  C CA  . GLU A 91  ? 1.9816 0.9104 1.0181 -0.1708 -0.1053 -0.1989 387 GLU A CA  
649  C C   . GLU A 91  ? 2.0314 0.9256 1.0602 -0.1110 -0.0963 -0.1931 387 GLU A C   
650  O O   . GLU A 91  ? 2.0150 0.9095 1.0433 -0.0433 -0.0891 -0.1984 387 GLU A O   
651  C CB  . GLU A 91  ? 1.8714 0.9304 1.0141 -0.1937 -0.1107 -0.2032 387 GLU A CB  
652  C CG  . GLU A 91  ? 1.7818 0.9166 0.9944 -0.1285 -0.1020 -0.2017 387 GLU A CG  
653  C CD  . GLU A 91  ? 1.7050 0.9902 1.0382 -0.1461 -0.1040 -0.1936 387 GLU A CD  
654  O OE1 . GLU A 91  ? 1.6283 0.9869 1.0228 -0.1015 -0.0966 -0.1887 387 GLU A OE1 
655  O OE2 . GLU A 91  ? 1.7217 1.0515 1.0833 -0.2039 -0.1130 -0.1917 387 GLU A OE2 
656  N N   . ILE A 92  ? 2.0314 0.9046 1.0555 -0.1327 -0.0959 -0.1815 388 ILE A N   
657  C CA  . ILE A 92  ? 1.9653 0.7985 0.9711 -0.0749 -0.0885 -0.1746 388 ILE A CA  
658  C C   . ILE A 92  ? 2.1159 0.8291 1.0075 -0.0350 -0.0854 -0.1709 388 ILE A C   
659  O O   . ILE A 92  ? 2.1243 0.8143 0.9954 0.0350  -0.0789 -0.1678 388 ILE A O   
660  C CB  . ILE A 92  ? 1.8826 0.7333 0.9185 -0.1103 -0.0893 -0.1630 388 ILE A CB  
661  C CG1 . ILE A 92  ? 1.7588 0.7320 0.9068 -0.1438 -0.0928 -0.1655 388 ILE A CG1 
662  C CG2 . ILE A 92  ? 1.9292 0.7420 0.9456 -0.0488 -0.0826 -0.1555 388 ILE A CG2 
663  C CD1 . ILE A 92  ? 1.7090 0.7104 0.8898 -0.1858 -0.0935 -0.1537 388 ILE A CD1 
664  N N   . GLU A 93  ? 2.2883 0.9273 1.1014 -0.0770 -0.0906 -0.1699 389 GLU A N   
665  C CA  . GLU A 93  ? 2.4397 0.9637 1.1388 -0.0353 -0.0890 -0.1683 389 GLU A CA  
666  C C   . GLU A 93  ? 2.4060 0.9574 1.1174 0.0246  -0.0847 -0.1796 389 GLU A C   
667  O O   . GLU A 93  ? 2.3735 0.9046 1.0580 0.1008  -0.0781 -0.1777 389 GLU A O   
668  C CB  . GLU A 93  ? 2.5952 1.0341 1.2052 -0.0995 -0.0960 -0.1652 389 GLU A CB  
669  C CG  . GLU A 93  ? 2.7162 1.1125 1.2889 -0.1538 -0.0984 -0.1520 389 GLU A CG  
670  C CD  . GLU A 93  ? 2.9067 1.1976 1.3873 -0.1055 -0.0953 -0.1412 389 GLU A CD  
671  O OE1 . GLU A 93  ? 2.9819 1.2115 1.4010 -0.0365 -0.0930 -0.1429 389 GLU A OE1 
672  O OE2 . GLU A 93  ? 2.9630 1.2368 1.4311 -0.1346 -0.0954 -0.1305 389 GLU A OE2 
673  N N   . SER A 94  ? 2.4634 1.0738 1.2196 -0.0082 -0.0882 -0.1907 390 SER A N   
674  C CA  . SER A 94  ? 2.4561 1.0848 1.2109 0.0391  -0.0843 -0.2016 390 SER A CA  
675  C C   . SER A 94  ? 2.4081 1.1188 1.2312 0.1114  -0.0741 -0.2038 390 SER A C   
676  O O   . SER A 94  ? 2.3593 1.0544 1.1482 0.1809  -0.0666 -0.2042 390 SER A O   
677  C CB  . SER A 94  ? 2.4316 1.1197 1.2290 -0.0164 -0.0913 -0.2122 390 SER A CB  
678  O OG  . SER A 94  ? 2.4004 1.1760 1.2629 0.0230  -0.0862 -0.2222 390 SER A OG  
679  N N   . THR A 95  ? 2.3480 1.1527 1.2672 0.0960  -0.0736 -0.2041 391 THR A N   
680  C CA  . THR A 95  ? 2.3052 1.2033 1.2977 0.1546  -0.0641 -0.2065 391 THR A CA  
681  C C   . THR A 95  ? 2.2443 1.1549 1.2598 0.1888  -0.0591 -0.1957 391 THR A C   
682  O O   . THR A 95  ? 2.1323 1.1325 1.2107 0.2422  -0.0498 -0.1917 391 THR A O   
683  C CB  . THR A 95  ? 2.2253 1.2559 1.3345 0.1150  -0.0665 -0.2050 391 THR A CB  
684  O OG1 . THR A 95  ? 2.3442 1.3489 1.4336 0.0419  -0.0788 -0.2122 391 THR A OG1 
685  C CG2 . THR A 95  ? 2.1167 1.2406 1.2785 0.1606  -0.0571 -0.2049 391 THR A CG2 
686  N N   . SER A 96  ? 2.2845 1.1281 1.2621 0.1554  -0.0646 -0.1862 392 SER A N   
687  C CA  . SER A 96  ? 2.2656 1.1243 1.2700 0.1762  -0.0618 -0.1757 392 SER A CA  
688  C C   . SER A 96  ? 2.0732 1.0654 1.2063 0.1559  -0.0606 -0.1710 392 SER A C   
689  O O   . SER A 96  ? 2.0578 1.1163 1.2485 0.1903  -0.0551 -0.1597 392 SER A O   
690  C CB  . SER A 96  ? 2.3579 1.2115 1.3321 0.2632  -0.0534 -0.1689 392 SER A CB  
691  O OG  . SER A 96  ? 2.2697 1.2239 1.3053 0.3146  -0.0444 -0.1745 392 SER A OG  
692  N N   . THR A 97  ? 1.8759 0.9328 1.0687 0.0976  -0.0659 -0.1722 393 THR A N   
693  C CA  . THR A 97  ? 1.6203 0.8151 0.9412 0.0662  -0.0662 -0.1606 393 THR A CA  
694  C C   . THR A 97  ? 1.5647 0.7804 0.9009 0.0000  -0.0753 -0.1663 393 THR A C   
695  O O   . THR A 97  ? 1.6404 0.7601 0.8878 -0.0308 -0.0821 -0.1777 393 THR A O   
696  C CB  . THR A 97  ? 1.4678 0.7820 0.8764 0.1137  -0.0570 -0.1535 393 THR A CB  
697  O OG1 . THR A 97  ? 1.4061 0.8327 0.9225 0.0818  -0.0583 -0.1424 393 THR A OG1 
698  C CG2 . THR A 97  ? 1.5214 0.8489 0.9165 0.1310  -0.0545 -0.1627 393 THR A CG2 
699  N N   . TYR A 98  ? 1.4462 0.7848 0.8883 -0.0220 -0.0761 -0.1584 394 TYR A N   
700  C CA  . TYR A 98  ? 1.4134 0.7873 0.8741 -0.0774 -0.0853 -0.1632 394 TYR A CA  
701  C C   . TYR A 98  ? 1.2909 0.7998 0.8640 -0.0759 -0.0839 -0.1538 394 TYR A C   
702  O O   . TYR A 98  ? 1.1958 0.7624 0.8277 -0.0417 -0.0763 -0.1436 394 TYR A O   
703  C CB  . TYR A 98  ? 1.4227 0.7541 0.8492 -0.1407 -0.0939 -0.1643 394 TYR A CB  
704  C CG  . TYR A 98  ? 1.4164 0.8149 0.9138 -0.1562 -0.0926 -0.1514 394 TYR A CG  
705  C CD1 . TYR A 98  ? 1.3505 0.8539 0.9254 -0.1926 -0.0973 -0.1467 394 TYR A CD1 
706  C CD2 . TYR A 98  ? 1.4157 0.7725 0.8980 -0.1309 -0.0868 -0.1443 394 TYR A CD2 
707  C CE1 . TYR A 98  ? 1.2504 0.8129 0.8843 -0.2033 -0.0956 -0.1360 394 TYR A CE1 
708  C CE2 . TYR A 98  ? 1.3347 0.7514 0.8790 -0.1455 -0.0855 -0.1330 394 TYR A CE2 
709  C CZ  . TYR A 98  ? 1.2265 0.7443 0.8453 -0.1819 -0.0895 -0.1293 394 TYR A CZ  
710  O OH  . TYR A 98  ? 1.1581 0.7353 0.8342 -0.1933 -0.0878 -0.1192 394 TYR A OH  
711  N N   . GLN A 99  ? 1.3465 0.9019 0.9419 -0.1133 -0.0920 -0.1574 395 GLN A N   
712  C CA  . GLN A 99  ? 1.2043 0.8726 0.8888 -0.1107 -0.0923 -0.1495 395 GLN A CA  
713  C C   . GLN A 99  ? 1.1008 0.8262 0.8244 -0.1582 -0.1010 -0.1463 395 GLN A C   
714  O O   . GLN A 99  ? 1.1228 0.8191 0.8035 -0.2036 -0.1097 -0.1540 395 GLN A O   
715  C CB  . GLN A 99  ? 1.1700 0.8556 0.8471 -0.1003 -0.0939 -0.1561 395 GLN A CB  
716  C CG  . GLN A 99  ? 1.1358 0.7865 0.7821 -0.0492 -0.0835 -0.1588 395 GLN A CG  
717  C CD  . GLN A 99  ? 1.1786 0.8921 0.8877 -0.0105 -0.0728 -0.1460 395 GLN A CD  
718  O OE1 . GLN A 99  ? 1.1586 0.9492 0.9376 -0.0192 -0.0736 -0.1357 395 GLN A OE1 
719  N NE2 . GLN A 99  ? 1.2117 0.8922 0.8905 0.0330  -0.0632 -0.1467 395 GLN A NE2 
720  N N   . LEU A 100 ? 0.9603 0.7677 0.7603 -0.1485 -0.0987 -0.1349 396 LEU A N   
721  C CA  . LEU A 100 ? 0.8490 0.7249 0.6905 -0.1829 -0.1058 -0.1312 396 LEU A CA  
722  C C   . LEU A 100 ? 0.8869 0.8262 0.7486 -0.1939 -0.1143 -0.1345 396 LEU A C   
723  O O   . LEU A 100 ? 0.8683 0.8240 0.7429 -0.1649 -0.1123 -0.1336 396 LEU A O   
724  C CB  . LEU A 100 ? 0.7330 0.6647 0.6391 -0.1625 -0.1003 -0.1187 396 LEU A CB  
725  C CG  . LEU A 100 ? 0.7815 0.6639 0.6732 -0.1561 -0.0936 -0.1144 396 LEU A CG  
726  C CD1 . LEU A 100 ? 0.7689 0.7018 0.7201 -0.1305 -0.0881 -0.1027 396 LEU A CD1 
727  C CD2 . LEU A 100 ? 0.9334 0.7959 0.7970 -0.2022 -0.0984 -0.1172 396 LEU A CD2 
728  N N   . LYS A 101 ? 0.8847 0.8661 0.7490 -0.2363 -0.1239 -0.1377 397 LYS A N   
729  C CA  . LYS A 101 ? 0.9329 0.9993 0.8297 -0.2416 -0.1330 -0.1382 397 LYS A CA  
730  C C   . LYS A 101 ? 0.8840 1.0208 0.8469 -0.2055 -0.1295 -0.1262 397 LYS A C   
731  O O   . LYS A 101 ? 0.8460 0.9838 0.8346 -0.1933 -0.1225 -0.1183 397 LYS A O   
732  C CB  . LYS A 101 ? 0.9198 1.0341 0.8095 -0.2950 -0.1438 -0.1431 397 LYS A CB  
733  C CG  . LYS A 101 ? 1.0437 1.0856 0.8570 -0.3409 -0.1499 -0.1556 397 LYS A CG  
734  C CD  . LYS A 101 ? 1.1272 1.1557 0.9131 -0.3327 -0.1559 -0.1640 397 LYS A CD  
735  C CE  . LYS A 101 ? 1.2914 1.2214 0.9864 -0.3714 -0.1608 -0.1775 397 LYS A CE  
736  N NZ  . LYS A 101 ? 1.3217 1.2278 0.9865 -0.3544 -0.1645 -0.1858 397 LYS A NZ  
737  N N   . ASP A 102 ? 0.7140 0.9029 0.6968 -0.1881 -0.1349 -0.1249 398 ASP A N   
738  C CA  . ASP A 102 ? 0.7589 1.0035 0.7894 -0.1548 -0.1333 -0.1138 398 ASP A CA  
739  C C   . ASP A 102 ? 0.7228 1.0246 0.7856 -0.1652 -0.1348 -0.1093 398 ASP A C   
740  O O   . ASP A 102 ? 0.6816 0.9902 0.7718 -0.1406 -0.1286 -0.1004 398 ASP A O   
741  C CB  . ASP A 102 ? 0.9302 1.2222 0.9656 -0.1390 -0.1416 -0.1136 398 ASP A CB  
742  C CG  . ASP A 102 ? 1.0549 1.2998 1.0703 -0.1150 -0.1366 -0.1128 398 ASP A CG  
743  O OD1 . ASP A 102 ? 1.0926 1.2746 1.0891 -0.1115 -0.1270 -0.1142 398 ASP A OD1 
744  O OD2 . ASP A 102 ? 1.0802 1.3549 1.0969 -0.0976 -0.1420 -0.1103 398 ASP A OD2 
745  N N   . THR A 103 ? 0.7031 1.0495 0.7605 -0.2036 -0.1430 -0.1156 399 THR A N   
746  C CA  . THR A 103 ? 0.7586 1.1698 0.8457 -0.2159 -0.1433 -0.1116 399 THR A CA  
747  C C   . THR A 103 ? 0.8016 1.1565 0.8852 -0.2226 -0.1328 -0.1079 399 THR A C   
748  O O   . THR A 103 ? 0.7565 1.1449 0.8713 -0.2081 -0.1284 -0.1007 399 THR A O   
749  C CB  . THR A 103 ? 0.7657 1.2393 0.8426 -0.2652 -0.1537 -0.1192 399 THR A CB  
750  O OG1 . THR A 103 ? 0.8900 1.2832 0.9129 -0.3070 -0.1543 -0.1281 399 THR A OG1 
751  C CG2 . THR A 103 ? 0.6339 1.1848 0.7222 -0.2524 -0.1648 -0.1210 399 THR A CG2 
752  N N   . GLU A 104 ? 0.8714 1.1378 0.9115 -0.2418 -0.1292 -0.1130 400 GLU A N   
753  C CA  . GLU A 104 ? 0.8361 1.0421 0.8638 -0.2460 -0.1203 -0.1097 400 GLU A CA  
754  C C   . GLU A 104 ? 0.7955 0.9818 0.8501 -0.1992 -0.1116 -0.1009 400 GLU A C   
755  O O   . GLU A 104 ? 0.7745 0.9586 0.8457 -0.1936 -0.1057 -0.0945 400 GLU A O   
756  C CB  . GLU A 104 ? 0.8366 0.9447 0.7985 -0.2700 -0.1198 -0.1178 400 GLU A CB  
757  C CG  . GLU A 104 ? 0.8304 0.9454 0.7544 -0.3274 -0.1287 -0.1262 400 GLU A CG  
758  C CD  . GLU A 104 ? 1.0438 1.0493 0.8876 -0.3477 -0.1303 -0.1362 400 GLU A CD  
759  O OE1 . GLU A 104 ? 1.1448 1.1385 0.9434 -0.4024 -0.1380 -0.1435 400 GLU A OE1 
760  O OE2 . GLU A 104 ? 1.1133 1.0458 0.9346 -0.3097 -0.1239 -0.1368 400 GLU A OE2 
761  N N   . LEU A 105 ? 0.6804 0.8537 0.7365 -0.1689 -0.1107 -0.1003 401 LEU A N   
762  C CA  . LEU A 105 ? 0.7373 0.8991 0.8157 -0.1315 -0.1032 -0.0917 401 LEU A CA  
763  C C   . LEU A 105 ? 0.6993 0.9189 0.8173 -0.1168 -0.1039 -0.0837 401 LEU A C   
764  O O   . LEU A 105 ? 0.5871 0.7946 0.7195 -0.1032 -0.0979 -0.0769 401 LEU A O   
765  C CB  . LEU A 105 ? 0.7155 0.8625 0.7847 -0.1090 -0.1024 -0.0922 401 LEU A CB  
766  C CG  . LEU A 105 ? 0.6449 0.7740 0.7263 -0.0791 -0.0939 -0.0839 401 LEU A CG  
767  C CD1 . LEU A 105 ? 0.6514 0.7266 0.7114 -0.0743 -0.0863 -0.0855 401 LEU A CD1 
768  C CD2 . LEU A 105 ? 0.6760 0.8141 0.7535 -0.0625 -0.0945 -0.0825 401 LEU A CD2 
769  N N   . ILE A 106 ? 0.6290 0.9119 0.7603 -0.1172 -0.1116 -0.0847 402 ILE A N   
770  C CA  . ILE A 106 ? 0.6213 0.9552 0.7804 -0.0947 -0.1125 -0.0778 402 ILE A CA  
771  C C   . ILE A 106 ? 0.6030 0.9599 0.7761 -0.1107 -0.1094 -0.0765 402 ILE A C   
772  O O   . ILE A 106 ? 0.5962 0.9528 0.7837 -0.0912 -0.1048 -0.0701 402 ILE A O   
773  C CB  . ILE A 106 ? 0.6303 1.0299 0.7942 -0.0839 -0.1223 -0.0794 402 ILE A CB  
774  C CG1 . ILE A 106 ? 0.6092 0.9774 0.7561 -0.0640 -0.1240 -0.0784 402 ILE A CG1 
775  C CG2 . ILE A 106 ? 0.6408 1.0944 0.8242 -0.0553 -0.1237 -0.0735 402 ILE A CG2 
776  C CD1 . ILE A 106 ? 0.5858 1.0085 0.7277 -0.0582 -0.1351 -0.0819 402 ILE A CD1 
777  N N   . TYR A 107 ? 0.6062 0.9794 0.7695 -0.1499 -0.1119 -0.0827 403 TYR A N   
778  C CA  . TYR A 107 ? 0.6393 1.0279 0.8090 -0.1723 -0.1079 -0.0811 403 TYR A CA  
779  C C   . TYR A 107 ? 0.6744 0.9893 0.8363 -0.1640 -0.0991 -0.0765 403 TYR A C   
780  O O   . TYR A 107 ? 0.5563 0.8838 0.7364 -0.1507 -0.0944 -0.0706 403 TYR A O   
781  C CB  . TYR A 107 ? 0.7220 1.1214 0.8679 -0.2250 -0.1121 -0.0884 403 TYR A CB  
782  C CG  . TYR A 107 ? 0.7689 1.1709 0.9109 -0.2559 -0.1069 -0.0861 403 TYR A CG  
783  C CD1 . TYR A 107 ? 0.7994 1.2958 0.9648 -0.2707 -0.1076 -0.0844 403 TYR A CD1 
784  C CD2 . TYR A 107 ? 0.8162 1.1268 0.9271 -0.2667 -0.1006 -0.0848 403 TYR A CD2 
785  C CE1 . TYR A 107 ? 0.7911 1.2802 0.9465 -0.2950 -0.0992 -0.0796 403 TYR A CE1 
786  C CE2 . TYR A 107 ? 0.7947 1.1006 0.8959 -0.2951 -0.0958 -0.0817 403 TYR A CE2 
787  C CZ  . TYR A 107 ? 0.7775 1.1773 0.9032 -0.3148 -0.0958 -0.0798 403 TYR A CZ  
788  O OH  . TYR A 107 ? 0.7268 1.1147 0.8372 -0.3382 -0.0879 -0.0743 403 TYR A OH  
789  N N   . GLY A 108 ? 0.6140 0.8540 0.7460 -0.1685 -0.0970 -0.0793 404 GLY A N   
790  C CA  . GLY A 108 ? 0.6064 0.7843 0.7292 -0.1569 -0.0896 -0.0750 404 GLY A CA  
791  C C   . GLY A 108 ? 0.6743 0.8622 0.8254 -0.1216 -0.0859 -0.0671 404 GLY A C   
792  O O   . GLY A 108 ? 0.5522 0.7309 0.7116 -0.1167 -0.0815 -0.0619 404 GLY A O   
793  N N   . ALA A 109 ? 0.6776 0.8793 0.8377 -0.0992 -0.0881 -0.0658 405 ALA A N   
794  C CA  . ALA A 109 ? 0.6137 0.8143 0.7888 -0.0720 -0.0854 -0.0582 405 ALA A CA  
795  C C   . ALA A 109 ? 0.5869 0.8259 0.7792 -0.0650 -0.0860 -0.0545 405 ALA A C   
796  O O   . ALA A 109 ? 0.5744 0.7972 0.7717 -0.0557 -0.0821 -0.0492 405 ALA A O   
797  C CB  . ALA A 109 ? 0.5412 0.7449 0.7124 -0.0543 -0.0882 -0.0570 405 ALA A CB  
798  N N   . LYS A 110 ? 0.4591 0.7540 0.6589 -0.0680 -0.0909 -0.0576 406 LYS A N   
799  C CA  . LYS A 110 ? 0.5380 0.8774 0.7513 -0.0536 -0.0908 -0.0546 406 LYS A CA  
800  C C   . LYS A 110 ? 0.5766 0.9114 0.7955 -0.0706 -0.0850 -0.0532 406 LYS A C   
801  O O   . LYS A 110 ? 0.6139 0.9562 0.8387 -0.0535 -0.0822 -0.0492 406 LYS A O   
802  C CB  . LYS A 110 ? 0.5689 0.9858 0.7908 -0.0532 -0.0971 -0.0585 406 LYS A CB  
803  C CG  . LYS A 110 ? 0.4975 0.9256 0.7114 -0.0210 -0.1033 -0.0574 406 LYS A CG  
804  C CD  . LYS A 110 ? 0.5078 1.0231 0.7307 -0.0202 -0.1109 -0.0617 406 LYS A CD  
805  C CE  . LYS A 110 ? 0.5421 1.0622 0.7501 0.0166  -0.1179 -0.0599 406 LYS A CE  
806  N NZ  . LYS A 110 ? 0.6128 1.2318 0.8304 0.0312  -0.1257 -0.0626 406 LYS A NZ  
807  N N   . HIS A 111 ? 0.5401 0.8548 0.7494 -0.1035 -0.0835 -0.0566 407 HIS A N   
808  C CA  . HIS A 111 ? 0.5597 0.8639 0.7664 -0.1225 -0.0782 -0.0546 407 HIS A CA  
809  C C   . HIS A 111 ? 0.6277 0.8657 0.8256 -0.1119 -0.0736 -0.0501 407 HIS A C   
810  O O   . HIS A 111 ? 0.5473 0.7800 0.7471 -0.1137 -0.0694 -0.0462 407 HIS A O   
811  C CB  . HIS A 111 ? 0.5842 0.8892 0.7720 -0.1657 -0.0792 -0.0595 407 HIS A CB  
812  C CG  . HIS A 111 ? 0.6192 1.0127 0.8213 -0.1840 -0.0824 -0.0623 407 HIS A CG  
813  N ND1 . HIS A 111 ? 0.6189 1.0651 0.8303 -0.1777 -0.0895 -0.0663 407 HIS A ND1 
814  C CD2 . HIS A 111 ? 0.5847 1.0343 0.7948 -0.2060 -0.0793 -0.0609 407 HIS A CD2 
815  C CE1 . HIS A 111 ? 0.6162 1.1528 0.8423 -0.1944 -0.0913 -0.0677 407 HIS A CE1 
816  N NE2 . HIS A 111 ? 0.6595 1.2021 0.8857 -0.2132 -0.0847 -0.0645 407 HIS A NE2 
817  N N   . ALA A 112 ? 0.5745 0.7701 0.7631 -0.1001 -0.0743 -0.0502 408 ALA A N   
818  C CA  . ALA A 112 ? 0.5064 0.6618 0.6932 -0.0841 -0.0708 -0.0450 408 ALA A CA  
819  C C   . ALA A 112 ? 0.5721 0.7448 0.7737 -0.0653 -0.0704 -0.0397 408 ALA A C   
820  O O   . ALA A 112 ? 0.5606 0.7147 0.7622 -0.0618 -0.0677 -0.0355 408 ALA A O   
821  C CB  . ALA A 112 ? 0.5094 0.6386 0.6879 -0.0726 -0.0713 -0.0458 408 ALA A CB  
822  N N   . TRP A 113 ? 0.4637 0.6671 0.6714 -0.0515 -0.0736 -0.0401 409 TRP A N   
823  C CA  . TRP A 113 ? 0.4962 0.7034 0.7036 -0.0312 -0.0736 -0.0359 409 TRP A CA  
824  C C   . TRP A 113 ? 0.4884 0.7268 0.7029 -0.0338 -0.0709 -0.0362 409 TRP A C   
825  O O   . TRP A 113 ? 0.5837 0.8050 0.7946 -0.0276 -0.0683 -0.0328 409 TRP A O   
826  C CB  . TRP A 113 ? 0.4413 0.6619 0.6405 -0.0102 -0.0782 -0.0361 409 TRP A CB  
827  C CG  . TRP A 113 ? 0.4556 0.6639 0.6381 0.0147  -0.0792 -0.0325 409 TRP A CG  
828  C CD1 . TRP A 113 ? 0.4908 0.6736 0.6653 0.0177  -0.0765 -0.0294 409 TRP A CD1 
829  C CD2 . TRP A 113 ? 0.5271 0.7388 0.6887 0.0424  -0.0837 -0.0320 409 TRP A CD2 
830  N NE1 . TRP A 113 ? 0.5195 0.6842 0.6655 0.0445  -0.0790 -0.0276 409 TRP A NE1 
831  C CE2 . TRP A 113 ? 0.5902 0.7700 0.7258 0.0622  -0.0833 -0.0289 409 TRP A CE2 
832  C CE3 . TRP A 113 ? 0.5274 0.7627 0.6841 0.0544  -0.0887 -0.0339 409 TRP A CE3 
833  C CZ2 . TRP A 113 ? 0.6128 0.7738 0.7108 0.0958  -0.0875 -0.0276 409 TRP A CZ2 
834  C CZ3 . TRP A 113 ? 0.6527 0.8775 0.7776 0.0888  -0.0930 -0.0319 409 TRP A CZ3 
835  C CH2 . TRP A 113 ? 0.6833 0.8672 0.7762 0.1107  -0.0923 -0.0288 409 TRP A CH2 
836  N N   . ARG A 114 ? 0.4784 0.7681 0.7019 -0.0451 -0.0715 -0.0402 410 ARG A N   
837  C CA  . ARG A 114 ? 0.5034 0.8378 0.7350 -0.0525 -0.0677 -0.0404 410 ARG A CA  
838  C C   . ARG A 114 ? 0.6016 0.8999 0.8280 -0.0707 -0.0625 -0.0374 410 ARG A C   
839  O O   . ARG A 114 ? 0.5328 0.8487 0.7612 -0.0666 -0.0584 -0.0353 410 ARG A O   
840  C CB  . ARG A 114 ? 0.5078 0.9046 0.7481 -0.0761 -0.0694 -0.0450 410 ARG A CB  
841  C CG  . ARG A 114 ? 0.5102 0.9777 0.7614 -0.0849 -0.0654 -0.0451 410 ARG A CG  
842  C CD  . ARG A 114 ? 0.4726 1.0037 0.7295 -0.1208 -0.0679 -0.0494 410 ARG A CD  
843  N NE  . ARG A 114 ? 0.5272 1.1538 0.7992 -0.1256 -0.0643 -0.0493 410 ARG A NE  
844  C CZ  . ARG A 114 ? 0.6248 1.3276 0.9024 -0.1574 -0.0656 -0.0521 410 ARG A CZ  
845  N NH1 . ARG A 114 ? 0.6013 1.3744 0.8812 -0.1537 -0.0583 -0.0496 410 ARG A NH1 
846  N NH2 . ARG A 114 ? 0.6861 1.3657 0.9490 -0.1862 -0.0706 -0.0554 410 ARG A NH2 
847  N N   . ASN A 115 ? 0.5891 0.8363 0.8049 -0.0866 -0.0627 -0.0372 411 ASN A N   
848  C CA  . ASN A 115 ? 0.5790 0.7860 0.7824 -0.1005 -0.0588 -0.0340 411 ASN A CA  
849  C C   . ASN A 115 ? 0.5550 0.7238 0.7566 -0.0805 -0.0587 -0.0293 411 ASN A C   
850  O O   . ASN A 115 ? 0.5451 0.6838 0.7362 -0.0865 -0.0564 -0.0260 411 ASN A O   
851  C CB  . ASN A 115 ? 0.5120 0.6786 0.6936 -0.1228 -0.0595 -0.0364 411 ASN A CB  
852  C CG  . ASN A 115 ? 0.6178 0.8148 0.7916 -0.1551 -0.0599 -0.0406 411 ASN A CG  
853  O OD1 . ASN A 115 ? 0.6197 0.8759 0.8074 -0.1643 -0.0581 -0.0405 411 ASN A OD1 
854  N ND2 . ASN A 115 ? 0.6248 0.7842 0.7726 -0.1737 -0.0624 -0.0448 411 ASN A ND2 
855  N N   . ALA A 116 ? 0.5053 0.6737 0.7120 -0.0594 -0.0617 -0.0286 412 ALA A N   
856  C CA  . ALA A 116 ? 0.5017 0.6390 0.7036 -0.0479 -0.0626 -0.0242 412 ALA A CA  
857  C C   . ALA A 116 ? 0.4975 0.6361 0.6957 -0.0426 -0.0607 -0.0217 412 ALA A C   
858  O O   . ALA A 116 ? 0.5245 0.6734 0.7175 -0.0274 -0.0615 -0.0222 412 ALA A O   
859  C CB  . ALA A 116 ? 0.5039 0.6357 0.7023 -0.0345 -0.0663 -0.0238 412 ALA A CB  
860  N N   . SER A 117 ? 0.4995 0.6223 0.6938 -0.0519 -0.0584 -0.0190 413 SER A N   
861  C CA  . SER A 117 ? 0.5113 0.6394 0.7008 -0.0488 -0.0559 -0.0172 413 SER A CA  
862  C C   . SER A 117 ? 0.5704 0.6782 0.7492 -0.0344 -0.0592 -0.0152 413 SER A C   
863  O O   . SER A 117 ? 0.5206 0.6307 0.6891 -0.0252 -0.0578 -0.0154 413 SER A O   
864  C CB  . SER A 117 ? 0.5851 0.6957 0.7669 -0.0631 -0.0530 -0.0140 413 SER A CB  
865  O OG  . SER A 117 ? 0.6078 0.6868 0.7838 -0.0604 -0.0563 -0.0111 413 SER A OG  
866  N N   . ARG A 118 ? 0.4880 0.5760 0.6643 -0.0341 -0.0636 -0.0135 414 ARG A N   
867  C CA  . ARG A 118 ? 0.5264 0.5909 0.6845 -0.0296 -0.0678 -0.0114 414 ARG A CA  
868  C C   . ARG A 118 ? 0.5775 0.6308 0.7166 -0.0170 -0.0700 -0.0135 414 ARG A C   
869  O O   . ARG A 118 ? 0.5430 0.5625 0.6536 -0.0166 -0.0740 -0.0118 414 ARG A O   
870  C CB  . ARG A 118 ? 0.5726 0.6303 0.7340 -0.0398 -0.0715 -0.0077 414 ARG A CB  
871  C CG  . ARG A 118 ? 0.5282 0.5900 0.6968 -0.0440 -0.0710 -0.0048 414 ARG A CG  
872  C CD  . ARG A 118 ? 0.6229 0.6936 0.7952 -0.0484 -0.0749 -0.0011 414 ARG A CD  
873  N NE  . ARG A 118 ? 0.6318 0.7063 0.8041 -0.0464 -0.0762 0.0023  414 ARG A NE  
874  C CZ  . ARG A 118 ? 0.6729 0.7683 0.8494 -0.0451 -0.0799 0.0060  414 ARG A CZ  
875  N NH1 . ARG A 118 ? 0.6966 0.8147 0.8798 -0.0498 -0.0816 0.0069  414 ARG A NH1 
876  N NH2 . ARG A 118 ? 0.6611 0.7596 0.8336 -0.0382 -0.0818 0.0093  414 ARG A NH2 
877  N N   . CYS A 119 ? 0.5110 0.5879 0.6581 -0.0070 -0.0682 -0.0168 415 CYS A N   
878  C CA  . CYS A 119 ? 0.6133 0.6775 0.7376 0.0105  -0.0711 -0.0181 415 CYS A CA  
879  C C   . CYS A 119 ? 0.6018 0.6775 0.7097 0.0358  -0.0693 -0.0212 415 CYS A C   
880  O O   . CYS A 119 ? 0.6153 0.7424 0.7456 0.0400  -0.0652 -0.0239 415 CYS A O   
881  C CB  . CYS A 119 ? 0.5206 0.6089 0.6609 0.0103  -0.0717 -0.0199 415 CYS A CB  
882  S SG  . CYS A 119 ? 0.5584 0.6332 0.6657 0.0383  -0.0758 -0.0210 415 CYS A SG  
883  N N   . VAL A 120 ? 0.6468 0.6750 0.7100 0.0526  -0.0723 -0.0209 416 VAL A N   
884  C CA  . VAL A 120 ? 0.5960 0.6300 0.6337 0.0861  -0.0704 -0.0243 416 VAL A CA  
885  C C   . VAL A 120 ? 0.6503 0.7030 0.6758 0.1164  -0.0722 -0.0265 416 VAL A C   
886  O O   . VAL A 120 ? 0.7400 0.8156 0.7480 0.1518  -0.0703 -0.0298 416 VAL A O   
887  C CB  . VAL A 120 ? 0.6357 0.5970 0.6185 0.0920  -0.0735 -0.0237 416 VAL A CB  
888  C CG1 . VAL A 120 ? 0.6483 0.5379 0.5788 0.0932  -0.0806 -0.0215 416 VAL A CG1 
889  C CG2 . VAL A 120 ? 0.7229 0.6909 0.6792 0.1275  -0.0697 -0.0279 416 VAL A CG2 
890  N N   . GLY A 121 ? 0.6181 0.6692 0.6528 0.1061  -0.0757 -0.0250 417 GLY A N   
891  C CA  . GLY A 121 ? 0.5273 0.5904 0.5455 0.1349  -0.0791 -0.0263 417 GLY A CA  
892  C C   . GLY A 121 ? 0.6101 0.7609 0.6760 0.1342  -0.0773 -0.0293 417 GLY A C   
893  O O   . GLY A 121 ? 0.6563 0.8264 0.7119 0.1576  -0.0812 -0.0304 417 GLY A O   
894  N N   . ARG A 122 ? 0.6068 0.8089 0.7177 0.1075  -0.0723 -0.0306 418 ARG A N   
895  C CA  . ARG A 122 ? 0.5225 0.7954 0.6725 0.0919  -0.0717 -0.0333 418 ARG A CA  
896  C C   . ARG A 122 ? 0.5428 0.8944 0.6978 0.1201  -0.0718 -0.0367 418 ARG A C   
897  O O   . ARG A 122 ? 0.5419 0.9575 0.7256 0.1039  -0.0728 -0.0392 418 ARG A O   
898  C CB  . ARG A 122 ? 0.4787 0.7711 0.6600 0.0542  -0.0664 -0.0333 418 ARG A CB  
899  C CG  . ARG A 122 ? 0.5265 0.7607 0.7085 0.0293  -0.0670 -0.0303 418 ARG A CG  
900  C CD  . ARG A 122 ? 0.5531 0.7971 0.7535 0.0004  -0.0623 -0.0299 418 ARG A CD  
901  N NE  . ARG A 122 ? 0.5925 0.8221 0.7845 0.0039  -0.0586 -0.0276 418 ARG A NE  
902  C CZ  . ARG A 122 ? 0.5443 0.7858 0.7453 -0.0164 -0.0538 -0.0265 418 ARG A CZ  
903  N NH1 . ARG A 122 ? 0.4430 0.7044 0.6559 -0.0430 -0.0523 -0.0276 418 ARG A NH1 
904  N NH2 . ARG A 122 ? 0.5950 0.8216 0.7860 -0.0118 -0.0508 -0.0243 418 ARG A NH2 
905  N N   . ILE A 123 ? 0.5972 0.9503 0.7223 0.1623  -0.0712 -0.0374 419 ILE A N   
906  C CA  . ILE A 123 ? 0.6402 1.0791 0.7685 0.1975  -0.0721 -0.0405 419 ILE A CA  
907  C C   . ILE A 123 ? 0.7012 1.1527 0.8275 0.2067  -0.0800 -0.0409 419 ILE A C   
908  O O   . ILE A 123 ? 0.6583 1.2024 0.8029 0.2210  -0.0822 -0.0437 419 ILE A O   
909  C CB  . ILE A 123 ? 0.6800 1.1008 0.7612 0.2536  -0.0708 -0.0414 419 ILE A CB  
910  C CG1 . ILE A 123 ? 0.7198 1.2625 0.8188 0.2856  -0.0678 -0.0449 419 ILE A CG1 
911  C CG2 . ILE A 123 ? 0.7147 1.0419 0.7334 0.2893  -0.0785 -0.0395 419 ILE A CG2 
912  C CD1 . ILE A 123 ? 0.9052 1.4395 0.9487 0.3594  -0.0706 -0.0465 419 ILE A CD1 
913  N N   . GLN A 124 ? 0.7377 1.1053 0.8433 0.1958  -0.0844 -0.0380 420 GLN A N   
914  C CA  . GLN A 124 ? 0.8401 1.2049 0.9360 0.2047  -0.0917 -0.0376 420 GLN A CA  
915  C C   . GLN A 124 ? 0.7153 1.1062 0.8523 0.1580  -0.0924 -0.0390 420 GLN A C   
916  O O   . GLN A 124 ? 0.6330 1.0115 0.7616 0.1593  -0.0980 -0.0386 420 GLN A O   
917  C CB  . GLN A 124 ? 0.9937 1.2479 1.0328 0.2196  -0.0955 -0.0329 420 GLN A CB  
918  C CG  . GLN A 124 ? 1.1637 1.3789 1.1390 0.2768  -0.0987 -0.0320 420 GLN A CG  
919  C CD  . GLN A 124 ? 1.2409 1.4838 1.1936 0.3170  -0.1062 -0.0321 420 GLN A CD  
920  O OE1 . GLN A 124 ? 1.2178 1.5312 1.2121 0.3013  -0.1089 -0.0339 420 GLN A OE1 
921  N NE2 . GLN A 124 ? 1.3788 1.5605 1.2583 0.3701  -0.1104 -0.0302 420 GLN A NE2 
922  N N   . TRP A 125 ? 0.6362 1.0568 0.8098 0.1184  -0.0869 -0.0408 421 TRP A N   
923  C CA  . TRP A 125 ? 0.5276 0.9336 0.7221 0.0750  -0.0869 -0.0418 421 TRP A CA  
924  C C   . TRP A 125 ? 0.5699 1.0297 0.7763 0.0683  -0.0930 -0.0456 421 TRP A C   
925  O O   . TRP A 125 ? 0.6015 1.0275 0.8063 0.0498  -0.0953 -0.0462 421 TRP A O   
926  C CB  . TRP A 125 ? 0.4865 0.9051 0.7044 0.0382  -0.0805 -0.0427 421 TRP A CB  
927  C CG  . TRP A 125 ? 0.5337 1.0443 0.7736 0.0250  -0.0792 -0.0462 421 TRP A CG  
928  C CD1 . TRP A 125 ? 0.5655 1.1329 0.8113 0.0394  -0.0748 -0.0461 421 TRP A CD1 
929  C CD2 . TRP A 125 ? 0.5589 1.1205 0.8146 -0.0089 -0.0822 -0.0504 421 TRP A CD2 
930  N NE1 . TRP A 125 ? 0.5270 1.1870 0.7952 0.0141  -0.0745 -0.0492 421 TRP A NE1 
931  C CE2 . TRP A 125 ? 0.5727 1.2273 0.8452 -0.0183 -0.0796 -0.0520 421 TRP A CE2 
932  C CE3 . TRP A 125 ? 0.4948 1.0323 0.7479 -0.0336 -0.0867 -0.0532 421 TRP A CE3 
933  C CZ2 . TRP A 125 ? 0.5241 1.2481 0.8098 -0.0578 -0.0823 -0.0559 421 TRP A CZ2 
934  C CZ3 . TRP A 125 ? 0.5381 1.1341 0.8003 -0.0692 -0.0897 -0.0580 421 TRP A CZ3 
935  C CH2 . TRP A 125 ? 0.5752 1.2636 0.8531 -0.0840 -0.0879 -0.0591 421 TRP A CH2 
936  N N   . SER A 126 ? 0.5981 1.1473 0.8157 0.0833  -0.0956 -0.0485 422 SER A N   
937  C CA  . SER A 126 ? 0.6777 1.2894 0.9068 0.0742  -0.1027 -0.0525 422 SER A CA  
938  C C   . SER A 126 ? 0.7181 1.3036 0.9200 0.1116  -0.1103 -0.0507 422 SER A C   
939  O O   . SER A 126 ? 0.7125 1.3295 0.9190 0.1022  -0.1170 -0.0536 422 SER A O   
940  C CB  . SER A 126 ? 0.6479 1.3807 0.8997 0.0757  -0.1034 -0.0556 422 SER A CB  
941  O OG  . SER A 126 ? 0.6271 1.3960 0.8631 0.1344  -0.1052 -0.0539 422 SER A OG  
942  N N   . LYS A 127 ? 0.7486 1.2713 0.9153 0.1515  -0.1099 -0.0459 423 LYS A N   
943  C CA  . LYS A 127 ? 0.6781 1.1516 0.8055 0.1834  -0.1165 -0.0425 423 LYS A CA  
944  C C   . LYS A 127 ? 0.7649 1.1384 0.8768 0.1581  -0.1133 -0.0387 423 LYS A C   
945  O O   . LYS A 127 ? 0.8170 1.1149 0.8964 0.1687  -0.1106 -0.0338 423 LYS A O   
946  C CB  . LYS A 127 ? 0.6914 1.1494 0.7746 0.2427  -0.1188 -0.0395 423 LYS A CB  
947  C CG  . LYS A 127 ? 0.7941 1.3652 0.8892 0.2789  -0.1228 -0.0430 423 LYS A CG  
948  C CD  . LYS A 127 ? 1.0266 1.5690 1.0611 0.3486  -0.1292 -0.0398 423 LYS A CD  
949  C CE  . LYS A 127 ? 1.1302 1.6134 1.1300 0.3549  -0.1370 -0.0362 423 LYS A CE  
950  N NZ  . LYS A 127 ? 1.2554 1.6604 1.1746 0.4173  -0.1421 -0.0310 423 LYS A NZ  
951  N N   . LEU A 128 ? 0.7529 1.1306 0.8857 0.1229  -0.1137 -0.0412 424 LEU A N   
952  C CA  . LEU A 128 ? 0.6946 0.9982 0.8175 0.1001  -0.1102 -0.0381 424 LEU A CA  
953  C C   . LEU A 128 ? 0.6515 0.9606 0.7692 0.0948  -0.1152 -0.0397 424 LEU A C   
954  O O   . LEU A 128 ? 0.6725 1.0403 0.8128 0.0801  -0.1187 -0.0459 424 LEU A O   
955  C CB  . LEU A 128 ? 0.5269 0.8238 0.6790 0.0621  -0.1031 -0.0404 424 LEU A CB  
956  C CG  . LEU A 128 ? 0.5335 0.7711 0.6801 0.0416  -0.0988 -0.0377 424 LEU A CG  
957  C CD1 . LEU A 128 ? 0.5617 0.7404 0.6798 0.0532  -0.0968 -0.0303 424 LEU A CD1 
958  C CD2 . LEU A 128 ? 0.4843 0.7219 0.6549 0.0116  -0.0932 -0.0409 424 LEU A CD2 
959  N N   . GLN A 129 ? 0.6975 0.9455 0.7812 0.1035  -0.1157 -0.0340 425 GLN A N   
960  C CA  . GLN A 129 ? 0.7082 0.9538 0.7818 0.0991  -0.1195 -0.0347 425 GLN A CA  
961  C C   . GLN A 129 ? 0.6690 0.8898 0.7582 0.0641  -0.1127 -0.0362 425 GLN A C   
962  O O   . GLN A 129 ? 0.7091 0.8816 0.7890 0.0549  -0.1064 -0.0310 425 GLN A O   
963  C CB  . GLN A 129 ? 0.7813 0.9718 0.8021 0.1262  -0.1231 -0.0267 425 GLN A CB  
964  C CG  . GLN A 129 ? 0.8184 1.0039 0.8238 0.1230  -0.1267 -0.0263 425 GLN A CG  
965  C CD  . GLN A 129 ? 0.9147 1.1764 0.9411 0.1292  -0.1349 -0.0338 425 GLN A CD  
966  O OE1 . GLN A 129 ? 0.9601 1.2795 0.9980 0.1495  -0.1403 -0.0368 425 GLN A OE1 
967  N NE2 . GLN A 129 ? 0.8904 1.1579 0.9203 0.1107  -0.1360 -0.0372 425 GLN A NE2 
968  N N   . VAL A 130 ? 0.6359 0.8909 0.7448 0.0451  -0.1141 -0.0437 426 VAL A N   
969  C CA  . VAL A 130 ? 0.6087 0.8402 0.7269 0.0186  -0.1075 -0.0467 426 VAL A CA  
970  C C   . VAL A 130 ? 0.5867 0.8006 0.6844 0.0195  -0.1083 -0.0463 426 VAL A C   
971  O O   . VAL A 130 ? 0.5868 0.8285 0.6778 0.0240  -0.1156 -0.0503 426 VAL A O   
972  C CB  . VAL A 130 ? 0.5904 0.8527 0.7297 -0.0053 -0.1079 -0.0557 426 VAL A CB  
973  C CG1 . VAL A 130 ? 0.6497 0.8749 0.7854 -0.0237 -0.1014 -0.0590 426 VAL A CG1 
974  C CG2 . VAL A 130 ? 0.5020 0.7853 0.6597 -0.0072 -0.1063 -0.0550 426 VAL A CG2 
975  N N   . PHE A 131 ? 0.5986 0.7733 0.6858 0.0144  -0.1009 -0.0411 427 PHE A N   
976  C CA  . PHE A 131 ? 0.6322 0.7918 0.6988 0.0137  -0.0993 -0.0398 427 PHE A CA  
977  C C   . PHE A 131 ? 0.5761 0.7345 0.6524 -0.0015 -0.0929 -0.0466 427 PHE A C   
978  O O   . PHE A 131 ? 0.5851 0.7318 0.6716 -0.0078 -0.0852 -0.0450 427 PHE A O   
979  C CB  . PHE A 131 ? 0.6314 0.7537 0.6722 0.0169  -0.0950 -0.0284 427 PHE A CB  
980  C CG  . PHE A 131 ? 0.6470 0.7503 0.6566 0.0372  -0.1022 -0.0217 427 PHE A CG  
981  C CD1 . PHE A 131 ? 0.6424 0.7542 0.6303 0.0542  -0.1102 -0.0224 427 PHE A CD1 
982  C CD2 . PHE A 131 ? 0.6820 0.7552 0.6776 0.0423  -0.1017 -0.0152 427 PHE A CD2 
983  C CE1 . PHE A 131 ? 0.7129 0.8015 0.6628 0.0808  -0.1173 -0.0159 427 PHE A CE1 
984  C CE2 . PHE A 131 ? 0.7416 0.7845 0.6957 0.0668  -0.1085 -0.0096 427 PHE A CE2 
985  C CZ  . PHE A 131 ? 0.7506 0.8001 0.6807 0.0883  -0.1161 -0.0096 427 PHE A CZ  
986  N N   . ASP A 132 ? 0.6913 0.8603 0.7594 -0.0050 -0.0966 -0.0547 428 ASP A N   
987  C CA  . ASP A 132 ? 0.5986 0.7557 0.6633 -0.0151 -0.0916 -0.0631 428 ASP A CA  
988  C C   . ASP A 132 ? 0.5988 0.7421 0.6471 -0.0090 -0.0835 -0.0595 428 ASP A C   
989  O O   . ASP A 132 ? 0.6426 0.7882 0.6721 -0.0048 -0.0860 -0.0592 428 ASP A O   
990  C CB  . ASP A 132 ? 0.5277 0.6969 0.5831 -0.0263 -0.1000 -0.0744 428 ASP A CB  
991  C CG  . ASP A 132 ? 0.6610 0.7992 0.6972 -0.0359 -0.0956 -0.0842 428 ASP A CG  
992  O OD1 . ASP A 132 ? 0.7148 0.8514 0.7341 -0.0519 -0.1026 -0.0943 428 ASP A OD1 
993  O OD2 . ASP A 132 ? 0.7135 0.8289 0.7466 -0.0269 -0.0856 -0.0820 428 ASP A OD2 
994  N N   . ALA A 133 ? 0.5801 0.7159 0.6352 -0.0079 -0.0737 -0.0562 429 ALA A N   
995  C CA  . ALA A 133 ? 0.6190 0.7575 0.6622 -0.0030 -0.0643 -0.0523 429 ALA A CA  
996  C C   . ALA A 133 ? 0.6160 0.7479 0.6505 0.0050  -0.0575 -0.0612 429 ALA A C   
997  O O   . ALA A 133 ? 0.6958 0.8422 0.7286 0.0133  -0.0475 -0.0579 429 ALA A O   
998  C CB  . ALA A 133 ? 0.6187 0.7658 0.6721 -0.0076 -0.0583 -0.0399 429 ALA A CB  
999  N N   . ARG A 134 ? 0.6636 0.7738 0.6876 0.0026  -0.0630 -0.0725 430 ARG A N   
1000 C CA  . ARG A 134 ? 0.7020 0.7861 0.7019 0.0132  -0.0579 -0.0819 430 ARG A CA  
1001 C C   . ARG A 134 ? 0.7457 0.8253 0.7150 0.0249  -0.0535 -0.0875 430 ARG A C   
1002 O O   . ARG A 134 ? 0.8238 0.8793 0.7651 0.0417  -0.0476 -0.0952 430 ARG A O   
1003 C CB  . ARG A 134 ? 0.6819 0.7316 0.6665 -0.0003 -0.0659 -0.0919 430 ARG A CB  
1004 C CG  . ARG A 134 ? 0.6479 0.6954 0.6547 -0.0064 -0.0664 -0.0876 430 ARG A CG  
1005 C CD  . ARG A 134 ? 0.7240 0.7416 0.7129 -0.0278 -0.0743 -0.0961 430 ARG A CD  
1006 N NE  . ARG A 134 ? 0.7623 0.8030 0.7537 -0.0474 -0.0843 -0.0995 430 ARG A NE  
1007 C CZ  . ARG A 134 ? 0.7749 0.8012 0.7443 -0.0731 -0.0925 -0.1084 430 ARG A CZ  
1008 N NH1 . ARG A 134 ? 0.8656 0.8394 0.8010 -0.0848 -0.0916 -0.1147 430 ARG A NH1 
1009 N NH2 . ARG A 134 ? 0.7194 0.7844 0.6962 -0.0883 -0.1022 -0.1106 430 ARG A NH2 
1010 N N   . ASP A 135 ? 0.6902 0.7881 0.6581 0.0198  -0.0562 -0.0839 431 ASP A N   
1011 C CA  . ASP A 135 ? 0.7995 0.8998 0.7402 0.0312  -0.0503 -0.0870 431 ASP A CA  
1012 C C   . ASP A 135 ? 0.7659 0.9039 0.7182 0.0394  -0.0378 -0.0754 431 ASP A C   
1013 O O   . ASP A 135 ? 0.7583 0.9082 0.6901 0.0481  -0.0309 -0.0760 431 ASP A O   
1014 C CB  . ASP A 135 ? 0.8325 0.9322 0.7587 0.0208  -0.0602 -0.0891 431 ASP A CB  
1015 C CG  . ASP A 135 ? 0.8781 0.9996 0.8270 0.0114  -0.0665 -0.0769 431 ASP A CG  
1016 O OD1 . ASP A 135 ? 0.8784 1.0042 0.8531 0.0059  -0.0692 -0.0721 431 ASP A OD1 
1017 O OD2 . ASP A 135 ? 0.8373 0.9659 0.7716 0.0119  -0.0691 -0.0725 431 ASP A OD2 
1018 N N   . CYS A 136 ? 0.6760 0.8355 0.6580 0.0336  -0.0349 -0.0650 432 CYS A N   
1019 C CA  . CYS A 136 ? 0.6488 0.8506 0.6406 0.0332  -0.0235 -0.0537 432 CYS A CA  
1020 C C   . CYS A 136 ? 0.7518 0.9769 0.7353 0.0581  -0.0116 -0.0591 432 CYS A C   
1021 O O   . CYS A 136 ? 0.7798 0.9785 0.7531 0.0765  -0.0126 -0.0693 432 CYS A O   
1022 C CB  . CYS A 136 ? 0.6690 0.8836 0.6894 0.0182  -0.0250 -0.0429 432 CYS A CB  
1023 S SG  . CYS A 136 ? 0.6850 0.9489 0.7102 0.0005  -0.0146 -0.0268 432 CYS A SG  
1024 N N   . THR A 137 ? 0.7687 1.0420 0.7491 0.0602  -0.0002 -0.0522 433 THR A N   
1025 C CA  . THR A 137 ? 0.6602 0.9721 0.6328 0.0900  0.0125  -0.0565 433 THR A CA  
1026 C C   . THR A 137 ? 0.5969 0.9906 0.5919 0.0827  0.0243  -0.0435 433 THR A C   
1027 O O   . THR A 137 ? 0.7258 1.1658 0.7245 0.1108  0.0335  -0.0458 433 THR A O   
1028 C CB  . THR A 137 ? 0.7599 1.0586 0.6938 0.1095  0.0172  -0.0664 433 THR A CB  
1029 O OG1 . THR A 137 ? 0.7321 1.0499 0.6608 0.0873  0.0193  -0.0578 433 THR A OG1 
1030 C CG2 . THR A 137 ? 0.8664 1.0871 0.7706 0.1161  0.0057  -0.0814 433 THR A CG2 
1031 N N   . THR A 138 ? 0.6759 1.0901 0.6802 0.0465  0.0242  -0.0300 434 THR A N   
1032 C CA  . THR A 138 ? 0.6674 1.1605 0.6874 0.0278  0.0347  -0.0168 434 THR A CA  
1033 C C   . THR A 138 ? 0.6298 1.1123 0.6670 -0.0087 0.0270  -0.0056 434 THR A C   
1034 O O   . THR A 138 ? 0.6524 1.0673 0.6857 -0.0187 0.0148  -0.0066 434 THR A O   
1035 C CB  . THR A 138 ? 0.6773 1.2016 0.6752 0.0098  0.0439  -0.0093 434 THR A CB  
1036 O OG1 . THR A 138 ? 0.7173 1.1784 0.6956 -0.0198 0.0341  -0.0032 434 THR A OG1 
1037 C CG2 . THR A 138 ? 0.7279 1.2577 0.7032 0.0465  0.0514  -0.0210 434 THR A CG2 
1038 N N   . ALA A 139 ? 0.7394 1.2942 0.7932 -0.0284 0.0343  0.0050  435 ALA A N   
1039 C CA  . ALA A 139 ? 0.6417 1.1847 0.7022 -0.0682 0.0275  0.0161  435 ALA A CA  
1040 C C   . ALA A 139 ? 0.7294 1.2162 0.7548 -0.1047 0.0229  0.0253  435 ALA A C   
1041 O O   . ALA A 139 ? 0.7808 1.2114 0.7965 -0.1258 0.0128  0.0301  435 ALA A O   
1042 C CB  . ALA A 139 ? 0.7391 1.3797 0.8196 -0.0874 0.0360  0.0255  435 ALA A CB  
1043 N N   . HIS A 140 ? 0.6840 1.1811 0.6840 -0.1093 0.0302  0.0279  436 HIS A N   
1044 C CA  . HIS A 140 ? 0.7289 1.1615 0.6856 -0.1369 0.0251  0.0364  436 HIS A CA  
1045 C C   . HIS A 140 ? 0.7262 1.0723 0.6738 -0.1150 0.0108  0.0281  436 HIS A C   
1046 O O   . HIS A 140 ? 0.8544 1.1366 0.7746 -0.1322 0.0012  0.0347  436 HIS A O   
1047 C CB  . HIS A 140 ? 0.8493 1.3130 0.7803 -0.1414 0.0363  0.0399  436 HIS A CB  
1048 C CG  . HIS A 140 ? 0.8242 1.3598 0.7462 -0.1834 0.0487  0.0542  436 HIS A CG  
1049 N ND1 . HIS A 140 ? 0.8217 1.4601 0.7804 -0.1830 0.0586  0.0547  436 HIS A ND1 
1050 C CD2 . HIS A 140 ? 0.8807 1.4032 0.7571 -0.2296 0.0525  0.0691  436 HIS A CD2 
1051 C CE1 . HIS A 140 ? 0.8848 1.5815 0.8262 -0.2304 0.0682  0.0691  436 HIS A CE1 
1052 N NE2 . HIS A 140 ? 0.8864 1.5087 0.7750 -0.2619 0.0650  0.0782  436 HIS A NE2 
1053 N N   . GLY A 141 ? 0.7179 1.0615 0.6826 -0.0770 0.0090  0.0135  437 GLY A N   
1054 C CA  . GLY A 141 ? 0.7122 0.9917 0.6747 -0.0602 -0.0048 0.0050  437 GLY A CA  
1055 C C   . GLY A 141 ? 0.7183 0.9730 0.6989 -0.0664 -0.0135 0.0065  437 GLY A C   
1056 O O   . GLY A 141 ? 0.7575 0.9599 0.7236 -0.0679 -0.0244 0.0077  437 GLY A O   
1057 N N   . MET A 142 ? 0.6633 0.9586 0.6736 -0.0666 -0.0087 0.0063  438 MET A N   
1058 C CA  . MET A 142 ? 0.5890 0.8636 0.6148 -0.0741 -0.0161 0.0082  438 MET A CA  
1059 C C   . MET A 142 ? 0.6448 0.8832 0.6402 -0.1064 -0.0203 0.0210  438 MET A C   
1060 O O   . MET A 142 ? 0.7469 0.9305 0.7304 -0.1044 -0.0305 0.0211  438 MET A O   
1061 C CB  . MET A 142 ? 0.5865 0.9175 0.6443 -0.0702 -0.0099 0.0075  438 MET A CB  
1062 C CG  . MET A 142 ? 0.5460 0.8941 0.6218 -0.0335 -0.0070 -0.0053 438 MET A CG  
1063 S SD  . MET A 142 ? 0.5962 1.0129 0.7016 -0.0212 -0.0003 -0.0044 438 MET A SD  
1064 C CE  . MET A 142 ? 0.6077 0.9898 0.7284 -0.0384 -0.0110 -0.0008 438 MET A CE  
1065 N N   . PHE A 143 ? 0.7007 0.9676 0.6767 -0.1366 -0.0124 0.0321  439 PHE A N   
1066 C CA  . PHE A 143 ? 0.7383 0.9547 0.6673 -0.1723 -0.0163 0.0450  439 PHE A CA  
1067 C C   . PHE A 143 ? 0.7872 0.9228 0.6757 -0.1587 -0.0261 0.0448  439 PHE A C   
1068 O O   . PHE A 143 ? 0.7885 0.8597 0.6469 -0.1630 -0.0353 0.0487  439 PHE A O   
1069 C CB  . PHE A 143 ? 0.8610 1.1203 0.7666 -0.2099 -0.0053 0.0567  439 PHE A CB  
1070 C CG  . PHE A 143 ? 0.9336 1.1254 0.7737 -0.2516 -0.0092 0.0706  439 PHE A CG  
1071 C CD1 . PHE A 143 ? 0.9173 1.0761 0.7054 -0.2663 -0.0064 0.0786  439 PHE A CD1 
1072 C CD2 . PHE A 143 ? 0.8601 1.0107 0.6815 -0.2754 -0.0162 0.0756  439 PHE A CD2 
1073 C CE1 . PHE A 143 ? 1.0151 1.0947 0.7283 -0.3048 -0.0105 0.0920  439 PHE A CE1 
1074 C CE2 . PHE A 143 ? 0.9843 1.0558 0.7308 -0.3137 -0.0204 0.0878  439 PHE A CE2 
1075 C CZ  . PHE A 143 ? 1.0174 1.0496 0.7073 -0.3284 -0.0178 0.0963  439 PHE A CZ  
1076 N N   . ASN A 144 ? 0.7222 0.8624 0.6073 -0.1381 -0.0248 0.0397  440 ASN A N   
1077 C CA  . ASN A 144 ? 0.7058 0.7822 0.5530 -0.1220 -0.0347 0.0396  440 ASN A CA  
1078 C C   . ASN A 144 ? 0.7612 0.8129 0.6292 -0.0931 -0.0464 0.0302  440 ASN A C   
1079 O O   . ASN A 144 ? 0.8647 0.8591 0.6976 -0.0847 -0.0562 0.0338  440 ASN A O   
1080 C CB  . ASN A 144 ? 0.8618 0.9588 0.7049 -0.1071 -0.0310 0.0348  440 ASN A CB  
1081 C CG  . ASN A 144 ? 0.8342 0.8726 0.6324 -0.0925 -0.0414 0.0369  440 ASN A CG  
1082 O OD1 . ASN A 144 ? 0.9470 0.9314 0.6888 -0.1088 -0.0437 0.0493  440 ASN A OD1 
1083 N ND2 . ASN A 144 ? 0.7735 0.8193 0.5907 -0.0623 -0.0488 0.0249  440 ASN A ND2 
1084 N N   . TYR A 145 ? 0.6932 0.7872 0.6130 -0.0761 -0.0454 0.0183  441 TYR A N   
1085 C CA  . TYR A 145 ? 0.7909 0.8709 0.7323 -0.0558 -0.0551 0.0101  441 TYR A CA  
1086 C C   . TYR A 145 ? 0.7494 0.7998 0.6831 -0.0658 -0.0587 0.0163  441 TYR A C   
1087 O O   . TYR A 145 ? 0.7732 0.7905 0.6955 -0.0501 -0.0680 0.0150  441 TYR A O   
1088 C CB  . TYR A 145 ? 0.7026 0.8239 0.6901 -0.0435 -0.0521 -0.0022 441 TYR A CB  
1089 C CG  . TYR A 145 ? 0.6498 0.7774 0.6400 -0.0258 -0.0558 -0.0134 441 TYR A CG  
1090 C CD1 . TYR A 145 ? 0.5557 0.7081 0.5491 -0.0213 -0.0482 -0.0194 441 TYR A CD1 
1091 C CD2 . TYR A 145 ? 0.7025 0.8147 0.6898 -0.0133 -0.0673 -0.0184 441 TYR A CD2 
1092 C CE1 . TYR A 145 ? 0.6514 0.8013 0.6392 -0.0085 -0.0526 -0.0307 441 TYR A CE1 
1093 C CE2 . TYR A 145 ? 0.6790 0.8011 0.6671 -0.0038 -0.0721 -0.0288 441 TYR A CE2 
1094 C CZ  . TYR A 145 ? 0.7064 0.8415 0.6921 -0.0033 -0.0651 -0.0352 441 TYR A CZ  
1095 O OH  . TYR A 145 ? 0.7461 0.8828 0.7244 0.0028  -0.0711 -0.0463 441 TYR A OH  
1096 N N   . ILE A 146 ? 0.7280 0.7952 0.6667 -0.0909 -0.0516 0.0226  442 ILE A N   
1097 C CA  . ILE A 146 ? 0.7060 0.7437 0.6343 -0.1039 -0.0553 0.0277  442 ILE A CA  
1098 C C   . ILE A 146 ? 0.8149 0.7769 0.6752 -0.1125 -0.0615 0.0375  442 ILE A C   
1099 O O   . ILE A 146 ? 0.8800 0.7949 0.7198 -0.1004 -0.0693 0.0373  442 ILE A O   
1100 C CB  . ILE A 146 ? 0.7168 0.8004 0.6655 -0.1316 -0.0472 0.0321  442 ILE A CB  
1101 C CG1 . ILE A 146 ? 0.6835 0.8228 0.6905 -0.1120 -0.0441 0.0219  442 ILE A CG1 
1102 C CG2 . ILE A 146 ? 0.6705 0.7129 0.5896 -0.1562 -0.0515 0.0398  442 ILE A CG2 
1103 C CD1 . ILE A 146 ? 0.7409 0.9389 0.7713 -0.1296 -0.0367 0.0254  442 ILE A CD1 
1104 N N   . CYS A 147 ? 0.8283 0.7730 0.6460 -0.1306 -0.0578 0.0460  443 CYS A N   
1105 C CA  . CYS A 147 ? 0.7804 0.6379 0.5184 -0.1363 -0.0641 0.0559  443 CYS A CA  
1106 C C   . CYS A 147 ? 0.8682 0.6887 0.5919 -0.0911 -0.0750 0.0502  443 CYS A C   
1107 O O   . CYS A 147 ? 1.0028 0.7523 0.6740 -0.0789 -0.0829 0.0540  443 CYS A O   
1108 C CB  . CYS A 147 ? 0.8152 0.6633 0.5099 -0.1609 -0.0580 0.0656  443 CYS A CB  
1109 S SG  . CYS A 147 ? 1.0901 0.9602 0.7650 -0.2246 -0.0471 0.0780  443 CYS A SG  
1110 N N   . ASN A 148 ? 0.7782 0.6474 0.5429 -0.0652 -0.0759 0.0410  444 ASN A N   
1111 C CA  . ASN A 148 ? 0.8885 0.7433 0.6461 -0.0244 -0.0868 0.0352  444 ASN A CA  
1112 C C   . ASN A 148 ? 0.7864 0.6456 0.5701 -0.0071 -0.0918 0.0291  444 ASN A C   
1113 O O   . ASN A 148 ? 0.8348 0.6560 0.5842 0.0219  -0.1006 0.0298  444 ASN A O   
1114 C CB  . ASN A 148 ? 0.9156 0.8278 0.7126 -0.0085 -0.0874 0.0256  444 ASN A CB  
1115 C CG  . ASN A 148 ? 0.9816 0.8797 0.7400 -0.0156 -0.0848 0.0317  444 ASN A CG  
1116 O OD1 . ASN A 148 ? 0.9635 0.8035 0.6600 -0.0304 -0.0837 0.0440  444 ASN A OD1 
1117 N ND2 . ASN A 148 ? 0.9362 0.8811 0.7236 -0.0068 -0.0842 0.0232  444 ASN A ND2 
1118 N N   . HIS A 149 ? 0.7496 0.6557 0.5902 -0.0216 -0.0860 0.0234  445 HIS A N   
1119 C CA  . HIS A 149 ? 0.8100 0.7192 0.6733 -0.0111 -0.0891 0.0189  445 HIS A CA  
1120 C C   . HIS A 149 ? 0.8782 0.7138 0.6818 -0.0151 -0.0924 0.0274  445 HIS A C   
1121 O O   . HIS A 149 ? 0.8705 0.6790 0.6535 0.0140  -0.0994 0.0254  445 HIS A O   
1122 C CB  . HIS A 149 ? 0.7397 0.7008 0.6616 -0.0298 -0.0816 0.0138  445 HIS A CB  
1123 C CG  . HIS A 149 ? 0.7250 0.6894 0.6695 -0.0235 -0.0837 0.0101  445 HIS A CG  
1124 N ND1 . HIS A 149 ? 0.6410 0.6536 0.6392 -0.0186 -0.0820 0.0011  445 HIS A ND1 
1125 C CD2 . HIS A 149 ? 0.7231 0.6434 0.6376 -0.0224 -0.0870 0.0141  445 HIS A CD2 
1126 C CE1 . HIS A 149 ? 0.6296 0.6339 0.6344 -0.0151 -0.0837 0.0004  445 HIS A CE1 
1127 N NE2 . HIS A 149 ? 0.7178 0.6682 0.6737 -0.0159 -0.0868 0.0076  445 HIS A NE2 
1128 N N   . VAL A 150 ? 0.8655 0.6696 0.6367 -0.0520 -0.0873 0.0365  446 VAL A N   
1129 C CA  . VAL A 150 ? 0.9921 0.7132 0.6936 -0.0640 -0.0910 0.0445  446 VAL A CA  
1130 C C   . VAL A 150 ? 1.1090 0.7519 0.7345 -0.0307 -0.0997 0.0482  446 VAL A C   
1131 O O   . VAL A 150 ? 1.1883 0.7812 0.7771 -0.0041 -0.1061 0.0469  446 VAL A O   
1132 C CB  . VAL A 150 ? 0.9297 0.6347 0.6013 -0.1175 -0.0846 0.0547  446 VAL A CB  
1133 C CG1 . VAL A 150 ? 1.0326 0.6324 0.6116 -0.1355 -0.0898 0.0634  446 VAL A CG1 
1134 C CG2 . VAL A 150 ? 0.8873 0.6699 0.6277 -0.1425 -0.0776 0.0512  446 VAL A CG2 
1135 N N   . LYS A 151 ? 1.0681 0.7010 0.6664 -0.0263 -0.1002 0.0524  447 LYS A N   
1136 C CA  . LYS A 151 ? 1.1867 0.7396 0.7027 0.0087  -0.1092 0.0572  447 LYS A CA  
1137 C C   . LYS A 151 ? 1.1527 0.7361 0.6936 0.0658  -0.1172 0.0477  447 LYS A C   
1138 O O   . LYS A 151 ? 1.2096 0.7267 0.6870 0.1009  -0.1246 0.0495  447 LYS A O   
1139 C CB  . LYS A 151 ? 1.1410 0.6885 0.6300 0.0040  -0.1083 0.0631  447 LYS A CB  
1140 C CG  . LYS A 151 ? 1.2669 0.7177 0.6550 0.0359  -0.1175 0.0709  447 LYS A CG  
1141 C CD  . LYS A 151 ? 1.2395 0.6776 0.5952 0.0170  -0.1146 0.0789  447 LYS A CD  
1142 C CE  . LYS A 151 ? 1.4758 0.7823 0.7015 0.0244  -0.1209 0.0921  447 LYS A CE  
1143 N NZ  . LYS A 151 ? 1.3976 0.7027 0.5986 0.0068  -0.1175 0.0997  447 LYS A NZ  
1144 N N   . TYR A 152 ? 1.0058 0.6900 0.6342 0.0751  -0.1157 0.0375  448 TYR A N   
1145 C CA  . TYR A 152 ? 1.0582 0.7907 0.7180 0.1203  -0.1225 0.0285  448 TYR A CA  
1146 C C   . TYR A 152 ? 1.0278 0.7447 0.6877 0.1304  -0.1228 0.0258  448 TYR A C   
1147 O O   . TYR A 152 ? 1.1616 0.8484 0.7785 0.1741  -0.1297 0.0255  448 TYR A O   
1148 C CB  . TYR A 152 ? 0.9753 0.8121 0.7235 0.1142  -0.1202 0.0181  448 TYR A CB  
1149 C CG  . TYR A 152 ? 0.9372 0.8356 0.7198 0.1505  -0.1268 0.0092  448 TYR A CG  
1150 C CD1 . TYR A 152 ? 1.0416 0.9660 0.8080 0.1878  -0.1361 0.0075  448 TYR A CD1 
1151 C CD2 . TYR A 152 ? 0.8502 0.7863 0.6791 0.1467  -0.1238 0.0031  448 TYR A CD2 
1152 C CE1 . TYR A 152 ? 1.0264 1.0234 0.8258 0.2183  -0.1420 -0.0002 448 TYR A CE1 
1153 C CE2 . TYR A 152 ? 0.8139 0.8147 0.6729 0.1752  -0.1287 -0.0042 448 TYR A CE2 
1154 C CZ  . TYR A 152 ? 0.9370 0.9731 0.7830 0.2097  -0.1377 -0.0059 448 TYR A CZ  
1155 O OH  . TYR A 152 ? 1.0077 1.1247 0.8865 0.2349  -0.1424 -0.0129 448 TYR A OH  
1156 N N   . ALA A 153 ? 0.8815 0.6218 0.5877 0.0945  -0.1154 0.0236  449 ALA A N   
1157 C CA  . ALA A 153 ? 0.9244 0.6618 0.6399 0.1033  -0.1153 0.0199  449 ALA A CA  
1158 C C   . ALA A 153 ? 1.0307 0.6604 0.6522 0.1144  -0.1194 0.0268  449 ALA A C   
1159 O O   . ALA A 153 ? 1.1431 0.7578 0.7496 0.1427  -0.1220 0.0232  449 ALA A O   
1160 C CB  . ALA A 153 ? 0.9196 0.6980 0.6959 0.0622  -0.1073 0.0174  449 ALA A CB  
1161 N N   . THR A 154 ? 1.0384 0.5880 0.5893 0.0912  -0.1198 0.0365  450 THR A N   
1162 C CA  . THR A 154 ? 1.1974 0.6247 0.6402 0.0985  -0.1246 0.0433  450 THR A CA  
1163 C C   . THR A 154 ? 1.3492 0.7300 0.7256 0.1638  -0.1336 0.0434  450 THR A C   
1164 O O   . THR A 154 ? 1.3609 0.6827 0.6805 0.1997  -0.1380 0.0418  450 THR A O   
1165 C CB  . THR A 154 ? 1.2404 0.5969 0.6233 0.0447  -0.1219 0.0546  450 THR A CB  
1166 O OG1 . THR A 154 ? 1.1773 0.5905 0.6237 -0.0091 -0.1141 0.0538  450 THR A OG1 
1167 C CG2 . THR A 154 ? 1.3507 0.5619 0.6045 0.0465  -0.1279 0.0619  450 THR A CG2 
1168 N N   . ASN A 155 ? 1.2972 0.7063 0.6771 0.1840  -0.1366 0.0448  451 ASN A N   
1169 C CA  . ASN A 155 ? 1.3105 0.6997 0.6386 0.2528  -0.1460 0.0443  451 ASN A CA  
1170 C C   . ASN A 155 ? 1.4868 0.7285 0.6813 0.2797  -0.1519 0.0511  451 ASN A C   
1171 O O   . ASN A 155 ? 1.6493 0.8734 0.8059 0.3409  -0.1576 0.0471  451 ASN A O   
1172 C CB  . ASN A 155 ? 1.2597 0.7632 0.6673 0.2949  -0.1476 0.0327  451 ASN A CB  
1173 C CG  . ASN A 155 ? 1.3458 0.8648 0.7163 0.3677  -0.1575 0.0315  451 ASN A CG  
1174 O OD1 . ASN A 155 ? 1.4710 0.9409 0.7801 0.3849  -0.1634 0.0383  451 ASN A OD1 
1175 N ND2 . ASN A 155 ? 1.3408 0.9346 0.7478 0.4112  -0.1594 0.0233  451 ASN A ND2 
1176 N N   . LYS A 156 ? 1.6004 0.7342 0.7180 0.2316  -0.1501 0.0613  452 LYS A N   
1177 C CA  . LYS A 156 ? 1.7879 0.7565 0.7573 0.2466  -0.1562 0.0691  452 LYS A CA  
1178 C C   . LYS A 156 ? 1.7872 0.7259 0.7404 0.2598  -0.1547 0.0595  452 LYS A C   
1179 O O   . LYS A 156 ? 2.0095 0.8722 0.8803 0.2917  -0.1539 0.0486  452 LYS A O   
1180 C CB  . LYS A 156 ? 1.8540 0.7978 0.7679 0.3079  -0.1590 0.0620  452 LYS A CB  
1181 C CG  . LYS A 156 ? 2.0548 1.0374 0.9849 0.3112  -0.1621 0.0695  452 LYS A CG  
1182 C CD  . LYS A 156 ? 2.2510 1.1896 1.1101 0.3690  -0.1637 0.0608  452 LYS A CD  
1183 C CE  . LYS A 156 ? 2.4359 1.3691 1.2674 0.4324  -0.1629 0.0447  452 LYS A CE  
1184 N NZ  . LYS A 156 ? 2.3834 1.4601 1.3195 0.4726  -0.1642 0.0380  452 LYS A NZ  
1185 N N   . GLY A 157 ? 1.6131 0.6339 0.6593 0.2314  -0.1500 0.0556  453 GLY A N   
1186 C CA  . GLY A 157 ? 1.6484 0.6430 0.6810 0.2434  -0.1499 0.0493  453 GLY A CA  
1187 C C   . GLY A 157 ? 1.5982 0.6985 0.7033 0.3054  -0.1499 0.0382  453 GLY A C   
1188 O O   . GLY A 157 ? 1.5201 0.6359 0.6474 0.3077  -0.1472 0.0317  453 GLY A O   
1189 N N   . ASN A 158 ? 1.5878 0.7641 0.7271 0.3540  -0.1531 0.0360  454 ASN A N   
1190 C CA  . ASN A 158 ? 1.5058 0.8122 0.7312 0.3997  -0.1522 0.0257  454 ASN A CA  
1191 C C   . ASN A 158 ? 1.3382 0.7789 0.7010 0.3479  -0.1447 0.0209  454 ASN A C   
1192 O O   . ASN A 158 ? 1.4048 0.9459 0.8360 0.3541  -0.1453 0.0181  454 ASN A O   
1193 C CB  . ASN A 158 ? 1.6340 0.9803 0.8411 0.4662  -0.1569 0.0222  454 ASN A CB  
1194 C CG  . ASN A 158 ? 1.6490 1.1418 0.9431 0.5061  -0.1549 0.0115  454 ASN A CG  
1195 O OD1 . ASN A 158 ? 1.7326 1.2643 1.0698 0.5013  -0.1516 0.0076  454 ASN A OD1 
1196 N ND2 . ASN A 158 ? 1.5976 1.1758 0.9178 0.5406  -0.1560 0.0065  454 ASN A ND2 
1197 N N   . LEU A 159 ? 1.3190 0.7532 0.7132 0.2967  -0.1382 0.0199  455 LEU A N   
1198 C CA  . LEU A 159 ? 1.1790 0.7071 0.6802 0.2419  -0.1310 0.0174  455 LEU A CA  
1199 C C   . LEU A 159 ? 1.1506 0.8144 0.7489 0.2621  -0.1295 0.0088  455 LEU A C   
1200 O O   . LEU A 159 ? 1.1750 0.8800 0.7807 0.3060  -0.1309 0.0032  455 LEU A O   
1201 C CB  . LEU A 159 ? 1.1710 0.6775 0.6855 0.1986  -0.1258 0.0168  455 LEU A CB  
1202 C CG  . LEU A 159 ? 1.2838 0.7081 0.7507 0.1405  -0.1245 0.0251  455 LEU A CG  
1203 C CD1 . LEU A 159 ? 1.4242 0.7351 0.7802 0.1492  -0.1303 0.0337  455 LEU A CD1 
1204 C CD2 . LEU A 159 ? 1.3118 0.6889 0.7544 0.1173  -0.1234 0.0242  455 LEU A CD2 
1205 N N   . ARG A 160 ? 0.9575 0.6903 0.6266 0.2267  -0.1262 0.0077  456 ARG A N   
1206 C CA  . ARG A 160 ? 0.9023 0.7541 0.6556 0.2323  -0.1254 0.0000  456 ARG A CA  
1207 C C   . ARG A 160 ? 0.8312 0.7264 0.6563 0.1797  -0.1178 -0.0025 456 ARG A C   
1208 O O   . ARG A 160 ? 0.8882 0.7506 0.7091 0.1432  -0.1146 0.0021  456 ARG A O   
1209 C CB  . ARG A 160 ? 0.8328 0.7149 0.5842 0.2480  -0.1311 0.0007  456 ARG A CB  
1210 C CG  . ARG A 160 ? 0.9637 0.8084 0.6412 0.3074  -0.1399 0.0037  456 ARG A CG  
1211 C CD  . ARG A 160 ? 1.0120 0.8969 0.6926 0.3220  -0.1464 0.0042  456 ARG A CD  
1212 N NE  . ARG A 160 ? 1.0643 0.8814 0.7113 0.2895  -0.1452 0.0117  456 ARG A NE  
1213 C CZ  . ARG A 160 ? 1.1668 0.9723 0.7788 0.3070  -0.1515 0.0156  456 ARG A CZ  
1214 N NH1 . ARG A 160 ? 1.1888 1.0484 0.7958 0.3587  -0.1606 0.0125  456 ARG A NH1 
1215 N NH2 . ARG A 160 ? 1.0926 0.8382 0.6733 0.2735  -0.1488 0.0229  456 ARG A NH2 
1216 N N   . SER A 161 ? 0.7348 0.7037 0.6207 0.1768  -0.1146 -0.0094 457 SER A N   
1217 C CA  . SER A 161 ? 0.7519 0.7491 0.6939 0.1327  -0.1079 -0.0115 457 SER A CA  
1218 C C   . SER A 161 ? 0.6669 0.7108 0.6461 0.1150  -0.1078 -0.0142 457 SER A C   
1219 O O   . SER A 161 ? 0.7089 0.7941 0.6922 0.1347  -0.1129 -0.0173 457 SER A O   
1220 C CB  . SER A 161 ? 0.8464 0.8935 0.8310 0.1315  -0.1043 -0.0169 457 SER A CB  
1221 O OG  . SER A 161 ? 0.9631 1.0872 0.9752 0.1530  -0.1068 -0.0227 457 SER A OG  
1222 N N   . ALA A 162 ? 0.6478 0.6856 0.6497 0.0796  -0.1022 -0.0133 458 ALA A N   
1223 C CA  . ALA A 162 ? 0.6229 0.6878 0.6462 0.0644  -0.1014 -0.0157 458 ALA A CA  
1224 C C   . ALA A 162 ? 0.6113 0.6824 0.6661 0.0332  -0.0940 -0.0165 458 ALA A C   
1225 O O   . ALA A 162 ? 0.6622 0.7095 0.7141 0.0210  -0.0904 -0.0127 458 ALA A O   
1226 C CB  . ALA A 162 ? 0.7190 0.7428 0.6966 0.0699  -0.1041 -0.0095 458 ALA A CB  
1227 N N   . ILE A 163 ? 0.5552 0.6574 0.6347 0.0225  -0.0924 -0.0218 459 ILE A N   
1228 C CA  . ILE A 163 ? 0.5910 0.6981 0.6926 0.0019  -0.0856 -0.0231 459 ILE A CA  
1229 C C   . ILE A 163 ? 0.6022 0.7175 0.7009 -0.0024 -0.0843 -0.0257 459 ILE A C   
1230 O O   . ILE A 163 ? 0.7287 0.8602 0.8239 0.0053  -0.0894 -0.0304 459 ILE A O   
1231 C CB  . ILE A 163 ? 0.5765 0.7074 0.7088 -0.0043 -0.0841 -0.0295 459 ILE A CB  
1232 C CG1 . ILE A 163 ? 0.5076 0.6354 0.6520 -0.0171 -0.0776 -0.0304 459 ILE A CG1 
1233 C CG2 . ILE A 163 ? 0.5955 0.7594 0.7380 -0.0029 -0.0887 -0.0374 459 ILE A CG2 
1234 C CD1 . ILE A 163 ? 0.4806 0.6155 0.6427 -0.0234 -0.0761 -0.0353 459 ILE A CD1 
1235 N N   . THR A 164 ? 0.5895 0.6989 0.6873 -0.0137 -0.0776 -0.0226 460 THR A N   
1236 C CA  . THR A 164 ? 0.5329 0.6511 0.6255 -0.0155 -0.0745 -0.0253 460 THR A CA  
1237 C C   . THR A 164 ? 0.5944 0.7260 0.7057 -0.0188 -0.0685 -0.0310 460 THR A C   
1238 O O   . THR A 164 ? 0.6171 0.7526 0.7387 -0.0229 -0.0638 -0.0273 460 THR A O   
1239 C CB  . THR A 164 ? 0.5418 0.6467 0.6089 -0.0226 -0.0709 -0.0161 460 THR A CB  
1240 O OG1 . THR A 164 ? 0.6380 0.7136 0.6742 -0.0159 -0.0774 -0.0105 460 THR A OG1 
1241 C CG2 . THR A 164 ? 0.5376 0.6560 0.5976 -0.0215 -0.0672 -0.0195 460 THR A CG2 
1242 N N   . ILE A 165 ? 0.5138 0.6490 0.6233 -0.0158 -0.0694 -0.0400 461 ILE A N   
1243 C CA  . ILE A 165 ? 0.4971 0.6279 0.6106 -0.0144 -0.0654 -0.0469 461 ILE A CA  
1244 C C   . ILE A 165 ? 0.6052 0.7370 0.7023 -0.0068 -0.0596 -0.0502 461 ILE A C   
1245 O O   . ILE A 165 ? 0.6230 0.7491 0.7037 -0.0064 -0.0627 -0.0563 461 ILE A O   
1246 C CB  . ILE A 165 ? 0.6279 0.7502 0.7408 -0.0212 -0.0715 -0.0556 461 ILE A CB  
1247 C CG1 . ILE A 165 ? 0.5897 0.7206 0.7208 -0.0257 -0.0749 -0.0513 461 ILE A CG1 
1248 C CG2 . ILE A 165 ? 0.6465 0.7449 0.7468 -0.0201 -0.0678 -0.0622 461 ILE A CG2 
1249 C CD1 . ILE A 165 ? 0.5484 0.6864 0.6824 -0.0372 -0.0805 -0.0578 461 ILE A CD1 
1250 N N   . PHE A 166 ? 0.6085 0.7541 0.7094 0.0002  -0.0515 -0.0461 462 PHE A N   
1251 C CA  . PHE A 166 ? 0.5766 0.7343 0.6629 0.0129  -0.0438 -0.0486 462 PHE A CA  
1252 C C   . PHE A 166 ? 0.6537 0.7837 0.7205 0.0283  -0.0427 -0.0596 462 PHE A C   
1253 O O   . PHE A 166 ? 0.6644 0.7680 0.7310 0.0244  -0.0472 -0.0632 462 PHE A O   
1254 C CB  . PHE A 166 ? 0.5776 0.7756 0.6769 0.0131  -0.0358 -0.0387 462 PHE A CB  
1255 C CG  . PHE A 166 ? 0.6789 0.8888 0.7780 -0.0066 -0.0364 -0.0283 462 PHE A CG  
1256 C CD1 . PHE A 166 ? 0.6589 0.8704 0.7386 -0.0093 -0.0346 -0.0273 462 PHE A CD1 
1257 C CD2 . PHE A 166 ? 0.5972 0.8055 0.7060 -0.0227 -0.0396 -0.0198 462 PHE A CD2 
1258 C CE1 . PHE A 166 ? 0.7346 0.9430 0.8015 -0.0281 -0.0356 -0.0168 462 PHE A CE1 
1259 C CE2 . PHE A 166 ? 0.5943 0.7950 0.6867 -0.0418 -0.0408 -0.0102 462 PHE A CE2 
1260 C CZ  . PHE A 166 ? 0.7213 0.9197 0.7911 -0.0446 -0.0389 -0.0083 462 PHE A CZ  
1261 N N   . PRO A 167 ? 0.6375 0.7666 0.6800 0.0458  -0.0367 -0.0653 463 PRO A N   
1262 C CA  . PRO A 167 ? 0.7258 0.8084 0.7318 0.0619  -0.0368 -0.0772 463 PRO A CA  
1263 C C   . PRO A 167 ? 0.7596 0.8254 0.7645 0.0739  -0.0356 -0.0766 463 PRO A C   
1264 O O   . PRO A 167 ? 0.7181 0.8240 0.7496 0.0811  -0.0313 -0.0680 463 PRO A O   
1265 C CB  . PRO A 167 ? 0.7303 0.8262 0.7117 0.0867  -0.0278 -0.0808 463 PRO A CB  
1266 C CG  . PRO A 167 ? 0.6754 0.8103 0.6743 0.0712  -0.0270 -0.0740 463 PRO A CG  
1267 C CD  . PRO A 167 ? 0.6306 0.7919 0.6681 0.0497  -0.0303 -0.0620 463 PRO A CD  
1268 N N   . GLN A 168 ? 0.7932 0.7968 0.7616 0.0734  -0.0402 -0.0859 464 GLN A N   
1269 C CA  . GLN A 168 ? 0.7481 0.7214 0.7052 0.0828  -0.0403 -0.0853 464 GLN A CA  
1270 C C   . GLN A 168 ? 0.8097 0.7811 0.7393 0.1263  -0.0321 -0.0867 464 GLN A C   
1271 O O   . GLN A 168 ? 0.7538 0.7221 0.6545 0.1491  -0.0269 -0.0926 464 GLN A O   
1272 C CB  . GLN A 168 ? 0.6748 0.5746 0.5903 0.0630  -0.0478 -0.0941 464 GLN A CB  
1273 C CG  . GLN A 168 ? 0.8294 0.6679 0.6800 0.0723  -0.0480 -0.1068 464 GLN A CG  
1274 C CD  . GLN A 168 ? 0.9531 0.7407 0.7730 0.0330  -0.0577 -0.1147 464 GLN A CD  
1275 O OE1 . GLN A 168 ? 0.9925 0.8206 0.8514 0.0011  -0.0637 -0.1117 464 GLN A OE1 
1276 N NE2 . GLN A 168 ? 1.1134 0.8121 0.8578 0.0348  -0.0595 -0.1246 464 GLN A NE2 
1277 N N   . ARG A 169 ? 0.8332 0.8107 0.7704 0.1413  -0.0308 -0.0812 465 ARG A N   
1278 C CA  . ARG A 169 ? 0.8362 0.8114 0.7410 0.1897  -0.0242 -0.0829 465 ARG A CA  
1279 C C   . ARG A 169 ? 0.9896 0.8699 0.8140 0.2103  -0.0249 -0.0959 465 ARG A C   
1280 O O   . ARG A 169 ? 1.0671 0.8698 0.8563 0.1836  -0.0321 -0.1018 465 ARG A O   
1281 C CB  . ARG A 169 ? 0.9265 0.9080 0.8419 0.2013  -0.0256 -0.0758 465 ARG A CB  
1282 C CG  . ARG A 169 ? 0.9937 0.9627 0.8644 0.2580  -0.0205 -0.0782 465 ARG A CG  
1283 C CD  . ARG A 169 ? 1.0708 1.0635 0.9590 0.2705  -0.0224 -0.0698 465 ARG A CD  
1284 N NE  . ARG A 169 ? 1.0173 1.1165 0.9794 0.2509  -0.0210 -0.0589 465 ARG A NE  
1285 C CZ  . ARG A 169 ? 0.9227 1.0413 0.9197 0.2283  -0.0259 -0.0509 465 ARG A CZ  
1286 N NH1 . ARG A 169 ? 1.0927 1.1381 1.0622 0.2233  -0.0314 -0.0521 465 ARG A NH1 
1287 N NH2 . ARG A 169 ? 0.7683 0.9742 0.8216 0.2075  -0.0252 -0.0418 465 ARG A NH2 
1288 N N   . THR A 170 ? 1.0629 0.9503 0.8533 0.2561  -0.0172 -0.1007 466 THR A N   
1289 C CA  . THR A 170 ? 1.1385 0.9244 0.8376 0.2853  -0.0173 -0.1136 466 THR A CA  
1290 C C   . THR A 170 ? 1.2346 1.0074 0.8947 0.3446  -0.0127 -0.1126 466 THR A C   
1291 O O   . THR A 170 ? 1.3304 1.0433 0.9626 0.3453  -0.0179 -0.1107 466 THR A O   
1292 C CB  . THR A 170 ? 1.1863 0.9762 0.8630 0.2947  -0.0127 -0.1221 466 THR A CB  
1293 O OG1 . THR A 170 ? 1.1494 1.0545 0.8803 0.3152  -0.0029 -0.1146 466 THR A OG1 
1294 C CG2 . THR A 170 ? 1.1288 0.8999 0.8196 0.2380  -0.0206 -0.1256 466 THR A CG2 
1295 N N   . ASP A 171 ? 1.2455 1.0776 0.9008 0.3979  -0.0030 -0.1131 467 ASP A N   
1296 C CA  . ASP A 171 ? 1.3806 1.2035 0.9909 0.4644  0.0009  -0.1129 467 ASP A CA  
1297 C C   . ASP A 171 ? 1.3624 1.2686 1.0368 0.4634  -0.0004 -0.0993 467 ASP A C   
1298 O O   . ASP A 171 ? 1.5689 1.4310 1.2037 0.4967  -0.0033 -0.0978 467 ASP A O   
1299 C CB  . ASP A 171 ? 1.5095 1.3913 1.1008 0.5239  0.0124  -0.1173 467 ASP A CB  
1300 C CG  . ASP A 171 ? 1.4791 1.5233 1.1659 0.5115  0.0200  -0.1064 467 ASP A CG  
1301 O OD1 . ASP A 171 ? 1.4180 1.5006 1.1712 0.4483  0.0162  -0.0995 467 ASP A OD1 
1302 O OD2 . ASP A 171 ? 1.5045 1.6377 1.1953 0.5644  0.0297  -0.1044 467 ASP A OD2 
1303 N N   . GLY A 172 ? 1.2476 1.2676 1.0134 0.4252  0.0011  -0.0893 468 GLY A N   
1304 C CA  . GLY A 172 ? 1.1657 1.2771 0.9915 0.4232  0.0003  -0.0768 468 GLY A CA  
1305 C C   . GLY A 172 ? 1.1482 1.4050 1.0313 0.4327  0.0091  -0.0695 468 GLY A C   
1306 O O   . GLY A 172 ? 1.0694 1.4099 1.0196 0.3951  0.0076  -0.0588 468 GLY A O   
1307 N N   . LYS A 173 ? 1.2255 1.5124 1.0774 0.4807  0.0185  -0.0754 469 LYS A N   
1308 C CA  . LYS A 173 ? 1.2066 1.6375 1.1078 0.4863  0.0286  -0.0688 469 LYS A CA  
1309 C C   . LYS A 173 ? 1.1835 1.6304 1.1114 0.4374  0.0321  -0.0689 469 LYS A C   
1310 O O   . LYS A 173 ? 1.1101 1.6695 1.0739 0.4325  0.0411  -0.0630 469 LYS A O   
1311 C CB  . LYS A 173 ? 1.2855 1.7537 1.1396 0.5651  0.0378  -0.0740 469 LYS A CB  
1312 C CG  . LYS A 173 ? 1.3965 1.8709 1.2274 0.5972  0.0309  -0.0665 469 LYS A CG  
1313 C CD  . LYS A 173 ? 1.5412 2.0376 1.3144 0.6533  0.0334  -0.0659 469 LYS A CD  
1314 C CE  . LYS A 173 ? 1.6688 2.1742 1.4148 0.6875  0.0265  -0.0590 469 LYS A CE  
1315 N NZ  . LYS A 173 ? 1.7955 2.3216 1.4777 0.7490  0.0277  -0.0582 469 LYS A NZ  
1316 N N   . HIS A 174 ? 1.2380 1.5788 1.1459 0.4010  0.0250  -0.0751 470 HIS A N   
1317 C CA  . HIS A 174 ? 1.2355 1.5838 1.1704 0.3501  0.0252  -0.0738 470 HIS A CA  
1318 C C   . HIS A 174 ? 1.2837 1.5967 1.2536 0.2937  0.0141  -0.0679 470 HIS A C   
1319 O O   . HIS A 174 ? 1.4062 1.6215 1.3483 0.2788  0.0059  -0.0747 470 HIS A O   
1320 C CB  . HIS A 174 ? 1.2448 1.5090 1.1217 0.3619  0.0261  -0.0871 470 HIS A CB  
1321 C CG  . HIS A 174 ? 1.3135 1.6023 1.1461 0.4236  0.0374  -0.0943 470 HIS A CG  
1322 N ND1 . HIS A 174 ? 1.3984 1.5955 1.1515 0.4766  0.0370  -0.1065 470 HIS A ND1 
1323 C CD2 . HIS A 174 ? 1.2983 1.6934 1.1497 0.4427  0.0499  -0.0908 470 HIS A CD2 
1324 C CE1 . HIS A 174 ? 1.4670 1.7117 1.1911 0.5315  0.0487  -0.1110 470 HIS A CE1 
1325 N NE2 . HIS A 174 ? 1.4032 1.7756 1.1902 0.5114  0.0572  -0.1015 470 HIS A NE2 
1326 N N   . ASP A 175 ? 1.1265 1.5202 1.1530 0.2620  0.0140  -0.0556 471 ASP A N   
1327 C CA  . ASP A 175 ? 0.8841 1.2505 0.9410 0.2150  0.0043  -0.0497 471 ASP A CA  
1328 C C   . ASP A 175 ? 0.8385 1.2486 0.9292 0.1689  0.0051  -0.0415 471 ASP A C   
1329 O O   . ASP A 175 ? 0.8864 1.3831 0.9963 0.1649  0.0127  -0.0342 471 ASP A O   
1330 C CB  . ASP A 175 ? 0.9175 1.3188 0.9974 0.2201  0.0011  -0.0424 471 ASP A CB  
1331 C CG  . ASP A 175 ? 0.9268 1.2423 0.9721 0.2420  -0.0052 -0.0486 471 ASP A CG  
1332 O OD1 . ASP A 175 ? 1.0248 1.2522 1.0260 0.2488  -0.0072 -0.0586 471 ASP A OD1 
1333 O OD2 . ASP A 175 ? 0.9622 1.2968 1.0203 0.2493  -0.0085 -0.0432 471 ASP A OD2 
1334 N N   . PHE A 176 ? 0.7563 1.1077 0.8491 0.1348  -0.0027 -0.0423 472 PHE A N   
1335 C CA  . PHE A 176 ? 0.6895 1.0643 0.8065 0.0921  -0.0046 -0.0331 472 PHE A CA  
1336 C C   . PHE A 176 ? 0.5733 0.9614 0.7169 0.0702  -0.0102 -0.0247 472 PHE A C   
1337 O O   . PHE A 176 ? 0.5777 0.9178 0.7204 0.0726  -0.0170 -0.0280 472 PHE A O   
1338 C CB  . PHE A 176 ? 0.6475 0.9585 0.7504 0.0733  -0.0110 -0.0378 472 PHE A CB  
1339 C CG  . PHE A 176 ? 0.6467 0.9504 0.7235 0.0867  -0.0062 -0.0446 472 PHE A CG  
1340 C CD1 . PHE A 176 ? 0.6628 0.9315 0.7067 0.1201  -0.0042 -0.0564 472 PHE A CD1 
1341 C CD2 . PHE A 176 ? 0.7401 1.0646 0.8168 0.0660  -0.0038 -0.0391 472 PHE A CD2 
1342 C CE1 . PHE A 176 ? 0.7691 1.0272 0.7830 0.1327  0.0001  -0.0637 472 PHE A CE1 
1343 C CE2 . PHE A 176 ? 0.7226 1.0412 0.7739 0.0782  0.0006  -0.0453 472 PHE A CE2 
1344 C CZ  . PHE A 176 ? 0.7524 1.0402 0.7739 0.1119  0.0026  -0.0581 472 PHE A CZ  
1345 N N   . ARG A 177 ? 0.5566 1.0093 0.7193 0.0465  -0.0071 -0.0141 473 ARG A N   
1346 C CA  . ARG A 177 ? 0.5339 0.9990 0.7156 0.0216  -0.0128 -0.0062 473 ARG A CA  
1347 C C   . ARG A 177 ? 0.5831 1.0612 0.7637 -0.0235 -0.0134 0.0039  473 ARG A C   
1348 O O   . ARG A 177 ? 0.6070 1.1333 0.7828 -0.0346 -0.0061 0.0086  473 ARG A O   
1349 C CB  . ARG A 177 ? 0.6039 1.1429 0.8021 0.0402  -0.0096 -0.0030 473 ARG A CB  
1350 C CG  . ARG A 177 ? 0.5361 1.0456 0.7252 0.0844  -0.0113 -0.0110 473 ARG A CG  
1351 C CD  . ARG A 177 ? 0.6588 1.0880 0.8447 0.0733  -0.0206 -0.0137 473 ARG A CD  
1352 N NE  . ARG A 177 ? 0.6743 1.1221 0.8805 0.0427  -0.0262 -0.0054 473 ARG A NE  
1353 C CZ  . ARG A 177 ? 0.6945 1.1818 0.9127 0.0519  -0.0282 -0.0016 473 ARG A CZ  
1354 N NH1 . ARG A 177 ? 0.6377 1.1511 0.8489 0.0955  -0.0250 -0.0049 473 ARG A NH1 
1355 N NH2 . ARG A 177 ? 0.6536 1.1511 0.8850 0.0201  -0.0340 0.0052  473 ARG A NH2 
1356 N N   . VAL A 178 ? 0.5293 0.9596 0.7072 -0.0486 -0.0217 0.0072  474 VAL A N   
1357 C CA  . VAL A 178 ? 0.5068 0.9432 0.6737 -0.0921 -0.0236 0.0178  474 VAL A CA  
1358 C C   . VAL A 178 ? 0.6479 1.1407 0.8327 -0.1038 -0.0247 0.0231  474 VAL A C   
1359 O O   . VAL A 178 ? 0.6568 1.1294 0.8528 -0.0914 -0.0304 0.0200  474 VAL A O   
1360 C CB  . VAL A 178 ? 0.5312 0.8827 0.6761 -0.1070 -0.0323 0.0182  474 VAL A CB  
1361 C CG1 . VAL A 178 ? 0.6154 0.9522 0.7287 -0.1504 -0.0339 0.0289  474 VAL A CG1 
1362 C CG2 . VAL A 178 ? 0.6120 0.9170 0.7466 -0.0860 -0.0332 0.0107  474 VAL A CG2 
1363 N N   . TRP A 179 ? 0.7043 1.2756 0.8919 -0.1280 -0.0192 0.0312  475 TRP A N   
1364 C CA  . TRP A 179 ? 0.6707 1.3117 0.8770 -0.1403 -0.0212 0.0362  475 TRP A CA  
1365 C C   . TRP A 179 ? 0.6082 1.2006 0.7957 -0.1830 -0.0307 0.0418  475 TRP A C   
1366 O O   . TRP A 179 ? 0.6454 1.2641 0.8465 -0.1867 -0.0360 0.0430  475 TRP A O   
1367 C CB  . TRP A 179 ? 0.6828 1.4394 0.8992 -0.1559 -0.0124 0.0433  475 TRP A CB  
1368 C CG  . TRP A 179 ? 0.5969 1.4180 0.8339 -0.1013 -0.0036 0.0368  475 TRP A CG  
1369 C CD1 . TRP A 179 ? 0.6554 1.4224 0.8861 -0.0546 -0.0010 0.0265  475 TRP A CD1 
1370 C CD2 . TRP A 179 ? 0.5795 1.5293 0.8394 -0.0854 0.0031  0.0399  475 TRP A CD2 
1371 N NE1 . TRP A 179 ? 0.6433 1.4840 0.8843 -0.0087 0.0072  0.0225  475 TRP A NE1 
1372 C CE2 . TRP A 179 ? 0.6070 1.5656 0.8684 -0.0227 0.0102  0.0307  475 TRP A CE2 
1373 C CE3 . TRP A 179 ? 0.5546 1.5740 0.8092 -0.1136 0.0030  0.0480  475 TRP A CE3 
1374 C CZ2 . TRP A 179 ? 0.5960 1.6496 0.8629 0.0157  0.0175  0.0301  475 TRP A CZ2 
1375 C CZ3 . TRP A 179 ? 0.5359 1.6409 0.7921 -0.0774 0.0093  0.0472  475 TRP A CZ3 
1376 C CH2 . TRP A 179 ? 0.5482 1.6681 0.8097 -0.0121 0.0163  0.0386  475 TRP A CH2 
1377 N N   . ASN A 180 ? 0.4782 0.9952 0.6284 -0.2124 -0.0334 0.0451  476 ASN A N   
1378 C CA  . ASN A 180 ? 0.6274 1.0733 0.7464 -0.2433 -0.0428 0.0484  476 ASN A CA  
1379 C C   . ASN A 180 ? 0.7010 1.0957 0.8344 -0.2094 -0.0490 0.0402  476 ASN A C   
1380 O O   . ASN A 180 ? 0.6654 1.0369 0.8143 -0.1702 -0.0473 0.0322  476 ASN A O   
1381 C CB  . ASN A 180 ? 0.7714 1.1319 0.8384 -0.2661 -0.0445 0.0521  476 ASN A CB  
1382 C CG  . ASN A 180 ? 0.7866 1.1870 0.8336 -0.2988 -0.0371 0.0604  476 ASN A CG  
1383 O OD1 . ASN A 180 ? 0.8471 1.3163 0.9227 -0.2788 -0.0282 0.0586  476 ASN A OD1 
1384 N ND2 . ASN A 180 ? 0.8424 1.1962 0.8332 -0.3504 -0.0405 0.0697  476 ASN A ND2 
1385 N N   . SER A 181 ? 0.6713 1.0466 0.7947 -0.2289 -0.0564 0.0423  477 SER A N   
1386 C CA  . SER A 181 ? 0.6300 0.9522 0.7601 -0.2024 -0.0620 0.0356  477 SER A CA  
1387 C C   . SER A 181 ? 0.6774 0.9028 0.7709 -0.1997 -0.0658 0.0334  477 SER A C   
1388 O O   . SER A 181 ? 0.6182 0.8092 0.7227 -0.1692 -0.0676 0.0266  477 SER A O   
1389 C CB  . SER A 181 ? 0.5860 0.9253 0.7171 -0.2210 -0.0683 0.0382  477 SER A CB  
1390 O OG  . SER A 181 ? 0.7001 1.0329 0.7925 -0.2729 -0.0719 0.0461  477 SER A OG  
1391 N N   . GLN A 182 ? 0.7256 0.9080 0.7713 -0.2306 -0.0673 0.0395  478 GLN A N   
1392 C CA  . GLN A 182 ? 0.7089 0.8040 0.7128 -0.2204 -0.0704 0.0381  478 GLN A CA  
1393 C C   . GLN A 182 ? 0.7125 0.8001 0.6852 -0.2400 -0.0666 0.0442  478 GLN A C   
1394 O O   . GLN A 182 ? 0.8486 0.9736 0.8096 -0.2791 -0.0639 0.0519  478 GLN A O   
1395 C CB  . GLN A 182 ? 0.7864 0.7995 0.7348 -0.2362 -0.0783 0.0401  478 GLN A CB  
1396 C CG  . GLN A 182 ? 0.8658 0.8732 0.8332 -0.2188 -0.0823 0.0346  478 GLN A CG  
1397 C CD  . GLN A 182 ? 0.9316 0.8598 0.8347 -0.2402 -0.0898 0.0370  478 GLN A CD  
1398 O OE1 . GLN A 182 ? 0.9485 0.7964 0.7864 -0.2461 -0.0928 0.0397  478 GLN A OE1 
1399 N NE2 . GLN A 182 ? 0.8715 0.8161 0.7853 -0.2505 -0.0933 0.0359  478 GLN A NE2 
1400 N N   . LEU A 183 ? 0.7644 0.8080 0.7222 -0.2145 -0.0667 0.0413  479 LEU A N   
1401 C CA  . LEU A 183 ? 0.7151 0.7442 0.6389 -0.2290 -0.0634 0.0472  479 LEU A CA  
1402 C C   . LEU A 183 ? 0.8621 0.8375 0.7151 -0.2776 -0.0663 0.0579  479 LEU A C   
1403 O O   . LEU A 183 ? 0.9778 0.9769 0.8116 -0.3115 -0.0612 0.0658  479 LEU A O   
1404 C CB  . LEU A 183 ? 0.7233 0.7018 0.6316 -0.1928 -0.0662 0.0426  479 LEU A CB  
1405 C CG  . LEU A 183 ? 0.7702 0.7911 0.7347 -0.1520 -0.0642 0.0322  479 LEU A CG  
1406 C CD1 . LEU A 183 ? 0.8223 0.7977 0.7614 -0.1252 -0.0685 0.0295  479 LEU A CD1 
1407 C CD2 . LEU A 183 ? 0.8158 0.9141 0.8215 -0.1537 -0.0555 0.0308  479 LEU A CD2 
1408 N N   . ILE A 184 ? 0.9142 0.8142 0.7217 -0.2836 -0.0741 0.0583  480 ILE A N   
1409 C CA  . ILE A 184 ? 0.8969 0.7191 0.6186 -0.3301 -0.0787 0.0675  480 ILE A CA  
1410 C C   . ILE A 184 ? 1.0394 0.8702 0.7618 -0.3570 -0.0833 0.0671  480 ILE A C   
1411 O O   . ILE A 184 ? 1.0505 0.8432 0.7729 -0.3297 -0.0886 0.0606  480 ILE A O   
1412 C CB  . ILE A 184 ? 0.9966 0.6954 0.6387 -0.3068 -0.0853 0.0679  480 ILE A CB  
1413 C CG1 . ILE A 184 ? 1.0857 0.7844 0.7258 -0.2841 -0.0816 0.0692  480 ILE A CG1 
1414 C CG2 . ILE A 184 ? 1.1821 0.7777 0.7180 -0.3548 -0.0910 0.0770  480 ILE A CG2 
1415 C CD1 . ILE A 184 ? 1.1092 0.7004 0.6767 -0.2497 -0.0885 0.0694  480 ILE A CD1 
1416 N N   . ARG A 185 ? 1.0630 0.9540 0.7886 -0.4103 -0.0810 0.0741  481 ARG A N   
1417 C CA  . ARG A 185 ? 1.0906 0.9956 0.8092 -0.4463 -0.0865 0.0752  481 ARG A CA  
1418 C C   . ARG A 185 ? 1.1719 1.0613 0.8224 -0.5140 -0.0873 0.0856  481 ARG A C   
1419 O O   . ARG A 185 ? 1.2350 1.1587 0.8785 -0.5338 -0.0806 0.0918  481 ARG A O   
1420 C CB  . ARG A 185 ? 1.0064 1.0432 0.8189 -0.4335 -0.0828 0.0712  481 ARG A CB  
1421 C CG  . ARG A 185 ? 1.0075 1.0596 0.8811 -0.3686 -0.0816 0.0607  481 ARG A CG  
1422 C CD  . ARG A 185 ? 0.9356 1.0647 0.8642 -0.3625 -0.0833 0.0573  481 ARG A CD  
1423 N NE  . ARG A 185 ? 1.0151 1.0823 0.9074 -0.3747 -0.0922 0.0557  481 ARG A NE  
1424 C CZ  . ARG A 185 ? 1.0037 1.1176 0.9324 -0.3678 -0.0955 0.0526  481 ARG A CZ  
1425 N NH1 . ARG A 185 ? 0.8276 1.0457 0.8259 -0.3460 -0.0908 0.0511  481 ARG A NH1 
1426 N NH2 . ARG A 185 ? 1.1334 1.1853 1.0233 -0.3792 -0.1035 0.0507  481 ARG A NH2 
1427 N N   . TYR A 186 ? 1.0939 0.9383 0.6936 -0.5335 -0.0939 0.0851  482 TYR A N   
1428 C CA  . TYR A 186 ? 1.1906 1.0272 0.7225 -0.5834 -0.0950 0.0916  482 TYR A CA  
1429 C C   . TYR A 186 ? 1.1867 1.1696 0.7808 -0.6029 -0.0901 0.0939  482 TYR A C   
1430 O O   . TYR A 186 ? 1.1234 1.1848 0.7917 -0.5780 -0.0891 0.0895  482 TYR A O   
1431 C CB  . TYR A 186 ? 1.3434 1.0622 0.7823 -0.5969 -0.1050 0.0900  482 TYR A CB  
1432 C CG  . TYR A 186 ? 1.4829 1.0499 0.8393 -0.5734 -0.1099 0.0881  482 TYR A CG  
1433 C CD1 . TYR A 186 ? 1.5817 1.0587 0.9079 -0.5392 -0.1165 0.0813  482 TYR A CD1 
1434 C CD2 . TYR A 186 ? 1.5113 1.0277 0.8186 -0.5798 -0.1077 0.0928  482 TYR A CD2 
1435 C CE1 . TYR A 186 ? 1.6655 1.0090 0.9129 -0.5068 -0.1207 0.0792  482 TYR A CE1 
1436 C CE2 . TYR A 186 ? 1.5521 0.9305 0.7798 -0.5493 -0.1124 0.0910  482 TYR A CE2 
1437 C CZ  . TYR A 186 ? 1.6843 0.9789 0.8821 -0.5100 -0.1189 0.0841  482 TYR A CZ  
1438 O OH  . TYR A 186 ? 1.7506 0.9165 0.8676 -0.4691 -0.1233 0.0816  482 TYR A OH  
1439 N N   . ALA A 187 ? 1.2658 1.2837 0.8237 -0.6458 -0.0876 0.1007  483 ALA A N   
1440 C CA  . ALA A 187 ? 1.2133 1.3760 0.8239 -0.6616 -0.0825 0.1036  483 ALA A CA  
1441 C C   . ALA A 187 ? 1.2813 1.4620 0.8776 -0.6816 -0.0890 0.1036  483 ALA A C   
1442 O O   . ALA A 187 ? 1.2847 1.3596 0.8041 -0.7028 -0.0975 0.1034  483 ALA A O   
1443 C CB  . ALA A 187 ? 1.3338 1.5281 0.9021 -0.7056 -0.0792 0.1106  483 ALA A CB  
1444 N N   . GLY A 188 ? 1.2014 1.5162 0.8676 -0.6722 -0.0847 0.1038  484 GLY A N   
1445 C CA  . GLY A 188 ? 1.3220 1.6738 0.9782 -0.6938 -0.0899 0.1052  484 GLY A CA  
1446 C C   . GLY A 188 ? 1.3536 1.8342 1.0191 -0.7253 -0.0862 0.1116  484 GLY A C   
1447 O O   . GLY A 188 ? 1.2805 1.8808 1.0199 -0.6946 -0.0785 0.1108  484 GLY A O   
1448 N N   . TYR A 189 ? 1.4527 1.9096 1.0376 -0.7859 -0.0921 0.1176  485 TYR A N   
1449 C CA  . TYR A 189 ? 1.4519 2.0325 1.0348 -0.8240 -0.0902 0.1241  485 TYR A CA  
1450 C C   . TYR A 189 ? 1.5095 2.1158 1.0742 -0.8487 -0.0964 0.1264  485 TYR A C   
1451 O O   . TYR A 189 ? 1.4828 1.9817 0.9676 -0.8848 -0.1049 0.1276  485 TYR A O   
1452 C CB  . TYR A 189 ? 1.5114 2.0578 1.0102 -0.8838 -0.0925 0.1299  485 TYR A CB  
1453 C CG  . TYR A 189 ? 1.4618 1.9216 0.9436 -0.8697 -0.0899 0.1277  485 TYR A CG  
1454 C CD1 . TYR A 189 ? 1.5348 1.8292 0.9403 -0.8767 -0.0966 0.1256  485 TYR A CD1 
1455 C CD2 . TYR A 189 ? 1.3834 1.9255 0.9198 -0.8478 -0.0806 0.1279  485 TYR A CD2 
1456 C CE1 . TYR A 189 ? 1.5278 1.7424 0.9135 -0.8624 -0.0944 0.1240  485 TYR A CE1 
1457 C CE2 . TYR A 189 ? 1.4185 1.8815 0.9374 -0.8369 -0.0779 0.1266  485 TYR A CE2 
1458 C CZ  . TYR A 189 ? 1.4472 1.7471 0.8908 -0.8449 -0.0849 0.1249  485 TYR A CZ  
1459 O OH  . TYR A 189 ? 1.3354 1.5554 0.7573 -0.8321 -0.0824 0.1241  485 TYR A OH  
1460 N N   . LYS A 190 ? 1.5189 2.2640 1.1527 -0.8270 -0.0922 0.1269  486 LYS A N   
1461 C CA  . LYS A 190 ? 1.6014 2.4030 1.2133 -0.8622 -0.0970 0.1314  486 LYS A CA  
1462 C C   . LYS A 190 ? 1.7318 2.5428 1.2566 -0.9406 -0.1007 0.1400  486 LYS A C   
1463 O O   . LYS A 190 ? 1.8046 2.6121 1.3028 -0.9609 -0.0985 0.1420  486 LYS A O   
1464 C CB  . LYS A 190 ? 1.5537 2.5134 1.2522 -0.8212 -0.0910 0.1307  486 LYS A CB  
1465 C CG  . LYS A 190 ? 1.5243 2.5869 1.2712 -0.7939 -0.0815 0.1308  486 LYS A CG  
1466 C CD  . LYS A 190 ? 1.4760 2.6968 1.2903 -0.7551 -0.0761 0.1308  486 LYS A CD  
1467 C CE  . LYS A 190 ? 1.3501 2.5617 1.2356 -0.6806 -0.0743 0.1225  486 LYS A CE  
1468 N NZ  . LYS A 190 ? 1.2801 2.6377 1.2261 -0.6307 -0.0675 0.1215  486 LYS A NZ  
1469 N N   . GLN A 191 ? 1.7558 2.5791 1.2327 -0.9873 -0.1070 0.1449  487 GLN A N   
1470 C CA  . GLN A 191 ? 1.8603 2.6728 1.2385 -1.0694 -0.1126 0.1529  487 GLN A CA  
1471 C C   . GLN A 191 ? 1.8866 2.8700 1.2818 -1.1008 -0.1108 0.1599  487 GLN A C   
1472 O O   . GLN A 191 ? 1.8408 2.9320 1.3140 -1.0590 -0.1066 0.1584  487 GLN A O   
1473 C CB  . GLN A 191 ? 1.9686 2.6286 1.2480 -1.1103 -0.1228 0.1538  487 GLN A CB  
1474 C CG  . GLN A 191 ? 1.9960 2.4775 1.2231 -1.0952 -0.1263 0.1485  487 GLN A CG  
1475 C CD  . GLN A 191 ? 2.0958 2.5274 1.2477 -1.1380 -0.1278 0.1511  487 GLN A CD  
1476 O OE1 . GLN A 191 ? 2.0748 2.6102 1.2673 -1.1386 -0.1218 0.1529  487 GLN A OE1 
1477 N NE2 . GLN A 191 ? 2.2121 2.4801 1.2488 -1.1719 -0.1364 0.1509  487 GLN A NE2 
1478 N N   . PRO A 192 ? 1.9803 2.9951 1.3004 -1.1739 -0.1142 0.1673  488 PRO A N   
1479 C CA  . PRO A 192 ? 2.0053 3.1841 1.3306 -1.2114 -0.1135 0.1746  488 PRO A CA  
1480 C C   . PRO A 192 ? 2.0265 3.2048 1.3336 -1.2313 -0.1183 0.1775  488 PRO A C   
1481 O O   . PRO A 192 ? 2.0173 3.3460 1.3665 -1.2303 -0.1154 0.1812  488 PRO A O   
1482 C CB  . PRO A 192 ? 2.1401 3.3163 1.3692 -1.2948 -0.1185 0.1813  488 PRO A CB  
1483 C CG  . PRO A 192 ? 2.2029 3.1788 1.3524 -1.3103 -0.1245 0.1778  488 PRO A CG  
1484 C CD  . PRO A 192 ? 2.0874 3.0038 1.3187 -1.2228 -0.1186 0.1688  488 PRO A CD  
1485 N N   . ASP A 193 ? 2.0437 3.0584 1.2870 -1.2471 -0.1256 0.1758  489 ASP A N   
1486 C CA  . ASP A 193 ? 2.0216 3.0218 1.2502 -1.2601 -0.1304 0.1776  489 ASP A CA  
1487 C C   . ASP A 193 ? 1.8722 2.8685 1.1964 -1.1774 -0.1274 0.1691  489 ASP A C   
1488 O O   . ASP A 193 ? 1.8360 2.7741 1.1443 -1.1791 -0.1327 0.1681  489 ASP A O   
1489 C CB  . ASP A 193 ? 2.1553 2.9788 1.2571 -1.3188 -0.1406 0.1800  489 ASP A CB  
1490 C CG  . ASP A 193 ? 2.1576 2.8053 1.2376 -1.2802 -0.1426 0.1720  489 ASP A CG  
1491 O OD1 . ASP A 193 ? 2.1635 2.7896 1.2434 -1.2700 -0.1397 0.1698  489 ASP A OD1 
1492 O OD2 . ASP A 193 ? 2.1568 2.6917 1.2194 -1.2589 -0.1470 0.1679  489 ASP A OD2 
1493 N N   . GLY A 194 ? 1.7648 2.8182 1.1830 -1.1070 -0.1195 0.1629  490 GLY A N   
1494 C CA  . GLY A 194 ? 1.6660 2.7310 1.1749 -1.0296 -0.1168 0.1548  490 GLY A CA  
1495 C C   . GLY A 194 ? 1.6766 2.5770 1.1794 -0.9945 -0.1206 0.1467  490 GLY A C   
1496 O O   . GLY A 194 ? 1.5976 2.5041 1.1757 -0.9293 -0.1188 0.1391  490 GLY A O   
1497 N N   . SER A 195 ? 1.7777 2.5307 1.1885 -1.0340 -0.1263 0.1476  491 SER A N   
1498 C CA  . SER A 195 ? 1.7745 2.3733 1.1740 -0.9975 -0.1297 0.1397  491 SER A CA  
1499 C C   . SER A 195 ? 1.7502 2.3233 1.1879 -0.9547 -0.1236 0.1347  491 SER A C   
1500 O O   . SER A 195 ? 1.6941 2.3848 1.1982 -0.9318 -0.1158 0.1352  491 SER A O   
1501 C CB  . SER A 195 ? 1.8678 2.3113 1.1423 -1.0517 -0.1388 0.1425  491 SER A CB  
1502 O OG  . SER A 195 ? 1.9760 2.3955 1.1689 -1.1089 -0.1399 0.1488  491 SER A OG  
1503 N N   . THR A 196 ? 1.7852 2.2068 1.1786 -0.9419 -0.1270 0.1300  492 THR A N   
1504 C CA  . THR A 196 ? 1.7002 2.0920 1.1339 -0.8967 -0.1214 0.1247  492 THR A CA  
1505 C C   . THR A 196 ? 1.7893 2.0177 1.1263 -0.9161 -0.1263 0.1239  492 THR A C   
1506 O O   . THR A 196 ? 1.8938 2.0014 1.1604 -0.9262 -0.1339 0.1222  492 THR A O   
1507 C CB  . THR A 196 ? 1.5692 1.9674 1.0935 -0.8243 -0.1190 0.1157  492 THR A CB  
1508 O OG1 . THR A 196 ? 1.4719 2.0167 1.0800 -0.8004 -0.1149 0.1158  492 THR A OG1 
1509 C CG2 . THR A 196 ? 1.4375 1.8034 0.9987 -0.7816 -0.1132 0.1108  492 THR A CG2 
1510 N N   . LEU A 197 ? 1.7164 1.9400 1.0465 -0.9181 -0.1220 0.1249  493 LEU A N   
1511 C CA  . LEU A 197 ? 1.7544 1.8280 1.0062 -0.9206 -0.1255 0.1227  493 LEU A CA  
1512 C C   . LEU A 197 ? 1.6314 1.6943 0.9563 -0.8566 -0.1191 0.1163  493 LEU A C   
1513 O O   . LEU A 197 ? 1.4074 1.5886 0.8277 -0.8269 -0.1108 0.1156  493 LEU A O   
1514 C CB  . LEU A 197 ? 1.7962 1.8591 0.9682 -0.9793 -0.1269 0.1289  493 LEU A CB  
1515 C CG  . LEU A 197 ? 1.8609 1.7584 0.9310 -0.9874 -0.1321 0.1267  493 LEU A CG  
1516 C CD1 . LEU A 197 ? 1.9338 1.6816 0.9219 -0.9821 -0.1409 0.1232  493 LEU A CD1 
1517 C CD2 . LEU A 197 ? 1.9540 1.8417 0.9343 -1.0550 -0.1356 0.1324  493 LEU A CD2 
1518 N N   . GLY A 198 ? 1.7762 1.6965 1.0506 -0.8344 -0.1231 0.1115  494 GLY A N   
1519 C CA  . GLY A 198 ? 1.7461 1.6423 1.0750 -0.7788 -0.1180 0.1060  494 GLY A CA  
1520 C C   . GLY A 198 ? 1.6338 1.5433 1.0377 -0.7256 -0.1178 0.0987  494 GLY A C   
1521 O O   . GLY A 198 ? 1.7848 1.6107 1.1463 -0.7199 -0.1247 0.0952  494 GLY A O   
1522 N N   . ASP A 199 ? 1.3380 1.3514 0.8477 -0.6873 -0.1103 0.0961  495 ASP A N   
1523 C CA  . ASP A 199 ? 1.1433 1.1742 0.7257 -0.6370 -0.1106 0.0883  495 ASP A CA  
1524 C C   . ASP A 199 ? 1.1483 1.3276 0.8172 -0.6264 -0.1065 0.0887  495 ASP A C   
1525 O O   . ASP A 199 ? 1.0319 1.3085 0.7628 -0.6097 -0.0985 0.0897  495 ASP A O   
1526 C CB  . ASP A 199 ? 1.1625 1.1618 0.7832 -0.5923 -0.1068 0.0833  495 ASP A CB  
1527 C CG  . ASP A 199 ? 1.2379 1.2081 0.8984 -0.5476 -0.1107 0.0744  495 ASP A CG  
1528 O OD1 . ASP A 199 ? 1.1449 1.1601 0.8340 -0.5444 -0.1137 0.0721  495 ASP A OD1 
1529 O OD2 . ASP A 199 ? 1.2074 1.1107 0.8673 -0.5169 -0.1112 0.0697  495 ASP A OD2 
1530 N N   . PRO A 200 ? 1.1603 1.3607 0.8323 -0.6321 -0.1115 0.0878  496 PRO A N   
1531 C CA  . PRO A 200 ? 1.0765 1.4168 0.8235 -0.6182 -0.1081 0.0884  496 PRO A CA  
1532 C C   . PRO A 200 ? 0.9920 1.3932 0.8310 -0.5585 -0.1031 0.0820  496 PRO A C   
1533 O O   . PRO A 200 ? 1.0141 1.5337 0.9097 -0.5408 -0.0979 0.0832  496 PRO A O   
1534 C CB  . PRO A 200 ? 1.1608 1.4809 0.8844 -0.6315 -0.1162 0.0875  496 PRO A CB  
1535 C CG  . PRO A 200 ? 1.2494 1.4359 0.8675 -0.6718 -0.1227 0.0897  496 PRO A CG  
1536 C CD  . PRO A 200 ? 1.2440 1.3404 0.8438 -0.6511 -0.1206 0.0864  496 PRO A CD  
1537 N N   . ALA A 201 ? 0.9940 1.3175 0.8432 -0.5263 -0.1046 0.0753  497 ALA A N   
1538 C CA  . ALA A 201 ? 0.9692 1.3440 0.8971 -0.4734 -0.1005 0.0694  497 ALA A CA  
1539 C C   . ALA A 201 ? 0.9884 1.4459 0.9518 -0.4640 -0.0907 0.0725  497 ALA A C   
1540 O O   . ALA A 201 ? 0.9484 1.4934 0.9747 -0.4253 -0.0860 0.0700  497 ALA A O   
1541 C CB  . ALA A 201 ? 0.9319 1.2056 0.8523 -0.4497 -0.1041 0.0628  497 ALA A CB  
1542 N N   . ASN A 202 ? 1.0828 1.5089 1.0002 -0.4968 -0.0875 0.0777  498 ASN A N   
1543 C CA  . ASN A 202 ? 1.0526 1.5375 0.9968 -0.4873 -0.0782 0.0799  498 ASN A CA  
1544 C C   . ASN A 202 ? 1.0733 1.6617 1.0145 -0.5133 -0.0730 0.0868  498 ASN A C   
1545 O O   . ASN A 202 ? 1.0322 1.6668 0.9817 -0.5140 -0.0653 0.0895  498 ASN A O   
1546 C CB  . ASN A 202 ? 1.0819 1.4673 0.9762 -0.5045 -0.0781 0.0815  498 ASN A CB  
1547 C CG  . ASN A 202 ? 1.0240 1.3031 0.9092 -0.4815 -0.0846 0.0750  498 ASN A CG  
1548 O OD1 . ASN A 202 ? 0.9640 1.2668 0.9074 -0.4396 -0.0850 0.0683  498 ASN A OD1 
1549 N ND2 . ASN A 202 ? 1.0853 1.2443 0.8905 -0.5070 -0.0904 0.0768  498 ASN A ND2 
1550 N N   . VAL A 203 ? 1.0353 1.6660 0.9645 -0.5344 -0.0771 0.0896  499 VAL A N   
1551 C CA  . VAL A 203 ? 1.0197 1.7446 0.9321 -0.5692 -0.0739 0.0970  499 VAL A CA  
1552 C C   . VAL A 203 ? 0.8730 1.7222 0.8472 -0.5299 -0.0643 0.0962  499 VAL A C   
1553 O O   . VAL A 203 ? 0.8939 1.8072 0.8553 -0.5514 -0.0589 0.1014  499 VAL A O   
1554 C CB  . VAL A 203 ? 1.0492 1.8011 0.9405 -0.5961 -0.0806 0.0999  499 VAL A CB  
1555 C CG1 . VAL A 203 ? 1.0571 1.9379 0.9486 -0.6203 -0.0766 0.1066  499 VAL A CG1 
1556 C CG2 . VAL A 203 ? 1.2072 1.8372 1.0150 -0.6459 -0.0892 0.1023  499 VAL A CG2 
1557 N N   . GLN A 204 ? 0.7914 1.6739 0.8270 -0.4708 -0.0624 0.0896  500 GLN A N   
1558 C CA  . GLN A 204 ? 0.8015 1.7856 0.8857 -0.4254 -0.0533 0.0878  500 GLN A CA  
1559 C C   . GLN A 204 ? 0.7911 1.7471 0.8784 -0.4165 -0.0464 0.0866  500 GLN A C   
1560 O O   . GLN A 204 ? 0.8231 1.8521 0.9115 -0.4186 -0.0389 0.0897  500 GLN A O   
1561 C CB  . GLN A 204 ? 0.7886 1.7969 0.9246 -0.3626 -0.0540 0.0807  500 GLN A CB  
1562 C CG  . GLN A 204 ? 0.7962 1.8937 0.9701 -0.3086 -0.0447 0.0780  500 GLN A CG  
1563 C CD  . GLN A 204 ? 0.9037 2.0246 1.1140 -0.2467 -0.0462 0.0720  500 GLN A CD  
1564 O OE1 . GLN A 204 ? 0.9481 2.0130 1.1630 -0.2420 -0.0543 0.0692  500 GLN A OE1 
1565 N NE2 . GLN A 204 ? 0.9418 2.1421 1.1717 -0.1974 -0.0389 0.0700  500 GLN A NE2 
1566 N N   . PHE A 205 ? 0.7956 1.6499 0.8834 -0.4060 -0.0491 0.0820  501 PHE A N   
1567 C CA  . PHE A 205 ? 0.8027 1.6262 0.8916 -0.3990 -0.0430 0.0810  501 PHE A CA  
1568 C C   . PHE A 205 ? 0.8146 1.6233 0.8486 -0.4549 -0.0412 0.0890  501 PHE A C   
1569 O O   . PHE A 205 ? 0.7966 1.6437 0.8351 -0.4519 -0.0331 0.0907  501 PHE A O   
1570 C CB  . PHE A 205 ? 0.8194 1.5359 0.9110 -0.3839 -0.0482 0.0753  501 PHE A CB  
1571 C CG  . PHE A 205 ? 0.9214 1.6007 1.0094 -0.3805 -0.0430 0.0749  501 PHE A CG  
1572 C CD1 . PHE A 205 ? 0.8891 1.6249 1.0227 -0.3350 -0.0349 0.0701  501 PHE A CD1 
1573 C CD2 . PHE A 205 ? 0.9989 1.5822 1.0305 -0.4212 -0.0464 0.0792  501 PHE A CD2 
1574 C CE1 . PHE A 205 ? 0.8472 1.5532 0.9769 -0.3335 -0.0301 0.0699  501 PHE A CE1 
1575 C CE2 . PHE A 205 ? 0.9186 1.4680 0.9439 -0.4185 -0.0419 0.0798  501 PHE A CE2 
1576 C CZ  . PHE A 205 ? 0.9110 1.5272 0.9889 -0.3766 -0.0335 0.0752  501 PHE A CZ  
1577 N N   . THR A 206 ? 0.7974 1.5460 0.7730 -0.5063 -0.0491 0.0938  502 THR A N   
1578 C CA  . THR A 206 ? 0.9565 1.6898 0.8686 -0.5630 -0.0491 0.1016  502 THR A CA  
1579 C C   . THR A 206 ? 1.0084 1.8767 0.9359 -0.5707 -0.0427 0.1057  502 THR A C   
1580 O O   . THR A 206 ? 0.9735 1.8576 0.8739 -0.5975 -0.0389 0.1101  502 THR A O   
1581 C CB  . THR A 206 ? 1.0252 1.6762 0.8654 -0.6139 -0.0597 0.1052  502 THR A CB  
1582 O OG1 . THR A 206 ? 1.0272 1.5447 0.8418 -0.6049 -0.0655 0.1013  502 THR A OG1 
1583 C CG2 . THR A 206 ? 0.9327 1.5711 0.6974 -0.6768 -0.0614 0.1129  502 THR A CG2 
1584 N N   . GLU A 207 ? 1.0623 2.0301 1.0306 -0.5455 -0.0419 0.1043  503 GLU A N   
1585 C CA  . GLU A 207 ? 1.1167 2.2208 1.0984 -0.5464 -0.0363 0.1078  503 GLU A CA  
1586 C C   . GLU A 207 ? 1.0225 2.1881 1.0533 -0.4916 -0.0258 0.1036  503 GLU A C   
1587 O O   . GLU A 207 ? 1.0242 2.2721 1.0499 -0.5011 -0.0205 0.1071  503 GLU A O   
1588 C CB  . GLU A 207 ? 1.1757 2.3634 1.1756 -0.5370 -0.0395 0.1084  503 GLU A CB  
1589 C CG  . GLU A 207 ? 1.3775 2.5644 1.3181 -0.6061 -0.0474 0.1156  503 GLU A CG  
1590 C CD  . GLU A 207 ? 1.5016 2.6901 1.4506 -0.6005 -0.0537 0.1145  503 GLU A CD  
1591 O OE1 . GLU A 207 ? 1.4778 2.7161 1.4827 -0.5422 -0.0511 0.1094  503 GLU A OE1 
1592 O OE2 . GLU A 207 ? 1.5890 2.7238 1.4834 -0.6542 -0.0617 0.1186  503 GLU A OE2 
1593 N N   . ILE A 208 ? 0.9336 2.0598 1.0075 -0.4354 -0.0233 0.0959  504 ILE A N   
1594 C CA  . ILE A 208 ? 0.8302 1.9993 0.9417 -0.3826 -0.0135 0.0910  504 ILE A CA  
1595 C C   . ILE A 208 ? 0.8312 1.9656 0.9170 -0.4108 -0.0086 0.0942  504 ILE A C   
1596 O O   . ILE A 208 ? 0.7294 1.9361 0.8255 -0.3943 -0.0002 0.0944  504 ILE A O   
1597 C CB  . ILE A 208 ? 0.7536 1.8722 0.9059 -0.3238 -0.0137 0.0818  504 ILE A CB  
1598 C CG1 . ILE A 208 ? 0.7057 1.8697 0.8818 -0.2897 -0.0177 0.0788  504 ILE A CG1 
1599 C CG2 . ILE A 208 ? 0.7547 1.8982 0.9337 -0.2736 -0.0038 0.0762  504 ILE A CG2 
1600 C CD1 . ILE A 208 ? 0.7308 1.8223 0.9333 -0.2495 -0.0224 0.0709  504 ILE A CD1 
1601 N N   . CYS A 209 ? 0.8641 1.8847 0.9114 -0.4514 -0.0138 0.0967  505 CYS A N   
1602 C CA  . CYS A 209 ? 0.8909 1.8696 0.9020 -0.4838 -0.0101 0.1012  505 CYS A CA  
1603 C C   . CYS A 209 ? 0.9560 2.0094 0.9322 -0.5297 -0.0095 0.1085  505 CYS A C   
1604 O O   . CYS A 209 ? 1.0144 2.1038 0.9869 -0.5328 -0.0023 0.1104  505 CYS A O   
1605 C CB  . CYS A 209 ? 0.9379 1.7729 0.8989 -0.5190 -0.0179 0.1033  505 CYS A CB  
1606 S SG  . CYS A 209 ? 0.9098 1.6573 0.9070 -0.4712 -0.0208 0.0949  505 CYS A SG  
1607 N N   . ILE A 210 ? 0.9459 2.0265 0.8944 -0.5677 -0.0173 0.1124  506 ILE A N   
1608 C CA  . ILE A 210 ? 1.0146 2.1810 0.9304 -0.6140 -0.0182 0.1190  506 ILE A CA  
1609 C C   . ILE A 210 ? 1.0108 2.3229 0.9771 -0.5695 -0.0096 0.1171  506 ILE A C   
1610 O O   . ILE A 210 ? 0.9959 2.3760 0.9491 -0.5891 -0.0060 0.1207  506 ILE A O   
1611 C CB  . ILE A 210 ? 1.0111 2.1819 0.8862 -0.6628 -0.0285 0.1233  506 ILE A CB  
1612 C CG1 . ILE A 210 ? 1.0273 2.0436 0.8394 -0.7044 -0.0377 0.1246  506 ILE A CG1 
1613 C CG2 . ILE A 210 ? 1.0962 2.3651 0.9359 -0.7145 -0.0304 0.1299  506 ILE A CG2 
1614 C CD1 . ILE A 210 ? 1.0073 2.0153 0.7852 -0.7395 -0.0473 0.1270  506 ILE A CD1 
1615 N N   . GLN A 211 ? 0.9908 2.3484 1.0105 -0.5067 -0.0067 0.1111  507 GLN A N   
1616 C CA  . GLN A 211 ? 0.9562 2.4369 1.0163 -0.4519 0.0013  0.1080  507 GLN A CA  
1617 C C   . GLN A 211 ? 0.9242 2.4000 0.9959 -0.4264 0.0109  0.1053  507 GLN A C   
1618 O O   . GLN A 211 ? 0.8275 2.4015 0.9017 -0.4189 0.0160  0.1069  507 GLN A O   
1619 C CB  . GLN A 211 ? 0.9165 2.4120 1.0206 -0.3851 0.0018  0.1009  507 GLN A CB  
1620 C CG  . GLN A 211 ? 0.9483 2.5253 1.0516 -0.3903 -0.0037 0.1037  507 GLN A CG  
1621 C CD  . GLN A 211 ? 0.9851 2.7090 1.1024 -0.3543 0.0011  0.1043  507 GLN A CD  
1622 O OE1 . GLN A 211 ? 1.0089 2.7619 1.1469 -0.3006 0.0088  0.0994  507 GLN A OE1 
1623 N NE2 . GLN A 211 ? 0.9735 2.7915 1.0754 -0.3829 -0.0036 0.1101  507 GLN A NE2 
1624 N N   . GLN A 212 ? 0.9778 2.3440 1.0552 -0.4129 0.0134  0.1014  508 GLN A N   
1625 C CA  . GLN A 212 ? 0.9983 2.3512 1.0833 -0.3911 0.0232  0.0990  508 GLN A CA  
1626 C C   . GLN A 212 ? 1.0166 2.3356 1.0540 -0.4552 0.0231  0.1067  508 GLN A C   
1627 O O   . GLN A 212 ? 0.9949 2.2910 1.0320 -0.4446 0.0315  0.1060  508 GLN A O   
1628 C CB  . GLN A 212 ? 1.0038 2.2603 1.1121 -0.3513 0.0257  0.0917  508 GLN A CB  
1629 C CG  . GLN A 212 ? 1.0103 2.2965 1.1621 -0.2801 0.0268  0.0825  508 GLN A CG  
1630 C CD  . GLN A 212 ? 1.0847 2.4787 1.2532 -0.2286 0.0348  0.0789  508 GLN A CD  
1631 O OE1 . GLN A 212 ? 1.1270 2.5981 1.3041 -0.2049 0.0322  0.0785  508 GLN A OE1 
1632 N NE2 . GLN A 212 ? 1.0618 2.4602 1.2302 -0.2089 0.0445  0.0763  508 GLN A NE2 
1633 N N   . GLY A 213 ? 1.0871 2.3970 1.0789 -0.5212 0.0138  0.1139  509 GLY A N   
1634 C CA  . GLY A 213 ? 1.1293 2.4153 1.0669 -0.5841 0.0122  0.1210  509 GLY A CA  
1635 C C   . GLY A 213 ? 1.1561 2.2946 1.0321 -0.6369 0.0042  0.1249  509 GLY A C   
1636 O O   . GLY A 213 ? 1.1675 2.2664 0.9898 -0.6863 0.0028  0.1302  509 GLY A O   
1637 N N   . TRP A 214 ? 1.1778 2.2296 1.0541 -0.6267 -0.0017 0.1221  510 TRP A N   
1638 C CA  . TRP A 214 ? 1.2639 2.1686 1.0724 -0.6710 -0.0104 0.1253  510 TRP A CA  
1639 C C   . TRP A 214 ? 1.3411 2.2421 1.0787 -0.7425 -0.0206 0.1311  510 TRP A C   
1640 O O   . TRP A 214 ? 1.2371 2.2292 0.9839 -0.7556 -0.0244 0.1319  510 TRP A O   
1641 C CB  . TRP A 214 ? 1.2370 2.0602 1.0595 -0.6446 -0.0159 0.1208  510 TRP A CB  
1642 C CG  . TRP A 214 ? 1.2664 1.9280 1.0185 -0.6743 -0.0237 0.1231  510 TRP A CG  
1643 C CD1 . TRP A 214 ? 1.2596 1.8315 0.9735 -0.6804 -0.0211 0.1258  510 TRP A CD1 
1644 C CD2 . TRP A 214 ? 1.2941 1.8609 0.9985 -0.6965 -0.0356 0.1227  510 TRP A CD2 
1645 N NE1 . TRP A 214 ? 1.3139 1.7383 0.9564 -0.7015 -0.0312 0.1269  510 TRP A NE1 
1646 C CE2 . TRP A 214 ? 1.3201 1.7385 0.9553 -0.7114 -0.0401 0.1245  510 TRP A CE2 
1647 C CE3 . TRP A 214 ? 1.2680 1.8588 0.9775 -0.7028 -0.0425 0.1211  510 TRP A CE3 
1648 C CZ2 . TRP A 214 ? 1.3727 1.6656 0.9417 -0.7286 -0.0516 0.1237  510 TRP A CZ2 
1649 C CZ3 . TRP A 214 ? 1.3032 1.7720 0.9506 -0.7244 -0.0533 0.1208  510 TRP A CZ3 
1650 C CH2 . TRP A 214 ? 1.4020 1.7231 0.9790 -0.7354 -0.0578 0.1216  510 TRP A CH2 
1651 N N   . LYS A 215 ? 1.4158 2.2089 1.0769 -0.7888 -0.0252 0.1350  511 LYS A N   
1652 C CA  . LYS A 215 ? 1.5194 2.2758 1.0951 -0.8610 -0.0366 0.1392  511 LYS A CA  
1653 C C   . LYS A 215 ? 1.4956 2.1043 1.0136 -0.8727 -0.0472 0.1377  511 LYS A C   
1654 O O   . LYS A 215 ? 1.5327 2.0075 1.0119 -0.8636 -0.0485 0.1370  511 LYS A O   
1655 C CB  . LYS A 215 ? 1.5756 2.3032 1.0933 -0.9048 -0.0360 0.1434  511 LYS A CB  
1656 C CG  . LYS A 215 ? 1.5944 2.4829 1.1591 -0.9040 -0.0276 0.1453  511 LYS A CG  
1657 C CD  . LYS A 215 ? 1.6957 2.6761 1.2245 -0.9650 -0.0358 0.1489  511 LYS A CD  
1658 C CE  . LYS A 215 ? 1.6314 2.7108 1.2056 -0.9462 -0.0384 0.1475  511 LYS A CE  
1659 N NZ  . LYS A 215 ? 1.6963 2.8153 1.2092 -1.0167 -0.0495 0.1518  511 LYS A NZ  
1660 N N   . ALA A 216 ? 1.4427 2.0771 0.9527 -0.8897 -0.0544 0.1375  512 ALA A N   
1661 C CA  . ALA A 216 ? 1.4094 1.9229 0.8816 -0.8871 -0.0629 0.1350  512 ALA A CA  
1662 C C   . ALA A 216 ? 1.5674 1.9594 0.9171 -0.9521 -0.0749 0.1374  512 ALA A C   
1663 O O   . ALA A 216 ? 1.6356 2.0814 0.9412 -1.0090 -0.0799 0.1412  512 ALA A O   
1664 C CB  . ALA A 216 ? 1.3264 1.9232 0.8492 -0.8704 -0.0641 0.1336  512 ALA A CB  
1665 N N   . PRO A 217 ? 1.6179 1.8448 0.9041 -0.9446 -0.0804 0.1350  513 PRO A N   
1666 C CA  . PRO A 217 ? 1.7546 1.8492 0.9115 -1.0001 -0.0928 0.1356  513 PRO A CA  
1667 C C   . PRO A 217 ? 1.8660 1.9293 0.9861 -1.0177 -0.1018 0.1347  513 PRO A C   
1668 O O   . PRO A 217 ? 2.0031 1.9177 1.0227 -1.0350 -0.1115 0.1326  513 PRO A O   
1669 C CB  . PRO A 217 ? 1.7733 1.7081 0.8825 -0.9689 -0.0941 0.1325  513 PRO A CB  
1670 C CG  . PRO A 217 ? 1.6500 1.6195 0.8622 -0.8976 -0.0856 0.1299  513 PRO A CG  
1671 C CD  . PRO A 217 ? 1.5795 1.7344 0.9021 -0.8845 -0.0752 0.1316  513 PRO A CD  
1672 N N   . ARG A 218 ? 1.8270 2.0277 1.0231 -1.0111 -0.0983 0.1362  514 ARG A N   
1673 C CA  . ARG A 218 ? 1.8135 2.0155 1.0022 -1.0180 -0.1041 0.1361  514 ARG A CA  
1674 C C   . ARG A 218 ? 1.8950 1.9245 0.9718 -1.0389 -0.1154 0.1341  514 ARG A C   
1675 O O   . ARG A 218 ? 1.9875 1.9925 0.9799 -1.0974 -0.1238 0.1372  514 ARG A O   
1676 C CB  . ARG A 218 ? 1.8628 2.2010 1.0531 -1.0683 -0.1052 0.1417  514 ARG A CB  
1677 C CG  . ARG A 218 ? 1.7755 2.2939 1.0853 -1.0307 -0.0943 0.1424  514 ARG A CG  
1678 C CD  . ARG A 218 ? 1.8013 2.4592 1.1238 -1.0642 -0.0956 0.1473  514 ARG A CD  
1679 N NE  . ARG A 218 ? 1.6706 2.4612 1.1076 -1.0038 -0.0867 0.1452  514 ARG A NE  
1680 C CZ  . ARG A 218 ? 1.5754 2.4691 1.0901 -0.9613 -0.0768 0.1437  514 ARG A CZ  
1681 N NH1 . ARG A 218 ? 1.4402 2.4398 1.0454 -0.9042 -0.0700 0.1409  514 ARG A NH1 
1682 N NH2 . ARG A 218 ? 1.6453 2.5317 1.1425 -0.9743 -0.0738 0.1446  514 ARG A NH2 
1683 N N   . GLY A 219 ? 1.8671 1.7787 0.9391 -0.9900 -0.1158 0.1288  515 GLY A N   
1684 C CA  . GLY A 219 ? 1.9420 1.6961 0.9187 -0.9922 -0.1258 0.1255  515 GLY A CA  
1685 C C   . GLY A 219 ? 1.8587 1.6003 0.9013 -0.9319 -0.1241 0.1207  515 GLY A C   
1686 O O   . GLY A 219 ? 1.6440 1.5117 0.7984 -0.9032 -0.1171 0.1206  515 GLY A O   
1687 N N   . ARG A 220 ? 2.0110 1.6007 0.9818 -0.9099 -0.1308 0.1159  516 ARG A N   
1688 C CA  . ARG A 220 ? 2.0231 1.5905 1.0482 -0.8524 -0.1302 0.1104  516 ARG A CA  
1689 C C   . ARG A 220 ? 1.9849 1.5636 1.0887 -0.7929 -0.1228 0.1068  516 ARG A C   
1690 O O   . ARG A 220 ? 1.9034 1.6089 1.1212 -0.7698 -0.1144 0.1071  516 ARG A O   
1691 C CB  . ARG A 220 ? 2.1371 1.5382 1.0484 -0.8475 -0.1402 0.1062  516 ARG A CB  
1692 C CG  . ARG A 220 ? 2.1154 1.5139 1.0593 -0.8186 -0.1425 0.1024  516 ARG A CG  
1693 C CD  . ARG A 220 ? 2.2397 1.6182 1.1058 -0.8727 -0.1498 0.1063  516 ARG A CD  
1694 N NE  . ARG A 220 ? 2.3044 1.5927 1.1302 -0.8484 -0.1557 0.1016  516 ARG A NE  
1695 C CZ  . ARG A 220 ? 2.2423 1.5982 1.1274 -0.8434 -0.1556 0.1013  516 ARG A CZ  
1696 N NH1 . ARG A 220 ? 2.1101 1.6243 1.0956 -0.8581 -0.1500 0.1052  516 ARG A NH1 
1697 N NH2 . ARG A 220 ? 2.3290 1.5943 1.1695 -0.8212 -0.1611 0.0967  516 ARG A NH2 
1698 N N   . PHE A 221 ? 1.9335 1.3763 0.9689 -0.7668 -0.1262 0.1034  517 PHE A N   
1699 C CA  . PHE A 221 ? 1.7907 1.2183 0.8832 -0.7069 -0.1211 0.0999  517 PHE A CA  
1700 C C   . PHE A 221 ? 1.8526 1.3306 0.9748 -0.7127 -0.1134 0.1045  517 PHE A C   
1701 O O   . PHE A 221 ? 1.9783 1.3664 1.0493 -0.6957 -0.1139 0.1044  517 PHE A O   
1702 C CB  . PHE A 221 ? 1.8382 1.1020 0.8398 -0.6701 -0.1283 0.0942  517 PHE A CB  
1703 C CG  . PHE A 221 ? 1.8570 1.0661 0.8199 -0.6640 -0.1355 0.0896  517 PHE A CG  
1704 C CD1 . PHE A 221 ? 2.0102 1.1184 0.8485 -0.6992 -0.1442 0.0895  517 PHE A CD1 
1705 C CD2 . PHE A 221 ? 1.6749 0.9310 0.7211 -0.6247 -0.1338 0.0851  517 PHE A CD2 
1706 C CE1 . PHE A 221 ? 2.1227 1.1790 0.9217 -0.6933 -0.1502 0.0860  517 PHE A CE1 
1707 C CE2 . PHE A 221 ? 1.8263 1.0321 0.8360 -0.6187 -0.1400 0.0809  517 PHE A CE2 
1708 C CZ  . PHE A 221 ? 1.9252 1.0324 0.8121 -0.6525 -0.1478 0.0819  517 PHE A CZ  
1709 N N   . ASP A 222 ? 1.7497 1.3778 0.9550 -0.7340 -0.1061 0.1084  518 ASP A N   
1710 C CA  . ASP A 222 ? 1.5698 1.2753 0.8197 -0.7383 -0.0970 0.1127  518 ASP A CA  
1711 C C   . ASP A 222 ? 1.4384 1.2094 0.7968 -0.6834 -0.0885 0.1105  518 ASP A C   
1712 O O   . ASP A 222 ? 1.3687 1.2551 0.8181 -0.6688 -0.0842 0.1084  518 ASP A O   
1713 C CB  . ASP A 222 ? 1.5002 1.3383 0.7769 -0.7851 -0.0937 0.1172  518 ASP A CB  
1714 C CG  . ASP A 222 ? 1.7263 1.5045 0.8915 -0.8475 -0.1029 0.1197  518 ASP A CG  
1715 O OD1 . ASP A 222 ? 1.8913 1.5175 0.9523 -0.8531 -0.1112 0.1174  518 ASP A OD1 
1716 O OD2 . ASP A 222 ? 1.7923 1.6749 0.9689 -0.8897 -0.1024 0.1235  518 ASP A OD2 
1717 N N   . VAL A 223 ? 1.4583 1.1522 0.8007 -0.6520 -0.0869 0.1107  519 VAL A N   
1718 C CA  . VAL A 223 ? 1.3588 1.1081 0.7933 -0.6056 -0.0795 0.1092  519 VAL A CA  
1719 C C   . VAL A 223 ? 1.2756 1.1869 0.8007 -0.6133 -0.0686 0.1111  519 VAL A C   
1720 O O   . VAL A 223 ? 1.2588 1.2114 0.7631 -0.6465 -0.0641 0.1163  519 VAL A O   
1721 C CB  . VAL A 223 ? 1.4027 1.0481 0.7907 -0.5791 -0.0791 0.1126  519 VAL A CB  
1722 C CG1 . VAL A 223 ? 1.2504 0.9460 0.7264 -0.5225 -0.0742 0.1079  519 VAL A CG1 
1723 C CG2 . VAL A 223 ? 1.5724 1.0545 0.8529 -0.5655 -0.0905 0.1099  519 VAL A CG2 
1724 N N   . LEU A 224 ? 1.2018 1.2058 0.8240 -0.5797 -0.0648 0.1057  520 LEU A N   
1725 C CA  . LEU A 224 ? 1.1322 1.2887 0.8368 -0.5736 -0.0545 0.1056  520 LEU A CA  
1726 C C   . LEU A 224 ? 1.0677 1.2465 0.8013 -0.5534 -0.0448 0.1077  520 LEU A C   
1727 O O   . LEU A 224 ? 1.0366 1.1221 0.7467 -0.5194 -0.0476 0.1047  520 LEU A O   
1728 C CB  . LEU A 224 ? 0.9552 1.1954 0.7434 -0.5390 -0.0549 0.0978  520 LEU A CB  
1729 C CG  . LEU A 224 ? 1.0231 1.2961 0.8020 -0.5599 -0.0604 0.0976  520 LEU A CG  
1730 C CD1 . LEU A 224 ? 0.8442 1.0988 0.6603 -0.5263 -0.0666 0.0899  520 LEU A CD1 
1731 C CD2 . LEU A 224 ? 0.9921 1.4107 0.8172 -0.5644 -0.0531 0.0996  520 LEU A CD2 
1732 N N   . PRO A 225 ? 1.0397 1.3390 0.8194 -0.5532 -0.0343 0.1090  521 PRO A N   
1733 C CA  . PRO A 225 ? 1.0446 1.3723 0.8548 -0.5230 -0.0242 0.1084  521 PRO A CA  
1734 C C   . PRO A 225 ? 0.9376 1.3196 0.8297 -0.4511 -0.0227 0.0948  521 PRO A C   
1735 O O   . PRO A 225 ? 0.8791 1.3339 0.8215 -0.4400 -0.0238 0.0905  521 PRO A O   
1736 C CB  . PRO A 225 ? 1.0257 1.4575 0.8394 -0.5522 -0.0144 0.1143  521 PRO A CB  
1737 C CG  . PRO A 225 ? 1.0192 1.5294 0.8555 -0.5601 -0.0190 0.1113  521 PRO A CG  
1738 C CD  . PRO A 225 ? 1.0644 1.4707 0.8561 -0.5763 -0.0320 0.1104  521 PRO A CD  
1739 N N   . LEU A 226 ? 0.8698 1.2096 0.7682 -0.4035 -0.0211 0.0880  522 LEU A N   
1740 C CA  . LEU A 226 ? 0.8051 1.1892 0.7696 -0.3412 -0.0190 0.0754  522 LEU A CA  
1741 C C   . LEU A 226 ? 0.7714 1.2888 0.7857 -0.3334 -0.0076 0.0750  522 LEU A C   
1742 O O   . LEU A 226 ? 0.8553 1.4247 0.8567 -0.3586 0.0016  0.0821  522 LEU A O   
1743 C CB  . LEU A 226 ? 0.8395 1.1583 0.7940 -0.3008 -0.0198 0.0688  522 LEU A CB  
1744 C CG  . LEU A 226 ? 0.8686 1.0687 0.7822 -0.2890 -0.0311 0.0668  522 LEU A CG  
1745 C CD1 . LEU A 226 ? 0.8696 1.0253 0.7639 -0.2613 -0.0310 0.0638  522 LEU A CD1 
1746 C CD2 . LEU A 226 ? 0.7499 0.9404 0.7011 -0.2562 -0.0379 0.0570  522 LEU A CD2 
1747 N N   . LEU A 227 ? 0.7275 1.3012 0.7942 -0.2970 -0.0080 0.0670  523 LEU A N   
1748 C CA  . LEU A 227 ? 0.7234 1.4135 0.8348 -0.2676 0.0022  0.0637  523 LEU A CA  
1749 C C   . LEU A 227 ? 0.6817 1.3383 0.8154 -0.2031 0.0023  0.0502  523 LEU A C   
1750 O O   . LEU A 227 ? 0.5622 1.1928 0.7152 -0.1756 -0.0043 0.0433  523 LEU A O   
1751 C CB  . LEU A 227 ? 0.6139 1.3985 0.7576 -0.2760 0.0012  0.0663  523 LEU A CB  
1752 C CG  . LEU A 227 ? 0.6558 1.5616 0.8047 -0.3003 0.0090  0.0739  523 LEU A CG  
1753 C CD1 . LEU A 227 ? 0.6029 1.5668 0.7765 -0.2727 0.0049  0.0704  523 LEU A CD1 
1754 C CD2 . LEU A 227 ? 0.6378 1.6113 0.7954 -0.2762 0.0225  0.0727  523 LEU A CD2 
1755 N N   . LEU A 228 ? 0.6086 1.2629 0.7346 -0.1823 0.0094  0.0466  524 LEU A N   
1756 C CA  . LEU A 228 ? 0.6604 1.2620 0.7925 -0.1317 0.0077  0.0338  524 LEU A CA  
1757 C C   . LEU A 228 ? 0.6603 1.3355 0.8116 -0.0886 0.0180  0.0269  524 LEU A C   
1758 O O   . LEU A 228 ? 0.7354 1.4724 0.8809 -0.0937 0.0285  0.0307  524 LEU A O   
1759 C CB  . LEU A 228 ? 0.6364 1.1571 0.7345 -0.1385 0.0050  0.0332  524 LEU A CB  
1760 C CG  . LEU A 228 ? 0.5672 1.0127 0.6325 -0.1768 -0.0043 0.0412  524 LEU A CG  
1761 C CD1 . LEU A 228 ? 0.6120 0.9894 0.6391 -0.1780 -0.0064 0.0419  524 LEU A CD1 
1762 C CD2 . LEU A 228 ? 0.5040 0.8988 0.5807 -0.1665 -0.0150 0.0365  524 LEU A CD2 
1763 N N   . GLN A 229 ? 0.7068 1.3710 0.8742 -0.0452 0.0152  0.0171  525 GLN A N   
1764 C CA  . GLN A 229 ? 0.6356 1.3418 0.8071 0.0066  0.0231  0.0084  525 GLN A CA  
1765 C C   . GLN A 229 ? 0.5981 1.2146 0.7469 0.0353  0.0202  -0.0038 525 GLN A C   
1766 O O   . GLN A 229 ? 0.6703 1.2083 0.8158 0.0349  0.0103  -0.0086 525 GLN A O   
1767 C CB  . GLN A 229 ? 0.4325 1.1781 0.6243 0.0355  0.0211  0.0065  525 GLN A CB  
1768 C CG  . GLN A 229 ? 0.5258 1.2500 0.7044 0.0984  0.0234  -0.0058 525 GLN A CG  
1769 C CD  . GLN A 229 ? 0.6749 1.4271 0.8661 0.1268  0.0198  -0.0061 525 GLN A CD  
1770 O OE1 . GLN A 229 ? 0.7004 1.4935 0.9154 0.0979  0.0151  0.0025  525 GLN A OE1 
1771 N NE2 . GLN A 229 ? 0.7302 1.4523 0.8977 0.1835  0.0212  -0.0160 525 GLN A NE2 
1772 N N   . ALA A 230 ? 0.5282 1.1599 0.6593 0.0570  0.0288  -0.0088 526 ALA A N   
1773 C CA  . ALA A 230 ? 0.5857 1.1366 0.6894 0.0802  0.0257  -0.0210 526 ALA A CA  
1774 C C   . ALA A 230 ? 0.6409 1.2046 0.7256 0.1352  0.0329  -0.0320 526 ALA A C   
1775 O O   . ALA A 230 ? 0.6913 1.3386 0.7778 0.1551  0.0445  -0.0297 526 ALA A O   
1776 C CB  . ALA A 230 ? 0.6783 1.2121 0.7638 0.0569  0.0276  -0.0187 526 ALA A CB  
1777 N N   . ASN A 231 ? 0.7101 1.1893 0.7709 0.1592  0.0259  -0.0437 527 ASN A N   
1778 C CA  . ASN A 231 ? 0.8017 1.2575 0.8245 0.2130  0.0305  -0.0559 527 ASN A CA  
1779 C C   . ASN A 231 ? 0.8167 1.3556 0.8495 0.2509  0.0386  -0.0525 527 ASN A C   
1780 O O   . ASN A 231 ? 0.8594 1.4341 0.8673 0.2964  0.0486  -0.0579 527 ASN A O   
1781 C CB  . ASN A 231 ? 0.8695 1.3128 0.8584 0.2263  0.0370  -0.0635 527 ASN A CB  
1782 C CG  . ASN A 231 ? 0.9302 1.2986 0.8611 0.2737  0.0370  -0.0793 527 ASN A CG  
1783 O OD1 . ASN A 231 ? 0.9422 1.2319 0.8521 0.2790  0.0280  -0.0856 527 ASN A OD1 
1784 N ND2 . ASN A 231 ? 0.9640 1.3520 0.8620 0.3071  0.0473  -0.0859 527 ASN A ND2 
1785 N N   . GLY A 232 ? 0.8636 1.4378 0.9313 0.2345  0.0340  -0.0436 528 GLY A N   
1786 C CA  . GLY A 232 ? 0.8855 1.5480 0.9671 0.2677  0.0393  -0.0393 528 GLY A CA  
1787 C C   . GLY A 232 ? 0.9024 1.7002 1.0116 0.2602  0.0508  -0.0300 528 GLY A C   
1788 O O   . GLY A 232 ? 0.9390 1.8313 1.0640 0.2875  0.0552  -0.0258 528 GLY A O   
1789 N N   . ASN A 233 ? 0.8981 1.7132 1.0115 0.2233  0.0558  -0.0259 529 ASN A N   
1790 C CA  . ASN A 233 ? 0.8420 1.7870 0.9767 0.2086  0.0678  -0.0161 529 ASN A CA  
1791 C C   . ASN A 233 ? 0.8098 1.8261 0.9845 0.1562  0.0639  -0.0017 529 ASN A C   
1792 O O   . ASN A 233 ? 0.8530 1.8039 1.0366 0.1228  0.0520  0.0012  529 ASN A O   
1793 C CB  . ASN A 233 ? 0.8133 1.7434 0.9325 0.1801  0.0738  -0.0150 529 ASN A CB  
1794 C CG  . ASN A 233 ? 0.7886 1.7053 0.8700 0.2342  0.0831  -0.0272 529 ASN A CG  
1795 O OD1 . ASN A 233 ? 0.8430 1.8610 0.9241 0.2558  0.0970  -0.0254 529 ASN A OD1 
1796 N ND2 . ASN A 233 ? 0.7221 1.5160 0.7678 0.2552  0.0754  -0.0401 529 ASN A ND2 
1797 N N   . ASP A 234 ? 0.8188 1.9692 1.0122 0.1467  0.0736  0.0072  530 ASP A N   
1798 C CA  . ASP A 234 ? 0.8375 2.0327 1.0487 0.0866  0.0661  0.0210  530 ASP A CA  
1799 C C   . ASP A 234 ? 0.7735 1.9212 0.9890 0.0179  0.0641  0.0283  530 ASP A C   
1800 O O   . ASP A 234 ? 0.8576 1.9699 1.0507 0.0038  0.0693  0.0283  530 ASP A O   
1801 C CB  . ASP A 234 ? 0.9280 2.2279 1.1300 0.0776  0.0693  0.0290  530 ASP A CB  
1802 C CG  . ASP A 234 ? 1.0046 2.3505 1.1935 0.1482  0.0696  0.0230  530 ASP A CG  
1803 O OD1 . ASP A 234 ? 1.0606 2.4781 1.2352 0.1667  0.0753  0.0242  530 ASP A OD1 
1804 O OD2 . ASP A 234 ? 1.0462 2.3536 1.2346 0.1861  0.0634  0.0174  530 ASP A OD2 
1805 N N   . PRO A 235 ? 0.6407 1.7522 0.8654 -0.0240 0.0525  0.0344  531 PRO A N   
1806 C CA  . PRO A 235 ? 0.6116 1.6226 0.8144 -0.0786 0.0448  0.0394  531 PRO A CA  
1807 C C   . PRO A 235 ? 0.5611 1.6245 0.7498 -0.1411 0.0513  0.0527  531 PRO A C   
1808 O O   . PRO A 235 ? 0.6325 1.7902 0.8222 -0.1544 0.0552  0.0589  531 PRO A O   
1809 C CB  . PRO A 235 ? 0.6129 1.5828 0.8264 -0.0967 0.0316  0.0412  531 PRO A CB  
1810 C CG  . PRO A 235 ? 0.6208 1.7053 0.8588 -0.0854 0.0337  0.0444  531 PRO A CG  
1811 C CD  . PRO A 235 ? 0.6159 1.7526 0.8543 -0.0205 0.0435  0.0364  531 PRO A CD  
1812 N N   . GLU A 236 ? 0.6707 1.6334 0.8249 -0.1756 0.0469  0.0559  532 GLU A N   
1813 C CA  . GLU A 236 ? 0.7512 1.7299 0.8745 -0.2350 0.0527  0.0687  532 GLU A CA  
1814 C C   . GLU A 236 ? 0.7663 1.6397 0.8530 -0.2880 0.0404  0.0762  532 GLU A C   
1815 O O   . GLU A 236 ? 0.7380 1.5092 0.8195 -0.2686 0.0292  0.0694  532 GLU A O   
1816 C CB  . GLU A 236 ? 0.8583 1.8087 0.9578 -0.2174 0.0609  0.0656  532 GLU A CB  
1817 C CG  . GLU A 236 ? 0.8679 1.8566 0.9886 -0.1463 0.0686  0.0522  532 GLU A CG  
1818 C CD  . GLU A 236 ? 0.8921 1.8153 0.9828 -0.1285 0.0719  0.0465  532 GLU A CD  
1819 O OE1 . GLU A 236 ? 0.9230 1.8258 0.9816 -0.1719 0.0746  0.0563  532 GLU A OE1 
1820 O OE2 . GLU A 236 ? 0.8722 1.7583 0.9652 -0.0731 0.0709  0.0325  532 GLU A OE2 
1821 N N   . LEU A 237 ? 0.8184 1.7153 0.8733 -0.3553 0.0430  0.0902  533 LEU A N   
1822 C CA  . LEU A 237 ? 0.8177 1.6118 0.8239 -0.4083 0.0316  0.0981  533 LEU A CA  
1823 C C   . LEU A 237 ? 0.9143 1.5889 0.8620 -0.4174 0.0294  0.1010  533 LEU A C   
1824 O O   . LEU A 237 ? 0.9370 1.6365 0.8687 -0.4218 0.0395  0.1047  533 LEU A O   
1825 C CB  . LEU A 237 ? 0.8084 1.6408 0.7827 -0.4637 0.0271  0.1065  533 LEU A CB  
1826 C CG  . LEU A 237 ? 0.7665 1.6731 0.7743 -0.4496 0.0208  0.1019  533 LEU A CG  
1827 C CD1 . LEU A 237 ? 0.8126 1.7791 0.7869 -0.4967 0.0172  0.1085  533 LEU A CD1 
1828 C CD2 . LEU A 237 ? 0.6734 1.4995 0.6802 -0.4508 0.0092  0.0993  533 LEU A CD2 
1829 N N   . PHE A 238 ? 0.9897 1.5371 0.9033 -0.4168 0.0163  0.0993  534 PHE A N   
1830 C CA  . PHE A 238 ? 1.0749 1.5030 0.9237 -0.4242 0.0119  0.1033  534 PHE A CA  
1831 C C   . PHE A 238 ? 1.1373 1.4531 0.9279 -0.4565 -0.0009 0.1088  534 PHE A C   
1832 O O   . PHE A 238 ? 1.1125 1.4137 0.9264 -0.4423 -0.0091 0.1027  534 PHE A O   
1833 C CB  . PHE A 238 ? 0.9554 1.3350 0.8229 -0.3588 0.0087  0.0907  534 PHE A CB  
1834 C CG  . PHE A 238 ? 0.8695 1.3421 0.7916 -0.3166 0.0192  0.0815  534 PHE A CG  
1835 C CD1 . PHE A 238 ? 0.8019 1.3386 0.7840 -0.2797 0.0199  0.0713  534 PHE A CD1 
1836 C CD2 . PHE A 238 ? 0.8844 1.3706 0.7895 -0.3105 0.0279  0.0828  534 PHE A CD2 
1837 C CE1 . PHE A 238 ? 0.7627 1.3691 0.7807 -0.2362 0.0290  0.0622  534 PHE A CE1 
1838 C CE2 . PHE A 238 ? 0.8300 1.3918 0.7757 -0.2684 0.0373  0.0732  534 PHE A CE2 
1839 C CZ  . PHE A 238 ? 0.7881 1.4065 0.7869 -0.2303 0.0379  0.0628  534 PHE A CZ  
1840 N N   . GLN A 239 ? 1.2702 1.4996 0.9777 -0.4976 -0.0026 0.1202  535 GLN A N   
1841 C CA  . GLN A 239 ? 1.2950 1.3992 0.9245 -0.5292 -0.0144 0.1263  535 GLN A CA  
1842 C C   . GLN A 239 ? 1.2701 1.2498 0.8607 -0.4803 -0.0239 0.1212  535 GLN A C   
1843 O O   . GLN A 239 ? 1.3087 1.2496 0.8635 -0.4699 -0.0216 0.1246  535 GLN A O   
1844 C CB  . GLN A 239 ? 1.3998 1.4726 0.9441 -0.6086 -0.0112 0.1431  535 GLN A CB  
1845 C CG  . GLN A 239 ? 1.5920 1.5107 1.0387 -0.6285 -0.0262 0.1447  535 GLN A CG  
1846 C CD  . GLN A 239 ? 1.7705 1.6021 1.1193 -0.6613 -0.0299 0.1498  535 GLN A CD  
1847 O OE1 . GLN A 239 ? 1.8984 1.5834 1.1604 -0.6520 -0.0393 0.1512  535 GLN A OE1 
1848 N NE2 . GLN A 239 ? 1.7888 1.7103 1.1489 -0.6965 -0.0230 0.1515  535 GLN A NE2 
1849 N N   . ILE A 240 ? 1.1627 1.0858 0.7583 -0.4503 -0.0346 0.1133  536 ILE A N   
1850 C CA  . ILE A 240 ? 1.2159 1.0295 0.7719 -0.4033 -0.0445 0.1088  536 ILE A CA  
1851 C C   . ILE A 240 ? 1.3825 1.0699 0.8191 -0.4374 -0.0490 0.1218  536 ILE A C   
1852 O O   . ILE A 240 ? 1.4255 1.0583 0.7995 -0.4885 -0.0524 0.1297  536 ILE A O   
1853 C CB  . ILE A 240 ? 1.2017 0.9859 0.7806 -0.3707 -0.0538 0.0992  536 ILE A CB  
1854 C CG1 . ILE A 240 ? 1.1598 1.0606 0.8455 -0.3452 -0.0493 0.0881  536 ILE A CG1 
1855 C CG2 . ILE A 240 ? 1.1594 0.8528 0.7039 -0.3165 -0.0631 0.0941  536 ILE A CG2 
1856 C CD1 . ILE A 240 ? 1.2003 1.1484 0.9088 -0.3796 -0.0493 0.0893  536 ILE A CD1 
1857 N N   . PRO A 241 ? 1.3673 1.0003 0.7623 -0.4121 -0.0500 0.1244  537 PRO A N   
1858 C CA  . PRO A 241 ? 1.5146 1.0131 0.7833 -0.4392 -0.0550 0.1374  537 PRO A CA  
1859 C C   . PRO A 241 ? 1.6414 1.0202 0.8374 -0.4367 -0.0670 0.1375  537 PRO A C   
1860 O O   . PRO A 241 ? 1.6077 0.9693 0.8316 -0.3787 -0.0747 0.1265  537 PRO A O   
1861 C CB  . PRO A 241 ? 1.5465 1.0139 0.8023 -0.3852 -0.0574 0.1354  537 PRO A CB  
1862 C CG  . PRO A 241 ? 1.3995 1.0071 0.7742 -0.3558 -0.0492 0.1242  537 PRO A CG  
1863 C CD  . PRO A 241 ? 1.3781 1.0571 0.8324 -0.3519 -0.0490 0.1144  537 PRO A CD  
1864 N N   . PRO A 242 ? 1.7448 1.0447 0.8472 -0.5020 -0.0685 0.1491  538 PRO A N   
1865 C CA  . PRO A 242 ? 1.7428 0.9515 0.7930 -0.4960 -0.0804 0.1405  538 PRO A CA  
1866 C C   . PRO A 242 ? 1.8534 0.9326 0.8318 -0.4303 -0.0911 0.1377  538 PRO A C   
1867 O O   . PRO A 242 ? 1.9735 1.0032 0.9377 -0.4022 -0.0989 0.1299  538 PRO A O   
1868 C CB  . PRO A 242 ? 1.7889 0.9687 0.7712 -0.5593 -0.0836 0.1364  538 PRO A CB  
1869 C CG  . PRO A 242 ? 1.7658 1.0788 0.8123 -0.6047 -0.0715 0.1426  538 PRO A CG  
1870 C CD  . PRO A 242 ? 1.7438 1.0827 0.8259 -0.5643 -0.0629 0.1511  538 PRO A CD  
1871 N N   . GLU A 243 ? 1.8059 0.8391 0.7426 -0.3994 -0.0916 0.1426  539 GLU A N   
1872 C CA  . GLU A 243 ? 1.7912 0.7301 0.6756 -0.3239 -0.1020 0.1385  539 GLU A CA  
1873 C C   . GLU A 243 ? 1.6998 0.7243 0.6881 -0.2593 -0.1041 0.1273  539 GLU A C   
1874 O O   . GLU A 243 ? 1.7188 0.6839 0.6749 -0.1954 -0.1133 0.1217  539 GLU A O   
1875 C CB  . GLU A 243 ? 1.9786 0.8778 0.8141 -0.3017 -0.1023 0.1433  539 GLU A CB  
1876 C CG  . GLU A 243 ? 1.8660 0.8848 0.7903 -0.2915 -0.0942 0.1475  539 GLU A CG  
1877 C CD  . GLU A 243 ? 1.8960 0.9644 0.8212 -0.3636 -0.0819 0.1585  539 GLU A CD  
1878 O OE1 . GLU A 243 ? 1.8923 0.9875 0.8244 -0.4264 -0.0769 0.1587  539 GLU A OE1 
1879 O OE2 . GLU A 243 ? 1.7910 0.8887 0.7223 -0.3535 -0.0775 0.1620  539 GLU A OE2 
1880 N N   . LEU A 244 ? 1.5248 0.6980 0.6423 -0.2707 -0.0956 0.1197  540 LEU A N   
1881 C CA  . LEU A 244 ? 1.4669 0.7297 0.6896 -0.2160 -0.0969 0.1048  540 LEU A CA  
1882 C C   . LEU A 244 ? 1.4137 0.6857 0.6637 -0.2236 -0.0988 0.0984  540 LEU A C   
1883 O O   . LEU A 244 ? 1.3486 0.6745 0.6681 -0.1776 -0.1009 0.0869  540 LEU A O   
1884 C CB  . LEU A 244 ? 1.4146 0.8203 0.7531 -0.2170 -0.0874 0.0989  540 LEU A CB  
1885 C CG  . LEU A 244 ? 1.4639 0.8841 0.7996 -0.1956 -0.0859 0.1008  540 LEU A CG  
1886 C CD1 . LEU A 244 ? 1.2494 0.8038 0.7006 -0.1842 -0.0783 0.0908  540 LEU A CD1 
1887 C CD2 . LEU A 244 ? 1.5719 0.9182 0.8549 -0.1338 -0.0973 0.0987  540 LEU A CD2 
1888 N N   . VAL A 245 ? 1.4831 0.7059 0.6778 -0.2829 -0.0984 0.1058  541 VAL A N   
1889 C CA  . VAL A 245 ? 1.5533 0.7864 0.7705 -0.2964 -0.1006 0.1002  541 VAL A CA  
1890 C C   . VAL A 245 ? 1.6204 0.6977 0.7147 -0.2827 -0.1109 0.1022  541 VAL A C   
1891 O O   . VAL A 245 ? 1.7151 0.6959 0.7075 -0.3321 -0.1136 0.1100  541 VAL A O   
1892 C CB  . VAL A 245 ? 1.5812 0.8792 0.8244 -0.3719 -0.0941 0.1058  541 VAL A CB  
1893 C CG1 . VAL A 245 ? 1.5860 0.9004 0.8558 -0.3822 -0.0977 0.0995  541 VAL A CG1 
1894 C CG2 . VAL A 245 ? 1.4535 0.8964 0.8033 -0.3759 -0.0835 0.1041  541 VAL A CG2 
1895 N N   . LEU A 246 ? 1.6285 0.6885 0.7330 -0.2130 -0.1165 0.0927  542 LEU A N   
1896 C CA  . LEU A 246 ? 1.7128 0.6305 0.7025 -0.1858 -0.1259 0.0926  542 LEU A CA  
1897 C C   . LEU A 246 ? 1.7571 0.6544 0.7354 -0.2232 -0.1275 0.0895  542 LEU A C   
1898 O O   . LEU A 246 ? 1.6206 0.6283 0.7041 -0.2290 -0.1235 0.0824  542 LEU A O   
1899 C CB  . LEU A 246 ? 1.7465 0.6754 0.7589 -0.0965 -0.1303 0.0829  542 LEU A CB  
1900 C CG  . LEU A 246 ? 1.8437 0.6560 0.7594 -0.0466 -0.1387 0.0786  542 LEU A CG  
1901 C CD1 . LEU A 246 ? 2.0060 0.7064 0.8003 -0.0463 -0.1412 0.0730  542 LEU A CD1 
1902 C CD2 . LEU A 246 ? 1.7900 0.6705 0.7658 0.0375  -0.1407 0.0689  542 LEU A CD2 
1903 N N   . GLU A 247 ? 1.8622 0.6677 0.7399 -0.2395 -0.1320 0.0822  543 GLU A N   
1904 C CA  . GLU A 247 ? 1.8693 0.6660 0.7302 -0.2746 -0.1344 0.0759  543 GLU A CA  
1905 C C   . GLU A 247 ? 1.9386 0.6179 0.6924 -0.2317 -0.1416 0.0649  543 GLU A C   
1906 O O   . GLU A 247 ? 2.0624 0.6523 0.7258 -0.2040 -0.1448 0.0615  543 GLU A O   
1907 C CB  . GLU A 247 ? 1.9148 0.7345 0.7554 -0.3593 -0.1328 0.0803  543 GLU A CB  
1908 C CG  . GLU A 247 ? 1.8205 0.7844 0.7816 -0.4019 -0.1245 0.0879  543 GLU A CG  
1909 C CD  . GLU A 247 ? 1.9525 0.9571 0.8960 -0.4769 -0.1222 0.0927  543 GLU A CD  
1910 O OE1 . GLU A 247 ? 2.0709 1.0187 0.9433 -0.4925 -0.1230 0.0953  543 GLU A OE1 
1911 O OE2 . GLU A 247 ? 1.8735 0.9706 0.8727 -0.5181 -0.1201 0.0934  543 GLU A OE2 
1912 N N   . VAL A 248 ? 1.9141 0.5966 0.6777 -0.2249 -0.1437 0.0587  544 VAL A N   
1913 C CA  . VAL A 248 ? 1.9981 0.5822 0.6670 -0.1830 -0.1494 0.0481  544 VAL A CA  
1914 C C   . VAL A 248 ? 2.1233 0.6604 0.7195 -0.2461 -0.1536 0.0472  544 VAL A C   
1915 O O   . VAL A 248 ? 2.0060 0.6163 0.6670 -0.2877 -0.1522 0.0503  544 VAL A O   
1916 C CB  . VAL A 248 ? 1.9571 0.5836 0.6898 -0.1222 -0.1483 0.0422  544 VAL A CB  
1917 C CG1 . VAL A 248 ? 2.1735 0.7030 0.8029 -0.0770 -0.1529 0.0312  544 VAL A CG1 
1918 C CG2 . VAL A 248 ? 1.8247 0.5140 0.6351 -0.0637 -0.1452 0.0445  544 VAL A CG2 
1919 N N   . PRO A 249 ? 2.3160 0.7342 0.7758 -0.2560 -0.1594 0.0433  545 PRO A N   
1920 C CA  . PRO A 249 ? 2.4432 0.8057 0.8195 -0.3087 -0.1652 0.0425  545 PRO A CA  
1921 C C   . PRO A 249 ? 2.3955 0.7238 0.7492 -0.2646 -0.1677 0.0354  545 PRO A C   
1922 O O   . PRO A 249 ? 2.4006 0.6731 0.7135 -0.1904 -0.1682 0.0274  545 PRO A O   
1923 C CB  . PRO A 249 ? 2.6087 0.8412 0.8354 -0.3237 -0.1710 0.0395  545 PRO A CB  
1924 C CG  . PRO A 249 ? 2.5398 0.7389 0.7577 -0.2509 -0.1689 0.0346  545 PRO A CG  
1925 C CD  . PRO A 249 ? 2.3875 0.7208 0.7621 -0.2295 -0.1612 0.0407  545 PRO A CD  
1926 N N   . ILE A 250 ? 2.4168 0.7871 0.7995 -0.3084 -0.1688 0.0385  546 ILE A N   
1927 C CA  . ILE A 250 ? 2.3554 0.7103 0.7342 -0.2720 -0.1702 0.0330  546 ILE A CA  
1928 C C   . ILE A 250 ? 2.5668 0.7835 0.7837 -0.2818 -0.1781 0.0300  546 ILE A C   
1929 O O   . ILE A 250 ? 2.6512 0.8453 0.8136 -0.3527 -0.1826 0.0358  546 ILE A O   
1930 C CB  . ILE A 250 ? 2.2548 0.7249 0.7477 -0.3102 -0.1674 0.0373  546 ILE A CB  
1931 C CG1 . ILE A 250 ? 2.0928 0.6932 0.7327 -0.3100 -0.1600 0.0410  546 ILE A CG1 
1932 C CG2 . ILE A 250 ? 2.1922 0.6499 0.6894 -0.2659 -0.1681 0.0307  546 ILE A CG2 
1933 C CD1 . ILE A 250 ? 2.0576 0.6700 0.7461 -0.2308 -0.1561 0.0355  546 ILE A CD1 
1934 N N   . ARG A 251 ? 2.6603 0.7875 0.7964 -0.2097 -0.1799 0.0214  547 ARG A N   
1935 C CA  . ARG A 251 ? 2.8076 0.8046 0.7988 -0.2063 -0.1859 0.0188  547 ARG A CA  
1936 C C   . ARG A 251 ? 2.7894 0.7800 0.7849 -0.1407 -0.1846 0.0127  547 ARG A C   
1937 O O   . ARG A 251 ? 2.6363 0.6969 0.7141 -0.0809 -0.1799 0.0077  547 ARG A O   
1938 C CB  . ARG A 251 ? 2.9449 0.8297 0.8255 -0.1796 -0.1872 0.0151  547 ARG A CB  
1939 C CG  . ARG A 251 ? 2.9347 0.8156 0.8232 -0.0843 -0.1835 0.0066  547 ARG A CG  
1940 C CD  . ARG A 251 ? 2.8551 0.8096 0.8209 -0.0831 -0.1804 0.0071  547 ARG A CD  
1941 N NE  . ARG A 251 ? 2.8104 0.7527 0.7668 0.0050  -0.1775 -0.0007 547 ARG A NE  
1942 C CZ  . ARG A 251 ? 2.7714 0.7849 0.8086 0.0271  -0.1734 -0.0001 547 ARG A CZ  
1943 N NH1 . ARG A 251 ? 2.8504 0.8549 0.8706 0.1088  -0.1713 -0.0073 547 ARG A NH1 
1944 N NH2 . ARG A 251 ? 2.5869 0.6895 0.7287 -0.0317 -0.1704 0.0094  547 ARG A NH2 
1945 N N   . HIS A 252 ? 2.8984 0.8100 0.8099 -0.1538 -0.1882 0.0136  548 HIS A N   
1946 C CA  . HIS A 252 ? 2.8978 0.7991 0.8057 -0.0885 -0.1867 0.0078  548 HIS A CA  
1947 C C   . HIS A 252 ? 3.0411 0.8367 0.8418 -0.0165 -0.1867 0.0012  548 HIS A C   
1948 O O   . HIS A 252 ? 3.0938 0.7922 0.7931 -0.0341 -0.1901 0.0023  548 HIS A O   
1949 C CB  . HIS A 252 ? 2.8547 0.7356 0.7370 -0.1334 -0.1903 0.0122  548 HIS A CB  
1950 C CG  . HIS A 252 ? 2.9320 0.8502 0.8583 -0.0810 -0.1877 0.0076  548 HIS A CG  
1951 N ND1 . HIS A 252 ? 2.9808 0.8187 0.8257 -0.0218 -0.1879 0.0026  548 HIS A ND1 
1952 C CD2 . HIS A 252 ? 2.7477 0.7745 0.7875 -0.0792 -0.1850 0.0075  548 HIS A CD2 
1953 C CE1 . HIS A 252 ? 2.8630 0.7634 0.7730 0.0139  -0.1847 -0.0006 548 HIS A CE1 
1954 N NE2 . HIS A 252 ? 2.7316 0.7434 0.7583 -0.0206 -0.1831 0.0021  548 HIS A NE2 
1955 N N   . PRO A 253 ? 2.9684 0.7847 0.7875 0.0664  -0.1828 -0.0057 549 PRO A N   
1956 C CA  . PRO A 253 ? 3.1495 0.8733 0.8644 0.1391  -0.1827 -0.0114 549 PRO A CA  
1957 C C   . PRO A 253 ? 3.3504 0.9610 0.9482 0.1343  -0.1873 -0.0103 549 PRO A C   
1958 O O   . PRO A 253 ? 3.4772 1.0150 0.9889 0.2014  -0.1873 -0.0150 549 PRO A O   
1959 C CB  . PRO A 253 ? 2.9682 0.7871 0.7653 0.2260  -0.1760 -0.0183 549 PRO A CB  
1960 C CG  . PRO A 253 ? 2.8151 0.7384 0.7264 0.1969  -0.1740 -0.0163 549 PRO A CG  
1961 C CD  . PRO A 253 ? 2.7755 0.7146 0.7190 0.1014  -0.1776 -0.0087 549 PRO A CD  
1962 N N   . LYS A 254 ? 3.3803 0.9765 0.9707 0.0579  -0.1915 -0.0040 550 LYS A N   
1963 C CA  . LYS A 254 ? 3.5293 1.0127 1.0032 0.0445  -0.1968 -0.0021 550 LYS A CA  
1964 C C   . LYS A 254 ? 3.5788 1.0054 0.9945 -0.0560 -0.2033 0.0059  550 LYS A C   
1965 O O   . LYS A 254 ? 3.8031 1.0981 1.0814 -0.0712 -0.2089 0.0072  550 LYS A O   
1966 C CB  . LYS A 254 ? 3.5188 1.0514 1.0432 0.0635  -0.1950 -0.0030 550 LYS A CB  
1967 C CG  . LYS A 254 ? 3.5240 1.1096 1.0923 0.1635  -0.1886 -0.0107 550 LYS A CG  
1968 C CD  . LYS A 254 ? 3.7604 1.2312 1.1983 0.2288  -0.1902 -0.0143 550 LYS A CD  
1969 C CE  . LYS A 254 ? 3.7125 1.2509 1.1970 0.3237  -0.1836 -0.0208 550 LYS A CE  
1970 N NZ  . LYS A 254 ? 3.6098 1.2243 1.1526 0.3834  -0.1780 -0.0258 550 LYS A NZ  
1971 N N   . PHE A 255 ? 3.3527 0.8800 0.8688 -0.1247 -0.2027 0.0114  551 PHE A N   
1972 C CA  . PHE A 255 ? 3.4215 0.9293 0.9042 -0.2239 -0.2082 0.0200  551 PHE A CA  
1973 C C   . PHE A 255 ? 3.4686 0.9682 0.9331 -0.2716 -0.2093 0.0233  551 PHE A C   
1974 O O   . PHE A 255 ? 3.2821 0.8915 0.8518 -0.3041 -0.2063 0.0263  551 PHE A O   
1975 C CB  . PHE A 255 ? 3.3450 0.9763 0.9465 -0.2685 -0.2069 0.0248  551 PHE A CB  
1976 C CG  . PHE A 255 ? 3.3702 1.0098 0.9899 -0.2247 -0.2059 0.0215  551 PHE A CG  
1977 C CD1 . PHE A 255 ? 3.2991 1.0182 1.0123 -0.1540 -0.1998 0.0151  551 PHE A CD1 
1978 C CD2 . PHE A 255 ? 3.4524 1.0211 0.9938 -0.2560 -0.2111 0.0249  551 PHE A CD2 
1979 C CE1 . PHE A 255 ? 3.2202 0.9500 0.9495 -0.1144 -0.1985 0.0119  551 PHE A CE1 
1980 C CE2 . PHE A 255 ? 3.3995 0.9754 0.9571 -0.2156 -0.2100 0.0218  551 PHE A CE2 
1981 C CZ  . PHE A 255 ? 3.2536 0.9108 0.9055 -0.1445 -0.2035 0.0152  551 PHE A CZ  
1982 N N   . ASP A 256 ? 3.6827 1.0471 1.0067 -0.2777 -0.2139 0.0229  552 ASP A N   
1983 C CA  . ASP A 256 ? 3.8128 1.1549 1.1038 -0.3227 -0.2153 0.0255  552 ASP A CA  
1984 C C   . ASP A 256 ? 3.7506 1.1514 1.0716 -0.4294 -0.2179 0.0349  552 ASP A C   
1985 O O   . ASP A 256 ? 3.8441 1.2404 1.1454 -0.4742 -0.2187 0.0378  552 ASP A O   
1986 C CB  . ASP A 256 ? 4.1246 1.2970 1.2456 -0.3037 -0.2202 0.0227  552 ASP A CB  
1987 C CG  . ASP A 256 ? 4.2041 1.3435 1.3086 -0.2043 -0.2165 0.0140  552 ASP A CG  
1988 O OD1 . ASP A 256 ? 4.2425 1.3385 1.3100 -0.1319 -0.2159 0.0088  552 ASP A OD1 
1989 O OD2 . ASP A 256 ? 4.1927 1.3554 1.3228 -0.1981 -0.2142 0.0125  552 ASP A OD2 
1990 N N   . TRP A 257 ? 3.5730 1.0315 0.9383 -0.4710 -0.2191 0.0400  553 TRP A N   
1991 C CA  . TRP A 257 ? 3.5221 1.0785 0.9489 -0.5634 -0.2198 0.0490  553 TRP A CA  
1992 C C   . TRP A 257 ? 3.3413 1.0615 0.9327 -0.5573 -0.2133 0.0498  553 TRP A C   
1993 O O   . TRP A 257 ? 3.2400 1.0601 0.8955 -0.6265 -0.2127 0.0572  553 TRP A O   
1994 C CB  . TRP A 257 ? 3.5414 1.0975 0.9459 -0.6136 -0.2240 0.0547  553 TRP A CB  
1995 C CG  . TRP A 257 ? 3.4668 1.0462 0.9213 -0.5547 -0.2220 0.0505  553 TRP A CG  
1996 C CD1 . TRP A 257 ? 3.6130 1.0808 0.9783 -0.5011 -0.2243 0.0455  553 TRP A CD1 
1997 C CD2 . TRP A 257 ? 3.3032 1.0253 0.9049 -0.5421 -0.2172 0.0509  553 TRP A CD2 
1998 N NE1 . TRP A 257 ? 3.4905 1.0262 0.9408 -0.4573 -0.2211 0.0426  553 TRP A NE1 
1999 C CE2 . TRP A 257 ? 3.3245 1.0129 0.9185 -0.4826 -0.2169 0.0457  553 TRP A CE2 
2000 C CE3 . TRP A 257 ? 3.1533 1.0266 0.8883 -0.5749 -0.2132 0.0553  553 TRP A CE3 
2001 C CZ2 . TRP A 257 ? 3.1634 0.9602 0.8763 -0.4574 -0.2131 0.0444  553 TRP A CZ2 
2002 C CZ3 . TRP A 257 ? 3.0101 0.9876 0.8603 -0.5490 -0.2097 0.0543  553 TRP A CZ3 
2003 C CH2 . TRP A 257 ? 2.9967 0.9337 0.8346 -0.4920 -0.2098 0.0487  553 TRP A CH2 
2004 N N   . PHE A 258 ? 3.3091 1.0600 0.9661 -0.4757 -0.2085 0.0426  554 PHE A N   
2005 C CA  . PHE A 258 ? 3.2088 1.1045 1.0139 -0.4669 -0.2028 0.0431  554 PHE A CA  
2006 C C   . PHE A 258 ? 3.1248 1.0617 0.9546 -0.5034 -0.2012 0.0463  554 PHE A C   
2007 O O   . PHE A 258 ? 2.9649 1.0282 0.8998 -0.5425 -0.1983 0.0517  554 PHE A O   
2008 C CB  . PHE A 258 ? 3.1543 1.0611 1.0072 -0.3712 -0.1985 0.0343  554 PHE A CB  
2009 C CG  . PHE A 258 ? 2.9302 0.9608 0.9122 -0.3608 -0.1951 0.0347  554 PHE A CG  
2010 C CD1 . PHE A 258 ? 2.9713 1.0017 0.9567 -0.3516 -0.1964 0.0342  554 PHE A CD1 
2011 C CD2 . PHE A 258 ? 2.7334 0.8811 0.8370 -0.3618 -0.1904 0.0358  554 PHE A CD2 
2012 C CE1 . PHE A 258 ? 2.7824 0.9265 0.8910 -0.3427 -0.1929 0.0339  554 PHE A CE1 
2013 C CE2 . PHE A 258 ? 2.6367 0.9081 0.8854 -0.3506 -0.1847 0.0350  554 PHE A CE2 
2014 C CZ  . PHE A 258 ? 2.6288 0.8979 0.8793 -0.3413 -0.1862 0.0333  554 PHE A CZ  
2015 N N   . LYS A 259 ? 3.0899 0.9216 0.8214 -0.4899 -0.2028 0.0431  555 LYS A N   
2016 C CA  . LYS A 259 ? 3.2312 1.0938 0.9786 -0.5235 -0.2013 0.0457  555 LYS A CA  
2017 C C   . LYS A 259 ? 3.2540 1.1813 1.0150 -0.6229 -0.2031 0.0555  555 LYS A C   
2018 O O   . LYS A 259 ? 3.0066 1.0384 0.8490 -0.6564 -0.1997 0.0597  555 LYS A O   
2019 C CB  . LYS A 259 ? 3.3046 1.0274 0.9255 -0.4969 -0.2038 0.0409  555 LYS A CB  
2020 C CG  . LYS A 259 ? 3.5025 1.0809 0.9938 -0.4578 -0.2082 0.0362  555 LYS A CG  
2021 C CD  . LYS A 259 ? 3.7778 1.2137 1.1261 -0.4582 -0.2121 0.0339  555 LYS A CD  
2022 C CE  . LYS A 259 ? 3.9548 1.2668 1.2035 -0.3737 -0.2136 0.0260  555 LYS A CE  
2023 N NZ  . LYS A 259 ? 3.8639 1.2366 1.1975 -0.2812 -0.2075 0.0189  555 LYS A NZ  
2024 N N   . ASP A 260 ? 3.3932 1.2650 1.0749 -0.6700 -0.2083 0.0594  556 ASP A N   
2025 C CA  . ASP A 260 ? 3.4592 1.3946 1.1449 -0.7652 -0.2102 0.0687  556 ASP A CA  
2026 C C   . ASP A 260 ? 3.2191 1.3296 1.0530 -0.7871 -0.2058 0.0742  556 ASP A C   
2027 O O   . ASP A 260 ? 3.1777 1.3854 1.0521 -0.8552 -0.2048 0.0818  556 ASP A O   
2028 C CB  . ASP A 260 ? 3.6907 1.5229 1.2541 -0.8067 -0.2172 0.0715  556 ASP A CB  
2029 C CG  . ASP A 260 ? 3.9665 1.6213 1.3701 -0.7946 -0.2222 0.0672  556 ASP A CG  
2030 O OD1 . ASP A 260 ? 4.0524 1.6830 1.4162 -0.8236 -0.2226 0.0680  556 ASP A OD1 
2031 O OD2 . ASP A 260 ? 4.1089 1.6475 1.4241 -0.7546 -0.2257 0.0630  556 ASP A OD2 
2032 N N   . LEU A 261 ? 3.0743 1.2291 0.9873 -0.7293 -0.2030 0.0705  557 LEU A N   
2033 C CA  . LEU A 261 ? 2.8808 1.1988 0.9366 -0.7401 -0.1984 0.0749  557 LEU A CA  
2034 C C   . LEU A 261 ? 2.8624 1.2748 0.9957 -0.7505 -0.1935 0.0770  557 LEU A C   
2035 O O   . LEU A 261 ? 2.7124 1.2661 0.9468 -0.7924 -0.1890 0.0835  557 LEU A O   
2036 C CB  . LEU A 261 ? 2.7382 1.0709 0.8560 -0.6688 -0.1964 0.0691  557 LEU A CB  
2037 C CG  . LEU A 261 ? 2.7871 1.0631 0.8585 -0.6598 -0.2002 0.0679  557 LEU A CG  
2038 C CD1 . LEU A 261 ? 2.6492 0.9375 0.7852 -0.5806 -0.1971 0.0601  557 LEU A CD1 
2039 C CD2 . LEU A 261 ? 2.8157 1.1833 0.9243 -0.7310 -0.2015 0.0771  557 LEU A CD2 
2040 N N   . GLY A 262 ? 2.9484 1.2915 1.0485 -0.7083 -0.1925 0.0710  558 GLY A N   
2041 C CA  . GLY A 262 ? 2.9714 1.3893 1.1373 -0.7186 -0.1873 0.0729  558 GLY A CA  
2042 C C   . GLY A 262 ? 2.7806 1.3437 1.1225 -0.6817 -0.1776 0.0734  558 GLY A C   
2043 O O   . GLY A 262 ? 2.6776 1.3651 1.1126 -0.7148 -0.1718 0.0793  558 GLY A O   
2044 N N   . LEU A 263 ? 2.6816 1.2306 1.0656 -0.6128 -0.1758 0.0670  559 LEU A N   
2045 C CA  . LEU A 263 ? 2.3778 1.0491 0.9168 -0.5750 -0.1675 0.0662  559 LEU A CA  
2046 C C   . LEU A 263 ? 2.2776 0.9220 0.8348 -0.5165 -0.1638 0.0621  559 LEU A C   
2047 O O   . LEU A 263 ? 2.2786 0.8003 0.7319 -0.4811 -0.1678 0.0567  559 LEU A O   
2048 C CB  . LEU A 263 ? 2.2646 0.9513 0.8476 -0.5394 -0.1678 0.0616  559 LEU A CB  
2049 C CG  . LEU A 263 ? 2.2657 0.9807 0.8346 -0.5924 -0.1715 0.0660  559 LEU A CG  
2050 C CD1 . LEU A 263 ? 2.2299 0.9375 0.8265 -0.5500 -0.1724 0.0599  559 LEU A CD1 
2051 C CD2 . LEU A 263 ? 2.1080 0.9778 0.7821 -0.6455 -0.1666 0.0735  559 LEU A CD2 
2052 N N   . LYS A 264 ? 2.1274 0.8898 0.8148 -0.5058 -0.1560 0.0648  560 LYS A N   
2053 C CA  . LYS A 264 ? 2.1382 0.8963 0.8633 -0.4498 -0.1518 0.0626  560 LYS A CA  
2054 C C   . LYS A 264 ? 1.9835 0.8768 0.8588 -0.4373 -0.1445 0.0644  560 LYS A C   
2055 O O   . LYS A 264 ? 1.8222 0.8218 0.7705 -0.4808 -0.1416 0.0684  560 LYS A O   
2056 C CB  . LYS A 264 ? 2.1351 0.8644 0.8144 -0.4709 -0.1509 0.0668  560 LYS A CB  
2057 C CG  . LYS A 264 ? 2.1584 0.9999 0.8987 -0.5384 -0.1461 0.0756  560 LYS A CG  
2058 C CD  . LYS A 264 ? 2.2760 1.0964 0.9845 -0.5508 -0.1439 0.0794  560 LYS A CD  
2059 C CE  . LYS A 264 ? 2.2322 1.1419 0.9614 -0.6256 -0.1410 0.0868  560 LYS A CE  
2060 N NZ  . LYS A 264 ? 2.1251 1.0179 0.8240 -0.6410 -0.1384 0.0904  560 LYS A NZ  
2061 N N   . TRP A 265 ? 1.9287 0.8189 0.8457 -0.3756 -0.1420 0.0611  561 TRP A N   
2062 C CA  . TRP A 265 ? 1.7107 0.7166 0.7590 -0.3636 -0.1359 0.0624  561 TRP A CA  
2063 C C   . TRP A 265 ? 1.6436 0.6434 0.7097 -0.3255 -0.1327 0.0656  561 TRP A C   
2064 O O   . TRP A 265 ? 1.7605 0.6645 0.7435 -0.2885 -0.1358 0.0643  561 TRP A O   
2065 C CB  . TRP A 265 ? 1.5224 0.5460 0.6190 -0.3252 -0.1373 0.0543  561 TRP A CB  
2066 C CG  . TRP A 265 ? 1.4435 0.5981 0.6685 -0.3401 -0.1330 0.0543  561 TRP A CG  
2067 C CD1 . TRP A 265 ? 1.3946 0.6355 0.7181 -0.2891 -0.1274 0.0490  561 TRP A CD1 
2068 C CD2 . TRP A 265 ? 1.5183 0.7746 0.8003 -0.3937 -0.1311 0.0569  561 TRP A CD2 
2069 N NE1 . TRP A 265 ? 1.3552 0.7277 0.7849 -0.3091 -0.1227 0.0481  561 TRP A NE1 
2070 C CE2 . TRP A 265 ? 1.4218 0.7978 0.8246 -0.3765 -0.1263 0.0535  561 TRP A CE2 
2071 C CE3 . TRP A 265 ? 1.5095 0.7780 0.7524 -0.4469 -0.1326 0.0614  561 TRP A CE3 
2072 C CZ2 . TRP A 265 ? 1.3479 0.8406 0.8259 -0.4130 -0.1243 0.0551  561 TRP A CZ2 
2073 C CZ3 . TRP A 265 ? 1.3956 0.7907 0.7196 -0.4806 -0.1296 0.0637  561 TRP A CZ3 
2074 C CH2 . TRP A 265 ? 1.2383 0.7431 0.6781 -0.4608 -0.1255 0.0604  561 TRP A CH2 
2075 N N   . TYR A 266 ? 1.5617 0.6663 0.7325 -0.3341 -0.1269 0.0697  562 TYR A N   
2076 C CA  . TYR A 266 ? 1.5593 0.6988 0.7683 -0.2887 -0.1223 0.0699  562 TYR A CA  
2077 C C   . TYR A 266 ? 1.5616 0.7197 0.8132 -0.2090 -0.1229 0.0592  562 TYR A C   
2078 O O   . TYR A 266 ? 1.4433 0.6424 0.7434 -0.1930 -0.1230 0.0515  562 TYR A O   
2079 C CB  . TYR A 266 ? 1.4288 0.7115 0.7467 -0.3126 -0.1134 0.0720  562 TYR A CB  
2080 C CG  . TYR A 266 ? 1.3403 0.7417 0.7623 -0.3210 -0.1100 0.0661  562 TYR A CG  
2081 C CD1 . TYR A 266 ? 1.1806 0.6562 0.6920 -0.2671 -0.1072 0.0564  562 TYR A CD1 
2082 C CD2 . TYR A 266 ? 1.2089 0.6493 0.6352 -0.3843 -0.1102 0.0707  562 TYR A CD2 
2083 C CE1 . TYR A 266 ? 1.1598 0.7312 0.7549 -0.2726 -0.1044 0.0518  562 TYR A CE1 
2084 C CE2 . TYR A 266 ? 1.2235 0.7715 0.7400 -0.3857 -0.1079 0.0657  562 TYR A CE2 
2085 C CZ  . TYR A 266 ? 1.2169 0.8229 0.8139 -0.3283 -0.1050 0.0565  562 TYR A CZ  
2086 O OH  . TYR A 266 ? 1.1441 0.8455 0.8209 -0.3276 -0.1031 0.0523  562 TYR A OH  
2087 N N   . GLY A 267 ? 1.4882 0.6217 0.7208 -0.1602 -0.1235 0.0593  563 GLY A N   
2088 C CA  . GLY A 267 ? 1.4373 0.5938 0.7023 -0.0865 -0.1246 0.0499  563 GLY A CA  
2089 C C   . GLY A 267 ? 1.3689 0.6727 0.7702 -0.0695 -0.1181 0.0427  563 GLY A C   
2090 O O   . GLY A 267 ? 1.2564 0.5976 0.6978 -0.0267 -0.1181 0.0343  563 GLY A O   
2091 N N   . LEU A 268 ? 1.2554 0.6411 0.7229 -0.1031 -0.1123 0.0458  564 LEU A N   
2092 C CA  . LEU A 268 ? 1.1355 0.6406 0.7131 -0.0816 -0.1069 0.0391  564 LEU A CA  
2093 C C   . LEU A 268 ? 1.0514 0.6383 0.7069 -0.1094 -0.1023 0.0359  564 LEU A C   
2094 O O   . LEU A 268 ? 0.9550 0.5789 0.6299 -0.1537 -0.0985 0.0410  564 LEU A O   
2095 C CB  . LEU A 268 ? 1.0928 0.6320 0.6878 -0.0886 -0.1035 0.0431  564 LEU A CB  
2096 C CG  . LEU A 268 ? 1.0367 0.6700 0.7180 -0.0549 -0.1005 0.0351  564 LEU A CG  
2097 C CD1 . LEU A 268 ? 1.1992 0.8077 0.8539 0.0002  -0.1064 0.0312  564 LEU A CD1 
2098 C CD2 . LEU A 268 ? 1.0323 0.7184 0.7480 -0.0762 -0.0950 0.0378  564 LEU A CD2 
2099 N N   . PRO A 269 ? 0.9878 0.6099 0.6878 -0.0840 -0.1021 0.0282  565 PRO A N   
2100 C CA  . PRO A 269 ? 0.8363 0.5403 0.6131 -0.1031 -0.0977 0.0253  565 PRO A CA  
2101 C C   . PRO A 269 ? 0.8086 0.5988 0.6626 -0.0881 -0.0924 0.0211  565 PRO A C   
2102 O O   . PRO A 269 ? 0.8249 0.6349 0.7022 -0.0522 -0.0926 0.0151  565 PRO A O   
2103 C CB  . PRO A 269 ? 0.8932 0.5841 0.6708 -0.0799 -0.1000 0.0193  565 PRO A CB  
2104 C CG  . PRO A 269 ? 1.0063 0.6613 0.7514 -0.0316 -0.1027 0.0158  565 PRO A CG  
2105 C CD  . PRO A 269 ? 1.0589 0.6512 0.7381 -0.0344 -0.1056 0.0222  565 PRO A CD  
2106 N N   . ALA A 270 ? 0.7434 0.5870 0.6333 -0.1160 -0.0877 0.0239  566 ALA A N   
2107 C CA  . ALA A 270 ? 0.7386 0.6455 0.6822 -0.1029 -0.0828 0.0202  566 ALA A CA  
2108 C C   . ALA A 270 ? 0.6875 0.6625 0.6834 -0.1194 -0.0778 0.0197  566 ALA A C   
2109 O O   . ALA A 270 ? 0.8283 0.8268 0.8204 -0.1482 -0.0749 0.0256  566 ALA A O   
2110 C CB  . ALA A 270 ? 0.7297 0.6212 0.6440 -0.1093 -0.0817 0.0250  566 ALA A CB  
2111 N N   . VAL A 271 ? 0.6249 0.6332 0.6652 -0.1004 -0.0767 0.0131  567 VAL A N   
2112 C CA  . VAL A 271 ? 0.6076 0.6722 0.6894 -0.1070 -0.0729 0.0124  567 VAL A CA  
2113 C C   . VAL A 271 ? 0.5543 0.6615 0.6622 -0.0985 -0.0674 0.0101  567 VAL A C   
2114 O O   . VAL A 271 ? 0.6258 0.7286 0.7424 -0.0785 -0.0670 0.0042  567 VAL A O   
2115 C CB  . VAL A 271 ? 0.5164 0.5873 0.6239 -0.0903 -0.0739 0.0071  567 VAL A CB  
2116 C CG1 . VAL A 271 ? 0.5287 0.6513 0.6730 -0.0876 -0.0701 0.0059  567 VAL A CG1 
2117 C CG2 . VAL A 271 ? 0.5599 0.5938 0.6403 -0.0997 -0.0786 0.0094  567 VAL A CG2 
2118 N N   . SER A 272 ? 0.5792 0.7324 0.6981 -0.1130 -0.0632 0.0141  568 SER A N   
2119 C CA  . SER A 272 ? 0.5645 0.7564 0.6990 -0.1030 -0.0570 0.0121  568 SER A CA  
2120 C C   . SER A 272 ? 0.5322 0.7810 0.6981 -0.0893 -0.0525 0.0098  568 SER A C   
2121 O O   . SER A 272 ? 0.7170 0.9984 0.8907 -0.0765 -0.0467 0.0076  568 SER A O   
2122 C CB  . SER A 272 ? 0.6985 0.8983 0.8076 -0.1281 -0.0542 0.0196  568 SER A CB  
2123 O OG  . SER A 272 ? 0.7141 0.9324 0.8109 -0.1612 -0.0549 0.0277  568 SER A OG  
2124 N N   . ASN A 273 ? 0.5486 0.8079 0.7274 -0.0877 -0.0552 0.0102  569 ASN A N   
2125 C CA  . ASN A 273 ? 0.5592 0.8725 0.7601 -0.0705 -0.0519 0.0094  569 ASN A CA  
2126 C C   . ASN A 273 ? 0.6171 0.9045 0.8258 -0.0413 -0.0528 0.0022  569 ASN A C   
2127 O O   . ASN A 273 ? 0.6071 0.9248 0.8246 -0.0212 -0.0512 0.0015  569 ASN A O   
2128 C CB  . ASN A 273 ? 0.5800 0.9358 0.7859 -0.0917 -0.0547 0.0165  569 ASN A CB  
2129 C CG  . ASN A 273 ? 0.6614 0.9722 0.8589 -0.1026 -0.0618 0.0169  569 ASN A CG  
2130 O OD1 . ASN A 273 ? 0.5924 0.8440 0.7798 -0.0956 -0.0640 0.0127  569 ASN A OD1 
2131 N ND2 . ASN A 273 ? 0.6118 0.9571 0.8124 -0.1195 -0.0655 0.0218  569 ASN A ND2 
2132 N N   . MET A 274 ? 0.5313 0.7654 0.7326 -0.0386 -0.0554 -0.0028 570 MET A N   
2133 C CA  . MET A 274 ? 0.4945 0.7014 0.6970 -0.0207 -0.0563 -0.0086 570 MET A CA  
2134 C C   . MET A 274 ? 0.5453 0.7352 0.7381 -0.0041 -0.0532 -0.0160 570 MET A C   
2135 O O   . MET A 274 ? 0.5986 0.7981 0.7869 -0.0042 -0.0506 -0.0172 570 MET A O   
2136 C CB  . MET A 274 ? 0.5559 0.7260 0.7558 -0.0310 -0.0608 -0.0093 570 MET A CB  
2137 C CG  . MET A 274 ? 0.5614 0.7381 0.7631 -0.0434 -0.0642 -0.0035 570 MET A CG  
2138 S SD  . MET A 274 ? 0.6137 0.7507 0.8088 -0.0471 -0.0679 -0.0053 570 MET A SD  
2139 C CE  . MET A 274 ? 0.5061 0.6354 0.7074 -0.0327 -0.0662 -0.0090 570 MET A CE  
2140 N N   . LEU A 275 ? 0.5418 0.7006 0.7251 0.0077  -0.0539 -0.0209 571 LEU A N   
2141 C CA  . LEU A 275 ? 0.5571 0.6863 0.7186 0.0214  -0.0519 -0.0287 571 LEU A CA  
2142 C C   . LEU A 275 ? 0.6210 0.7115 0.7746 0.0063  -0.0555 -0.0335 571 LEU A C   
2143 O O   . LEU A 275 ? 0.6114 0.6888 0.7675 -0.0011 -0.0576 -0.0319 571 LEU A O   
2144 C CB  . LEU A 275 ? 0.6358 0.7550 0.7779 0.0483  -0.0496 -0.0299 571 LEU A CB  
2145 C CG  . LEU A 275 ? 0.7332 0.8200 0.8396 0.0704  -0.0465 -0.0377 571 LEU A CG  
2146 C CD1 . LEU A 275 ? 0.8326 0.9375 0.9241 0.1075  -0.0430 -0.0362 571 LEU A CD1 
2147 C CD2 . LEU A 275 ? 0.7647 0.7814 0.8376 0.0606  -0.0495 -0.0444 571 LEU A CD2 
2148 N N   . LEU A 276 ? 0.5479 0.6277 0.6922 0.0004  -0.0563 -0.0393 572 LEU A N   
2149 C CA  . LEU A 276 ? 0.6445 0.7026 0.7809 -0.0165 -0.0601 -0.0446 572 LEU A CA  
2150 C C   . LEU A 276 ? 0.7009 0.7115 0.7993 -0.0147 -0.0596 -0.0518 572 LEU A C   
2151 O O   . LEU A 276 ? 0.7828 0.7773 0.8580 -0.0011 -0.0575 -0.0565 572 LEU A O   
2152 C CB  . LEU A 276 ? 0.5972 0.6740 0.7406 -0.0243 -0.0627 -0.0467 572 LEU A CB  
2153 C CG  . LEU A 276 ? 0.6433 0.7159 0.7793 -0.0412 -0.0675 -0.0531 572 LEU A CG  
2154 C CD1 . LEU A 276 ? 0.5609 0.6394 0.7069 -0.0539 -0.0692 -0.0514 572 LEU A CD1 
2155 C CD2 . LEU A 276 ? 0.6582 0.7584 0.8038 -0.0413 -0.0709 -0.0529 572 LEU A CD2 
2156 N N   . GLU A 277 ? 0.7238 0.7067 0.8086 -0.0290 -0.0613 -0.0526 573 GLU A N   
2157 C CA  . GLU A 277 ? 0.8558 0.7780 0.8909 -0.0357 -0.0618 -0.0590 573 GLU A CA  
2158 C C   . GLU A 277 ? 0.8422 0.7637 0.8706 -0.0708 -0.0661 -0.0641 573 GLU A C   
2159 O O   . GLU A 277 ? 0.7052 0.6594 0.7592 -0.0889 -0.0675 -0.0608 573 GLU A O   
2160 C CB  . GLU A 277 ? 0.9679 0.8514 0.9798 -0.0290 -0.0604 -0.0552 573 GLU A CB  
2161 C CG  . GLU A 277 ? 1.0951 0.9514 1.0790 0.0085  -0.0573 -0.0546 573 GLU A CG  
2162 C CD  . GLU A 277 ? 1.2486 1.0328 1.1777 0.0140  -0.0575 -0.0542 573 GLU A CD  
2163 O OE1 . GLU A 277 ? 1.2680 0.9984 1.1574 -0.0156 -0.0597 -0.0583 573 GLU A OE1 
2164 O OE2 . GLU A 277 ? 1.3099 1.0925 1.2322 0.0463  -0.0559 -0.0494 573 GLU A OE2 
2165 N N   . ILE A 278 ? 0.8596 0.7483 0.8513 -0.0802 -0.0683 -0.0725 574 ILE A N   
2166 C CA  . ILE A 278 ? 0.8436 0.7377 0.8239 -0.1178 -0.0737 -0.0783 574 ILE A CA  
2167 C C   . ILE A 278 ? 0.9341 0.7447 0.8414 -0.1318 -0.0752 -0.0865 574 ILE A C   
2168 O O   . ILE A 278 ? 0.9934 0.7665 0.8695 -0.1095 -0.0742 -0.0917 574 ILE A O   
2169 C CB  . ILE A 278 ? 0.8069 0.7570 0.8175 -0.1184 -0.0773 -0.0810 574 ILE A CB  
2170 C CG1 . ILE A 278 ? 0.8074 0.8239 0.8747 -0.1047 -0.0766 -0.0729 574 ILE A CG1 
2171 C CG2 . ILE A 278 ? 0.8369 0.7989 0.8315 -0.1574 -0.0840 -0.0878 574 ILE A CG2 
2172 C CD1 . ILE A 278 ? 0.7489 0.8071 0.8367 -0.0959 -0.0797 -0.0737 574 ILE A CD1 
2173 N N   . GLY A 279 ? 1.0219 0.7991 0.8952 -0.1688 -0.0774 -0.0876 575 GLY A N   
2174 C CA  . GLY A 279 ? 1.1189 0.8004 0.9073 -0.1893 -0.0799 -0.0954 575 GLY A CA  
2175 C C   . GLY A 279 ? 1.1424 0.7406 0.8774 -0.1461 -0.0760 -0.0968 575 GLY A C   
2176 O O   . GLY A 279 ? 1.2176 0.7420 0.8848 -0.1441 -0.0779 -0.1057 575 GLY A O   
2177 N N   . GLY A 280 ? 1.1201 0.7312 0.8813 -0.1090 -0.0709 -0.0886 576 GLY A N   
2178 C CA  . GLY A 280 ? 1.2234 0.7746 0.9398 -0.0606 -0.0671 -0.0890 576 GLY A CA  
2179 C C   . GLY A 280 ? 1.1210 0.7134 0.8635 -0.0197 -0.0639 -0.0914 576 GLY A C   
2180 O O   . GLY A 280 ? 1.1414 0.7044 0.8539 0.0268  -0.0599 -0.0913 576 GLY A O   
2181 N N   . LEU A 281 ? 1.0154 0.6770 0.8092 -0.0340 -0.0653 -0.0930 577 LEU A N   
2182 C CA  . LEU A 281 ? 0.9954 0.7045 0.8179 -0.0016 -0.0616 -0.0936 577 LEU A CA  
2183 C C   . LEU A 281 ? 0.9195 0.7119 0.8149 0.0140  -0.0581 -0.0828 577 LEU A C   
2184 O O   . LEU A 281 ? 0.8955 0.7273 0.8336 -0.0092 -0.0604 -0.0770 577 LEU A O   
2185 C CB  . LEU A 281 ? 1.0470 0.7831 0.8811 -0.0255 -0.0656 -0.0999 577 LEU A CB  
2186 C CG  . LEU A 281 ? 1.0327 0.6942 0.7947 -0.0475 -0.0706 -0.1119 577 LEU A CG  
2187 C CD1 . LEU A 281 ? 1.0230 0.7317 0.8085 -0.0673 -0.0752 -0.1168 577 LEU A CD1 
2188 C CD2 . LEU A 281 ? 1.0566 0.6388 0.7468 -0.0077 -0.0662 -0.1181 577 LEU A CD2 
2189 N N   . GLU A 282 ? 0.9075 0.7287 0.8130 0.0522  -0.0525 -0.0804 578 GLU A N   
2190 C CA  . GLU A 282 ? 0.8771 0.7707 0.8395 0.0646  -0.0494 -0.0701 578 GLU A CA  
2191 C C   . GLU A 282 ? 0.8043 0.7609 0.8037 0.0654  -0.0468 -0.0682 578 GLU A C   
2192 O O   . GLU A 282 ? 0.7743 0.7342 0.7545 0.0881  -0.0424 -0.0722 578 GLU A O   
2193 C CB  . GLU A 282 ? 0.8828 0.7711 0.8263 0.1050  -0.0452 -0.0669 578 GLU A CB  
2194 C CG  . GLU A 282 ? 1.0748 0.8960 0.9775 0.1056  -0.0480 -0.0665 578 GLU A CG  
2195 C CD  . GLU A 282 ? 1.2277 1.0467 1.1081 0.1526  -0.0449 -0.0630 578 GLU A CD  
2196 O OE1 . GLU A 282 ? 1.2310 1.0802 1.1058 0.1892  -0.0401 -0.0647 578 GLU A OE1 
2197 O OE2 . GLU A 282 ? 1.3576 1.1507 1.2260 0.1547  -0.0472 -0.0581 578 GLU A OE2 
2198 N N   . PHE A 283 ? 0.6526 0.6548 0.6984 0.0424  -0.0493 -0.0620 579 PHE A N   
2199 C CA  . PHE A 283 ? 0.6307 0.6831 0.7043 0.0390  -0.0476 -0.0584 579 PHE A CA  
2200 C C   . PHE A 283 ? 0.5930 0.6968 0.6988 0.0444  -0.0443 -0.0481 579 PHE A C   
2201 O O   . PHE A 283 ? 0.6889 0.8060 0.8189 0.0276  -0.0476 -0.0421 579 PHE A O   
2202 C CB  . PHE A 283 ? 0.6410 0.6980 0.7291 0.0122  -0.0537 -0.0590 579 PHE A CB  
2203 C CG  . PHE A 283 ? 0.6283 0.6483 0.6860 0.0010  -0.0580 -0.0691 579 PHE A CG  
2204 C CD1 . PHE A 283 ? 0.6444 0.6325 0.6873 -0.0177 -0.0626 -0.0731 579 PHE A CD1 
2205 C CD2 . PHE A 283 ? 0.6731 0.6904 0.7121 0.0059  -0.0575 -0.0748 579 PHE A CD2 
2206 C CE1 . PHE A 283 ? 0.7196 0.6762 0.7297 -0.0361 -0.0675 -0.0824 579 PHE A CE1 
2207 C CE2 . PHE A 283 ? 0.7668 0.7500 0.7737 -0.0087 -0.0628 -0.0847 579 PHE A CE2 
2208 C CZ  . PHE A 283 ? 0.7671 0.7204 0.7589 -0.0316 -0.0681 -0.0886 579 PHE A CZ  
2209 N N   . SER A 284 ? 0.6080 0.7440 0.7106 0.0675  -0.0379 -0.0465 580 SER A N   
2210 C CA  . SER A 284 ? 0.5894 0.7836 0.7186 0.0705  -0.0351 -0.0371 580 SER A CA  
2211 C C   . SER A 284 ? 0.5983 0.8308 0.7521 0.0429  -0.0355 -0.0293 580 SER A C   
2212 O O   . SER A 284 ? 0.5337 0.8061 0.7062 0.0323  -0.0353 -0.0211 580 SER A O   
2213 C CB  . SER A 284 ? 0.5933 0.8245 0.7106 0.1050  -0.0278 -0.0380 580 SER A CB  
2214 O OG  . SER A 284 ? 0.6650 0.8949 0.7640 0.1140  -0.0231 -0.0435 580 SER A OG  
2215 N N   . ALA A 285 ? 0.6516 0.8693 0.7988 0.0303  -0.0365 -0.0314 581 ALA A N   
2216 C CA  . ALA A 285 ? 0.5511 0.7856 0.7072 0.0055  -0.0377 -0.0236 581 ALA A CA  
2217 C C   . ALA A 285 ? 0.6140 0.8062 0.7638 -0.0055 -0.0448 -0.0268 581 ALA A C   
2218 O O   . ALA A 285 ? 0.5869 0.7614 0.7232 -0.0005 -0.0459 -0.0335 581 ALA A O   
2219 C CB  . ALA A 285 ? 0.5434 0.8141 0.6927 0.0049  -0.0310 -0.0208 581 ALA A CB  
2220 N N   . CYS A 286 ? 0.5650 0.7455 0.7223 -0.0187 -0.0498 -0.0224 582 CYS A N   
2221 C CA  . CYS A 286 ? 0.5321 0.6843 0.6854 -0.0229 -0.0565 -0.0253 582 CYS A CA  
2222 C C   . CYS A 286 ? 0.5434 0.6862 0.6928 -0.0343 -0.0602 -0.0177 582 CYS A C   
2223 O O   . CYS A 286 ? 0.5970 0.7264 0.7509 -0.0337 -0.0642 -0.0186 582 CYS A O   
2224 C CB  . CYS A 286 ? 0.5545 0.6910 0.7135 -0.0183 -0.0590 -0.0319 582 CYS A CB  
2225 S SG  . CYS A 286 ? 0.5708 0.7112 0.7423 -0.0171 -0.0574 -0.0278 582 CYS A SG  
2226 N N   . PRO A 287 ? 0.5607 0.7050 0.6945 -0.0455 -0.0588 -0.0102 583 PRO A N   
2227 C CA  . PRO A 287 ? 0.5455 0.6638 0.6600 -0.0580 -0.0627 -0.0030 583 PRO A CA  
2228 C C   . PRO A 287 ? 0.6062 0.6946 0.7101 -0.0453 -0.0694 -0.0061 583 PRO A C   
2229 O O   . PRO A 287 ? 0.5644 0.6516 0.6633 -0.0340 -0.0719 -0.0101 583 PRO A O   
2230 C CB  . PRO A 287 ? 0.5603 0.6742 0.6471 -0.0736 -0.0604 0.0044  583 PRO A CB  
2231 C CG  . PRO A 287 ? 0.6214 0.7515 0.7123 -0.0616 -0.0576 -0.0006 583 PRO A CG  
2232 C CD  . PRO A 287 ? 0.6082 0.7654 0.7300 -0.0472 -0.0547 -0.0090 583 PRO A CD  
2233 N N   . PHE A 288 ? 0.5341 0.6035 0.6328 -0.0456 -0.0725 -0.0044 584 PHE A N   
2234 C CA  . PHE A 288 ? 0.5023 0.5545 0.5914 -0.0282 -0.0779 -0.0074 584 PHE A CA  
2235 C C   . PHE A 288 ? 0.6409 0.6478 0.6916 -0.0291 -0.0813 -0.0017 584 PHE A C   
2236 O O   . PHE A 288 ? 0.5609 0.5563 0.6051 -0.0469 -0.0801 0.0025  584 PHE A O   
2237 C CB  . PHE A 288 ? 0.5443 0.6227 0.6663 -0.0212 -0.0775 -0.0143 584 PHE A CB  
2238 C CG  . PHE A 288 ? 0.5781 0.6585 0.7140 -0.0306 -0.0749 -0.0128 584 PHE A CG  
2239 C CD1 . PHE A 288 ? 0.6043 0.6626 0.7256 -0.0296 -0.0771 -0.0100 584 PHE A CD1 
2240 C CD2 . PHE A 288 ? 0.6043 0.7059 0.7624 -0.0362 -0.0708 -0.0145 584 PHE A CD2 
2241 C CE1 . PHE A 288 ? 0.4948 0.5567 0.6276 -0.0382 -0.0756 -0.0086 584 PHE A CE1 
2242 C CE2 . PHE A 288 ? 0.4817 0.5872 0.6501 -0.0409 -0.0695 -0.0127 584 PHE A CE2 
2243 C CZ  . PHE A 288 ? 0.5114 0.5995 0.6694 -0.0438 -0.0721 -0.0096 584 PHE A CZ  
2244 N N   . SER A 289 ? 0.6573 0.6369 0.6765 -0.0082 -0.0863 -0.0018 585 SER A N   
2245 C CA  . SER A 289 ? 0.7115 0.6293 0.6754 -0.0045 -0.0901 0.0034  585 SER A CA  
2246 C C   . SER A 289 ? 0.7126 0.6243 0.6633 0.0309  -0.0943 -0.0008 585 SER A C   
2247 O O   . SER A 289 ? 0.6939 0.6486 0.6683 0.0518  -0.0958 -0.0059 585 SER A O   
2248 C CB  . SER A 289 ? 0.7604 0.6278 0.6690 -0.0127 -0.0921 0.0107  585 SER A CB  
2249 O OG  . SER A 289 ? 0.7545 0.6332 0.6594 0.0096  -0.0946 0.0089  585 SER A OG  
2250 N N   . GLY A 290 ? 0.7709 0.6330 0.6813 0.0368  -0.0964 0.0012  586 GLY A N   
2251 C CA  . GLY A 290 ? 0.7508 0.5973 0.6315 0.0771  -0.1001 -0.0018 586 GLY A CA  
2252 C C   . GLY A 290 ? 0.9312 0.6792 0.7235 0.0854  -0.1046 0.0035  586 GLY A C   
2253 O O   . GLY A 290 ? 1.0255 0.7207 0.7701 0.0742  -0.1070 0.0096  586 GLY A O   
2254 N N   . TRP A 291 ? 0.9054 0.6210 0.6671 0.1046  -0.1058 0.0012  587 TRP A N   
2255 C CA  . TRP A 291 ? 0.9816 0.5874 0.6480 0.1079  -0.1102 0.0053  587 TRP A CA  
2256 C C   . TRP A 291 ? 1.0385 0.6272 0.7044 0.0867  -0.1087 0.0037  587 TRP A C   
2257 O O   . TRP A 291 ? 0.9029 0.5635 0.6363 0.0850  -0.1044 -0.0010 587 TRP A O   
2258 C CB  . TRP A 291 ? 1.1181 0.6788 0.7179 0.1679  -0.1151 0.0035  587 TRP A CB  
2259 C CG  . TRP A 291 ? 1.1021 0.7406 0.7462 0.2109  -0.1129 -0.0042 587 TRP A CG  
2260 C CD1 . TRP A 291 ? 1.1273 0.7659 0.7665 0.2277  -0.1106 -0.0089 587 TRP A CD1 
2261 C CD2 . TRP A 291 ? 1.0727 0.8056 0.7695 0.2405  -0.1127 -0.0080 587 TRP A CD2 
2262 N NE1 . TRP A 291 ? 1.0578 0.7912 0.7460 0.2652  -0.1079 -0.0147 587 TRP A NE1 
2263 C CE2 . TRP A 291 ? 1.1211 0.9153 0.8455 0.2714  -0.1097 -0.0143 587 TRP A CE2 
2264 C CE3 . TRP A 291 ? 1.1030 0.8783 0.8252 0.2410  -0.1149 -0.0067 587 TRP A CE3 
2265 C CZ2 . TRP A 291 ? 1.1268 1.0287 0.9039 0.2984  -0.1090 -0.0190 587 TRP A CZ2 
2266 C CZ3 . TRP A 291 ? 1.1160 0.9917 0.8883 0.2692  -0.1153 -0.0120 587 TRP A CZ3 
2267 C CH2 . TRP A 291 ? 1.1060 1.0470 0.9061 0.2953  -0.1125 -0.0179 587 TRP A CH2 
2268 N N   . TYR A 292 ? 1.0977 0.5858 0.6806 0.0675  -0.1128 0.0080  588 TYR A N   
2269 C CA  . TYR A 292 ? 1.0689 0.5357 0.6442 0.0393  -0.1129 0.0070  588 TYR A CA  
2270 C C   . TYR A 292 ? 1.1472 0.5929 0.6957 0.0829  -0.1132 0.0003  588 TYR A C   
2271 O O   . TYR A 292 ? 1.1750 0.5684 0.6600 0.1318  -0.1159 -0.0017 588 TYR A O   
2272 C CB  . TYR A 292 ? 1.2188 0.5834 0.7065 -0.0042 -0.1181 0.0136  588 TYR A CB  
2273 C CG  . TYR A 292 ? 1.2027 0.6121 0.7323 -0.0665 -0.1163 0.0196  588 TYR A CG  
2274 C CD1 . TYR A 292 ? 1.1972 0.5779 0.6929 -0.0962 -0.1171 0.0273  588 TYR A CD1 
2275 C CD2 . TYR A 292 ? 1.1471 0.6297 0.7455 -0.0933 -0.1136 0.0179  588 TYR A CD2 
2276 C CE1 . TYR A 292 ? 1.1948 0.6277 0.7275 -0.1509 -0.1146 0.0329  588 TYR A CE1 
2277 C CE2 . TYR A 292 ? 1.1590 0.6919 0.7932 -0.1435 -0.1121 0.0233  588 TYR A CE2 
2278 C CZ  . TYR A 292 ? 1.1145 0.6275 0.7179 -0.1722 -0.1122 0.0305  588 TYR A CZ  
2279 O OH  . TYR A 292 ? 1.0817 0.6597 0.7234 -0.2196 -0.1096 0.0359  588 TYR A OH  
2280 N N   . MET A 293 ? 1.0702 0.5581 0.6639 0.0676  -0.1102 -0.0031 589 MET A N   
2281 C CA  . MET A 293 ? 1.1075 0.5497 0.6550 0.0907  -0.1111 -0.0080 589 MET A CA  
2282 C C   . MET A 293 ? 1.2755 0.6132 0.7398 0.0498  -0.1175 -0.0048 589 MET A C   
2283 O O   . MET A 293 ? 1.2514 0.6088 0.7426 -0.0060 -0.1186 0.0000  589 MET A O   
2284 C CB  . MET A 293 ? 0.9287 0.4635 0.5599 0.0902  -0.1051 -0.0124 589 MET A CB  
2285 C CG  . MET A 293 ? 0.9869 0.4887 0.5769 0.1204  -0.1043 -0.0183 589 MET A CG  
2286 S SD  . MET A 293 ? 1.0098 0.6266 0.6964 0.1247  -0.0957 -0.0224 589 MET A SD  
2287 C CE  . MET A 293 ? 0.9841 0.6227 0.7178 0.0597  -0.0974 -0.0177 589 MET A CE  
2288 N N   . GLY A 294 ? 1.3377 0.5640 0.6947 0.0780  -0.1221 -0.0073 590 GLY A N   
2289 C CA  . GLY A 294 ? 1.3948 0.4998 0.6495 0.0363  -0.1297 -0.0042 590 GLY A CA  
2290 C C   . GLY A 294 ? 1.4235 0.5648 0.7182 -0.0262 -0.1310 -0.0028 590 GLY A C   
2291 O O   . GLY A 294 ? 1.5331 0.6368 0.7937 -0.0854 -0.1360 0.0034  590 GLY A O   
2292 N N   . THR A 295 ? 1.3031 0.5237 0.6700 -0.0147 -0.1265 -0.0078 591 THR A N   
2293 C CA  . THR A 295 ? 1.2893 0.5346 0.6800 -0.0646 -0.1292 -0.0072 591 THR A CA  
2294 C C   . THR A 295 ? 1.2472 0.5728 0.7088 -0.1178 -0.1289 0.0000  591 THR A C   
2295 O O   . THR A 295 ? 1.2102 0.5379 0.6644 -0.1700 -0.1340 0.0029  591 THR A O   
2296 C CB  . THR A 295 ? 1.1495 0.4659 0.6038 -0.0369 -0.1237 -0.0131 591 THR A CB  
2297 O OG1 . THR A 295 ? 1.0967 0.5119 0.6403 -0.0036 -0.1153 -0.0139 591 THR A OG1 
2298 C CG2 . THR A 295 ? 1.2445 0.4764 0.6154 0.0039  -0.1248 -0.0205 591 THR A CG2 
2299 N N   . GLU A 296 ? 1.1071 0.5050 0.6369 -0.1041 -0.1232 0.0024  592 GLU A N   
2300 C CA  . GLU A 296 ? 1.0609 0.5348 0.6526 -0.1470 -0.1219 0.0087  592 GLU A CA  
2301 C C   . GLU A 296 ? 1.1693 0.5806 0.6897 -0.2021 -0.1284 0.0155  592 GLU A C   
2302 O O   . GLU A 296 ? 1.2054 0.6644 0.7498 -0.2519 -0.1307 0.0197  592 GLU A O   
2303 C CB  . GLU A 296 ? 0.9688 0.5033 0.6198 -0.1206 -0.1155 0.0095  592 GLU A CB  
2304 C CG  . GLU A 296 ? 0.9870 0.5911 0.7088 -0.0769 -0.1092 0.0036  592 GLU A CG  
2305 C CD  . GLU A 296 ? 0.9498 0.6065 0.7196 -0.0595 -0.1046 0.0042  592 GLU A CD  
2306 O OE1 . GLU A 296 ? 0.9359 0.6582 0.7636 -0.0821 -0.1018 0.0070  592 GLU A OE1 
2307 O OE2 . GLU A 296 ? 1.0574 0.6887 0.8013 -0.0221 -0.1044 0.0019  592 GLU A OE2 
2308 N N   . ILE A 297 ? 1.2105 0.5152 0.6374 -0.1940 -0.1316 0.0170  593 ILE A N   
2309 C CA  . ILE A 297 ? 1.2873 0.5070 0.6221 -0.2504 -0.1383 0.0238  593 ILE A CA  
2310 C C   . ILE A 297 ? 1.4509 0.5973 0.7109 -0.2795 -0.1459 0.0215  593 ILE A C   
2311 O O   . ILE A 297 ? 1.4873 0.6758 0.7505 -0.3335 -0.1472 0.0273  593 ILE A O   
2312 C CB  . ILE A 297 ? 1.4052 0.5184 0.6501 -0.2271 -0.1397 0.0264  593 ILE A CB  
2313 C CG1 . ILE A 297 ? 1.3715 0.5629 0.6925 -0.1884 -0.1324 0.0272  593 ILE A CG1 
2314 C CG2 . ILE A 297 ? 1.4823 0.5444 0.6500 -0.2846 -0.1427 0.0350  593 ILE A CG2 
2315 C CD1 . ILE A 297 ? 1.4086 0.5044 0.6482 -0.1444 -0.1343 0.0278  593 ILE A CD1 
2316 N N   . GLY A 298 ? 1.4920 0.5542 0.6889 -0.2325 -0.1475 0.0144  594 GLY A N   
2317 C CA  . GLY A 298 ? 1.6130 0.6054 0.7229 -0.2470 -0.1518 0.0141  594 GLY A CA  
2318 C C   . GLY A 298 ? 1.5351 0.5861 0.6908 -0.2744 -0.1540 0.0116  594 GLY A C   
2319 O O   . GLY A 298 ? 1.5936 0.6097 0.6888 -0.3086 -0.1581 0.0150  594 GLY A O   
2320 N N   . VAL A 299 ? 1.4709 0.6081 0.7271 -0.2611 -0.1522 0.0061  595 VAL A N   
2321 C CA  . VAL A 299 ? 1.4897 0.6893 0.7940 -0.2818 -0.1550 0.0031  595 VAL A CA  
2322 C C   . VAL A 299 ? 1.3369 0.6627 0.7327 -0.3275 -0.1546 0.0099  595 VAL A C   
2323 O O   . VAL A 299 ? 1.4554 0.8186 0.8473 -0.3712 -0.1571 0.0158  595 VAL A O   
2324 C CB  . VAL A 299 ? 1.3736 0.6172 0.7352 -0.2182 -0.1479 -0.0043 595 VAL A CB  
2325 C CG1 . VAL A 299 ? 1.3478 0.6520 0.7528 -0.2389 -0.1506 -0.0059 595 VAL A CG1 
2326 C CG2 . VAL A 299 ? 1.4314 0.5621 0.7012 -0.1688 -0.1479 -0.0115 595 VAL A CG2 
2327 N N   . ARG A 300 ? 1.1662 0.5878 0.6562 -0.3005 -0.1458 0.0121  596 ARG A N   
2328 C CA  . ARG A 300 ? 1.0728 0.6174 0.6493 -0.3303 -0.1441 0.0177  596 ARG A CA  
2329 C C   . ARG A 300 ? 1.2425 0.7866 0.7878 -0.3857 -0.1468 0.0260  596 ARG A C   
2330 O O   . ARG A 300 ? 1.2119 0.8200 0.7687 -0.4231 -0.1469 0.0323  596 ARG A O   
2331 C CB  . ARG A 300 ? 0.9848 0.6147 0.6573 -0.2812 -0.1339 0.0163  596 ARG A CB  
2332 C CG  . ARG A 300 ? 0.9995 0.6278 0.6954 -0.2310 -0.1303 0.0091  596 ARG A CG  
2333 C CD  . ARG A 300 ? 1.0679 0.7183 0.7701 -0.2485 -0.1355 0.0077  596 ARG A CD  
2334 N NE  . ARG A 300 ? 0.9176 0.6666 0.6796 -0.2795 -0.1374 0.0132  596 ARG A NE  
2335 C CZ  . ARG A 300 ? 0.8540 0.6923 0.6982 -0.2566 -0.1308 0.0146  596 ARG A CZ  
2336 N NH1 . ARG A 300 ? 0.7855 0.6266 0.6626 -0.2113 -0.1226 0.0110  596 ARG A NH1 
2337 N NH2 . ARG A 300 ? 0.9011 0.8261 0.7895 -0.2788 -0.1330 0.0195  596 ARG A NH2 
2338 N N   . ASP A 301 ? 1.2758 0.7705 0.7896 -0.3752 -0.1432 0.0283  597 ASP A N   
2339 C CA  . ASP A 301 ? 1.2649 0.7819 0.7606 -0.4155 -0.1403 0.0381  597 ASP A CA  
2340 C C   . ASP A 301 ? 1.3641 0.8303 0.7728 -0.4561 -0.1436 0.0437  597 ASP A C   
2341 O O   . ASP A 301 ? 1.4414 0.9743 0.8586 -0.4993 -0.1419 0.0516  597 ASP A O   
2342 C CB  . ASP A 301 ? 1.2132 0.6701 0.6782 -0.3969 -0.1374 0.0395  597 ASP A CB  
2343 C CG  . ASP A 301 ? 1.1717 0.7184 0.7361 -0.3527 -0.1292 0.0372  597 ASP A CG  
2344 O OD1 . ASP A 301 ? 1.2070 0.8708 0.8584 -0.3589 -0.1256 0.0381  597 ASP A OD1 
2345 O OD2 . ASP A 301 ? 1.2476 0.7516 0.8004 -0.3068 -0.1259 0.0346  597 ASP A OD2 
2346 N N   . TYR A 302 ? 1.4170 0.7681 0.7383 -0.4418 -0.1485 0.0396  598 TYR A N   
2347 C CA  . TYR A 302 ? 1.5096 0.7890 0.7276 -0.4800 -0.1528 0.0452  598 TYR A CA  
2348 C C   . TYR A 302 ? 1.5567 0.8664 0.7762 -0.5046 -0.1571 0.0452  598 TYR A C   
2349 O O   . TYR A 302 ? 1.5590 0.8630 0.7236 -0.5536 -0.1599 0.0527  598 TYR A O   
2350 C CB  . TYR A 302 ? 1.7036 0.8315 0.8082 -0.4481 -0.1561 0.0414  598 TYR A CB  
2351 C CG  . TYR A 302 ? 1.8042 0.8738 0.8582 -0.4410 -0.1542 0.0448  598 TYR A CG  
2352 C CD1 . TYR A 302 ? 1.8782 0.8314 0.8532 -0.3907 -0.1557 0.0397  598 TYR A CD1 
2353 C CD2 . TYR A 302 ? 1.7250 0.8589 0.8065 -0.4813 -0.1507 0.0529  598 TYR A CD2 
2354 C CE1 . TYR A 302 ? 1.8492 0.7482 0.7740 -0.3814 -0.1547 0.0425  598 TYR A CE1 
2355 C CE2 . TYR A 302 ? 1.8127 0.8903 0.8444 -0.4759 -0.1494 0.0557  598 TYR A CE2 
2356 C CZ  . TYR A 302 ? 1.8303 0.7889 0.7836 -0.4266 -0.1519 0.0505  598 TYR A CZ  
2357 O OH  . TYR A 302 ? 1.7836 0.6867 0.6846 -0.4194 -0.1511 0.0531  598 TYR A OH  
2358 N N   . CYS A 303 ? 1.4090 0.7516 0.6869 -0.4738 -0.1581 0.0373  599 CYS A N   
2359 C CA  . CYS A 303 ? 1.4809 0.8300 0.7460 -0.4899 -0.1631 0.0362  599 CYS A CA  
2360 C C   . CYS A 303 ? 1.4023 0.8870 0.7763 -0.4942 -0.1626 0.0353  599 CYS A C   
2361 O O   . CYS A 303 ? 1.4292 0.9325 0.7967 -0.5120 -0.1671 0.0356  599 CYS A O   
2362 C CB  . CYS A 303 ? 1.5316 0.7740 0.7391 -0.4473 -0.1662 0.0267  599 CYS A CB  
2363 S SG  . CYS A 303 ? 1.7145 0.7905 0.7770 -0.4318 -0.1677 0.0276  599 CYS A SG  
2364 N N   . ASP A 304 ? 1.3475 0.9243 0.8157 -0.4762 -0.1578 0.0346  600 ASP A N   
2365 C CA  . ASP A 304 ? 1.3382 1.0503 0.8998 -0.4817 -0.1572 0.0363  600 ASP A CA  
2366 C C   . ASP A 304 ? 1.4175 1.1836 0.9596 -0.5317 -0.1577 0.0459  600 ASP A C   
2367 O O   . ASP A 304 ? 1.5467 1.2859 1.0358 -0.5640 -0.1556 0.0530  600 ASP A O   
2368 C CB  . ASP A 304 ? 1.2823 1.0809 0.9316 -0.4594 -0.1510 0.0367  600 ASP A CB  
2369 C CG  . ASP A 304 ? 1.1456 0.9627 0.8566 -0.4147 -0.1523 0.0283  600 ASP A CG  
2370 O OD1 . ASP A 304 ? 1.1472 0.8959 0.8263 -0.3981 -0.1573 0.0211  600 ASP A OD1 
2371 O OD2 . ASP A 304 ? 0.9929 0.8916 0.7797 -0.3956 -0.1482 0.0291  600 ASP A OD2 
2372 N N   . ASN A 305 ? 1.4056 1.2460 0.9846 -0.5389 -0.1611 0.0463  601 ASN A N   
2373 C CA  . ASN A 305 ? 1.3716 1.2714 0.9324 -0.5863 -0.1619 0.0553  601 ASN A CA  
2374 C C   . ASN A 305 ? 1.2433 1.2440 0.8483 -0.6000 -0.1546 0.0627  601 ASN A C   
2375 O O   . ASN A 305 ? 1.2929 1.3048 0.8511 -0.6460 -0.1535 0.0712  601 ASN A O   
2376 C CB  . ASN A 305 ? 1.3366 1.3073 0.9373 -0.5836 -0.1670 0.0539  601 ASN A CB  
2377 C CG  . ASN A 305 ? 1.4988 1.3832 1.0187 -0.6081 -0.1745 0.0530  601 ASN A CG  
2378 O OD1 . ASN A 305 ? 1.6530 1.4462 1.0812 -0.6408 -0.1757 0.0571  601 ASN A OD1 
2379 N ND2 . ASN A 305 ? 1.4493 1.3587 0.9971 -0.5921 -0.1801 0.0481  601 ASN A ND2 
2380 N N   . SER A 306 ? 1.2099 1.2844 0.8998 -0.5611 -0.1494 0.0597  602 SER A N   
2381 C CA  . SER A 306 ? 1.2232 1.3945 0.9574 -0.5651 -0.1415 0.0656  602 SER A CA  
2382 C C   . SER A 306 ? 1.2097 1.3244 0.9253 -0.5603 -0.1364 0.0656  602 SER A C   
2383 O O   . SER A 306 ? 1.1710 1.3612 0.9350 -0.5501 -0.1292 0.0681  602 SER A O   
2384 C CB  . SER A 306 ? 1.1940 1.4822 1.0252 -0.5232 -0.1385 0.0631  602 SER A CB  
2385 O OG  . SER A 306 ? 1.1789 1.4289 1.0452 -0.4782 -0.1398 0.0548  602 SER A OG  
2386 N N   . ARG A 307 ? 1.2292 1.2118 0.8723 -0.5638 -0.1400 0.0628  603 ARG A N   
2387 C CA  . ARG A 307 ? 1.2405 1.1596 0.8472 -0.5653 -0.1362 0.0643  603 ARG A CA  
2388 C C   . ARG A 307 ? 1.3680 1.1992 0.8646 -0.6127 -0.1396 0.0706  603 ARG A C   
2389 O O   . ARG A 307 ? 1.4719 1.3536 0.9473 -0.6560 -0.1403 0.0777  603 ARG A O   
2390 C CB  . ARG A 307 ? 1.1087 0.9452 0.7186 -0.5206 -0.1373 0.0557  603 ARG A CB  
2391 C CG  . ARG A 307 ? 0.9639 0.8826 0.6749 -0.4779 -0.1347 0.0500  603 ARG A CG  
2392 C CD  . ARG A 307 ? 0.9420 0.9548 0.7150 -0.4721 -0.1265 0.0539  603 ARG A CD  
2393 N NE  . ARG A 307 ? 0.9687 0.9165 0.7048 -0.4743 -0.1235 0.0555  603 ARG A NE  
2394 C CZ  . ARG A 307 ? 1.0870 0.9680 0.8214 -0.4430 -0.1246 0.0497  603 ARG A CZ  
2395 N NH1 . ARG A 307 ? 0.9907 0.8648 0.7589 -0.4068 -0.1277 0.0420  603 ARG A NH1 
2396 N NH2 . ARG A 307 ? 1.2463 1.0692 0.9425 -0.4451 -0.1221 0.0522  603 ARG A NH2 
2397 N N   . TYR A 308 ? 1.3920 1.0908 0.8116 -0.6041 -0.1421 0.0682  604 TYR A N   
2398 C CA  . TYR A 308 ? 1.4913 1.0988 0.7959 -0.6470 -0.1456 0.0744  604 TYR A CA  
2399 C C   . TYR A 308 ? 1.6624 1.2182 0.8973 -0.6744 -0.1529 0.0754  604 TYR A C   
2400 O O   . TYR A 308 ? 1.7943 1.3182 0.9466 -0.7254 -0.1560 0.0828  604 TYR A O   
2401 C CB  . TYR A 308 ? 1.5313 1.0098 0.7675 -0.6220 -0.1464 0.0713  604 TYR A CB  
2402 C CG  . TYR A 308 ? 1.5814 1.0919 0.8363 -0.6273 -0.1403 0.0755  604 TYR A CG  
2403 C CD1 . TYR A 308 ? 1.4560 1.0653 0.8190 -0.5986 -0.1333 0.0736  604 TYR A CD1 
2404 C CD2 . TYR A 308 ? 1.7476 1.1886 0.9074 -0.6627 -0.1420 0.0812  604 TYR A CD2 
2405 C CE1 . TYR A 308 ? 1.4027 1.0428 0.7820 -0.6036 -0.1274 0.0777  604 TYR A CE1 
2406 C CE2 . TYR A 308 ? 1.6901 1.1616 0.8657 -0.6690 -0.1365 0.0850  604 TYR A CE2 
2407 C CZ  . TYR A 308 ? 1.5688 1.1410 0.8561 -0.6387 -0.1288 0.0835  604 TYR A CZ  
2408 O OH  . TYR A 308 ? 1.5355 1.1387 0.8383 -0.6441 -0.1229 0.0875  604 TYR A OH  
2409 N N   . ASN A 309 ? 1.5676 1.1122 0.8294 -0.6434 -0.1561 0.0682  605 ASN A N   
2410 C CA  . ASN A 309 ? 1.6548 1.1829 0.8759 -0.6680 -0.1623 0.0692  605 ASN A CA  
2411 C C   . ASN A 309 ? 1.8608 1.2497 0.9399 -0.6995 -0.1681 0.0731  605 ASN A C   
2412 O O   . ASN A 309 ? 1.9590 1.3531 0.9811 -0.7549 -0.1712 0.0813  605 ASN A O   
2413 C CB  . ASN A 309 ? 1.6344 1.3039 0.9144 -0.7048 -0.1608 0.0760  605 ASN A CB  
2414 C CG  . ASN A 309 ? 1.6095 1.2809 0.8685 -0.7237 -0.1669 0.0763  605 ASN A CG  
2415 O OD1 . ASN A 309 ? 1.5714 1.1738 0.8156 -0.6942 -0.1711 0.0687  605 ASN A OD1 
2416 N ND2 . ASN A 309 ? 1.6829 1.4337 0.9368 -0.7734 -0.1675 0.0850  605 ASN A ND2 
2417 N N   . ILE A 310 ? 1.8686 1.1308 0.8849 -0.6616 -0.1696 0.0672  606 ILE A N   
2418 C CA  . ILE A 310 ? 1.9942 1.1118 0.8660 -0.6809 -0.1748 0.0702  606 ILE A CA  
2419 C C   . ILE A 310 ? 2.0605 1.0750 0.8573 -0.6640 -0.1809 0.0658  606 ILE A C   
2420 O O   . ILE A 310 ? 2.2064 1.0901 0.8721 -0.6751 -0.1859 0.0680  606 ILE A O   
2421 C CB  . ILE A 310 ? 2.0652 1.1018 0.8959 -0.6485 -0.1727 0.0676  606 ILE A CB  
2422 C CG1 . ILE A 310 ? 2.0233 1.0119 0.8793 -0.5742 -0.1713 0.0566  606 ILE A CG1 
2423 C CG2 . ILE A 310 ? 1.8450 0.9838 0.7524 -0.6631 -0.1663 0.0718  606 ILE A CG2 
2424 C CD1 . ILE A 310 ? 1.9134 0.8049 0.7077 -0.5367 -0.1705 0.0537  606 ILE A CD1 
2425 N N   . LEU A 311 ? 1.9557 1.0206 0.8250 -0.6364 -0.1808 0.0592  607 LEU A N   
2426 C CA  . LEU A 311 ? 2.0330 1.0038 0.8293 -0.6224 -0.1863 0.0552  607 LEU A CA  
2427 C C   . LEU A 311 ? 2.1110 1.0269 0.8000 -0.6851 -0.1924 0.0649  607 LEU A C   
2428 O O   . LEU A 311 ? 2.1569 0.9403 0.7285 -0.6787 -0.1973 0.0645  607 LEU A O   
2429 C CB  . LEU A 311 ? 1.7691 0.8209 0.6626 -0.5970 -0.1860 0.0477  607 LEU A CB  
2430 C CG  . LEU A 311 ? 1.7418 0.8054 0.7070 -0.5282 -0.1818 0.0358  607 LEU A CG  
2431 C CD1 . LEU A 311 ? 1.7064 0.8551 0.7608 -0.5135 -0.1828 0.0290  607 LEU A CD1 
2432 C CD2 . LEU A 311 ? 1.7623 0.6846 0.6329 -0.4775 -0.1821 0.0295  607 LEU A CD2 
2433 N N   . GLU A 312 ? 2.3246 1.3405 1.0465 -0.7448 -0.1919 0.0740  608 GLU A N   
2434 C CA  . GLU A 312 ? 2.5933 1.5736 1.2153 -0.8151 -0.1971 0.0848  608 GLU A CA  
2435 C C   . GLU A 312 ? 2.6844 1.4962 1.1468 -0.8251 -0.2018 0.0878  608 GLU A C   
2436 O O   . GLU A 312 ? 2.7034 1.4028 1.0572 -0.8341 -0.2079 0.0891  608 GLU A O   
2437 C CB  . GLU A 312 ? 2.6898 1.8034 1.3683 -0.8685 -0.1936 0.0937  608 GLU A CB  
2438 C CG  . GLU A 312 ? 2.6371 1.9199 1.4516 -0.8685 -0.1902 0.0931  608 GLU A CG  
2439 C CD  . GLU A 312 ? 2.7301 2.0408 1.5159 -0.9163 -0.1954 0.0989  608 GLU A CD  
2440 O OE1 . GLU A 312 ? 2.8512 2.0368 1.5233 -0.9338 -0.2018 0.1004  608 GLU A OE1 
2441 O OE2 . GLU A 312 ? 2.6688 2.1267 1.5425 -0.9350 -0.1931 0.1021  608 GLU A OE2 
2442 N N   . GLU A 313 ? 2.6864 1.4773 1.1290 -0.8229 -0.1992 0.0887  609 GLU A N   
2443 C CA  . GLU A 313 ? 2.8944 1.5322 1.1781 -0.8402 -0.2046 0.0920  609 GLU A CA  
2444 C C   . GLU A 313 ? 2.9105 1.4040 1.1182 -0.7712 -0.2068 0.0834  609 GLU A C   
2445 O O   . GLU A 313 ? 3.1646 1.5150 1.2268 -0.7803 -0.2130 0.0849  609 GLU A O   
2446 C CB  . GLU A 313 ? 2.9622 1.6274 1.2483 -0.8607 -0.2016 0.0949  609 GLU A CB  
2447 C CG  . GLU A 313 ? 3.0607 1.8073 1.3371 -0.9452 -0.2024 0.1059  609 GLU A CG  
2448 C CD  . GLU A 313 ? 3.2896 1.9132 1.4066 -1.0023 -0.2103 0.1111  609 GLU A CD  
2449 O OE1 . GLU A 313 ? 3.3466 1.8968 1.4025 -1.0053 -0.2151 0.1109  609 GLU A OE1 
2450 O OE2 . GLU A 313 ? 3.3870 1.9892 1.4516 -1.0417 -0.2110 0.1133  609 GLU A OE2 
2451 N N   . VAL A 314 ? 2.6294 1.1604 0.9332 -0.7003 -0.2014 0.0735  610 VAL A N   
2452 C CA  . VAL A 314 ? 2.5894 0.9978 0.8251 -0.6291 -0.2026 0.0650  610 VAL A CA  
2453 C C   . VAL A 314 ? 2.6663 1.0020 0.8346 -0.6230 -0.2075 0.0645  610 VAL A C   
2454 O O   . VAL A 314 ? 2.7811 0.9760 0.8255 -0.5887 -0.2113 0.0623  610 VAL A O   
2455 C CB  . VAL A 314 ? 2.3987 0.8794 0.7586 -0.5596 -0.1953 0.0550  610 VAL A CB  
2456 C CG1 . VAL A 314 ? 2.4611 0.8360 0.7601 -0.4816 -0.1956 0.0459  610 VAL A CG1 
2457 C CG2 . VAL A 314 ? 2.2937 0.8210 0.6968 -0.5643 -0.1911 0.0564  610 VAL A CG2 
2458 N N   . ALA A 315 ? 2.5952 1.0232 0.8386 -0.6533 -0.2076 0.0663  611 ALA A N   
2459 C CA  . ALA A 315 ? 2.7127 1.0680 0.8830 -0.6575 -0.2128 0.0671  611 ALA A CA  
2460 C C   . ALA A 315 ? 2.9407 1.1737 0.9459 -0.7143 -0.2203 0.0776  611 ALA A C   
2461 O O   . ALA A 315 ? 3.1371 1.2408 1.0373 -0.6903 -0.2240 0.0738  611 ALA A O   
2462 C CB  . ALA A 315 ? 2.6194 1.1041 0.9017 -0.6845 -0.2121 0.0670  611 ALA A CB  
2463 N N   . LYS A 316 ? 2.9363 1.2215 0.9402 -0.7847 -0.2210 0.0860  612 LYS A N   
2464 C CA  . LYS A 316 ? 3.1454 1.3430 1.0278 -0.8455 -0.2266 0.0911  612 LYS A CA  
2465 C C   . LYS A 316 ? 3.2713 1.3012 1.0271 -0.8068 -0.2291 0.0844  612 LYS A C   
2466 O O   . LYS A 316 ? 3.3831 1.2910 1.0304 -0.8018 -0.2341 0.0829  612 LYS A O   
2467 C CB  . LYS A 316 ? 3.0548 1.3495 0.9686 -0.9179 -0.2254 0.0997  612 LYS A CB  
2468 C CG  . LYS A 316 ? 2.9879 1.4434 1.0026 -0.9656 -0.2237 0.1081  612 LYS A CG  
2469 C CD  . LYS A 316 ? 3.0604 1.5849 1.0623 -1.0486 -0.2243 0.1174  612 LYS A CD  
2470 C CE  . LYS A 316 ? 3.3211 1.7033 1.1669 -1.0954 -0.2314 0.1192  612 LYS A CE  
2471 N NZ  . LYS A 316 ? 3.3952 1.8236 1.2144 -1.1693 -0.2317 0.1263  612 LYS A NZ  
2472 N N   . LYS A 317 ? 3.1723 1.1948 0.9395 -0.7762 -0.2255 0.0803  613 LYS A N   
2473 C CA  . LYS A 317 ? 3.3259 1.1969 0.9714 -0.7423 -0.2277 0.0746  613 LYS A CA  
2474 C C   . LYS A 317 ? 3.3872 1.1643 0.9920 -0.6558 -0.2273 0.0654  613 LYS A C   
2475 O O   . LYS A 317 ? 3.5214 1.1623 1.0092 -0.6240 -0.2298 0.0610  613 LYS A O   
2476 C CB  . LYS A 317 ? 3.2889 1.1899 0.9689 -0.7290 -0.2235 0.0725  613 LYS A CB  
2477 C CG  . LYS A 317 ? 3.2545 1.2384 0.9593 -0.8126 -0.2237 0.0812  613 LYS A CG  
2478 C CD  . LYS A 317 ? 3.2542 1.2626 0.9888 -0.7994 -0.2198 0.0790  613 LYS A CD  
2479 C CE  . LYS A 317 ? 3.2684 1.3596 1.0200 -0.8846 -0.2199 0.0878  613 LYS A CE  
2480 N NZ  . LYS A 317 ? 3.1180 1.3480 0.9588 -0.9320 -0.2189 0.0956  613 LYS A NZ  
2481 N N   . MET A 318 ? 3.3124 1.1598 1.0067 -0.6163 -0.2243 0.0625  614 MET A N   
2482 C CA  . MET A 318 ? 3.4000 1.1709 1.0579 -0.5377 -0.2238 0.0542  614 MET A CA  
2483 C C   . MET A 318 ? 3.4902 1.1796 1.0600 -0.5591 -0.2295 0.0566  614 MET A C   
2484 O O   . MET A 318 ? 3.5731 1.1799 1.0883 -0.4956 -0.2296 0.0502  614 MET A O   
2485 C CB  . MET A 318 ? 3.2007 1.0823 0.9914 -0.4845 -0.2179 0.0494  614 MET A CB  
2486 C CG  . MET A 318 ? 3.1762 1.1000 1.0293 -0.4314 -0.2121 0.0437  614 MET A CG  
2487 S SD  . MET A 318 ? 2.9736 1.0172 0.9693 -0.3728 -0.2061 0.0380  614 MET A SD  
2488 C CE  . MET A 318 ? 2.9829 0.9353 0.9087 -0.3078 -0.2067 0.0310  614 MET A CE  
2489 N N   . ASP A 319 ? 3.5833 1.2979 1.1373 -0.6457 -0.2342 0.0658  615 ASP A N   
2490 C CA  . ASP A 319 ? 3.7652 1.4236 1.2512 -0.6767 -0.2400 0.0693  615 ASP A CA  
2491 C C   . ASP A 319 ? 3.6118 1.3418 1.1884 -0.6381 -0.2374 0.0660  615 ASP A C   
2492 O O   . ASP A 319 ? 3.6786 1.3362 1.2175 -0.5704 -0.2367 0.0588  615 ASP A O   
2493 C CB  . ASP A 319 ? 4.0331 1.5084 1.3545 -0.6502 -0.2448 0.0659  615 ASP A CB  
2494 C CG  . ASP A 319 ? 4.2162 1.6195 1.4418 -0.7086 -0.2524 0.0720  615 ASP A CG  
2495 O OD1 . ASP A 319 ? 4.2471 1.7012 1.4761 -0.7969 -0.2558 0.0811  615 ASP A OD1 
2496 O OD2 . ASP A 319 ? 4.3207 1.6170 1.4633 -0.6664 -0.2550 0.0680  615 ASP A OD2 
2497 N N   . LEU A 320 ? 3.4239 1.2983 1.1179 -0.6793 -0.2358 0.0714  616 LEU A N   
2498 C CA  . LEU A 320 ? 3.2317 1.1851 1.0188 -0.6494 -0.2336 0.0689  616 LEU A CA  
2499 C C   . LEU A 320 ? 3.2112 1.2335 1.0218 -0.7240 -0.2378 0.0780  616 LEU A C   
2500 O O   . LEU A 320 ? 3.1734 1.2526 0.9896 -0.7979 -0.2395 0.0869  616 LEU A O   
2501 C CB  . LEU A 320 ? 2.9611 1.0450 0.8968 -0.6108 -0.2262 0.0633  616 LEU A CB  
2502 C CG  . LEU A 320 ? 2.9116 0.9473 0.8383 -0.5308 -0.2215 0.0552  616 LEU A CG  
2503 C CD1 . LEU A 320 ? 2.7238 0.9069 0.8219 -0.4992 -0.2136 0.0462  616 LEU A CD1 
2504 C CD2 . LEU A 320 ? 2.9746 0.9044 0.8284 -0.4603 -0.2218 0.0475  616 LEU A CD2 
2505 N N   . ASP A 321 ? 3.1960 1.2246 1.0320 -0.7009 -0.2388 0.0730  617 ASP A N   
2506 C CA  . ASP A 321 ? 3.1865 1.2990 1.0721 -0.7591 -0.2422 0.0762  617 ASP A CA  
2507 C C   . ASP A 321 ? 2.8732 1.1789 0.9380 -0.7687 -0.2372 0.0720  617 ASP A C   
2508 O O   . ASP A 321 ? 2.7087 1.0882 0.8836 -0.7145 -0.2330 0.0601  617 ASP A O   
2509 C CB  . ASP A 321 ? 3.3453 1.4035 1.2068 -0.7229 -0.2447 0.0691  617 ASP A CB  
2510 C CG  . ASP A 321 ? 3.3951 1.5622 1.3354 -0.7695 -0.2479 0.0686  617 ASP A CG  
2511 O OD1 . ASP A 321 ? 3.3368 1.5741 1.3742 -0.7270 -0.2458 0.0566  617 ASP A OD1 
2512 O OD2 . ASP A 321 ? 3.5093 1.6950 1.4119 -0.8488 -0.2528 0.0800  617 ASP A OD2 
2513 N N   . MET A 322 ? 2.8426 1.2310 0.9318 -0.8371 -0.2376 0.0819  618 MET A N   
2514 C CA  . MET A 322 ? 2.7959 1.3678 1.0455 -0.8460 -0.2328 0.0797  618 MET A CA  
2515 C C   . MET A 322 ? 2.8693 1.5565 1.1869 -0.8893 -0.2361 0.0816  618 MET A C   
2516 O O   . MET A 322 ? 2.7771 1.6205 1.2289 -0.8884 -0.2327 0.0791  618 MET A O   
2517 C CB  . MET A 322 ? 2.8452 1.4593 1.0942 -0.8865 -0.2299 0.0887  618 MET A CB  
2518 C CG  . MET A 322 ? 2.7879 1.3848 1.0666 -0.8301 -0.2240 0.0824  618 MET A CG  
2519 S SD  . MET A 322 ? 2.8723 1.5055 1.1376 -0.8774 -0.2212 0.0921  618 MET A SD  
2520 C CE  . MET A 322 ? 2.7360 1.5917 1.1592 -0.9183 -0.2172 0.0957  618 MET A CE  
2521 N N   . ARG A 323 ? 2.9888 1.6032 1.2148 -0.9246 -0.2428 0.0859  619 ARG A N   
2522 C CA  . ARG A 323 ? 2.9898 1.7155 1.2762 -0.9669 -0.2467 0.0876  619 ARG A CA  
2523 C C   . ARG A 323 ? 2.8774 1.6800 1.2794 -0.9094 -0.2461 0.0734  619 ARG A C   
2524 O O   . ARG A 323 ? 2.7990 1.7525 1.3123 -0.9225 -0.2466 0.0721  619 ARG A O   
2525 C CB  . ARG A 323 ? 3.1744 1.7922 1.3245 -1.0208 -0.2546 0.0958  619 ARG A CB  
2526 C CG  . ARG A 323 ? 3.3269 1.8706 1.3514 -1.0887 -0.2563 0.1109  619 ARG A CG  
2527 C CD  . ARG A 323 ? 3.5577 1.9181 1.4076 -1.1115 -0.2636 0.1165  619 ARG A CD  
2528 N NE  . ARG A 323 ? 3.6161 1.8498 1.4238 -1.0308 -0.2633 0.1059  619 ARG A NE  
2529 C CZ  . ARG A 323 ? 3.8155 1.8632 1.4613 -1.0233 -0.2679 0.1094  619 ARG A CZ  
2530 N NH1 . ARG A 323 ? 4.0021 1.9654 1.5187 -1.0929 -0.2737 0.1200  619 ARG A NH1 
2531 N NH2 . ARG A 323 ? 3.8204 1.7734 1.4406 -0.9420 -0.2664 0.0993  619 ARG A NH2 
2532 N N   . LYS A 324 ? 2.8580 1.5613 1.2316 -0.8439 -0.2452 0.0626  620 LYS A N   
2533 C CA  . LYS A 324 ? 2.7225 1.4779 1.1821 -0.7916 -0.2452 0.0487  620 LYS A CA  
2534 C C   . LYS A 324 ? 2.5959 1.4146 1.1588 -0.7306 -0.2378 0.0395  620 LYS A C   
2535 O O   . LYS A 324 ? 2.6680 1.4086 1.1907 -0.6958 -0.2329 0.0384  620 LYS A O   
2536 C CB  . LYS A 324 ? 2.8090 1.4213 1.1693 -0.7574 -0.2482 0.0422  620 LYS A CB  
2537 C CG  . LYS A 324 ? 2.9182 1.5069 1.2202 -0.8064 -0.2566 0.0459  620 LYS A CG  
2538 C CD  . LYS A 324 ? 3.0432 1.5874 1.2461 -0.8866 -0.2608 0.0625  620 LYS A CD  
2539 C CE  . LYS A 324 ? 3.0324 1.5759 1.1917 -0.9412 -0.2694 0.0662  620 LYS A CE  
2540 N NZ  . LYS A 324 ? 3.1291 1.6502 1.2000 -1.0271 -0.2730 0.0830  620 LYS A NZ  
2541 N N   . THR A 325 ? 2.3506 1.3100 1.0417 -0.7178 -0.2376 0.0332  621 THR A N   
2542 C CA  . THR A 325 ? 2.0715 1.0940 0.8608 -0.6630 -0.2312 0.0246  621 THR A CA  
2543 C C   . THR A 325 ? 2.0442 0.9605 0.7934 -0.5947 -0.2275 0.0129  621 THR A C   
2544 O O   . THR A 325 ? 1.9574 0.8574 0.7246 -0.5543 -0.2210 0.0093  621 THR A O   
2545 C CB  . THR A 325 ? 2.0142 1.1903 0.9292 -0.6589 -0.2335 0.0202  621 THR A CB  
2546 O OG1 . THR A 325 ? 1.9749 1.1841 0.9655 -0.5995 -0.2286 0.0099  621 THR A OG1 
2547 C CG2 . THR A 325 ? 2.1930 1.3683 1.0908 -0.6684 -0.2413 0.0161  621 THR A CG2 
2548 N N   . SER A 326 ? 2.2107 1.0547 0.9010 -0.5803 -0.2310 0.0072  622 SER A N   
2549 C CA  . SER A 326 ? 2.1838 0.9463 0.8423 -0.5114 -0.2267 -0.0050 622 SER A CA  
2550 C C   . SER A 326 ? 2.2560 0.8657 0.7897 -0.4866 -0.2238 -0.0019 622 SER A C   
2551 O O   . SER A 326 ? 2.2934 0.8318 0.7889 -0.4246 -0.2194 -0.0110 622 SER A O   
2552 C CB  . SER A 326 ? 2.1259 0.8829 0.7729 -0.5073 -0.2317 -0.0121 622 SER A CB  
2553 O OG  . SER A 326 ? 2.1939 0.9298 0.7819 -0.5709 -0.2398 -0.0024 622 SER A OG  
2554 N N   . SER A 327 ? 2.3135 0.8718 0.7763 -0.5313 -0.2261 0.0110  623 SER A N   
2555 C CA  . SER A 327 ? 2.4825 0.9040 0.8321 -0.5009 -0.2237 0.0144  623 SER A CA  
2556 C C   . SER A 327 ? 2.4252 0.8715 0.8291 -0.4449 -0.2156 0.0084  623 SER A C   
2557 O O   . SER A 327 ? 2.5904 0.9323 0.9082 -0.4057 -0.2132 0.0095  623 SER A O   
2558 C CB  . SER A 327 ? 2.6415 1.0020 0.8950 -0.5677 -0.2288 0.0300  623 SER A CB  
2559 O OG  . SER A 327 ? 2.5410 1.0130 0.8754 -0.6115 -0.2274 0.0361  623 SER A OG  
2560 N N   . LEU A 328 ? 2.1992 0.7796 0.7387 -0.4393 -0.2119 0.0025  624 LEU A N   
2561 C CA  . LEU A 328 ? 2.1489 0.7657 0.7502 -0.3936 -0.2045 -0.0028 624 LEU A CA  
2562 C C   . LEU A 328 ? 2.2594 0.8171 0.7974 -0.4072 -0.2038 0.0067  624 LEU A C   
2563 O O   . LEU A 328 ? 2.2797 0.8125 0.8169 -0.3581 -0.1984 0.0028  624 LEU A O   
2564 C CB  . LEU A 328 ? 2.1586 0.7348 0.7537 -0.3116 -0.1979 -0.0157 624 LEU A CB  
2565 C CG  . LEU A 328 ? 2.0818 0.7130 0.7332 -0.2942 -0.1977 -0.0264 624 LEU A CG  
2566 C CD1 . LEU A 328 ? 1.9540 0.5801 0.6243 -0.2134 -0.1883 -0.0394 624 LEU A CD1 
2567 C CD2 . LEU A 328 ? 2.0282 0.7988 0.7997 -0.3365 -0.2008 -0.0262 624 LEU A CD2 
2568 N N   . TRP A 329 ? 2.2753 0.8142 0.7582 -0.4753 -0.2095 0.0192  625 TRP A N   
2569 C CA  . TRP A 329 ? 2.3477 0.8401 0.7721 -0.4961 -0.2092 0.0283  625 TRP A CA  
2570 C C   . TRP A 329 ? 2.2163 0.8123 0.7519 -0.4848 -0.2033 0.0258  625 TRP A C   
2571 O O   . TRP A 329 ? 2.2727 0.8213 0.7710 -0.4667 -0.2007 0.0275  625 TRP A O   
2572 C CB  . TRP A 329 ? 2.4433 0.9255 0.8059 -0.5794 -0.2154 0.0419  625 TRP A CB  
2573 C CG  . TRP A 329 ? 2.3200 0.9558 0.7966 -0.6305 -0.2158 0.0450  625 TRP A CG  
2574 C CD1 . TRP A 329 ? 2.3160 1.0151 0.8356 -0.6530 -0.2194 0.0436  625 TRP A CD1 
2575 C CD2 . TRP A 329 ? 2.3103 1.0600 0.8705 -0.6608 -0.2124 0.0500  625 TRP A CD2 
2576 N NE1 . TRP A 329 ? 2.1835 1.0315 0.8072 -0.6931 -0.2187 0.0478  625 TRP A NE1 
2577 C CE2 . TRP A 329 ? 2.2089 1.0910 0.8595 -0.6977 -0.2140 0.0520  625 TRP A CE2 
2578 C CE3 . TRP A 329 ? 2.1598 0.9136 0.7255 -0.6578 -0.2082 0.0530  625 TRP A CE3 
2579 C CZ2 . TRP A 329 ? 2.0788 1.0977 0.8227 -0.7279 -0.2108 0.0573  625 TRP A CZ2 
2580 C CZ3 . TRP A 329 ? 2.0652 0.9506 0.7233 -0.6917 -0.2050 0.0580  625 TRP A CZ3 
2581 C CH2 . TRP A 329 ? 2.0523 1.0699 0.7981 -0.7246 -0.2060 0.0603  625 TRP A CH2 
2582 N N   . LYS A 330 ? 2.0887 0.8233 0.7562 -0.4940 -0.2015 0.0220  626 LYS A N   
2583 C CA  . LYS A 330 ? 2.0788 0.9098 0.8512 -0.4806 -0.1959 0.0199  626 LYS A CA  
2584 C C   . LYS A 330 ? 2.0135 0.8042 0.7950 -0.4059 -0.1902 0.0093  626 LYS A C   
2585 O O   . LYS A 330 ? 2.0285 0.8157 0.8185 -0.3897 -0.1862 0.0103  626 LYS A O   
2586 C CB  . LYS A 330 ? 1.9970 0.9778 0.8991 -0.4986 -0.1960 0.0180  626 LYS A CB  
2587 C CG  . LYS A 330 ? 1.9827 1.0454 0.9048 -0.5681 -0.1992 0.0296  626 LYS A CG  
2588 C CD  . LYS A 330 ? 1.7790 1.0018 0.8384 -0.5716 -0.1968 0.0290  626 LYS A CD  
2589 C CE  . LYS A 330 ? 1.7628 1.0790 0.8423 -0.6333 -0.1995 0.0399  626 LYS A CE  
2590 N NZ  . LYS A 330 ? 1.6443 1.1152 0.8499 -0.6267 -0.1985 0.0387  626 LYS A NZ  
2591 N N   . ASP A 331 ? 1.9922 0.7576 0.7721 -0.3591 -0.1892 -0.0009 627 ASP A N   
2592 C CA  . ASP A 331 ? 1.9590 0.6972 0.7475 -0.2841 -0.1825 -0.0114 627 ASP A CA  
2593 C C   . ASP A 331 ? 2.0091 0.6299 0.6867 -0.2535 -0.1815 -0.0081 627 ASP A C   
2594 O O   . ASP A 331 ? 1.9973 0.6205 0.6932 -0.2131 -0.1764 -0.0110 627 ASP A O   
2595 C CB  . ASP A 331 ? 2.0120 0.7401 0.8015 -0.2431 -0.1812 -0.0222 627 ASP A CB  
2596 C CG  . ASP A 331 ? 1.9480 0.7829 0.8325 -0.2729 -0.1840 -0.0257 627 ASP A CG  
2597 O OD1 . ASP A 331 ? 1.8973 0.7553 0.7761 -0.3311 -0.1907 -0.0179 627 ASP A OD1 
2598 O OD2 . ASP A 331 ? 1.8820 0.7790 0.8428 -0.2371 -0.1797 -0.0359 627 ASP A OD2 
2599 N N   . GLN A 332 ? 2.1158 0.6308 0.6724 -0.2714 -0.1870 -0.0016 628 GLN A N   
2600 C CA  . GLN A 332 ? 2.3727 0.7635 0.8052 -0.2391 -0.1877 0.0018  628 GLN A CA  
2601 C C   . GLN A 332 ? 2.3175 0.7071 0.7396 -0.2667 -0.1881 0.0089  628 GLN A C   
2602 O O   . GLN A 332 ? 2.2958 0.6372 0.6784 -0.2191 -0.1855 0.0068  628 GLN A O   
2603 C CB  . GLN A 332 ? 2.6512 0.9261 0.9503 -0.2616 -0.1948 0.0084  628 GLN A CB  
2604 C CG  . GLN A 332 ? 2.7887 0.9445 0.9746 -0.1907 -0.1941 0.0056  628 GLN A CG  
2605 C CD  . GLN A 332 ? 2.9010 0.9495 0.9671 -0.2080 -0.2008 0.0111  628 GLN A CD  
2606 O OE1 . GLN A 332 ? 2.9250 0.9870 0.9904 -0.2775 -0.2061 0.0172  628 GLN A OE1 
2607 N NE2 . GLN A 332 ? 3.0097 0.9543 0.9721 -0.1433 -0.2007 0.0095  628 GLN A NE2 
2608 N N   . ALA A 333 ? 2.2449 0.6900 0.6982 -0.3420 -0.1913 0.0175  629 ALA A N   
2609 C CA  . ALA A 333 ? 2.3265 0.7816 0.7771 -0.3695 -0.1908 0.0239  629 ALA A CA  
2610 C C   . ALA A 333 ? 2.2148 0.7654 0.7861 -0.3340 -0.1837 0.0175  629 ALA A C   
2611 O O   . ALA A 333 ? 2.1756 0.7091 0.7328 -0.3243 -0.1818 0.0193  629 ALA A O   
2612 C CB  . ALA A 333 ? 2.3035 0.8105 0.7623 -0.4569 -0.1947 0.0349  629 ALA A CB  
2613 N N   . LEU A 334 ? 2.0252 0.6699 0.7085 -0.3134 -0.1801 0.0098  630 LEU A N   
2614 C CA  . LEU A 334 ? 1.8932 0.6246 0.6862 -0.2826 -0.1737 0.0042  630 LEU A CA  
2615 C C   . LEU A 334 ? 1.9656 0.6352 0.7215 -0.2066 -0.1693 -0.0026 630 LEU A C   
2616 O O   . LEU A 334 ? 1.9957 0.6940 0.7916 -0.1883 -0.1655 -0.0027 630 LEU A O   
2617 C CB  . LEU A 334 ? 1.8255 0.6628 0.7330 -0.2797 -0.1720 -0.0027 630 LEU A CB  
2618 C CG  . LEU A 334 ? 1.6792 0.6053 0.6984 -0.2509 -0.1663 -0.0083 630 LEU A CG  
2619 C CD1 . LEU A 334 ? 1.5478 0.5644 0.6390 -0.3007 -0.1662 0.0002  630 LEU A CD1 
2620 C CD2 . LEU A 334 ? 1.5877 0.5735 0.6783 -0.2277 -0.1652 -0.0184 630 LEU A CD2 
2621 N N   . VAL A 335 ? 1.9971 0.5875 0.6761 -0.1593 -0.1695 -0.0078 631 VAL A N   
2622 C CA  . VAL A 335 ? 2.0600 0.6056 0.7020 -0.0793 -0.1647 -0.0140 631 VAL A CA  
2623 C C   . VAL A 335 ? 2.1635 0.6259 0.7106 -0.0774 -0.1675 -0.0078 631 VAL A C   
2624 O O   . VAL A 335 ? 2.1131 0.5937 0.6843 -0.0379 -0.1634 -0.0101 631 VAL A O   
2625 C CB  . VAL A 335 ? 2.2411 0.7311 0.8209 -0.0282 -0.1639 -0.0199 631 VAL A CB  
2626 C CG1 . VAL A 335 ? 2.3974 0.8416 0.9205 0.0542  -0.1597 -0.0239 631 VAL A CG1 
2627 C CG2 . VAL A 335 ? 2.1424 0.7226 0.8236 -0.0171 -0.1593 -0.0288 631 VAL A CG2 
2628 N N   . GLU A 336 ? 2.2687 0.6374 0.7021 -0.1207 -0.1748 0.0000  632 GLU A N   
2629 C CA  . GLU A 336 ? 2.4560 0.7373 0.7872 -0.1245 -0.1782 0.0051  632 GLU A CA  
2630 C C   . GLU A 336 ? 2.3069 0.6598 0.7161 -0.1517 -0.1755 0.0079  632 GLU A C   
2631 O O   . GLU A 336 ? 2.3480 0.6637 0.7190 -0.1208 -0.1745 0.0069  632 GLU A O   
2632 C CB  . GLU A 336 ? 2.6673 0.8500 0.8737 -0.1853 -0.1866 0.0141  632 GLU A CB  
2633 C CG  . GLU A 336 ? 2.7813 0.9032 0.9213 -0.1778 -0.1901 0.0140  632 GLU A CG  
2634 C CD  . GLU A 336 ? 2.9658 0.9868 1.0009 -0.0974 -0.1901 0.0092  632 GLU A CD  
2635 O OE1 . GLU A 336 ? 3.0065 0.9893 1.0034 -0.0581 -0.1882 0.0058  632 GLU A OE1 
2636 O OE2 . GLU A 336 ? 3.0055 0.9987 1.0139 -0.0718 -0.1904 0.0069  632 GLU A OE2 
2637 N N   . ILE A 337 ? 2.1828 0.6393 0.6975 -0.2090 -0.1744 0.0117  633 ILE A N   
2638 C CA  . ILE A 337 ? 2.1531 0.6830 0.7422 -0.2386 -0.1716 0.0160  633 ILE A CA  
2639 C C   . ILE A 337 ? 2.1707 0.7468 0.8340 -0.1745 -0.1651 0.0093  633 ILE A C   
2640 O O   . ILE A 337 ? 2.2493 0.8295 0.9186 -0.1722 -0.1635 0.0121  633 ILE A O   
2641 C CB  . ILE A 337 ? 1.9481 0.5925 0.6383 -0.3047 -0.1712 0.0211  633 ILE A CB  
2642 C CG1 . ILE A 337 ? 2.0749 0.6809 0.6850 -0.3757 -0.1774 0.0304  633 ILE A CG1 
2643 C CG2 . ILE A 337 ? 1.8414 0.5843 0.6329 -0.3211 -0.1665 0.0243  633 ILE A CG2 
2644 C CD1 . ILE A 337 ? 2.0645 0.7890 0.7673 -0.4320 -0.1773 0.0349  633 ILE A CD1 
2645 N N   . ASN A 338 ? 2.1273 0.7384 0.8434 -0.1214 -0.1613 0.0008  634 ASN A N   
2646 C CA  . ASN A 338 ? 1.9531 0.6187 0.7426 -0.0605 -0.1549 -0.0051 634 ASN A CA  
2647 C C   . ASN A 338 ? 2.0212 0.6145 0.7272 0.0131  -0.1538 -0.0093 634 ASN A C   
2648 O O   . ASN A 338 ? 1.9970 0.6258 0.7423 0.0532  -0.1499 -0.0106 634 ASN A O   
2649 C CB  . ASN A 338 ? 1.8360 0.5831 0.7221 -0.0384 -0.1507 -0.0128 634 ASN A CB  
2650 C CG  . ASN A 338 ? 1.7260 0.5701 0.7180 -0.0984 -0.1511 -0.0098 634 ASN A CG  
2651 O OD1 . ASN A 338 ? 1.7220 0.6378 0.7998 -0.0961 -0.1480 -0.0093 634 ASN A OD1 
2652 N ND2 . ASN A 338 ? 1.6493 0.4988 0.6322 -0.1518 -0.1556 -0.0070 634 ASN A ND2 
2653 N N   . ILE A 339 ? 2.0487 0.5451 0.6382 0.0334  -0.1574 -0.0110 635 ILE A N   
2654 C CA  . ILE A 339 ? 2.1395 0.5598 0.6308 0.0968  -0.1577 -0.0140 635 ILE A CA  
2655 C C   . ILE A 339 ? 2.2247 0.5976 0.6653 0.0678  -0.1611 -0.0086 635 ILE A C   
2656 O O   . ILE A 339 ? 2.2609 0.6162 0.6722 0.1190  -0.1595 -0.0116 635 ILE A O   
2657 C CB  . ILE A 339 ? 2.3379 0.6504 0.6978 0.1188  -0.1621 -0.0153 635 ILE A CB  
2658 C CG1 . ILE A 339 ? 2.2451 0.6034 0.6503 0.1531  -0.1580 -0.0209 635 ILE A CG1 
2659 C CG2 . ILE A 339 ? 2.3951 0.6269 0.6435 0.1862  -0.1631 -0.0185 635 ILE A CG2 
2660 C CD1 . ILE A 339 ? 2.4904 0.7427 0.7663 0.1761  -0.1624 -0.0205 635 ILE A CD1 
2661 N N   . ALA A 340 ? 2.2240 0.5857 0.6572 -0.0147 -0.1653 -0.0007 636 ALA A N   
2662 C CA  . ALA A 340 ? 2.3906 0.7056 0.7682 -0.0519 -0.1685 0.0048  636 ALA A CA  
2663 C C   . ALA A 340 ? 2.2745 0.6830 0.7631 -0.0518 -0.1633 0.0068  636 ALA A C   
2664 O O   . ALA A 340 ? 2.1982 0.5736 0.6492 -0.0317 -0.1633 0.0068  636 ALA A O   
2665 C CB  . ALA A 340 ? 2.4860 0.7731 0.8201 -0.1412 -0.1741 0.0132  636 ALA A CB  
2666 N N   . VAL A 341 ? 2.1325 0.6544 0.7530 -0.0754 -0.1593 0.0088  637 VAL A N   
2667 C CA  . VAL A 341 ? 1.9480 0.5561 0.6713 -0.0713 -0.1546 0.0116  637 VAL A CA  
2668 C C   . VAL A 341 ? 2.0398 0.6481 0.7660 0.0143  -0.1514 0.0055  637 VAL A C   
2669 O O   . VAL A 341 ? 2.0645 0.6659 0.7815 0.0296  -0.1508 0.0080  637 VAL A O   
2670 C CB  . VAL A 341 ? 1.8832 0.6072 0.7391 -0.1007 -0.1512 0.0128  637 VAL A CB  
2671 C CG1 . VAL A 341 ? 1.7688 0.5728 0.7212 -0.0904 -0.1469 0.0160  637 VAL A CG1 
2672 C CG2 . VAL A 341 ? 1.9521 0.6979 0.8114 -0.1840 -0.1541 0.0194  637 VAL A CG2 
2673 N N   . LEU A 342 ? 1.9669 0.5873 0.7011 0.0720  -0.1492 -0.0024 638 LEU A N   
2674 C CA  . LEU A 342 ? 1.9289 0.5736 0.6715 0.1569  -0.1454 -0.0085 638 LEU A CA  
2675 C C   . LEU A 342 ? 2.0534 0.6054 0.6779 0.1877  -0.1484 -0.0100 638 LEU A C   
2676 O O   . LEU A 342 ? 2.0668 0.6432 0.7082 0.2190  -0.1469 -0.0095 638 LEU A O   
2677 C CB  . LEU A 342 ? 2.0283 0.6965 0.7793 0.2077  -0.1422 -0.0167 638 LEU A CB  
2678 C CG  . LEU A 342 ? 1.8337 0.6016 0.7055 0.1948  -0.1381 -0.0182 638 LEU A CG  
2679 C CD1 . LEU A 342 ? 1.8036 0.6008 0.6781 0.2581  -0.1334 -0.0269 638 LEU A CD1 
2680 C CD2 . LEU A 342 ? 1.7087 0.5696 0.6877 0.1969  -0.1355 -0.0141 638 LEU A CD2 
2681 N N   . TYR A 343 ? 2.1940 0.6356 0.6920 0.1812  -0.1531 -0.0122 639 TYR A N   
2682 C CA  . TYR A 343 ? 2.4010 0.7391 0.7680 0.2155  -0.1566 -0.0155 639 TYR A CA  
2683 C C   . TYR A 343 ? 2.4182 0.7323 0.7713 0.1767  -0.1586 -0.0102 639 TYR A C   
2684 O O   . TYR A 343 ? 2.4345 0.7203 0.7423 0.2217  -0.1584 -0.0137 639 TYR A O   
2685 C CB  . TYR A 343 ? 2.5622 0.7755 0.7882 0.2001  -0.1628 -0.0165 639 TYR A CB  
2686 C CG  . TYR A 343 ? 2.7473 0.8339 0.8224 0.2215  -0.1674 -0.0192 639 TYR A CG  
2687 C CD1 . TYR A 343 ? 2.7778 0.8429 0.8056 0.3074  -0.1646 -0.0259 639 TYR A CD1 
2688 C CD2 . TYR A 343 ? 2.7507 0.7578 0.7583 0.1541  -0.1722 -0.0135 639 TYR A CD2 
2689 C CE1 . TYR A 343 ? 2.8905 0.8495 0.8037 0.3280  -0.1670 -0.0271 639 TYR A CE1 
2690 C CE2 . TYR A 343 ? 2.8769 0.7741 0.7677 0.1721  -0.1745 -0.0150 639 TYR A CE2 
2691 C CZ  . TYR A 343 ? 2.9451 0.8142 0.7872 0.2604  -0.1721 -0.0219 639 TYR A CZ  
2692 O OH  . TYR A 343 ? 3.0937 0.8487 0.8136 0.2814  -0.1749 -0.0235 639 TYR A OH  
2693 N N   . SER A 344 ? 2.3328 0.6629 0.7234 0.0936  -0.1602 -0.0018 640 SER A N   
2694 C CA  . SER A 344 ? 2.3385 0.6515 0.7162 0.0508  -0.1615 0.0042  640 SER A CA  
2695 C C   . SER A 344 ? 2.2364 0.6361 0.7109 0.0894  -0.1566 0.0058  640 SER A C   
2696 O O   . SER A 344 ? 2.2175 0.5788 0.6453 0.1084  -0.1574 0.0054  640 SER A O   
2697 C CB  . SER A 344 ? 2.2176 0.5614 0.6335 -0.0442 -0.1628 0.0134  640 SER A CB  
2698 O OG  . SER A 344 ? 2.4748 0.7365 0.7909 -0.0820 -0.1685 0.0131  640 SER A OG  
2699 N N   . PHE A 345 ? 2.2072 0.7221 0.8128 0.1011  -0.1521 0.0077  641 PHE A N   
2700 C CA  . PHE A 345 ? 2.0598 0.6632 0.7584 0.1379  -0.1485 0.0105  641 PHE A CA  
2701 C C   . PHE A 345 ? 2.1250 0.7201 0.7840 0.2266  -0.1478 0.0020  641 PHE A C   
2702 O O   . PHE A 345 ? 2.0995 0.7044 0.7583 0.2512  -0.1478 0.0037  641 PHE A O   
2703 C CB  . PHE A 345 ? 1.9151 0.6345 0.7482 0.1343  -0.1449 0.0130  641 PHE A CB  
2704 C CG  . PHE A 345 ? 1.7414 0.5097 0.6476 0.0571  -0.1441 0.0233  641 PHE A CG  
2705 C CD1 . PHE A 345 ? 1.8150 0.5505 0.6895 -0.0166 -0.1457 0.0260  641 PHE A CD1 
2706 C CD2 . PHE A 345 ? 1.6103 0.4715 0.6202 0.0601  -0.1419 0.0299  641 PHE A CD2 
2707 C CE1 . PHE A 345 ? 1.7145 0.5179 0.6632 -0.0847 -0.1437 0.0340  641 PHE A CE1 
2708 C CE2 . PHE A 345 ? 1.4643 0.4133 0.5602 -0.0082 -0.1373 0.0340  641 PHE A CE2 
2709 C CZ  . PHE A 345 ? 1.6187 0.5180 0.6725 -0.0794 -0.1396 0.0387  641 PHE A CZ  
2710 N N   . GLN A 346 ? 2.1426 0.7270 0.7682 0.2761  -0.1467 -0.0071 642 GLN A N   
2711 C CA  . GLN A 346 ? 2.0495 0.6487 0.6449 0.3624  -0.1448 -0.0156 642 GLN A CA  
2712 C C   . GLN A 346 ? 2.1742 0.6628 0.6411 0.3779  -0.1484 -0.0187 642 GLN A C   
2713 O O   . GLN A 346 ? 2.1965 0.7142 0.6660 0.4270  -0.1472 -0.0211 642 GLN A O   
2714 C CB  . GLN A 346 ? 2.1376 0.7393 0.7064 0.4077  -0.1426 -0.0239 642 GLN A CB  
2715 C CG  . GLN A 346 ? 2.1353 0.8547 0.8288 0.4096  -0.1379 -0.0236 642 GLN A CG  
2716 C CD  . GLN A 346 ? 2.2826 0.9710 0.9302 0.4261  -0.1369 -0.0293 642 GLN A CD  
2717 O OE1 . GLN A 346 ? 2.4401 1.0627 1.0521 0.3728  -0.1401 -0.0268 642 GLN A OE1 
2718 N NE2 . GLN A 346 ? 2.3094 1.0473 0.9521 0.4993  -0.1327 -0.0365 642 GLN A NE2 
2719 N N   . SER A 347 ? 2.3142 0.6750 0.6625 0.3366  -0.1532 -0.0191 643 SER A N   
2720 C CA  . SER A 347 ? 2.5219 0.7628 0.7330 0.3490  -0.1572 -0.0231 643 SER A CA  
2721 C C   . SER A 347 ? 2.5774 0.8272 0.8160 0.3184  -0.1576 -0.0166 643 SER A C   
2722 O O   . SER A 347 ? 2.5515 0.7208 0.6937 0.3412  -0.1598 -0.0207 643 SER A O   
2723 C CB  . SER A 347 ? 2.6123 0.7154 0.6882 0.3016  -0.1633 -0.0238 643 SER A CB  
2724 O OG  . SER A 347 ? 2.6411 0.7321 0.6908 0.3262  -0.1633 -0.0273 643 SER A OG  
2725 N N   . ASP A 348 ? 2.4549 0.7992 0.8183 0.2705  -0.1553 -0.0065 644 ASP A N   
2726 C CA  . ASP A 348 ? 2.4701 0.8351 0.8685 0.2417  -0.1552 0.0019  644 ASP A CA  
2727 C C   . ASP A 348 ? 2.3303 0.8180 0.8414 0.2928  -0.1519 0.0045  644 ASP A C   
2728 O O   . ASP A 348 ? 2.1151 0.6346 0.6683 0.2707  -0.1519 0.0133  644 ASP A O   
2729 C CB  . ASP A 348 ? 2.3784 0.7637 0.8269 0.1475  -0.1552 0.0132  644 ASP A CB  
2730 C CG  . ASP A 348 ? 2.5330 0.8024 0.8632 0.0844  -0.1597 0.0124  644 ASP A CG  
2731 O OD1 . ASP A 348 ? 2.6717 0.8278 0.8699 0.1127  -0.1636 0.0034  644 ASP A OD1 
2732 O OD2 . ASP A 348 ? 2.4328 0.7293 0.7997 0.0055  -0.1594 0.0210  644 ASP A OD2 
2733 N N   . LYS A 349 ? 2.3995 0.9630 0.9597 0.3574  -0.1494 -0.0023 645 LYS A N   
2734 C CA  . LYS A 349 ? 2.3866 1.0840 1.0583 0.4030  -0.1472 -0.0007 645 LYS A CA  
2735 C C   . LYS A 349 ? 2.2199 1.0089 1.0152 0.3526  -0.1470 0.0116  645 LYS A C   
2736 O O   . LYS A 349 ? 2.0618 0.9454 0.9370 0.3718  -0.1476 0.0162  645 LYS A O   
2737 C CB  . LYS A 349 ? 2.5454 1.2332 1.1791 0.4444  -0.1486 -0.0022 645 LYS A CB  
2738 C CG  . LYS A 349 ? 2.6006 1.3670 1.2498 0.5310  -0.1463 -0.0123 645 LYS A CG  
2739 C CD  . LYS A 349 ? 2.7461 1.4295 1.2798 0.5769  -0.1451 -0.0247 645 LYS A CD  
2740 C CE  . LYS A 349 ? 2.7854 1.5411 1.3153 0.6637  -0.1422 -0.0343 645 LYS A CE  
2741 N NZ  . LYS A 349 ? 2.6551 1.5806 1.3180 0.6869  -0.1380 -0.0348 645 LYS A NZ  
2742 N N   . VAL A 350 ? 2.1548 0.9189 0.9625 0.2877  -0.1468 0.0167  646 VAL A N   
2743 C CA  . VAL A 350 ? 1.8817 0.7312 0.8008 0.2432  -0.1461 0.0273  646 VAL A CA  
2744 C C   . VAL A 350 ? 1.7981 0.7322 0.7961 0.2728  -0.1442 0.0217  646 VAL A C   
2745 O O   . VAL A 350 ? 1.8267 0.7219 0.7898 0.2714  -0.1427 0.0147  646 VAL A O   
2746 C CB  . VAL A 350 ? 1.8153 0.6105 0.7128 0.1545  -0.1457 0.0350  646 VAL A CB  
2747 C CG1 . VAL A 350 ? 1.5910 0.4982 0.6140 0.1086  -0.1421 0.0423  646 VAL A CG1 
2748 C CG2 . VAL A 350 ? 1.8364 0.5459 0.6450 0.1229  -0.1469 0.0385  646 VAL A CG2 
2749 N N   . THR A 351 ? 1.6943 0.7596 0.8042 0.2929  -0.1427 0.0215  647 THR A N   
2750 C CA  . THR A 351 ? 1.5483 0.7274 0.7503 0.3153  -0.1375 0.0120  647 THR A CA  
2751 C C   . THR A 351 ? 1.5635 0.7400 0.7946 0.2595  -0.1333 0.0103  647 THR A C   
2752 O O   . THR A 351 ? 1.5077 0.6913 0.7704 0.1931  -0.1313 0.0152  647 THR A O   
2753 C CB  . THR A 351 ? 1.4608 0.7952 0.7888 0.3145  -0.1336 0.0092  647 THR A CB  
2754 O OG1 . THR A 351 ? 1.4833 0.8233 0.7823 0.3633  -0.1389 0.0111  647 THR A OG1 
2755 C CG2 . THR A 351 ? 1.2379 0.6875 0.6529 0.3343  -0.1282 0.0002  647 THR A CG2 
2756 N N   . ILE A 352 ? 1.5044 0.6718 0.7192 0.2900  -0.1322 0.0036  648 ILE A N   
2757 C CA  . ILE A 352 ? 1.4270 0.6061 0.6750 0.2476  -0.1286 0.0006  648 ILE A CA  
2758 C C   . ILE A 352 ? 1.4396 0.6706 0.7094 0.3015  -0.1250 -0.0083 648 ILE A C   
2759 O O   . ILE A 352 ? 1.5411 0.7519 0.7576 0.3707  -0.1270 -0.0115 648 ILE A O   
2760 C CB  . ILE A 352 ? 1.5606 0.5918 0.6970 0.2063  -0.1340 0.0049  648 ILE A CB  
2761 C CG1 . ILE A 352 ? 1.4958 0.5648 0.6878 0.1459  -0.1311 0.0037  648 ILE A CG1 
2762 C CG2 . ILE A 352 ? 1.6411 0.5707 0.6614 0.2581  -0.1366 -0.0012 648 ILE A CG2 
2763 C CD1 . ILE A 352 ? 1.7019 0.6551 0.8045 0.0847  -0.1368 0.0093  648 ILE A CD1 
2764 N N   . VAL A 353 ? 1.3572 0.6609 0.7045 0.2724  -0.1194 -0.0119 649 VAL A N   
2765 C CA  . VAL A 353 ? 1.3353 0.6958 0.7077 0.3152  -0.1145 -0.0197 649 VAL A CA  
2766 C C   . VAL A 353 ? 1.3603 0.6630 0.7023 0.2853  -0.1143 -0.0218 649 VAL A C   
2767 O O   . VAL A 353 ? 1.3692 0.6638 0.7360 0.2211  -0.1152 -0.0180 649 VAL A O   
2768 C CB  . VAL A 353 ? 1.2176 0.7386 0.7191 0.3127  -0.1074 -0.0222 649 VAL A CB  
2769 C CG1 . VAL A 353 ? 1.0972 0.6653 0.6789 0.2428  -0.1048 -0.0190 649 VAL A CG1 
2770 C CG2 . VAL A 353 ? 1.2685 0.8568 0.7942 0.3540  -0.1013 -0.0293 649 VAL A CG2 
2771 N N   . ASP A 354 ? 1.4852 0.7466 0.7670 0.3337  -0.1135 -0.0280 650 ASP A N   
2772 C CA  . ASP A 354 ? 1.4286 0.6366 0.6792 0.3073  -0.1136 -0.0310 650 ASP A CA  
2773 C C   . ASP A 354 ? 1.3384 0.6766 0.7026 0.2934  -0.1052 -0.0341 650 ASP A C   
2774 O O   . ASP A 354 ? 1.2445 0.7016 0.6925 0.3143  -0.0990 -0.0352 650 ASP A O   
2775 C CB  . ASP A 354 ? 1.6274 0.7188 0.7511 0.3635  -0.1165 -0.0368 650 ASP A CB  
2776 C CG  . ASP A 354 ? 1.6553 0.8368 0.8049 0.4358  -0.1085 -0.0437 650 ASP A CG  
2777 O OD1 . ASP A 354 ? 1.7504 0.9329 0.8516 0.4846  -0.1077 -0.0451 650 ASP A OD1 
2778 O OD2 . ASP A 354 ? 1.5982 0.8671 0.8204 0.4348  -0.1016 -0.0475 650 ASP A OD2 
2779 N N   . HIS A 355 ? 1.3151 0.6296 0.6793 0.2524  -0.1056 -0.0348 651 HIS A N   
2780 C CA  . HIS A 355 ? 1.1980 0.6258 0.6647 0.2330  -0.0983 -0.0361 651 HIS A CA  
2781 C C   . HIS A 355 ? 1.2640 0.7537 0.7452 0.2890  -0.0901 -0.0426 651 HIS A C   
2782 O O   . HIS A 355 ? 1.2761 0.8756 0.8470 0.2793  -0.0827 -0.0428 651 HIS A O   
2783 C CB  . HIS A 355 ? 1.2752 0.6673 0.7368 0.1781  -0.1018 -0.0348 651 HIS A CB  
2784 C CG  . HIS A 355 ? 1.3609 0.6211 0.7043 0.1820  -0.1083 -0.0383 651 HIS A CG  
2785 N ND1 . HIS A 355 ? 1.3977 0.5364 0.6421 0.1678  -0.1172 -0.0358 651 HIS A ND1 
2786 C CD2 . HIS A 355 ? 1.4682 0.6923 0.7704 0.1926  -0.1078 -0.0441 651 HIS A CD2 
2787 C CE1 . HIS A 355 ? 1.6338 0.6614 0.7762 0.1696  -0.1223 -0.0403 651 HIS A CE1 
2788 N NE2 . HIS A 355 ? 1.5618 0.6400 0.7381 0.1868  -0.1168 -0.0458 651 HIS A NE2 
2789 N N   . HIS A 356 ? 1.3240 0.7449 0.7136 0.3476  -0.0910 -0.0477 652 HIS A N   
2790 C CA  . HIS A 356 ? 1.2694 0.7631 0.6716 0.4071  -0.0823 -0.0539 652 HIS A CA  
2791 C C   . HIS A 356 ? 1.2473 0.8569 0.7139 0.4391  -0.0780 -0.0530 652 HIS A C   
2792 O O   . HIS A 356 ? 1.1411 0.8785 0.6910 0.4412  -0.0693 -0.0541 652 HIS A O   
2793 C CB  . HIS A 356 ? 1.4179 0.7976 0.6929 0.4658  -0.0848 -0.0602 652 HIS A CB  
2794 C CG  . HIS A 356 ? 1.5677 0.8238 0.7677 0.4297  -0.0906 -0.0617 652 HIS A CG  
2795 N ND1 . HIS A 356 ? 1.5134 0.7922 0.7325 0.4153  -0.0859 -0.0654 652 HIS A ND1 
2796 C CD2 . HIS A 356 ? 1.6466 0.7584 0.7516 0.3990  -0.1014 -0.0596 652 HIS A CD2 
2797 C CE1 . HIS A 356 ? 1.6328 0.7884 0.7726 0.3796  -0.0943 -0.0663 652 HIS A CE1 
2798 N NE2 . HIS A 356 ? 1.7245 0.7778 0.7933 0.3665  -0.1038 -0.0628 652 HIS A NE2 
2799 N N   . SER A 357 ? 1.3495 0.9163 0.7757 0.4599  -0.0846 -0.0505 653 SER A N   
2800 C CA  . SER A 357 ? 1.3313 1.0106 0.8180 0.4865  -0.0824 -0.0495 653 SER A CA  
2801 C C   . SER A 357 ? 1.0891 0.8703 0.6919 0.4243  -0.0794 -0.0454 653 SER A C   
2802 O O   . SER A 357 ? 1.0609 0.9700 0.7387 0.4312  -0.0734 -0.0467 653 SER A O   
2803 C CB  . SER A 357 ? 1.4290 1.0317 0.8433 0.5186  -0.0911 -0.0469 653 SER A CB  
2804 O OG  . SER A 357 ? 1.4784 1.1883 0.9236 0.5665  -0.0884 -0.0486 653 SER A OG  
2805 N N   . ALA A 358 ? 1.0711 0.7980 0.6853 0.3626  -0.0835 -0.0407 654 ALA A N   
2806 C CA  . ALA A 358 ? 1.0021 0.8125 0.7142 0.3099  -0.0812 -0.0371 654 ALA A CA  
2807 C C   . ALA A 358 ? 0.9391 0.8364 0.7193 0.2919  -0.0727 -0.0391 654 ALA A C   
2808 O O   . ALA A 358 ? 0.8037 0.8007 0.6591 0.2754  -0.0683 -0.0386 654 ALA A O   
2809 C CB  . ALA A 358 ? 0.9515 0.6908 0.6559 0.2540  -0.0868 -0.0317 654 ALA A CB  
2810 N N   . THR A 359 ? 0.9350 0.7901 0.6837 0.2915  -0.0705 -0.0412 655 THR A N   
2811 C CA  . THR A 359 ? 0.8389 0.7717 0.6464 0.2739  -0.0622 -0.0420 655 THR A CA  
2812 C C   . THR A 359 ? 0.8262 0.8513 0.6487 0.3194  -0.0540 -0.0463 655 THR A C   
2813 O O   . THR A 359 ? 0.8178 0.9392 0.7058 0.2993  -0.0466 -0.0456 655 THR A O   
2814 C CB  . THR A 359 ? 0.8351 0.7002 0.6084 0.2551  -0.0630 -0.0425 655 THR A CB  
2815 O OG1 . THR A 359 ? 0.9993 0.7845 0.6818 0.3000  -0.0650 -0.0473 655 THR A OG1 
2816 C CG2 . THR A 359 ? 0.8589 0.6635 0.6321 0.2039  -0.0707 -0.0376 655 THR A CG2 
2817 N N   . GLU A 360 ? 0.9016 0.9031 0.6617 0.3806  -0.0553 -0.0503 656 GLU A N   
2818 C CA  . GLU A 360 ? 0.9887 1.1024 0.7704 0.4267  -0.0474 -0.0539 656 GLU A CA  
2819 C C   . GLU A 360 ? 0.9198 1.1454 0.7770 0.4085  -0.0469 -0.0516 656 GLU A C   
2820 O O   . GLU A 360 ? 0.8476 1.1925 0.7632 0.3993  -0.0389 -0.0522 656 GLU A O   
2821 C CB  . GLU A 360 ? 1.0848 1.1551 0.7805 0.5051  -0.0497 -0.0587 656 GLU A CB  
2822 C CG  . GLU A 360 ? 1.2006 1.4073 0.9221 0.5568  -0.0407 -0.0626 656 GLU A CG  
2823 C CD  . GLU A 360 ? 1.4349 1.6101 1.0726 0.6191  -0.0438 -0.0645 656 GLU A CD  
2824 O OE1 . GLU A 360 ? 1.4849 1.7713 1.1369 0.6436  -0.0382 -0.0651 656 GLU A OE1 
2825 O OE2 . GLU A 360 ? 1.5640 1.6005 1.1152 0.6341  -0.0523 -0.0643 656 GLU A OE2 
2826 N N   . SER A 361 ? 0.9391 1.1261 0.7917 0.3987  -0.0556 -0.0489 657 SER A N   
2827 C CA  A SER A 361 ? 0.8594 1.1438 0.7756 0.3816  -0.0565 -0.0475 657 SER A CA  
2828 C CA  B SER A 361 ? 0.8607 1.1444 0.7769 0.3812  -0.0566 -0.0475 657 SER A CA  
2829 C C   . SER A 361 ? 0.7873 1.1222 0.7776 0.3141  -0.0521 -0.0449 657 SER A C   
2830 O O   . SER A 361 ? 0.7470 1.1896 0.7922 0.2974  -0.0486 -0.0453 657 SER A O   
2831 C CB  A SER A 361 ? 0.8533 1.0725 0.7410 0.3853  -0.0666 -0.0450 657 SER A CB  
2832 C CB  B SER A 361 ? 0.8519 1.0699 0.7406 0.3833  -0.0666 -0.0449 657 SER A CB  
2833 O OG  A SER A 361 ? 0.8748 1.0239 0.6775 0.4478  -0.0713 -0.0466 657 SER A OG  
2834 O OG  B SER A 361 ? 0.8283 0.9803 0.7322 0.3258  -0.0697 -0.0408 657 SER A OG  
2835 N N   . PHE A 362 ? 0.7623 1.0196 0.7490 0.2747  -0.0527 -0.0422 658 PHE A N   
2836 C CA  . PHE A 362 ? 0.6994 0.9918 0.7448 0.2176  -0.0491 -0.0395 658 PHE A CA  
2837 C C   . PHE A 362 ? 0.6715 1.0472 0.7463 0.2113  -0.0391 -0.0405 658 PHE A C   
2838 O O   . PHE A 362 ? 0.6313 1.0713 0.7538 0.1728  -0.0356 -0.0389 658 PHE A O   
2839 C CB  . PHE A 362 ? 0.7387 0.9393 0.7717 0.1836  -0.0525 -0.0361 658 PHE A CB  
2840 C CG  . PHE A 362 ? 0.7093 0.9366 0.7919 0.1341  -0.0495 -0.0331 658 PHE A CG  
2841 C CD1 . PHE A 362 ? 0.6276 0.8698 0.7421 0.1067  -0.0525 -0.0316 658 PHE A CD1 
2842 C CD2 . PHE A 362 ? 0.7203 0.9560 0.8114 0.1180  -0.0435 -0.0319 658 PHE A CD2 
2843 C CE1 . PHE A 362 ? 0.6064 0.8614 0.7537 0.0666  -0.0499 -0.0293 658 PHE A CE1 
2844 C CE2 . PHE A 362 ? 0.6512 0.9011 0.7766 0.0764  -0.0412 -0.0287 658 PHE A CE2 
2845 C CZ  . PHE A 362 ? 0.6383 0.8945 0.7890 0.0519  -0.0445 -0.0275 658 PHE A CZ  
2846 N N   . ILE A 363 ? 0.7506 1.1222 0.7914 0.2468  -0.0343 -0.0430 659 ILE A N   
2847 C CA  . ILE A 363 ? 0.7563 1.2228 0.8234 0.2456  -0.0234 -0.0438 659 ILE A CA  
2848 C C   . ILE A 363 ? 0.7061 1.2972 0.8083 0.2563  -0.0210 -0.0454 659 ILE A C   
2849 O O   . ILE A 363 ? 0.6677 1.3456 0.8153 0.2171  -0.0150 -0.0436 659 ILE A O   
2850 C CB  . ILE A 363 ? 0.7626 1.2037 0.7801 0.2907  -0.0184 -0.0472 659 ILE A CB  
2851 C CG1 . ILE A 363 ? 0.6831 1.0113 0.6688 0.2701  -0.0214 -0.0456 659 ILE A CG1 
2852 C CG2 . ILE A 363 ? 0.8510 1.4082 0.8961 0.2943  -0.0058 -0.0479 659 ILE A CG2 
2853 C CD1 . ILE A 363 ? 0.6776 1.0255 0.7024 0.2177  -0.0158 -0.0413 659 ILE A CD1 
2854 N N   . LYS A 364 ? 0.7337 1.3341 0.8100 0.3077  -0.0263 -0.0484 660 LYS A N   
2855 C CA  . LYS A 364 ? 0.7755 1.5017 0.8855 0.3195  -0.0261 -0.0499 660 LYS A CA  
2856 C C   . LYS A 364 ? 0.6655 1.4185 0.8252 0.2575  -0.0301 -0.0473 660 LYS A C   
2857 O O   . LYS A 364 ? 0.6737 1.5393 0.8760 0.2282  -0.0261 -0.0472 660 LYS A O   
2858 C CB  . LYS A 364 ? 0.7536 1.4667 0.8190 0.3886  -0.0335 -0.0528 660 LYS A CB  
2859 C CG  . LYS A 364 ? 0.8029 1.6210 0.8667 0.4029  -0.0293 -0.0538 660 LYS A CG  
2860 C CD  . LYS A 364 ? 1.0386 1.8220 1.0542 0.4488  -0.0376 -0.0551 660 LYS A CD  
2861 C CE  . LYS A 364 ? 1.0543 1.9510 1.0916 0.4393  -0.0369 -0.0554 660 LYS A CE  
2862 N NZ  . LYS A 364 ? 1.1168 1.9857 1.1531 0.4376  -0.0466 -0.0551 660 LYS A NZ  
2863 N N   . HIS A 365 ? 0.6351 1.2852 0.7851 0.2353  -0.0379 -0.0453 661 HIS A N   
2864 C CA  . HIS A 365 ? 0.6194 1.2788 0.8076 0.1795  -0.0414 -0.0436 661 HIS A CA  
2865 C C   . HIS A 365 ? 0.5971 1.2815 0.8149 0.1238  -0.0339 -0.0412 661 HIS A C   
2866 O O   . HIS A 365 ? 0.6339 1.3806 0.8822 0.0821  -0.0334 -0.0411 661 HIS A O   
2867 C CB  . HIS A 365 ? 0.7176 1.2621 0.8869 0.1686  -0.0491 -0.0416 661 HIS A CB  
2868 C CG  . HIS A 365 ? 0.7314 1.2713 0.9322 0.1150  -0.0515 -0.0402 661 HIS A CG  
2869 N ND1 . HIS A 365 ? 0.6808 1.1515 0.8841 0.0783  -0.0504 -0.0373 661 HIS A ND1 
2870 C CD2 . HIS A 365 ? 0.7043 1.2986 0.9295 0.0945  -0.0552 -0.0420 661 HIS A CD2 
2871 C CE1 . HIS A 365 ? 0.6928 1.1695 0.9166 0.0415  -0.0527 -0.0375 661 HIS A CE1 
2872 N NE2 . HIS A 365 ? 0.7248 1.2726 0.9613 0.0478  -0.0558 -0.0405 661 HIS A NE2 
2873 N N   . MET A 366 ? 0.5298 1.1590 0.7316 0.1204  -0.0288 -0.0392 662 MET A N   
2874 C CA  . MET A 366 ? 0.4827 1.1281 0.7031 0.0716  -0.0215 -0.0360 662 MET A CA  
2875 C C   . MET A 366 ? 0.4670 1.2404 0.7112 0.0598  -0.0136 -0.0366 662 MET A C   
2876 O O   . MET A 366 ? 0.4559 1.2637 0.7194 0.0057  -0.0110 -0.0344 662 MET A O   
2877 C CB  . MET A 366 ? 0.4521 1.0276 0.6478 0.0790  -0.0177 -0.0339 662 MET A CB  
2878 C CG  . MET A 366 ? 0.5075 1.0126 0.7059 0.0341  -0.0188 -0.0295 662 MET A CG  
2879 S SD  . MET A 366 ? 0.6524 1.0873 0.8196 0.0497  -0.0162 -0.0276 662 MET A SD  
2880 C CE  . MET A 366 ? 0.6738 1.0848 0.8509 -0.0052 -0.0127 -0.0213 662 MET A CE  
2881 N N   . GLU A 367 ? 0.5154 1.3607 0.7530 0.1099  -0.0098 -0.0396 663 GLU A N   
2882 C CA  . GLU A 367 ? 0.6064 1.5950 0.8689 0.1021  -0.0018 -0.0401 663 GLU A CA  
2883 C C   . GLU A 367 ? 0.6601 1.6835 0.9331 0.0625  -0.0068 -0.0398 663 GLU A C   
2884 O O   . GLU A 367 ? 0.7001 1.7675 0.9785 0.0098  -0.0019 -0.0371 663 GLU A O   
2885 C CB  . GLU A 367 ? 0.7401 1.7651 0.9711 0.1711  0.0011  -0.0432 663 GLU A CB  
2886 C CG  . GLU A 367 ? 0.8968 1.8861 1.1035 0.2149  0.0076  -0.0447 663 GLU A CG  
2887 C CD  . GLU A 367 ? 1.0089 2.0174 1.1693 0.2854  0.0085  -0.0482 663 GLU A CD  
2888 O OE1 . GLU A 367 ? 1.0769 2.1530 1.2319 0.2946  0.0059  -0.0485 663 GLU A OE1 
2889 O OE2 . GLU A 367 ? 1.0184 1.9693 1.1412 0.3323  0.0110  -0.0509 663 GLU A OE2 
2890 N N   . ASN A 368 ? 0.6784 1.6770 0.9479 0.0872  -0.0169 -0.0425 664 ASN A N   
2891 C CA  . ASN A 368 ? 0.6501 1.6794 0.9264 0.0545  -0.0218 -0.0431 664 ASN A CA  
2892 C C   . ASN A 368 ? 0.6336 1.6218 0.9234 -0.0161 -0.0231 -0.0409 664 ASN A C   
2893 O O   . ASN A 368 ? 0.6644 1.6885 0.9517 -0.0618 -0.0218 -0.0402 664 ASN A O   
2894 C CB  . ASN A 368 ? 0.6134 1.6120 0.8805 0.0967  -0.0323 -0.0459 664 ASN A CB  
2895 C CG  . ASN A 368 ? 0.6876 1.7067 0.9241 0.1699  -0.0316 -0.0479 664 ASN A CG  
2896 O OD1 . ASN A 368 ? 0.8319 1.9189 1.0571 0.1861  -0.0240 -0.0480 664 ASN A OD1 
2897 N ND2 . ASN A 368 ? 0.6064 1.5611 0.8213 0.2147  -0.0402 -0.0492 664 ASN A ND2 
2898 N N   . GLU A 369 ? 0.5543 1.4624 0.8506 -0.0248 -0.0262 -0.0402 665 GLU A N   
2899 C CA  . GLU A 369 ? 0.4677 1.3206 0.7646 -0.0861 -0.0279 -0.0384 665 GLU A CA  
2900 C C   . GLU A 369 ? 0.6363 1.5096 0.9230 -0.1342 -0.0179 -0.0342 665 GLU A C   
2901 O O   . GLU A 369 ? 0.7010 1.5627 0.9725 -0.1854 -0.0179 -0.0330 665 GLU A O   
2902 C CB  . GLU A 369 ? 0.5350 1.2532 0.8114 -0.0748 -0.0306 -0.0363 665 GLU A CB  
2903 C CG  . GLU A 369 ? 0.6272 1.2932 0.8983 -0.0427 -0.0397 -0.0386 665 GLU A CG  
2904 C CD  . GLU A 369 ? 0.6784 1.3112 0.9503 -0.0788 -0.0459 -0.0401 665 GLU A CD  
2905 O OE1 . GLU A 369 ? 0.7575 1.3051 1.0159 -0.1005 -0.0460 -0.0380 665 GLU A OE1 
2906 O OE2 . GLU A 369 ? 0.4667 1.1620 0.7499 -0.0834 -0.0507 -0.0437 665 GLU A OE2 
2907 N N   . TYR A 370 ? 0.6897 1.5884 0.9775 -0.1179 -0.0093 -0.0318 666 TYR A N   
2908 C CA  . TYR A 370 ? 0.7051 1.6231 0.9787 -0.1636 0.0005  -0.0270 666 TYR A CA  
2909 C C   . TYR A 370 ? 0.7778 1.7793 1.0411 -0.1836 0.0033  -0.0271 666 TYR A C   
2910 O O   . TYR A 370 ? 0.7925 1.7926 1.0346 -0.2392 0.0070  -0.0235 666 TYR A O   
2911 C CB  . TYR A 370 ? 0.6735 1.6084 0.9505 -0.1375 0.0096  -0.0248 666 TYR A CB  
2912 C CG  . TYR A 370 ? 0.6286 1.4330 0.8832 -0.1407 0.0082  -0.0213 666 TYR A CG  
2913 C CD1 . TYR A 370 ? 0.5977 1.3183 0.8441 -0.0957 0.0011  -0.0235 666 TYR A CD1 
2914 C CD2 . TYR A 370 ? 0.7276 1.4879 0.9620 -0.1899 0.0134  -0.0154 666 TYR A CD2 
2915 C CE1 . TYR A 370 ? 0.6505 1.2624 0.8765 -0.0991 -0.0011 -0.0201 666 TYR A CE1 
2916 C CE2 . TYR A 370 ? 0.7906 1.4345 1.0013 -0.1871 0.0110  -0.0119 666 TYR A CE2 
2917 C CZ  . TYR A 370 ? 0.7594 1.3370 0.9698 -0.1418 0.0036  -0.0145 666 TYR A CZ  
2918 O OH  . TYR A 370 ? 0.8351 1.3130 1.0248 -0.1401 0.0005  -0.0110 666 TYR A OH  
2919 N N   . ARG A 371 ? 0.8179 1.8887 1.0893 -0.1399 0.0006  -0.0309 667 ARG A N   
2920 C CA  . ARG A 371 ? 0.8923 2.0556 1.1539 -0.1570 0.0023  -0.0312 667 ARG A CA  
2921 C C   . ARG A 371 ? 0.9270 2.0696 1.1798 -0.2019 -0.0047 -0.0324 667 ARG A C   
2922 O O   . ARG A 371 ? 0.9684 2.1127 1.1998 -0.2611 -0.0024 -0.0298 667 ARG A O   
2923 C CB  . ARG A 371 ? 0.9704 2.2123 1.2362 -0.0905 0.0016  -0.0348 667 ARG A CB  
2924 C CG  . ARG A 371 ? 1.1120 2.4695 1.3673 -0.1014 0.0042  -0.0348 667 ARG A CG  
2925 C CD  . ARG A 371 ? 1.1919 2.6165 1.4430 -0.0279 0.0026  -0.0383 667 ARG A CD  
2926 N NE  . ARG A 371 ? 1.2460 2.6061 1.5003 0.0175  -0.0053 -0.0417 667 ARG A NE  
2927 C CZ  . ARG A 371 ? 1.3382 2.6904 1.5956 0.0085  -0.0131 -0.0438 667 ARG A CZ  
2928 N NH1 . ARG A 371 ? 1.4013 2.8046 1.6581 -0.0440 -0.0138 -0.0433 667 ARG A NH1 
2929 N NH2 . ARG A 371 ? 1.3397 2.6305 1.5965 0.0507  -0.0205 -0.0463 667 ARG A NH2 
2930 N N   . CYS A 372 ? 0.9014 2.0184 1.1645 -0.1745 -0.0135 -0.0364 668 CYS A N   
2931 C CA  . CYS A 372 ? 0.8956 2.0024 1.1498 -0.2086 -0.0203 -0.0385 668 CYS A CA  
2932 C C   . CYS A 372 ? 0.8211 1.8145 1.0659 -0.2442 -0.0253 -0.0384 668 CYS A C   
2933 O O   . CYS A 372 ? 0.8819 1.8500 1.1196 -0.2604 -0.0325 -0.0413 668 CYS A O   
2934 C CB  . CYS A 372 ? 0.9756 2.1213 1.2412 -0.1598 -0.0274 -0.0428 668 CYS A CB  
2935 S SG  . CYS A 372 ? 0.9921 2.0528 1.2728 -0.1049 -0.0354 -0.0451 668 CYS A SG  
2936 N N   . ARG A 373 ? 0.7024 1.6276 0.9434 -0.2549 -0.0217 -0.0353 669 ARG A N   
2937 C CA  . ARG A 373 ? 0.7016 1.5172 0.9260 -0.2850 -0.0264 -0.0352 669 ARG A CA  
2938 C C   . ARG A 373 ? 0.7988 1.5577 1.0006 -0.3176 -0.0197 -0.0299 669 ARG A C   
2939 O O   . ARG A 373 ? 0.7966 1.4624 0.9680 -0.3506 -0.0221 -0.0290 669 ARG A O   
2940 C CB  . ARG A 373 ? 0.6737 1.4404 0.9201 -0.2432 -0.0341 -0.0384 669 ARG A CB  
2941 C CG  . ARG A 373 ? 0.6822 1.3489 0.9090 -0.2699 -0.0407 -0.0402 669 ARG A CG  
2942 C CD  . ARG A 373 ? 0.6473 1.2650 0.8915 -0.2310 -0.0473 -0.0425 669 ARG A CD  
2943 N NE  . ARG A 373 ? 0.7202 1.2485 0.9392 -0.2485 -0.0530 -0.0448 669 ARG A NE  
2944 C CZ  . ARG A 373 ? 0.6711 1.1112 0.8808 -0.2210 -0.0545 -0.0437 669 ARG A CZ  
2945 N NH1 . ARG A 373 ? 0.5577 0.9823 0.7792 -0.1811 -0.0519 -0.0401 669 ARG A NH1 
2946 N NH2 . ARG A 373 ? 0.6603 1.0298 0.8450 -0.2343 -0.0587 -0.0463 669 ARG A NH2 
2947 N N   . GLY A 374 ? 0.8928 1.7032 1.1038 -0.3058 -0.0111 -0.0265 670 GLY A N   
2948 C CA  . GLY A 374 ? 0.9517 1.7149 1.1386 -0.3371 -0.0041 -0.0206 670 GLY A CA  
2949 C C   . GLY A 374 ? 0.9526 1.6451 1.1488 -0.3166 -0.0046 -0.0189 670 GLY A C   
2950 O O   . GLY A 374 ? 1.0077 1.6318 1.1745 -0.3464 -0.0011 -0.0137 670 GLY A O   
2951 N N   . GLY A 375 ? 0.8672 1.5696 1.0969 -0.2668 -0.0096 -0.0228 671 GLY A N   
2952 C CA  . GLY A 375 ? 0.7827 1.3849 1.0002 -0.2327 -0.0104 -0.0204 671 GLY A CA  
2953 C C   . GLY A 375 ? 0.7005 1.2629 0.9292 -0.1886 -0.0193 -0.0246 671 GLY A C   
2954 O O   . GLY A 375 ? 0.6678 1.2672 0.9101 -0.1843 -0.0251 -0.0291 671 GLY A O   
2955 N N   . CYS A 376 ? 0.5963 1.0839 0.8161 -0.1587 -0.0206 -0.0225 672 CYS A N   
2956 C CA  . CYS A 376 ? 0.5757 1.0168 0.7995 -0.1212 -0.0281 -0.0249 672 CYS A CA  
2957 C C   . CYS A 376 ? 0.6216 0.9720 0.8277 -0.1164 -0.0295 -0.0210 672 CYS A C   
2958 O O   . CYS A 376 ? 0.6672 1.0064 0.8671 -0.1001 -0.0263 -0.0185 672 CYS A O   
2959 C CB  . CYS A 376 ? 0.5002 0.9858 0.7336 -0.0738 -0.0281 -0.0275 672 CYS A CB  
2960 S SG  . CYS A 376 ? 0.6047 1.0248 0.8297 -0.0335 -0.0371 -0.0293 672 CYS A SG  
2961 N N   . PRO A 377 ? 0.5909 0.8801 0.7864 -0.1285 -0.0342 -0.0205 673 PRO A N   
2962 C CA  . PRO A 377 ? 0.5396 0.7581 0.7211 -0.1180 -0.0364 -0.0166 673 PRO A CA  
2963 C C   . PRO A 377 ? 0.5540 0.7662 0.7430 -0.0829 -0.0397 -0.0171 673 PRO A C   
2964 O O   . PRO A 377 ? 0.4632 0.6897 0.6613 -0.0658 -0.0435 -0.0204 673 PRO A O   
2965 C CB  . PRO A 377 ? 0.6115 0.7832 0.7821 -0.1283 -0.0411 -0.0177 673 PRO A CB  
2966 C CG  . PRO A 377 ? 0.4877 0.7029 0.6735 -0.1311 -0.0437 -0.0233 673 PRO A CG  
2967 C CD  . PRO A 377 ? 0.5175 0.8058 0.7138 -0.1438 -0.0388 -0.0243 673 PRO A CD  
2968 N N   . ALA A 378 ? 0.5823 0.7681 0.7608 -0.0743 -0.0388 -0.0137 674 ALA A N   
2969 C CA  . ALA A 378 ? 0.5196 0.6918 0.6938 -0.0474 -0.0423 -0.0144 674 ALA A CA  
2970 C C   . ALA A 378 ? 0.5228 0.6497 0.6836 -0.0474 -0.0451 -0.0102 674 ALA A C   
2971 O O   . ALA A 378 ? 0.6406 0.7600 0.7932 -0.0583 -0.0418 -0.0067 674 ALA A O   
2972 C CB  . ALA A 378 ? 0.4583 0.6713 0.6293 -0.0286 -0.0377 -0.0171 674 ALA A CB  
2973 N N   . ASP A 379 ? 0.5421 0.6417 0.6982 -0.0372 -0.0517 -0.0100 675 ASP A N   
2974 C CA  . ASP A 379 ? 0.5112 0.5800 0.6566 -0.0387 -0.0564 -0.0063 675 ASP A CA  
2975 C C   . ASP A 379 ? 0.6335 0.6877 0.7575 -0.0268 -0.0584 -0.0078 675 ASP A C   
2976 O O   . ASP A 379 ? 0.5526 0.5891 0.6636 -0.0200 -0.0631 -0.0096 675 ASP A O   
2977 C CB  . ASP A 379 ? 0.5081 0.5653 0.6601 -0.0415 -0.0623 -0.0048 675 ASP A CB  
2978 C CG  . ASP A 379 ? 0.6278 0.6718 0.7733 -0.0445 -0.0674 -0.0003 675 ASP A CG  
2979 O OD1 . ASP A 379 ? 0.6345 0.6818 0.7878 -0.0452 -0.0702 0.0018  675 ASP A OD1 
2980 O OD2 . ASP A 379 ? 0.6331 0.6674 0.7641 -0.0441 -0.0689 0.0008  675 ASP A OD2 
2981 N N   . TRP A 380 ? 0.5242 0.5791 0.6371 -0.0252 -0.0548 -0.0070 676 TRP A N   
2982 C CA  . TRP A 380 ? 0.4927 0.5266 0.5764 -0.0122 -0.0562 -0.0093 676 TRP A CA  
2983 C C   . TRP A 380 ? 0.5343 0.5298 0.5985 -0.0182 -0.0659 -0.0084 676 TRP A C   
2984 O O   . TRP A 380 ? 0.6166 0.5813 0.6494 -0.0091 -0.0694 -0.0117 676 TRP A O   
2985 C CB  . TRP A 380 ? 0.4983 0.5369 0.5733 -0.0138 -0.0514 -0.0075 676 TRP A CB  
2986 C CG  . TRP A 380 ? 0.5668 0.5908 0.6096 0.0041  -0.0499 -0.0114 676 TRP A CG  
2987 C CD1 . TRP A 380 ? 0.6548 0.7088 0.6914 0.0227  -0.0410 -0.0150 676 TRP A CD1 
2988 C CD2 . TRP A 380 ? 0.6316 0.6085 0.6382 0.0056  -0.0573 -0.0126 676 TRP A CD2 
2989 N NE1 . TRP A 380 ? 0.6987 0.7205 0.6941 0.0415  -0.0420 -0.0187 676 TRP A NE1 
2990 C CE2 . TRP A 380 ? 0.6654 0.6339 0.6391 0.0287  -0.0524 -0.0175 676 TRP A CE2 
2991 C CE3 . TRP A 380 ? 0.5858 0.5313 0.5819 -0.0114 -0.0678 -0.0102 676 TRP A CE3 
2992 C CZ2 . TRP A 380 ? 0.6923 0.6067 0.6155 0.0348  -0.0581 -0.0208 676 TRP A CZ2 
2993 C CZ3 . TRP A 380 ? 0.6649 0.5653 0.6152 -0.0115 -0.0742 -0.0128 676 TRP A CZ3 
2994 C CH2 . TRP A 380 ? 0.6570 0.5351 0.5682 0.0111  -0.0695 -0.0184 676 TRP A CH2 
2995 N N   . VAL A 381 ? 0.5781 0.5748 0.6550 -0.0337 -0.0707 -0.0038 677 VAL A N   
2996 C CA  . VAL A 381 ? 0.5162 0.4940 0.5784 -0.0459 -0.0803 -0.0021 677 VAL A CA  
2997 C C   . VAL A 381 ? 0.6552 0.6185 0.7077 -0.0482 -0.0833 -0.0040 677 VAL A C   
2998 O O   . VAL A 381 ? 0.5926 0.5249 0.6128 -0.0596 -0.0902 -0.0042 677 VAL A O   
2999 C CB  . VAL A 381 ? 0.6285 0.6301 0.7131 -0.0556 -0.0841 0.0034  677 VAL A CB  
3000 C CG1 . VAL A 381 ? 0.5522 0.5574 0.6304 -0.0715 -0.0934 0.0055  677 VAL A CG1 
3001 C CG2 . VAL A 381 ? 0.6242 0.6263 0.7035 -0.0537 -0.0836 0.0064  677 VAL A CG2 
3002 N N   . TRP A 382 ? 0.6752 0.6564 0.7492 -0.0405 -0.0788 -0.0052 678 TRP A N   
3003 C CA  . TRP A 382 ? 0.6165 0.5839 0.6802 -0.0412 -0.0813 -0.0063 678 TRP A CA  
3004 C C   . TRP A 382 ? 0.5834 0.5307 0.6219 -0.0193 -0.0785 -0.0109 678 TRP A C   
3005 O O   . TRP A 382 ? 0.6603 0.5704 0.6649 -0.0179 -0.0826 -0.0115 678 TRP A O   
3006 C CB  . TRP A 382 ? 0.5884 0.5884 0.6879 -0.0447 -0.0793 -0.0048 678 TRP A CB  
3007 C CG  . TRP A 382 ? 0.5667 0.5825 0.6784 -0.0609 -0.0837 -0.0004 678 TRP A CG  
3008 C CD1 . TRP A 382 ? 0.6954 0.7284 0.8171 -0.0656 -0.0858 0.0029  678 TRP A CD1 
3009 C CD2 . TRP A 382 ? 0.5936 0.6174 0.7073 -0.0720 -0.0864 0.0016  678 TRP A CD2 
3010 N NE1 . TRP A 382 ? 0.6595 0.7188 0.7919 -0.0758 -0.0898 0.0065  678 TRP A NE1 
3011 C CE2 . TRP A 382 ? 0.6591 0.7150 0.7878 -0.0820 -0.0896 0.0058  678 TRP A CE2 
3012 C CE3 . TRP A 382 ? 0.5087 0.5192 0.6114 -0.0729 -0.0863 0.0007  678 TRP A CE3 
3013 C CZ2 . TRP A 382 ? 0.7155 0.7987 0.8515 -0.0944 -0.0916 0.0088  678 TRP A CZ2 
3014 C CZ3 . TRP A 382 ? 0.5884 0.6164 0.6953 -0.0884 -0.0883 0.0041  678 TRP A CZ3 
3015 C CH2 . TRP A 382 ? 0.6490 0.7172 0.7743 -0.0996 -0.0904 0.0080  678 TRP A CH2 
3016 N N   . ILE A 383 ? 0.5935 0.5658 0.6428 -0.0017 -0.0717 -0.0137 679 ILE A N   
3017 C CA  . ILE A 383 ? 0.6662 0.6347 0.6928 0.0265  -0.0689 -0.0182 679 ILE A CA  
3018 C C   . ILE A 383 ? 0.7438 0.6539 0.7113 0.0402  -0.0723 -0.0206 679 ILE A C   
3019 O O   . ILE A 383 ? 0.7235 0.5948 0.6481 0.0609  -0.0747 -0.0232 679 ILE A O   
3020 C CB  . ILE A 383 ? 0.6326 0.6599 0.6885 0.0378  -0.0602 -0.0201 679 ILE A CB  
3021 C CG1 . ILE A 383 ? 0.5183 0.5888 0.6184 0.0214  -0.0580 -0.0186 679 ILE A CG1 
3022 C CG2 . ILE A 383 ? 0.5483 0.5886 0.5807 0.0740  -0.0569 -0.0249 679 ILE A CG2 
3023 C CD1 . ILE A 383 ? 0.6600 0.7356 0.7632 0.0290  -0.0610 -0.0202 679 ILE A CD1 
3024 N N   . VAL A 384 ? 0.7178 0.6134 0.6741 0.0303  -0.0731 -0.0201 680 VAL A N   
3025 C CA  . VAL A 384 ? 0.7714 0.6044 0.6632 0.0426  -0.0764 -0.0236 680 VAL A CA  
3026 C C   . VAL A 384 ? 0.8251 0.5907 0.6695 0.0250  -0.0862 -0.0224 680 VAL A C   
3027 O O   . VAL A 384 ? 0.8124 0.5855 0.6764 -0.0096 -0.0915 -0.0177 680 VAL A O   
3028 C CB  . VAL A 384 ? 0.7589 0.5925 0.6494 0.0309  -0.0763 -0.0230 680 VAL A CB  
3029 C CG1 . VAL A 384 ? 0.7805 0.5376 0.5948 0.0381  -0.0815 -0.0273 680 VAL A CG1 
3030 C CG2 . VAL A 384 ? 0.8089 0.7032 0.7358 0.0457  -0.0656 -0.0235 680 VAL A CG2 
3031 N N   . PRO A 385 ? 0.9243 0.6237 0.7012 0.0475  -0.0887 -0.0261 681 PRO A N   
3032 C CA  . PRO A 385 ? 0.9378 0.5630 0.6583 0.0249  -0.0978 -0.0241 681 PRO A CA  
3033 C C   . PRO A 385 ? 1.0261 0.6141 0.7169 -0.0143 -0.1057 -0.0227 681 PRO A C   
3034 O O   . PRO A 385 ? 1.0029 0.5899 0.6861 -0.0104 -0.1050 -0.0255 681 PRO A O   
3035 C CB  . PRO A 385 ? 1.1258 0.6761 0.7654 0.0665  -0.0983 -0.0291 681 PRO A CB  
3036 C CG  . PRO A 385 ? 1.1427 0.7647 0.8266 0.1105  -0.0887 -0.0321 681 PRO A CG  
3037 C CD  . PRO A 385 ? 1.0493 0.7456 0.7986 0.0975  -0.0828 -0.0316 681 PRO A CD  
3038 N N   . PRO A 386 ? 0.9742 0.5306 0.6410 -0.0544 -0.1137 -0.0184 682 PRO A N   
3039 C CA  . PRO A 386 ? 1.0293 0.5685 0.6739 -0.0996 -0.1224 -0.0163 682 PRO A CA  
3040 C C   . PRO A 386 ? 1.1404 0.5719 0.6811 -0.1049 -0.1296 -0.0210 682 PRO A C   
3041 O O   . PRO A 386 ? 1.1531 0.5610 0.6618 -0.1508 -0.1389 -0.0194 682 PRO A O   
3042 C CB  . PRO A 386 ? 1.0004 0.5560 0.6567 -0.1407 -0.1270 -0.0096 682 PRO A CB  
3043 C CG  . PRO A 386 ? 0.9797 0.4805 0.5946 -0.1176 -0.1247 -0.0103 682 PRO A CG  
3044 C CD  . PRO A 386 ? 0.9757 0.5208 0.6370 -0.0634 -0.1149 -0.0145 682 PRO A CD  
3045 N N   . MET A 387 ? 1.1974 0.5628 0.6792 -0.0597 -0.1262 -0.0270 683 MET A N   
3046 C CA  . MET A 387 ? 1.3008 0.5589 0.6781 -0.0529 -0.1316 -0.0333 683 MET A CA  
3047 C C   . MET A 387 ? 1.2774 0.5362 0.6466 0.0142  -0.1221 -0.0403 683 MET A C   
3048 O O   . MET A 387 ? 1.1967 0.5182 0.6199 0.0510  -0.1134 -0.0397 683 MET A O   
3049 C CB  . MET A 387 ? 1.5216 0.6556 0.7881 -0.0707 -0.1402 -0.0329 683 MET A CB  
3050 C CG  . MET A 387 ? 1.5488 0.6399 0.7784 -0.0155 -0.1351 -0.0348 683 MET A CG  
3051 S SD  . MET A 387 ? 1.7932 0.7316 0.8881 -0.0377 -0.1451 -0.0321 683 MET A SD  
3052 C CE  . MET A 387 ? 1.8588 0.6916 0.8336 -0.0336 -0.1495 -0.0343 683 MET A CE  
3053 N N   . SER A 388 ? 1.4205 0.6185 0.7237 0.0286  -0.1237 -0.0470 684 SER A N   
3054 C CA  . SER A 388 ? 1.4317 0.6250 0.7112 0.0954  -0.1144 -0.0543 684 SER A CA  
3055 C C   . SER A 388 ? 1.2791 0.6084 0.6717 0.1198  -0.1018 -0.0524 684 SER A C   
3056 O O   . SER A 388 ? 1.3258 0.6865 0.7246 0.1734  -0.0929 -0.0556 684 SER A O   
3057 C CB  . SER A 388 ? 1.5256 0.6342 0.7206 0.1418  -0.1147 -0.0576 684 SER A CB  
3058 O OG  . SER A 388 ? 1.7026 0.6787 0.7900 0.1085  -0.1269 -0.0574 684 SER A OG  
3059 N N   . GLY A 389 ? 1.1453 0.5554 0.6225 0.0796  -0.1016 -0.0468 685 GLY A N   
3060 C CA  . GLY A 389 ? 0.9966 0.5237 0.5738 0.0919  -0.0908 -0.0437 685 GLY A CA  
3061 C C   . GLY A 389 ? 1.0472 0.6086 0.6234 0.1420  -0.0794 -0.0491 685 GLY A C   
3062 O O   . GLY A 389 ? 1.0263 0.6507 0.6404 0.1731  -0.0709 -0.0493 685 GLY A O   
3063 N N   . SER A 390 ? 1.0874 0.6129 0.6178 0.1501  -0.0790 -0.0538 686 SER A N   
3064 C CA  . SER A 390 ? 1.0930 0.6738 0.6360 0.1917  -0.0662 -0.0576 686 SER A CA  
3065 C C   . SER A 390 ? 1.2164 0.7682 0.6976 0.2552  -0.0610 -0.0649 686 SER A C   
3066 O O   . SER A 390 ? 1.2408 0.8586 0.7380 0.2947  -0.0489 -0.0679 686 SER A O   
3067 C CB  . SER A 390 ? 1.1025 0.6630 0.6209 0.1803  -0.0664 -0.0599 686 SER A CB  
3068 O OG  . SER A 390 ? 1.1686 0.6110 0.5852 0.1816  -0.0763 -0.0661 686 SER A OG  
3069 N N   . ILE A 391 ? 1.2942 0.7511 0.7005 0.2683  -0.0695 -0.0674 687 ILE A N   
3070 C CA  . ILE A 391 ? 1.2904 0.7255 0.6391 0.3368  -0.0649 -0.0734 687 ILE A CA  
3071 C C   . ILE A 391 ? 1.2978 0.8059 0.7048 0.3500  -0.0622 -0.0691 687 ILE A C   
3072 O O   . ILE A 391 ? 1.3792 0.8751 0.7414 0.4076  -0.0603 -0.0729 687 ILE A O   
3073 C CB  . ILE A 391 ? 1.5005 0.7752 0.7123 0.3556  -0.0751 -0.0793 687 ILE A CB  
3074 C CG1 . ILE A 391 ? 1.5531 0.7547 0.7434 0.3066  -0.0880 -0.0737 687 ILE A CG1 
3075 C CG2 . ILE A 391 ? 1.5949 0.7946 0.7372 0.3485  -0.0776 -0.0856 687 ILE A CG2 
3076 C CD1 . ILE A 391 ? 1.7068 0.7484 0.7545 0.3305  -0.0972 -0.0782 687 ILE A CD1 
3077 N N   . THR A 392 ? 1.2317 0.8148 0.7335 0.3009  -0.0625 -0.0616 688 THR A N   
3078 C CA  . THR A 392 ? 1.1619 0.8370 0.7331 0.3098  -0.0582 -0.0581 688 THR A CA  
3079 C C   . THR A 392 ? 1.0473 0.8529 0.7068 0.3048  -0.0464 -0.0564 688 THR A C   
3080 O O   . THR A 392 ? 0.9965 0.8182 0.6805 0.2757  -0.0435 -0.0548 688 THR A O   
3081 C CB  . THR A 392 ? 1.1912 0.8538 0.7976 0.2605  -0.0665 -0.0513 688 THR A CB  
3082 O OG1 . THR A 392 ? 1.1001 0.8058 0.7736 0.2067  -0.0664 -0.0463 688 THR A OG1 
3083 C CG2 . THR A 392 ? 1.2534 0.7848 0.7690 0.2507  -0.0782 -0.0515 688 THR A CG2 
3084 N N   . PRO A 393 ? 1.0784 0.9784 0.7812 0.3313  -0.0397 -0.0564 689 PRO A N   
3085 C CA  . PRO A 393 ? 0.9978 1.0206 0.7712 0.3244  -0.0277 -0.0550 689 PRO A CA  
3086 C C   . PRO A 393 ? 0.8473 0.9113 0.6958 0.2614  -0.0278 -0.0480 689 PRO A C   
3087 O O   . PRO A 393 ? 0.8602 0.9945 0.7501 0.2438  -0.0189 -0.0459 689 PRO A O   
3088 C CB  . PRO A 393 ? 1.0787 1.1884 0.8698 0.3670  -0.0232 -0.0570 689 PRO A CB  
3089 C CG  . PRO A 393 ? 1.0905 1.1350 0.8569 0.3698  -0.0343 -0.0559 689 PRO A CG  
3090 C CD  . PRO A 393 ? 1.1925 1.0941 0.8757 0.3691  -0.0429 -0.0576 689 PRO A CD  
3091 N N   . VAL A 394 ? 0.8180 0.8391 0.6796 0.2283  -0.0370 -0.0442 690 VAL A N   
3092 C CA  . VAL A 394 ? 0.6804 0.7355 0.6047 0.1765  -0.0371 -0.0381 690 VAL A CA  
3093 C C   . VAL A 394 ? 0.6908 0.7114 0.6097 0.1485  -0.0379 -0.0356 690 VAL A C   
3094 O O   . VAL A 394 ? 0.6874 0.7490 0.6511 0.1173  -0.0343 -0.0310 690 VAL A O   
3095 C CB  . VAL A 394 ? 0.6451 0.6719 0.5843 0.1537  -0.0459 -0.0350 690 VAL A CB  
3096 C CG1 . VAL A 394 ? 0.7178 0.7959 0.6748 0.1756  -0.0448 -0.0365 690 VAL A CG1 
3097 C CG2 . VAL A 394 ? 0.6955 0.6214 0.5767 0.1512  -0.0558 -0.0354 690 VAL A CG2 
3098 N N   . PHE A 395 ? 0.8369 0.7805 0.6951 0.1599  -0.0428 -0.0388 691 PHE A N   
3099 C CA  . PHE A 395 ? 0.7183 0.6358 0.5690 0.1355  -0.0443 -0.0368 691 PHE A CA  
3100 C C   . PHE A 395 ? 0.7660 0.7505 0.6437 0.1383  -0.0325 -0.0358 691 PHE A C   
3101 O O   . PHE A 395 ? 0.7545 0.7461 0.6535 0.1084  -0.0323 -0.0310 691 PHE A O   
3102 C CB  . PHE A 395 ? 0.8483 0.6724 0.6187 0.1496  -0.0513 -0.0420 691 PHE A CB  
3103 C CG  . PHE A 395 ? 0.8687 0.6639 0.6258 0.1232  -0.0551 -0.0405 691 PHE A CG  
3104 C CD1 . PHE A 395 ? 0.8858 0.6385 0.6380 0.0842  -0.0671 -0.0370 691 PHE A CD1 
3105 C CD2 . PHE A 395 ? 0.8638 0.6797 0.6109 0.1381  -0.0469 -0.0426 691 PHE A CD2 
3106 C CE1 . PHE A 395 ? 0.9305 0.6648 0.6698 0.0615  -0.0720 -0.0356 691 PHE A CE1 
3107 C CE2 . PHE A 395 ? 0.9283 0.7176 0.6607 0.1150  -0.0512 -0.0411 691 PHE A CE2 
3108 C CZ  . PHE A 395 ? 0.9086 0.6574 0.6372 0.0776  -0.0644 -0.0377 691 PHE A CZ  
3109 N N   . HIS A 396 ? 0.7876 0.8245 0.6614 0.1745  -0.0226 -0.0398 692 HIS A N   
3110 C CA  . HIS A 396 ? 0.7590 0.8652 0.6501 0.1785  -0.0099 -0.0391 692 HIS A CA  
3111 C C   . HIS A 396 ? 0.7389 0.9395 0.6937 0.1544  -0.0021 -0.0340 692 HIS A C   
3112 O O   . HIS A 396 ? 0.7064 0.9739 0.6772 0.1498  0.0093  -0.0322 692 HIS A O   
3113 C CB  . HIS A 396 ? 0.9391 1.0570 0.7840 0.2341  -0.0028 -0.0467 692 HIS A CB  
3114 C CG  . HIS A 396 ? 1.0402 1.0485 0.8066 0.2577  -0.0112 -0.0526 692 HIS A CG  
3115 N ND1 . HIS A 396 ? 1.0277 0.9791 0.7625 0.2411  -0.0142 -0.0529 692 HIS A ND1 
3116 C CD2 . HIS A 396 ? 1.1018 1.0380 0.8080 0.2917  -0.0186 -0.0582 692 HIS A CD2 
3117 C CE1 . HIS A 396 ? 1.1609 1.0114 0.8187 0.2611  -0.0230 -0.0590 692 HIS A CE1 
3118 N NE2 . HIS A 396 ? 1.1405 0.9746 0.7762 0.2920  -0.0256 -0.0621 692 HIS A NE2 
3119 N N   . GLN A 397 ? 0.6635 0.8673 0.6495 0.1352  -0.0082 -0.0316 693 GLN A N   
3120 C CA  . GLN A 397 ? 0.6676 0.9494 0.7046 0.1103  -0.0030 -0.0280 693 GLN A CA  
3121 C C   . GLN A 397 ? 0.5658 0.8203 0.6254 0.0628  -0.0064 -0.0211 693 GLN A C   
3122 O O   . GLN A 397 ? 0.6043 0.8028 0.6640 0.0515  -0.0164 -0.0198 693 GLN A O   
3123 C CB  . GLN A 397 ? 0.6531 0.9524 0.7017 0.1257  -0.0079 -0.0309 693 GLN A CB  
3124 C CG  . GLN A 397 ? 0.5842 0.9634 0.6800 0.0988  -0.0041 -0.0284 693 GLN A CG  
3125 C CD  . GLN A 397 ? 0.6310 1.1139 0.7414 0.1037  0.0082  -0.0290 693 GLN A CD  
3126 O OE1 . GLN A 397 ? 0.5979 1.1315 0.6964 0.1479  0.0120  -0.0338 693 GLN A OE1 
3127 N NE2 . GLN A 397 ? 0.6455 1.1619 0.7770 0.0587  0.0147  -0.0236 693 GLN A NE2 
3128 N N   . GLU A 398 ? 0.6308 0.9235 0.7036 0.0368  0.0021  -0.0164 694 GLU A N   
3129 C CA  . GLU A 398 ? 0.6273 0.8963 0.7152 -0.0046 -0.0005 -0.0096 694 GLU A CA  
3130 C C   . GLU A 398 ? 0.6437 0.9291 0.7580 -0.0191 -0.0043 -0.0100 694 GLU A C   
3131 O O   . GLU A 398 ? 0.6535 1.0006 0.7832 -0.0104 -0.0008 -0.0136 694 GLU A O   
3132 C CB  . GLU A 398 ? 0.5474 0.8528 0.6351 -0.0319 0.0103  -0.0041 694 GLU A CB  
3133 C CG  . GLU A 398 ? 0.5810 0.8575 0.6399 -0.0238 0.0132  -0.0021 694 GLU A CG  
3134 C CD  . GLU A 398 ? 0.7075 1.0313 0.7625 -0.0473 0.0260  0.0032  694 GLU A CD  
3135 O OE1 . GLU A 398 ? 0.7453 1.0578 0.7764 -0.0383 0.0304  0.0044  694 GLU A OE1 
3136 O OE2 . GLU A 398 ? 0.7567 1.1267 0.8281 -0.0781 0.0316  0.0064  694 GLU A OE2 
3137 N N   . MET A 399 ? 0.6174 0.8504 0.7347 -0.0386 -0.0120 -0.0066 695 MET A N   
3138 C CA  . MET A 399 ? 0.6297 0.8659 0.7658 -0.0518 -0.0163 -0.0074 695 MET A CA  
3139 C C   . MET A 399 ? 0.6688 0.8646 0.7998 -0.0819 -0.0182 -0.0018 695 MET A C   
3140 O O   . MET A 399 ? 0.7033 0.8484 0.8204 -0.0796 -0.0231 0.0017  695 MET A O   
3141 C CB  . MET A 399 ? 0.5651 0.7679 0.7023 -0.0304 -0.0257 -0.0109 695 MET A CB  
3142 C CG  . MET A 399 ? 0.5488 0.7673 0.6760 0.0040  -0.0260 -0.0163 695 MET A CG  
3143 S SD  . MET A 399 ? 0.5835 0.7361 0.6932 0.0194  -0.0376 -0.0180 695 MET A SD  
3144 C CE  . MET A 399 ? 0.5439 0.6927 0.6168 0.0621  -0.0364 -0.0237 695 MET A CE  
3145 N N   . LEU A 400 ? 0.5764 0.7920 0.7133 -0.1084 -0.0157 -0.0013 696 LEU A N   
3146 C CA  . LEU A 400 ? 0.5987 0.7616 0.7186 -0.1323 -0.0185 0.0028  696 LEU A CA  
3147 C C   . LEU A 400 ? 0.6726 0.8091 0.8021 -0.1220 -0.0268 -0.0003 696 LEU A C   
3148 O O   . LEU A 400 ? 0.6059 0.7774 0.7542 -0.1188 -0.0279 -0.0053 696 LEU A O   
3149 C CB  . LEU A 400 ? 0.6289 0.8118 0.7361 -0.1720 -0.0120 0.0048  696 LEU A CB  
3150 C CG  . LEU A 400 ? 0.6097 0.8282 0.7053 -0.1914 -0.0020 0.0089  696 LEU A CG  
3151 C CD1 . LEU A 400 ? 0.6491 0.8943 0.7311 -0.2392 0.0034  0.0104  696 LEU A CD1 
3152 C CD2 . LEU A 400 ? 0.7310 0.8901 0.7966 -0.1889 -0.0015 0.0158  696 LEU A CD2 
3153 N N   . ASN A 401 ? 0.6880 0.7692 0.8040 -0.1146 -0.0325 0.0028  697 ASN A N   
3154 C CA  . ASN A 401 ? 0.6187 0.6773 0.7405 -0.1052 -0.0391 0.0007  697 ASN A CA  
3155 C C   . ASN A 401 ? 0.7318 0.7479 0.8260 -0.1231 -0.0390 0.0023  697 ASN A C   
3156 O O   . ASN A 401 ? 0.7179 0.6908 0.7803 -0.1284 -0.0384 0.0076  697 ASN A O   
3157 C CB  . ASN A 401 ? 0.5830 0.6203 0.7072 -0.0827 -0.0458 0.0027  697 ASN A CB  
3158 C CG  . ASN A 401 ? 0.6257 0.6623 0.7635 -0.0722 -0.0511 -0.0002 697 ASN A CG  
3159 O OD1 . ASN A 401 ? 0.5426 0.5960 0.6906 -0.0772 -0.0501 -0.0045 697 ASN A OD1 
3160 N ND2 . ASN A 401 ? 0.5727 0.5973 0.7106 -0.0589 -0.0568 0.0022  697 ASN A ND2 
3161 N N   . TYR A 402 ? 0.7246 0.7461 0.8233 -0.1310 -0.0403 -0.0024 698 TYR A N   
3162 C CA  . TYR A 402 ? 0.6659 0.6350 0.7289 -0.1454 -0.0413 -0.0025 698 TYR A CA  
3163 C C   . TYR A 402 ? 0.7353 0.7113 0.8120 -0.1376 -0.0452 -0.0086 698 TYR A C   
3164 O O   . TYR A 402 ? 0.6173 0.6418 0.7298 -0.1272 -0.0464 -0.0120 698 TYR A O   
3165 C CB  . TYR A 402 ? 0.7985 0.7617 0.8322 -0.1855 -0.0358 -0.0012 698 TYR A CB  
3166 C CG  . TYR A 402 ? 0.7905 0.8338 0.8552 -0.2047 -0.0316 -0.0046 698 TYR A CG  
3167 C CD1 . TYR A 402 ? 0.7533 0.8266 0.8277 -0.2199 -0.0334 -0.0107 698 TYR A CD1 
3168 C CD2 . TYR A 402 ? 0.6726 0.7661 0.7544 -0.2047 -0.0259 -0.0020 698 TYR A CD2 
3169 C CE1 . TYR A 402 ? 0.7255 0.8833 0.8282 -0.2330 -0.0304 -0.0136 698 TYR A CE1 
3170 C CE2 . TYR A 402 ? 0.6662 0.8440 0.7750 -0.2153 -0.0217 -0.0053 698 TYR A CE2 
3171 C CZ  . TYR A 402 ? 0.7299 0.9426 0.8501 -0.2287 -0.0244 -0.0109 698 TYR A CZ  
3172 O OH  . TYR A 402 ? 0.6603 0.9673 0.8076 -0.2354 -0.0213 -0.0140 698 TYR A OH  
3173 N N   . ARG A 403 ? 0.7447 0.6651 0.7856 -0.1396 -0.0472 -0.0097 699 ARG A N   
3174 C CA  . ARG A 403 ? 0.8165 0.7345 0.8642 -0.1261 -0.0508 -0.0151 699 ARG A CA  
3175 C C   . ARG A 403 ? 0.8291 0.7401 0.8567 -0.1574 -0.0505 -0.0207 699 ARG A C   
3176 O O   . ARG A 403 ? 0.9250 0.7729 0.8991 -0.1762 -0.0502 -0.0210 699 ARG A O   
3177 C CB  . ARG A 403 ? 0.9767 0.8413 0.9955 -0.0982 -0.0535 -0.0133 699 ARG A CB  
3178 C CG  . ARG A 403 ? 1.0447 0.9229 1.0801 -0.0713 -0.0551 -0.0075 699 ARG A CG  
3179 C CD  . ARG A 403 ? 1.1475 1.0812 1.2299 -0.0556 -0.0574 -0.0088 699 ARG A CD  
3180 N NE  . ARG A 403 ? 1.3181 1.2464 1.3961 -0.0297 -0.0598 -0.0092 699 ARG A NE  
3181 C CZ  . ARG A 403 ? 1.3854 1.3520 1.4921 -0.0213 -0.0611 -0.0112 699 ARG A CZ  
3182 N NH1 . ARG A 403 ? 1.3929 1.3943 1.5290 -0.0344 -0.0610 -0.0130 699 ARG A NH1 
3183 N NH2 . ARG A 403 ? 1.4119 1.3821 1.5134 0.0022  -0.0621 -0.0111 699 ARG A NH2 
3184 N N   . LEU A 404 ? 0.8210 0.7935 0.8851 -0.1636 -0.0512 -0.0251 700 LEU A N   
3185 C CA  . LEU A 404 ? 0.7898 0.7674 0.8401 -0.1909 -0.0529 -0.0313 700 LEU A CA  
3186 C C   . LEU A 404 ? 0.7761 0.7396 0.8285 -0.1701 -0.0568 -0.0364 700 LEU A C   
3187 O O   . LEU A 404 ? 0.6927 0.6716 0.7727 -0.1379 -0.0577 -0.0350 700 LEU A O   
3188 C CB  . LEU A 404 ? 0.7287 0.7924 0.8155 -0.2077 -0.0520 -0.0332 700 LEU A CB  
3189 C CG  . LEU A 404 ? 0.7392 0.8402 0.8293 -0.2300 -0.0467 -0.0290 700 LEU A CG  
3190 C CD1 . LEU A 404 ? 0.6028 0.8018 0.7287 -0.2389 -0.0464 -0.0322 700 LEU A CD1 
3191 C CD2 . LEU A 404 ? 0.8972 0.9412 0.9323 -0.2715 -0.0446 -0.0271 700 LEU A CD2 
3192 N N   . THR A 405 ? 0.7466 0.6809 0.7652 -0.1926 -0.0592 -0.0423 701 THR A N   
3193 C CA  . THR A 405 ? 0.8320 0.7611 0.8523 -0.1761 -0.0625 -0.0480 701 THR A CA  
3194 C C   . THR A 405 ? 0.7770 0.7569 0.8101 -0.2029 -0.0660 -0.0540 701 THR A C   
3195 O O   . THR A 405 ? 0.7357 0.7344 0.7570 -0.2417 -0.0662 -0.0549 701 THR A O   
3196 C CB  . THR A 405 ? 0.9542 0.7918 0.9124 -0.1692 -0.0631 -0.0509 701 THR A CB  
3197 O OG1 . THR A 405 ? 0.9273 0.7660 0.8936 -0.1401 -0.0645 -0.0549 701 THR A OG1 
3198 C CG2 . THR A 405 ? 1.0019 0.7893 0.9015 -0.2132 -0.0651 -0.0560 701 THR A CG2 
3199 N N   . PRO A 406 ? 0.7758 0.7865 0.8332 -0.1846 -0.0691 -0.0577 702 PRO A N   
3200 C CA  . PRO A 406 ? 0.7053 0.7132 0.7808 -0.1462 -0.0689 -0.0568 702 PRO A CA  
3201 C C   . PRO A 406 ? 0.6649 0.6983 0.7753 -0.1209 -0.0662 -0.0493 702 PRO A C   
3202 O O   . PRO A 406 ? 0.6055 0.6780 0.7378 -0.1272 -0.0653 -0.0462 702 PRO A O   
3203 C CB  . PRO A 406 ? 0.6814 0.7378 0.7777 -0.1471 -0.0732 -0.0613 702 PRO A CB  
3204 C CG  . PRO A 406 ? 0.6993 0.7590 0.7710 -0.1857 -0.0768 -0.0674 702 PRO A CG  
3205 C CD  . PRO A 406 ? 0.7539 0.8055 0.8121 -0.2123 -0.0739 -0.0641 702 PRO A CD  
3206 N N   . SER A 407 ? 0.6253 0.6413 0.7385 -0.0934 -0.0649 -0.0467 703 SER A N   
3207 C CA  . SER A 407 ? 0.6483 0.6817 0.7857 -0.0761 -0.0633 -0.0398 703 SER A CA  
3208 C C   . SER A 407 ? 0.5543 0.5966 0.7033 -0.0537 -0.0631 -0.0377 703 SER A C   
3209 O O   . SER A 407 ? 0.6217 0.6497 0.7563 -0.0456 -0.0627 -0.0412 703 SER A O   
3210 C CB  . SER A 407 ? 0.7194 0.7176 0.8375 -0.0749 -0.0611 -0.0358 703 SER A CB  
3211 O OG  . SER A 407 ? 0.8776 0.8321 0.9647 -0.0593 -0.0605 -0.0372 703 SER A OG  
3212 N N   . PHE A 408 ? 0.5230 0.5887 0.6936 -0.0460 -0.0633 -0.0321 704 PHE A N   
3213 C CA  . PHE A 408 ? 0.5955 0.6729 0.7740 -0.0323 -0.0629 -0.0282 704 PHE A CA  
3214 C C   . PHE A 408 ? 0.6193 0.6896 0.7937 -0.0227 -0.0618 -0.0239 704 PHE A C   
3215 O O   . PHE A 408 ? 0.6005 0.6673 0.7775 -0.0270 -0.0625 -0.0208 704 PHE A O   
3216 C CB  . PHE A 408 ? 0.5056 0.6040 0.6978 -0.0344 -0.0649 -0.0244 704 PHE A CB  
3217 C CG  . PHE A 408 ? 0.5550 0.6624 0.7470 -0.0362 -0.0668 -0.0276 704 PHE A CG  
3218 C CD1 . PHE A 408 ? 0.5776 0.6953 0.7723 -0.0387 -0.0689 -0.0294 704 PHE A CD1 
3219 C CD2 . PHE A 408 ? 0.5682 0.6794 0.7560 -0.0327 -0.0664 -0.0284 704 PHE A CD2 
3220 C CE1 . PHE A 408 ? 0.5368 0.6694 0.7299 -0.0353 -0.0718 -0.0320 704 PHE A CE1 
3221 C CE2 . PHE A 408 ? 0.4399 0.5585 0.6242 -0.0323 -0.0692 -0.0308 704 PHE A CE2 
3222 C CZ  . PHE A 408 ? 0.4629 0.5925 0.6496 -0.0324 -0.0724 -0.0326 704 PHE A CZ  
3223 N N   . GLU A 409 ? 0.5021 0.5748 0.6687 -0.0068 -0.0601 -0.0236 705 GLU A N   
3224 C CA  . GLU A 409 ? 0.5756 0.6510 0.7368 0.0089  -0.0598 -0.0195 705 GLU A CA  
3225 C C   . GLU A 409 ? 0.6422 0.7674 0.8218 0.0148  -0.0598 -0.0145 705 GLU A C   
3226 O O   . GLU A 409 ? 0.7432 0.8904 0.9304 0.0110  -0.0582 -0.0150 705 GLU A O   
3227 C CB  . GLU A 409 ? 0.6366 0.6736 0.7626 0.0291  -0.0580 -0.0232 705 GLU A CB  
3228 C CG  . GLU A 409 ? 0.8467 0.8272 0.9429 0.0145  -0.0583 -0.0280 705 GLU A CG  
3229 C CD  . GLU A 409 ? 0.9905 0.9592 1.0878 -0.0004 -0.0595 -0.0241 705 GLU A CD  
3230 O OE1 . GLU A 409 ? 1.0090 1.0056 1.1267 0.0045  -0.0607 -0.0183 705 GLU A OE1 
3231 O OE2 . GLU A 409 ? 1.0692 1.0023 1.1443 -0.0198 -0.0593 -0.0269 705 GLU A OE2 
3232 N N   . TYR A 410 ? 0.5398 0.6856 0.7246 0.0207  -0.0617 -0.0091 706 TYR A N   
3233 C CA  . TYR A 410 ? 0.4851 0.6890 0.6848 0.0235  -0.0619 -0.0042 706 TYR A CA  
3234 C C   . TYR A 410 ? 0.4578 0.6818 0.6470 0.0539  -0.0580 -0.0061 706 TYR A C   
3235 O O   . TYR A 410 ? 0.6356 0.8163 0.7979 0.0765  -0.0565 -0.0107 706 TYR A O   
3236 C CB  . TYR A 410 ? 0.5343 0.7630 0.7417 0.0193  -0.0664 0.0018  706 TYR A CB  
3237 C CG  . TYR A 410 ? 0.6157 0.8239 0.8269 -0.0081 -0.0699 0.0033  706 TYR A CG  
3238 C CD1 . TYR A 410 ? 0.7364 0.9068 0.9394 -0.0084 -0.0714 0.0024  706 TYR A CD1 
3239 C CD2 . TYR A 410 ? 0.6519 0.8732 0.8672 -0.0325 -0.0713 0.0055  706 TYR A CD2 
3240 C CE1 . TYR A 410 ? 0.7815 0.9347 0.9839 -0.0273 -0.0738 0.0030  706 TYR A CE1 
3241 C CE2 . TYR A 410 ? 0.7476 0.9389 0.9545 -0.0510 -0.0746 0.0060  706 TYR A CE2 
3242 C CZ  . TYR A 410 ? 0.8488 1.0097 1.0511 -0.0458 -0.0756 0.0044  706 TYR A CZ  
3243 O OH  . TYR A 410 ? 0.8413 0.9746 1.0317 -0.0582 -0.0780 0.0042  706 TYR A OH  
3244 N N   . GLN A 411 ? 0.4769 0.7653 0.6815 0.0542  -0.0562 -0.0026 707 GLN A N   
3245 C CA  . GLN A 411 ? 0.6110 0.9306 0.8060 0.0877  -0.0513 -0.0046 707 GLN A CA  
3246 C C   . GLN A 411 ? 0.6284 1.0433 0.8462 0.0857  -0.0510 0.0024  707 GLN A C   
3247 O O   . GLN A 411 ? 0.6392 1.0833 0.8753 0.0484  -0.0539 0.0078  707 GLN A O   
3248 C CB  . GLN A 411 ? 0.7018 0.9989 0.8867 0.0875  -0.0464 -0.0106 707 GLN A CB  
3249 C CG  . GLN A 411 ? 0.7322 1.0725 0.9371 0.0591  -0.0445 -0.0070 707 GLN A CG  
3250 C CD  . GLN A 411 ? 0.7591 1.0686 0.9513 0.0584  -0.0408 -0.0130 707 GLN A CD  
3251 O OE1 . GLN A 411 ? 0.8173 1.0966 0.9862 0.0853  -0.0380 -0.0200 707 GLN A OE1 
3252 N NE2 . GLN A 411 ? 0.7817 1.0915 0.9818 0.0281  -0.0416 -0.0104 707 GLN A NE2 
3253 N N   . PRO A 412 ? 0.7042 1.1695 0.9164 0.1250  -0.0480 0.0026  708 PRO A N   
3254 C CA  . PRO A 412 ? 0.7508 1.3272 0.9877 0.1222  -0.0478 0.0097  708 PRO A CA  
3255 C C   . PRO A 412 ? 0.7589 1.3808 1.0137 0.0824  -0.0440 0.0129  708 PRO A C   
3256 O O   . PRO A 412 ? 0.7588 1.3389 1.0041 0.0758  -0.0395 0.0087  708 PRO A O   
3257 C CB  . PRO A 412 ? 0.8281 1.4444 1.0486 0.1821  -0.0432 0.0072  708 PRO A CB  
3258 C CG  . PRO A 412 ? 0.8799 1.3886 1.0594 0.2143  -0.0446 0.0006  708 PRO A CG  
3259 C CD  . PRO A 412 ? 0.8150 1.2364 0.9909 0.1753  -0.0452 -0.0036 708 PRO A CD  
3260 N N   . ASP A 413 ? 0.7579 1.4626 1.0334 0.0521  -0.0465 0.0208  709 ASP A N   
3261 C CA  . ASP A 413 ? 0.7841 1.5398 1.0680 0.0140  -0.0421 0.0253  709 ASP A CA  
3262 C C   . ASP A 413 ? 0.7824 1.6003 1.0674 0.0496  -0.0320 0.0230  709 ASP A C   
3263 O O   . ASP A 413 ? 0.7575 1.6309 1.0444 0.0979  -0.0301 0.0218  709 ASP A O   
3264 C CB  . ASP A 413 ? 0.8763 1.7125 1.1748 -0.0304 -0.0472 0.0344  709 ASP A CB  
3265 C CG  . ASP A 413 ? 0.9539 1.7152 1.2394 -0.0775 -0.0555 0.0364  709 ASP A CG  
3266 O OD1 . ASP A 413 ? 0.9623 1.6275 1.2308 -0.0839 -0.0550 0.0323  709 ASP A OD1 
3267 O OD2 . ASP A 413 ? 0.9654 1.7555 1.2496 -0.1050 -0.0616 0.0413  709 ASP A OD2 
3268 N N   . PRO A 414 ? 0.7857 1.5923 1.0642 0.0319  -0.0255 0.0223  710 PRO A N   
3269 C CA  . PRO A 414 ? 0.8335 1.6833 1.1068 0.0712  -0.0152 0.0182  710 PRO A CA  
3270 C C   . PRO A 414 ? 0.8704 1.8419 1.1521 0.0832  -0.0094 0.0236  710 PRO A C   
3271 O O   . PRO A 414 ? 0.9580 1.9538 1.2246 0.1373  -0.0028 0.0187  710 PRO A O   
3272 C CB  . PRO A 414 ? 0.7991 1.6108 1.0622 0.0367  -0.0107 0.0184  710 PRO A CB  
3273 C CG  . PRO A 414 ? 0.7628 1.4808 1.0182 -0.0027 -0.0196 0.0193  710 PRO A CG  
3274 C CD  . PRO A 414 ? 0.8163 1.5599 1.0848 -0.0188 -0.0275 0.0245  710 PRO A CD  
3275 N N   . TRP A 415 ? 0.8274 1.8437 1.1112 0.0325  -0.0114 0.0325  711 TRP A N   
3276 C CA  . TRP A 415 ? 0.8448 1.9566 1.1197 0.0360  -0.0061 0.0374  711 TRP A CA  
3277 C C   . TRP A 415 ? 0.8098 1.9518 1.0800 0.0831  -0.0091 0.0358  711 TRP A C   
3278 O O   . TRP A 415 ? 0.8156 2.0428 1.0757 0.1000  -0.0047 0.0385  711 TRP A O   
3279 C CB  . TRP A 415 ? 0.8269 1.9711 1.0966 -0.0356 -0.0085 0.0471  711 TRP A CB  
3280 C CG  . TRP A 415 ? 0.7279 1.8225 0.9988 -0.0716 -0.0194 0.0498  711 TRP A CG  
3281 C CD1 . TRP A 415 ? 0.7240 1.8509 0.9942 -0.0728 -0.0252 0.0525  711 TRP A CD1 
3282 C CD2 . TRP A 415 ? 0.6825 1.6864 0.9510 -0.1100 -0.0260 0.0499  711 TRP A CD2 
3283 N NE1 . TRP A 415 ? 0.6272 1.6870 0.8948 -0.1096 -0.0347 0.0539  711 TRP A NE1 
3284 C CE2 . TRP A 415 ? 0.6676 1.6500 0.9322 -0.1319 -0.0356 0.0522  711 TRP A CE2 
3285 C CE3 . TRP A 415 ? 0.7106 1.6506 0.9764 -0.1266 -0.0252 0.0481  711 TRP A CE3 
3286 C CZ2 . TRP A 415 ? 0.7011 1.5966 0.9558 -0.1672 -0.0441 0.0524  711 TRP A CZ2 
3287 C CZ3 . TRP A 415 ? 0.6499 1.5061 0.9061 -0.1617 -0.0341 0.0488  711 TRP A CZ3 
3288 C CH2 . TRP A 415 ? 0.7284 1.5612 0.9777 -0.1804 -0.0433 0.0506  711 TRP A CH2 
3289 N N   . ASN A 416 ? 0.7736 1.8505 1.0474 0.1050  -0.0169 0.0319  712 ASN A N   
3290 C CA  . ASN A 416 ? 0.8692 1.9618 1.1305 0.1562  -0.0195 0.0302  712 ASN A CA  
3291 C C   . ASN A 416 ? 0.8738 1.9351 1.1091 0.2284  -0.0142 0.0219  712 ASN A C   
3292 O O   . ASN A 416 ? 0.9156 1.9970 1.1268 0.2781  -0.0141 0.0207  712 ASN A O   
3293 C CB  . ASN A 416 ? 0.8729 1.9058 1.1420 0.1474  -0.0307 0.0305  712 ASN A CB  
3294 C CG  . ASN A 416 ? 0.9372 1.9871 1.2204 0.0792  -0.0369 0.0377  712 ASN A CG  
3295 O OD1 . ASN A 416 ? 1.0250 2.1462 1.3060 0.0454  -0.0335 0.0435  712 ASN A OD1 
3296 N ND2 . ASN A 416 ? 0.9023 1.8831 1.1930 0.0586  -0.0463 0.0372  712 ASN A ND2 
3297 N N   . THR A 417 ? 0.8040 1.8118 1.0365 0.2355  -0.0100 0.0160  713 THR A N   
3298 C CA  . THR A 417 ? 0.8433 1.7887 1.0406 0.2999  -0.0065 0.0065  713 THR A CA  
3299 C C   . THR A 417 ? 0.9195 1.8916 1.1013 0.3186  0.0044  0.0025  713 THR A C   
3300 O O   . THR A 417 ? 0.9534 1.8897 1.0918 0.3784  0.0081  -0.0048 713 THR A O   
3301 C CB  . THR A 417 ? 0.8484 1.6858 1.0462 0.2991  -0.0127 0.0006  713 THR A CB  
3302 O OG1 . THR A 417 ? 0.8165 1.6400 1.0405 0.2382  -0.0127 0.0025  713 THR A OG1 
3303 C CG2 . THR A 417 ? 0.8078 1.6079 1.0079 0.2979  -0.0236 0.0034  713 THR A CG2 
3304 N N   . HIS A 418 ? 0.9094 1.9363 1.1171 0.2692  0.0091  0.0074  714 HIS A N   
3305 C CA  . HIS A 418 ? 0.9212 1.9661 1.1171 0.2804  0.0192  0.0038  714 HIS A CA  
3306 C C   . HIS A 418 ? 0.9979 2.1232 1.1677 0.3202  0.0251  0.0050  714 HIS A C   
3307 O O   . HIS A 418 ? 1.0164 2.2298 1.1956 0.3023  0.0236  0.0132  714 HIS A O   
3308 C CB  . HIS A 418 ? 0.8472 1.9236 1.0728 0.2111  0.0217  0.0104  714 HIS A CB  
3309 C CG  . HIS A 418 ? 0.8262 1.9184 1.0415 0.2170  0.0323  0.0073  714 HIS A CG  
3310 N ND1 . HIS A 418 ? 0.8635 1.8941 1.0528 0.2677  0.0373  -0.0043 714 HIS A ND1 
3311 C CD2 . HIS A 418 ? 0.8351 1.9920 1.0568 0.1769  0.0388  0.0142  714 HIS A CD2 
3312 C CE1 . HIS A 418 ? 0.8612 1.9232 1.0451 0.2607  0.0470  -0.0048 714 HIS A CE1 
3313 N NE2 . HIS A 418 ? 0.8347 1.9750 1.0394 0.2057  0.0480  0.0069  714 HIS A NE2 
3314 N N   . VAL A 419 ? 1.0306 2.1248 1.1628 0.3744  0.0312  -0.0034 715 VAL A N   
3315 C CA  . VAL A 419 ? 1.0803 2.2500 1.1832 0.4155  0.0365  -0.0026 715 VAL A CA  
3316 C C   . VAL A 419 ? 1.0955 2.3362 1.2183 0.3763  0.0442  0.0019  715 VAL A C   
3317 O O   . VAL A 419 ? 1.0452 2.2427 1.1573 0.3838  0.0506  -0.0045 715 VAL A O   
3318 C CB  . VAL A 419 ? 1.0653 2.1557 1.1067 0.4921  0.0378  -0.0134 715 VAL A CB  
3319 C CG1 . VAL A 419 ? 1.1190 2.2911 1.1283 0.5352  0.0425  -0.0118 715 VAL A CG1 
3320 C CG2 . VAL A 419 ? 0.9537 1.9705 0.9666 0.5267  0.0296  -0.0161 715 VAL A CG2 
3321 N N   . TRP A 420 ? 1.1744 2.5209 1.3215 0.3320  0.0435  0.0128  716 TRP A N   
3322 C CA  . TRP A 420 ? 1.2479 2.6590 1.4118 0.2809  0.0492  0.0192  716 TRP A CA  
3323 C C   . TRP A 420 ? 1.5099 2.9719 1.6462 0.3257  0.0566  0.0164  716 TRP A C   
3324 O O   . TRP A 420 ? 1.5526 2.9785 1.6527 0.3963  0.0575  0.0082  716 TRP A O   
3325 C CB  . TRP A 420 ? 1.1534 2.6558 1.3375 0.2220  0.0447  0.0313  716 TRP A CB  
3326 C CG  . TRP A 420 ? 1.0542 2.5061 1.2631 0.1557  0.0389  0.0360  716 TRP A CG  
3327 C CD1 . TRP A 420 ? 1.0045 2.4074 1.2233 0.1525  0.0307  0.0354  716 TRP A CD1 
3328 C CD2 . TRP A 420 ? 1.0103 2.4512 1.2299 0.0836  0.0399  0.0424  716 TRP A CD2 
3329 N NE1 . TRP A 420 ? 0.9466 2.3095 1.1821 0.0843  0.0262  0.0407  716 TRP A NE1 
3330 C CE2 . TRP A 420 ? 0.9851 2.3663 1.2179 0.0413  0.0316  0.0452  716 TRP A CE2 
3331 C CE3 . TRP A 420 ? 1.0255 2.4966 1.2394 0.0512  0.0465  0.0463  716 TRP A CE3 
3332 C CZ2 . TRP A 420 ? 0.9639 2.3080 1.1978 -0.0296 0.0293  0.0516  716 TRP A CZ2 
3333 C CZ3 . TRP A 420 ? 1.0072 2.4414 1.2229 -0.0212 0.0447  0.0532  716 TRP A CZ3 
3334 C CH2 . TRP A 420 ? 0.9510 2.3190 1.1737 -0.0597 0.0360  0.0557  716 TRP A CH2 
# 
